CNRS Nantes University US2B US2B
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***  ENDOCYTOSIS 30-SEP-14 4WJG  ***

elNémo ID: 2609021359551401765

Job options:

ID        	=	 2609021359551401765
JOBID     	=	 ENDOCYTOSIS 30-SEP-14 4WJG
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    ENDOCYTOSIS                             30-SEP-14   4WJG              
TITLE     STRUCTURE OF T. BRUCEI HAPTOGLOBIN-HEMOGLOBIN RECEPTOR BINDING TO     
TITLE    2 HUMAN HAPTOGLOBIN-HEMOGLOBIN                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;                                  
COMPND   3 CHAIN: A, F, K, P, U, Z;                                             
COMPND   4 SYNONYM: ALPHA-GLOBIN,HEMOGLOBIN ALPHA CHAIN;                        
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HEMOGLOBIN SUBUNIT BETA;                                   
COMPND   7 CHAIN: B, G, L, Q, V, 1;                                             
COMPND   8 SYNONYM: BETA-GLOBIN,HEMOGLOBIN BETA CHAIN;                          
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: HAPTOGLOBIN;                                               
COMPND  11 CHAIN: C, H, M, R, W, 2;                                             
COMPND  12 SYNONYM: ZONULIN;                                                    
COMPND  13 MOL_ID: 4;                                                           
COMPND  14 MOLECULE: IRON-REGULATED SURFACE DETERMINANT PROTEIN H;              
COMPND  15 CHAIN: D, I, N, S, X, 3;                                             
COMPND  16 SYNONYM: HAPTOGLOBIN RECEPTOR A,STAPHYLOCOCCUS AUREUS SURFACE PROTEIN
COMPND  17 I;                                                                   
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 OTHER_DETAILS: FIRST NEAT DOMAIN;                                    
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: HAPTOGLOBIN-HEMOGLOBIN RECEPTOR;                           
COMPND  22 CHAIN: E, J, O, T, Y, 4;                                             
COMPND  23 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   7 ORGANISM_COMMON: HUMAN;                                              
SOURCE   8 ORGANISM_TAXID: 9606;                                                
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS N315;       
SOURCE  15 ORGANISM_TAXID: 158879;                                              
SOURCE  16 GENE: ISDH, HARA, SASI, SA1552;                                      
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: ROSETTA;                                   
SOURCE  20 MOL_ID: 5;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: TRYPANOSOMA BRUCEI BRUCEI;                      
SOURCE  22 ORGANISM_TAXID: 5702;                                                
SOURCE  23 GENE: HPHBR;                                                         
SOURCE  24 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE  25 EXPRESSION_SYSTEM_TAXID: 4922;                                       
SOURCE  26 EXPRESSION_SYSTEM_STRAIN: X33;                                       
SOURCE  27 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  28 EXPRESSION_SYSTEM_PLASMID: PPICZ ALPHA A                             
KEYWDS    ENDOCYTOSIS, TRYPANOSOME, RECEPTOR                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.STOEDKILDE,M.TORVUND-JENSEN,S.K.MOESTRUP,C.B.F.ANDERSEN             
REVDAT   6   26-AUG-26 4WJG    1       REMARK                                   
REVDAT   5   16-OCT-24 4WJG    1       HETSYN                                   
REVDAT   4   29-JUL-20 4WJG    1       COMPND SOURCE REMARK HETNAM              
REVDAT   4 2                   1       LINK   SITE   ATOM                       
REVDAT   3   28-FEB-18 4WJG    1       SOURCE                                   
REVDAT   2   03-DEC-14 4WJG    1       JRNL                                     
REVDAT   1   26-NOV-14 4WJG    0                                                
JRNL        AUTH   K.STDKILDE,M.TORVUND-JENSEN,S.K.MOESTRUP,C.B.ANDERSEN        
JRNL        TITL   STRUCTURAL BASIS FOR TRYPANOSOMAL HAEM ACQUISITION AND       
JRNL        TITL 2 SUSCEPTIBILITY TO THE HOST INNATE IMMUNE SYSTEM.             
JRNL        REF    NAT COMMUN                    V.   5  5487 2014              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   25410714                                                     
JRNL        DOI    10.1038/NCOMMS6487                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1702)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 182377                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.255                           
REMARK   3   R VALUE            (WORKING SET) : 0.255                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.960                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1750                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.9841 -  7.2538    0.91    13511    87  0.1822 0.1853        
REMARK   3     2  7.2538 -  5.7725    0.96    13884   197  0.2329 0.2497        
REMARK   3     3  5.7725 -  5.0472    0.96    13967   100  0.2350 0.2649        
REMARK   3     4  5.0472 -  4.5877    0.96    13943   192  0.2205 0.2467        
REMARK   3     5  4.5877 -  4.2599    0.97    14132    98  0.2236 0.2281        
REMARK   3     6  4.2599 -  4.0095    0.97    14118    97  0.2420 0.2603        
REMARK   3     7  4.0095 -  3.8091    0.95    13685   196  0.2659 0.2782        
REMARK   3     8  3.8091 -  3.6436    0.96    13977    97  0.2783 0.2907        
REMARK   3     9  3.6436 -  3.5036    0.97    14066   159  0.2967 0.3221        
REMARK   3    10  3.5036 -  3.3829    0.97    14025   135  0.3152 0.3157        
REMARK   3    11  3.3829 -  3.2773    0.97    14050   100  0.3405 0.4031        
REMARK   3    12  3.2773 -  3.1837    0.97    13830   194  0.3757 0.3596        
REMARK   3    13  3.1837 -  3.1000    0.97    14029    98  0.4074 0.4514        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 37.140           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.011          48930                                  
REMARK   3   ANGLE     :  1.552          66526                                  
REMARK   3   CHIRALITY :  0.065           7487                                  
REMARK   3   PLANARITY :  0.007           8482                                  
REMARK   3   DIHEDRAL  : 18.507          17611                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4WJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-OCT-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000203888.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 184077                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 7.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.440                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% POLYETHYLENE GLYCOL (PEG) 1500,      
REMARK 280  0.1M BIS-TRIS, PH 6.0, VAPOR DIFFUSION, SITTING DROP,               
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       70.47500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: a, b, c                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K, L, M, N, O, P, Q, R, S, T,         
REMARK 350                    AND CHAINS: d, e, f, g                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DECAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: U, V, W, X, Y, Z, 1, 2, 3, 4,         
REMARK 350                    AND CHAINS: h, i, j                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     PRO C   157A                                                     
REMARK 465     VAL C   157B                                                     
REMARK 465     GLN C   157C                                                     
REMARK 465     ARG C   157D                                                     
REMARK 465     ASN C   402                                                      
REMARK 465     GLY D    84                                                      
REMARK 465     SER D    85                                                      
REMARK 465     MET E   297                                                      
REMARK 465     LYS E   298                                                      
REMARK 465     ARG E   299                                                      
REMARK 465     ASN E   300                                                      
REMARK 465     GLY E   301                                                      
REMARK 465     ASN E   302                                                      
REMARK 465     PRO E   303                                                      
REMARK 465     ILE E   304                                                      
REMARK 465     GLU E   305                                                      
REMARK 465     ASN E   306                                                      
REMARK 465     GLU E   307                                                      
REMARK 465     SER E   308                                                      
REMARK 465     GLU E   309                                                      
REMARK 465     THR E   310                                                      
REMARK 465     ASN E   311                                                      
REMARK 465     SER E   312                                                      
REMARK 465     GLY E   313                                                      
REMARK 465     GLY E   314                                                      
REMARK 465     ASN E   315                                                      
REMARK 465     ALA E   316                                                      
REMARK 465     GLU E   317                                                      
REMARK 465     SER E   318                                                      
REMARK 465     GLN E   319                                                      
REMARK 465     GLY E   320                                                      
REMARK 465     ASN E   321                                                      
REMARK 465     GLY E   322                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     ARG E   324                                                      
REMARK 465     GLU E   325                                                      
REMARK 465     ASP E   326                                                      
REMARK 465     LYS E   327                                                      
REMARK 465     ASN E   328                                                      
REMARK 465     ASP E   329                                                      
REMARK 465     GLU E   330                                                      
REMARK 465     GLN E   331                                                      
REMARK 465     GLN E   332                                                      
REMARK 465     GLN E   333                                                      
REMARK 465     VAL E   334                                                      
REMARK 465     ASP E   335                                                      
REMARK 465     GLU E   336                                                      
REMARK 465     GLU E   337                                                      
REMARK 465     GLU E   338                                                      
REMARK 465     THR E   339                                                      
REMARK 465     LYS E   340                                                      
REMARK 465     VAL E   341                                                      
REMARK 465     GLU E   342                                                      
REMARK 465     ASN E   343                                                      
REMARK 465     GLY E   344                                                      
REMARK 465     SER E   345                                                      
REMARK 465     SER E   346                                                      
REMARK 465     GLU E   347                                                      
REMARK 465     GLU E   348                                                      
REMARK 465     GLY E   349                                                      
REMARK 465     SER E   350                                                      
REMARK 465     CYS E   351                                                      
REMARK 465     CYS E   352                                                      
REMARK 465     GLY E   353                                                      
REMARK 465     ASN E   354                                                      
REMARK 465     GLU E   355                                                      
REMARK 465     SER E   356                                                      
REMARK 465     ASN E   357                                                      
REMARK 465     GLY E   358                                                      
REMARK 465     PRO E   359                                                      
REMARK 465     HIS E   360                                                      
REMARK 465     VAL E   361                                                      
REMARK 465     MET E   362                                                      
REMARK 465     LYS E   363                                                      
REMARK 465     LYS E   364                                                      
REMARK 465     ARG E   365                                                      
REMARK 465     HIS E   366                                                      
REMARK 465     GLY E   367                                                      
REMARK 465     VAL E   368                                                      
REMARK 465     GLU E   369                                                      
REMARK 465     GLY E   370                                                      
REMARK 465     PRO E   371                                                      
REMARK 465     ARG E   372                                                      
REMARK 465     PRO E   373                                                      
REMARK 465     VAL E   374                                                      
REMARK 465     ASP E   375                                                      
REMARK 465     VAL E   376                                                      
REMARK 465     VAL E   377                                                      
REMARK 465     SER E   378                                                      
REMARK 465     PRO H   157A                                                     
REMARK 465     VAL H   157B                                                     
REMARK 465     GLN H   157C                                                     
REMARK 465     ARG H   157D                                                     
REMARK 465     ASN H   402                                                      
REMARK 465     GLY I    84                                                      
REMARK 465     SER I    85                                                      
REMARK 465     MET J   297                                                      
REMARK 465     LYS J   298                                                      
REMARK 465     ARG J   299                                                      
REMARK 465     ASN J   300                                                      
REMARK 465     GLY J   301                                                      
REMARK 465     ASN J   302                                                      
REMARK 465     PRO J   303                                                      
REMARK 465     ILE J   304                                                      
REMARK 465     GLU J   305                                                      
REMARK 465     ASN J   306                                                      
REMARK 465     GLU J   307                                                      
REMARK 465     SER J   308                                                      
REMARK 465     GLU J   309                                                      
REMARK 465     THR J   310                                                      
REMARK 465     ASN J   311                                                      
REMARK 465     SER J   312                                                      
REMARK 465     GLY J   313                                                      
REMARK 465     GLY J   314                                                      
REMARK 465     ASN J   315                                                      
REMARK 465     ALA J   316                                                      
REMARK 465     GLU J   317                                                      
REMARK 465     SER J   318                                                      
REMARK 465     GLN J   319                                                      
REMARK 465     GLY J   320                                                      
REMARK 465     ASN J   321                                                      
REMARK 465     GLY J   322                                                      
REMARK 465     ASP J   323                                                      
REMARK 465     ARG J   324                                                      
REMARK 465     GLU J   325                                                      
REMARK 465     ASP J   326                                                      
REMARK 465     LYS J   327                                                      
REMARK 465     ASN J   328                                                      
REMARK 465     ASP J   329                                                      
REMARK 465     GLU J   330                                                      
REMARK 465     GLN J   331                                                      
REMARK 465     GLN J   332                                                      
REMARK 465     GLN J   333                                                      
REMARK 465     VAL J   334                                                      
REMARK 465     ASP J   335                                                      
REMARK 465     GLU J   336                                                      
REMARK 465     GLU J   337                                                      
REMARK 465     GLU J   338                                                      
REMARK 465     THR J   339                                                      
REMARK 465     LYS J   340                                                      
REMARK 465     VAL J   341                                                      
REMARK 465     GLU J   342                                                      
REMARK 465     ASN J   343                                                      
REMARK 465     GLY J   344                                                      
REMARK 465     SER J   345                                                      
REMARK 465     SER J   346                                                      
REMARK 465     GLU J   347                                                      
REMARK 465     GLU J   348                                                      
REMARK 465     GLY J   349                                                      
REMARK 465     SER J   350                                                      
REMARK 465     CYS J   351                                                      
REMARK 465     CYS J   352                                                      
REMARK 465     GLY J   353                                                      
REMARK 465     ASN J   354                                                      
REMARK 465     GLU J   355                                                      
REMARK 465     SER J   356                                                      
REMARK 465     ASN J   357                                                      
REMARK 465     GLY J   358                                                      
REMARK 465     PRO J   359                                                      
REMARK 465     HIS J   360                                                      
REMARK 465     VAL J   361                                                      
REMARK 465     MET J   362                                                      
REMARK 465     LYS J   363                                                      
REMARK 465     LYS J   364                                                      
REMARK 465     ARG J   365                                                      
REMARK 465     HIS J   366                                                      
REMARK 465     GLY J   367                                                      
REMARK 465     VAL J   368                                                      
REMARK 465     GLU J   369                                                      
REMARK 465     GLY J   370                                                      
REMARK 465     PRO J   371                                                      
REMARK 465     ARG J   372                                                      
REMARK 465     PRO J   373                                                      
REMARK 465     VAL J   374                                                      
REMARK 465     ASP J   375                                                      
REMARK 465     VAL J   376                                                      
REMARK 465     VAL J   377                                                      
REMARK 465     SER J   378                                                      
REMARK 465     PRO M   157A                                                     
REMARK 465     VAL M   157B                                                     
REMARK 465     GLN M   157C                                                     
REMARK 465     ARG M   157D                                                     
REMARK 465     ASN M   402                                                      
REMARK 465     GLY N    84                                                      
REMARK 465     SER N    85                                                      
REMARK 465     MET O   297                                                      
REMARK 465     LYS O   298                                                      
REMARK 465     ARG O   299                                                      
REMARK 465     ASN O   300                                                      
REMARK 465     GLY O   301                                                      
REMARK 465     ASN O   302                                                      
REMARK 465     PRO O   303                                                      
REMARK 465     ILE O   304                                                      
REMARK 465     GLU O   305                                                      
REMARK 465     ASN O   306                                                      
REMARK 465     GLU O   307                                                      
REMARK 465     SER O   308                                                      
REMARK 465     GLU O   309                                                      
REMARK 465     THR O   310                                                      
REMARK 465     ASN O   311                                                      
REMARK 465     SER O   312                                                      
REMARK 465     GLY O   313                                                      
REMARK 465     GLY O   314                                                      
REMARK 465     ASN O   315                                                      
REMARK 465     ALA O   316                                                      
REMARK 465     GLU O   317                                                      
REMARK 465     SER O   318                                                      
REMARK 465     GLN O   319                                                      
REMARK 465     GLY O   320                                                      
REMARK 465     ASN O   321                                                      
REMARK 465     GLY O   322                                                      
REMARK 465     ASP O   323                                                      
REMARK 465     ARG O   324                                                      
REMARK 465     GLU O   325                                                      
REMARK 465     ASP O   326                                                      
REMARK 465     LYS O   327                                                      
REMARK 465     ASN O   328                                                      
REMARK 465     ASP O   329                                                      
REMARK 465     GLU O   330                                                      
REMARK 465     GLN O   331                                                      
REMARK 465     GLN O   332                                                      
REMARK 465     GLN O   333                                                      
REMARK 465     VAL O   334                                                      
REMARK 465     ASP O   335                                                      
REMARK 465     GLU O   336                                                      
REMARK 465     GLU O   337                                                      
REMARK 465     GLU O   338                                                      
REMARK 465     THR O   339                                                      
REMARK 465     LYS O   340                                                      
REMARK 465     VAL O   341                                                      
REMARK 465     GLU O   342                                                      
REMARK 465     ASN O   343                                                      
REMARK 465     GLY O   344                                                      
REMARK 465     SER O   345                                                      
REMARK 465     SER O   346                                                      
REMARK 465     GLU O   347                                                      
REMARK 465     GLU O   348                                                      
REMARK 465     GLY O   349                                                      
REMARK 465     SER O   350                                                      
REMARK 465     CYS O   351                                                      
REMARK 465     CYS O   352                                                      
REMARK 465     GLY O   353                                                      
REMARK 465     ASN O   354                                                      
REMARK 465     GLU O   355                                                      
REMARK 465     SER O   356                                                      
REMARK 465     ASN O   357                                                      
REMARK 465     GLY O   358                                                      
REMARK 465     PRO O   359                                                      
REMARK 465     HIS O   360                                                      
REMARK 465     VAL O   361                                                      
REMARK 465     MET O   362                                                      
REMARK 465     LYS O   363                                                      
REMARK 465     LYS O   364                                                      
REMARK 465     ARG O   365                                                      
REMARK 465     HIS O   366                                                      
REMARK 465     GLY O   367                                                      
REMARK 465     VAL O   368                                                      
REMARK 465     GLU O   369                                                      
REMARK 465     GLY O   370                                                      
REMARK 465     PRO O   371                                                      
REMARK 465     ARG O   372                                                      
REMARK 465     PRO O   373                                                      
REMARK 465     VAL O   374                                                      
REMARK 465     ASP O   375                                                      
REMARK 465     VAL O   376                                                      
REMARK 465     VAL O   377                                                      
REMARK 465     SER O   378                                                      
REMARK 465     PRO R   157A                                                     
REMARK 465     VAL R   157B                                                     
REMARK 465     GLN R   157C                                                     
REMARK 465     ARG R   157D                                                     
REMARK 465     ASN R   402                                                      
REMARK 465     GLY S    84                                                      
REMARK 465     SER S    85                                                      
REMARK 465     MET T   297                                                      
REMARK 465     LYS T   298                                                      
REMARK 465     ARG T   299                                                      
REMARK 465     ASN T   300                                                      
REMARK 465     GLY T   301                                                      
REMARK 465     ASN T   302                                                      
REMARK 465     PRO T   303                                                      
REMARK 465     ILE T   304                                                      
REMARK 465     GLU T   305                                                      
REMARK 465     ASN T   306                                                      
REMARK 465     GLU T   307                                                      
REMARK 465     SER T   308                                                      
REMARK 465     GLU T   309                                                      
REMARK 465     THR T   310                                                      
REMARK 465     ASN T   311                                                      
REMARK 465     SER T   312                                                      
REMARK 465     GLY T   313                                                      
REMARK 465     GLY T   314                                                      
REMARK 465     ASN T   315                                                      
REMARK 465     ALA T   316                                                      
REMARK 465     GLU T   317                                                      
REMARK 465     SER T   318                                                      
REMARK 465     GLN T   319                                                      
REMARK 465     GLY T   320                                                      
REMARK 465     ASN T   321                                                      
REMARK 465     GLY T   322                                                      
REMARK 465     ASP T   323                                                      
REMARK 465     ARG T   324                                                      
REMARK 465     GLU T   325                                                      
REMARK 465     ASP T   326                                                      
REMARK 465     LYS T   327                                                      
REMARK 465     ASN T   328                                                      
REMARK 465     ASP T   329                                                      
REMARK 465     GLU T   330                                                      
REMARK 465     GLN T   331                                                      
REMARK 465     GLN T   332                                                      
REMARK 465     GLN T   333                                                      
REMARK 465     VAL T   334                                                      
REMARK 465     ASP T   335                                                      
REMARK 465     GLU T   336                                                      
REMARK 465     GLU T   337                                                      
REMARK 465     GLU T   338                                                      
REMARK 465     THR T   339                                                      
REMARK 465     LYS T   340                                                      
REMARK 465     VAL T   341                                                      
REMARK 465     GLU T   342                                                      
REMARK 465     ASN T   343                                                      
REMARK 465     GLY T   344                                                      
REMARK 465     SER T   345                                                      
REMARK 465     SER T   346                                                      
REMARK 465     GLU T   347                                                      
REMARK 465     GLU T   348                                                      
REMARK 465     GLY T   349                                                      
REMARK 465     SER T   350                                                      
REMARK 465     CYS T   351                                                      
REMARK 465     CYS T   352                                                      
REMARK 465     GLY T   353                                                      
REMARK 465     ASN T   354                                                      
REMARK 465     GLU T   355                                                      
REMARK 465     SER T   356                                                      
REMARK 465     ASN T   357                                                      
REMARK 465     GLY T   358                                                      
REMARK 465     PRO T   359                                                      
REMARK 465     HIS T   360                                                      
REMARK 465     VAL T   361                                                      
REMARK 465     MET T   362                                                      
REMARK 465     LYS T   363                                                      
REMARK 465     LYS T   364                                                      
REMARK 465     ARG T   365                                                      
REMARK 465     HIS T   366                                                      
REMARK 465     GLY T   367                                                      
REMARK 465     VAL T   368                                                      
REMARK 465     GLU T   369                                                      
REMARK 465     GLY T   370                                                      
REMARK 465     PRO T   371                                                      
REMARK 465     ARG T   372                                                      
REMARK 465     PRO T   373                                                      
REMARK 465     VAL T   374                                                      
REMARK 465     ASP T   375                                                      
REMARK 465     VAL T   376                                                      
REMARK 465     VAL T   377                                                      
REMARK 465     SER T   378                                                      
REMARK 465     PRO W   157A                                                     
REMARK 465     VAL W   157B                                                     
REMARK 465     GLN W   157C                                                     
REMARK 465     ARG W   157D                                                     
REMARK 465     ASN W   402                                                      
REMARK 465     GLY X    84                                                      
REMARK 465     SER X    85                                                      
REMARK 465     MET Y   297                                                      
REMARK 465     LYS Y   298                                                      
REMARK 465     ARG Y   299                                                      
REMARK 465     ASN Y   300                                                      
REMARK 465     GLY Y   301                                                      
REMARK 465     ASN Y   302                                                      
REMARK 465     PRO Y   303                                                      
REMARK 465     ILE Y   304                                                      
REMARK 465     GLU Y   305                                                      
REMARK 465     ASN Y   306                                                      
REMARK 465     GLU Y   307                                                      
REMARK 465     SER Y   308                                                      
REMARK 465     GLU Y   309                                                      
REMARK 465     THR Y   310                                                      
REMARK 465     ASN Y   311                                                      
REMARK 465     SER Y   312                                                      
REMARK 465     GLY Y   313                                                      
REMARK 465     GLY Y   314                                                      
REMARK 465     ASN Y   315                                                      
REMARK 465     ALA Y   316                                                      
REMARK 465     GLU Y   317                                                      
REMARK 465     SER Y   318                                                      
REMARK 465     GLN Y   319                                                      
REMARK 465     GLY Y   320                                                      
REMARK 465     ASN Y   321                                                      
REMARK 465     GLY Y   322                                                      
REMARK 465     ASP Y   323                                                      
REMARK 465     ARG Y   324                                                      
REMARK 465     GLU Y   325                                                      
REMARK 465     ASP Y   326                                                      
REMARK 465     LYS Y   327                                                      
REMARK 465     ASN Y   328                                                      
REMARK 465     ASP Y   329                                                      
REMARK 465     GLU Y   330                                                      
REMARK 465     GLN Y   331                                                      
REMARK 465     GLN Y   332                                                      
REMARK 465     GLN Y   333                                                      
REMARK 465     VAL Y   334                                                      
REMARK 465     ASP Y   335                                                      
REMARK 465     GLU Y   336                                                      
REMARK 465     GLU Y   337                                                      
REMARK 465     GLU Y   338                                                      
REMARK 465     THR Y   339                                                      
REMARK 465     LYS Y   340                                                      
REMARK 465     VAL Y   341                                                      
REMARK 465     GLU Y   342                                                      
REMARK 465     ASN Y   343                                                      
REMARK 465     GLY Y   344                                                      
REMARK 465     SER Y   345                                                      
REMARK 465     SER Y   346                                                      
REMARK 465     GLU Y   347                                                      
REMARK 465     GLU Y   348                                                      
REMARK 465     GLY Y   349                                                      
REMARK 465     SER Y   350                                                      
REMARK 465     CYS Y   351                                                      
REMARK 465     CYS Y   352                                                      
REMARK 465     GLY Y   353                                                      
REMARK 465     ASN Y   354                                                      
REMARK 465     GLU Y   355                                                      
REMARK 465     SER Y   356                                                      
REMARK 465     ASN Y   357                                                      
REMARK 465     GLY Y   358                                                      
REMARK 465     PRO Y   359                                                      
REMARK 465     HIS Y   360                                                      
REMARK 465     VAL Y   361                                                      
REMARK 465     MET Y   362                                                      
REMARK 465     LYS Y   363                                                      
REMARK 465     LYS Y   364                                                      
REMARK 465     ARG Y   365                                                      
REMARK 465     HIS Y   366                                                      
REMARK 465     GLY Y   367                                                      
REMARK 465     VAL Y   368                                                      
REMARK 465     GLU Y   369                                                      
REMARK 465     GLY Y   370                                                      
REMARK 465     PRO Y   371                                                      
REMARK 465     ARG Y   372                                                      
REMARK 465     PRO Y   373                                                      
REMARK 465     VAL Y   374                                                      
REMARK 465     ASP Y   375                                                      
REMARK 465     VAL Y   376                                                      
REMARK 465     VAL Y   377                                                      
REMARK 465     SER Y   378                                                      
REMARK 465     PRO 2   157A                                                     
REMARK 465     VAL 2   157B                                                     
REMARK 465     GLN 2   157C                                                     
REMARK 465     ARG 2   157D                                                     
REMARK 465     ASN 2   402                                                      
REMARK 465     GLY 3    84                                                      
REMARK 465     SER 3    85                                                      
REMARK 465     MET 4   297                                                      
REMARK 465     LYS 4   298                                                      
REMARK 465     ARG 4   299                                                      
REMARK 465     ASN 4   300                                                      
REMARK 465     GLY 4   301                                                      
REMARK 465     ASN 4   302                                                      
REMARK 465     PRO 4   303                                                      
REMARK 465     ILE 4   304                                                      
REMARK 465     GLU 4   305                                                      
REMARK 465     ASN 4   306                                                      
REMARK 465     GLU 4   307                                                      
REMARK 465     SER 4   308                                                      
REMARK 465     GLU 4   309                                                      
REMARK 465     THR 4   310                                                      
REMARK 465     ASN 4   311                                                      
REMARK 465     SER 4   312                                                      
REMARK 465     GLY 4   313                                                      
REMARK 465     GLY 4   314                                                      
REMARK 465     ASN 4   315                                                      
REMARK 465     ALA 4   316                                                      
REMARK 465     GLU 4   317                                                      
REMARK 465     SER 4   318                                                      
REMARK 465     GLN 4   319                                                      
REMARK 465     GLY 4   320                                                      
REMARK 465     ASN 4   321                                                      
REMARK 465     GLY 4   322                                                      
REMARK 465     ASP 4   323                                                      
REMARK 465     ARG 4   324                                                      
REMARK 465     GLU 4   325                                                      
REMARK 465     ASP 4   326                                                      
REMARK 465     LYS 4   327                                                      
REMARK 465     ASN 4   328                                                      
REMARK 465     ASP 4   329                                                      
REMARK 465     GLU 4   330                                                      
REMARK 465     GLN 4   331                                                      
REMARK 465     GLN 4   332                                                      
REMARK 465     GLN 4   333                                                      
REMARK 465     VAL 4   334                                                      
REMARK 465     ASP 4   335                                                      
REMARK 465     GLU 4   336                                                      
REMARK 465     GLU 4   337                                                      
REMARK 465     GLU 4   338                                                      
REMARK 465     THR 4   339                                                      
REMARK 465     LYS 4   340                                                      
REMARK 465     VAL 4   341                                                      
REMARK 465     GLU 4   342                                                      
REMARK 465     ASN 4   343                                                      
REMARK 465     GLY 4   344                                                      
REMARK 465     SER 4   345                                                      
REMARK 465     SER 4   346                                                      
REMARK 465     GLU 4   347                                                      
REMARK 465     GLU 4   348                                                      
REMARK 465     GLY 4   349                                                      
REMARK 465     SER 4   350                                                      
REMARK 465     CYS 4   351                                                      
REMARK 465     CYS 4   352                                                      
REMARK 465     GLY 4   353                                                      
REMARK 465     ASN 4   354                                                      
REMARK 465     GLU 4   355                                                      
REMARK 465     SER 4   356                                                      
REMARK 465     ASN 4   357                                                      
REMARK 465     GLY 4   358                                                      
REMARK 465     PRO 4   359                                                      
REMARK 465     HIS 4   360                                                      
REMARK 465     VAL 4   361                                                      
REMARK 465     MET 4   362                                                      
REMARK 465     LYS 4   363                                                      
REMARK 465     LYS 4   364                                                      
REMARK 465     ARG 4   365                                                      
REMARK 465     HIS 4   366                                                      
REMARK 465     GLY 4   367                                                      
REMARK 465     VAL 4   368                                                      
REMARK 465     GLU 4   369                                                      
REMARK 465     GLY 4   370                                                      
REMARK 465     PRO 4   371                                                      
REMARK 465     ARG 4   372                                                      
REMARK 465     PRO 4   373                                                      
REMARK 465     VAL 4   374                                                      
REMARK 465     ASP 4   375                                                      
REMARK 465     VAL 4   376                                                      
REMARK 465     VAL 4   377                                                      
REMARK 465     SER 4   378                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG1  THR M   196     OD1  ASN M   199              2.08            
REMARK 500   OH   TYR M   109     O    PRO R    96              2.09            
REMARK 500   ND2  ASN W   203     O5   NAG W  1002              2.09            
REMARK 500   OG1  THR C   196     OD1  ASN C   199              2.10            
REMARK 500   OG1  THR H   196     OD1  ASN H   199              2.10            
REMARK 500   ND2  ASN M   203     O5   NAG d     1              2.13            
REMARK 500   OG1  THR 2   196     OD1  ASN 2   199              2.14            
REMARK 500   OG1  THR W   196     OD1  ASN W   199              2.14            
REMARK 500   OD2  ASP E    43     CE   LYS E    47              2.15            
REMARK 500   O4   NAG e     1     C2   NAG e     2              2.16            
REMARK 500   ND2  ASN R   203     O5   NAG f     1              2.16            
REMARK 500   OH   TYR C   109     O    PRO H    96              2.16            
REMARK 500   O    ASN E   287     OG1  THR E   291              2.18            
REMARK 500   ND2  ASN H   157     O    THR J    68              2.18            
REMARK 500   O    ASN Y   287     OG1  THR Y   291              2.18            
REMARK 500   O    ASN J   287     OG1  THR J   291              2.18            
REMARK 500   OD2  ASP J   147     NZ   LYS J   151              2.18            
REMARK 500   OD2  ASP Y   147     NZ   LYS Y   151              2.19            
REMARK 500   O    ASN T   287     OG1  THR T   291              2.19            
REMARK 500   OD2  ASP 4   147     NZ   LYS 4   151              2.19            
REMARK 500   O    ASN O   287     OG1  THR O   291              2.19            
REMARK 500   OG1  THR R   196     OD1  ASN R   199              2.19            
REMARK 500   OD2  ASP T   147     NZ   LYS T   151              2.19            
REMARK 500   O    ASN 4   287     OG1  THR 4   291              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    VAL F   1   CG1 -  CB  -  CG2 ANGL. DEV. =   9.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A   2       76.14     55.83                                   
REMARK 500    LYS A  16       -9.48    -55.19                                   
REMARK 500    SER A  49     -176.82    -68.55                                   
REMARK 500    HIS A  89      -63.40    -92.29                                   
REMARK 500    ARG A  92       71.73     40.58                                   
REMARK 500    PRO A  95      -18.83    -47.05                                   
REMARK 500    GLU B  22      -57.38   -126.81                                   
REMARK 500    PRO C  93       84.51    -65.86                                   
REMARK 500    THR C 119      162.88    171.94                                   
REMARK 500    HIS C 162       75.84     60.54                                   
REMARK 500    HIS C 179       37.66    -95.28                                   
REMARK 500    LYS C 223      -84.35    -89.51                                   
REMARK 500    GLU C 230      -70.14    -87.79                                   
REMARK 500    MET C 259      138.77   -175.39                                   
REMARK 500    ASN C 283     -166.94   -122.84                                   
REMARK 500    SER C 312      -74.06   -102.41                                   
REMARK 500    THR C 313     -104.54     67.10                                   
REMARK 500    CYS C 347     -167.36   -125.09                                   
REMARK 500    SER C 372      -61.37    -92.77                                   
REMARK 500    CYS C 377     -133.89     50.03                                   
REMARK 500    LYS D 142      -74.19   -103.22                                   
REMARK 500    LYS D 157      -73.74   -116.87                                   
REMARK 500    VAL D 173      -60.58   -102.53                                   
REMARK 500    GLU D 180      -62.61    -94.93                                   
REMARK 500    GLN D 194      -57.55   -127.30                                   
REMARK 500    ASP D 205     -119.85     54.44                                   
REMARK 500    LEU E  39      176.53    167.43                                   
REMARK 500    LYS E  40     -159.49   -172.89                                   
REMARK 500    LYS E  42       -8.41    -57.69                                   
REMARK 500    GLU E 109      -76.37    -99.62                                   
REMARK 500    ASN E 114       65.32     36.52                                   
REMARK 500    THR E 116     -105.05     61.27                                   
REMARK 500    ALA E 118      -61.05    -93.02                                   
REMARK 500    ASN E 185      -18.84     75.85                                   
REMARK 500    ALA E 188      -18.19     65.60                                   
REMARK 500    ALA E 194      -61.12    -95.48                                   
REMARK 500    ASN E 219      -71.86    -55.85                                   
REMARK 500    LEU E 223      -38.43    -39.25                                   
REMARK 500    HIS E 289      -61.42   -100.81                                   
REMARK 500    LYS E 292      -60.01    -99.96                                   
REMARK 500    LEU F   2       76.77     58.13                                   
REMARK 500    SER F  49     -175.90    -68.95                                   
REMARK 500    HIS F  89      -64.82    -92.83                                   
REMARK 500    ARG F  92       72.54     41.00                                   
REMARK 500    PRO F  95      -19.46    -46.97                                   
REMARK 500    THR F 118      150.80    -46.90                                   
REMARK 500    ALA F 123      -70.42    -56.64                                   
REMARK 500    GLU G  22      -56.70   -127.08                                   
REMARK 500    ASN G  80       48.02    -97.16                                   
REMARK 500    PRO H  93       85.26    -65.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     245 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU C  120     GLY C  121                   39.63                    
REMARK 500 GLY C  311     SER C  312                 -137.42                    
REMARK 500 SER C  312     THR C  313                 -129.66                    
REMARK 500 ALA C  378     VAL C  379                 -149.85                    
REMARK 500 PRO D  177     VAL D  178                 -140.00                    
REMARK 500 GLY E   38     LEU E   39                  147.53                    
REMARK 500 GLU H  120     GLY H  121                   39.26                    
REMARK 500 GLY H  311     SER H  312                 -137.43                    
REMARK 500 SER H  312     THR H  313                 -129.30                    
REMARK 500 PRO I  177     VAL I  178                 -138.27                    
REMARK 500 GLY J   38     LEU J   39                  147.96                    
REMARK 500 GLU M  120     GLY M  121                   39.35                    
REMARK 500 GLY M  311     SER M  312                 -137.00                    
REMARK 500 SER M  312     THR M  313                 -131.28                    
REMARK 500 ALA M  378     VAL M  379                 -149.89                    
REMARK 500 PRO N  177     VAL N  178                 -139.72                    
REMARK 500 GLY O   38     LEU O   39                  147.80                    
REMARK 500 GLU R  120     GLY R  121                   38.90                    
REMARK 500 GLY R  311     SER R  312                 -136.82                    
REMARK 500 SER R  312     THR R  313                 -129.28                    
REMARK 500 PRO S  177     VAL S  178                 -139.17                    
REMARK 500 GLY T   38     LEU T   39                  147.63                    
REMARK 500 GLU W  120     GLY W  121                   37.61                    
REMARK 500 GLY W  311     SER W  312                 -137.71                    
REMARK 500 SER W  312     THR W  313                 -129.89                    
REMARK 500 PRO X  177     VAL X  178                 -139.75                    
REMARK 500 GLY Y   38     LEU Y   39                  147.69                    
REMARK 500 GLU 2  120     GLY 2  121                   38.31                    
REMARK 500 GLY 2  311     SER 2  312                 -138.54                    
REMARK 500 SER 2  312     THR 2  313                 -129.33                    
REMARK 500 PRO 3  177     VAL 3  178                 -139.38                    
REMARK 500 GLY 4   38     LEU 4   39                  148.43                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A  87   NE2                                                    
REMARK 620 2 HEM A 201   NA   80.9                                              
REMARK 620 3 HEM A 201   NB   91.9  94.1                                        
REMARK 620 4 HEM A 201   NC  112.1 166.9  83.7                                  
REMARK 620 5 HEM A 201   ND  102.4  85.7 165.5  93.2                            
REMARK 620 6 OXY A 202   O1  156.1  75.4  92.9  91.7  73.0                      
REMARK 620 7 OXY A 202   O2  169.3 101.5  98.3  66.1  67.6  27.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  92   NE2                                                    
REMARK 620 2 HEM B 201   NA   96.1                                              
REMARK 620 3 HEM B 201   NB   78.0  94.3                                        
REMARK 620 4 HEM B 201   NC  105.8 153.2  75.6                                  
REMARK 620 5 HEM B 201   ND  128.5  79.5 153.1  98.1                            
REMARK 620 6 OXY B 202   O2  139.9  72.4  65.1  80.8  88.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM F 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  87   NE2                                                    
REMARK 620 2 HEM F 201   NA   83.4                                              
REMARK 620 3 HEM F 201   NB   86.8  92.7                                        
REMARK 620 4 HEM F 201   NC  109.9 166.8  88.1                                  
REMARK 620 5 HEM F 201   ND  107.1  82.9 164.8  93.0                            
REMARK 620 6 OXY F 202   O1  157.2  76.0  84.6  90.9  80.2                      
REMARK 620 7 OXY F 202   O2  173.0  97.3 100.1  69.5  66.3  27.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM G 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G  92   NE2                                                    
REMARK 620 2 HEM G 201   NA   94.7                                              
REMARK 620 3 HEM G 201   NB   79.7  87.5                                        
REMARK 620 4 HEM G 201   NC  109.2 151.8  82.3                                  
REMARK 620 5 HEM G 201   ND  126.7  83.8 152.7  93.3                            
REMARK 620 6 OXY G 202   O1  145.9  71.9  68.8  79.9  83.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM K 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K  87   NE2                                                    
REMARK 620 2 HEM K 201   NA   87.8                                              
REMARK 620 3 HEM K 201   NB   93.4  95.5                                        
REMARK 620 4 HEM K 201   NC  108.6 163.5  85.4                                  
REMARK 620 5 HEM K 201   ND  105.3  82.7 161.1  91.1                            
REMARK 620 6 OXY K 202   O1  168.5  81.6  83.4  82.1  77.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM L 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L  92   NE2                                                    
REMARK 620 2 HEM L 201   NA   92.7                                              
REMARK 620 3 HEM L 201   NB   79.8  93.4                                        
REMARK 620 4 HEM L 201   NC  110.1 150.7  73.7                                  
REMARK 620 5 HEM L 201   ND  128.5  77.0 149.9 100.8                            
REMARK 620 6 OXY L 202   O1  143.4  69.0  70.4  81.8  79.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM P 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS P  87   NE2                                                    
REMARK 620 2 HEM P 201   NA   80.6                                              
REMARK 620 3 HEM P 201   NB   85.3  94.8                                        
REMARK 620 4 HEM P 201   NC  113.3 165.6  83.1                                  
REMARK 620 5 HEM P 201   ND  108.3  78.8 163.5  99.3                            
REMARK 620 6 OXY P 202   O1  141.5  73.4  69.3  92.6  94.2                      
REMARK 620 7 OXY P 202   O2  167.6  87.3  92.8  78.6  71.8  29.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM Q 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Q  92   NE2                                                    
REMARK 620 2 HEM Q 201   NA   97.1                                              
REMARK 620 3 HEM Q 201   NB   79.4  90.1                                        
REMARK 620 4 HEM Q 201   NC  106.2 150.7  77.4                                  
REMARK 620 5 HEM Q 201   ND  129.0  80.3 150.7  97.7                            
REMARK 620 6 OXY Q 202   O2  160.2  81.3  80.8  70.7  70.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM U 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS U  87   NE2                                                    
REMARK 620 2 HEM U 201   NA   71.2                                              
REMARK 620 3 HEM U 201   NB   87.4  87.7                                        
REMARK 620 4 HEM U 201   NC  114.1 174.2  90.2                                  
REMARK 620 5 HEM U 201   ND   96.2  85.3 170.6  96.2                            
REMARK 620 6 OXY U 202   O2  162.6  91.5  94.1  83.3  79.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  92   NE2                                                    
REMARK 620 2 HEM V 201   NA   91.4                                              
REMARK 620 3 HEM V 201   NB   76.8  88.0                                        
REMARK 620 4 HEM V 201   NC  100.2 163.0  82.7                                  
REMARK 620 5 HEM V 201   ND  119.8  89.8 163.3  95.1                            
REMARK 620 6 OXY V 202   O2  169.7  85.5  93.2  80.9  70.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM Z 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS Z  87   NE2                                                    
REMARK 620 2 HEM Z 201   NA   83.8                                              
REMARK 620 3 HEM Z 201   NB   93.5  90.0                                        
REMARK 620 4 HEM Z 201   NC  107.7 168.4  87.8                                  
REMARK 620 5 HEM Z 201   ND   99.0  86.2 166.4  93.3                            
REMARK 620 6 OXY Z 202   O1  151.5  67.7  88.3 100.8  78.2                      
REMARK 620 7 OXY Z 202   O2  177.4  94.4  88.3  74.2  79.1  26.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM 1 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS 1  92   NE2                                                    
REMARK 620 2 HEM 1 201   NA   87.8                                              
REMARK 620 3 HEM 1 201   NB   76.5  94.0                                        
REMARK 620 4 HEM 1 201   NC  106.2 162.5  79.5                                  
REMARK 620 5 HEM 1 201   ND  121.5  82.8 161.4  98.2                            
REMARK 620 6 OXY 1 202   O1  137.8  69.2  70.7  93.3  91.1                      
REMARK 620 7 OXY 1 202   O2  165.4  83.6  92.4  80.5  69.0  27.6                
REMARK 620 N                    1     2     3     4     5     6                 
DBREF  4WJG A    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4WJG B    1   146  UNP    P68871   HBB_HUMAN        2    147             
DBREF  4WJG C   92   402  UNP    P00738   HPT_HUMAN       92    406             
DBREF  4WJG D   86   229  UNP    Q99TD3   ISDH_STAAN      86    229             
DBREF  4WJG E   36   378  UNP    I7BA80   I7BA80_TRYBB    36    378             
DBREF  4WJG F    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4WJG G    1   146  UNP    P68871   HBB_HUMAN        2    147             
DBREF  4WJG H   92   402  UNP    P00738   HPT_HUMAN       92    406             
DBREF  4WJG I   86   229  UNP    Q99TD3   ISDH_STAAN      86    229             
DBREF  4WJG J   36   378  UNP    I7BA80   I7BA80_TRYBB    36    378             
DBREF  4WJG K    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4WJG L    1   146  UNP    P68871   HBB_HUMAN        2    147             
DBREF  4WJG M   92   402  UNP    P00738   HPT_HUMAN       92    406             
DBREF  4WJG N   86   229  UNP    Q99TD3   ISDH_STAAN      86    229             
DBREF  4WJG O   36   378  UNP    I7BA80   I7BA80_TRYBB    36    378             
DBREF  4WJG P    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4WJG Q    1   146  UNP    P68871   HBB_HUMAN        2    147             
DBREF  4WJG R   92   402  UNP    P00738   HPT_HUMAN       92    406             
DBREF  4WJG S   86   229  UNP    Q99TD3   ISDH_STAAN      86    229             
DBREF  4WJG T   36   378  UNP    I7BA80   I7BA80_TRYBB    36    378             
DBREF  4WJG U    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4WJG V    1   146  UNP    P68871   HBB_HUMAN        2    147             
DBREF  4WJG W   92   402  UNP    P00738   HPT_HUMAN       92    406             
DBREF  4WJG X   86   229  UNP    Q99TD3   ISDH_STAAN      86    229             
DBREF  4WJG Y   36   378  UNP    I7BA80   I7BA80_TRYBB    36    378             
DBREF  4WJG Z    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4WJG 1    1   146  UNP    P68871   HBB_HUMAN        2    147             
DBREF  4WJG 2   92   402  UNP    P00738   HPT_HUMAN       92    406             
DBREF  4WJG 3   86   229  UNP    Q99TD3   ISDH_STAAN      86    229             
DBREF  4WJG 4   36   378  UNP    I7BA80   I7BA80_TRYBB    36    378             
SEQADV 4WJG GLY D   84  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG SER D   85  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG GLY I   84  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG SER I   85  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG GLY N   84  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG SER N   85  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG GLY S   84  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG SER S   85  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG GLY X   84  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG SER X   85  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG GLY 3   84  UNP  Q99TD3              EXPRESSION TAG                 
SEQADV 4WJG SER 3   85  UNP  Q99TD3              EXPRESSION TAG                 
SEQRES   1 A  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 A  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 A  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 A  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 A  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 A  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 A  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 A  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 A  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 A  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 A  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 B  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 B  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 B  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 B  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 B  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 B  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 B  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 B  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 B  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 B  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 B  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 B  146  LYS TYR HIS                                                  
SEQRES   1 C  315  CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU          
SEQRES   2 C  315  HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU          
SEQRES   3 C  315  ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU          
SEQRES   4 C  315  LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO          
SEQRES   5 C  315  GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA          
SEQRES   6 C  315  ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA          
SEQRES   7 C  315  LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS          
SEQRES   8 C  315  HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN          
SEQRES   9 C  315  TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS          
SEQRES  10 C  315  SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU          
SEQRES  11 C  315  THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU          
SEQRES  12 C  315  LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE          
SEQRES  13 C  315  GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU          
SEQRES  14 C  315  ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA          
SEQRES  15 C  315  GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG          
SEQRES  16 C  315  ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL          
SEQRES  17 C  315  MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS          
SEQRES  18 C  315  TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS          
SEQRES  19 C  315  SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR          
SEQRES  20 C  315  PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS          
SEQRES  21 C  315  TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU          
SEQRES  22 C  315  GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE          
SEQRES  23 C  315  ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL          
SEQRES  24 C  315  LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE          
SEQRES  25 C  315  ALA GLU ASN                                                  
SEQRES   1 D  146  GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP          
SEQRES   2 D  146  PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG          
SEQRES   3 D  146  GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU          
SEQRES   4 D  146  THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA          
SEQRES   5 D  146  ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU          
SEQRES   6 D  146  ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL          
SEQRES   7 D  146  TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER          
SEQRES   8 D  146  TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE          
SEQRES   9 D  146  PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER          
SEQRES  10 D  146  SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP          
SEQRES  11 D  146  TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP          
SEQRES  12 D  146  PRO SER LEU                                                  
SEQRES   1 E  343  ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA          
SEQRES   2 E  343  CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR          
SEQRES   3 E  343  LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL          
SEQRES   4 E  343  GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA          
SEQRES   5 E  343  ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL          
SEQRES   6 E  343  ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA          
SEQRES   7 E  343  ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR          
SEQRES   8 E  343  SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR          
SEQRES   9 E  343  GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS          
SEQRES  10 E  343  ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU          
SEQRES  11 E  343  LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU          
SEQRES  12 E  343  ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS          
SEQRES  13 E  343  ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER          
SEQRES  14 E  343  THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA          
SEQRES  15 E  343  ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR          
SEQRES  16 E  343  GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER          
SEQRES  17 E  343  VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS          
SEQRES  18 E  343  HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS          
SEQRES  19 E  343  ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE          
SEQRES  20 E  343  GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU          
SEQRES  21 E  343  GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER          
SEQRES  22 E  343  GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN          
SEQRES  23 E  343  GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL          
SEQRES  24 E  343  ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU          
SEQRES  25 E  343  GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS          
SEQRES  26 E  343  VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO          
SEQRES  27 E  343  VAL ASP VAL VAL SER                                          
SEQRES   1 F  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 F  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 F  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 F  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 F  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 F  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 F  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 F  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 F  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 F  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 F  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 G  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 G  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 G  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 G  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 G  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 G  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 G  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 G  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 G  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 G  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 G  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 G  146  LYS TYR HIS                                                  
SEQRES   1 H  315  CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU          
SEQRES   2 H  315  HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU          
SEQRES   3 H  315  ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU          
SEQRES   4 H  315  LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO          
SEQRES   5 H  315  GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA          
SEQRES   6 H  315  ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA          
SEQRES   7 H  315  LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS          
SEQRES   8 H  315  HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN          
SEQRES   9 H  315  TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS          
SEQRES  10 H  315  SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU          
SEQRES  11 H  315  THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU          
SEQRES  12 H  315  LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE          
SEQRES  13 H  315  GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU          
SEQRES  14 H  315  ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA          
SEQRES  15 H  315  GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG          
SEQRES  16 H  315  ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL          
SEQRES  17 H  315  MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS          
SEQRES  18 H  315  TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS          
SEQRES  19 H  315  SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR          
SEQRES  20 H  315  PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS          
SEQRES  21 H  315  TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU          
SEQRES  22 H  315  GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE          
SEQRES  23 H  315  ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL          
SEQRES  24 H  315  LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE          
SEQRES  25 H  315  ALA GLU ASN                                                  
SEQRES   1 I  146  GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP          
SEQRES   2 I  146  PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG          
SEQRES   3 I  146  GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU          
SEQRES   4 I  146  THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA          
SEQRES   5 I  146  ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU          
SEQRES   6 I  146  ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL          
SEQRES   7 I  146  TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER          
SEQRES   8 I  146  TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE          
SEQRES   9 I  146  PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER          
SEQRES  10 I  146  SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP          
SEQRES  11 I  146  TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP          
SEQRES  12 I  146  PRO SER LEU                                                  
SEQRES   1 J  343  ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA          
SEQRES   2 J  343  CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR          
SEQRES   3 J  343  LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL          
SEQRES   4 J  343  GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA          
SEQRES   5 J  343  ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL          
SEQRES   6 J  343  ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA          
SEQRES   7 J  343  ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR          
SEQRES   8 J  343  SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR          
SEQRES   9 J  343  GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS          
SEQRES  10 J  343  ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU          
SEQRES  11 J  343  LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU          
SEQRES  12 J  343  ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS          
SEQRES  13 J  343  ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER          
SEQRES  14 J  343  THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA          
SEQRES  15 J  343  ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR          
SEQRES  16 J  343  GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER          
SEQRES  17 J  343  VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS          
SEQRES  18 J  343  HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS          
SEQRES  19 J  343  ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE          
SEQRES  20 J  343  GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU          
SEQRES  21 J  343  GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER          
SEQRES  22 J  343  GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN          
SEQRES  23 J  343  GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL          
SEQRES  24 J  343  ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU          
SEQRES  25 J  343  GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS          
SEQRES  26 J  343  VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO          
SEQRES  27 J  343  VAL ASP VAL VAL SER                                          
SEQRES   1 K  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 K  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 K  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 K  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 K  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 K  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 K  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 K  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 K  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 K  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 K  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 L  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 L  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 L  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 L  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 L  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 L  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 L  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 L  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 L  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 L  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 L  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 L  146  LYS TYR HIS                                                  
SEQRES   1 M  315  CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU          
SEQRES   2 M  315  HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU          
SEQRES   3 M  315  ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU          
SEQRES   4 M  315  LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO          
SEQRES   5 M  315  GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA          
SEQRES   6 M  315  ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA          
SEQRES   7 M  315  LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS          
SEQRES   8 M  315  HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN          
SEQRES   9 M  315  TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS          
SEQRES  10 M  315  SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU          
SEQRES  11 M  315  THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU          
SEQRES  12 M  315  LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE          
SEQRES  13 M  315  GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU          
SEQRES  14 M  315  ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA          
SEQRES  15 M  315  GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG          
SEQRES  16 M  315  ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL          
SEQRES  17 M  315  MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS          
SEQRES  18 M  315  TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS          
SEQRES  19 M  315  SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR          
SEQRES  20 M  315  PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS          
SEQRES  21 M  315  TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU          
SEQRES  22 M  315  GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE          
SEQRES  23 M  315  ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL          
SEQRES  24 M  315  LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE          
SEQRES  25 M  315  ALA GLU ASN                                                  
SEQRES   1 N  146  GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP          
SEQRES   2 N  146  PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG          
SEQRES   3 N  146  GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU          
SEQRES   4 N  146  THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA          
SEQRES   5 N  146  ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU          
SEQRES   6 N  146  ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL          
SEQRES   7 N  146  TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER          
SEQRES   8 N  146  TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE          
SEQRES   9 N  146  PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER          
SEQRES  10 N  146  SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP          
SEQRES  11 N  146  TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP          
SEQRES  12 N  146  PRO SER LEU                                                  
SEQRES   1 O  343  ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA          
SEQRES   2 O  343  CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR          
SEQRES   3 O  343  LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL          
SEQRES   4 O  343  GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA          
SEQRES   5 O  343  ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL          
SEQRES   6 O  343  ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA          
SEQRES   7 O  343  ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR          
SEQRES   8 O  343  SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR          
SEQRES   9 O  343  GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS          
SEQRES  10 O  343  ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU          
SEQRES  11 O  343  LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU          
SEQRES  12 O  343  ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS          
SEQRES  13 O  343  ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER          
SEQRES  14 O  343  THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA          
SEQRES  15 O  343  ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR          
SEQRES  16 O  343  GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER          
SEQRES  17 O  343  VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS          
SEQRES  18 O  343  HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS          
SEQRES  19 O  343  ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE          
SEQRES  20 O  343  GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU          
SEQRES  21 O  343  GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER          
SEQRES  22 O  343  GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN          
SEQRES  23 O  343  GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL          
SEQRES  24 O  343  ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU          
SEQRES  25 O  343  GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS          
SEQRES  26 O  343  VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO          
SEQRES  27 O  343  VAL ASP VAL VAL SER                                          
SEQRES   1 P  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 P  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 P  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 P  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 P  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 P  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 P  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 P  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 P  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 P  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 P  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 Q  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 Q  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 Q  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 Q  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 Q  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 Q  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 Q  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 Q  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 Q  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 Q  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 Q  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 Q  146  LYS TYR HIS                                                  
SEQRES   1 R  315  CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU          
SEQRES   2 R  315  HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU          
SEQRES   3 R  315  ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU          
SEQRES   4 R  315  LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO          
SEQRES   5 R  315  GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA          
SEQRES   6 R  315  ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA          
SEQRES   7 R  315  LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS          
SEQRES   8 R  315  HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN          
SEQRES   9 R  315  TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS          
SEQRES  10 R  315  SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU          
SEQRES  11 R  315  THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU          
SEQRES  12 R  315  LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE          
SEQRES  13 R  315  GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU          
SEQRES  14 R  315  ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA          
SEQRES  15 R  315  GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG          
SEQRES  16 R  315  ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL          
SEQRES  17 R  315  MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS          
SEQRES  18 R  315  TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS          
SEQRES  19 R  315  SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR          
SEQRES  20 R  315  PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS          
SEQRES  21 R  315  TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU          
SEQRES  22 R  315  GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE          
SEQRES  23 R  315  ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL          
SEQRES  24 R  315  LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE          
SEQRES  25 R  315  ALA GLU ASN                                                  
SEQRES   1 S  146  GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP          
SEQRES   2 S  146  PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG          
SEQRES   3 S  146  GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU          
SEQRES   4 S  146  THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA          
SEQRES   5 S  146  ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU          
SEQRES   6 S  146  ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL          
SEQRES   7 S  146  TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER          
SEQRES   8 S  146  TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE          
SEQRES   9 S  146  PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER          
SEQRES  10 S  146  SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP          
SEQRES  11 S  146  TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP          
SEQRES  12 S  146  PRO SER LEU                                                  
SEQRES   1 T  343  ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA          
SEQRES   2 T  343  CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR          
SEQRES   3 T  343  LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL          
SEQRES   4 T  343  GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA          
SEQRES   5 T  343  ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL          
SEQRES   6 T  343  ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA          
SEQRES   7 T  343  ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR          
SEQRES   8 T  343  SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR          
SEQRES   9 T  343  GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS          
SEQRES  10 T  343  ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU          
SEQRES  11 T  343  LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU          
SEQRES  12 T  343  ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS          
SEQRES  13 T  343  ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER          
SEQRES  14 T  343  THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA          
SEQRES  15 T  343  ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR          
SEQRES  16 T  343  GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER          
SEQRES  17 T  343  VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS          
SEQRES  18 T  343  HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS          
SEQRES  19 T  343  ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE          
SEQRES  20 T  343  GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU          
SEQRES  21 T  343  GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER          
SEQRES  22 T  343  GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN          
SEQRES  23 T  343  GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL          
SEQRES  24 T  343  ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU          
SEQRES  25 T  343  GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS          
SEQRES  26 T  343  VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO          
SEQRES  27 T  343  VAL ASP VAL VAL SER                                          
SEQRES   1 U  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 U  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 U  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 U  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 U  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 U  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 U  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 U  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 U  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 U  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 U  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 V  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 V  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 V  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 V  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 V  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 V  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 V  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 V  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 V  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 V  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 V  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 V  146  LYS TYR HIS                                                  
SEQRES   1 W  315  CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU          
SEQRES   2 W  315  HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU          
SEQRES   3 W  315  ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU          
SEQRES   4 W  315  LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO          
SEQRES   5 W  315  GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA          
SEQRES   6 W  315  ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA          
SEQRES   7 W  315  LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS          
SEQRES   8 W  315  HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN          
SEQRES   9 W  315  TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS          
SEQRES  10 W  315  SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU          
SEQRES  11 W  315  THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU          
SEQRES  12 W  315  LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE          
SEQRES  13 W  315  GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU          
SEQRES  14 W  315  ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA          
SEQRES  15 W  315  GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG          
SEQRES  16 W  315  ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL          
SEQRES  17 W  315  MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS          
SEQRES  18 W  315  TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS          
SEQRES  19 W  315  SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR          
SEQRES  20 W  315  PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS          
SEQRES  21 W  315  TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU          
SEQRES  22 W  315  GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE          
SEQRES  23 W  315  ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL          
SEQRES  24 W  315  LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE          
SEQRES  25 W  315  ALA GLU ASN                                                  
SEQRES   1 X  146  GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP          
SEQRES   2 X  146  PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG          
SEQRES   3 X  146  GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU          
SEQRES   4 X  146  THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA          
SEQRES   5 X  146  ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU          
SEQRES   6 X  146  ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL          
SEQRES   7 X  146  TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER          
SEQRES   8 X  146  TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE          
SEQRES   9 X  146  PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER          
SEQRES  10 X  146  SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP          
SEQRES  11 X  146  TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP          
SEQRES  12 X  146  PRO SER LEU                                                  
SEQRES   1 Y  343  ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA          
SEQRES   2 Y  343  CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR          
SEQRES   3 Y  343  LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL          
SEQRES   4 Y  343  GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA          
SEQRES   5 Y  343  ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL          
SEQRES   6 Y  343  ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA          
SEQRES   7 Y  343  ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR          
SEQRES   8 Y  343  SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR          
SEQRES   9 Y  343  GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS          
SEQRES  10 Y  343  ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU          
SEQRES  11 Y  343  LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU          
SEQRES  12 Y  343  ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS          
SEQRES  13 Y  343  ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER          
SEQRES  14 Y  343  THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA          
SEQRES  15 Y  343  ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR          
SEQRES  16 Y  343  GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER          
SEQRES  17 Y  343  VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS          
SEQRES  18 Y  343  HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS          
SEQRES  19 Y  343  ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE          
SEQRES  20 Y  343  GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU          
SEQRES  21 Y  343  GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER          
SEQRES  22 Y  343  GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN          
SEQRES  23 Y  343  GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL          
SEQRES  24 Y  343  ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU          
SEQRES  25 Y  343  GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS          
SEQRES  26 Y  343  VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO          
SEQRES  27 Y  343  VAL ASP VAL VAL SER                                          
SEQRES   1 Z  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 Z  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 Z  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 Z  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 Z  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 Z  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 Z  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 Z  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 Z  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 Z  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 Z  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 1  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 1  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 1  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 1  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 1  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 1  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 1  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 1  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 1  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 1  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 1  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 1  146  LYS TYR HIS                                                  
SEQRES   1 2  315  CYS PRO LYS PRO PRO GLU ILE ALA HIS GLY TYR VAL GLU          
SEQRES   2 2  315  HIS SER VAL ARG TYR GLN CYS LYS ASN TYR TYR LYS LEU          
SEQRES   3 2  315  ARG THR GLU GLY ASP GLY VAL TYR THR LEU ASN ASN GLU          
SEQRES   4 2  315  LYS GLN TRP ILE ASN LYS ALA VAL GLY ASP LYS LEU PRO          
SEQRES   5 2  315  GLU CYS GLU ALA VAL CYS GLY LYS PRO LYS ASN PRO ALA          
SEQRES   6 2  315  ASN PRO VAL GLN ARG ILE LEU GLY GLY HIS LEU ASP ALA          
SEQRES   7 2  315  LYS GLY SER PHE PRO TRP GLN ALA LYS MET VAL SER HIS          
SEQRES   8 2  315  HIS ASN LEU THR THR GLY ALA THR LEU ILE ASN GLU GLN          
SEQRES   9 2  315  TRP LEU LEU THR THR ALA LYS ASN LEU PHE LEU ASN HIS          
SEQRES  10 2  315  SER GLU ASN ALA THR ALA LYS ASP ILE ALA PRO THR LEU          
SEQRES  11 2  315  THR LEU TYR VAL GLY LYS LYS GLN LEU VAL GLU ILE GLU          
SEQRES  12 2  315  LYS VAL VAL LEU HIS PRO ASN TYR SER GLN VAL ASP ILE          
SEQRES  13 2  315  GLY LEU ILE LYS LEU LYS GLN LYS VAL SER VAL ASN GLU          
SEQRES  14 2  315  ARG VAL MET PRO ILE CYS LEU PRO SER LYS ASP TYR ALA          
SEQRES  15 2  315  GLU VAL GLY ARG VAL GLY TYR VAL SER GLY TRP GLY ARG          
SEQRES  16 2  315  ASN ALA ASN PHE LYS PHE THR ASP HIS LEU LYS TYR VAL          
SEQRES  17 2  315  MET LEU PRO VAL ALA ASP GLN ASP GLN CYS ILE ARG HIS          
SEQRES  18 2  315  TYR GLU GLY SER THR VAL PRO GLU LYS LYS THR PRO LYS          
SEQRES  19 2  315  SER PRO VAL GLY VAL GLN PRO ILE LEU ASN GLU HIS THR          
SEQRES  20 2  315  PHE CYS ALA GLY MET SER LYS TYR GLN GLU ASP THR CYS          
SEQRES  21 2  315  TYR GLY ASP ALA GLY SER ALA PHE ALA VAL HIS ASP LEU          
SEQRES  22 2  315  GLU GLU ASP THR TRP TYR ALA THR GLY ILE LEU SER PHE          
SEQRES  23 2  315  ASP LYS SER CYS ALA VAL ALA GLU TYR GLY VAL TYR VAL          
SEQRES  24 2  315  LYS VAL THR SER ILE GLN ASP TRP VAL GLN LYS THR ILE          
SEQRES  25 2  315  ALA GLU ASN                                                  
SEQRES   1 3  146  GLY SER ALA ASP GLU SER LEU LYS ASP ALA ILE LYS ASP          
SEQRES   2 3  146  PRO ALA LEU GLU ASN LYS GLU HIS ASP ILE GLY PRO ARG          
SEQRES   3 3  146  GLU GLN VAL ASN PHE GLN LEU LEU ASP LYS ASN ASN GLU          
SEQRES   4 3  146  THR GLN TYR TYR HIS PHE PHE SER ILE LYS ASP PRO ALA          
SEQRES   5 3  146  ASP VAL TYR TYR THR LYS LYS LYS ALA GLU VAL GLU LEU          
SEQRES   6 3  146  ASP ILE ASN THR ALA SER THR TRP LYS LYS PHE GLU VAL          
SEQRES   7 3  146  TYR GLU ASN ASN GLN LYS LEU PRO VAL ARG LEU VAL SER          
SEQRES   8 3  146  TYR SER PRO VAL PRO GLU ASP HIS ALA TYR ILE ARG PHE          
SEQRES   9 3  146  PRO VAL SER ASP GLY THR GLN GLU LEU LYS ILE VAL SER          
SEQRES  10 3  146  SER THR GLN ILE ASP ASP GLY GLU GLU THR ASN TYR ASP          
SEQRES  11 3  146  TYR THR LYS LEU VAL PHE ALA LYS PRO ILE TYR ASN ASP          
SEQRES  12 3  146  PRO SER LEU                                                  
SEQRES   1 4  343  ALA GLU GLY LEU LYS THR LYS ASP GLU VAL GLU LYS ALA          
SEQRES   2 4  343  CYS HIS LEU ALA GLN GLN LEU LYS GLU VAL SER ILE THR          
SEQRES   3 4  343  LEU GLY VAL ILE TYR ARG THR THR GLU ARG HIS SER VAL          
SEQRES   4 4  343  GLN VAL GLU ALA HIS LYS THR ALA ILE ASP LYS HIS ALA          
SEQRES   5 4  343  ASP ALA VAL SER ARG ALA VAL GLU ALA LEU THR ARG VAL          
SEQRES   6 4  343  ASP VAL ALA LEU GLN ARG LEU LYS GLU LEU GLY LYS ALA          
SEQRES   7 4  343  ASN ASP THR LYS ALA VAL LYS ILE ILE GLU ASN ILE THR          
SEQRES   8 4  343  SER ALA ARG GLU ASN LEU ALA LEU PHE ASN ASN GLU THR          
SEQRES   9 4  343  GLN ALA VAL LEU THR ALA ARG ASP HIS VAL HIS LYS HIS          
SEQRES  10 4  343  ARG ALA ALA ALA LEU GLN GLY TRP SER ASP ALA LYS GLU          
SEQRES  11 4  343  LYS GLY ASP ALA ALA ALA GLU ASP VAL TRP VAL LEU LEU          
SEQRES  12 4  343  ASN ALA ALA LYS LYS GLY ASN GLY SER ALA ASP VAL LYS          
SEQRES  13 4  343  ALA ALA ALA GLU LYS CYS SER ARG TYR SER SER SER SER          
SEQRES  14 4  343  THR SER GLU THR GLU LEU GLN LYS ALA ILE ASP ALA ALA          
SEQRES  15 4  343  ALA ASN VAL GLY GLY LEU SER ALA HIS LYS SER LYS TYR          
SEQRES  16 4  343  GLY ASP VAL LEU ASN LYS PHE LYS LEU SER ASN ALA SER          
SEQRES  17 4  343  VAL GLY ALA VAL ARG ASP THR SER GLY ARG GLY GLY LYS          
SEQRES  18 4  343  HIS MET GLU LYS VAL ASN ASN VAL ALA LYS LEU LEU LYS          
SEQRES  19 4  343  ASP ALA GLU VAL SER LEU ALA ALA ALA ALA ALA GLU ILE          
SEQRES  20 4  343  GLU GLU VAL LYS ASN ALA HIS GLU THR LYS ALA GLN GLU          
SEQRES  21 4  343  GLU MET LYS ARG ASN GLY ASN PRO ILE GLU ASN GLU SER          
SEQRES  22 4  343  GLU THR ASN SER GLY GLY ASN ALA GLU SER GLN GLY ASN          
SEQRES  23 4  343  GLY ASP ARG GLU ASP LYS ASN ASP GLU GLN GLN GLN VAL          
SEQRES  24 4  343  ASP GLU GLU GLU THR LYS VAL GLU ASN GLY SER SER GLU          
SEQRES  25 4  343  GLU GLY SER CYS CYS GLY ASN GLU SER ASN GLY PRO HIS          
SEQRES  26 4  343  VAL MET LYS LYS ARG HIS GLY VAL GLU GLY PRO ARG PRO          
SEQRES  27 4  343  VAL ASP VAL VAL SER                                          
HET    NAG  a   1      14                                                       
HET    NAG  a   2      14                                                       
HET    NAG  b   1      14                                                       
HET    NAG  b   2      14                                                       
HET    NAG  c   1      14                                                       
HET    NAG  c   2      14                                                       
HET    NAG  d   1      14                                                       
HET    NAG  d   2      14                                                       
HET    NAG  e   1      14                                                       
HET    NAG  e   2      14                                                       
HET    NAG  f   1      14                                                       
HET    NAG  f   2      14                                                       
HET    NAG  g   1      14                                                       
HET    NAG  g   2      14                                                       
HET    NAG  h   1      14                                                       
HET    NAG  h   2      14                                                       
HET    NAG  i   1      14                                                       
HET    NAG  i   2      14                                                       
HET    NAG  j   1      14                                                       
HET    NAG  j   2      14                                                       
HET    HEM  A 201      43                                                       
HET    OXY  A 202       2                                                       
HET    HEM  B 201      43                                                       
HET    OXY  B 202       2                                                       
HET    NAG  C1001      14                                                       
HET    NAG  C1004      14                                                       
HET    NAG  E1001      14                                                       
HET    NAG  E1002      14                                                       
HET    HEM  F 201      43                                                       
HET    OXY  F 202       2                                                       
HET    HEM  G 201      43                                                       
HET    OXY  G 202       2                                                       
HET    NAG  H1001      14                                                       
HET    NAG  H1002      14                                                       
HET    NAG  J1001      14                                                       
HET    NAG  J1002      14                                                       
HET    HEM  K 201      43                                                       
HET    OXY  K 202       2                                                       
HET    HEM  L 201      43                                                       
HET    OXY  L 202       2                                                       
HET    NAG  M1001      14                                                       
HET    NAG  M1004      14                                                       
HET    NAG  O1001      14                                                       
HET    NAG  O1002      14                                                       
HET    HEM  P 201      43                                                       
HET    OXY  P 202       2                                                       
HET    HEM  Q 201      43                                                       
HET    OXY  Q 202       2                                                       
HET    NAG  R1001      14                                                       
HET    NAG  R1004      14                                                       
HET    NAG  T1001      14                                                       
HET    NAG  T1002      14                                                       
HET    HEM  U 201      43                                                       
HET    OXY  U 202       2                                                       
HET    HEM  V 201      43                                                       
HET    OXY  V 202       2                                                       
HET    NAG  W1001      14                                                       
HET    NAG  W1002      14                                                       
HET    NAG  Y1001      14                                                       
HET    NAG  Y1002      14                                                       
HET    HEM  Z 201      43                                                       
HET    OXY  Z 202       2                                                       
HET    HEM  1 201      43                                                       
HET    OXY  1 202       2                                                       
HET    NAG  21001      14                                                       
HET    NAG  41001      14                                                       
HET    NAG  41002      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     OXY OXYGEN MOLECULE                                                  
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
HETSYN     HEM HEME                                                             
FORMUL  31  NAG    43(C8 H15 N O6)                                              
FORMUL  41  HEM    12(C34 H32 FE N4 O4)                                         
FORMUL  42  OXY    12(O2)                                                       
HELIX    1 AA1 SER A    3  LYS A   16  1                                  14    
HELIX    2 AA2 VAL A   17  ALA A   19  5                                   3    
HELIX    3 AA3 HIS A   20  PHE A   36  1                                  17    
HELIX    4 AA4 PRO A   37  PHE A   43  5                                   7    
HELIX    5 AA5 SER A   52  HIS A   72  1                                  21    
HELIX    6 AA6 ASP A   75  HIS A   89  1                                  15    
HELIX    7 AA7 PRO A   95  LEU A  113  1                                  19    
HELIX    8 AA8 PRO A  114  PHE A  117  5                                   4    
HELIX    9 AA9 THR A  118  SER A  138  1                                  21    
HELIX   10 AB1 THR B    4  VAL B   18  1                                  15    
HELIX   11 AB2 GLU B   22  TYR B   35  1                                  14    
HELIX   12 AB3 THR B   38  GLU B   43  1                                   6    
HELIX   13 AB4 SER B   44  GLY B   46  5                                   3    
HELIX   14 AB5 THR B   50  ASN B   57  1                                   8    
HELIX   15 AB6 ASN B   57  HIS B   77  1                                  21    
HELIX   16 AB7 ASN B   80  PHE B   85  1                                   6    
HELIX   17 AB8 PHE B   85  ASP B   94  1                                  10    
HELIX   18 AB9 PRO B  100  GLY B  119  1                                  20    
HELIX   19 AC1 LYS B  120  PHE B  122  5                                   3    
HELIX   20 AC2 THR B  123  ALA B  142  1                                  20    
HELIX   21 AC3 HIS B  143  HIS B  146  5                                   4    
HELIX   22 AC4 THR C  196  PHE C  201  1                                   6    
HELIX   23 AC5 THR C  209  ALA C  214  1                                   6    
HELIX   24 AC6 ASP C  301  GLU C  310  1                                  10    
HELIX   25 AC7 ILE C  391  ALA C  400  1                                  10    
HELIX   26 AC8 SER D   89  ILE D   94  1                                   6    
HELIX   27 AC9 LYS D   95  GLU D  100  5                                   6    
HELIX   28 AD1 GLN D  124  ILE D  131  1                                   8    
HELIX   29 AD2 THR D  152  SER D  154  5                                   3    
HELIX   30 AD3 THR E   41  THR E   69  1                                  29    
HELIX   31 AD4 THR E   69  VAL E   90  1                                  22    
HELIX   32 AD5 VAL E   90  ALA E  103  1                                  14    
HELIX   33 AD6 GLN E  105  GLU E  109  5                                   5    
HELIX   34 AD7 LYS E  120  ILE E  125  1                                   6    
HELIX   35 AD8 ILE E  125  ALA E  181  1                                  57    
HELIX   36 AD9 ALA E  188  LYS E  196  1                                   9    
HELIX   37 AE1 SER E  206  ASN E  219  1                                  14    
HELIX   38 AE2 HIS E  226  ALA E  271  1                                  46    
HELIX   39 AE3 ALA E  271  ALA E  280  1                                  10    
HELIX   40 AE4 GLU E  281  GLU E  283  5                                   3    
HELIX   41 AE5 LYS E  286  GLN E  294  1                                   9    
HELIX   42 AE6 SER F    3  LYS F   16  1                                  14    
HELIX   43 AE7 VAL F   17  ALA F   19  5                                   3    
HELIX   44 AE8 HIS F   20  PHE F   36  1                                  17    
HELIX   45 AE9 PRO F   37  PHE F   43  5                                   7    
HELIX   46 AF1 SER F   52  HIS F   72  1                                  21    
HELIX   47 AF2 ASP F   75  HIS F   89  1                                  15    
HELIX   48 AF3 PRO F   95  LEU F  113  1                                  19    
HELIX   49 AF4 PRO F  114  PHE F  117  5                                   4    
HELIX   50 AF5 THR F  118  SER F  138  1                                  21    
HELIX   51 AF6 THR G    4  LYS G   17  1                                  14    
HELIX   52 AF7 GLU G   22  TYR G   35  1                                  14    
HELIX   53 AF8 THR G   38  GLU G   43  1                                   6    
HELIX   54 AF9 SER G   44  GLY G   46  5                                   3    
HELIX   55 AG1 THR G   50  ASN G   57  1                                   8    
HELIX   56 AG2 ASN G   57  HIS G   77  1                                  21    
HELIX   57 AG3 ASN G   80  PHE G   85  1                                   6    
HELIX   58 AG4 PHE G   85  ASP G   94  1                                  10    
HELIX   59 AG5 PRO G  100  GLY G  119  1                                  20    
HELIX   60 AG6 LYS G  120  PHE G  122  5                                   3    
HELIX   61 AG7 THR G  123  ALA G  142  1                                  20    
HELIX   62 AG8 HIS G  143  HIS G  146  5                                   4    
HELIX   63 AG9 THR H  196  PHE H  201  1                                   6    
HELIX   64 AH1 THR H  209  ALA H  214  1                                   6    
HELIX   65 AH2 PRO H  215  LEU H  217  5                                   3    
HELIX   66 AH3 ASP H  301  GLU H  310  1                                  10    
HELIX   67 AH4 ILE H  391  ALA H  400  1                                  10    
HELIX   68 AH5 SER I   89  ILE I   94  1                                   6    
HELIX   69 AH6 LYS I   95  GLU I  100  5                                   6    
HELIX   70 AH7 GLN I  124  ILE I  131  1                                   8    
HELIX   71 AH8 THR I  152  SER I  154  5                                   3    
HELIX   72 AH9 ASP J   43  THR J   69  1                                  27    
HELIX   73 AI1 THR J   69  VAL J   90  1                                  22    
HELIX   74 AI2 VAL J   90  ALA J  103  1                                  14    
HELIX   75 AI3 LYS J  120  ILE J  125  1                                   6    
HELIX   76 AI4 ILE J  125  VAL J  174  1                                  50    
HELIX   77 AI5 TRP J  175  ALA J  181  1                                   7    
HELIX   78 AI6 ALA J  188  LYS J  196  1                                   9    
HELIX   79 AI7 SER J  206  ASN J  219  1                                  14    
HELIX   80 AI8 HIS J  226  ALA J  271  1                                  46    
HELIX   81 AI9 ALA J  271  ALA J  280  1                                  10    
HELIX   82 AJ1 GLU J  281  GLU J  283  5                                   3    
HELIX   83 AJ2 LYS J  286  GLN J  294  1                                   9    
HELIX   84 AJ3 SER K    3  LYS K   16  1                                  14    
HELIX   85 AJ4 VAL K   17  ALA K   19  5                                   3    
HELIX   86 AJ5 HIS K   20  PHE K   36  1                                  17    
HELIX   87 AJ6 PRO K   37  PHE K   43  5                                   7    
HELIX   88 AJ7 SER K   52  HIS K   72  1                                  21    
HELIX   89 AJ8 ASP K   75  HIS K   89  1                                  15    
HELIX   90 AJ9 PRO K   95  LEU K  113  1                                  19    
HELIX   91 AK1 PRO K  114  PHE K  117  5                                   4    
HELIX   92 AK2 THR K  118  SER K  138  1                                  21    
HELIX   93 AK3 THR L    4  VAL L   18  1                                  15    
HELIX   94 AK4 GLU L   22  TYR L   35  1                                  14    
HELIX   95 AK5 THR L   38  GLU L   43  1                                   6    
HELIX   96 AK6 SER L   44  GLY L   46  5                                   3    
HELIX   97 AK7 THR L   50  ASN L   57  1                                   8    
HELIX   98 AK8 ASN L   57  HIS L   77  1                                  21    
HELIX   99 AK9 ASN L   80  PHE L   85  1                                   6    
HELIX  100 AL1 PHE L   85  ASP L   94  1                                  10    
HELIX  101 AL2 PRO L  100  GLY L  119  1                                  20    
HELIX  102 AL3 LYS L  120  PHE L  122  5                                   3    
HELIX  103 AL4 THR L  123  ALA L  142  1                                  20    
HELIX  104 AL5 HIS L  143  HIS L  146  5                                   4    
HELIX  105 AL6 THR M  196  PHE M  201  1                                   6    
HELIX  106 AL7 THR M  209  ALA M  214  1                                   6    
HELIX  107 AL8 ASP M  301  GLU M  310  1                                  10    
HELIX  108 AL9 ILE M  391  ALA M  400  1                                  10    
HELIX  109 AM1 SER N   89  ILE N   94  1                                   6    
HELIX  110 AM2 LYS N   95  GLU N  100  5                                   6    
HELIX  111 AM3 GLN N  124  ILE N  131  1                                   8    
HELIX  112 AM4 THR N  152  SER N  154  5                                   3    
HELIX  113 AM5 ASP O   43  THR O   69  1                                  27    
HELIX  114 AM6 THR O   69  VAL O   90  1                                  22    
HELIX  115 AM7 VAL O   90  ALA O  103  1                                  14    
HELIX  116 AM8 GLN O  105  GLU O  109  5                                   5    
HELIX  117 AM9 LYS O  120  ILE O  125  1                                   6    
HELIX  118 AN1 ILE O  125  ALA O  181  1                                  57    
HELIX  119 AN2 ALA O  188  LYS O  196  1                                   9    
HELIX  120 AN3 SER O  206  ASN O  219  1                                  14    
HELIX  121 AN4 HIS O  226  ALA O  271  1                                  46    
HELIX  122 AN5 ALA O  271  ALA O  280  1                                  10    
HELIX  123 AN6 GLU O  281  GLU O  283  5                                   3    
HELIX  124 AN7 LYS O  286  GLN O  294  1                                   9    
HELIX  125 AN8 SER P    3  LYS P   16  1                                  14    
HELIX  126 AN9 VAL P   17  ALA P   19  5                                   3    
HELIX  127 AO1 HIS P   20  PHE P   36  1                                  17    
HELIX  128 AO2 PRO P   37  PHE P   43  5                                   7    
HELIX  129 AO3 SER P   52  HIS P   72  1                                  21    
HELIX  130 AO4 ASP P   75  LEU P   80  1                                   6    
HELIX  131 AO5 LEU P   80  HIS P   89  1                                  10    
HELIX  132 AO6 PRO P   95  LEU P  113  1                                  19    
HELIX  133 AO7 PRO P  114  PHE P  117  5                                   4    
HELIX  134 AO8 THR P  118  SER P  138  1                                  21    
HELIX  135 AO9 THR Q    4  LYS Q   17  1                                  14    
HELIX  136 AP1 GLU Q   22  TYR Q   35  1                                  14    
HELIX  137 AP2 THR Q   38  GLU Q   43  1                                   6    
HELIX  138 AP3 SER Q   44  GLY Q   46  5                                   3    
HELIX  139 AP4 THR Q   50  ASN Q   57  1                                   8    
HELIX  140 AP5 ASN Q   57  HIS Q   77  1                                  21    
HELIX  141 AP6 ASN Q   80  PHE Q   85  1                                   6    
HELIX  142 AP7 PHE Q   85  ASP Q   94  1                                  10    
HELIX  143 AP8 PRO Q  100  GLY Q  119  1                                  20    
HELIX  144 AP9 LYS Q  120  PHE Q  122  5                                   3    
HELIX  145 AQ1 THR Q  123  ALA Q  142  1                                  20    
HELIX  146 AQ2 HIS Q  143  HIS Q  146  5                                   4    
HELIX  147 AQ3 THR R  196  PHE R  201  1                                   6    
HELIX  148 AQ4 THR R  209  ALA R  214  1                                   6    
HELIX  149 AQ5 ASP R  301  GLU R  310  1                                  10    
HELIX  150 AQ6 ILE R  391  ALA R  400  1                                  10    
HELIX  151 AQ7 SER S   89  ILE S   94  1                                   6    
HELIX  152 AQ8 LYS S   95  GLU S  100  5                                   6    
HELIX  153 AQ9 GLN S  124  ILE S  131  1                                   8    
HELIX  154 AR1 THR S  152  SER S  154  5                                   3    
HELIX  155 AR2 THR T   41  THR T   69  1                                  29    
HELIX  156 AR3 THR T   69  VAL T   90  1                                  22    
HELIX  157 AR4 VAL T   90  ALA T  103  1                                  14    
HELIX  158 AR5 LYS T  120  ILE T  125  1                                   6    
HELIX  159 AR6 ILE T  125  ALA T  181  1                                  57    
HELIX  160 AR7 ALA T  188  LYS T  196  1                                   9    
HELIX  161 AR8 SER T  206  ASN T  219  1                                  14    
HELIX  162 AR9 HIS T  226  ALA T  271  1                                  46    
HELIX  163 AS1 ALA T  271  ALA T  280  1                                  10    
HELIX  164 AS2 GLU T  281  GLU T  283  5                                   3    
HELIX  165 AS3 LYS T  286  GLN T  294  1                                   9    
HELIX  166 AS4 SER U    3  LYS U   16  1                                  14    
HELIX  167 AS5 VAL U   17  ALA U   19  5                                   3    
HELIX  168 AS6 HIS U   20  PHE U   36  1                                  17    
HELIX  169 AS7 PRO U   37  PHE U   43  5                                   7    
HELIX  170 AS8 SER U   52  HIS U   72  1                                  21    
HELIX  171 AS9 ASP U   75  LEU U   80  1                                   6    
HELIX  172 AT1 LEU U   80  HIS U   89  1                                  10    
HELIX  173 AT2 PRO U   95  LEU U  113  1                                  19    
HELIX  174 AT3 PRO U  114  PHE U  117  5                                   4    
HELIX  175 AT4 THR U  118  SER U  138  1                                  21    
HELIX  176 AT5 THR V    4  VAL V   18  1                                  15    
HELIX  177 AT6 GLU V   22  TYR V   35  1                                  14    
HELIX  178 AT7 THR V   38  GLU V   43  1                                   6    
HELIX  179 AT8 SER V   44  GLY V   46  5                                   3    
HELIX  180 AT9 THR V   50  ASN V   57  1                                   8    
HELIX  181 AU1 ASN V   57  HIS V   77  1                                  21    
HELIX  182 AU2 ASN V   80  PHE V   85  1                                   6    
HELIX  183 AU3 PHE V   85  ASP V   94  1                                  10    
HELIX  184 AU4 PRO V  100  GLY V  119  1                                  20    
HELIX  185 AU5 LYS V  120  PHE V  122  5                                   3    
HELIX  186 AU6 THR V  123  ALA V  142  1                                  20    
HELIX  187 AU7 HIS V  143  HIS V  146  5                                   4    
HELIX  188 AU8 THR W  196  PHE W  201  1                                   6    
HELIX  189 AU9 THR W  209  ALA W  214  1                                   6    
HELIX  190 AV1 ASP W  301  GLU W  310  1                                  10    
HELIX  191 AV2 ILE W  391  ALA W  400  1                                  10    
HELIX  192 AV3 SER X   89  ILE X   94  1                                   6    
HELIX  193 AV4 LYS X   95  GLU X  100  5                                   6    
HELIX  194 AV5 GLN X  124  ILE X  131  1                                   8    
HELIX  195 AV6 THR X  152  SER X  154  5                                   3    
HELIX  196 AV7 THR Y   41  THR Y   69  1                                  29    
HELIX  197 AV8 THR Y   69  VAL Y   90  1                                  22    
HELIX  198 AV9 VAL Y   90  ALA Y  103  1                                  14    
HELIX  199 AW1 LYS Y  120  ILE Y  125  1                                   6    
HELIX  200 AW2 ILE Y  125  ALA Y  181  1                                  57    
HELIX  201 AW3 ALA Y  188  LYS Y  196  1                                   9    
HELIX  202 AW4 SER Y  206  ASN Y  219  1                                  14    
HELIX  203 AW5 HIS Y  226  ALA Y  271  1                                  46    
HELIX  204 AW6 ALA Y  271  ALA Y  280  1                                  10    
HELIX  205 AW7 GLU Y  281  GLU Y  283  5                                   3    
HELIX  206 AW8 LYS Y  286  GLN Y  294  1                                   9    
HELIX  207 AW9 SER Z    3  LYS Z   16  1                                  14    
HELIX  208 AX1 VAL Z   17  ALA Z   19  5                                   3    
HELIX  209 AX2 HIS Z   20  PHE Z   36  1                                  17    
HELIX  210 AX3 PRO Z   37  PHE Z   43  5                                   7    
HELIX  211 AX4 SER Z   52  HIS Z   72  1                                  21    
HELIX  212 AX5 ASP Z   75  HIS Z   89  1                                  15    
HELIX  213 AX6 PRO Z   95  LEU Z  113  1                                  19    
HELIX  214 AX7 PRO Z  114  PHE Z  117  5                                   4    
HELIX  215 AX8 THR Z  118  SER Z  138  1                                  21    
HELIX  216 AX9 THR 1    4  VAL 1   18  1                                  15    
HELIX  217 AY1 GLU 1   22  TYR 1   35  1                                  14    
HELIX  218 AY2 THR 1   38  GLU 1   43  1                                   6    
HELIX  219 AY3 SER 1   44  GLY 1   46  5                                   3    
HELIX  220 AY4 THR 1   50  ASN 1   57  1                                   8    
HELIX  221 AY5 ASN 1   57  HIS 1   77  1                                  21    
HELIX  222 AY6 ASN 1   80  PHE 1   85  1                                   6    
HELIX  223 AY7 PHE 1   85  ASP 1   94  1                                  10    
HELIX  224 AY8 PRO 1  100  GLY 1  119  1                                  20    
HELIX  225 AY9 LYS 1  120  PHE 1  122  5                                   3    
HELIX  226 AZ1 THR 1  123  ALA 1  142  1                                  20    
HELIX  227 AZ2 HIS 1  143  HIS 1  146  5                                   4    
HELIX  228 AZ3 THR 2  196  PHE 2  201  1                                   6    
HELIX  229 AZ4 THR 2  209  ALA 2  214  1                                   6    
HELIX  230 AZ5 ASP 2  301  GLU 2  310  1                                  10    
HELIX  231 AZ6 ILE 2  391  ALA 2  400  1                                  10    
HELIX  232 AZ7 SER 3   89  ILE 3   94  1                                   6    
HELIX  233 AZ8 LYS 3   95  GLU 3  100  5                                   6    
HELIX  234 AZ9 GLN 3  124  ILE 3  131  1                                   8    
HELIX  235 BA1 THR 3  152  SER 3  154  5                                   3    
HELIX  236 BA2 THR 4   41  THR 4   69  1                                  29    
HELIX  237 BA3 THR 4   69  VAL 4   90  1                                  22    
HELIX  238 BA4 VAL 4   90  ALA 4  103  1                                  14    
HELIX  239 BA5 GLN 4  105  GLU 4  109  5                                   5    
HELIX  240 BA6 LYS 4  120  ILE 4  125  1                                   6    
HELIX  241 BA7 ILE 4  125  ALA 4  181  1                                  57    
HELIX  242 BA8 ALA 4  188  LYS 4  196  1                                   9    
HELIX  243 BA9 SER 4  206  ASN 4  219  1                                  14    
HELIX  244 BB1 HIS 4  226  ALA 4  271  1                                  46    
HELIX  245 BB2 ALA 4  271  ALA 4  280  1                                  10    
HELIX  246 BB3 GLU 4  281  GLU 4  283  5                                   3    
HELIX  247 BB4 LYS 4  286  GLN 4  294  1                                   9    
SHEET    1 AA1 6 TRP C 133  ILE C 134  0                                        
SHEET    2 AA1 6 VAL C 124  LEU C 127 -1  N  THR C 126   O  ILE C 134           
SHEET    3 AA1 6 GLY C 101  CYS C 111 -1  N  HIS C 105   O  LEU C 127           
SHEET    4 AA1 6 GLY H 101  CYS H 111 -1  O  TYR H 102   N  GLN C 110           
SHEET    5 AA1 6 VAL H 124  LEU H 127 -1  O  TYR H 125   N  VAL H 107           
SHEET    6 AA1 6 TRP H 133  ILE H 134 -1  O  ILE H 134   N  THR H 126           
SHEET    1 AA2 2 TYR C 115  ARG C 118  0                                        
SHEET    2 AA2 2 GLU C 144  ALA C 147 -1  O  GLU C 146   N  LYS C 116           
SHEET    1 AA3 7 GLN C 225  LEU C 226  0                                        
SHEET    2 AA3 7 THR C 218  VAL C 221 -1  N  VAL C 221   O  GLN C 225           
SHEET    3 AA3 7 GLN C 172  VAL C 176 -1  N  LYS C 174   O  TYR C 220           
SHEET    4 AA3 7 THR C 182  ASN C 189 -1  O  THR C 183   N  MET C 175           
SHEET    5 AA3 7 TRP C 192  THR C 195 -1  O  LEU C 194   N  THR C 186           
SHEET    6 AA3 7 GLY C 244  LEU C 248 -1  O  GLY C 244   N  THR C 195           
SHEET    7 AA3 7 ILE C 229  LEU C 234 -1  N  VAL C 233   O  LEU C 245           
SHEET    1 AA4 7 VAL C 274  GLY C 279  0                                        
SHEET    2 AA4 7 LYS C 293  ALA C 300 -1  O  VAL C 295   N  VAL C 277           
SHEET    3 AA4 7 THR C 334  ALA C 337 -1  O  CYS C 336   N  ALA C 300           
SHEET    4 AA4 7 GLY C 383  LYS C 387 -1  O  TYR C 385   N  PHE C 335           
SHEET    5 AA4 7 THR C 364  PHE C 373 -1  N  SER C 372   O  VAL C 384           
SHEET    6 AA4 7 ALA C 354  ASP C 359 -1  N  PHE C 355   O  GLY C 369           
SHEET    7 AA4 7 VAL C 274  GLY C 279 -1  N  TYR C 276   O  ALA C 356           
SHEET    1 AA5 5 ARG D 109  VAL D 112  0                                        
SHEET    2 AA5 5 ALA D 135  TYR D 138 -1  O  VAL D 137   N  GLU D 110           
SHEET    3 AA5 5 ALA D 144  ILE D 150 -1  O  GLU D 145   N  TYR D 138           
SHEET    4 AA5 5 HIS D 182  VAL D 189 -1  O  ALA D 183   N  ILE D 150           
SHEET    5 AA5 5 ARG D 171  SER D 176 -1  N  VAL D 173   O  TYR D 184           
SHEET    1 AA6 5 PHE D 114  LEU D 117  0                                        
SHEET    2 AA6 5 LYS D 216  PHE D 219 -1  O  LYS D 216   N  LEU D 117           
SHEET    3 AA6 5 GLU D 195  GLN D 203 -1  N  LEU D 196   O  LEU D 217           
SHEET    4 AA6 5 TRP D 156  GLU D 163 -1  N  TYR D 162   O  LYS D 197           
SHEET    5 AA6 5 GLN D 166  LYS D 167 -1  O  GLN D 166   N  GLU D 163           
SHEET    1 AA7 4 PHE D 114  LEU D 117  0                                        
SHEET    2 AA7 4 LYS D 216  PHE D 219 -1  O  LYS D 216   N  LEU D 117           
SHEET    3 AA7 4 GLU D 195  GLN D 203 -1  N  LEU D 196   O  LEU D 217           
SHEET    4 AA7 4 GLU D 209  TYR D 212 -1  O  TYR D 212   N  SER D 200           
SHEET    1 AA8 2 TYR H 115  ARG H 118  0                                        
SHEET    2 AA8 2 GLU H 144  ALA H 147 -1  O  GLU H 146   N  LYS H 116           
SHEET    1 AA9 7 GLN H 225  VAL H 227  0                                        
SHEET    2 AA9 7 THR H 218  VAL H 221 -1  N  VAL H 221   O  GLN H 225           
SHEET    3 AA9 7 GLN H 172  VAL H 176 -1  N  LYS H 174   O  TYR H 220           
SHEET    4 AA9 7 THR H 182  ASN H 189 -1  O  THR H 183   N  MET H 175           
SHEET    5 AA9 7 TRP H 192  THR H 195 -1  O  LEU H 194   N  THR H 186           
SHEET    6 AA9 7 GLY H 244  LEU H 248 -1  O  ILE H 246   N  LEU H 193           
SHEET    7 AA9 7 ILE H 229  LEU H 234 -1  N  VAL H 233   O  LEU H 245           
SHEET    1 AB1 7 VAL H 274  GLY H 279  0                                        
SHEET    2 AB1 7 LYS H 293  ALA H 300 -1  O  VAL H 295   N  VAL H 277           
SHEET    3 AB1 7 THR H 334  ALA H 337 -1  O  CYS H 336   N  ALA H 300           
SHEET    4 AB1 7 GLY H 383  LYS H 387 -1  O  TYR H 385   N  PHE H 335           
SHEET    5 AB1 7 THR H 364  PHE H 373 -1  N  SER H 372   O  VAL H 384           
SHEET    6 AB1 7 ALA H 354  ASP H 359 -1  N  PHE H 355   O  GLY H 369           
SHEET    7 AB1 7 VAL H 274  GLY H 279 -1  N  TYR H 276   O  ALA H 356           
SHEET    1 AB2 5 ARG I 109  VAL I 112  0                                        
SHEET    2 AB2 5 ALA I 135  TYR I 138 -1  O  VAL I 137   N  GLU I 110           
SHEET    3 AB2 5 ALA I 144  ILE I 150 -1  O  GLU I 145   N  TYR I 138           
SHEET    4 AB2 5 HIS I 182  VAL I 189 -1  O  ALA I 183   N  ILE I 150           
SHEET    5 AB2 5 ARG I 171  SER I 176 -1  N  VAL I 173   O  TYR I 184           
SHEET    1 AB3 5 PHE I 114  LEU I 117  0                                        
SHEET    2 AB3 5 LYS I 216  PHE I 219 -1  O  LYS I 216   N  LEU I 117           
SHEET    3 AB3 5 GLU I 195  GLN I 203 -1  N  LEU I 196   O  LEU I 217           
SHEET    4 AB3 5 TRP I 156  GLU I 163 -1  N  LYS I 157   O  SER I 201           
SHEET    5 AB3 5 GLN I 166  LYS I 167 -1  O  GLN I 166   N  GLU I 163           
SHEET    1 AB4 4 PHE I 114  LEU I 117  0                                        
SHEET    2 AB4 4 LYS I 216  PHE I 219 -1  O  LYS I 216   N  LEU I 117           
SHEET    3 AB4 4 GLU I 195  GLN I 203 -1  N  LEU I 196   O  LEU I 217           
SHEET    4 AB4 4 GLU I 209  TYR I 212 -1  O  TYR I 212   N  SER I 200           
SHEET    1 AB5 6 TRP M 133  ILE M 134  0                                        
SHEET    2 AB5 6 VAL M 124  LEU M 127 -1  N  THR M 126   O  ILE M 134           
SHEET    3 AB5 6 GLY M 101  CYS M 111 -1  N  VAL M 107   O  TYR M 125           
SHEET    4 AB5 6 GLY R 101  CYS R 111 -1  O  TYR R 102   N  GLN M 110           
SHEET    5 AB5 6 VAL R 124  LEU R 127 -1  O  TYR R 125   N  VAL R 107           
SHEET    6 AB5 6 TRP R 133  ILE R 134 -1  O  ILE R 134   N  THR R 126           
SHEET    1 AB6 2 TYR M 115  ARG M 118  0                                        
SHEET    2 AB6 2 GLU M 144  ALA M 147 -1  O  GLU M 146   N  LYS M 116           
SHEET    1 AB7 7 GLN M 225  LEU M 226  0                                        
SHEET    2 AB7 7 THR M 218  VAL M 221 -1  N  VAL M 221   O  GLN M 225           
SHEET    3 AB7 7 GLN M 172  VAL M 176 -1  N  VAL M 176   O  THR M 218           
SHEET    4 AB7 7 THR M 182  LEU M 187 -1  O  THR M 183   N  MET M 175           
SHEET    5 AB7 7 TRP M 192  THR M 195 -1  O  LEU M 194   N  THR M 186           
SHEET    6 AB7 7 GLY M 244  LEU M 248 -1  O  GLY M 244   N  THR M 195           
SHEET    7 AB7 7 ILE M 229  LEU M 234 -1  N  VAL M 233   O  LEU M 245           
SHEET    1 AB8 7 VAL M 274  GLY M 279  0                                        
SHEET    2 AB8 7 LYS M 293  ALA M 300 -1  O  VAL M 295   N  VAL M 277           
SHEET    3 AB8 7 THR M 334  ALA M 337 -1  O  CYS M 336   N  ALA M 300           
SHEET    4 AB8 7 GLY M 383  LYS M 387 -1  O  TYR M 385   N  PHE M 335           
SHEET    5 AB8 7 THR M 364  PHE M 373 -1  N  SER M 372   O  VAL M 384           
SHEET    6 AB8 7 ALA M 354  ASP M 359 -1  N  PHE M 355   O  GLY M 369           
SHEET    7 AB8 7 VAL M 274  GLY M 279 -1  N  TYR M 276   O  ALA M 356           
SHEET    1 AB9 5 ARG N 109  VAL N 112  0                                        
SHEET    2 AB9 5 ALA N 135  TYR N 138 -1  O  VAL N 137   N  GLU N 110           
SHEET    3 AB9 5 ALA N 144  ILE N 150 -1  O  GLU N 145   N  TYR N 138           
SHEET    4 AB9 5 HIS N 182  VAL N 189 -1  O  ALA N 183   N  ILE N 150           
SHEET    5 AB9 5 ARG N 171  SER N 176 -1  N  VAL N 173   O  TYR N 184           
SHEET    1 AC1 5 PHE N 114  LEU N 117  0                                        
SHEET    2 AC1 5 GLU N 209  PHE N 219 -1  O  LYS N 216   N  LEU N 117           
SHEET    3 AC1 5 GLU N 195  GLN N 203 -1  N  LEU N 196   O  LEU N 217           
SHEET    4 AC1 5 TRP N 156  GLU N 163 -1  N  LYS N 157   O  SER N 201           
SHEET    5 AC1 5 GLN N 166  LYS N 167 -1  O  GLN N 166   N  GLU N 163           
SHEET    1 AC2 2 TYR R 115  ARG R 118  0                                        
SHEET    2 AC2 2 GLU R 144  ALA R 147 -1  O  GLU R 146   N  LYS R 116           
SHEET    1 AC3 7 GLN R 225  VAL R 227  0                                        
SHEET    2 AC3 7 THR R 218  VAL R 221 -1  N  VAL R 221   O  GLN R 225           
SHEET    3 AC3 7 GLN R 172  VAL R 176 -1  N  LYS R 174   O  TYR R 220           
SHEET    4 AC3 7 THR R 182  LEU R 187 -1  O  THR R 183   N  MET R 175           
SHEET    5 AC3 7 TRP R 192  THR R 195 -1  O  LEU R 194   N  THR R 186           
SHEET    6 AC3 7 GLY R 244  LEU R 248 -1  O  GLY R 244   N  THR R 195           
SHEET    7 AC3 7 ILE R 229  LEU R 234 -1  N  VAL R 233   O  LEU R 245           
SHEET    1 AC4 7 VAL R 274  GLY R 279  0                                        
SHEET    2 AC4 7 LYS R 293  ALA R 300 -1  O  VAL R 295   N  VAL R 277           
SHEET    3 AC4 7 THR R 334  ALA R 337 -1  O  CYS R 336   N  ALA R 300           
SHEET    4 AC4 7 GLY R 383  LYS R 387 -1  O  TYR R 385   N  PHE R 335           
SHEET    5 AC4 7 THR R 364  PHE R 373 -1  N  SER R 372   O  VAL R 384           
SHEET    6 AC4 7 ALA R 354  ASP R 359 -1  N  PHE R 355   O  GLY R 369           
SHEET    7 AC4 7 VAL R 274  GLY R 279 -1  N  TYR R 276   O  ALA R 356           
SHEET    1 AC5 5 ARG S 109  VAL S 112  0                                        
SHEET    2 AC5 5 ALA S 135  TYR S 138 -1  O  VAL S 137   N  GLU S 110           
SHEET    3 AC5 5 ALA S 144  ILE S 150 -1  O  GLU S 145   N  TYR S 138           
SHEET    4 AC5 5 HIS S 182  VAL S 189 -1  O  ALA S 183   N  ILE S 150           
SHEET    5 AC5 5 ARG S 171  SER S 176 -1  N  VAL S 173   O  TYR S 184           
SHEET    1 AC6 5 PHE S 114  LEU S 117  0                                        
SHEET    2 AC6 5 LYS S 216  PHE S 219 -1  O  LYS S 216   N  LEU S 117           
SHEET    3 AC6 5 GLU S 195  GLN S 203 -1  N  LEU S 196   O  LEU S 217           
SHEET    4 AC6 5 TRP S 156  GLU S 163 -1  N  LYS S 157   O  SER S 201           
SHEET    5 AC6 5 GLN S 166  LYS S 167 -1  O  GLN S 166   N  GLU S 163           
SHEET    1 AC7 4 PHE S 114  LEU S 117  0                                        
SHEET    2 AC7 4 LYS S 216  PHE S 219 -1  O  LYS S 216   N  LEU S 117           
SHEET    3 AC7 4 GLU S 195  GLN S 203 -1  N  LEU S 196   O  LEU S 217           
SHEET    4 AC7 4 GLU S 209  TYR S 212 -1  O  TYR S 212   N  SER S 200           
SHEET    1 AC8 6 TRP W 133  ILE W 134  0                                        
SHEET    2 AC8 6 VAL W 124  LEU W 127 -1  N  THR W 126   O  ILE W 134           
SHEET    3 AC8 6 GLY W 101  CYS W 111 -1  N  VAL W 107   O  TYR W 125           
SHEET    4 AC8 6 GLY 2 101  CYS 2 111 -1  O  TYR 2 102   N  GLN W 110           
SHEET    5 AC8 6 VAL 2 124  LEU 2 127 -1  O  TYR 2 125   N  VAL 2 107           
SHEET    6 AC8 6 TRP 2 133  ILE 2 134 -1  O  ILE 2 134   N  THR 2 126           
SHEET    1 AC9 2 TYR W 115  ARG W 118  0                                        
SHEET    2 AC9 2 GLU W 144  ALA W 147 -1  O  GLU W 146   N  LYS W 116           
SHEET    1 AD1 7 GLN W 225  LEU W 226  0                                        
SHEET    2 AD1 7 THR W 218  VAL W 221 -1  N  VAL W 221   O  GLN W 225           
SHEET    3 AD1 7 GLN W 172  VAL W 176 -1  N  LYS W 174   O  TYR W 220           
SHEET    4 AD1 7 THR W 182  LEU W 187 -1  O  THR W 183   N  MET W 175           
SHEET    5 AD1 7 TRP W 192  THR W 195 -1  O  LEU W 194   N  THR W 186           
SHEET    6 AD1 7 GLY W 244  LEU W 248 -1  O  GLY W 244   N  THR W 195           
SHEET    7 AD1 7 ILE W 229  LEU W 234 -1  N  VAL W 233   O  LEU W 245           
SHEET    1 AD2 7 VAL W 274  GLY W 279  0                                        
SHEET    2 AD2 7 LYS W 293  ALA W 300 -1  O  VAL W 295   N  VAL W 277           
SHEET    3 AD2 7 THR W 334  ALA W 337 -1  O  CYS W 336   N  ALA W 300           
SHEET    4 AD2 7 GLY W 383  LYS W 387 -1  O  TYR W 385   N  PHE W 335           
SHEET    5 AD2 7 THR W 364  PHE W 373 -1  N  SER W 372   O  VAL W 384           
SHEET    6 AD2 7 ALA W 354  ASP W 359 -1  N  PHE W 355   O  GLY W 369           
SHEET    7 AD2 7 VAL W 274  GLY W 279 -1  N  TYR W 276   O  ALA W 356           
SHEET    1 AD3 5 ARG X 109  VAL X 112  0                                        
SHEET    2 AD3 5 ALA X 135  TYR X 138 -1  O  VAL X 137   N  GLU X 110           
SHEET    3 AD3 5 ALA X 144  ILE X 150 -1  O  GLU X 145   N  TYR X 138           
SHEET    4 AD3 5 HIS X 182  VAL X 189 -1  O  ALA X 183   N  ILE X 150           
SHEET    5 AD3 5 ARG X 171  SER X 176 -1  N  VAL X 173   O  TYR X 184           
SHEET    1 AD4 4 PHE X 114  LEU X 117  0                                        
SHEET    2 AD4 4 LYS X 216  PHE X 219 -1  O  LYS X 216   N  LEU X 117           
SHEET    3 AD4 4 GLU X 195  GLN X 203 -1  N  LEU X 196   O  LEU X 217           
SHEET    4 AD4 4 TRP X 156  TYR X 162 -1  N  LYS X 157   O  SER X 201           
SHEET    1 AD5 4 PHE X 114  LEU X 117  0                                        
SHEET    2 AD5 4 LYS X 216  PHE X 219 -1  O  LYS X 216   N  LEU X 117           
SHEET    3 AD5 4 GLU X 195  GLN X 203 -1  N  LEU X 196   O  LEU X 217           
SHEET    4 AD5 4 GLU X 209  TYR X 212 -1  O  TYR X 212   N  SER X 200           
SHEET    1 AD6 2 TYR 2 115  ARG 2 118  0                                        
SHEET    2 AD6 2 GLU 2 144  ALA 2 147 -1  O  GLU 2 146   N  LYS 2 116           
SHEET    1 AD7 7 GLN 2 225  VAL 2 227  0                                        
SHEET    2 AD7 7 THR 2 218  VAL 2 221 -1  N  VAL 2 221   O  GLN 2 225           
SHEET    3 AD7 7 GLN 2 172  VAL 2 176 -1  N  LYS 2 174   O  TYR 2 220           
SHEET    4 AD7 7 THR 2 182  LEU 2 187 -1  O  THR 2 183   N  MET 2 175           
SHEET    5 AD7 7 TRP 2 192  THR 2 195 -1  O  LEU 2 194   N  THR 2 186           
SHEET    6 AD7 7 GLY 2 244  LEU 2 248 -1  O  ILE 2 246   N  LEU 2 193           
SHEET    7 AD7 7 ILE 2 229  LEU 2 234 -1  N  VAL 2 233   O  LEU 2 245           
SHEET    1 AD8 7 VAL 2 274  GLY 2 279  0                                        
SHEET    2 AD8 7 LYS 2 293  ALA 2 300 -1  O  VAL 2 295   N  VAL 2 277           
SHEET    3 AD8 7 THR 2 334  ALA 2 337 -1  O  CYS 2 336   N  ALA 2 300           
SHEET    4 AD8 7 GLY 2 383  LYS 2 387 -1  O  TYR 2 385   N  PHE 2 335           
SHEET    5 AD8 7 THR 2 364  PHE 2 373 -1  N  SER 2 372   O  VAL 2 384           
SHEET    6 AD8 7 ALA 2 354  ASP 2 359 -1  N  PHE 2 355   O  GLY 2 369           
SHEET    7 AD8 7 VAL 2 274  GLY 2 279 -1  N  TYR 2 276   O  ALA 2 356           
SHEET    1 AD9 5 ARG 3 109  VAL 3 112  0                                        
SHEET    2 AD9 5 ALA 3 135  TYR 3 138 -1  O  VAL 3 137   N  GLU 3 110           
SHEET    3 AD9 5 ALA 3 144  ILE 3 150 -1  O  GLU 3 145   N  TYR 3 138           
SHEET    4 AD9 5 HIS 3 182  VAL 3 189 -1  O  ALA 3 183   N  ILE 3 150           
SHEET    5 AD9 5 ARG 3 171  SER 3 176 -1  N  VAL 3 173   O  TYR 3 184           
SHEET    1 AE1 5 PHE 3 114  LEU 3 117  0                                        
SHEET    2 AE1 5 GLU 3 209  PHE 3 219 -1  O  LYS 3 216   N  LEU 3 117           
SHEET    3 AE1 5 GLU 3 195  GLN 3 203 -1  N  LEU 3 196   O  LEU 3 217           
SHEET    4 AE1 5 TRP 3 156  GLU 3 163 -1  N  LYS 3 157   O  SER 3 201           
SHEET    5 AE1 5 GLN 3 166  LYS 3 167 -1  O  GLN 3 166   N  GLU 3 163           
SSBOND   1 CYS C   92    CYS H   92                          1555   1555  2.07  
SSBOND   2 CYS C  111    CYS C  145                          1555   1555  2.03  
SSBOND   3 CYS C  149    CYS C  262                          1555   1555  2.05  
SSBOND   4 CYS C  305    CYS C  336                          1555   1555  2.03  
SSBOND   5 CYS C  347    CYS C  377                          1555   1555  2.05  
SSBOND   6 CYS E   49    CYS E  197                          1555   1555  2.05  
SSBOND   7 CYS H  111    CYS H  145                          1555   1555  2.04  
SSBOND   8 CYS H  149    CYS H  262                          1555   1555  2.05  
SSBOND   9 CYS H  305    CYS H  336                          1555   1555  2.04  
SSBOND  10 CYS H  347    CYS H  377                          1555   1555  2.03  
SSBOND  11 CYS J   49    CYS J  197                          1555   1555  2.04  
SSBOND  12 CYS M   92    CYS R   92                          1555   1555  2.07  
SSBOND  13 CYS M  111    CYS M  145                          1555   1555  2.04  
SSBOND  14 CYS M  149    CYS M  262                          1555   1555  2.06  
SSBOND  15 CYS M  305    CYS M  336                          1555   1555  2.05  
SSBOND  16 CYS M  347    CYS M  377                          1555   1555  2.03  
SSBOND  17 CYS O   49    CYS O  197                          1555   1555  2.04  
SSBOND  18 CYS R  111    CYS R  145                          1555   1555  2.04  
SSBOND  19 CYS R  149    CYS R  262                          1555   1555  2.04  
SSBOND  20 CYS R  305    CYS R  336                          1555   1555  2.03  
SSBOND  21 CYS R  347    CYS R  377                          1555   1555  2.04  
SSBOND  22 CYS T   49    CYS T  197                          1555   1555  2.04  
SSBOND  23 CYS W   92    CYS 2   92                          1555   1555  2.04  
SSBOND  24 CYS W  111    CYS W  145                          1555   1555  2.03  
SSBOND  25 CYS W  149    CYS W  262                          1555   1555  2.04  
SSBOND  26 CYS W  305    CYS W  336                          1555   1555  2.02  
SSBOND  27 CYS W  347    CYS W  377                          1555   1555  2.02  
SSBOND  28 CYS Y   49    CYS Y  197                          1555   1555  2.03  
SSBOND  29 CYS 2  111    CYS 2  145                          1555   1555  2.03  
SSBOND  30 CYS 2  149    CYS 2  262                          1555   1555  2.04  
SSBOND  31 CYS 2  305    CYS 2  336                          1555   1555  2.02  
SSBOND  32 CYS 2  347    CYS 2  377                          1555   1555  2.04  
SSBOND  33 CYS 4   49    CYS 4  197                          1555   1555  2.03  
LINK         ND2 ASN C 180                 C1  NAG C1001     1555   1555  1.45  
LINK         ND2 ASN C 203                 C1  NAG a   1     1555   1555  1.46  
LINK         ND2 ASN C 207                 C1  NAG C1004     1555   1555  1.44  
LINK         ND2 ASN C 237                 C1  NAG b   1     1555   1555  1.43  
LINK         ND2 ASN E 137                 C1  NAG E1001     1555   1555  1.44  
LINK         ND2 ASN E 241                 C1  NAG E1002     1555   1555  1.45  
LINK         ND2 ASN H 180                 C1  NAG H1001     1555   1555  1.45  
LINK         ND2 ASN H 203                 C1  NAG H1002     1555   1555  1.44  
LINK         ND2 ASN H 237                 C1  NAG c   1     1555   1555  1.45  
LINK         ND2 ASN J 137                 C1  NAG J1001     1555   1555  1.45  
LINK         ND2 ASN J 241                 C1  NAG J1002     1555   1555  1.43  
LINK         ND2 ASN M 180                 C1  NAG M1001     1555   1555  1.44  
LINK         ND2 ASN M 203                 C1  NAG d   1     1555   1555  1.44  
LINK         ND2 ASN M 207                 C1  NAG M1004     1555   1555  1.45  
LINK         ND2 ASN M 237                 C1  NAG e   1     1555   1555  1.44  
LINK         ND2 ASN O 137                 C1  NAG O1001     1555   1555  1.44  
LINK         ND2 ASN O 241                 C1  NAG O1002     1555   1555  1.44  
LINK         ND2 ASN R 180                 C1  NAG R1001     1555   1555  1.45  
LINK         ND2 ASN R 203                 C1  NAG f   1     1555   1555  1.45  
LINK         ND2 ASN R 207                 C1  NAG R1004     1555   1555  1.43  
LINK         ND2 ASN R 237                 C1  NAG g   1     1555   1555  1.43  
LINK         ND2 ASN T 137                 C1  NAG T1001     1555   1555  1.44  
LINK         ND2 ASN T 241                 C1  NAG T1002     1555   1555  1.43  
LINK         ND2 ASN W 180                 C1  NAG W1001     1555   1555  1.46  
LINK         ND2 ASN W 203                 C1  NAG W1002     1555   1555  1.45  
LINK         ND2 ASN W 237                 C1  NAG h   1     1555   1555  1.43  
LINK         ND2 ASN Y 137                 C1  NAG Y1001     1555   1555  1.44  
LINK         ND2 ASN Y 241                 C1  NAG Y1002     1555   1555  1.44  
LINK         ND2 ASN 2 180                 C1  NAG 21001     1555   1555  1.45  
LINK         ND2 ASN 2 203                 C1  NAG i   1     1555   1555  1.46  
LINK         ND2 ASN 2 237                 C1  NAG j   1     1555   1555  1.43  
LINK         ND2 ASN 4 137                 C1  NAG 41001     1555   1555  1.44  
LINK         ND2 ASN 4 241                 C1  NAG 41002     1555   1555  1.44  
LINK         O4  NAG a   1                 C1  NAG a   2     1555   1555  1.46  
LINK         O4  NAG b   1                 C1  NAG b   2     1555   1555  1.44  
LINK         O4  NAG c   1                 C1  NAG c   2     1555   1555  1.44  
LINK         O4  NAG d   1                 C1  NAG d   2     1555   1555  1.47  
LINK         O4  NAG e   1                 C1  NAG e   2     1555   1555  1.42  
LINK         O4  NAG f   1                 C1  NAG f   2     1555   1555  1.47  
LINK         O4  NAG g   1                 C1  NAG g   2     1555   1555  1.47  
LINK         O4  NAG h   1                 C1  NAG h   2     1555   1555  1.44  
LINK         O4  NAG i   1                 C1  NAG i   2     1555   1555  1.46  
LINK         O4  NAG j   1                 C1  NAG j   2     1555   1555  1.44  
LINK         NE2 HIS A  87                FE   HEM A 201     1555   1555  2.38  
LINK        FE   HEM A 201                 O1  OXY A 202     1555   1555  2.39  
LINK        FE   HEM A 201                 O2  OXY A 202     1555   1555  2.67  
LINK         NE2 HIS B  92                FE   HEM B 201     1555   1555  2.44  
LINK        FE   HEM B 201                 O2  OXY B 202     1555   1555  2.69  
LINK         NE2 HIS F  87                FE   HEM F 201     1555   1555  2.43  
LINK        FE   HEM F 201                 O1  OXY F 202     1555   1555  2.49  
LINK        FE   HEM F 201                 O2  OXY F 202     1555   1555  2.66  
LINK         NE2 HIS G  92                FE   HEM G 201     1555   1555  2.42  
LINK        FE   HEM G 201                 O1  OXY G 202     1555   1555  2.57  
LINK         NE2 HIS K  87                FE   HEM K 201     1555   1555  2.37  
LINK        FE   HEM K 201                 O1  OXY K 202     1555   1555  2.34  
LINK         NE2 HIS L  92                FE   HEM L 201     1555   1555  2.53  
LINK        FE   HEM L 201                 O1  OXY L 202     1555   1555  2.59  
LINK         NE2 HIS P  87                FE   HEM P 201     1555   1555  2.37  
LINK        FE   HEM P 201                 O1  OXY P 202     1555   1555  2.43  
LINK        FE   HEM P 201                 O2  OXY P 202     1555   1555  2.41  
LINK         NE2 HIS Q  92                FE   HEM Q 201     1555   1555  2.40  
LINK        FE   HEM Q 201                 O2  OXY Q 202     1555   1555  2.67  
LINK         NE2 HIS U  87                FE   HEM U 201     1555   1555  2.47  
LINK        FE   HEM U 201                 O2  OXY U 202     1555   1555  2.64  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.58  
LINK        FE   HEM V 201                 O2  OXY V 202     1555   1555  2.66  
LINK         NE2 HIS Z  87                FE   HEM Z 201     1555   1555  2.42  
LINK        FE   HEM Z 201                 O1  OXY Z 202     1555   1555  2.70  
LINK        FE   HEM Z 201                 O2  OXY Z 202     1555   1555  2.50  
LINK         NE2 HIS 1  92                FE   HEM 1 201     1555   1555  2.53  
LINK        FE   HEM 1 201                 O1  OXY 1 202     1555   1555  2.55  
LINK        FE   HEM 1 201                 O2  OXY 1 202     1555   1555  2.50  
CISPEP   1 ASP D  133    PRO D  134          0        11.24                     
CISPEP   2 ASP I  133    PRO I  134          0        12.35                     
CISPEP   3 ASP N  133    PRO N  134          0         9.64                     
CISPEP   4 ASP S  133    PRO S  134          0        10.96                     
CISPEP   5 ASP X  133    PRO X  134          0        11.14                     
CISPEP   6 ASP 3  133    PRO 3  134          0        10.55                     
CRYST1  143.230  140.950  267.180  90.00  98.54  90.00 P 1 21 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006982  0.000000  0.001049        0.00000                         
SCALE2      0.000000  0.007095  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003785        0.00000                         
ATOM      1  N   VAL A   1      -1.691 -10.711  49.814  1.00 49.21           N  
ANISOU    1  N   VAL A   1     6749   7440   4509   1423  -1157    487       N  
ATOM      2  CA  VAL A   1      -2.043 -11.596  50.922  1.00 49.49           C  
ANISOU    2  CA  VAL A   1     6772   7469   4563   1430  -1159    494       C  
ATOM      3  C   VAL A   1      -3.128 -10.957  51.799  1.00 50.26           C  
ANISOU    3  C   VAL A   1     6890   7553   4655   1474  -1126    541       C  
ATOM      4  O   VAL A   1      -3.732 -11.644  52.638  1.00 50.60           O  
ANISOU    4  O   VAL A   1     6919   7586   4719   1485  -1124    562       O  
ATOM      5  CB  VAL A   1      -0.815 -11.956  51.773  1.00 49.85           C  
ANISOU    5  CB  VAL A   1     6828   7528   4584   1418  -1170    432       C  
ATOM      6  CG1 VAL A   1      -0.597 -10.922  52.879  1.00 50.83           C  
ANISOU    6  CG1 VAL A   1     6998   7654   4662   1454  -1143    419       C  
ATOM      7  CG2 VAL A   1      -0.935 -13.360  52.317  1.00 49.83           C  
ANISOU    7  CG2 VAL A   1     6795   7523   4616   1402  -1190    431       C  
ATOM      8  N   LEU A   2      -3.376  -9.656  51.589  1.00 44.55           N  
ANISOU    8  N   LEU A   2     6197   6826   3905   1500  -1099    560       N  
ATOM      9  CA  LEU A   2      -4.600  -8.966  52.051  1.00 45.42           C  
ANISOU    9  CA  LEU A   2     6321   6917   4018   1539  -1064    617       C  
ATOM     10  C   LEU A   2      -4.875  -9.068  53.536  1.00 46.13           C  
ANISOU   10  C   LEU A   2     6428   7002   4099   1569  -1046    623       C  
ATOM     11  O   LEU A   2      -5.679  -9.879  53.974  1.00 46.02           O  
ANISOU   11  O   LEU A   2     6388   6977   4120   1572  -1048    654       O  
ATOM     12  CB  LEU A   2      -5.789  -9.464  51.277  1.00 44.97           C  
ANISOU   12  CB  LEU A   2     6229   6845   4012   1532  -1069    673       C  
ATOM     13  CG  LEU A   2      -5.816  -8.665  49.977  1.00 44.86           C  
ANISOU   13  CG  LEU A   2     6220   6832   3993   1525  -1065    684       C  
ATOM     14  CD1 LEU A   2      -5.097  -9.401  48.848  1.00 43.77           C  
ANISOU   14  CD1 LEU A   2     6054   6706   3871   1482  -1102    652       C  
ATOM     15  CD2 LEU A   2      -7.248  -8.259  49.562  1.00 45.18           C  
ANISOU   15  CD2 LEU A   2     6251   6850   4064   1544  -1043    753       C  
ATOM     16  N   SER A   3      -4.121  -8.290  54.298  1.00 44.69           N  
ANISOU   16  N   SER A   3     6285   6826   3868   1587  -1031    588       N  
ATOM     17  CA  SER A   3      -4.273  -8.119  55.736  1.00 44.93           C  
ANISOU   17  CA  SER A   3     6342   6851   3879   1619  -1009    588       C  
ATOM     18  C   SER A   3      -5.548  -7.411  56.022  1.00 45.34           C  
ANISOU   18  C   SER A   3     6407   6883   3939   1657   -972    652       C  
ATOM     19  O   SER A   3      -6.175  -6.909  55.097  1.00 45.47           O  
ANISOU   19  O   SER A   3     6417   6890   3969   1657   -962    689       O  
ATOM     20  CB  SER A   3      -3.121  -7.289  56.304  1.00 45.18           C  
ANISOU   20  CB  SER A   3     6419   6893   3855   1627  -1002    534       C  
ATOM     21  OG  SER A   3      -3.335  -5.884  56.135  1.00 45.68           O  
ANISOU   21  OG  SER A   3     6509   6931   3915   1629   -955    543       O  
ATOM     22  N   PRO A   4      -5.943  -7.345  57.298  1.00 45.62           N  
ANISOU   22  N   PRO A   4     6460   6909   3965   1689   -949    665       N  
ATOM     23  CA  PRO A   4      -7.061  -6.456  57.600  1.00 46.50           C  
ANISOU   23  CA  PRO A   4     6591   6999   4078   1727   -907    722       C  
ATOM     24  C   PRO A   4      -6.862  -5.051  57.009  1.00 46.57           C  
ANISOU   24  C   PRO A   4     6626   6989   4079   1713   -871    712       C  
ATOM     25  O   PRO A   4      -7.780  -4.504  56.391  1.00 46.53           O  
ANISOU   25  O   PRO A   4     6616   6968   4095   1721   -850    761       O  
ATOM     26  CB  PRO A   4      -7.051  -6.406  59.125  1.00 47.75           C  
ANISOU   26  CB  PRO A   4     6775   7151   4217   1755   -886    713       C  
ATOM     27  CG  PRO A   4      -6.496  -7.684  59.534  1.00 47.47           C  
ANISOU   27  CG  PRO A   4     6714   7131   4192   1736   -920    679       C  
ATOM     28  CD  PRO A   4      -5.479  -8.053  58.499  1.00 46.22           C  
ANISOU   28  CD  PRO A   4     6538   6990   4032   1693   -958    633       C  
ATOM     29  N   ALA A   5      -5.664  -4.496  57.168  1.00 47.71           N  
ANISOU   29  N   ALA A   5     6796   7135   4198   1691   -866    649       N  
ATOM     30  CA  ALA A   5      -5.354  -3.173  56.632  1.00 47.93           C  
ANISOU   30  CA  ALA A   5     6847   7145   4219   1675   -833    633       C  
ATOM     31  C   ALA A   5      -5.675  -3.074  55.138  1.00 46.93           C  
ANISOU   31  C   ALA A   5     6698   7021   4113   1656   -844    659       C  
ATOM     32  O   ALA A   5      -6.456  -2.216  54.725  1.00 47.27           O  
ANISOU   32  O   ALA A   5     6748   7043   4170   1664   -811    699       O  
ATOM     33  CB  ALA A   5      -3.903  -2.841  56.876  1.00 48.10           C  
ANISOU   33  CB  ALA A   5     6891   7173   4213   1649   -837    558       C  
ATOM     34  N   ASP A   6      -5.085  -3.959  54.339  1.00 47.75           N  
ANISOU   34  N   ASP A   6     6775   7150   4218   1633   -891    638       N  
ATOM     35  CA  ASP A   6      -5.371  -3.994  52.918  1.00 46.84           C  
ANISOU   35  CA  ASP A   6     6636   7040   4121   1617   -907    662       C  
ATOM     36  C   ASP A   6      -6.854  -4.006  52.681  1.00 46.97           C  
ANISOU   36  C   ASP A   6     6638   7042   4166   1642   -894    737       C  
ATOM     37  O   ASP A   6      -7.361  -3.196  51.911  1.00 47.12           O  
ANISOU   37  O   ASP A   6     6660   7045   4197   1640   -870    765       O  
ATOM     38  CB  ASP A   6      -4.782  -5.233  52.262  1.00 45.73           C  
ANISOU   38  CB  ASP A   6     6464   6930   3980   1597   -965    639       C  
ATOM     39  CG  ASP A   6      -3.327  -5.432  52.593  1.00 45.58           C  
ANISOU   39  CG  ASP A   6     6456   6929   3933   1574   -984    566       C  
ATOM     40  OD1 ASP A   6      -2.481  -4.616  52.121  1.00 45.72           O  
ANISOU   40  OD1 ASP A   6     6491   6943   3938   1549   -971    527       O  
ATOM     41  OD2 ASP A   6      -3.025  -6.421  53.298  1.00 45.40           O  
ANISOU   41  OD2 ASP A   6     6424   6923   3903   1579  -1012    548       O  
ATOM     42  N   LYS A   7      -7.542  -4.934  53.355  1.00 46.31           N  
ANISOU   42  N   LYS A   7     6537   6964   4093   1668   -909    769       N  
ATOM     43  CA  LYS A   7      -8.949  -5.210  53.085  1.00 46.37           C  
ANISOU   43  CA  LYS A   7     6520   6958   4139   1685   -903    838       C  
ATOM     44  C   LYS A   7      -9.709  -3.901  53.241  1.00 47.36           C  
ANISOU   44  C   LYS A   7     6674   7057   4265   1707   -850    876       C  
ATOM     45  O   LYS A   7     -10.439  -3.502  52.335  1.00 47.22           O  
ANISOU   45  O   LYS A   7     6646   7028   4268   1707   -840    917       O  
ATOM     46  CB  LYS A   7      -9.500  -6.303  54.016  1.00 46.61           C  
ANISOU   46  CB  LYS A   7     6526   6982   4202   1689   -909    852       C  
ATOM     47  CG  LYS A   7      -9.058  -7.760  53.725  1.00 45.59           C  
ANISOU   47  CG  LYS A   7     6355   6866   4101   1651   -955    823       C  
ATOM     48  CD  LYS A   7      -9.663  -8.722  54.792  1.00 46.02           C  
ANISOU   48  CD  LYS A   7     6390   6912   4184   1660   -955    841       C  
ATOM     49  CE  LYS A   7      -8.973 -10.097  54.898  1.00 45.59           C  
ANISOU   49  CE  LYS A   7     6306   6872   4144   1627   -996    801       C  
ATOM     50  NZ  LYS A   7      -9.151 -10.882  53.661  1.00 44.93           N  
ANISOU   50  NZ  LYS A   7     6182   6788   4102   1590  -1027    808       N  
ATOM     51  N   THR A   8      -9.479  -3.215  54.363  1.00 44.76           N  
ANISOU   51  N   THR A   8     6377   6713   3916   1720   -813    856       N  
ATOM     52  CA  THR A   8     -10.088  -1.911  54.634  1.00 45.69           C  
ANISOU   52  CA  THR A   8     6524   6800   4036   1735   -757    882       C  
ATOM     53  C   THR A   8      -9.859  -0.928  53.490  1.00 45.81           C  
ANISOU   53  C   THR A   8     6546   6805   4053   1711   -742    875       C  
ATOM     54  O   THR A   8     -10.796  -0.359  52.957  1.00 46.07           O  
ANISOU   54  O   THR A   8     6576   6821   4106   1721   -719    924       O  
ATOM     55  CB  THR A   8      -9.536  -1.273  55.921  1.00 46.43           C  
ANISOU   55  CB  THR A   8     6656   6883   4103   1745   -725    844       C  
ATOM     56  OG1 THR A   8      -9.936  -2.028  57.064  1.00 46.49           O  
ANISOU   56  OG1 THR A   8     6660   6894   4110   1774   -729    860       O  
ATOM     57  CG2 THR A   8     -10.066   0.097  56.063  1.00 47.35           C  
ANISOU   57  CG2 THR A   8     6801   6969   4221   1757   -670    866       C  
ATOM     58  N   ASN A   9      -8.602  -0.742  53.106  1.00 46.69           N  
ANISOU   58  N   ASN A   9     6666   6929   4144   1680   -756    814       N  
ATOM     59  CA  ASN A   9      -8.245   0.169  52.020  1.00 46.51           C  
ANISOU   59  CA  ASN A   9     6651   6899   4121   1654   -743    802       C  
ATOM     60  C   ASN A   9      -8.996  -0.105  50.730  1.00 45.79           C  
ANISOU   60  C   ASN A   9     6531   6812   4057   1650   -760    848       C  
ATOM     61  O   ASN A   9      -9.536   0.814  50.112  1.00 46.25           O  
ANISOU   61  O   ASN A   9     6596   6852   4126   1651   -730    877       O  
ATOM     62  CB  ASN A   9      -6.747   0.093  51.751  1.00 45.93           C  
ANISOU   62  CB  ASN A   9     6583   6844   4024   1621   -766    730       C  
ATOM     63  CG  ASN A   9      -5.952   0.857  52.755  1.00 46.85           C  
ANISOU   63  CG  ASN A   9     6736   6948   4115   1619   -738    682       C  
ATOM     64  OD1 ASN A   9      -5.854   0.480  53.932  1.00 47.15           O  
ANISOU   64  OD1 ASN A   9     6784   6988   4142   1636   -738    669       O  
ATOM     65  ND2 ASN A   9      -5.381   1.962  52.308  1.00 47.40           N  
ANISOU   65  ND2 ASN A   9     6827   7006   4178   1599   -713    656       N  
ATOM     66  N   VAL A  10      -9.039  -1.373  50.326  1.00 46.01           N  
ANISOU   66  N   VAL A  10     6524   6863   4093   1647   -809    855       N  
ATOM     67  CA  VAL A  10      -9.687  -1.725  49.071  1.00 45.33           C  
ANISOU   67  CA  VAL A  10     6409   6782   4031   1643   -832    895       C  
ATOM     68  C   VAL A  10     -11.174  -1.386  49.109  1.00 46.04           C  
ANISOU   68  C   VAL A  10     6495   6850   4149   1671   -804    968       C  
ATOM     69  O   VAL A  10     -11.718  -0.860  48.134  1.00 46.10           O  
ANISOU   69  O   VAL A  10     6497   6847   4173   1668   -793   1000       O  
ATOM     70  CB  VAL A  10      -9.521  -3.195  48.739  1.00 44.24           C  
ANISOU   70  CB  VAL A  10     6236   6673   3900   1637   -890    891       C  
ATOM     71  CG1 VAL A  10      -9.872  -3.428  47.281  1.00 43.52           C  
ANISOU   71  CG1 VAL A  10     6119   6588   3829   1624   -915    917       C  
ATOM     72  CG2 VAL A  10      -8.099  -3.611  48.994  1.00 43.75           C  
ANISOU   72  CG2 VAL A  10     6180   6633   3811   1614   -916    821       C  
ATOM     73  N   LYS A  11     -11.827  -1.680  50.230  1.00 44.05           N  
ANISOU   73  N   LYS A  11     6245   6590   3902   1701   -791    995       N  
ATOM     74  CA  LYS A  11     -13.241  -1.348  50.363  1.00 44.52           C  
ANISOU   74  CA  LYS A  11     6302   6627   3987   1730   -762   1064       C  
ATOM     75  C   LYS A  11     -13.442   0.174  50.312  1.00 45.39           C  
ANISOU   75  C   LYS A  11     6443   6709   4093   1731   -707   1072       C  
ATOM     76  O   LYS A  11     -14.265   0.680  49.531  1.00 45.54           O  
ANISOU   76  O   LYS A  11     6456   6715   4133   1735   -691   1116       O  
ATOM     77  CB  LYS A  11     -13.821  -1.916  51.661  1.00 44.77           C  
ANISOU   77  CB  LYS A  11     6332   6655   4022   1762   -756   1088       C  
ATOM     78  CG  LYS A  11     -14.188  -3.355  51.584  1.00 44.01           C  
ANISOU   78  CG  LYS A  11     6188   6562   3973   1738   -791   1092       C  
ATOM     79  CD  LYS A  11     -14.827  -3.807  52.863  1.00 44.33           C  
ANISOU   79  CD  LYS A  11     6225   6590   4030   1759   -775   1112       C  
ATOM     80  CE  LYS A  11     -14.039  -3.356  54.052  1.00 44.99           C  
ANISOU   80  CE  LYS A  11     6350   6683   4063   1784   -759   1078       C  
ATOM     81  NZ  LYS A  11     -14.582  -3.961  55.288  1.00 45.40           N  
ANISOU   81  NZ  LYS A  11     6394   6726   4131   1802   -748   1093       N  
ATOM     82  N   ALA A  12     -12.667   0.882  51.138  1.00 44.85           N  
ANISOU   82  N   ALA A  12     6408   6634   3998   1728   -679   1026       N  
ATOM     83  CA  ALA A  12     -12.788   2.316  51.260  1.00 45.06           C  
ANISOU   83  CA  ALA A  12     6468   6634   4019   1730   -626   1028       C  
ATOM     84  C   ALA A  12     -12.480   2.964  49.919  1.00 45.03           C  
ANISOU   84  C   ALA A  12     6463   6629   4019   1703   -626   1020       C  
ATOM     85  O   ALA A  12     -13.102   3.927  49.533  1.00 45.18           O  
ANISOU   85  O   ALA A  12     6492   6626   4048   1708   -590   1052       O  
ATOM     86  CB  ALA A  12     -11.879   2.832  52.340  1.00 45.34           C  
ANISOU   86  CB  ALA A  12     6538   6665   4025   1729   -605    975       C  
ATOM     87  N   ALA A  13     -11.554   2.410  49.171  1.00 44.38           N  
ANISOU   87  N   ALA A  13     6366   6570   3928   1674   -665    980       N  
ATOM     88  CA  ALA A  13     -11.222   3.033  47.900  1.00 44.37           C  
ANISOU   88  CA  ALA A  13     6363   6567   3928   1649   -664    971       C  
ATOM     89  C   ALA A  13     -12.238   2.712  46.805  1.00 44.32           C  
ANISOU   89  C   ALA A  13     6327   6561   3950   1654   -679   1029       C  
ATOM     90  O   ALA A  13     -12.495   3.527  45.927  1.00 44.39           O  
ANISOU   90  O   ALA A  13     6341   6558   3968   1646   -659   1046       O  
ATOM     91  CB  ALA A  13      -9.806   2.609  47.460  1.00 44.20           C  
ANISOU   91  CB  ALA A  13     6337   6571   3886   1616   -699    906       C  
ATOM     92  N   TRP A  14     -12.788   1.504  46.846  1.00 47.47           N  
ANISOU   92  N   TRP A  14     6697   6974   4365   1667   -716   1057       N  
ATOM     93  CA  TRP A  14     -13.674   1.037  45.787  1.00 46.86           C  
ANISOU   93  CA  TRP A  14     6589   6900   4316   1671   -739   1108       C  
ATOM     94  C   TRP A  14     -15.068   1.606  46.011  1.00 47.58           C  
ANISOU   94  C   TRP A  14     6683   6964   4431   1700   -701   1174       C  
ATOM     95  O   TRP A  14     -15.884   1.700  45.082  1.00 47.37           O  
ANISOU   95  O   TRP A  14     6640   6931   4427   1703   -704   1220       O  
ATOM     96  CB  TRP A  14     -13.700  -0.494  45.745  1.00 45.93           C  
ANISOU   96  CB  TRP A  14     6438   6808   4207   1673   -795   1111       C  
ATOM     97  CG  TRP A  14     -14.406  -1.077  44.551  1.00 45.18           C  
ANISOU   97  CG  TRP A  14     6304   6709   4153   1657   -821   1143       C  
ATOM     98  CD1 TRP A  14     -15.619  -1.708  44.540  1.00 45.02           C  
ANISOU   98  CD1 TRP A  14     6251   6668   4187   1652   -823   1185       C  
ATOM     99  CD2 TRP A  14     -13.929  -1.098  43.198  1.00 44.46           C  
ANISOU   99  CD2 TRP A  14     6202   6631   4061   1631   -846   1126       C  
ATOM    100  NE1 TRP A  14     -15.922  -2.122  43.264  1.00 44.26           N  
ANISOU  100  NE1 TRP A  14     6125   6569   4122   1626   -848   1196       N  
ATOM    101  CE2 TRP A  14     -14.907  -1.746  42.423  1.00 43.91           C  
ANISOU  101  CE2 TRP A  14     6094   6546   4045   1614   -862   1161       C  
ATOM    102  CE3 TRP A  14     -12.778  -0.622  42.571  1.00 44.26           C  
ANISOU  102  CE3 TRP A  14     6195   6624   3997   1618   -854   1084       C  
ATOM    103  CZ2 TRP A  14     -14.770  -1.919  41.053  1.00 43.19           C  
ANISOU  103  CZ2 TRP A  14     5985   6459   3966   1589   -887   1157       C  
ATOM    104  CZ3 TRP A  14     -12.638  -0.803  41.216  1.00 43.53           C  
ANISOU  104  CZ3 TRP A  14     6084   6541   3914   1597   -880   1082       C  
ATOM    105  CH2 TRP A  14     -13.625  -1.447  40.470  1.00 43.00           C  
ANISOU  105  CH2 TRP A  14     5980   6458   3901   1582   -895   1117       C  
ATOM    106  N   GLY A  15     -15.320   1.993  47.262  1.00 48.21           N  
ANISOU  106  N   GLY A  15     6785   7029   4505   1721   -667   1179       N  
ATOM    107  CA  GLY A  15     -16.516   2.729  47.620  1.00 49.95           C  
ANISOU  107  CA  GLY A  15     7015   7221   4742   1748   -623   1236       C  
ATOM    108  C   GLY A  15     -16.436   4.079  46.952  1.00 50.95           C  
ANISOU  108  C   GLY A  15     7164   7329   4865   1735   -585   1233       C  
ATOM    109  O   GLY A  15     -17.261   4.411  46.115  1.00 51.74           O  
ANISOU  109  O   GLY A  15     7253   7418   4986   1739   -577   1279       O  
ATOM    110  N   LYS A  16     -15.372   4.818  47.223  1.00 50.55           N  
ANISOU  110  N   LYS A  16     7142   7277   4787   1717   -566   1177       N  
ATOM    111  CA  LYS A  16     -15.182   6.137  46.625  1.00 51.55           C  
ANISOU  111  CA  LYS A  16     7292   7387   4909   1703   -530   1170       C  
ATOM    112  C   LYS A  16     -15.245   6.067  45.094  1.00 50.85           C  
ANISOU  112  C   LYS A  16     7181   7306   4834   1684   -552   1183       C  
ATOM    113  O   LYS A  16     -15.225   7.089  44.419  1.00 51.62           O  
ANISOU  113  O   LYS A  16     7292   7389   4931   1673   -525   1185       O  
ATOM    114  CB  LYS A  16     -13.842   6.748  47.059  1.00 51.49           C  
ANISOU  114  CB  LYS A  16     7313   7380   4870   1682   -517   1100       C  
ATOM    115  CG  LYS A  16     -13.772   7.279  48.501  1.00 52.44           C  
ANISOU  115  CG  LYS A  16     7465   7484   4975   1701   -480   1086       C  
ATOM    116  CD  LYS A  16     -14.542   8.610  48.648  1.00 54.42           C  
ANISOU  116  CD  LYS A  16     7741   7703   5234   1717   -424   1120       C  
ATOM    117  CE  LYS A  16     -13.897   9.583  49.666  1.00 55.11           C  
ANISOU  117  CE  LYS A  16     7869   7774   5297   1718   -386   1079       C  
ATOM    118  NZ  LYS A  16     -13.998   9.169  51.119  1.00 56.04           N  
ANISOU  118  NZ  LYS A  16     7998   7890   5404   1744   -380   1074       N  
ATOM    119  N   VAL A  17     -15.259   4.860  44.545  1.00 50.37           N  
ANISOU  119  N   VAL A  17     7088   7269   4783   1679   -603   1188       N  
ATOM    120  CA  VAL A  17     -15.429   4.679  43.115  1.00 49.91           C  
ANISOU  120  CA  VAL A  17     7007   7218   4738   1664   -628   1206       C  
ATOM    121  C   VAL A  17     -16.921   4.739  42.787  1.00 50.08           C  
ANISOU  121  C   VAL A  17     7013   7222   4792   1688   -617   1280       C  
ATOM    122  O   VAL A  17     -17.346   5.400  41.836  1.00 50.22           O  
ANISOU  122  O   VAL A  17     7031   7229   4822   1684   -603   1306       O  
ATOM    123  CB  VAL A  17     -14.757   3.339  42.635  1.00 49.00           C  
ANISOU  123  CB  VAL A  17     6863   7135   4619   1648   -690   1177       C  
ATOM    124  CG1 VAL A  17     -15.120   3.006  41.213  1.00 48.51           C  
ANISOU  124  CG1 VAL A  17     6775   7081   4574   1640   -719   1203       C  
ATOM    125  CG2 VAL A  17     -13.251   3.432  42.754  1.00 48.87           C  
ANISOU  125  CG2 VAL A  17     6862   7134   4571   1621   -698   1103       C  
ATOM    126  N   GLY A  18     -17.718   4.066  43.603  1.00 54.10           N  
ANISOU  126  N   GLY A  18     7511   7729   5316   1715   -622   1315       N  
ATOM    127  CA  GLY A  18     -19.177   4.144  43.494  1.00 55.96           C  
ANISOU  127  CA  GLY A  18     7733   7946   5583   1741   -608   1388       C  
ATOM    128  C   GLY A  18     -19.763   3.769  42.143  1.00 55.92           C  
ANISOU  128  C   GLY A  18     7694   7937   5615   1720   -633   1412       C  
ATOM    129  O   GLY A  18     -19.234   2.877  41.469  1.00 54.31           O  
ANISOU  129  O   GLY A  18     7466   7752   5418   1694   -678   1383       O  
ATOM    130  N   ALA A  19     -20.821   4.470  41.735  1.00 51.97           N  
ANISOU  130  N   ALA A  19     7193   7410   5142   1726   -602   1460       N  
ATOM    131  CA  ALA A  19     -21.512   4.160  40.483  1.00 51.78           C  
ANISOU  131  CA  ALA A  19     7136   7377   5160   1703   -622   1483       C  
ATOM    132  C   ALA A  19     -20.612   4.268  39.254  1.00 51.44           C  
ANISOU  132  C   ALA A  19     7095   7355   5094   1685   -648   1454       C  
ATOM    133  O   ALA A  19     -20.946   3.816  38.157  1.00 51.17           O  
ANISOU  133  O   ALA A  19     7033   7319   5090   1663   -675   1462       O  
ATOM    134  CB  ALA A  19     -22.715   5.064  40.313  1.00 52.36           C  
ANISOU  134  CB  ALA A  19     7214   7420   5261   1715   -580   1536       C  
ATOM    135  N   HIS A  20     -19.453   4.871  39.432  1.00 54.74           N  
ANISOU  135  N   HIS A  20     7547   7794   5458   1694   -640   1420       N  
ATOM    136  CA  HIS A  20     -18.531   4.979  38.318  1.00 53.66           C  
ANISOU  136  CA  HIS A  20     7410   7673   5304   1668   -661   1383       C  
ATOM    137  C   HIS A  20     -17.790   3.653  38.094  1.00 51.69           C  
ANISOU  137  C   HIS A  20     7136   7453   5049   1652   -719   1346       C  
ATOM    138  O   HIS A  20     -17.125   3.461  37.065  1.00 50.85           O  
ANISOU  138  O   HIS A  20     7023   7366   4933   1632   -747   1322       O  
ATOM    139  CB  HIS A  20     -17.576   6.129  38.567  1.00 53.64           C  
ANISOU  139  CB  HIS A  20     7443   7664   5275   1650   -621   1336       C  
ATOM    140  CG  HIS A  20     -18.271   7.389  38.959  1.00 55.87           C  
ANISOU  140  CG  HIS A  20     7750   7915   5564   1665   -563   1367       C  
ATOM    141  ND1 HIS A  20     -18.724   8.304  38.033  1.00 57.01           N  
ANISOU  141  ND1 HIS A  20     7899   8044   5719   1661   -538   1394       N  
ATOM    142  CD2 HIS A  20     -18.625   7.871  40.174  1.00 57.33           C  
ANISOU  142  CD2 HIS A  20     7954   8081   5747   1684   -524   1376       C  
ATOM    143  CE1 HIS A  20     -19.307   9.305  38.665  1.00 59.07           C  
ANISOU  143  CE1 HIS A  20     8183   8277   5984   1677   -487   1418       C  
ATOM    144  NE2 HIS A  20     -19.259   9.067  39.964  1.00 59.31           N  
ANISOU  144  NE2 HIS A  20     8223   8306   6007   1691   -478   1408       N  
ATOM    145  N   ALA A  21     -17.952   2.721  39.030  1.00 51.74           N  
ANISOU  145  N   ALA A  21     7127   7460   5073   1651   -734   1339       N  
ATOM    146  CA  ALA A  21     -17.349   1.414  38.897  1.00 50.80           C  
ANISOU  146  CA  ALA A  21     6980   7361   4961   1626   -784   1300       C  
ATOM    147  C   ALA A  21     -17.588   0.865  37.499  1.00 50.15           C  
ANISOU  147  C   ALA A  21     6866   7279   4911   1598   -818   1305       C  
ATOM    148  O   ALA A  21     -16.678   0.353  36.867  1.00 49.28           O  
ANISOU  148  O   ALA A  21     6747   7190   4786   1577   -853   1265       O  
ATOM    149  CB  ALA A  21     -17.886   0.466  39.951  1.00 51.08           C  
ANISOU  149  CB  ALA A  21     6995   7387   5026   1628   -792   1307       C  
ATOM    150  N   GLY A  22     -18.784   1.022  36.975  1.00 51.55           N  
ANISOU  150  N   GLY A  22     7027   7429   5129   1597   -807   1351       N  
ATOM    151  CA  GLY A  22     -19.011   0.559  35.623  1.00 51.60           C  
ANISOU  151  CA  GLY A  22     7007   7435   5164   1571   -839   1355       C  
ATOM    152  C   GLY A  22     -18.159   1.278  34.596  1.00 51.27           C  
ANISOU  152  C   GLY A  22     6984   7411   5087   1567   -839   1335       C  
ATOM    153  O   GLY A  22     -17.512   0.669  33.759  1.00 50.57           O  
ANISOU  153  O   GLY A  22     6881   7339   4996   1544   -876   1304       O  
ATOM    154  N   GLU A  23     -18.160   2.598  34.683  1.00 55.23           N  
ANISOU  154  N   GLU A  23     7518   7907   5560   1590   -795   1352       N  
ATOM    155  CA  GLU A  23     -17.589   3.444  33.652  1.00 55.29           C  
ANISOU  155  CA  GLU A  23     7544   7926   5539   1588   -788   1345       C  
ATOM    156  C   GLU A  23     -16.056   3.343  33.674  1.00 53.50           C  
ANISOU  156  C   GLU A  23     7333   7732   5262   1581   -807   1288       C  
ATOM    157  O   GLU A  23     -15.400   3.476  32.630  1.00 53.15           O  
ANISOU  157  O   GLU A  23     7290   7703   5203   1566   -823   1267       O  
ATOM    158  CB  GLU A  23     -18.107   4.880  33.842  1.00 56.89           C  
ANISOU  158  CB  GLU A  23     7778   8109   5729   1614   -733   1383       C  
ATOM    159  CG  GLU A  23     -17.047   5.974  33.888  1.00 58.14           C  
ANISOU  159  CG  GLU A  23     7969   8267   5856   1598   -698   1338       C  
ATOM    160  CD  GLU A  23     -17.559   7.272  34.539  1.00 59.20           C  
ANISOU  160  CD  GLU A  23     8131   8371   5993   1609   -635   1359       C  
ATOM    161  OE1 GLU A  23     -18.686   7.236  35.130  1.00 58.91           O  
ANISOU  161  OE1 GLU A  23     8090   8316   5977   1635   -621   1409       O  
ATOM    162  OE2 GLU A  23     -16.823   8.314  34.455  1.00 60.48           O  
ANISOU  162  OE2 GLU A  23     8318   8526   6136   1593   -602   1326       O  
ATOM    163  N   TYR A  24     -15.490   3.066  34.850  1.00 53.81           N  
ANISOU  163  N   TYR A  24     7383   7780   5283   1585   -806   1257       N  
ATOM    164  CA  TYR A  24     -14.042   2.871  34.960  1.00 52.43           C  
ANISOU  164  CA  TYR A  24     7216   7626   5078   1561   -821   1189       C  
ATOM    165  C   TYR A  24     -13.655   1.583  34.278  1.00 51.44           C  
ANISOU  165  C   TYR A  24     7062   7528   4956   1549   -881   1172       C  
ATOM    166  O   TYR A  24     -12.673   1.539  33.536  1.00 50.97           O  
ANISOU  166  O   TYR A  24     7004   7488   4875   1530   -900   1133       O  
ATOM    167  CB  TYR A  24     -13.564   2.832  36.410  1.00 51.91           C  
ANISOU  167  CB  TYR A  24     7167   7560   4998   1564   -805   1158       C  
ATOM    168  CG  TYR A  24     -13.741   4.127  37.161  1.00 52.88           C  
ANISOU  168  CG  TYR A  24     7321   7654   5116   1571   -745   1162       C  
ATOM    169  CD1 TYR A  24     -13.594   4.154  38.536  1.00 54.35           C  
ANISOU  169  CD1 TYR A  24     7523   7835   5293   1581   -726   1147       C  
ATOM    170  CD2 TYR A  24     -14.069   5.329  36.496  1.00 52.71           C  
ANISOU  170  CD2 TYR A  24     7315   7613   5099   1568   -706   1183       C  
ATOM    171  CE1 TYR A  24     -13.750   5.322  39.242  1.00 55.63           C  
ANISOU  171  CE1 TYR A  24     7715   7972   5451   1588   -672   1150       C  
ATOM    172  CE2 TYR A  24     -14.229   6.505  37.196  1.00 53.97           C  
ANISOU  172  CE2 TYR A  24     7504   7747   5255   1574   -651   1186       C  
ATOM    173  CZ  TYR A  24     -14.069   6.496  38.574  1.00 55.46           C  
ANISOU  173  CZ  TYR A  24     7707   7930   5434   1585   -635   1169       C  
ATOM    174  OH  TYR A  24     -14.220   7.640  39.320  1.00 56.92           O  
ANISOU  174  OH  TYR A  24     7923   8090   5615   1593   -582   1171       O  
ATOM    175  N   GLY A  25     -14.437   0.539  34.532  1.00 54.01           N  
ANISOU  175  N   GLY A  25     7354   7839   5327   1538   -902   1187       N  
ATOM    176  CA  GLY A  25     -14.194  -0.756  33.936  1.00 53.32           C  
ANISOU  176  CA  GLY A  25     7233   7761   5266   1507   -951   1162       C  
ATOM    177  C   GLY A  25     -13.990  -0.667  32.437  1.00 53.70           C  
ANISOU  177  C   GLY A  25     7272   7814   5317   1489   -968   1159       C  
ATOM    178  O   GLY A  25     -13.138  -1.353  31.876  1.00 53.13           O  
ANISOU  178  O   GLY A  25     7188   7761   5238   1465  -1003   1119       O  
ATOM    179  N   ALA A  26     -14.754   0.198  31.790  1.00 55.58           N  
ANISOU  179  N   ALA A  26     7517   8035   5564   1500   -943   1200       N  
ATOM    180  CA  ALA A  26     -14.633   0.362  30.357  1.00 56.10           C  
ANISOU  180  CA  ALA A  26     7577   8106   5634   1486   -956   1200       C  
ATOM    181  C   ALA A  26     -13.426   1.210  30.015  1.00 55.76           C  
ANISOU  181  C   ALA A  26     7563   8087   5535   1490   -945   1168       C  
ATOM    182  O   ALA A  26     -12.703   0.912  29.065  1.00 55.47           O  
ANISOU  182  O   ALA A  26     7519   8068   5490   1471   -971   1139       O  
ATOM    183  CB  ALA A  26     -15.870   0.980  29.793  1.00 57.62           C  
ANISOU  183  CB  ALA A  26     7766   8271   5856   1495   -933   1255       C  
ATOM    184  N   GLU A  27     -13.219   2.286  30.768  1.00 58.63           N  
ANISOU  184  N   GLU A  27     7961   8451   5863   1516   -905   1174       N  
ATOM    185  CA  GLU A  27     -12.073   3.151  30.522  1.00 58.37           C  
ANISOU  185  CA  GLU A  27     7952   8424   5802   1496   -881   1128       C  
ATOM    186  C   GLU A  27     -10.809   2.319  30.666  1.00 56.96           C  
ANISOU  186  C   GLU A  27     7768   8275   5601   1477   -918   1068       C  
ATOM    187  O   GLU A  27      -9.890   2.437  29.854  1.00 56.84           O  
ANISOU  187  O   GLU A  27     7754   8274   5568   1457   -928   1033       O  
ATOM    188  CB  GLU A  27     -12.048   4.343  31.485  1.00 58.69           C  
ANISOU  188  CB  GLU A  27     8023   8440   5837   1497   -822   1122       C  
ATOM    189  CG  GLU A  27     -11.218   5.540  30.997  1.00 59.14           C  
ANISOU  189  CG  GLU A  27     8103   8490   5876   1476   -786   1091       C  
ATOM    190  CD  GLU A  27     -10.612   6.360  32.150  1.00 59.14           C  
ANISOU  190  CD  GLU A  27     8132   8478   5861   1470   -744   1057       C  
ATOM    191  OE1 GLU A  27     -10.147   7.497  31.923  1.00 59.84           O  
ANISOU  191  OE1 GLU A  27     8242   8554   5940   1457   -706   1040       O  
ATOM    192  OE2 GLU A  27     -10.585   5.860  33.291  1.00 58.52           O  
ANISOU  192  OE2 GLU A  27     8055   8401   5780   1479   -749   1046       O  
ATOM    193  N   ALA A  28     -10.786   1.460  31.689  1.00 56.95           N  
ANISOU  193  N   ALA A  28     7758   8281   5599   1485   -938   1059       N  
ATOM    194  CA  ALA A  28      -9.654   0.569  31.945  1.00 55.64           C  
ANISOU  194  CA  ALA A  28     7585   8142   5413   1470   -975   1005       C  
ATOM    195  C   ALA A  28      -9.389  -0.334  30.737  1.00 55.23           C  
ANISOU  195  C   ALA A  28     7505   8104   5377   1445  -1020    990       C  
ATOM    196  O   ALA A  28      -8.273  -0.359  30.219  1.00 54.58           O  
ANISOU  196  O   ALA A  28     7427   8044   5267   1430  -1035    948       O  
ATOM    197  CB  ALA A  28      -9.897  -0.258  33.190  1.00 55.07           C  
ANISOU  197  CB  ALA A  28     7504   8070   5351   1478   -987   1003       C  
ATOM    198  N   LEU A  29     -10.413  -1.043  30.267  1.00 56.98           N  
ANISOU  198  N   LEU A  29     7695   8305   5648   1435  -1036   1023       N  
ATOM    199  CA  LEU A  29     -10.264  -1.910  29.095  1.00 56.87           C  
ANISOU  199  CA  LEU A  29     7653   8295   5659   1405  -1074   1009       C  
ATOM    200  C   LEU A  29      -9.745  -1.139  27.908  1.00 57.28           C  
ANISOU  200  C   LEU A  29     7719   8360   5686   1404  -1068   1003       C  
ATOM    201  O   LEU A  29      -8.905  -1.617  27.165  1.00 56.75           O  
ANISOU  201  O   LEU A  29     7643   8310   5611   1381  -1095    967       O  
ATOM    202  CB  LEU A  29     -11.587  -2.560  28.698  1.00 57.63           C  
ANISOU  202  CB  LEU A  29     7720   8364   5811   1398  -1087   1051       C  
ATOM    203  CG  LEU A  29     -12.259  -3.590  29.582  1.00 57.50           C  
ANISOU  203  CG  LEU A  29     7682   8333   5834   1393  -1102   1062       C  
ATOM    204  CD1 LEU A  29     -13.741  -3.438  29.401  1.00 58.34           C  
ANISOU  204  CD1 LEU A  29     7776   8408   5982   1402  -1089   1118       C  
ATOM    205  CD2 LEU A  29     -11.801  -4.991  29.194  1.00 57.33           C  
ANISOU  205  CD2 LEU A  29     7630   8317   5835   1359  -1149   1028       C  
ATOM    206  N   GLU A  30     -10.273   0.057  27.717  1.00 63.86           N  
ANISOU  206  N   GLU A  30     8574   9183   6508   1427  -1032   1039       N  
ATOM    207  CA  GLU A  30      -9.915   0.826  26.541  1.00 64.63           C  
ANISOU  207  CA  GLU A  30     8683   9289   6584   1427  -1023   1040       C  
ATOM    208  C   GLU A  30      -8.423   1.050  26.509  1.00 63.98           C  
ANISOU  208  C   GLU A  30     8619   9237   6454   1420  -1029    987       C  
ATOM    209  O   GLU A  30      -7.798   0.828  25.480  1.00 64.10           O  
ANISOU  209  O   GLU A  30     8626   9266   6463   1402  -1049    964       O  
ATOM    210  CB  GLU A  30     -10.629   2.170  26.502  1.00 66.17           C  
ANISOU  210  CB  GLU A  30     8904   9469   6770   1454   -978   1087       C  
ATOM    211  CG  GLU A  30     -10.073   3.053  25.408  1.00 67.27           C  
ANISOU  211  CG  GLU A  30     9055   9609   6894   1441   -959   1074       C  
ATOM    212  CD  GLU A  30     -11.029   4.148  25.037  1.00 68.69           C  
ANISOU  212  CD  GLU A  30     9247   9762   7090   1452   -917   1122       C  
ATOM    213  OE1 GLU A  30     -11.017   4.550  23.850  1.00 69.39           O  
ANISOU  213  OE1 GLU A  30     9336   9852   7178   1447   -915   1131       O  
ATOM    214  OE2 GLU A  30     -11.793   4.595  25.932  1.00 69.21           O  
ANISOU  214  OE2 GLU A  30     9321   9805   7170   1466   -885   1150       O  
ATOM    215  N   ARG A  31      -7.876   1.485  27.645  1.00 60.68           N  
ANISOU  215  N   ARG A  31     8220   8814   6020   1416  -1001    959       N  
ATOM    216  CA  ARG A  31      -6.445   1.714  27.797  1.00 60.12           C  
ANISOU  216  CA  ARG A  31     8162   8757   5922   1392   -995    896       C  
ATOM    217  C   ARG A  31      -5.672   0.477  27.377  1.00 59.30           C  
ANISOU  217  C   ARG A  31     8038   8686   5806   1382  -1052    863       C  
ATOM    218  O   ARG A  31      -4.668   0.576  26.667  1.00 59.44           O  
ANISOU  218  O   ARG A  31     8059   8720   5806   1363  -1059    826       O  
ATOM    219  CB  ARG A  31      -6.084   2.061  29.244  1.00 59.58           C  
ANISOU  219  CB  ARG A  31     8113   8679   5847   1390   -966    871       C  
ATOM    220  CG  ARG A  31      -6.730   3.307  29.797  1.00 60.41           C  
ANISOU  220  CG  ARG A  31     8240   8751   5961   1399   -908    898       C  
ATOM    221  CD  ARG A  31      -6.072   3.706  31.123  1.00 59.95           C  
ANISOU  221  CD  ARG A  31     8203   8685   5889   1393   -881    859       C  
ATOM    222  NE  ARG A  31      -6.679   4.900  31.705  1.00 60.81           N  
ANISOU  222  NE  ARG A  31     8336   8763   6007   1403   -826    884       N  
ATOM    223  CZ  ARG A  31      -6.558   6.136  31.211  1.00 61.82           C  
ANISOU  223  CZ  ARG A  31     8481   8874   6132   1394   -785    886       C  
ATOM    224  NH1 ARG A  31      -7.161   7.143  31.821  1.00 62.65           N  
ANISOU  224  NH1 ARG A  31     8607   8951   6247   1405   -737    909       N  
ATOM    225  NH2 ARG A  31      -5.844   6.377  30.115  1.00 62.09           N  
ANISOU  225  NH2 ARG A  31     8514   8920   6158   1375   -791    865       N  
ATOM    226  N   MET A  32      -6.161  -0.686  27.818  1.00 61.76           N  
ANISOU  226  N   MET A  32     8326   8997   6143   1382  -1083    870       N  
ATOM    227  CA  MET A  32      -5.481  -1.962  27.584  1.00 61.06           C  
ANISOU  227  CA  MET A  32     8211   8919   6070   1350  -1125    829       C  
ATOM    228  C   MET A  32      -5.378  -2.279  26.093  1.00 61.61           C  
ANISOU  228  C   MET A  32     8263   8991   6155   1330  -1146    827       C  
ATOM    229  O   MET A  32      -4.329  -2.699  25.607  1.00 61.26           O  
ANISOU  229  O   MET A  32     8213   8965   6097   1308  -1167    784       O  
ATOM    230  CB  MET A  32      -6.193  -3.110  28.313  1.00 60.50           C  
ANISOU  230  CB  MET A  32     8113   8832   6041   1342  -1144    840       C  
ATOM    231  CG  MET A  32      -5.715  -4.484  27.865  1.00 60.32           C  
ANISOU  231  CG  MET A  32     8060   8814   6044   1307  -1186    807       C  
ATOM    232  SD  MET A  32      -6.105  -5.833  29.001  1.00 59.87           S  
ANISOU  232  SD  MET A  32     7978   8745   6024   1295  -1208    803       S  
ATOM    233  CE  MET A  32      -7.685  -6.408  28.393  1.00 60.46           C  
ANISOU  233  CE  MET A  32     8025   8789   6158   1292  -1219    860       C  
ATOM    234  N   PHE A  33      -6.465  -2.074  25.364  1.00 63.46           N  
ANISOU  234  N   PHE A  33     8489   9207   6417   1337  -1140    875       N  
ATOM    235  CA  PHE A  33      -6.452  -2.349  23.937  1.00 64.15           C  
ANISOU  235  CA  PHE A  33     8561   9294   6519   1320  -1160    876       C  
ATOM    236  C   PHE A  33      -5.567  -1.320  23.213  1.00 64.72           C  
ANISOU  236  C   PHE A  33     8657   9386   6546   1326  -1143    859       C  
ATOM    237  O   PHE A  33      -4.977  -1.613  22.171  1.00 65.15           O  
ANISOU  237  O   PHE A  33     8703   9452   6598   1308  -1162    838       O  
ATOM    238  CB  PHE A  33      -7.881  -2.342  23.371  1.00 65.20           C  
ANISOU  238  CB  PHE A  33     8680   9400   6693   1327  -1157    931       C  
ATOM    239  CG  PHE A  33      -8.800  -3.357  24.008  1.00 64.97           C  
ANISOU  239  CG  PHE A  33     8627   9349   6710   1319  -1175    950       C  
ATOM    240  CD1 PHE A  33      -8.494  -4.710  23.962  1.00 64.47           C  
ANISOU  240  CD1 PHE A  33     8536   9286   6672   1291  -1213    922       C  
ATOM    241  CD2 PHE A  33      -9.973  -2.961  24.636  1.00 65.48           C  
ANISOU  241  CD2 PHE A  33     8693   9391   6794   1340  -1151    996       C  
ATOM    242  CE1 PHE A  33      -9.344  -5.656  24.549  1.00 64.41           C  
ANISOU  242  CE1 PHE A  33     8507   9259   6708   1283  -1229    940       C  
ATOM    243  CE2 PHE A  33     -10.821  -3.887  25.217  1.00 65.44           C  
ANISOU  243  CE2 PHE A  33     8665   9366   6832   1334  -1167   1014       C  
ATOM    244  CZ  PHE A  33     -10.510  -5.234  25.176  1.00 64.90           C  
ANISOU  244  CZ  PHE A  33     8572   9300   6788   1305  -1206    986       C  
ATOM    245  N   LEU A  34      -5.489  -0.112  23.763  1.00 63.84           N  
ANISOU  245  N   LEU A  34     8577   9279   6400   1352  -1106    870       N  
ATOM    246  CA  LEU A  34      -4.689   0.950  23.165  1.00 64.52           C  
ANISOU  246  CA  LEU A  34     8688   9380   6446   1356  -1084    856       C  
ATOM    247  C   LEU A  34      -3.214   0.819  23.532  1.00 63.71           C  
ANISOU  247  C   LEU A  34     8592   9296   6318   1333  -1088    791       C  
ATOM    248  O   LEU A  34      -2.319   1.012  22.702  1.00 64.08           O  
ANISOU  248  O   LEU A  34     8642   9357   6350   1317  -1091    763       O  
ATOM    249  CB  LEU A  34      -5.198   2.313  23.606  1.00 65.28           C  
ANISOU  249  CB  LEU A  34     8807   9445   6552   1359  -1023    879       C  
ATOM    250  CG  LEU A  34      -6.232   2.980  22.726  1.00 66.60           C  
ANISOU  250  CG  LEU A  34     8975   9593   6736   1373  -1003    932       C  
ATOM    251  CD1 LEU A  34      -7.561   2.217  22.707  1.00 66.80           C  
ANISOU  251  CD1 LEU A  34     8981   9614   6786   1397  -1032    984       C  
ATOM    252  CD2 LEU A  34      -6.423   4.381  23.264  1.00 67.13           C  
ANISOU  252  CD2 LEU A  34     9068   9632   6807   1371   -940    941       C  
ATOM    253  N   SER A  35      -2.963   0.516  24.794  1.00 61.99           N  
ANISOU  253  N   SER A  35     8378   9078   6098   1331  -1087    769       N  
ATOM    254  CA  SER A  35      -1.601   0.364  25.252  1.00 61.27           C  
ANISOU  254  CA  SER A  35     8292   9002   5984   1310  -1092    708       C  
ATOM    255  C   SER A  35      -1.005  -0.958  24.760  1.00 60.81           C  
ANISOU  255  C   SER A  35     8211   8972   5921   1299  -1147    681       C  
ATOM    256  O   SER A  35       0.079  -0.953  24.196  1.00 60.98           O  
ANISOU  256  O   SER A  35     8235   9014   5922   1283  -1157    642       O  
ATOM    257  CB  SER A  35      -1.554   0.466  26.774  1.00 60.50           C  
ANISOU  257  CB  SER A  35     8207   8894   5888   1311  -1072    694       C  
ATOM    258  OG  SER A  35      -2.088   1.723  27.181  1.00 60.96           O  
ANISOU  258  OG  SER A  35     8286   8921   5955   1316  -1016    717       O  
ATOM    259  N   PHE A  36      -1.719  -2.073  24.940  1.00 56.92           N  
ANISOU  259  N   PHE A  36     6446   9595   5586   1310  -2457   -109       N  
ATOM    260  CA  PHE A  36      -1.202  -3.407  24.618  1.00 56.89           C  
ANISOU  260  CA  PHE A  36     6469   9609   5538   1319  -2436   -118       C  
ATOM    261  C   PHE A  36      -2.063  -4.149  23.600  1.00 57.07           C  
ANISOU  261  C   PHE A  36     6496   9657   5531   1323  -2435   -144       C  
ATOM    262  O   PHE A  36      -2.836  -5.040  23.962  1.00 57.03           O  
ANISOU  262  O   PHE A  36     6502   9660   5508   1318  -2429   -192       O  
ATOM    263  CB  PHE A  36      -1.102  -4.223  25.890  1.00 56.67           C  
ANISOU  263  CB  PHE A  36     6459   9573   5501   1312  -2424   -150       C  
ATOM    264  CG  PHE A  36      -0.600  -3.436  27.057  1.00 56.50           C  
ANISOU  264  CG  PHE A  36     6430   9526   5513   1304  -2429   -136       C  
ATOM    265  CD1 PHE A  36      -1.462  -2.992  28.032  1.00 56.43           C  
ANISOU  265  CD1 PHE A  36     6408   9503   5530   1291  -2440   -167       C  
ATOM    266  CD2 PHE A  36       0.733  -3.109  27.168  1.00 56.43           C  
ANISOU  266  CD2 PHE A  36     6424   9507   5510   1309  -2423    -91       C  
ATOM    267  CE1 PHE A  36      -0.996  -2.265  29.118  1.00 56.29           C  
ANISOU  267  CE1 PHE A  36     6382   9462   5542   1283  -2445   -154       C  
ATOM    268  CE2 PHE A  36       1.186  -2.392  28.237  1.00 56.28           C  
ANISOU  268  CE2 PHE A  36     6398   9466   5521   1301  -2427    -79       C  
ATOM    269  CZ  PHE A  36       0.316  -1.968  29.215  1.00 56.21           C  
ANISOU  269  CZ  PHE A  36     6377   9444   5537   1288  -2439   -111       C  
ATOM    270  N   PRO A  37      -1.898  -3.821  22.311  1.00 58.57           N  
ANISOU  270  N   PRO A  37     6679   9860   5714   1332  -2439   -114       N  
ATOM    271  CA  PRO A  37      -2.762  -4.251  21.200  1.00 58.78           C  
ANISOU  271  CA  PRO A  37     6704   9912   5718   1336  -2442   -133       C  
ATOM    272  C   PRO A  37      -2.938  -5.746  21.103  1.00 58.76           C  
ANISOU  272  C   PRO A  37     6727   9929   5672   1339  -2424   -171       C  
ATOM    273  O   PRO A  37      -3.816  -6.216  20.401  1.00 58.92           O  
ANISOU  273  O   PRO A  37     6746   9968   5672   1339  -2426   -197       O  
ATOM    274  CB  PRO A  37      -2.028  -3.731  19.955  1.00 58.95           C  
ANISOU  274  CB  PRO A  37     6719   9942   5736   1347  -2445    -83       C  
ATOM    275  CG  PRO A  37      -0.662  -3.449  20.397  1.00 58.80           C  
ANISOU  275  CG  PRO A  37     6708   9907   5728   1351  -2436    -43       C  
ATOM    276  CD  PRO A  37      -0.782  -3.004  21.826  1.00 58.60           C  
ANISOU  276  CD  PRO A  37     6676   9857   5733   1339  -2441    -57       C  
ATOM    277  N   THR A  38      -2.075  -6.492  21.776  1.00 63.02           N  
ANISOU  277  N   THR A  38     7287  10463   6196   1342  -2407   -171       N  
ATOM    278  CA  THR A  38      -2.122  -7.950  21.708  1.00 63.23           C  
ANISOU  278  CA  THR A  38     7338  10507   6179   1346  -2388   -205       C  
ATOM    279  C   THR A  38      -3.342  -8.473  22.470  1.00 62.40           C  
ANISOU  279  C   THR A  38     7235  10401   6074   1334  -2390   -263       C  
ATOM    280  O   THR A  38      -3.865  -9.544  22.158  1.00 63.03           O  
ANISOU  280  O   THR A  38     7327  10499   6121   1335  -2381   -299       O  
ATOM    281  CB  THR A  38      -0.853  -8.591  22.275  1.00 62.65           C  
ANISOU  281  CB  THR A  38     7286  10427   6090   1352  -2369   -189       C  
ATOM    282  OG1 THR A  38      -1.150  -9.117  23.572  1.00 62.09           O  
ANISOU  282  OG1 THR A  38     7225  10345   6022   1343  -2363   -226       O  
ATOM    283  CG2 THR A  38       0.277  -7.558  22.373  1.00 63.57           C  
ANISOU  283  CG2 THR A  38     7393  10526   6234   1355  -2373   -133       C  
ATOM    284  N   THR A  39      -3.821  -7.707  23.445  1.00 63.28           N  
ANISOU  284  N   THR A  39     7331  10491   6220   1322  -2403   -273       N  
ATOM    285  CA  THR A  39      -4.963  -8.166  24.218  1.00 62.52           C  
ANISOU  285  CA  THR A  39     7236  10392   6125   1310  -2404   -328       C  
ATOM    286  C   THR A  39      -6.238  -8.187  23.391  1.00 63.69           C  
ANISOU  286  C   THR A  39     7373  10557   6268   1307  -2415   -354       C  
ATOM    287  O   THR A  39      -7.226  -8.774  23.807  1.00 63.41           O  
ANISOU  287  O   THR A  39     7342  10525   6227   1299  -2414   -403       O  
ATOM    288  CB  THR A  39      -5.202  -7.299  25.460  1.00 61.75           C  
ANISOU  288  CB  THR A  39     7125  10269   6069   1298  -2416   -333       C  
ATOM    289  OG1 THR A  39      -5.581  -5.979  25.062  1.00 61.87           O  
ANISOU  289  OG1 THR A  39     7113  10277   6118   1296  -2436   -309       O  
ATOM    290  CG2 THR A  39      -3.953  -7.209  26.275  1.00 61.56           C  
ANISOU  290  CG2 THR A  39     7110  10228   6052   1300  -2406   -305       C  
ATOM    291  N   LYS A  40      -6.212  -7.552  22.223  1.00 64.27           N  
ANISOU  291  N   LYS A  40     7433  10642   6345   1314  -2425   -323       N  
ATOM    292  CA  LYS A  40      -7.388  -7.501  21.358  1.00 65.59           C  
ANISOU  292  CA  LYS A  40     7587  10826   6507   1312  -2436   -344       C  
ATOM    293  C   LYS A  40      -7.718  -8.879  20.735  1.00 66.68           C  
ANISOU  293  C   LYS A  40     7746  10990   6600   1316  -2421   -378       C  
ATOM    294  O   LYS A  40      -8.867  -9.136  20.335  1.00 67.69           O  
ANISOU  294  O   LYS A  40     7868  11131   6719   1310  -2427   -412       O  
ATOM    295  CB  LYS A  40      -7.196  -6.449  20.256  1.00 66.90           C  
ANISOU  295  CB  LYS A  40     7733  10998   6687   1318  -2450   -298       C  
ATOM    296  CG  LYS A  40      -6.746  -5.084  20.772  1.00 66.02           C  
ANISOU  296  CG  LYS A  40     7602  10861   6620   1316  -2464   -260       C  
ATOM    297  CD  LYS A  40      -7.032  -3.973  19.775  1.00 67.43           C  
ANISOU  297  CD  LYS A  40     7757  11045   6820   1318  -2482   -227       C  
ATOM    298  CE  LYS A  40      -6.647  -4.345  18.344  1.00 69.18           C  
ANISOU  298  CE  LYS A  40     7985  11292   7010   1330  -2476   -205       C  
ATOM    299  NZ  LYS A  40      -7.163  -3.339  17.347  1.00 70.79           N  
ANISOU  299  NZ  LYS A  40     8163  11503   7232   1331  -2495   -180       N  
ATOM    300  N   THR A  41      -6.724  -9.772  20.680  1.00 69.96           N  
ANISOU  300  N   THR A  41     8184  11413   6985   1325  -2402   -369       N  
ATOM    301  CA  THR A  41      -6.902 -11.082  20.031  1.00 71.13           C  
ANISOU  301  CA  THR A  41     8352  11586   7088   1330  -2387   -397       C  
ATOM    302  C   THR A  41      -7.803 -12.026  20.836  1.00 70.42           C  
ANISOU  302  C   THR A  41     8273  11495   6987   1320  -2380   -457       C  
ATOM    303  O   THR A  41      -8.097 -13.151  20.407  1.00 71.41           O  
ANISOU  303  O   THR A  41     8416  11640   7078   1322  -2367   -487       O  
ATOM    304  CB  THR A  41      -5.558 -11.786  19.801  1.00 71.40           C  
ANISOU  304  CB  THR A  41     8408  11627   7094   1343  -2367   -372       C  
ATOM    305  OG1 THR A  41      -5.161 -12.463  20.999  1.00 69.98           O  
ANISOU  305  OG1 THR A  41     8246  11434   6911   1340  -2353   -391       O  
ATOM    306  CG2 THR A  41      -4.508 -10.774  19.403  1.00 71.48           C  
ANISOU  306  CG2 THR A  41     8408  11629   7123   1351  -2373   -311       C  
ATOM    307  N   TYR A  42      -8.193 -11.590  22.026  1.00 68.96           N  
ANISOU  307  N   TYR A  42     8081  11287   6833   1308  -2386   -473       N  
ATOM    308  CA  TYR A  42      -9.156 -12.337  22.811  1.00 68.27           C  
ANISOU  308  CA  TYR A  42     8002  11197   6741   1297  -2382   -530       C  
ATOM    309  C   TYR A  42     -10.609 -11.871  22.537  1.00 68.85           C  
ANISOU  309  C   TYR A  42     8056  11274   6831   1286  -2399   -558       C  
ATOM    310  O   TYR A  42     -11.579 -12.573  22.869  1.00 68.90           O  
ANISOU  310  O   TYR A  42     8068  11283   6828   1277  -2396   -608       O  
ATOM    311  CB  TYR A  42      -8.797 -12.218  24.289  1.00 66.37           C  
ANISOU  311  CB  TYR A  42     7767  10930   6522   1290  -2378   -536       C  
ATOM    312  CG  TYR A  42      -7.613 -13.078  24.666  1.00 66.00           C  
ANISOU  312  CG  TYR A  42     7744  10883   6451   1298  -2357   -525       C  
ATOM    313  CD1 TYR A  42      -7.771 -14.193  25.490  1.00 65.49           C  
ANISOU  313  CD1 TYR A  42     7699  10816   6368   1293  -2342   -566       C  
ATOM    314  CD2 TYR A  42      -6.347 -12.801  24.185  1.00 66.34           C  
ANISOU  314  CD2 TYR A  42     7790  10928   6488   1311  -2353   -474       C  
ATOM    315  CE1 TYR A  42      -6.711 -14.996  25.829  1.00 65.32           C  
ANISOU  315  CE1 TYR A  42     7700  10796   6324   1301  -2323   -556       C  
ATOM    316  CE2 TYR A  42      -5.266 -13.607  24.530  1.00 66.16           C  
ANISOU  316  CE2 TYR A  42     7789  10905   6443   1319  -2333   -464       C  
ATOM    317  CZ  TYR A  42      -5.461 -14.701  25.357  1.00 65.64           C  
ANISOU  317  CZ  TYR A  42     7742  10838   6360   1314  -2318   -505       C  
ATOM    318  OH  TYR A  42      -4.389 -15.494  25.708  1.00 65.56           O  
ANISOU  318  OH  TYR A  42     7753  10828   6328   1322  -2299   -493       O  
ATOM    319  N   PHE A  43     -10.746 -10.720  21.874  1.00 67.89           N  
ANISOU  319  N   PHE A  43     7911  11152   6732   1288  -2417   -525       N  
ATOM    320  CA  PHE A  43     -12.052 -10.098  21.639  1.00 68.14           C  
ANISOU  320  CA  PHE A  43     7921  11185   6784   1279  -2435   -545       C  
ATOM    321  C   PHE A  43     -12.285  -9.844  20.162  1.00 68.69           C  
ANISOU  321  C   PHE A  43     7980  11278   6841   1286  -2444   -525       C  
ATOM    322  O   PHE A  43     -12.428  -8.690  19.743  1.00 68.89           O  
ANISOU  322  O   PHE A  43     7982  11300   6894   1286  -2461   -494       O  
ATOM    323  CB  PHE A  43     -12.160  -8.767  22.387  1.00 67.93           C  
ANISOU  323  CB  PHE A  43     7872  11133   6806   1272  -2453   -526       C  
ATOM    324  CG  PHE A  43     -12.084  -8.899  23.864  1.00 67.42           C  
ANISOU  324  CG  PHE A  43     7814  11045   6757   1263  -2447   -548       C  
ATOM    325  CD1 PHE A  43     -10.873  -8.879  24.509  1.00 67.06           C  
ANISOU  325  CD1 PHE A  43     7780  10986   6714   1268  -2438   -522       C  
ATOM    326  CD2 PHE A  43     -13.228  -9.041  24.610  1.00 67.30           C  
ANISOU  326  CD2 PHE A  43     7795  11021   6755   1250  -2451   -596       C  
ATOM    327  CE1 PHE A  43     -10.803  -9.005  25.867  1.00 66.61           C  
ANISOU  327  CE1 PHE A  43     7729  10908   6671   1259  -2433   -543       C  
ATOM    328  CE2 PHE A  43     -13.166  -9.164  25.977  1.00 66.84           C  
ANISOU  328  CE2 PHE A  43     7744  10942   6712   1241  -2446   -617       C  
ATOM    329  CZ  PHE A  43     -11.948  -9.149  26.604  1.00 66.50           C  
ANISOU  329  CZ  PHE A  43     7711  10886   6669   1245  -2437   -590       C  
ATOM    330  N   PRO A  44     -12.324 -10.912  19.363  1.00 73.55           N  
ANISOU  330  N   PRO A  44     8611  11918   7415   1291  -2431   -541       N  
ATOM    331  CA  PRO A  44     -12.334 -10.726  17.911  1.00 74.10           C  
ANISOU  331  CA  PRO A  44     8673  12013   7469   1299  -2437   -517       C  
ATOM    332  C   PRO A  44     -13.529  -9.938  17.423  1.00 74.41           C  
ANISOU  332  C   PRO A  44     8686  12056   7529   1292  -2458   -524       C  
ATOM    333  O   PRO A  44     -13.347  -8.954  16.709  1.00 74.69           O  
ANISOU  333  O   PRO A  44     8703  12094   7580   1297  -2471   -483       O  
ATOM    334  CB  PRO A  44     -12.399 -12.155  17.373  1.00 74.31           C  
ANISOU  334  CB  PRO A  44     8723  12064   7449   1303  -2419   -548       C  
ATOM    335  CG  PRO A  44     -11.982 -13.025  18.525  1.00 73.84           C  
ANISOU  335  CG  PRO A  44     8685  11990   7380   1301  -2401   -574       C  
ATOM    336  CD  PRO A  44     -12.435 -12.325  19.748  1.00 73.41           C  
ANISOU  336  CD  PRO A  44     8619  11909   7366   1289  -2412   -585       C  
ATOM    337  N   HIS A  45     -14.725 -10.324  17.862  1.00 78.52           N  
ANISOU  337  N   HIS A  45     9205  12577   8052   1280  -2460   -573       N  
ATOM    338  CA  HIS A  45     -15.960  -9.842  17.243  1.00 79.93           C  
ANISOU  338  CA  HIS A  45     9363  12766   8242   1273  -2477   -586       C  
ATOM    339  C   HIS A  45     -16.450  -8.550  17.867  1.00 79.26           C  
ANISOU  339  C   HIS A  45     9252  12658   8204   1266  -2497   -575       C  
ATOM    340  O   HIS A  45     -17.417  -7.943  17.386  1.00 80.58           O  
ANISOU  340  O   HIS A  45     9398  12832   8387   1261  -2513   -578       O  
ATOM    341  CB  HIS A  45     -17.061 -10.898  17.343  1.00 80.55           C  
ANISOU  341  CB  HIS A  45     9451  12856   8299   1263  -2470   -646       C  
ATOM    342  CG  HIS A  45     -16.686 -12.227  16.760  1.00 81.53           C  
ANISOU  342  CG  HIS A  45     9600  13003   8375   1269  -2451   -662       C  
ATOM    343  ND1 HIS A  45     -15.389 -12.559  16.423  1.00 80.80           N  
ANISOU  343  ND1 HIS A  45     9523  12916   8260   1282  -2437   -631       N  
ATOM    344  CD2 HIS A  45     -17.441 -13.310  16.457  1.00 83.29           C  
ANISOU  344  CD2 HIS A  45     9835  13243   8568   1264  -2442   -708       C  
ATOM    345  CE1 HIS A  45     -15.360 -13.789  15.942  1.00 82.05           C  
ANISOU  345  CE1 HIS A  45     9702  13096   8378   1285  -2421   -656       C  
ATOM    346  NE2 HIS A  45     -16.592 -14.267  15.950  1.00 83.58           N  
ANISOU  346  NE2 HIS A  45     9894  13297   8566   1274  -2423   -704       N  
ATOM    347  N   PHE A  46     -15.795  -8.139  18.948  1.00 74.95           N  
ANISOU  347  N   PHE A  46     8708  12086   7683   1265  -2495   -562       N  
ATOM    348  CA  PHE A  46     -16.153  -6.892  19.597  1.00 74.24           C  
ANISOU  348  CA  PHE A  46     8594  11973   7639   1258  -2512   -550       C  
ATOM    349  C   PHE A  46     -15.758  -5.721  18.710  1.00 75.25           C  
ANISOU  349  C   PHE A  46     8701  12104   7785   1266  -2527   -496       C  
ATOM    350  O   PHE A  46     -14.714  -5.745  18.042  1.00 75.79           O  
ANISOU  350  O   PHE A  46     8777  12182   7838   1278  -2521   -458       O  
ATOM    351  CB  PHE A  46     -15.488  -6.752  20.967  1.00 72.06           C  
ANISOU  351  CB  PHE A  46     8326  11670   7384   1255  -2506   -550       C  
ATOM    352  CG  PHE A  46     -16.063  -7.651  22.024  1.00 71.03           C  
ANISOU  352  CG  PHE A  46     8211  11531   7246   1244  -2495   -604       C  
ATOM    353  CD1 PHE A  46     -16.002  -7.284  23.357  1.00 69.25           C  
ANISOU  353  CD1 PHE A  46     7983  11278   7049   1236  -2497   -614       C  
ATOM    354  CD2 PHE A  46     -16.641  -8.867  21.698  1.00 71.90           C  
ANISOU  354  CD2 PHE A  46     8337  11659   7322   1242  -2484   -645       C  
ATOM    355  CE1 PHE A  46     -16.514  -8.107  24.346  1.00 68.38           C  
ANISOU  355  CE1 PHE A  46     7888  11160   6934   1226  -2486   -663       C  
ATOM    356  CE2 PHE A  46     -17.151  -9.694  22.683  1.00 71.01           C  
ANISOU  356  CE2 PHE A  46     8239  11537   7204   1231  -2474   -695       C  
ATOM    357  CZ  PHE A  46     -17.090  -9.308  24.008  1.00 69.23           C  
ANISOU  357  CZ  PHE A  46     8012  11285   7008   1223  -2475   -703       C  
ATOM    358  N   ASP A  47     -16.611  -4.702  18.696  1.00 78.65           N  
ANISOU  358  N   ASP A  47     9106  12529   8250   1260  -2547   -493       N  
ATOM    359  CA  ASP A  47     -16.198  -3.418  18.184  1.00 79.12           C  
ANISOU  359  CA  ASP A  47     9143  12583   8337   1266  -2562   -441       C  
ATOM    360  C   ASP A  47     -15.314  -2.810  19.268  1.00 77.08           C  
ANISOU  360  C   ASP A  47     8884  12295   8107   1266  -2560   -419       C  
ATOM    361  O   ASP A  47     -15.778  -2.556  20.383  1.00 75.81           O  
ANISOU  361  O   ASP A  47     8718  12114   7972   1256  -2564   -444       O  
ATOM    362  CB  ASP A  47     -17.401  -2.539  17.895  1.00 80.36           C  
ANISOU  362  CB  ASP A  47     9271  12741   8522   1259  -2582   -446       C  
ATOM    363  CG  ASP A  47     -17.007  -1.185  17.404  1.00 80.95           C  
ANISOU  363  CG  ASP A  47     9321  12808   8627   1265  -2598   -392       C  
ATOM    364  OD1 ASP A  47     -16.215  -1.109  16.443  1.00 82.51           O  
ANISOU  364  OD1 ASP A  47     9522  13019   8809   1276  -2596   -353       O  
ATOM    365  OD2 ASP A  47     -17.474  -0.192  17.989  1.00 79.90           O  
ANISOU  365  OD2 ASP A  47     9167  12656   8535   1259  -2612   -389       O  
ATOM    366  N   LEU A  48     -14.042  -2.583  18.947  1.00 77.29           N  
ANISOU  366  N   LEU A  48     8917  12321   8129   1276  -2555   -374       N  
ATOM    367  CA  LEU A  48     -13.075  -2.166  19.957  1.00 75.49           C  
ANISOU  367  CA  LEU A  48     8693  12067   7923   1277  -2550   -354       C  
ATOM    368  C   LEU A  48     -12.839  -0.651  19.977  1.00 75.57           C  
ANISOU  368  C   LEU A  48     8677  12060   7977   1277  -2568   -311       C  
ATOM    369  O   LEU A  48     -12.047  -0.138  20.776  1.00 74.27           O  
ANISOU  369  O   LEU A  48     8512  11874   7834   1277  -2566   -290       O  
ATOM    370  CB  LEU A  48     -11.766  -2.923  19.748  1.00 75.11           C  
ANISOU  370  CB  LEU A  48     8670  12026   7843   1287  -2531   -333       C  
ATOM    371  CG  LEU A  48     -11.872  -4.315  20.364  1.00 74.66           C  
ANISOU  371  CG  LEU A  48     8639  11973   7754   1283  -2513   -380       C  
ATOM    372  CD1 LEU A  48     -10.546  -5.058  20.329  1.00 74.87           C  
ANISOU  372  CD1 LEU A  48     8691  12004   7753   1293  -2494   -360       C  
ATOM    373  CD2 LEU A  48     -12.387  -4.221  21.798  1.00 72.84           C  
ANISOU  373  CD2 LEU A  48     8408  11720   7549   1271  -2515   -414       C  
ATOM    374  N   SER A  49     -13.575   0.065  19.132  1.00 77.43           N  
ANISOU  374  N   SER A  49     8889  12305   8225   1278  -2584   -299       N  
ATOM    375  CA  SER A  49     -13.347   1.491  18.930  1.00 77.94           C  
ANISOU  375  CA  SER A  49     8928  12357   8330   1280  -2600   -254       C  
ATOM    376  C   SER A  49     -13.717   2.312  20.161  1.00 76.62           C  
ANISOU  376  C   SER A  49     8745  12161   8205   1270  -2610   -265       C  
ATOM    377  O   SER A  49     -14.057   1.766  21.209  1.00 75.19           O  
ANISOU  377  O   SER A  49     8574  11971   8023   1262  -2604   -306       O  
ATOM    378  CB  SER A  49     -14.135   1.974  17.724  1.00 80.15           C  
ANISOU  378  CB  SER A  49     9188  12655   8612   1282  -2615   -242       C  
ATOM    379  OG  SER A  49     -15.416   1.387  17.736  1.00 81.02           O  
ANISOU  379  OG  SER A  49     9297  12777   8710   1274  -2618   -290       O  
ATOM    380  N   HIS A  50     -13.605   3.627  20.049  1.00 79.58           N  
ANISOU  380  N   HIS A  50     9094  12523   8618   1271  -2626   -228       N  
ATOM    381  CA  HIS A  50     -13.798   4.478  21.212  1.00 78.34           C  
ANISOU  381  CA  HIS A  50     8923  12340   8504   1263  -2635   -233       C  
ATOM    382  C   HIS A  50     -15.254   4.468  21.698  1.00 78.28           C  
ANISOU  382  C   HIS A  50     8903  12330   8510   1252  -2644   -281       C  
ATOM    383  O   HIS A  50     -16.184   4.660  20.913  1.00 79.85           O  
ANISOU  383  O   HIS A  50     9087  12544   8710   1252  -2655   -286       O  
ATOM    384  CB  HIS A  50     -13.346   5.907  20.907  1.00 79.05           C  
ANISOU  384  CB  HIS A  50     8987  12417   8632   1268  -2649   -181       C  
ATOM    385  CG  HIS A  50     -13.313   6.799  22.111  1.00 77.59           C  
ANISOU  385  CG  HIS A  50     8788  12203   8489   1260  -2656   -182       C  
ATOM    386  ND1 HIS A  50     -13.635   6.355  23.380  1.00 76.12           N  
ANISOU  386  ND1 HIS A  50     8611  12004   8306   1251  -2650   -225       N  
ATOM    387  CD2 HIS A  50     -12.997   8.110  22.242  1.00 77.44           C  
ANISOU  387  CD2 HIS A  50     8746  12167   8512   1261  -2669   -145       C  
ATOM    388  CE1 HIS A  50     -13.521   7.354  24.239  1.00 75.17           C  
ANISOU  388  CE1 HIS A  50     8474  11860   8226   1246  -2659   -215       C  
ATOM    389  NE2 HIS A  50     -13.134   8.431  23.575  1.00 76.00           N  
ANISOU  389  NE2 HIS A  50     8559  11962   8356   1252  -2671   -167       N  
ATOM    390  N   GLY A  51     -15.423   4.219  23.000  1.00 74.99           N  
ANISOU  390  N   GLY A  51     8494  11897   8103   1243  -2639   -316       N  
ATOM    391  CA  GLY A  51     -16.712   4.241  23.669  1.00 74.99           C  
ANISOU  391  CA  GLY A  51     8483  11889   8119   1232  -2646   -362       C  
ATOM    392  C   GLY A  51     -17.747   3.314  23.056  1.00 75.11           C  
ANISOU  392  C   GLY A  51     8506  11928   8105   1229  -2644   -400       C  
ATOM    393  O   GLY A  51     -18.963   3.551  23.171  1.00 75.21           O  
ANISOU  393  O   GLY A  51     8502  11940   8134   1222  -2654   -429       O  
ATOM    394  N   SER A  52     -17.259   2.270  22.386  1.00 73.57           N  
ANISOU  394  N   SER A  52     8334  11753   7867   1236  -2629   -400       N  
ATOM    395  CA  SER A  52     -18.113   1.261  21.779  1.00 74.88           C  
ANISOU  395  CA  SER A  52     8510  11942   7999   1234  -2625   -436       C  
ATOM    396  C   SER A  52     -19.065   0.711  22.831  1.00 74.15           C  
ANISOU  396  C   SER A  52     8423  11839   7910   1221  -2621   -494       C  
ATOM    397  O   SER A  52     -18.634   0.414  23.944  1.00 72.46           O  
ANISOU  397  O   SER A  52     8223  11609   7700   1216  -2612   -510       O  
ATOM    398  CB  SER A  52     -17.263   0.137  21.174  1.00 75.13           C  
ANISOU  398  CB  SER A  52     8569  11992   7984   1242  -2606   -430       C  
ATOM    399  OG  SER A  52     -18.067  -0.953  20.733  1.00 76.73           O  
ANISOU  399  OG  SER A  52     8784  12216   8153   1239  -2600   -471       O  
ATOM    400  N   ALA A  53     -20.348   0.605  22.492  1.00 70.54           N  
ANISOU  400  N   ALA A  53     9339  10788   6675   1325   -169   -446       N  
ATOM    401  CA  ALA A  53     -21.334   0.031  23.402  1.00 70.10           C  
ANISOU  401  CA  ALA A  53     9291  10730   6615   1305   -183   -442       C  
ATOM    402  C   ALA A  53     -20.895  -1.346  23.890  1.00 68.55           C  
ANISOU  402  C   ALA A  53     9132  10499   6416   1290   -199   -473       C  
ATOM    403  O   ALA A  53     -21.067  -1.694  25.061  1.00 66.64           O  
ANISOU  403  O   ALA A  53     8898  10235   6187   1282   -202   -473       O  
ATOM    404  CB  ALA A  53     -22.679  -0.061  22.727  1.00 72.69           C  
ANISOU  404  CB  ALA A  53     9613  11096   6909   1285   -201   -431       C  
ATOM    405  N   GLN A  54     -20.304  -2.117  22.985  1.00 70.83           N  
ANISOU  405  N   GLN A  54     9444  10782   6686   1285   -210   -501       N  
ATOM    406  CA  GLN A  54     -19.836  -3.464  23.310  1.00 69.80           C  
ANISOU  406  CA  GLN A  54     9350  10620   6551   1272   -228   -534       C  
ATOM    407  C   GLN A  54     -18.739  -3.444  24.368  1.00 67.04           C  
ANISOU  407  C   GLN A  54     9006  10230   6238   1289   -214   -542       C  
ATOM    408  O   GLN A  54     -18.819  -4.193  25.347  1.00 65.53           O  
ANISOU  408  O   GLN A  54     8834  10013   6052   1277   -225   -551       O  
ATOM    409  CB  GLN A  54     -19.340  -4.176  22.055  1.00 71.57           C  
ANISOU  409  CB  GLN A  54     9594  10849   6750   1268   -241   -563       C  
ATOM    410  CG  GLN A  54     -19.651  -5.653  22.033  1.00 73.55           C  
ANISOU  410  CG  GLN A  54     9880  11088   6977   1243   -272   -592       C  
ATOM    411  CD  GLN A  54     -19.541  -6.226  20.632  1.00 76.22           C  
ANISOU  411  CD  GLN A  54    10234  11443   7284   1236   -286   -615       C  
ATOM    412  OE1 GLN A  54     -19.548  -5.486  19.644  1.00 77.24           O  
ANISOU  412  OE1 GLN A  54    10345  11600   7402   1245   -276   -605       O  
ATOM    413  NE2 GLN A  54     -19.429  -7.551  20.536  1.00 77.51           N  
ANISOU  413  NE2 GLN A  54    10429  11589   7431   1221   -312   -648       N  
ATOM    414  N   VAL A  55     -17.724  -2.597  24.166  1.00 66.68           N  
ANISOU  414  N   VAL A  55     8943  10178   6214   1316   -191   -538       N  
ATOM    415  CA  VAL A  55     -16.698  -2.338  25.179  1.00 64.21           C  
ANISOU  415  CA  VAL A  55     8628   9829   5939   1335   -175   -539       C  
ATOM    416  C   VAL A  55     -17.296  -1.834  26.492  1.00 62.20           C  
ANISOU  416  C   VAL A  55     8360   9568   5705   1334   -168   -514       C  
ATOM    417  O   VAL A  55     -16.959  -2.311  27.573  1.00 60.28           O  
ANISOU  417  O   VAL A  55     8132   9292   5479   1332   -171   -522       O  
ATOM    418  CB  VAL A  55     -15.680  -1.297  24.686  1.00 64.38           C  
ANISOU  418  CB  VAL A  55     8628   9852   5980   1364   -151   -532       C  
ATOM    419  CG1 VAL A  55     -14.742  -0.885  25.822  1.00 61.83           C  
ANISOU  419  CG1 VAL A  55     8299   9494   5698   1385   -136   -528       C  
ATOM    420  CG2 VAL A  55     -14.905  -1.830  23.506  1.00 66.45           C  
ANISOU  420  CG2 VAL A  55     8906  10118   6225   1366   -156   -560       C  
ATOM    421  N   LYS A  56     -18.200  -0.862  26.366  1.00 66.98           N  
ANISOU  421  N   LYS A  56     8936  10206   6308   1336   -159   -484       N  
ATOM    422  CA  LYS A  56     -18.759  -0.126  27.497  1.00 65.45           C  
ANISOU  422  CA  LYS A  56     8721  10012   6136   1340   -147   -457       C  
ATOM    423  C   LYS A  56     -19.555  -1.052  28.402  1.00 64.97           C  
ANISOU  423  C   LYS A  56     8681   9942   6064   1313   -165   -462       C  
ATOM    424  O   LYS A  56     -19.521  -0.917  29.642  1.00 63.00           O  
ANISOU  424  O   LYS A  56     8430   9671   5836   1315   -157   -454       O  
ATOM    425  CB  LYS A  56     -19.643   1.033  27.005  1.00 66.85           C  
ANISOU  425  CB  LYS A  56     8862  10230   6307   1347   -138   -426       C  
ATOM    426  CG  LYS A  56     -20.202   1.906  28.126  1.00 65.89           C  
ANISOU  426  CG  LYS A  56     8714  10112   6208   1354   -124   -398       C  
ATOM    427  CD  LYS A  56     -21.200   2.958  27.617  1.00 67.88           C  
ANISOU  427  CD  LYS A  56     8931  10409   6452   1359   -118   -370       C  
ATOM    428  CE  LYS A  56     -20.560   3.942  26.601  1.00 68.61           C  
ANISOU  428  CE  LYS A  56     9003  10516   6551   1384   -105   -361       C  
ATOM    429  NZ  LYS A  56     -19.139   4.351  26.935  1.00 66.57           N  
ANISOU  429  NZ  LYS A  56     8743  10225   6324   1409    -88   -366       N  
ATOM    430  N   GLY A  57     -20.272  -1.985  27.774  1.00 61.85           N  
ANISOU  430  N   GLY A  57     8306   9562   5634   1288   -188   -475       N  
ATOM    431  CA  GLY A  57     -21.097  -2.922  28.512  1.00 61.74           C  
ANISOU  431  CA  GLY A  57     8313   9542   5605   1259   -208   -479       C  
ATOM    432  C   GLY A  57     -20.260  -3.995  29.173  1.00 60.24           C  
ANISOU  432  C   GLY A  57     8157   9308   5422   1253   -219   -507       C  
ATOM    433  O   GLY A  57     -20.423  -4.311  30.358  1.00 58.69           O  
ANISOU  433  O   GLY A  57     7972   9092   5235   1243   -221   -504       O  
ATOM    434  N   HIS A  58     -19.342  -4.548  28.390  1.00 62.37           N  
ANISOU  434  N   HIS A  58     8446   9565   5688   1261   -226   -534       N  
ATOM    435  CA  HIS A  58     -18.404  -5.527  28.899  1.00 61.18           C  
ANISOU  435  CA  HIS A  58     8327   9373   5546   1260   -236   -563       C  
ATOM    436  C   HIS A  58     -17.688  -5.032  30.157  1.00 58.48           C  
ANISOU  436  C   HIS A  58     7978   8999   5241   1277   -218   -554       C  
ATOM    437  O   HIS A  58     -17.460  -5.813  31.097  1.00 57.27           O  
ANISOU  437  O   HIS A  58     7851   8815   5093   1267   -229   -567       O  
ATOM    438  CB  HIS A  58     -17.387  -5.875  27.831  1.00 62.29           C  
ANISOU  438  CB  HIS A  58     8478   9507   5682   1273   -239   -590       C  
ATOM    439  CG  HIS A  58     -16.402  -6.904  28.271  1.00 61.57           C  
ANISOU  439  CG  HIS A  58     8418   9375   5601   1275   -251   -622       C  
ATOM    440  ND1 HIS A  58     -16.667  -8.255  28.226  1.00 62.37           N  
ANISOU  440  ND1 HIS A  58     8553   9465   5678   1251   -282   -648       N  
ATOM    441  CD2 HIS A  58     -15.161  -6.780  28.800  1.00 60.22           C  
ANISOU  441  CD2 HIS A  58     8251   9171   5460   1297   -240   -633       C  
ATOM    442  CE1 HIS A  58     -15.622  -8.921  28.687  1.00 61.57           C  
ANISOU  442  CE1 HIS A  58     8474   9325   5593   1260   -288   -674       C  
ATOM    443  NE2 HIS A  58     -14.696  -8.048  29.042  1.00 60.27           N  
ANISOU  443  NE2 HIS A  58     8291   9146   5461   1288   -263   -665       N  
ATOM    444  N   GLY A  59     -17.346  -3.739  30.166  1.00 58.49           N  
ANISOU  444  N   GLY A  59     7948   9010   5267   1302   -191   -532       N  
ATOM    445  CA  GLY A  59     -16.739  -3.104  31.325  1.00 56.12           C  
ANISOU  445  CA  GLY A  59     7637   8683   5002   1320   -173   -520       C  
ATOM    446  C   GLY A  59     -17.643  -3.155  32.547  1.00 55.04           C  
ANISOU  446  C   GLY A  59     7502   8545   4867   1302   -175   -503       C  
ATOM    447  O   GLY A  59     -17.176  -3.217  33.687  1.00 53.18           O  
ANISOU  447  O   GLY A  59     7275   8278   4653   1306   -170   -503       O  
ATOM    448  N   LYS A  60     -18.952  -3.128  32.314  1.00 55.99           N  
ANISOU  448  N   LYS A  60     7613   8699   4962   1282   -182   -488       N  
ATOM    449  CA  LYS A  60     -19.893  -3.197  33.417  1.00 55.33           C  
ANISOU  449  CA  LYS A  60     7529   8618   4875   1262   -185   -473       C  
ATOM    450  C   LYS A  60     -19.837  -4.592  34.018  1.00 54.81           C  
ANISOU  450  C   LYS A  60     7505   8524   4795   1237   -209   -495       C  
ATOM    451  O   LYS A  60     -20.080  -4.762  35.217  1.00 53.41           O  
ANISOU  451  O   LYS A  60     7337   8331   4624   1225   -209   -488       O  
ATOM    452  CB  LYS A  60     -21.322  -2.842  32.959  1.00 57.42           C  
ANISOU  452  CB  LYS A  60     7773   8928   5115   1247   -188   -452       C  
ATOM    453  CG  LYS A  60     -22.420  -2.929  34.049  1.00 57.27           C  
ANISOU  453  CG  LYS A  60     7753   8919   5089   1224   -191   -435       C  
ATOM    454  CD  LYS A  60     -21.950  -2.316  35.378  1.00 55.89           C  
ANISOU  454  CD  LYS A  60     7569   8720   4947   1238   -170   -423       C  
ATOM    455  CE  LYS A  60     -23.080  -1.812  36.263  1.00 55.75           C  
ANISOU  455  CE  LYS A  60     7530   8724   4927   1226   -162   -398       C  
ATOM    456  NZ  LYS A  60     -24.064  -2.870  36.668  1.00 57.27           N  
ANISOU  456  NZ  LYS A  60     7748   8923   5088   1188   -185   -402       N  
ATOM    457  N   LYS A  61     -19.520  -5.598  33.198  1.00 54.36           N  
ANISOU  457  N   LYS A  61     7475   8461   4719   1228   -230   -523       N  
ATOM    458  CA  LYS A  61     -19.421  -6.966  33.727  1.00 54.26           C  
ANISOU  458  CA  LYS A  61     7503   8419   4693   1205   -257   -546       C  
ATOM    459  C   LYS A  61     -18.180  -7.060  34.608  1.00 52.24           C  
ANISOU  459  C   LYS A  61     7261   8119   4468   1222   -249   -558       C  
ATOM    460  O   LYS A  61     -18.272  -7.420  35.799  1.00 50.99           O  
ANISOU  460  O   LYS A  61     7120   7939   4315   1209   -254   -555       O  
ATOM    461  CB  LYS A  61     -19.382  -7.998  32.599  1.00 56.28           C  
ANISOU  461  CB  LYS A  61     7783   8680   4922   1193   -283   -574       C  
ATOM    462  CG  LYS A  61     -20.712  -8.711  32.363  1.00 58.03           C  
ANISOU  462  CG  LYS A  61     8016   8927   5107   1158   -308   -571       C  
ATOM    463  CD  LYS A  61     -20.917  -9.078  30.885  1.00 60.54           C  
ANISOU  463  CD  LYS A  61     8336   9269   5399   1155   -324   -586       C  
ATOM    464  CE  LYS A  61     -21.964 -10.192  30.694  1.00 62.53           C  
ANISOU  464  CE  LYS A  61     8612   9532   5614   1118   -359   -594       C  
ATOM    465  NZ  LYS A  61     -23.337  -9.855  31.190  1.00 63.59           N  
ANISOU  465  NZ  LYS A  61     8731   9695   5735   1097   -359   -565       N  
ATOM    466  N   VAL A  62     -17.042  -6.671  34.025  1.00 53.37           N  
ANISOU  466  N   VAL A  62     7396   8251   4631   1251   -237   -569       N  
ATOM    467  CA  VAL A  62     -15.746  -6.693  34.699  1.00 51.68           C  
ANISOU  467  CA  VAL A  62     7192   7996   4448   1273   -230   -582       C  
ATOM    468  C   VAL A  62     -15.761  -5.870  35.967  1.00 49.75           C  
ANISOU  468  C   VAL A  62     6933   7741   4230   1280   -210   -557       C  
ATOM    469  O   VAL A  62     -15.160  -6.252  36.978  1.00 48.40           O  
ANISOU  469  O   VAL A  62     6782   7534   4075   1282   -214   -565       O  
ATOM    470  CB  VAL A  62     -14.636  -6.157  33.797  1.00 51.89           C  
ANISOU  470  CB  VAL A  62     7203   8020   4491   1304   -216   -592       C  
ATOM    471  CG1 VAL A  62     -13.294  -6.340  34.459  1.00 50.36           C  
ANISOU  471  CG1 VAL A  62     7024   7783   4328   1324   -213   -608       C  
ATOM    472  CG2 VAL A  62     -14.663  -6.838  32.425  1.00 54.11           C  
ANISOU  472  CG2 VAL A  62     7495   8318   4745   1298   -232   -615       C  
ATOM    473  N   ALA A  63     -16.441  -4.729  35.902  1.00 50.51           N  
ANISOU  473  N   ALA A  63     6993   7867   4330   1287   -190   -528       N  
ATOM    474  CA  ALA A  63     -16.650  -3.889  37.071  1.00 48.90           C  
ANISOU  474  CA  ALA A  63     6771   7659   4148   1292   -171   -502       C  
ATOM    475  C   ALA A  63     -17.303  -4.693  38.179  1.00 48.59           C  
ANISOU  475  C   ALA A  63     6758   7608   4095   1262   -186   -502       C  
ATOM    476  O   ALA A  63     -16.899  -4.643  39.349  1.00 48.11           O  
ANISOU  476  O   ALA A  63     6706   7519   4054   1264   -180   -499       O  
ATOM    477  CB  ALA A  63     -17.505  -2.702  36.705  1.00 49.48           C  
ANISOU  477  CB  ALA A  63     6805   7774   4222   1299   -153   -473       C  
ATOM    478  N   ASP A  64     -18.310  -5.463  37.780  1.00 50.45           N  
ANISOU  478  N   ASP A  64     7008   7865   4296   1232   -206   -506       N  
ATOM    479  CA  ASP A  64     -19.199  -6.099  38.738  1.00 50.46           C  
ANISOU  479  CA  ASP A  64     7029   7866   4279   1199   -219   -500       C  
ATOM    480  C   ASP A  64     -18.520  -7.289  39.362  1.00 49.80           C  
ANISOU  480  C   ASP A  64     6987   7740   4193   1187   -241   -525       C  
ATOM    481  O   ASP A  64     -18.655  -7.538  40.569  1.00 48.87           O  
ANISOU  481  O   ASP A  64     6885   7605   4077   1172   -243   -519       O  
ATOM    482  CB  ASP A  64     -20.514  -6.494  38.072  1.00 52.70           C  
ANISOU  482  CB  ASP A  64     7311   8188   4526   1171   -236   -495       C  
ATOM    483  CG  ASP A  64     -21.482  -5.325  37.954  1.00 53.40           C  
ANISOU  483  CG  ASP A  64     7358   8318   4615   1176   -215   -464       C  
ATOM    484  OD1 ASP A  64     -21.051  -4.141  38.057  1.00 52.40           O  
ANISOU  484  OD1 ASP A  64     7200   8193   4517   1206   -189   -449       O  
ATOM    485  OD2 ASP A  64     -22.679  -5.605  37.754  1.00 55.08           O  
ANISOU  485  OD2 ASP A  64     7569   8560   4799   1151   -227   -456       O  
ATOM    486  N   ALA A  65     -17.774  -8.006  38.530  1.00 50.09           N  
ANISOU  486  N   ALA A  65     7043   7762   4226   1194   -257   -553       N  
ATOM    487  CA  ALA A  65     -16.872  -9.053  39.011  1.00 49.62           C  
ANISOU  487  CA  ALA A  65     7022   7660   4172   1192   -278   -580       C  
ATOM    488  C   ALA A  65     -16.024  -8.523  40.169  1.00 47.56           C  
ANISOU  488  C   ALA A  65     6759   7367   3945   1211   -260   -573       C  
ATOM    489  O   ALA A  65     -15.976  -9.112  41.263  1.00 46.86           O  
ANISOU  489  O   ALA A  65     6697   7252   3856   1195   -272   -576       O  
ATOM    490  CB  ALA A  65     -15.987  -9.540  37.875  1.00 50.64           C  
ANISOU  490  CB  ALA A  65     7159   7779   4301   1209   -289   -610       C  
ATOM    491  N   LEU A  66     -15.405  -7.371  39.930  1.00 48.40           N  
ANISOU  491  N   LEU A  66     6833   7476   4079   1244   -233   -562       N  
ATOM    492  CA  LEU A  66     -14.560  -6.747  40.930  1.00 46.59           C  
ANISOU  492  CA  LEU A  66     6598   7218   3885   1266   -215   -555       C  
ATOM    493  C   LEU A  66     -15.307  -6.357  42.202  1.00 45.55           C  
ANISOU  493  C   LEU A  66     6463   7090   3755   1250   -206   -530       C  
ATOM    494  O   LEU A  66     -14.826  -6.586  43.322  1.00 44.42           O  
ANISOU  494  O   LEU A  66     6338   6914   3624   1249   -208   -532       O  
ATOM    495  CB  LEU A  66     -13.890  -5.531  40.335  1.00 46.16           C  
ANISOU  495  CB  LEU A  66     6508   7173   3859   1302   -190   -545       C  
ATOM    496  CG  LEU A  66     -12.738  -5.890  39.426  1.00 47.00           C  
ANISOU  496  CG  LEU A  66     6622   7262   3972   1324   -197   -572       C  
ATOM    497  CD1 LEU A  66     -12.364  -4.680  38.581  1.00 47.15           C  
ANISOU  497  CD1 LEU A  66     6603   7303   4009   1353   -173   -559       C  
ATOM    498  CD2 LEU A  66     -11.572  -6.384  40.299  1.00 46.06           C  
ANISOU  498  CD2 LEU A  66     6529   7095   3877   1336   -205   -590       C  
ATOM    499  N   THR A  67     -16.477  -5.750  42.029  1.00 46.89           N  
ANISOU  499  N   THR A  67     6606   7299   3910   1238   -195   -506       N  
ATOM    500  CA  THR A  67     -17.257  -5.317  43.177  1.00 46.11           C  
ANISOU  500  CA  THR A  67     6500   7209   3812   1222   -183   -482       C  
ATOM    501  C   THR A  67     -17.633  -6.516  44.018  1.00 46.29           C  
ANISOU  501  C   THR A  67     6563   7214   3810   1186   -207   -491       C  
ATOM    502  O   THR A  67     -17.661  -6.461  45.261  1.00 45.22           O  
ANISOU  502  O   THR A  67     6438   7063   3682   1177   -202   -482       O  
ATOM    503  CB  THR A  67     -18.502  -4.613  42.755  1.00 47.33           C  
ANISOU  503  CB  THR A  67     6622   7411   3952   1214   -172   -459       C  
ATOM    504  OG1 THR A  67     -18.276  -4.024  41.469  1.00 48.02           O  
ANISOU  504  OG1 THR A  67     6683   7518   4044   1238   -164   -460       O  
ATOM    505  CG2 THR A  67     -18.890  -3.565  43.807  1.00 46.49           C  
ANISOU  505  CG2 THR A  67     6489   7312   3863   1220   -147   -432       C  
ATOM    506  N   ASN A  68     -17.929  -7.602  43.306  1.00 47.78           N  
ANISOU  506  N   ASN A  68     6776   7407   3970   1166   -235   -510       N  
ATOM    507  CA  ASN A  68     -18.316  -8.847  43.929  1.00 48.30           C  
ANISOU  507  CA  ASN A  68     6883   7458   4009   1129   -263   -520       C  
ATOM    508  C   ASN A  68     -17.171  -9.259  44.811  1.00 47.05           C  
ANISOU  508  C   ASN A  68     6753   7252   3873   1139   -269   -535       C  
ATOM    509  O   ASN A  68     -17.364  -9.594  45.996  1.00 46.49           O  
ANISOU  509  O   ASN A  68     6702   7165   3796   1118   -275   -528       O  
ATOM    510  CB  ASN A  68     -18.629  -9.917  42.881  1.00 50.09           C  
ANISOU  510  CB  ASN A  68     7130   7694   4207   1111   -294   -541       C  
ATOM    511  CG  ASN A  68     -19.159 -11.192  43.500  1.00 50.97           C  
ANISOU  511  CG  ASN A  68     7283   7795   4289   1071   -326   -548       C  
ATOM    512  OD1 ASN A  68     -19.659 -11.198  44.635  1.00 50.47           O  
ANISOU  512  OD1 ASN A  68     7227   7729   4219   1049   -324   -532       O  
ATOM    513  ND2 ASN A  68     -19.041 -12.292  42.761  1.00 52.42           N  
ANISOU  513  ND2 ASN A  68     7492   7970   4454   1060   -358   -574       N  
ATOM    514  N   ALA A  69     -15.974  -9.194  44.219  1.00 46.96           N  
ANISOU  514  N   ALA A  69     6739   7218   3884   1172   -268   -554       N  
ATOM    515  CA  ALA A  69     -14.766  -9.591  44.911  1.00 46.01           C  
ANISOU  515  CA  ALA A  69     6644   7051   3786   1187   -276   -572       C  
ATOM    516  C   ALA A  69     -14.610  -8.808  46.210  1.00 44.41           C  
ANISOU  516  C   ALA A  69     6432   6835   3605   1194   -254   -551       C  
ATOM    517  O   ALA A  69     -14.306  -9.390  47.230  1.00 43.88           O  
ANISOU  517  O   ALA A  69     6396   6738   3540   1182   -267   -556       O  
ATOM    518  CB  ALA A  69     -13.573  -9.407  44.028  1.00 46.00           C  
ANISOU  518  CB  ALA A  69     6634   7035   3808   1224   -272   -592       C  
ATOM    519  N   VAL A  70     -14.847  -7.500  46.199  1.00 44.19           N  
ANISOU  519  N   VAL A  70     6364   6830   3595   1211   -223   -526       N  
ATOM    520  CA  VAL A  70     -14.627  -6.766  47.432  1.00 43.87           C  
ANISOU  520  CA  VAL A  70     6316   6776   3578   1220   -204   -509       C  
ATOM    521  C   VAL A  70     -15.810  -7.004  48.368  1.00 44.02           C  
ANISOU  521  C   VAL A  70     6344   6810   3570   1181   -206   -491       C  
ATOM    522  O   VAL A  70     -15.675  -6.925  49.612  1.00 43.87           O  
ANISOU  522  O   VAL A  70     6338   6772   3560   1174   -201   -483       O  
ATOM    523  CB  VAL A  70     -14.351  -5.280  47.133  1.00 43.54           C  
ANISOU  523  CB  VAL A  70     6227   6749   3567   1255   -172   -491       C  
ATOM    524  CG1 VAL A  70     -14.869  -4.929  45.796  1.00 43.68           C  
ANISOU  524  CG1 VAL A  70     6218   6804   3573   1260   -167   -488       C  
ATOM    525  CG2 VAL A  70     -14.871  -4.369  48.226  1.00 43.32           C  
ANISOU  525  CG2 VAL A  70     6179   6730   3549   1252   -149   -464       C  
ATOM    526  N   ALA A  71     -16.949  -7.360  47.760  1.00 48.43           N  
ANISOU  526  N   ALA A  71     6900   7404   4096   1154   -215   -487       N  
ATOM    527  CA  ALA A  71     -18.174  -7.681  48.510  1.00 49.14           C  
ANISOU  527  CA  ALA A  71     7000   7514   4156   1113   -221   -471       C  
ATOM    528  C   ALA A  71     -17.953  -8.890  49.422  1.00 49.13           C  
ANISOU  528  C   ALA A  71     7048   7480   4139   1085   -248   -483       C  
ATOM    529  O   ALA A  71     -18.270  -8.851  50.618  1.00 48.88           O  
ANISOU  529  O   ALA A  71     7027   7444   4103   1066   -243   -469       O  
ATOM    530  CB  ALA A  71     -19.338  -7.930  47.572  1.00 51.00           C  
ANISOU  530  CB  ALA A  71     7226   7791   4360   1092   -230   -466       C  
ATOM    531  N   HIS A  72     -17.441  -9.982  48.875  1.00 48.75           N  
ANISOU  531  N   HIS A  72     7031   7410   4082   1081   -278   -510       N  
ATOM    532  CA  HIS A  72     -16.849 -10.944  49.772  1.00 49.16           C  
ANISOU  532  CA  HIS A  72     7126   7421   4130   1068   -302   -524       C  
ATOM    533  C   HIS A  72     -15.383 -11.046  49.438  1.00 48.40           C  
ANISOU  533  C   HIS A  72     7039   7286   4066   1105   -307   -549       C  
ATOM    534  O   HIS A  72     -14.982 -11.886  48.625  1.00 49.30           O  
ANISOU  534  O   HIS A  72     7170   7388   4173   1108   -332   -574       O  
ATOM    535  CB  HIS A  72     -17.526 -12.288  49.601  1.00 51.15           C  
ANISOU  535  CB  HIS A  72     7415   7677   4344   1027   -340   -535       C  
ATOM    536  CG  HIS A  72     -18.885 -12.183  49.000  1.00 52.30           C  
ANISOU  536  CG  HIS A  72     7541   7870   4460   1002   -339   -519       C  
ATOM    537  ND1 HIS A  72     -19.085 -12.050  47.643  1.00 52.95           N  
ANISOU  537  ND1 HIS A  72     7603   7977   4539   1015   -339   -526       N  
ATOM    538  CD2 HIS A  72     -20.110 -12.140  49.574  1.00 53.21           C  
ANISOU  538  CD2 HIS A  72     7654   8015   4548    967   -336   -496       C  
ATOM    539  CE1 HIS A  72     -20.382 -11.961  47.403  1.00 54.26           C  
ANISOU  539  CE1 HIS A  72     7755   8184   4676    989   -338   -509       C  
ATOM    540  NE2 HIS A  72     -21.024 -12.008  48.559  1.00 54.45           N  
ANISOU  540  NE2 HIS A  72     7790   8213   4687    960   -336   -490       N  
ATOM    541  N   VAL A  73     -14.559 -10.277  50.135  1.00 51.25           N  
ANISOU  541  N   VAL A  73     7388   7624   4459   1133   -286   -543       N  
ATOM    542  CA  VAL A  73     -13.154 -10.276  49.799  1.00 50.61           C  
ANISOU  542  CA  VAL A  73     7311   7508   4409   1171   -288   -565       C  
ATOM    543  C   VAL A  73     -12.495 -11.343  50.664  1.00 51.25           C  
ANISOU  543  C   VAL A  73     7440   7544   4490   1162   -318   -583       C  
ATOM    544  O   VAL A  73     -11.409 -11.867  50.341  1.00 51.45           O  
ANISOU  544  O   VAL A  73     7482   7535   4531   1184   -335   -610       O  
ATOM    545  CB  VAL A  73     -12.525  -8.859  49.965  1.00 48.76           C  
ANISOU  545  CB  VAL A  73     7039   7274   4214   1210   -253   -550       C  
ATOM    546  CG1 VAL A  73     -12.456  -8.446  51.413  1.00 47.97           C  
ANISOU  546  CG1 VAL A  73     6944   7156   4125   1206   -241   -533       C  
ATOM    547  CG2 VAL A  73     -11.160  -8.821  49.321  1.00 48.28           C  
ANISOU  547  CG2 VAL A  73     6977   7186   4183   1250   -255   -572       C  
ATOM    548  N   ASP A  74     -13.205 -11.742  51.716  1.00 52.30           N  
ANISOU  548  N   ASP A  74     7595   7676   4601   1125   -327   -570       N  
ATOM    549  CA  ASP A  74     -12.622 -12.667  52.666  1.00 52.97           C  
ANISOU  549  CA  ASP A  74     7725   7718   4685   1114   -355   -583       C  
ATOM    550  C   ASP A  74     -12.683 -14.078  52.146  1.00 54.84           C  
ANISOU  550  C   ASP A  74     7998   7942   4898   1094   -397   -608       C  
ATOM    551  O   ASP A  74     -12.028 -14.948  52.672  1.00 55.67           O  
ANISOU  551  O   ASP A  74     8141   8006   5005   1092   -427   -626       O  
ATOM    552  CB  ASP A  74     -13.305 -12.543  54.009  1.00 52.96           C  
ANISOU  552  CB  ASP A  74     7734   7721   4668   1083   -349   -559       C  
ATOM    553  CG  ASP A  74     -12.925 -11.274  54.697  1.00 51.18           C  
ANISOU  553  CG  ASP A  74     7481   7493   4473   1108   -313   -540       C  
ATOM    554  OD1 ASP A  74     -12.313 -10.426  54.008  1.00 50.04           O  
ANISOU  554  OD1 ASP A  74     7303   7351   4358   1148   -292   -543       O  
ATOM    555  OD2 ASP A  74     -13.205 -11.120  55.907  1.00 51.00           O  
ANISOU  555  OD2 ASP A  74     7468   7465   4445   1089   -307   -523       O  
ATOM    556  N   ASP A  75     -13.515 -14.316  51.146  1.00 52.01           N  
ANISOU  556  N   ASP A  75     7628   7618   4514   1078   -403   -609       N  
ATOM    557  CA  ASP A  75     -13.361 -15.493  50.323  1.00 53.54           C  
ANISOU  557  CA  ASP A  75     7847   7800   4694   1071   -440   -638       C  
ATOM    558  C   ASP A  75     -13.467 -15.063  48.879  1.00 53.45           C  
ANISOU  558  C   ASP A  75     7804   7821   4685   1091   -426   -645       C  
ATOM    559  O   ASP A  75     -14.566 -15.002  48.344  1.00 54.05           O  
ANISOU  559  O   ASP A  75     7865   7936   4734   1068   -424   -632       O  
ATOM    560  CB  ASP A  75     -14.460 -16.508  50.670  1.00 55.31           C  
ANISOU  560  CB  ASP A  75     8102   8037   4878   1019   -472   -633       C  
ATOM    561  CG  ASP A  75     -14.395 -17.782  49.831  1.00 57.07           C  
ANISOU  561  CG  ASP A  75     8352   8248   5084   1009   -514   -663       C  
ATOM    562  OD1 ASP A  75     -14.032 -17.741  48.628  1.00 57.65           O  
ANISOU  562  OD1 ASP A  75     8410   8329   5166   1034   -512   -682       O  
ATOM    563  OD2 ASP A  75     -14.728 -18.845  50.401  1.00 57.97           O  
ANISOU  563  OD2 ASP A  75     8504   8346   5175    975   -551   -667       O  
ATOM    564  N   MET A  76     -12.351 -14.859  48.206  1.00 50.62           N  
ANISOU  564  N   MET A  76     7436   7443   4355   1131   -421   -666       N  
ATOM    565  CA  MET A  76     -12.427 -14.621  46.777  1.00 50.96           C  
ANISOU  565  CA  MET A  76     7453   7514   4395   1146   -413   -675       C  
ATOM    566  C   MET A  76     -12.640 -15.826  45.868  1.00 53.00           C  
ANISOU  566  C   MET A  76     7735   7774   4630   1130   -449   -702       C  
ATOM    567  O   MET A  76     -13.350 -15.703  44.884  1.00 53.63           O  
ANISOU  567  O   MET A  76     7796   7890   4691   1122   -445   -699       O  
ATOM    568  CB  MET A  76     -11.222 -13.844  46.323  1.00 49.72           C  
ANISOU  568  CB  MET A  76     7273   7344   4276   1194   -390   -684       C  
ATOM    569  CG  MET A  76     -11.625 -12.433  45.998  1.00 48.46           C  
ANISOU  569  CG  MET A  76     7065   7222   4126   1208   -350   -656       C  
ATOM    570  SD  MET A  76     -10.521 -11.186  46.620  1.00 46.25           S  
ANISOU  570  SD  MET A  76     6761   6921   3892   1250   -317   -644       S  
ATOM    571  CE  MET A  76      -9.580 -12.134  47.830  1.00 46.39           C  
ANISOU  571  CE  MET A  76     6825   6879   3921   1250   -345   -663       C  
ATOM    572  N   PRO A  77     -11.968 -16.969  46.135  1.00 50.03           N  
ANISOU  572  N   PRO A  77     7398   7355   4255   1128   -485   -731       N  
ATOM    573  CA  PRO A  77     -12.076 -18.046  45.133  1.00 52.05           C  
ANISOU  573  CA  PRO A  77     7672   7613   4493   1119   -519   -760       C  
ATOM    574  C   PRO A  77     -13.481 -18.674  45.024  1.00 53.63           C  
ANISOU  574  C   PRO A  77     7883   7842   4651   1072   -541   -749       C  
ATOM    575  O   PRO A  77     -13.876 -19.074  43.929  1.00 54.94           O  
ANISOU  575  O   PRO A  77     8045   8029   4799   1066   -554   -762       O  
ATOM    576  CB  PRO A  77     -11.052 -19.084  45.618  1.00 52.82           C  
ANISOU  576  CB  PRO A  77     7810   7655   4605   1127   -555   -792       C  
ATOM    577  CG  PRO A  77     -10.192 -18.366  46.633  1.00 51.01           C  
ANISOU  577  CG  PRO A  77     7577   7397   4407   1152   -533   -781       C  
ATOM    578  CD  PRO A  77     -11.085 -17.366  47.254  1.00 49.68           C  
ANISOU  578  CD  PRO A  77     7384   7261   4230   1136   -500   -740       C  
ATOM    579  N   ASN A  78     -14.222 -18.770  46.122  1.00 53.02           N  
ANISOU  579  N   ASN A  78     7820   7767   4558   1039   -546   -725       N  
ATOM    580  CA  ASN A  78     -15.617 -19.155  45.995  1.00 54.41           C  
ANISOU  580  CA  ASN A  78     8000   7979   4696    995   -560   -709       C  
ATOM    581  C   ASN A  78     -16.389 -18.151  45.145  1.00 53.88           C  
ANISOU  581  C   ASN A  78     7889   7962   4621   1000   -527   -689       C  
ATOM    582  O   ASN A  78     -17.056 -18.528  44.182  1.00 55.31           O  
ANISOU  582  O   ASN A  78     8066   8170   4779    986   -541   -695       O  
ATOM    583  CB  ASN A  78     -16.279 -19.289  47.365  1.00 54.43           C  
ANISOU  583  CB  ASN A  78     8020   7978   4682    959   -566   -684       C  
ATOM    584  CG  ASN A  78     -15.832 -20.540  48.107  1.00 55.48           C  
ANISOU  584  CG  ASN A  78     8202   8066   4812    942   -610   -703       C  
ATOM    585  OD1 ASN A  78     -14.679 -20.652  48.492  1.00 54.94           O  
ANISOU  585  OD1 ASN A  78     8149   7955   4772    969   -614   -720       O  
ATOM    586  ND2 ASN A  78     -16.753 -21.485  48.310  1.00 57.13           N  
ANISOU  586  ND2 ASN A  78     8436   8282   4987    897   -645   -699       N  
ATOM    587  N   ALA A  79     -16.283 -16.877  45.502  1.00 51.04           N  
ANISOU  587  N   ALA A  79     7496   7614   4281   1020   -485   -665       N  
ATOM    588  CA  ALA A  79     -16.950 -15.826  44.753  1.00 50.48           C  
ANISOU  588  CA  ALA A  79     7383   7590   4208   1029   -454   -645       C  
ATOM    589  C   ALA A  79     -16.560 -15.840  43.273  1.00 51.12           C  
ANISOU  589  C   ALA A  79     7449   7681   4292   1053   -455   -667       C  
ATOM    590  O   ALA A  79     -17.407 -15.738  42.388  1.00 52.20           O  
ANISOU  590  O   ALA A  79     7570   7856   4409   1042   -455   -660       O  
ATOM    591  CB  ALA A  79     -16.646 -14.479  45.368  1.00 48.30           C  
ANISOU  591  CB  ALA A  79     7075   7316   3959   1054   -411   -621       C  
ATOM    592  N   LEU A  80     -15.276 -15.992  42.995  1.00 51.86           N  
ANISOU  592  N   LEU A  80     7551   7743   4412   1085   -457   -693       N  
ATOM    593  CA  LEU A  80     -14.803 -15.879  41.615  1.00 52.38           C  
ANISOU  593  CA  LEU A  80     7600   7819   4483   1111   -453   -713       C  
ATOM    594  C   LEU A  80     -14.724 -17.210  40.904  1.00 54.58           C  
ANISOU  594  C   LEU A  80     7909   8086   4743   1099   -493   -747       C  
ATOM    595  O   LEU A  80     -14.258 -17.273  39.771  1.00 55.33           O  
ANISOU  595  O   LEU A  80     7995   8187   4840   1119   -494   -768       O  
ATOM    596  CB  LEU A  80     -13.439 -15.212  41.572  1.00 50.90           C  
ANISOU  596  CB  LEU A  80     7398   7609   4334   1155   -430   -723       C  
ATOM    597  CG  LEU A  80     -13.437 -13.695  41.703  1.00 49.09           C  
ANISOU  597  CG  LEU A  80     7127   7400   4126   1177   -386   -692       C  
ATOM    598  CD1 LEU A  80     -12.542 -13.307  42.857  1.00 47.33           C  
ANISOU  598  CD1 LEU A  80     6908   7141   3934   1196   -374   -688       C  
ATOM    599  CD2 LEU A  80     -12.943 -13.115  40.402  1.00 49.27           C  
ANISOU  599  CD2 LEU A  80     7121   7441   4158   1206   -369   -701       C  
ATOM    600  N   SER A  81     -15.180 -18.258  41.588  1.00 53.09           N  
ANISOU  600  N   SER A  81     7756   7882   4535   1065   -528   -752       N  
ATOM    601  CA  SER A  81     -15.083 -19.636  41.114  1.00 55.31           C  
ANISOU  601  CA  SER A  81     8071   8145   4801   1051   -573   -785       C  
ATOM    602  C   SER A  81     -15.590 -19.831  39.688  1.00 56.88           C  
ANISOU  602  C   SER A  81     8257   8377   4979   1048   -581   -797       C  
ATOM    603  O   SER A  81     -14.894 -20.384  38.851  1.00 57.89           O  
ANISOU  603  O   SER A  81     8393   8490   5111   1065   -596   -830       O  
ATOM    604  CB  SER A  81     -15.842 -20.552  42.064  1.00 56.40           C  
ANISOU  604  CB  SER A  81     8242   8271   4915   1008   -607   -778       C  
ATOM    605  OG  SER A  81     -16.070 -21.813  41.479  1.00 58.70           O  
ANISOU  605  OG  SER A  81     8561   8555   5186    989   -652   -804       O  
ATOM    606  N   ALA A  82     -16.789 -19.364  39.391  1.00 54.11           N  
ANISOU  606  N   ALA A  82     7886   8070   4605   1027   -570   -770       N  
ATOM    607  CA  ALA A  82     -17.308 -19.557  38.047  1.00 55.78           C  
ANISOU  607  CA  ALA A  82     8087   8312   4795   1022   -579   -780       C  
ATOM    608  C   ALA A  82     -16.455 -18.809  37.040  1.00 55.12           C  
ANISOU  608  C   ALA A  82     7976   8236   4731   1063   -551   -791       C  
ATOM    609  O   ALA A  82     -16.415 -19.166  35.869  1.00 56.66           O  
ANISOU  609  O   ALA A  82     8170   8444   4915   1068   -562   -813       O  
ATOM    610  CB  ALA A  82     -18.757 -19.112  37.960  1.00 56.16           C  
ANISOU  610  CB  ALA A  82     8117   8406   4816    994   -571   -747       C  
ATOM    611  N   LEU A  83     -15.791 -17.751  37.495  1.00 55.08           N  
ANISOU  611  N   LEU A  83     7949   8225   4755   1091   -514   -777       N  
ATOM    612  CA  LEU A  83     -14.850 -17.009  36.649  1.00 54.71           C  
ANISOU  612  CA  LEU A  83     7876   8181   4730   1131   -487   -786       C  
ATOM    613  C   LEU A  83     -13.450 -17.668  36.580  1.00 54.93           C  
ANISOU  613  C   LEU A  83     7925   8166   4780   1156   -501   -824       C  
ATOM    614  O   LEU A  83     -12.708 -17.469  35.595  1.00 55.09           O  
ANISOU  614  O   LEU A  83     7932   8190   4809   1182   -492   -843       O  
ATOM    615  CB  LEU A  83     -14.733 -15.561  37.130  1.00 53.44           C  
ANISOU  615  CB  LEU A  83     7681   8032   4593   1151   -444   -753       C  
ATOM    616  CG  LEU A  83     -15.872 -14.662  36.668  1.00 53.24           C  
ANISOU  616  CG  LEU A  83     7622   8054   4551   1140   -423   -722       C  
ATOM    617  CD1 LEU A  83     -15.692 -13.293  37.205  1.00 52.01           C  
ANISOU  617  CD1 LEU A  83     7435   7906   4422   1161   -384   -692       C  
ATOM    618  CD2 LEU A  83     -15.929 -14.629  35.165  1.00 53.88           C  
ANISOU  618  CD2 LEU A  83     7690   8163   4618   1149   -424   -735       C  
ATOM    619  N   SER A  84     -13.091 -18.437  37.618  1.00 55.51           N  
ANISOU  619  N   SER A  84     8030   8199   4861   1148   -525   -836       N  
ATOM    620  CA  SER A  84     -11.845 -19.202  37.609  1.00 56.09           C  
ANISOU  620  CA  SER A  84     8127   8229   4954   1169   -545   -874       C  
ATOM    621  C   SER A  84     -11.836 -19.980  36.326  1.00 58.38           C  
ANISOU  621  C   SER A  84     8425   8530   5228   1168   -568   -906       C  
ATOM    622  O   SER A  84     -10.930 -19.845  35.505  1.00 58.69           O  
ANISOU  622  O   SER A  84     8453   8566   5281   1198   -558   -929       O  
ATOM    623  CB  SER A  84     -11.735 -20.170  38.794  1.00 56.38           C  
ANISOU  623  CB  SER A  84     8203   8224   4993   1151   -578   -883       C  
ATOM    624  OG  SER A  84     -11.449 -19.527  40.020  1.00 54.42           O  
ANISOU  624  OG  SER A  84     7953   7959   4767   1158   -559   -860       O  
ATOM    625  N   ASP A  85     -12.909 -20.745  36.149  1.00 57.27           N  
ANISOU  625  N   ASP A  85     8300   8404   5055   1132   -597   -906       N  
ATOM    626  CA  ASP A  85     -13.007 -21.750  35.106  1.00 59.80           C  
ANISOU  626  CA  ASP A  85     8637   8729   5357   1125   -629   -939       C  
ATOM    627  C   ASP A  85     -13.195 -21.113  33.751  1.00 60.27           C  
ANISOU  627  C   ASP A  85     8666   8830   5405   1137   -606   -938       C  
ATOM    628  O   ASP A  85     -12.809 -21.667  32.728  1.00 61.99           O  
ANISOU  628  O   ASP A  85     8888   9048   5617   1146   -621   -970       O  
ATOM    629  CB  ASP A  85     -14.165 -22.707  35.413  1.00 61.45           C  
ANISOU  629  CB  ASP A  85     8872   8942   5536   1080   -668   -935       C  
ATOM    630  CG  ASP A  85     -14.073 -23.292  36.820  1.00 61.12           C  
ANISOU  630  CG  ASP A  85     8860   8861   5502   1064   -690   -931       C  
ATOM    631  OD1 ASP A  85     -13.128 -22.876  37.554  1.00 59.39           O  
ANISOU  631  OD1 ASP A  85     8641   8613   5313   1089   -673   -931       O  
ATOM    632  OD2 ASP A  85     -14.929 -24.148  37.188  1.00 62.71           O  
ANISOU  632  OD2 ASP A  85     9087   9061   5680   1027   -726   -929       O  
ATOM    633  N   LEU A  86     -13.791 -19.935  33.743  1.00 59.54           N  
ANISOU  633  N   LEU A  86     8542   8772   5310   1136   -571   -900       N  
ATOM    634  CA  LEU A  86     -14.155 -19.322  32.479  1.00 60.13           C  
ANISOU  634  CA  LEU A  86     8588   8888   5369   1143   -553   -894       C  
ATOM    635  C   LEU A  86     -12.909 -18.880  31.730  1.00 59.80           C  
ANISOU  635  C   LEU A  86     8530   8841   5349   1181   -531   -914       C  
ATOM    636  O   LEU A  86     -12.763 -19.144  30.531  1.00 61.52           O  
ANISOU  636  O   LEU A  86     8746   9075   5555   1187   -537   -937       O  
ATOM    637  CB  LEU A  86     -15.103 -18.139  32.700  1.00 58.73           C  
ANISOU  637  CB  LEU A  86     8380   8748   5187   1134   -522   -849       C  
ATOM    638  CG  LEU A  86     -15.519 -17.403  31.428  1.00 59.44           C  
ANISOU  638  CG  LEU A  86     8440   8882   5261   1141   -503   -839       C  
ATOM    639  CD1 LEU A  86     -16.028 -18.371  30.355  1.00 62.24           C  
ANISOU  639  CD1 LEU A  86     8811   9253   5586   1123   -535   -863       C  
ATOM    640  CD2 LEU A  86     -16.554 -16.345  31.765  1.00 58.21           C  
ANISOU  640  CD2 LEU A  86     8257   8760   5101   1130   -479   -794       C  
ATOM    641  N   HIS A  87     -12.014 -18.203  32.438  1.00 60.57           N  
ANISOU  641  N   HIS A  87     8618   8917   5479   1207   -507   -906       N  
ATOM    642  CA  HIS A  87     -10.797 -17.717  31.816  1.00 60.22           C  
ANISOU  642  CA  HIS A  87     8557   8867   5457   1243   -485   -923       C  
ATOM    643  C   HIS A  87      -9.753 -18.818  31.721  1.00 61.45           C  
ANISOU  643  C   HIS A  87     8741   8984   5625   1256   -512   -969       C  
ATOM    644  O   HIS A  87      -9.075 -18.959  30.700  1.00 62.65           O  
ANISOU  644  O   HIS A  87     8887   9141   5777   1274   -511   -996       O  
ATOM    645  CB  HIS A  87     -10.264 -16.532  32.593  1.00 57.66           C  
ANISOU  645  CB  HIS A  87     8209   8535   5164   1265   -450   -895       C  
ATOM    646  CG  HIS A  87     -11.277 -15.454  32.771  1.00 56.68           C  
ANISOU  646  CG  HIS A  87     8058   8446   5032   1254   -424   -851       C  
ATOM    647  ND1 HIS A  87     -12.355 -15.589  33.619  1.00 56.63           N  
ANISOU  647  ND1 HIS A  87     8060   8444   5011   1225   -434   -828       N  
ATOM    648  CD2 HIS A  87     -11.411 -14.242  32.180  1.00 55.91           C  
ANISOU  648  CD2 HIS A  87     7924   8382   4938   1267   -391   -827       C  
ATOM    649  CE1 HIS A  87     -13.094 -14.495  33.559  1.00 55.81           C  
ANISOU  649  CE1 HIS A  87     7926   8375   4905   1222   -407   -792       C  
ATOM    650  NE2 HIS A  87     -12.545 -13.664  32.694  1.00 55.36           N  
ANISOU  650  NE2 HIS A  87     7842   8335   4859   1248   -382   -791       N  
ATOM    651  N   ALA A  88      -9.630 -19.610  32.778  1.00 58.72           N  
ANISOU  651  N   ALA A  88     8425   8600   5287   1246   -539   -978       N  
ATOM    652  CA  ALA A  88      -8.616 -20.637  32.784  1.00 59.98           C  
ANISOU  652  CA  ALA A  88     8610   8718   5461   1260   -567  -1021       C  
ATOM    653  C   ALA A  88      -8.859 -21.607  31.631  1.00 62.75           C  
ANISOU  653  C   ALA A  88     8974   9081   5787   1249   -595  -1055       C  
ATOM    654  O   ALA A  88      -8.027 -21.722  30.730  1.00 63.79           O  
ANISOU  654  O   ALA A  88     9099   9212   5925   1272   -592  -1084       O  
ATOM    655  CB  ALA A  88      -8.601 -21.367  34.124  1.00 59.54           C  
ANISOU  655  CB  ALA A  88     8587   8620   5415   1246   -595  -1023       C  
ATOM    656  N   HIS A  89     -10.031 -22.244  31.625  1.00 62.18           N  
ANISOU  656  N   HIS A  89     8918   9022   5686   1214   -622  -1049       N  
ATOM    657  CA  HIS A  89     -10.293 -23.390  30.749  1.00 65.09           C  
ANISOU  657  CA  HIS A  89     9307   9393   6033   1201   -659  -1084       C  
ATOM    658  C   HIS A  89     -10.922 -23.024  29.401  1.00 66.44           C  
ANISOU  658  C   HIS A  89     9456   9612   6176   1195   -646  -1080       C  
ATOM    659  O   HIS A  89     -10.334 -23.264  28.337  1.00 67.92           O  
ANISOU  659  O   HIS A  89     9639   9806   6361   1212   -647  -1111       O  
ATOM    660  CB  HIS A  89     -11.192 -24.391  31.473  1.00 66.26           C  
ANISOU  660  CB  HIS A  89     9486   9525   6164   1164   -701  -1082       C  
ATOM    661  CG  HIS A  89     -10.564 -24.991  32.691  1.00 65.56           C  
ANISOU  661  CG  HIS A  89     9425   9384   6099   1167   -722  -1093       C  
ATOM    662  ND1 HIS A  89     -11.294 -25.352  33.807  1.00 65.12           N  
ANISOU  662  ND1 HIS A  89     9390   9315   6036   1136   -743  -1072       N  
ATOM    663  CD2 HIS A  89      -9.272 -25.296  32.971  1.00 65.36           C  
ANISOU  663  CD2 HIS A  89     9410   9317   6105   1195   -728  -1122       C  
ATOM    664  CE1 HIS A  89     -10.476 -25.846  34.725  1.00 64.64           C  
ANISOU  664  CE1 HIS A  89     9354   9207   6001   1146   -761  -1087       C  
ATOM    665  NE2 HIS A  89      -9.244 -25.824  34.242  1.00 64.77           N  
ANISOU  665  NE2 HIS A  89     9364   9204   6042   1183   -753  -1118       N  
ATOM    666  N   LYS A  90     -12.130 -22.471  29.452  1.00 66.52           N  
ANISOU  666  N   LYS A  90     9453   9658   6164   1171   -636  -1042       N  
ATOM    667  CA  LYS A  90     -12.902 -22.205  28.242  1.00 67.99           C  
ANISOU  667  CA  LYS A  90     9622   9890   6321   1161   -630  -1036       C  
ATOM    668  C   LYS A  90     -12.170 -21.212  27.352  1.00 67.39           C  
ANISOU  668  C   LYS A  90     9516   9836   6255   1192   -591  -1035       C  
ATOM    669  O   LYS A  90     -11.833 -21.522  26.205  1.00 69.25           O  
ANISOU  669  O   LYS A  90     9750  10083   6479   1201   -596  -1063       O  
ATOM    670  CB  LYS A  90     -14.299 -21.689  28.611  1.00 67.31           C  
ANISOU  670  CB  LYS A  90     9526   9835   6215   1132   -624   -993       C  
ATOM    671  CG  LYS A  90     -15.299 -21.595  27.460  1.00 69.01           C  
ANISOU  671  CG  LYS A  90     9729  10096   6396   1115   -628   -985       C  
ATOM    672  CD  LYS A  90     -16.727 -21.513  28.015  1.00 68.64           C  
ANISOU  672  CD  LYS A  90     9682  10069   6328   1080   -638   -950       C  
ATOM    673  CE  LYS A  90     -17.640 -20.631  27.150  1.00 69.44           C  
ANISOU  673  CE  LYS A  90     9754  10221   6408   1074   -618   -922       C  
ATOM    674  NZ  LYS A  90     -18.911 -20.222  27.852  1.00 68.94           N  
ANISOU  674  NZ  LYS A  90     9683  10178   6333   1047   -616   -882       N  
ATOM    675  N   LEU A  91     -11.896 -20.035  27.915  1.00 66.01           N  
ANISOU  675  N   LEU A  91     9317   9664   6101   1208   -554  -1004       N  
ATOM    676  CA  LEU A  91     -11.294 -18.915  27.192  1.00 65.14           C  
ANISOU  676  CA  LEU A  91     9175   9576   6001   1235   -515   -995       C  
ATOM    677  C   LEU A  91      -9.765 -18.987  27.035  1.00 65.05           C  
ANISOU  677  C   LEU A  91     9163   9537   6016   1269   -506  -1026       C  
ATOM    678  O   LEU A  91      -9.214 -18.323  26.150  1.00 65.48           O  
ANISOU  678  O   LEU A  91     9195   9611   6073   1288   -481  -1028       O  
ATOM    679  CB  LEU A  91     -11.669 -17.607  27.890  1.00 62.49           C  
ANISOU  679  CB  LEU A  91     8811   9254   5677   1238   -481   -948       C  
ATOM    680  CG  LEU A  91     -13.123 -17.181  27.674  1.00 62.81           C  
ANISOU  680  CG  LEU A  91     8839   9335   5691   1212   -479   -914       C  
ATOM    681  CD1 LEU A  91     -13.499 -16.019  28.588  1.00 60.79           C  
ANISOU  681  CD1 LEU A  91     8559   9086   5451   1214   -449   -870       C  
ATOM    682  CD2 LEU A  91     -13.364 -16.801  26.218  1.00 63.09           C  
ANISOU  682  CD2 LEU A  91     8856   9410   5704   1215   -469   -916       C  
ATOM    683  N   ARG A  92      -9.106 -19.775  27.892  1.00 62.22           N  
ANISOU  683  N   ARG A  92     8829   9133   5678   1274   -528  -1048       N  
ATOM    684  CA  ARG A  92      -7.644 -19.890  27.953  1.00 62.07           C  
ANISOU  684  CA  ARG A  92     8812   9083   5690   1305   -522  -1077       C  
ATOM    685  C   ARG A  92      -6.915 -18.546  27.787  1.00 60.28           C  
ANISOU  685  C   ARG A  92     8551   8869   5484   1333   -478  -1056       C  
ATOM    686  O   ARG A  92      -6.308 -18.285  26.737  1.00 61.30           O  
ANISOU  686  O   ARG A  92     8666   9016   5611   1349   -463  -1072       O  
ATOM    687  CB  ARG A  92      -7.117 -20.901  26.922  1.00 64.93           C  
ANISOU  687  CB  ARG A  92     9190   9440   6042   1311   -546  -1126       C  
ATOM    688  CG  ARG A  92      -6.086 -21.891  27.545  1.00 65.45           C  
ANISOU  688  CG  ARG A  92     9282   9453   6134   1325   -573  -1164       C  
ATOM    689  CD  ARG A  92      -5.558 -22.960  26.577  1.00 68.40           C  
ANISOU  689  CD  ARG A  92     9670   9819   6501   1331   -600  -1216       C  
ATOM    690  NE  ARG A  92      -4.152 -22.753  26.228  1.00 68.67           N  
ANISOU  690  NE  ARG A  92     9692   9839   6559   1364   -583  -1242       N  
ATOM    691  CZ  ARG A  92      -3.111 -23.171  26.960  1.00 68.02           C  
ANISOU  691  CZ  ARG A  92     9623   9711   6510   1383   -595  -1263       C  
ATOM    692  NH1 ARG A  92      -3.300 -23.835  28.100  1.00 67.06           N  
ANISOU  692  NH1 ARG A  92     9528   9551   6400   1373   -624  -1263       N  
ATOM    693  NH2 ARG A  92      -1.867 -22.922  26.552  1.00 68.45           N  
ANISOU  693  NH2 ARG A  92     9663   9758   6586   1412   -578  -1285       N  
ATOM    694  N   VAL A  93      -6.994 -17.691  28.808  1.00 61.18           N  
ANISOU  694  N   VAL A  93     8653   8976   5617   1337   -457  -1021       N  
ATOM    695  CA  VAL A  93      -6.340 -16.381  28.755  1.00 59.94           C  
ANISOU  695  CA  VAL A  93     8463   8830   5482   1362   -417   -998       C  
ATOM    696  C   VAL A  93      -4.936 -16.430  29.353  1.00 59.42           C  
ANISOU  696  C   VAL A  93     8402   8723   5453   1390   -415  -1017       C  
ATOM    697  O   VAL A  93      -4.773 -16.806  30.511  1.00 58.93           O  
ANISOU  697  O   VAL A  93     8358   8625   5408   1389   -429  -1017       O  
ATOM    698  CB  VAL A  93      -7.162 -15.303  29.487  1.00 58.54           C  
ANISOU  698  CB  VAL A  93     8266   8669   5308   1353   -395   -949       C  
ATOM    699  CG1 VAL A  93      -6.515 -13.955  29.280  1.00 57.40           C  
ANISOU  699  CG1 VAL A  93     8086   8537   5185   1379   -356   -927       C  
ATOM    700  CG2 VAL A  93      -8.602 -15.297  28.984  1.00 59.08           C  
ANISOU  700  CG2 VAL A  93     8331   8776   5341   1324   -400   -930       C  
ATOM    701  N   ASP A  94      -3.929 -16.043  28.579  1.00 56.96           N  
ANISOU  701  N   ASP A  94     8074   8417   5153   1414   -397  -1032       N  
ATOM    702  CA  ASP A  94      -2.553 -16.119  29.056  1.00 56.58           C  
ANISOU  702  CA  ASP A  94     8028   8331   5139   1441   -395  -1052       C  
ATOM    703  C   ASP A  94      -2.308 -15.208  30.259  1.00 54.86           C  
ANISOU  703  C   ASP A  94     7798   8095   4951   1452   -376  -1018       C  
ATOM    704  O   ASP A  94      -2.341 -13.981  30.121  1.00 53.86           O  
ANISOU  704  O   ASP A  94     7641   7992   4830   1460   -344   -986       O  
ATOM    705  CB  ASP A  94      -1.592 -15.751  27.930  1.00 57.01           C  
ANISOU  705  CB  ASP A  94     8063   8402   5198   1462   -376  -1070       C  
ATOM    706  CG  ASP A  94      -0.138 -16.063  28.266  1.00 56.94           C  
ANISOU  706  CG  ASP A  94     8059   8353   5221   1488   -380  -1099       C  
ATOM    707  OD1 ASP A  94       0.309 -15.853  29.437  1.00 55.91           O  
ANISOU  707  OD1 ASP A  94     7933   8189   5120   1498   -380  -1087       O  
ATOM    708  OD2 ASP A  94       0.562 -16.519  27.329  1.00 58.77           O  
ANISOU  708  OD2 ASP A  94     8292   8589   5449   1497   -384  -1135       O  
ATOM    709  N   PRO A  95      -1.962 -15.792  31.417  1.00 53.28           N  
ANISOU  709  N   PRO A  95     7622   7852   4771   1454   -396  -1026       N  
ATOM    710  CA  PRO A  95      -1.854 -15.096  32.708  1.00 51.75           C  
ANISOU  710  CA  PRO A  95     7423   7637   4603   1461   -383   -995       C  
ATOM    711  C   PRO A  95      -1.074 -13.770  32.670  1.00 50.52           C  
ANISOU  711  C   PRO A  95     7233   7490   4473   1486   -347   -973       C  
ATOM    712  O   PRO A  95      -1.195 -12.967  33.606  1.00 49.18           O  
ANISOU  712  O   PRO A  95     7053   7313   4320   1490   -332   -941       O  
ATOM    713  CB  PRO A  95      -1.119 -16.114  33.581  1.00 52.06           C  
ANISOU  713  CB  PRO A  95     7494   7624   4661   1467   -414  -1024       C  
ATOM    714  CG  PRO A  95      -1.645 -17.401  33.110  1.00 53.59           C  
ANISOU  714  CG  PRO A  95     7716   7817   4830   1447   -449  -1055       C  
ATOM    715  CD  PRO A  95      -1.850 -17.247  31.595  1.00 54.50           C  
ANISOU  715  CD  PRO A  95     7813   7975   4921   1446   -437  -1065       C  
ATOM    716  N   VAL A  96      -0.265 -13.562  31.633  1.00 54.28           N  
ANISOU  716  N   VAL A  96     7694   7979   4952   1503   -335   -991       N  
ATOM    717  CA  VAL A  96       0.401 -12.281  31.470  1.00 53.29           C  
ANISOU  717  CA  VAL A  96     7535   7865   4847   1524   -302   -969       C  
ATOM    718  C   VAL A  96      -0.610 -11.166  31.213  1.00 52.73           C  
ANISOU  718  C   VAL A  96     7437   7835   4762   1514   -276   -926       C  
ATOM    719  O   VAL A  96      -0.343  -9.979  31.542  1.00 51.27           O  
ANISOU  719  O   VAL A  96     7227   7655   4597   1527   -251   -896       O  
ATOM    720  CB  VAL A  96       1.414 -12.288  30.316  1.00 54.26           C  
ANISOU  720  CB  VAL A  96     7646   7998   4971   1541   -293   -996       C  
ATOM    721  CG1 VAL A  96       0.705 -12.173  28.953  1.00 55.72           C  
ANISOU  721  CG1 VAL A  96     7820   8230   5120   1527   -284   -997       C  
ATOM    722  CG2 VAL A  96       2.413 -11.156  30.506  1.00 53.29           C  
ANISOU  722  CG2 VAL A  96     7498   7871   4880   1564   -266   -978       C  
ATOM    723  N   ASN A  97      -1.768 -11.526  30.642  1.00 50.90           N  
ANISOU  723  N   ASN A  97     7212   7633   4496   1490   -285   -924       N  
ATOM    724  CA  ASN A  97      -2.697 -10.505  30.172  1.00 50.77           C  
ANISOU  724  CA  ASN A  97     7168   7658   4463   1481   -262   -888       C  
ATOM    725  C   ASN A  97      -3.383  -9.828  31.333  1.00 49.52           C  
ANISOU  725  C   ASN A  97     7002   7496   4317   1474   -253   -850       C  
ATOM    726  O   ASN A  97      -3.592  -8.628  31.292  1.00 48.73           O  
ANISOU  726  O   ASN A  97     6873   7417   4224   1481   -228   -817       O  
ATOM    727  CB  ASN A  97      -3.686 -11.106  29.195  1.00 52.46           C  
ANISOU  727  CB  ASN A  97     7390   7904   4638   1457   -275   -898       C  
ATOM    728  CG  ASN A  97      -3.088 -11.275  27.806  1.00 53.71           C  
ANISOU  728  CG  ASN A  97     7543   8082   4782   1466   -272   -926       C  
ATOM    729  OD1 ASN A  97      -2.554 -10.322  27.231  1.00 53.75           O  
ANISOU  729  OD1 ASN A  97     7522   8105   4795   1481   -246   -914       O  
ATOM    730  ND2 ASN A  97      -3.140 -12.498  27.272  1.00 54.85           N  
ANISOU  730  ND2 ASN A  97     7713   8222   4907   1455   -298   -963       N  
ATOM    731  N   PHE A  98      -3.665 -10.593  32.384  1.00 48.71           N  
ANISOU  731  N   PHE A  98     6926   7364   4217   1462   -275   -855       N  
ATOM    732  CA  PHE A  98      -4.288 -10.079  33.593  1.00 48.05           C  
ANISOU  732  CA  PHE A  98     6840   7274   4144   1454   -268   -823       C  
ATOM    733  C   PHE A  98      -3.451  -8.969  34.233  1.00 47.16           C  
ANISOU  733  C   PHE A  98     6704   7146   4068   1480   -244   -801       C  
ATOM    734  O   PHE A  98      -3.994  -8.008  34.785  1.00 46.57           O  
ANISOU  734  O   PHE A  98     6609   7083   4001   1479   -226   -766       O  
ATOM    735  CB  PHE A  98      -4.523 -11.219  34.588  1.00 48.26           C  
ANISOU  735  CB  PHE A  98     6902   7266   4167   1438   -298   -838       C  
ATOM    736  CG  PHE A  98      -5.547 -12.198  34.126  1.00 49.06           C  
ANISOU  736  CG  PHE A  98     7025   7384   4232   1408   -322   -851       C  
ATOM    737  CD1 PHE A  98      -6.773 -12.298  34.751  1.00 49.06           C  
ANISOU  737  CD1 PHE A  98     7032   7394   4214   1380   -329   -829       C  
ATOM    738  CD2 PHE A  98      -5.311 -12.999  33.013  1.00 49.86           C  
ANISOU  738  CD2 PHE A  98     7137   7492   4315   1407   -338   -885       C  
ATOM    739  CE1 PHE A  98      -7.746 -13.188  34.268  1.00 49.84           C  
ANISOU  739  CE1 PHE A  98     7149   7510   4278   1351   -353   -840       C  
ATOM    740  CE2 PHE A  98      -6.271 -13.888  32.547  1.00 50.63           C  
ANISOU  740  CE2 PHE A  98     7253   7605   4379   1380   -362   -896       C  
ATOM    741  CZ  PHE A  98      -7.488 -13.978  33.172  1.00 50.61           C  
ANISOU  741  CZ  PHE A  98     7257   7612   4359   1352   -370   -873       C  
ATOM    742  N   LYS A  99      -2.129  -9.081  34.131  1.00 48.28           N  
ANISOU  742  N   LYS A  99     6848   7263   4232   1504   -244   -823       N  
ATOM    743  CA  LYS A  99      -1.245  -8.112  34.753  1.00 46.82           C  
ANISOU  743  CA  LYS A  99     6645   7062   4084   1528   -226   -805       C  
ATOM    744  C   LYS A  99      -1.246  -6.773  33.986  1.00 46.46           C  
ANISOU  744  C   LYS A  99     6560   7051   4040   1540   -195   -779       C  
ATOM    745  O   LYS A  99      -1.026  -5.698  34.575  1.00 45.34           O  
ANISOU  745  O   LYS A  99     6397   6906   3923   1553   -177   -750       O  
ATOM    746  CB  LYS A  99       0.156  -8.691  34.875  1.00 46.65           C  
ANISOU  746  CB  LYS A  99     6639   7003   4084   1548   -238   -838       C  
ATOM    747  CG  LYS A  99       0.350  -9.371  36.211  1.00 46.09           C  
ANISOU  747  CG  LYS A  99     6596   6887   4028   1547   -259   -845       C  
ATOM    748  CD  LYS A  99      -0.370  -8.554  37.275  1.00 45.50           C  
ANISOU  748  CD  LYS A  99     6512   6815   3962   1540   -245   -805       C  
ATOM    749  CE  LYS A  99      -0.570  -9.305  38.589  1.00 45.19           C  
ANISOU  749  CE  LYS A  99     6504   6739   3927   1529   -267   -809       C  
ATOM    750  NZ  LYS A  99       0.717  -9.630  39.220  1.00 44.73           N  
ANISOU  750  NZ  LYS A  99     6461   6636   3898   1551   -279   -828       N  
ATOM    751  N   LEU A 100      -1.511  -6.839  32.683  1.00 49.83           N  
ANISOU  751  N   LEU A 100     6980   7512   4443   1533   -192   -788       N  
ATOM    752  CA  LEU A 100      -1.763  -5.641  31.910  1.00 49.87           C  
ANISOU  752  CA  LEU A 100     6950   7554   4443   1539   -167   -761       C  
ATOM    753  C   LEU A 100      -2.999  -4.915  32.447  1.00 49.58           C  
ANISOU  753  C   LEU A 100     6899   7537   4402   1526   -157   -723       C  
ATOM    754  O   LEU A 100      -2.929  -3.773  32.940  1.00 48.55           O  
ANISOU  754  O   LEU A 100     6744   7408   4293   1539   -138   -692       O  
ATOM    755  CB  LEU A 100      -1.984  -6.006  30.456  1.00 51.38           C  
ANISOU  755  CB  LEU A 100     7142   7778   4603   1530   -169   -780       C  
ATOM    756  CG  LEU A 100      -0.825  -6.734  29.806  1.00 51.99           C  
ANISOU  756  CG  LEU A 100     7232   7841   4682   1541   -177   -820       C  
ATOM    757  CD1 LEU A 100      -1.219  -7.337  28.474  1.00 53.64           C  
ANISOU  757  CD1 LEU A 100     7446   8079   4854   1528   -184   -842       C  
ATOM    758  CD2 LEU A 100       0.309  -5.745  29.629  1.00 51.46           C  
ANISOU  758  CD2 LEU A 100     7141   7772   4641   1566   -155   -811       C  
ATOM    759  N   LEU A 101      -4.136  -5.601  32.380  1.00 49.42           N  
ANISOU  759  N   LEU A 101     6894   7531   4353   1500   -172   -726       N  
ATOM    760  CA  LEU A 101      -5.380  -5.008  32.781  1.00 49.41           C  
ANISOU  760  CA  LEU A 101     6880   7552   4343   1486   -164   -693       C  
ATOM    761  C   LEU A 101      -5.288  -4.619  34.245  1.00 48.08           C  
ANISOU  761  C   LEU A 101     6710   7355   4202   1491   -160   -674       C  
ATOM    762  O   LEU A 101      -5.871  -3.620  34.642  1.00 47.63           O  
ANISOU  762  O   LEU A 101     6630   7314   4153   1492   -143   -641       O  
ATOM    763  CB  LEU A 101      -6.532  -5.969  32.538  1.00 50.80           C  
ANISOU  763  CB  LEU A 101     7076   7743   4483   1455   -185   -702       C  
ATOM    764  CG  LEU A 101      -7.915  -5.597  33.096  1.00 50.92           C  
ANISOU  764  CG  LEU A 101     7082   7778   4487   1435   -182   -672       C  
ATOM    765  CD1 LEU A 101      -8.507  -4.420  32.347  1.00 51.23           C  
ANISOU  765  CD1 LEU A 101     7086   7859   4520   1439   -161   -643       C  
ATOM    766  CD2 LEU A 101      -8.852  -6.799  33.069  1.00 52.20           C  
ANISOU  766  CD2 LEU A 101     7272   7944   4616   1404   -208   -687       C  
ATOM    767  N   SER A 102      -4.553  -5.392  35.043  1.00 49.65           N  
ANISOU  767  N   SER A 102     6935   7513   4415   1496   -175   -695       N  
ATOM    768  CA  SER A 102      -4.344  -5.041  36.447  1.00 48.47           C  
ANISOU  768  CA  SER A 102     6788   7335   4294   1502   -171   -678       C  
ATOM    769  C   SER A 102      -3.823  -3.633  36.506  1.00 47.45           C  
ANISOU  769  C   SER A 102     6625   7212   4193   1527   -146   -652       C  
ATOM    770  O   SER A 102      -4.257  -2.833  37.313  1.00 46.73           O  
ANISOU  770  O   SER A 102     6519   7122   4115   1528   -133   -623       O  
ATOM    771  CB  SER A 102      -3.324  -5.969  37.145  1.00 48.10           C  
ANISOU  771  CB  SER A 102     6772   7240   4263   1511   -190   -707       C  
ATOM    772  OG  SER A 102      -3.849  -7.231  37.580  1.00 49.53           O  
ANISOU  772  OG  SER A 102     6988   7406   4424   1487   -217   -726       O  
ATOM    773  N   HIS A 103      -2.872  -3.344  35.632  1.00 47.44           N  
ANISOU  773  N   HIS A 103     6612   7214   4199   1546   -138   -663       N  
ATOM    774  CA  HIS A 103      -2.156  -2.075  35.638  1.00 46.54           C  
ANISOU  774  CA  HIS A 103     6468   7101   4113   1570   -117   -641       C  
ATOM    775  C   HIS A 103      -2.995  -1.006  35.001  1.00 46.59           C  
ANISOU  775  C   HIS A 103     6442   7150   4109   1568    -99   -611       C  
ATOM    776  O   HIS A 103      -3.137   0.061  35.566  1.00 46.04           O  
ANISOU  776  O   HIS A 103     6351   7084   4060   1578    -84   -581       O  
ATOM    777  CB  HIS A 103      -0.808  -2.243  34.925  1.00 46.18           C  
ANISOU  777  CB  HIS A 103     6424   7045   4078   1588   -118   -665       C  
ATOM    778  CG  HIS A 103      -0.200  -0.978  34.428  1.00 45.49           C  
ANISOU  778  CG  HIS A 103     6304   6972   4007   1608    -96   -645       C  
ATOM    779  ND1 HIS A 103       0.243   0.017  35.271  1.00 44.68           N  
ANISOU  779  ND1 HIS A 103     6186   6855   3936   1625    -85   -620       N  
ATOM    780  CD2 HIS A 103       0.073  -0.563  33.169  1.00 45.52           C  
ANISOU  780  CD2 HIS A 103     6291   7004   3999   1613    -85   -648       C  
ATOM    781  CE1 HIS A 103       0.741   1.006  34.549  1.00 44.25           C  
ANISOU  781  CE1 HIS A 103     6105   6819   3890   1639    -69   -606       C  
ATOM    782  NE2 HIS A 103       0.653   0.676  33.271  1.00 44.74           N  
ANISOU  782  NE2 HIS A 103     6167   6908   3926   1632    -68   -623       N  
ATOM    783  N   CYS A 104      -3.591  -1.282  33.851  1.00 46.92           N  
ANISOU  783  N   CYS A 104     6483   7225   4120   1555   -101   -619       N  
ATOM    784  CA  CYS A 104      -4.600  -0.355  33.344  1.00 47.34           C  
ANISOU  784  CA  CYS A 104     6508   7318   4160   1549    -87   -590       C  
ATOM    785  C   CYS A 104      -5.675  -0.002  34.413  1.00 46.87           C  
ANISOU  785  C   CYS A 104     6443   7261   4105   1538    -84   -563       C  
ATOM    786  O   CYS A 104      -6.049   1.145  34.557  1.00 46.41           O  
ANISOU  786  O   CYS A 104     6356   7219   4057   1547    -69   -533       O  
ATOM    787  CB  CYS A 104      -5.274  -0.916  32.097  1.00 48.86           C  
ANISOU  787  CB  CYS A 104     6706   7543   4314   1532    -94   -603       C  
ATOM    788  SG  CYS A 104      -4.307  -0.746  30.569  1.00 49.52           S  
ANISOU  788  SG  CYS A 104     6782   7645   4390   1545    -86   -621       S  
ATOM    789  N   LEU A 105      -6.144  -0.972  35.184  1.00 45.69           N  
ANISOU  789  N   LEU A 105     6321   7094   3946   1519   -101   -575       N  
ATOM    790  CA  LEU A 105      -7.061  -0.677  36.265  1.00 45.51           C  
ANISOU  790  CA  LEU A 105     6294   7071   3927   1508    -98   -552       C  
ATOM    791  C   LEU A 105      -6.442   0.181  37.331  1.00 45.09           C  
ANISOU  791  C   LEU A 105     6228   6994   3911   1528    -86   -533       C  
ATOM    792  O   LEU A 105      -7.139   0.829  38.106  1.00 44.90           O  
ANISOU  792  O   LEU A 105     6189   6977   3895   1525    -77   -508       O  
ATOM    793  CB  LEU A 105      -7.580  -1.959  36.891  1.00 45.69           C  
ANISOU  793  CB  LEU A 105     6352   7077   3931   1482   -119   -570       C  
ATOM    794  CG  LEU A 105      -8.785  -2.487  36.091  1.00 46.05           C  
ANISOU  794  CG  LEU A 105     6402   7158   3938   1455   -129   -572       C  
ATOM    795  CD1 LEU A 105      -8.915  -4.019  36.157  1.00 46.36           C  
ANISOU  795  CD1 LEU A 105     6481   7180   3954   1433   -156   -603       C  
ATOM    796  CD2 LEU A 105     -10.102  -1.779  36.507  1.00 45.98           C  
ANISOU  796  CD2 LEU A 105     6372   7176   3921   1442   -119   -540       C  
ATOM    797  N   LEU A 106      -5.121   0.155  37.410  1.00 47.82           N  
ANISOU  797  N   LEU A 106     6580   7311   4280   1549    -86   -547       N  
ATOM    798  CA  LEU A 106      -4.404   1.005  38.365  1.00 46.68           C  
ANISOU  798  CA  LEU A 106     6422   7142   4171   1571    -76   -530       C  
ATOM    799  C   LEU A 106      -4.190   2.406  37.797  1.00 46.48           C  
ANISOU  799  C   LEU A 106     6360   7140   4161   1591    -57   -505       C  
ATOM    800  O   LEU A 106      -4.344   3.406  38.509  1.00 45.88           O  
ANISOU  800  O   LEU A 106     6264   7064   4106   1602    -45   -478       O  
ATOM    801  CB  LEU A 106      -3.099   0.352  38.787  1.00 46.00           C  
ANISOU  801  CB  LEU A 106     6360   7014   4104   1583    -88   -554       C  
ATOM    802  CG  LEU A 106      -3.343  -0.692  39.875  1.00 45.92           C  
ANISOU  802  CG  LEU A 106     6383   6974   4089   1566   -105   -568       C  
ATOM    803  CD1 LEU A 106      -2.083  -1.331  40.314  1.00 45.39           C  
ANISOU  803  CD1 LEU A 106     6341   6866   4041   1580   -118   -592       C  
ATOM    804  CD2 LEU A 106      -3.953  -0.084  41.073  1.00 45.61           C  
ANISOU  804  CD2 LEU A 106     6337   6931   4063   1563    -97   -541       C  
ATOM    805  N   VAL A 107      -3.851   2.471  36.515  1.00 48.83           N  
ANISOU  805  N   VAL A 107     6649   7457   4446   1596    -54   -514       N  
ATOM    806  CA  VAL A 107      -3.737   3.752  35.847  1.00 48.91           C  
ANISOU  806  CA  VAL A 107     6626   7494   4465   1613    -37   -490       C  
ATOM    807  C   VAL A 107      -5.078   4.491  35.921  1.00 49.45           C  
ANISOU  807  C   VAL A 107     6670   7594   4523   1604    -28   -461       C  
ATOM    808  O   VAL A 107      -5.127   5.674  36.298  1.00 49.05           O  
ANISOU  808  O   VAL A 107     6593   7549   4493   1620    -16   -433       O  
ATOM    809  CB  VAL A 107      -3.318   3.605  34.381  1.00 49.77           C  
ANISOU  809  CB  VAL A 107     6732   7625   4555   1615    -35   -506       C  
ATOM    810  CG1 VAL A 107      -3.462   4.925  33.671  1.00 50.21           C  
ANISOU  810  CG1 VAL A 107     6753   7712   4613   1627    -18   -479       C  
ATOM    811  CG2 VAL A 107      -1.904   3.133  34.281  1.00 49.37           C  
ANISOU  811  CG2 VAL A 107     6697   7545   4518   1627    -40   -531       C  
ATOM    812  N   THR A 108      -6.150   3.772  35.574  1.00 50.32           N  
ANISOU  812  N   THR A 108     6792   7726   4603   1580    -36   -469       N  
ATOM    813  CA  THR A 108      -7.510   4.307  35.544  1.00 51.14           C  
ANISOU  813  CA  THR A 108     6876   7863   4692   1569    -30   -445       C  
ATOM    814  C   THR A 108      -7.967   4.870  36.885  1.00 50.54           C  
ANISOU  814  C   THR A 108     6790   7776   4636   1571    -24   -423       C  
ATOM    815  O   THR A 108      -8.454   6.006  36.965  1.00 50.76           O  
ANISOU  815  O   THR A 108     6787   7824   4674   1581    -12   -396       O  
ATOM    816  CB  THR A 108      -8.511   3.243  35.121  1.00 52.31           C  
ANISOU  816  CB  THR A 108     7044   8029   4804   1539    -44   -460       C  
ATOM    817  OG1 THR A 108      -8.438   3.069  33.703  1.00 53.49           O  
ANISOU  817  OG1 THR A 108     7192   8202   4929   1537    -46   -472       O  
ATOM    818  CG2 THR A 108      -9.925   3.677  35.490  1.00 52.62           C  
ANISOU  818  CG2 THR A 108     7067   8094   4831   1525    -40   -436       C  
ATOM    819  N   LEU A 109      -7.823   4.075  37.937  1.00 50.86           N  
ANISOU  819  N   LEU A 109     6857   7784   4682   1561    -34   -436       N  
ATOM    820  CA  LEU A 109      -8.206   4.541  39.264  1.00 50.39           C  
ANISOU  820  CA  LEU A 109     6791   7713   4642   1561    -28   -417       C  
ATOM    821  C   LEU A 109      -7.372   5.734  39.677  1.00 49.37           C  
ANISOU  821  C   LEU A 109     6638   7571   4548   1591    -16   -398       C  
ATOM    822  O   LEU A 109      -7.853   6.605  40.393  1.00 49.04           O  
ANISOU  822  O   LEU A 109     6576   7536   4521   1597     -7   -374       O  
ATOM    823  CB  LEU A 109      -8.054   3.442  40.302  1.00 50.00           C  
ANISOU  823  CB  LEU A 109     6777   7629   4591   1546    -42   -435       C  
ATOM    824  CG  LEU A 109      -9.096   2.349  40.297  1.00 51.02           C  
ANISOU  824  CG  LEU A 109     6929   7769   4686   1513    -55   -448       C  
ATOM    825  CD1 LEU A 109      -8.837   1.448  41.487  1.00 50.50           C  
ANISOU  825  CD1 LEU A 109     6897   7666   4624   1501    -67   -462       C  
ATOM    826  CD2 LEU A 109     -10.404   3.007  40.384  1.00 51.74           C  
ANISOU  826  CD2 LEU A 109     6997   7896   4766   1502    -45   -423       C  
ATOM    827  N   ALA A 110      -6.118   5.769  39.233  1.00 54.08           N  
ANISOU  827  N   ALA A 110     7239   8149   5159   1609    -17   -409       N  
ATOM    828  CA  ALA A 110      -5.243   6.888  39.589  1.00 53.26           C  
ANISOU  828  CA  ALA A 110     7115   8033   5090   1637     -8   -391       C  
ATOM    829  C   ALA A 110      -5.852   8.173  39.025  1.00 53.86           C  
ANISOU  829  C   ALA A 110     7153   8146   5166   1648      5   -363       C  
ATOM    830  O   ALA A 110      -6.152   9.117  39.780  1.00 53.82           O  
ANISOU  830  O   ALA A 110     7127   8142   5180   1658     13   -339       O  
ATOM    831  CB  ALA A 110      -3.816   6.672  39.076  1.00 52.74           C  
ANISOU  831  CB  ALA A 110     7059   7945   5035   1652    -12   -409       C  
ATOM    832  N   ALA A 111      -6.081   8.176  37.716  1.00 54.36           N  
ANISOU  832  N   ALA A 111     7208   8239   5207   1645      7   -367       N  
ATOM    833  CA  ALA A 111      -6.590   9.351  37.039  1.00 55.27           C  
ANISOU  833  CA  ALA A 111     7289   8391   5321   1656     18   -341       C  
ATOM    834  C   ALA A 111      -7.851   9.910  37.715  1.00 55.85           C  
ANISOU  834  C   ALA A 111     7344   8484   5394   1651     23   -319       C  
ATOM    835  O   ALA A 111      -7.912  11.114  37.990  1.00 56.05           O  
ANISOU  835  O   ALA A 111     7341   8518   5439   1670     32   -293       O  
ATOM    836  CB  ALA A 111      -6.861   9.032  35.589  1.00 56.21           C  
ANISOU  836  CB  ALA A 111     7408   8542   5409   1646     17   -352       C  
ATOM    837  N   HIS A 112      -8.836   9.052  38.016  1.00 52.42           N  
ANISOU  837  N   HIS A 112     6925   8056   4938   1625     17   -328       N  
ATOM    838  CA  HIS A 112     -10.138   9.543  38.511  1.00 53.38           C  
ANISOU  838  CA  HIS A 112     7026   8202   5053   1617     22   -307       C  
ATOM    839  C   HIS A 112     -10.128   9.817  40.006  1.00 52.74           C  
ANISOU  839  C   HIS A 112     6945   8096   4997   1621     25   -298       C  
ATOM    840  O   HIS A 112     -11.026  10.505  40.500  1.00 53.56           O  
ANISOU  840  O   HIS A 112     7027   8220   5104   1622     32   -278       O  
ATOM    841  CB  HIS A 112     -11.283   8.566  38.189  1.00 54.52           C  
ANISOU  841  CB  HIS A 112     7185   8368   5161   1586     14   -319       C  
ATOM    842  CG  HIS A 112     -11.555   8.423  36.730  1.00 55.65           C  
ANISOU  842  CG  HIS A 112     7324   8542   5277   1581     11   -324       C  
ATOM    843  ND1 HIS A 112     -12.592   9.066  36.105  1.00 57.18           N  
ANISOU  843  ND1 HIS A 112     7492   8778   5455   1579     15   -306       N  
ATOM    844  CD2 HIS A 112     -10.908   7.729  35.762  1.00 55.60           C  
ANISOU  844  CD2 HIS A 112     7337   8533   5257   1577      4   -346       C  
ATOM    845  CE1 HIS A 112     -12.586   8.769  34.816  1.00 58.03           C  
ANISOU  845  CE1 HIS A 112     7603   8906   5539   1574     11   -316       C  
ATOM    846  NE2 HIS A 112     -11.571   7.960  34.582  1.00 57.10           N  
ANISOU  846  NE2 HIS A 112     7513   8761   5421   1572      4   -340       N  
ATOM    847  N   LEU A 113      -9.142   9.302  40.736  1.00 53.15           N  
ANISOU  847  N   LEU A 113     7325   7510   5361   1208  -1471   -755       N  
ATOM    848  CA  LEU A 113      -9.218   9.415  42.191  1.00 53.31           C  
ANISOU  848  CA  LEU A 113     7349   7515   5393   1245  -1467   -765       C  
ATOM    849  C   LEU A 113      -7.971   9.886  42.905  1.00 52.44           C  
ANISOU  849  C   LEU A 113     7260   7347   5317   1284  -1466   -780       C  
ATOM    850  O   LEU A 113      -7.532   9.243  43.868  1.00 51.91           O  
ANISOU  850  O   LEU A 113     7207   7257   5259   1293  -1459   -792       O  
ATOM    851  CB  LEU A 113      -9.581   8.062  42.787  1.00 53.10           C  
ANISOU  851  CB  LEU A 113     7325   7502   5349   1219  -1458   -770       C  
ATOM    852  CG  LEU A 113     -11.017   7.778  43.201  1.00 54.39           C  
ANISOU  852  CG  LEU A 113     7466   7714   5485   1211  -1457   -762       C  
ATOM    853  CD1 LEU A 113     -11.895   7.447  41.973  1.00 54.93           C  
ANISOU  853  CD1 LEU A 113     7518   7831   5523   1165  -1460   -747       C  
ATOM    854  CD2 LEU A 113     -10.988   6.648  44.219  1.00 54.19           C  
ANISOU  854  CD2 LEU A 113     7452   7683   5455   1203  -1447   -773       C  
ATOM    855  N   PRO A 114      -7.451  11.053  42.511  1.00 58.82           N  
ANISOU  855  N   PRO A 114     8070   8134   6144   1310  -1474   -778       N  
ATOM    856  CA  PRO A 114      -6.171  11.504  43.069  1.00 57.99           C  
ANISOU  856  CA  PRO A 114     7987   7973   6072   1344  -1472   -793       C  
ATOM    857  C   PRO A 114      -6.079  11.414  44.596  1.00 57.94           C  
ANISOU  857  C   PRO A 114     7988   7946   6079   1379  -1467   -806       C  
ATOM    858  O   PRO A 114      -5.038  10.996  45.085  1.00 57.04           O  
ANISOU  858  O   PRO A 114     7897   7792   5985   1387  -1462   -819       O  
ATOM    859  CB  PRO A 114      -6.089  12.962  42.602  1.00 58.71           C  
ANISOU  859  CB  PRO A 114     8073   8057   6176   1372  -1482   -787       C  
ATOM    860  CG  PRO A 114      -6.799  12.956  41.286  1.00 59.28           C  
ANISOU  860  CG  PRO A 114     8128   8171   6225   1336  -1487   -770       C  
ATOM    861  CD  PRO A 114      -7.954  11.982  41.479  1.00 59.75           C  
ANISOU  861  CD  PRO A 114     8171   8276   6254   1307  -1483   -764       C  
ATOM    862  N   ALA A 115      -7.125  11.756  45.333  1.00 54.94           N  
ANISOU  862  N   ALA A 115     7592   7594   5690   1398  -1468   -802       N  
ATOM    863  CA  ALA A 115      -6.978  11.881  46.779  1.00 55.04           C  
ANISOU  863  CA  ALA A 115     7612   7583   5717   1436  -1464   -814       C  
ATOM    864  C   ALA A 115      -6.827  10.576  47.539  1.00 54.40           C  
ANISOU  864  C   ALA A 115     7542   7496   5632   1421  -1454   -824       C  
ATOM    865  O   ALA A 115      -6.257  10.606  48.619  1.00 54.07           O  
ANISOU  865  O   ALA A 115     7514   7421   5610   1452  -1450   -837       O  
ATOM    866  CB  ALA A 115      -8.148  12.651  47.350  1.00 56.56           C  
ANISOU  866  CB  ALA A 115     7784   7807   5901   1461  -1467   -807       C  
ATOM    867  N   GLU A 116      -7.360   9.460  47.025  1.00 53.26           N  
ANISOU  867  N   GLU A 116     7392   7384   5462   1376  -1450   -817       N  
ATOM    868  CA  GLU A 116      -7.303   8.173  47.762  1.00 52.88           C  
ANISOU  868  CA  GLU A 116     7353   7332   5406   1359  -1440   -825       C  
ATOM    869  C   GLU A 116      -6.102   7.284  47.370  1.00 51.66           C  
ANISOU  869  C   GLU A 116     7223   7144   5262   1335  -1434   -834       C  
ATOM    870  O   GLU A 116      -5.828   6.279  48.002  1.00 51.46           O  
ANISOU  870  O   GLU A 116     7210   7107   5236   1325  -1426   -842       O  
ATOM    871  CB  GLU A 116      -8.586   7.351  47.564  1.00 53.75           C  
ANISOU  871  CB  GLU A 116     7445   7496   5480   1322  -1438   -815       C  
ATOM    872  CG  GLU A 116      -9.806   7.883  48.274  1.00 55.31           C  
ANISOU  872  CG  GLU A 116     7621   7727   5666   1344  -1441   -809       C  
ATOM    873  CD  GLU A 116     -10.374   9.127  47.585  1.00 56.44           C  
ANISOU  873  CD  GLU A 116     7745   7892   5808   1357  -1451   -796       C  
ATOM    874  OE1 GLU A 116     -10.095   9.295  46.371  1.00 56.22           O  
ANISOU  874  OE1 GLU A 116     7717   7867   5777   1335  -1455   -789       O  
ATOM    875  OE2 GLU A 116     -11.081   9.939  48.241  1.00 57.64           O  
ANISOU  875  OE2 GLU A 116     7883   8058   5961   1389  -1454   -794       O  
ATOM    876  N   PHE A 117      -5.364   7.696  46.354  1.00 49.35           N  
ANISOU  876  N   PHE A 117     6937   6835   4980   1328  -1439   -832       N  
ATOM    877  CA  PHE A 117      -4.349   6.902  45.698  1.00 48.81           C  
ANISOU  877  CA  PHE A 117     6887   6742   4917   1298  -1434   -837       C  
ATOM    878  C   PHE A 117      -3.009   7.042  46.425  1.00 48.14           C  
ANISOU  878  C   PHE A 117     6826   6600   4866   1331  -1431   -852       C  
ATOM    879  O   PHE A 117      -1.944   6.885  45.829  1.00 47.56           O  
ANISOU  879  O   PHE A 117     6768   6496   4806   1320  -1430   -856       O  
ATOM    880  CB  PHE A 117      -4.241   7.292  44.232  1.00 48.67           C  
ANISOU  880  CB  PHE A 117     6864   6736   4894   1274  -1440   -827       C  
ATOM    881  CG  PHE A 117      -3.829   6.172  43.355  1.00 48.46           C  
ANISOU  881  CG  PHE A 117     6846   6711   4855   1225  -1434   -826       C  
ATOM    882  CD1 PHE A 117      -4.767   5.327  42.812  1.00 48.97           C  
ANISOU  882  CD1 PHE A 117     6899   6821   4888   1181  -1430   -818       C  
ATOM    883  CD2 PHE A 117      -2.491   5.937  43.091  1.00 47.77           C  
ANISOU  883  CD2 PHE A 117     6781   6581   4789   1223  -1430   -836       C  
ATOM    884  CE1 PHE A 117      -4.380   4.260  42.010  1.00 48.79           C  
ANISOU  884  CE1 PHE A 117     6886   6799   4853   1134  -1423   -818       C  
ATOM    885  CE2 PHE A 117      -2.104   4.868  42.295  1.00 47.58           C  
ANISOU  885  CE2 PHE A 117     6767   6559   4754   1177  -1423   -836       C  
ATOM    886  CZ  PHE A 117      -3.055   4.034  41.750  1.00 48.09           C  
ANISOU  886  CZ  PHE A 117     6819   6668   4786   1132  -1420   -827       C  
ATOM    887  N   THR A 118      -3.073   7.448  47.688  1.00 47.42           N  
ANISOU  887  N   THR A 118     6737   6494   4788   1372  -1431   -860       N  
ATOM    888  CA  THR A 118      -1.909   7.447  48.584  1.00 47.01           C  
ANISOU  888  CA  THR A 118     6707   6390   4766   1403  -1427   -875       C  
ATOM    889  C   THR A 118      -1.157   6.145  48.485  1.00 46.46           C  
ANISOU  889  C   THR A 118     6655   6301   4695   1372  -1418   -881       C  
ATOM    890  O   THR A 118      -1.783   5.115  48.247  1.00 46.63           O  
ANISOU  890  O   THR A 118     6671   6353   4692   1334  -1412   -876       O  
ATOM    891  CB  THR A 118      -2.324   7.590  50.054  1.00 47.60           C  
ANISOU  891  CB  THR A 118     6780   6461   4846   1439  -1425   -882       C  
ATOM    892  OG1 THR A 118      -2.881   6.348  50.525  1.00 48.47           O  
ANISOU  892  OG1 THR A 118     6889   6593   4936   1414  -1416   -882       O  
ATOM    893  CG2 THR A 118      -3.358   8.715  50.219  1.00 47.99           C  
ANISOU  893  CG2 THR A 118     6807   6538   4888   1464  -1432   -875       C  
ATOM    894  N   PRO A 119       0.177   6.167  48.661  1.00 44.80           N  
ANISOU  894  N   PRO A 119     6466   6042   4513   1388  -1416   -892       N  
ATOM    895  CA  PRO A 119       0.966   4.953  48.468  1.00 44.51           C  
ANISOU  895  CA  PRO A 119     6448   5987   4478   1358  -1407   -897       C  
ATOM    896  C   PRO A 119       0.358   3.754  49.179  1.00 44.66           C  
ANISOU  896  C   PRO A 119     6466   6025   4478   1339  -1398   -898       C  
ATOM    897  O   PRO A 119       0.166   2.735  48.500  1.00 44.75           O  
ANISOU  897  O   PRO A 119     6478   6056   4468   1292  -1392   -894       O  
ATOM    898  CB  PRO A 119       2.311   5.328  49.072  1.00 44.04           C  
ANISOU  898  CB  PRO A 119     6408   5871   4454   1395  -1408   -909       C  
ATOM    899  CG  PRO A 119       2.391   6.744  48.853  1.00 44.06           C  
ANISOU  899  CG  PRO A 119     6404   5865   4470   1427  -1418   -908       C  
ATOM    900  CD  PRO A 119       1.023   7.270  49.114  1.00 44.51           C  
ANISOU  900  CD  PRO A 119     6440   5964   4509   1435  -1422   -900       C  
ATOM    901  N   ALA A 120      -0.034   3.907  50.453  1.00 42.50           N  
ANISOU  901  N   ALA A 120     6191   5749   4209   1371  -1397   -903       N  
ATOM    902  CA  ALA A 120      -0.655   2.805  51.204  1.00 42.77           C  
ANISOU  902  CA  ALA A 120     6225   5802   4225   1354  -1388   -905       C  
ATOM    903  C   ALA A 120      -1.778   2.129  50.415  1.00 43.54           C  
ANISOU  903  C   ALA A 120     6306   5951   4285   1306  -1386   -894       C  
ATOM    904  O   ALA A 120      -1.907   0.926  50.413  1.00 43.55           O  
ANISOU  904  O   ALA A 120     6314   5963   4269   1271  -1377   -895       O  
ATOM    905  CB  ALA A 120      -1.173   3.292  52.545  1.00 43.25           C  
ANISOU  905  CB  ALA A 120     6280   5863   4291   1397  -1390   -909       C  
ATOM    906  N   VAL A 121      -2.578   2.901  49.709  1.00 43.29           N  
ANISOU  906  N   VAL A 121     6255   5953   4240   1302  -1394   -883       N  
ATOM    907  CA  VAL A 121      -3.689   2.307  48.982  1.00 44.18           C  
ANISOU  907  CA  VAL A 121     6352   6117   4318   1258  -1392   -872       C  
ATOM    908  C   VAL A 121      -3.179   1.641  47.723  1.00 43.79           C  
ANISOU  908  C   VAL A 121     6311   6068   4261   1212  -1389   -869       C  
ATOM    909  O   VAL A 121      -3.638   0.559  47.338  1.00 44.13           O  
ANISOU  909  O   VAL A 121     6352   6137   4278   1167  -1381   -866       O  
ATOM    910  CB  VAL A 121      -4.750   3.341  48.632  1.00 45.29           C  
ANISOU  910  CB  VAL A 121     6467   6295   4447   1269  -1402   -860       C  
ATOM    911  CG1 VAL A 121      -5.892   2.663  47.941  1.00 46.36           C  
ANISOU  911  CG1 VAL A 121     6586   6483   4545   1222  -1401   -849       C  
ATOM    912  CG2 VAL A 121      -5.212   4.013  49.902  1.00 45.65           C  
ANISOU  912  CG2 VAL A 121     6505   6338   4501   1315  -1405   -864       C  
ATOM    913  N   HIS A 122      -2.195   2.285  47.107  1.00 47.51           N  
ANISOU  913  N   HIS A 122     6790   6508   4754   1224  -1394   -871       N  
ATOM    914  CA  HIS A 122      -1.616   1.786  45.870  1.00 47.20           C  
ANISOU  914  CA  HIS A 122     6758   6465   4710   1184  -1391   -868       C  
ATOM    915  C   HIS A 122      -1.133   0.370  46.076  1.00 46.67           C  
ANISOU  915  C   HIS A 122     6709   6385   4638   1153  -1378   -876       C  
ATOM    916  O   HIS A 122      -1.217  -0.462  45.182  1.00 46.87           O  
ANISOU  916  O   HIS A 122     6736   6429   4645   1106  -1372   -872       O  
ATOM    917  CB  HIS A 122      -0.458   2.670  45.407  1.00 46.50           C  
ANISOU  917  CB  HIS A 122     6680   6337   4651   1207  -1397   -872       C  
ATOM    918  CG  HIS A 122       0.006   2.353  44.019  1.00 46.52           C  
ANISOU  918  CG  HIS A 122     6686   6342   4647   1167  -1396   -867       C  
ATOM    919  ND1 HIS A 122       1.296   2.587  43.592  1.00 46.08           N  
ANISOU  919  ND1 HIS A 122     6647   6246   4617   1174  -1397   -873       N  
ATOM    920  CD2 HIS A 122      -0.653   1.820  42.959  1.00 47.05           C  
ANISOU  920  CD2 HIS A 122     6742   6447   4686   1120  -1394   -858       C  
ATOM    921  CE1 HIS A 122       1.407   2.215  42.326  1.00 46.35           C  
ANISOU  921  CE1 HIS A 122     6679   6293   4637   1133  -1395   -867       C  
ATOM    922  NE2 HIS A 122       0.242   1.746  41.918  1.00 46.91           N  
ANISOU  922  NE2 HIS A 122     6735   6412   4677   1099  -1394   -858       N  
ATOM    923  N   ALA A 123      -0.609   0.134  47.273  1.00 43.46           N  
ANISOU  923  N   ALA A 123     6316   5947   4249   1181  -1373   -886       N  
ATOM    924  CA  ALA A 123      -0.163  -1.176  47.716  1.00 43.05           C  
ANISOU  924  CA  ALA A 123     6282   5880   4195   1159  -1360   -894       C  
ATOM    925  C   ALA A 123      -1.328  -2.169  47.693  1.00 43.95           C  
ANISOU  925  C   ALA A 123     6387   6039   4273   1119  -1353   -890       C  
ATOM    926  O   ALA A 123      -1.350  -3.099  46.868  1.00 44.12           O  
ANISOU  926  O   ALA A 123     6412   6075   4275   1070  -1345   -888       O  
ATOM    927  CB  ALA A 123       0.445  -1.080  49.123  1.00 42.51           C  
ANISOU  927  CB  ALA A 123     6227   5773   4151   1203  -1358   -905       C  
ATOM    928  N   SER A 124      -2.297  -1.949  48.584  1.00 41.63           N  
ANISOU  928  N   SER A 124     6080   5768   3969   1138  -1355   -888       N  
ATOM    929  CA  SER A 124      -3.396  -2.874  48.768  1.00 41.82           C  
ANISOU  929  CA  SER A 124     6097   5833   3961   1105  -1348   -885       C  
ATOM    930  C   SER A 124      -4.329  -2.913  47.568  1.00 42.04           C  
ANISOU  930  C   SER A 124     6107   5909   3959   1064  -1351   -873       C  
ATOM    931  O   SER A 124      -5.066  -3.877  47.389  1.00 42.52           O  
ANISOU  931  O   SER A 124     6164   6001   3991   1024  -1344   -870       O  
ATOM    932  CB  SER A 124      -4.178  -2.529  50.021  1.00 41.91           C  
ANISOU  932  CB  SER A 124     6098   5856   3970   1139  -1351   -886       C  
ATOM    933  OG  SER A 124      -4.097  -1.145  50.302  1.00 41.87           O  
ANISOU  933  OG  SER A 124     6084   5839   3987   1188  -1362   -884       O  
ATOM    934  N   LEU A 125      -4.298  -1.905  46.714  1.00 40.24           N  
ANISOU  934  N   LEU A 125     5867   5686   3737   1073  -1362   -865       N  
ATOM    935  CA  LEU A 125      -5.125  -2.021  45.513  1.00 41.16           C  
ANISOU  935  CA  LEU A 125     5968   5847   3825   1032  -1364   -853       C  
ATOM    936  C   LEU A 125      -4.482  -3.022  44.580  1.00 40.79           C  
ANISOU  936  C   LEU A 125     5936   5792   3771    984  -1355   -856       C  
ATOM    937  O   LEU A 125      -5.174  -3.818  43.943  1.00 41.54           O  
ANISOU  937  O   LEU A 125     6025   5923   3837    937  -1350   -851       O  
ATOM    938  CB  LEU A 125      -5.343  -0.664  44.821  1.00 41.49           C  
ANISOU  938  CB  LEU A 125     5992   5899   3874   1053  -1378   -844       C  
ATOM    939  CG  LEU A 125      -6.631   0.087  45.251  1.00 42.71           C  
ANISOU  939  CG  LEU A 125     6122   6091   4015   1074  -1386   -835       C  
ATOM    940  CD1 LEU A 125      -6.822   1.432  44.552  1.00 42.84           C  
ANISOU  940  CD1 LEU A 125     6122   6117   4038   1094  -1400   -825       C  
ATOM    941  CD2 LEU A 125      -7.849  -0.789  45.024  1.00 44.06           C  
ANISOU  941  CD2 LEU A 125     6279   6312   4148   1031  -1382   -828       C  
ATOM    942  N   ASP A 126      -3.147  -2.999  44.550  1.00 41.87           N  
ANISOU  942  N   ASP A 126     6092   5882   3936    997  -1352   -864       N  
ATOM    943  CA  ASP A 126      -2.346  -3.862  43.675  1.00 41.52           C  
ANISOU  943  CA  ASP A 126     6063   5823   3890    957  -1343   -868       C  
ATOM    944  C   ASP A 126      -2.351  -5.298  44.142  1.00 41.59           C  
ANISOU  944  C   ASP A 126     6086   5831   3884    926  -1328   -875       C  
ATOM    945  O   ASP A 126      -2.388  -6.227  43.326  1.00 42.00           O  
ANISOU  945  O   ASP A 126     6144   5898   3917    876  -1319   -874       O  
ATOM    946  CB  ASP A 126      -0.910  -3.381  43.599  1.00 40.42           C  
ANISOU  946  CB  ASP A 126     5940   5632   3785    983  -1345   -875       C  
ATOM    947  CG  ASP A 126      -0.054  -4.287  42.752  1.00 40.10           C  
ANISOU  947  CG  ASP A 126     5916   5576   3745    943  -1335   -878       C  
ATOM    948  OD1 ASP A 126       0.445  -5.309  43.292  1.00 39.75           O  
ANISOU  948  OD1 ASP A 126     5890   5512   3703    931  -1323   -887       O  
ATOM    949  OD2 ASP A 126       0.100  -3.981  41.540  1.00 40.32           O  
ANISOU  949  OD2 ASP A 126     5939   5612   3769    922  -1339   -872       O  
ATOM    950  N   LYS A 127      -2.254  -5.463  45.457  1.00 41.23           N  
ANISOU  950  N   LYS A 127     6049   5767   3850    955  -1325   -883       N  
ATOM    951  CA  LYS A 127      -2.369  -6.771  46.060  1.00 41.46           C  
ANISOU  951  CA  LYS A 127     6091   5798   3865    930  -1310   -889       C  
ATOM    952  C   LYS A 127      -3.728  -7.330  45.668  1.00 42.76           C  
ANISOU  952  C   LYS A 127     6240   6016   3990    888  -1308   -882       C  
ATOM    953  O   LYS A 127      -3.832  -8.460  45.170  1.00 43.22           O  
ANISOU  953  O   LYS A 127     6306   6087   4027    840  -1296   -883       O  
ATOM    954  CB  LYS A 127      -2.193  -6.693  47.581  1.00 41.10           C  
ANISOU  954  CB  LYS A 127     6053   5727   3837    973  -1309   -897       C  
ATOM    955  CG  LYS A 127      -0.718  -6.446  47.986  1.00 39.93           C  
ANISOU  955  CG  LYS A 127     5924   5521   3726   1006  -1309   -906       C  
ATOM    956  CD  LYS A 127      -0.533  -6.196  49.490  1.00 39.63           C  
ANISOU  956  CD  LYS A 127     5892   5458   3707   1054  -1310   -913       C  
ATOM    957  CE  LYS A 127      -0.693  -7.468  50.314  1.00 40.22           C  
ANISOU  957  CE  LYS A 127     5980   5532   3770   1035  -1296   -919       C  
ATOM    958  NZ  LYS A 127      -0.598  -7.201  51.780  1.00 39.94           N  
ANISOU  958  NZ  LYS A 127     5949   5476   3752   1081  -1297   -925       N  
ATOM    959  N   PHE A 128      -4.764  -6.505  45.842  1.00 39.63           N  
ANISOU  959  N   PHE A 128     5822   5652   3584    907  -1319   -873       N  
ATOM    960  CA  PHE A 128      -6.130  -6.915  45.548  1.00 40.97           C  
ANISOU  960  CA  PHE A 128     5974   5875   3717    873  -1318   -865       C  
ATOM    961  C   PHE A 128      -6.261  -7.378  44.109  1.00 41.45           C  
ANISOU  961  C   PHE A 128     6033   5959   3757    821  -1315   -859       C  
ATOM    962  O   PHE A 128      -6.773  -8.443  43.888  1.00 42.18           O  
ANISOU  962  O   PHE A 128     6128   6075   3822    776  -1305   -860       O  
ATOM    963  CB  PHE A 128      -7.133  -5.789  45.838  1.00 41.69           C  
ANISOU  963  CB  PHE A 128     6040   5995   3804    905  -1331   -856       C  
ATOM    964  CG  PHE A 128      -8.515  -6.031  45.238  1.00 43.19           C  
ANISOU  964  CG  PHE A 128     6210   6242   3957    868  -1333   -845       C  
ATOM    965  CD1 PHE A 128      -9.442  -6.838  45.877  1.00 44.13           C  
ANISOU  965  CD1 PHE A 128     6327   6390   4052    849  -1326   -846       C  
ATOM    966  CD2 PHE A 128      -8.860  -5.461  44.030  1.00 43.77           C  
ANISOU  966  CD2 PHE A 128     6269   6341   4022    852  -1342   -834       C  
ATOM    967  CE1 PHE A 128     -10.654  -7.078  45.323  1.00 45.57           C  
ANISOU  967  CE1 PHE A 128     6491   6623   4201    815  -1327   -836       C  
ATOM    968  CE2 PHE A 128     -10.070  -5.698  43.472  1.00 45.20           C  
ANISOU  968  CE2 PHE A 128     6431   6572   4170    819  -1343   -823       C  
ATOM    969  CZ  PHE A 128     -10.973  -6.504  44.116  1.00 46.10           C  
ANISOU  969  CZ  PHE A 128     6543   6714   4259    800  -1336   -825       C  
ATOM    970  N   LEU A 129      -5.810  -6.613  43.125  1.00 39.80           N  
ANISOU  970  N   LEU A 129     5819   5744   3560    824  -1324   -854       N  
ATOM    971  CA  LEU A 129      -5.857  -7.122  41.755  1.00 39.90           C  
ANISOU  971  CA  LEU A 129     5831   5776   3553    773  -1320   -849       C  
ATOM    972  C   LEU A 129      -4.872  -8.270  41.529  1.00 39.57           C  
ANISOU  972  C   LEU A 129     5814   5706   3516    742  -1305   -859       C  
ATOM    973  O   LEU A 129      -5.049  -9.099  40.637  1.00 39.70           O  
ANISOU  973  O   LEU A 129     5832   5742   3509    691  -1297   -858       O  
ATOM    974  CB  LEU A 129      -5.563  -6.028  40.761  1.00 39.83           C  
ANISOU  974  CB  LEU A 129     5812   5766   3557    785  -1333   -841       C  
ATOM    975  CG  LEU A 129      -6.377  -4.778  40.941  1.00 40.11           C  
ANISOU  975  CG  LEU A 129     5824   5823   3593    820  -1347   -831       C  
ATOM    976  CD1 LEU A 129      -5.802  -3.745  40.008  1.00 39.95           C  
ANISOU  976  CD1 LEU A 129     5799   5791   3591    834  -1358   -825       C  
ATOM    977  CD2 LEU A 129      -7.812  -5.107  40.601  1.00 40.66           C  
ANISOU  977  CD2 LEU A 129     5874   5949   3625    787  -1348   -820       C  
ATOM    978  N   ALA A 130      -3.799  -8.298  42.309  1.00 43.79           N  
ANISOU  978  N   ALA A 130     6367   6194   4079    772  -1301   -870       N  
ATOM    979  CA  ALA A 130      -2.943  -9.474  42.270  1.00 43.43           C  
ANISOU  979  CA  ALA A 130     6345   6122   4036    744  -1285   -880       C  
ATOM    980  C   ALA A 130      -3.809 -10.653  42.679  1.00 44.37           C  
ANISOU  980  C   ALA A 130     6465   6269   4124    708  -1273   -882       C  
ATOM    981  O   ALA A 130      -4.135 -11.517  41.851  1.00 45.18           O  
ANISOU  981  O   ALA A 130     6570   6396   4202    656  -1265   -881       O  
ATOM    982  CB  ALA A 130      -1.743  -9.324  43.179  1.00 42.24           C  
ANISOU  982  CB  ALA A 130     6212   5918   3921    785  -1283   -890       C  
ATOM    983  N   SER A 131      -4.247 -10.615  43.938  1.00 40.35           N  
ANISOU  983  N   SER A 131     5955   5760   3616    737  -1274   -885       N  
ATOM    984  CA  SER A 131      -5.045 -11.676  44.527  1.00 41.30           C  
ANISOU  984  CA  SER A 131     6079   5903   3710    709  -1262   -888       C  
ATOM    985  C   SER A 131      -6.151 -12.108  43.592  1.00 42.64           C  
ANISOU  985  C   SER A 131     6235   6124   3842    659  -1261   -879       C  
ATOM    986  O   SER A 131      -6.377 -13.274  43.397  1.00 43.38           O  
ANISOU  986  O   SER A 131     6338   6231   3914    614  -1248   -883       O  
ATOM    987  CB  SER A 131      -5.624 -11.220  45.849  1.00 41.46           C  
ANISOU  987  CB  SER A 131     6091   5927   3735    751  -1268   -888       C  
ATOM    988  OG  SER A 131      -5.983 -12.326  46.639  1.00 42.21           O  
ANISOU  988  OG  SER A 131     6196   6027   3813    732  -1255   -895       O  
ATOM    989  N   VAL A 132      -6.816 -11.177  42.955  1.00 41.73           N  
ANISOU  989  N   VAL A 132     6097   6038   3720    665  -1275   -868       N  
ATOM    990  CA  VAL A 132      -7.830 -11.575  42.007  1.00 42.25           C  
ANISOU  990  CA  VAL A 132     6150   6152   3751    617  -1274   -859       C  
ATOM    991  C   VAL A 132      -7.173 -12.156  40.759  1.00 41.91           C  
ANISOU  991  C   VAL A 132     6118   6102   3704    574  -1267   -861       C  
ATOM    992  O   VAL A 132      -7.513 -13.265  40.341  1.00 42.31           O  
ANISOU  992  O   VAL A 132     6176   6172   3728    523  -1255   -863       O  
ATOM    993  CB  VAL A 132      -8.765 -10.400  41.638  1.00 43.02           C  
ANISOU  993  CB  VAL A 132     6220   6283   3841    635  -1292   -845       C  
ATOM    994  CG1 VAL A 132      -9.424 -10.631  40.291  1.00 43.77           C  
ANISOU  994  CG1 VAL A 132     6304   6419   3909    586  -1293   -836       C  
ATOM    995  CG2 VAL A 132      -9.784 -10.211  42.743  1.00 43.83           C  
ANISOU  995  CG2 VAL A 132     6310   6408   3934    658  -1295   -843       C  
ATOM    996  N   SER A 133      -6.208 -11.442  40.183  1.00 46.29           N  
ANISOU  996  N   SER A 133     6675   6628   4284    593  -1274   -860       N  
ATOM    997  CA  SER A 133      -5.704 -11.844  38.867  1.00 46.48           C  
ANISOU  997  CA  SER A 133     6705   6652   4303    552  -1269   -859       C  
ATOM    998  C   SER A 133      -5.089 -13.219  38.973  1.00 46.45           C  
ANISOU  998  C   SER A 133     6725   6630   4295    518  -1249   -871       C  
ATOM    999  O   SER A 133      -5.045 -13.951  37.982  1.00 47.13           O  
ANISOU  999  O   SER A 133     6815   6728   4363    469  -1241   -871       O  
ATOM   1000  CB  SER A 133      -4.681 -10.853  38.305  1.00 45.55           C  
ANISOU 1000  CB  SER A 133     6588   6504   4216    580  -1278   -858       C  
ATOM   1001  OG  SER A 133      -5.235 -10.112  37.240  1.00 46.62           O  
ANISOU 1001  OG  SER A 133     6704   6669   4340    571  -1290   -845       O  
ATOM   1002  N   THR A 134      -4.637 -13.574  40.178  1.00 45.17           N  
ANISOU 1002  N   THR A 134     6578   6438   4148    542  -1242   -881       N  
ATOM   1003  CA  THR A 134      -4.133 -14.915  40.432  1.00 45.27           C  
ANISOU 1003  CA  THR A 134     6612   6432   4155    512  -1223   -892       C  
ATOM   1004  C   THR A 134      -5.251 -15.950  40.297  1.00 46.75           C  
ANISOU 1004  C   THR A 134     6797   6662   4303    462  -1213   -891       C  
ATOM   1005  O   THR A 134      -5.114 -16.907  39.517  1.00 47.37           O  
ANISOU 1005  O   THR A 134     6885   6747   4365    413  -1200   -895       O  
ATOM   1006  CB  THR A 134      -3.506 -15.042  41.824  1.00 44.44           C  
ANISOU 1006  CB  THR A 134     6523   6289   4075    551  -1218   -902       C  
ATOM   1007  OG1 THR A 134      -2.279 -14.307  41.867  1.00 43.05           O  
ANISOU 1007  OG1 THR A 134     6353   6068   3935    590  -1224   -905       O  
ATOM   1008  CG2 THR A 134      -3.189 -16.489  42.123  1.00 44.79           C  
ANISOU 1008  CG2 THR A 134     6588   6321   4109    517  -1198   -913       C  
ATOM   1009  N   VAL A 135      -6.356 -15.733  41.032  1.00 43.35           N  
ANISOU 1009  N   VAL A 135     6354   6260   3857    474  -1219   -887       N  
ATOM   1010  CA  VAL A 135      -7.429 -16.737  41.206  1.00 44.43           C  
ANISOU 1010  CA  VAL A 135     6491   6433   3957    433  -1209   -887       C  
ATOM   1011  C   VAL A 135      -8.019 -17.170  39.880  1.00 45.12           C  
ANISOU 1011  C   VAL A 135     6571   6557   4014    377  -1207   -880       C  
ATOM   1012  O   VAL A 135      -8.400 -18.329  39.712  1.00 45.64           O  
ANISOU 1012  O   VAL A 135     6648   6641   4054    329  -1193   -884       O  
ATOM   1013  CB  VAL A 135      -8.556 -16.218  42.135  1.00 45.31           C  
ANISOU 1013  CB  VAL A 135     6586   6571   4058    459  -1219   -881       C  
ATOM   1014  CG1 VAL A 135      -9.756 -17.102  42.082  1.00 46.51           C  
ANISOU 1014  CG1 VAL A 135     6735   6767   4171    414  -1211   -879       C  
ATOM   1015  CG2 VAL A 135      -8.066 -16.144  43.570  1.00 44.79           C  
ANISOU 1015  CG2 VAL A 135     6531   6472   4017    505  -1216   -890       C  
ATOM   1016  N   LEU A 136      -8.059 -16.252  38.927  1.00 46.65           N  
ANISOU 1016  N   LEU A 136     6750   6763   4213    382  -1220   -870       N  
ATOM   1017  CA  LEU A 136      -8.534 -16.578  37.591  1.00 47.79           C  
ANISOU 1017  CA  LEU A 136     6888   6940   4331    332  -1220   -863       C  
ATOM   1018  C   LEU A 136      -7.530 -17.429  36.867  1.00 47.55           C  
ANISOU 1018  C   LEU A 136     6876   6886   4304    297  -1205   -872       C  
ATOM   1019  O   LEU A 136      -7.887 -18.356  36.138  1.00 48.71           O  
ANISOU 1019  O   LEU A 136     7028   7055   4424    243  -1195   -872       O  
ATOM   1020  CB  LEU A 136      -8.813 -15.326  36.779  1.00 47.78           C  
ANISOU 1020  CB  LEU A 136     6865   6956   4335    349  -1238   -850       C  
ATOM   1021  CG  LEU A 136      -9.771 -14.381  37.497  1.00 47.98           C  
ANISOU 1021  CG  LEU A 136     6869   7003   4358    388  -1253   -841       C  
ATOM   1022  CD1 LEU A 136      -9.888 -13.065  36.756  1.00 47.61           C  
ANISOU 1022  CD1 LEU A 136     6802   6967   4322    411  -1271   -829       C  
ATOM   1023  CD2 LEU A 136     -11.120 -15.030  37.644  1.00 49.63           C  
ANISOU 1023  CD2 LEU A 136     7071   7256   4530    354  -1250   -836       C  
ATOM   1024  N   THR A 137      -6.265 -17.129  37.089  1.00 46.63           N  
ANISOU 1024  N   THR A 137     6771   6724   4223    329  -1204   -879       N  
ATOM   1025  CA  THR A 137      -5.200 -17.837  36.397  1.00 45.87           C  
ANISOU 1025  CA  THR A 137     6692   6602   4134    301  -1191   -887       C  
ATOM   1026  C   THR A 137      -4.782 -19.219  36.972  1.00 45.70           C  
ANISOU 1026  C   THR A 137     6693   6563   4108    277  -1169   -901       C  
ATOM   1027  O   THR A 137      -4.344 -20.081  36.235  1.00 45.52           O  
ANISOU 1027  O   THR A 137     6682   6537   4078    236  -1156   -907       O  
ATOM   1028  CB  THR A 137      -3.977 -16.919  36.320  1.00 44.68           C  
ANISOU 1028  CB  THR A 137     6544   6410   4023    344  -1199   -889       C  
ATOM   1029  OG1 THR A 137      -3.744 -16.323  37.609  1.00 44.30           O  
ANISOU 1029  OG1 THR A 137     6498   6336   3999    399  -1205   -891       O  
ATOM   1030  CG2 THR A 137      -4.245 -15.833  35.286  1.00 44.83           C  
ANISOU 1030  CG2 THR A 137     6543   6448   4042    349  -1216   -876       C  
ATOM   1031  N   SER A 138      -4.942 -19.432  38.269  1.00 45.61           N  
ANISOU 1031  N   SER A 138     6689   6541   4101    301  -1166   -907       N  
ATOM   1032  CA  SER A 138      -4.316 -20.577  38.895  1.00 45.25           C  
ANISOU 1032  CA  SER A 138     6666   6468   4059    289  -1146   -920       C  
ATOM   1033  C   SER A 138      -4.868 -21.895  38.407  1.00 46.02           C  
ANISOU 1033  C   SER A 138     6770   6593   4122    226  -1129   -924       C  
ATOM   1034  O   SER A 138      -4.314 -22.926  38.708  1.00 46.28           O  
ANISOU 1034  O   SER A 138     6822   6606   4156    209  -1111   -936       O  
ATOM   1035  CB  SER A 138      -4.421 -20.498  40.425  1.00 45.22           C  
ANISOU 1035  CB  SER A 138     6668   6448   4067    329  -1147   -924       C  
ATOM   1036  OG  SER A 138      -5.729 -20.725  40.883  1.00 46.35           O  
ANISOU 1036  OG  SER A 138     6801   6630   4180    316  -1148   -920       O  
ATOM   1037  N   LYS A 139      -5.955 -21.888  37.661  1.00 51.37           N  
ANISOU 1037  N   LYS A 139     7433   7316   4768    192  -1134   -915       N  
ATOM   1038  CA  LYS A 139      -6.457 -23.120  37.048  1.00 53.01           C  
ANISOU 1038  CA  LYS A 139     7648   7551   4941    129  -1118   -919       C  
ATOM   1039  C   LYS A 139      -5.995 -23.242  35.594  1.00 53.31           C  
ANISOU 1039  C   LYS A 139     7685   7594   4977     94  -1116   -917       C  
ATOM   1040  O   LYS A 139      -6.505 -24.063  34.827  1.00 54.84           O  
ANISOU 1040  O   LYS A 139     7880   7816   5141     40  -1106   -918       O  
ATOM   1041  CB  LYS A 139      -7.977 -23.204  37.149  1.00 54.45           C  
ANISOU 1041  CB  LYS A 139     7819   7781   5088    107  -1124   -910       C  
ATOM   1042  CG  LYS A 139      -8.450 -23.340  38.594  1.00 54.35           C  
ANISOU 1042  CG  LYS A 139     7810   7767   5075    133  -1122   -914       C  
ATOM   1043  CD  LYS A 139      -9.975 -23.372  38.685  1.00 55.84           C  
ANISOU 1043  CD  LYS A 139     7986   8003   5228    112  -1128   -904       C  
ATOM   1044  CE  LYS A 139     -10.434 -23.497  40.128  1.00 56.13           C  
ANISOU 1044  CE  LYS A 139     8026   8037   5264    139  -1126   -908       C  
ATOM   1045  NZ  LYS A 139     -11.867 -23.905  40.217  1.00 57.58           N  
ANISOU 1045  NZ  LYS A 139     8204   8265   5409    107  -1127   -902       N  
ATOM   1046  N   TYR A 140      -5.091 -22.361  35.188  1.00 58.79           N  
ANISOU 1046  N   TYR A 140     8375   8261   5700    125  -1125   -915       N  
ATOM   1047  CA  TYR A 140      -4.459 -22.475  33.879  1.00 58.93           C  
ANISOU 1047  CA  TYR A 140     8393   8277   5721     97  -1122   -915       C  
ATOM   1048  C   TYR A 140      -3.725 -23.839  33.834  1.00 59.40           C  
ANISOU 1048  C   TYR A 140     8473   8317   5779     63  -1098   -930       C  
ATOM   1049  O   TYR A 140      -3.366 -24.387  34.893  1.00 58.93           O  
ANISOU 1049  O   TYR A 140     8427   8233   5729     79  -1087   -940       O  
ATOM   1050  CB  TYR A 140      -3.507 -21.287  33.645  1.00 57.29           C  
ANISOU 1050  CB  TYR A 140     8180   8037   5549    142  -1136   -911       C  
ATOM   1051  CG  TYR A 140      -3.198 -20.959  32.207  1.00 57.67           C  
ANISOU 1051  CG  TYR A 140     8221   8094   5597    120  -1141   -906       C  
ATOM   1052  CD1 TYR A 140      -4.185 -20.525  31.340  1.00 58.92           C  
ANISOU 1052  CD1 TYR A 140     8361   8295   5731     98  -1152   -893       C  
ATOM   1053  CD2 TYR A 140      -1.907 -21.062  31.721  1.00 56.91           C  
ANISOU 1053  CD2 TYR A 140     8135   7963   5525    122  -1134   -913       C  
ATOM   1054  CE1 TYR A 140      -3.897 -20.213  30.005  1.00 59.42           C  
ANISOU 1054  CE1 TYR A 140     8418   8366   5794     78  -1156   -888       C  
ATOM   1055  CE2 TYR A 140      -1.597 -20.755  30.392  1.00 57.41           C  
ANISOU 1055  CE2 TYR A 140     8191   8034   5589    102  -1137   -908       C  
ATOM   1056  CZ  TYR A 140      -2.596 -20.332  29.540  1.00 58.66           C  
ANISOU 1056  CZ  TYR A 140     8331   8235   5722     80  -1149   -896       C  
ATOM   1057  OH  TYR A 140      -2.295 -20.034  28.226  1.00 59.27           O  
ANISOU 1057  OH  TYR A 140     8402   8320   5799     59  -1153   -891       O  
ATOM   1058  N   ARG A 141      -3.573 -24.412  32.635  1.00 63.81           N  
ANISOU 1058  N   ARG A 141     9031   8889   6323     17  -1088   -932       N  
ATOM   1059  CA  ARG A 141      -2.815 -25.649  32.442  1.00 64.36           C  
ANISOU 1059  CA  ARG A 141     9117   8942   6393    -14  -1065   -947       C  
ATOM   1060  C   ARG A 141      -2.537 -25.827  30.952  1.00 65.31           C  
ANISOU 1060  C   ARG A 141     9232   9078   6506    -53  -1062   -947       C  
ATOM   1061  O   ARG A 141      -2.868 -24.932  30.170  1.00 65.32           O  
ANISOU 1061  O   ARG A 141     9218   9096   6503    -51  -1078   -934       O  
ATOM   1062  CB  ARG A 141      -3.565 -26.861  33.007  1.00 65.74           C  
ANISOU 1062  CB  ARG A 141     9300   9139   6538    -49  -1049   -955       C  
ATOM   1063  CG  ARG A 141      -4.916 -27.133  32.343  1.00 66.33           C  
ANISOU 1063  CG  ARG A 141     9363   9267   6571    -97  -1050   -947       C  
ATOM   1064  CD  ARG A 141      -5.665 -28.331  32.952  1.00 66.74           C  
ANISOU 1064  CD  ARG A 141     9425   9340   6594   -131  -1034   -955       C  
ATOM   1065  NE  ARG A 141      -7.115 -28.205  32.753  1.00 67.36           N  
ANISOU 1065  NE  ARG A 141     9494   9464   6637   -157  -1043   -943       N  
ATOM   1066  CZ  ARG A 141      -7.841 -28.928  31.893  1.00 67.27           C  
ANISOU 1066  CZ  ARG A 141     9482   9488   6590   -215  -1036   -941       C  
ATOM   1067  NH1 ARG A 141      -7.258 -29.865  31.143  1.00 66.57           N  
ANISOU 1067  NH1 ARG A 141     9396   9400   6496   -253  -1016   -954       N  
ATOM   1068  NH2 ARG A 141      -9.157 -28.720  31.788  1.00 67.99           N  
ANISOU 1068  NH2 ARG A 141     9569   9614   6651   -234  -1048   -927       N  
ATOM   1069  OXT ARG A 141      -1.978 -26.833  30.488  1.00 66.27           O  
ANISOU 1069  OXT ARG A 141     9362   9193   6624    -86  -1043   -959       O  
TER    1070      ARG A 141                                                      
ATOM   1071  N   VAL B   1      11.506   2.763  19.793  1.00102.43           N  
ANISOU 1071  N   VAL B   1    11020  12556  15342    667   -340   2723       N  
ATOM   1072  CA  VAL B   1      10.524   2.354  18.789  1.00104.69           C  
ANISOU 1072  CA  VAL B   1    11272  12889  15616    669   -327   2742       C  
ATOM   1073  C   VAL B   1      10.002   3.615  18.083  1.00108.29           C  
ANISOU 1073  C   VAL B   1    11711  13364  16071    664   -296   2789       C  
ATOM   1074  O   VAL B   1      10.270   4.739  18.520  1.00108.33           O  
ANISOU 1074  O   VAL B   1    11737  13340  16085    663   -285   2808       O  
ATOM   1075  CB  VAL B   1       9.341   1.495  19.430  1.00100.77           C  
ANISOU 1075  CB  VAL B   1    10800  12373  15115    684   -325   2742       C  
ATOM   1076  CG1 VAL B   1       8.486   2.310  20.394  1.00 96.78           C  
ANISOU 1076  CG1 VAL B   1    10338  11818  14615    694   -303   2775       C  
ATOM   1077  CG2 VAL B   1       8.466   0.827  18.363  1.00103.42           C  
ANISOU 1077  CG2 VAL B   1    11097  12761  15438    684   -317   2752       C  
ATOM   1078  N   HIS B   2       9.293   3.421  16.973  1.00108.37           N  
ANISOU 1078  N   HIS B   2    11682  13424  16070    662   -284   2807       N  
ATOM   1079  CA  HIS B   2       8.685   4.520  16.230  1.00111.96           C  
ANISOU 1079  CA  HIS B   2    12117  13899  16522    659   -254   2853       C  
ATOM   1080  C   HIS B   2       7.569   5.181  17.033  1.00108.72           C  
ANISOU 1080  C   HIS B   2    11745  13448  16115    671   -230   2889       C  
ATOM   1081  O   HIS B   2       6.844   4.525  17.791  1.00105.24           O  
ANISOU 1081  O   HIS B   2    11333  12981  15674    683   -233   2884       O  
ATOM   1082  CB  HIS B   2       8.124   4.030  14.881  1.00116.79           C  
ANISOU 1082  CB  HIS B   2    12679  14574  17121    655   -247   2863       C  
ATOM   1083  CG  HIS B   2       9.167   3.529  13.923  1.00120.86           C  
ANISOU 1083  CG  HIS B   2    13153  15137  17633    642   -266   2834       C  
ATOM   1084  ND1 HIS B   2       9.737   4.331  12.954  1.00125.29           N  
ANISOU 1084  ND1 HIS B   2    13679  15732  18193    629   -259   2848       N  
ATOM   1085  CD2 HIS B   2       9.726   2.305  13.774  1.00121.69           C  
ANISOU 1085  CD2 HIS B   2    13243  15259  17734    640   -293   2792       C  
ATOM   1086  CE1 HIS B   2      10.607   3.623  12.256  1.00128.77           C  
ANISOU 1086  CE1 HIS B   2    14086  16210  18629    619   -279   2816       C  
ATOM   1087  NE2 HIS B   2      10.621   2.391  12.733  1.00126.29           N  
ANISOU 1087  NE2 HIS B   2    13784  15887  18314    626   -300   2781       N  
ATOM   1088  N   LEU B   3       7.431   6.487  16.853  1.00103.29           N  
ANISOU 1088  N   LEU B   3    11058  12756  15432    667   -207   2926       N  
ATOM   1089  CA  LEU B   3       6.370   7.232  17.514  1.00100.68           C  
ANISOU 1089  CA  LEU B   3    10761  12389  15105    678   -182   2963       C  
ATOM   1090  C   LEU B   3       5.759   8.245  16.546  1.00105.05           C  
ANISOU 1090  C   LEU B   3    11285  12974  15654    673   -153   3009       C  
ATOM   1091  O   LEU B   3       6.482   9.052  15.941  1.00110.12           O  
ANISOU 1091  O   LEU B   3    11906  13635  16299    662   -150   3017       O  
ATOM   1092  CB  LEU B   3       6.909   7.944  18.764  1.00 97.62           C  
ANISOU 1092  CB  LEU B   3    10420  11940  14730    681   -185   2960       C  
ATOM   1093  CG  LEU B   3       6.183   7.683  20.087  1.00 92.00           C  
ANISOU 1093  CG  LEU B   3     9760  11173  14022    696   -183   2960       C  
ATOM   1094  CD1 LEU B   3       6.459   6.276  20.579  1.00 90.75           C  
ANISOU 1094  CD1 LEU B   3     9612  11008  13862    701   -212   2916       C  
ATOM   1095  CD2 LEU B   3       6.549   8.718  21.140  1.00 89.90           C  
ANISOU 1095  CD2 LEU B   3     9537  10853  13769    698   -178   2970       C  
ATOM   1096  N   THR B   4       4.435   8.203  16.403  1.00 98.54           N  
ANISOU 1096  N   THR B   4    10461  12155  14823    682   -133   3038       N  
ATOM   1097  CA  THR B   4       3.732   9.178  15.577  1.00102.29           C  
ANISOU 1097  CA  THR B   4    10914  12657  15296    679   -104   3084       C  
ATOM   1098  C   THR B   4       4.005  10.578  16.124  1.00102.64           C  
ANISOU 1098  C   THR B   4    10984  12664  15351    677    -89   3109       C  
ATOM   1099  O   THR B   4       4.105  10.759  17.334  1.00 98.78           O  
ANISOU 1099  O   THR B   4    10540  12120  14870    685    -92   3102       O  
ATOM   1100  CB  THR B   4       2.207   8.908  15.531  1.00100.53           C  
ANISOU 1100  CB  THR B   4    10694  12437  15065    690    -84   3112       C  
ATOM   1101  OG1 THR B   4       1.517   9.814  16.405  1.00 97.41           O  
ANISOU 1101  OG1 THR B   4    10339  11995  14678    699    -63   3144       O  
ATOM   1102  CG2 THR B   4       1.897   7.467  15.923  1.00 97.56           C  
ANISOU 1102  CG2 THR B   4    10326  12058  14683    699   -103   3081       C  
ATOM   1103  N   PRO B   5       4.163  11.566  15.231  1.00100.17           N  
ANISOU 1103  N   PRO B   5    10641  12380  15038    667    -72   3137       N  
ATOM   1104  CA  PRO B   5       4.451  12.948  15.647  1.00101.39           C  
ANISOU 1104  CA  PRO B   5    10817  12503  15203    665    -57   3161       C  
ATOM   1105  C   PRO B   5       3.498  13.497  16.727  1.00 96.97           C  
ANISOU 1105  C   PRO B   5    10305  11891  14650    678    -38   3188       C  
ATOM   1106  O   PRO B   5       3.949  14.181  17.646  1.00 95.94           O  
ANISOU 1106  O   PRO B   5    10209  11713  14529    680    -38   3188       O  
ATOM   1107  CB  PRO B   5       4.312  13.732  14.336  1.00107.25           C  
ANISOU 1107  CB  PRO B   5    11515  13294  15941    655    -38   3194       C  
ATOM   1108  CG  PRO B   5       4.732  12.745  13.284  1.00110.33           C  
ANISOU 1108  CG  PRO B   5    11860  13741  16321    647    -55   3168       C  
ATOM   1109  CD  PRO B   5       4.245  11.399  13.767  1.00105.49           C  
ANISOU 1109  CD  PRO B   5    11260  13119  15702    657    -70   3141       C  
ATOM   1110  N   GLU B   6       2.208  13.188  16.628  1.00103.11           N  
ANISOU 1110  N   GLU B   6    11082  12674  15420    688    -23   3210       N  
ATOM   1111  CA  GLU B   6       1.242  13.666  17.619  1.00 99.34           C  
ANISOU 1111  CA  GLU B   6    10648  12148  14947    701     -4   3237       C  
ATOM   1112  C   GLU B   6       1.321  12.839  18.901  1.00 94.27           C  
ANISOU 1112  C   GLU B   6    10049  11459  14309    711    -23   3205       C  
ATOM   1113  O   GLU B   6       0.812  13.246  19.948  1.00 91.79           O  
ANISOU 1113  O   GLU B   6     9779  11096  14002    722    -12   3218       O  
ATOM   1114  CB  GLU B   6      -0.184  13.636  17.066  1.00 98.90           C  
ANISOU 1114  CB  GLU B   6    10577  12116  14883    708     20   3272       C  
ATOM   1115  CG  GLU B   6      -0.273  13.781  15.557  1.00104.06           C  
ANISOU 1115  CG  GLU B   6    11176  12834  15528    697     29   3289       C  
ATOM   1116  CD  GLU B   6      -0.134  12.446  14.836  1.00106.93           C  
ANISOU 1116  CD  GLU B   6    11505  13242  15881    694      9   3259       C  
ATOM   1117  OE1 GLU B   6       0.897  11.762  15.020  1.00105.75           O  
ANISOU 1117  OE1 GLU B   6    11355  13092  15732    689    -18   3217       O  
ATOM   1118  OE2 GLU B   6      -1.068  12.078  14.091  1.00110.60           O  
ANISOU 1118  OE2 GLU B   6    11945  13743  16336    696     21   3276       O  
ATOM   1119  N   GLU B   7       1.943  11.669  18.820  1.00 95.72           N  
ANISOU 1119  N   GLU B   7    10222  11659  14489    709    -50   3162       N  
ATOM   1120  CA  GLU B   7       2.250  10.937  20.036  1.00 91.21           C  
ANISOU 1120  CA  GLU B   7     9691  11042  13922    717    -71   3128       C  
ATOM   1121  C   GLU B   7       3.353  11.666  20.765  1.00 90.95           C  
ANISOU 1121  C   GLU B   7     9685  10971  13901    712    -80   3116       C  
ATOM   1122  O   GLU B   7       3.178  12.050  21.918  1.00 87.98           O  
ANISOU 1122  O   GLU B   7     9355  10541  13533    720    -76   3121       O  
ATOM   1123  CB  GLU B   7       2.664   9.499  19.747  1.00 91.25           C  
ANISOU 1123  CB  GLU B   7     9677  11074  13920    715    -99   3086       C  
ATOM   1124  CG  GLU B   7       1.520   8.611  19.361  1.00 87.23           C  
ANISOU 1124  CG  GLU B   7     9154  10590  13400    723    -93   3093       C  
ATOM   1125  CD  GLU B   7       1.640   7.254  19.979  1.00 86.64           C  
ANISOU 1125  CD  GLU B   7     9095  10502  13324    730   -119   3052       C  
ATOM   1126  OE1 GLU B   7       0.611   6.724  20.465  1.00 89.27           O  
ANISOU 1126  OE1 GLU B   7     9448  10818  13653    742   -113   3059       O  
ATOM   1127  OE2 GLU B   7       2.770   6.721  19.979  1.00 83.85           O  
ANISOU 1127  OE2 GLU B   7     8734  10154  12972    723   -145   3013       O  
ATOM   1128  N   LYS B   8       4.470  11.888  20.068  1.00 89.95           N  
ANISOU 1128  N   LYS B   8     9528  10873  13776    698    -92   3102       N  
ATOM   1129  CA  LYS B   8       5.638  12.558  20.641  1.00 90.57           C  
ANISOU 1129  CA  LYS B   8     9626  10920  13865    692   -102   3088       C  
ATOM   1130  C   LYS B   8       5.257  13.957  21.112  1.00 90.71           C  
ANISOU 1130  C   LYS B   8     9671  10904  13892    695    -76   3127       C  
ATOM   1131  O   LYS B   8       5.775  14.447  22.119  1.00 88.94           O  
ANISOU 1131  O   LYS B   8     9484  10631  13677    697    -81   3120       O  
ATOM   1132  CB  LYS B   8       6.791  12.632  19.624  1.00 95.65           C  
ANISOU 1132  CB  LYS B   8    10227  11608  14508    676   -115   3072       C  
ATOM   1133  CG  LYS B   8       8.080  13.249  20.186  1.00 97.05           C  
ANISOU 1133  CG  LYS B   8    10423  11756  14697    669   -128   3054       C  
ATOM   1134  CD  LYS B   8       9.079  13.665  19.093  1.00103.03           C  
ANISOU 1134  CD  LYS B   8    11136  12556  15453    653   -133   3050       C  
ATOM   1135  CE  LYS B   8       9.845  12.481  18.483  1.00105.04           C  
ANISOU 1135  CE  LYS B   8    11359  12849  15701    646   -160   3008       C  
ATOM   1136  NZ  LYS B   8      10.816  12.945  17.444  1.00111.43           N  
ANISOU 1136  NZ  LYS B   8    12127  13700  16511    631   -164   3006       N  
ATOM   1137  N   SER B   9       4.331  14.587  20.392  1.00 89.40           N  
ANISOU 1137  N   SER B   9     9484  10762  13721    695    -49   3169       N  
ATOM   1138  CA  SER B   9       3.920  15.943  20.727  1.00 90.07           C  
ANISOU 1138  CA  SER B   9     9591  10819  13814    697    -23   3209       C  
ATOM   1139  C   SER B   9       3.085  15.941  22.000  1.00 85.42           C  
ANISOU 1139  C   SER B   9     9052  10174  13228    712    -14   3218       C  
ATOM   1140  O   SER B   9       3.287  16.770  22.886  1.00 84.50           O  
ANISOU 1140  O   SER B   9     8973  10011  13122    715     -8   3226       O  
ATOM   1141  CB  SER B   9       3.143  16.577  19.577  1.00 94.38           C  
ANISOU 1141  CB  SER B   9    10099  11407  14353    694      4   3251       C  
ATOM   1142  OG  SER B   9       3.219  17.994  19.643  1.00 95.68           O  
ANISOU 1142  OG  SER B   9    10273  11554  14526    690     24   3283       O  
ATOM   1143  N   ALA B  10       2.155  14.994  22.091  1.00 89.43           N  
ANISOU 1143  N   ALA B  10     9564  10687  13729    722    -15   3215       N  
ATOM   1144  CA  ALA B  10       1.337  14.844  23.291  1.00 85.13           C  
ANISOU 1144  CA  ALA B  10     9067  10092  13188    737     -8   3220       C  
ATOM   1145  C   ALA B  10       2.199  14.422  24.473  1.00 82.09           C  
ANISOU 1145  C   ALA B  10     8721   9660  12810    740    -33   3181       C  
ATOM   1146  O   ALA B  10       1.948  14.835  25.613  1.00 79.81           O  
ANISOU 1146  O   ALA B  10     8478   9318  12529    748    -27   3188       O  
ATOM   1147  CB  ALA B  10       0.229  13.841  23.062  1.00 83.59           C  
ANISOU 1147  CB  ALA B  10     8862   9915  12982    746     -6   3222       C  
ATOM   1148  N   VAL B  11       3.214  13.601  24.188  1.00 81.55           N  
ANISOU 1148  N   VAL B  11     8632   9613  12739    732    -61   3141       N  
ATOM   1149  CA  VAL B  11       4.174  13.145  25.194  1.00 79.17           C  
ANISOU 1149  CA  VAL B  11     8363   9273  12445    733    -88   3101       C  
ATOM   1150  C   VAL B  11       5.032  14.285  25.728  1.00 80.14           C  
ANISOU 1150  C   VAL B  11     8508   9362  12579    727    -86   3105       C  
ATOM   1151  O   VAL B  11       5.058  14.528  26.936  1.00 77.50           O  
ANISOU 1151  O   VAL B  11     8220   8973  12252    734    -88   3101       O  
ATOM   1152  CB  VAL B  11       5.110  12.045  24.638  1.00 80.42           C  
ANISOU 1152  CB  VAL B  11     8491   9467  12598    724   -118   3057       C  
ATOM   1153  CG1 VAL B  11       6.288  11.839  25.565  1.00 79.13           C  
ANISOU 1153  CG1 VAL B  11     8356   9267  12443    722   -144   3019       C  
ATOM   1154  CG2 VAL B  11       4.359  10.738  24.453  1.00 78.63           C  
ANISOU 1154  CG2 VAL B  11     8253   9261  12361    732   -125   3044       C  
ATOM   1155  N   THR B  12       5.721  14.991  24.836  1.00 78.36           N  
ANISOU 1155  N   THR B  12     8250   9169  12356    714    -83   3114       N  
ATOM   1156  CA  THR B  12       6.682  16.000  25.280  1.00 80.11           C  
ANISOU 1156  CA  THR B  12     8489   9361  12588    707    -84   3114       C  
ATOM   1157  C   THR B  12       5.944  17.131  25.978  1.00 79.43           C  
ANISOU 1157  C   THR B  12     8438   9233  12509    715    -58   3152       C  
ATOM   1158  O   THR B  12       6.376  17.607  27.032  1.00 77.62           O  
ANISOU 1158  O   THR B  12     8249   8954  12289    717    -62   3146       O  
ATOM   1159  CB  THR B  12       7.535  16.559  24.112  1.00 85.38           C  
ANISOU 1159  CB  THR B  12     9112  10074  13256    691    -85   3117       C  
ATOM   1160  OG1 THR B  12       6.827  16.384  22.877  1.00 87.61           O  
ANISOU 1160  OG1 THR B  12     9349  10411  13527    689    -71   3138       O  
ATOM   1161  CG2 THR B  12       8.889  15.848  24.030  1.00 86.23           C  
ANISOU 1161  CG2 THR B  12     9206  10193  13364    682   -117   3071       C  
ATOM   1162  N   ALA B  13       4.814  17.536  25.402  1.00 78.68           N  
ANISOU 1162  N   ALA B  13     8329   9158  12409    719    -31   3191       N  
ATOM   1163  CA  ALA B  13       4.036  18.646  25.949  1.00 78.60           C  
ANISOU 1163  CA  ALA B  13     8348   9112  12404    726     -3   3231       C  
ATOM   1164  C   ALA B  13       3.570  18.325  27.357  1.00 74.16           C  
ANISOU 1164  C   ALA B  13     7839   8492  11845    739     -6   3223       C  
ATOM   1165  O   ALA B  13       3.491  19.211  28.212  1.00 73.95           O  
ANISOU 1165  O   ALA B  13     7850   8419  11828    744      6   3239       O  
ATOM   1166  CB  ALA B  13       2.863  18.962  25.064  1.00 80.60           C  
ANISOU 1166  CB  ALA B  13     8574   9399  12650    728     24   3272       C  
ATOM   1167  N   LEU B  14       3.277  17.050  27.603  1.00 75.94           N  
ANISOU 1167  N   LEU B  14     8068   8720  12065    746    -22   3197       N  
ATOM   1168  CA  LEU B  14       2.861  16.643  28.933  1.00 72.07           C  
ANISOU 1168  CA  LEU B  14     7629   8177  11578    759    -27   3186       C  
ATOM   1169  C   LEU B  14       4.072  16.624  29.845  1.00 71.45           C  
ANISOU 1169  C   LEU B  14     7579   8059  11508    756    -50   3152       C  
ATOM   1170  O   LEU B  14       4.005  17.068  30.991  1.00 71.00           O  
ANISOU 1170  O   LEU B  14     7569   7949  11459    763    -47   3155       O  
ATOM   1171  CB  LEU B  14       2.177  15.285  28.908  1.00 70.88           C  
ANISOU 1171  CB  LEU B  14     7473   8040  11418    768    -37   3169       C  
ATOM   1172  CG  LEU B  14       1.196  15.102  30.066  1.00 70.79           C  
ANISOU 1172  CG  LEU B  14     7508   7980  11408    784    -28   3178       C  
ATOM   1173  CD1 LEU B  14      -0.049  14.373  29.580  1.00 70.70           C  
ANISOU 1173  CD1 LEU B  14     7480   7997  11387    792    -17   3192       C  
ATOM   1174  CD2 LEU B  14       1.814  14.357  31.238  1.00 70.70           C  
ANISOU 1174  CD2 LEU B  14     7535   7927  11401    788    -54   3137       C  
ATOM   1175  N   TRP B  15       5.192  16.141  29.316  1.00 70.30           N  
ANISOU 1175  N   TRP B  15     7406   7942  11361    745    -74   3119       N  
ATOM   1176  CA  TRP B  15       6.413  15.995  30.108  1.00 70.29           C  
ANISOU 1176  CA  TRP B  15     7429   7910  11368    741   -100   3083       C  
ATOM   1177  C   TRP B  15       6.868  17.361  30.598  1.00 70.40           C  
ANISOU 1177  C   TRP B  15     7467   7888  11393    737    -88   3102       C  
ATOM   1178  O   TRP B  15       7.493  17.488  31.657  1.00 70.39           O  
ANISOU 1178  O   TRP B  15     7504   7841  11400    739   -101   3083       O  
ATOM   1179  CB  TRP B  15       7.510  15.307  29.291  1.00 70.31           C  
ANISOU 1179  CB  TRP B  15     7392   7954  11367    729   -125   3048       C  
ATOM   1180  CG  TRP B  15       8.675  14.773  30.122  1.00 70.27           C  
ANISOU 1180  CG  TRP B  15     7411   7920  11369    727   -156   3003       C  
ATOM   1181  CD1 TRP B  15       9.982  15.217  30.103  1.00 70.55           C  
ANISOU 1181  CD1 TRP B  15     7442   7952  11411    715   -171   2985       C  
ATOM   1182  CD2 TRP B  15       8.639  13.694  31.075  1.00 70.14           C  
ANISOU 1182  CD2 TRP B  15     7425   7874  11352    736   -176   2971       C  
ATOM   1183  NE1 TRP B  15      10.739  14.482  30.985  1.00 70.29           N  
ANISOU 1183  NE1 TRP B  15     7435   7889  11382    717   -198   2945       N  
ATOM   1184  CE2 TRP B  15       9.941  13.542  31.588  1.00 70.16           C  
ANISOU 1184  CE2 TRP B  15     7440   7856  11361    729   -202   2935       C  
ATOM   1185  CE3 TRP B  15       7.636  12.852  31.541  1.00 70.02           C  
ANISOU 1185  CE3 TRP B  15     7428   7847  11331    749   -175   2970       C  
ATOM   1186  CZ2 TRP B  15      10.253  12.592  32.546  1.00 70.06           C  
ANISOU 1186  CZ2 TRP B  15     7457   7812  11350    735   -226   2899       C  
ATOM   1187  CZ3 TRP B  15       7.960  11.905  32.484  1.00 69.92           C  
ANISOU 1187  CZ3 TRP B  15     7444   7804  11320    754   -199   2933       C  
ATOM   1188  CH2 TRP B  15       9.249  11.789  32.980  1.00 69.94           C  
ANISOU 1188  CH2 TRP B  15     7458   7786  11329    748   -224   2898       C  
ATOM   1189  N   GLY B  16       6.522  18.382  29.818  1.00 73.84           N  
ANISOU 1189  N   GLY B  16     7880   8347  11829    733    -63   3140       N  
ATOM   1190  CA  GLY B  16       6.763  19.755  30.205  1.00 76.61           C  
ANISOU 1190  CA  GLY B  16     8251   8667  12190    730    -47   3164       C  
ATOM   1191  C   GLY B  16       6.123  20.091  31.543  1.00 74.49           C  
ANISOU 1191  C   GLY B  16     8039   8337  11928    743    -37   3176       C  
ATOM   1192  O   GLY B  16       6.750  20.725  32.399  1.00 75.84           O  
ANISOU 1192  O   GLY B  16     8242   8465  12108    742    -41   3170       O  
ATOM   1193  N   LYS B  17       4.885  19.656  31.743  1.00 70.53           N  
ANISOU 1193  N   LYS B  17     7548   7831  11420    755    -24   3191       N  
ATOM   1194  CA  LYS B  17       4.180  20.025  32.958  1.00 70.49           C  
ANISOU 1194  CA  LYS B  17     7594   7769  11420    767    -11   3206       C  
ATOM   1195  C   LYS B  17       4.640  19.195  34.169  1.00 70.39           C  
ANISOU 1195  C   LYS B  17     7621   7714  11411    773    -36   3167       C  
ATOM   1196  O   LYS B  17       4.232  19.443  35.305  1.00 70.36           O  
ANISOU 1196  O   LYS B  17     7664   7658  11411    783    -30   3173       O  
ATOM   1197  CB  LYS B  17       2.667  19.891  32.756  1.00 70.44           C  
ANISOU 1197  CB  LYS B  17     7585   7772  11407    778     13   3238       C  
ATOM   1198  CG  LYS B  17       2.101  20.674  31.575  1.00 70.53           C  
ANISOU 1198  CG  LYS B  17     7558   7825  11415    773     39   3279       C  
ATOM   1199  CD  LYS B  17       0.561  20.671  31.596  1.00 70.48           C  
ANISOU 1199  CD  LYS B  17     7559   7817  11403    785     65   3313       C  
ATOM   1200  CE  LYS B  17      -0.042  21.500  30.465  1.00 70.57           C  
ANISOU 1200  CE  LYS B  17     7534   7868  11412    781     92   3356       C  
ATOM   1201  NZ  LYS B  17      -1.508  21.566  30.608  1.00 70.53           N  
ANISOU 1201  NZ  LYS B  17     7540   7854  11403    793    117   3389       N  
ATOM   1202  N   VAL B  18       5.496  18.214  33.935  1.00 70.58           N  
ANISOU 1202  N   VAL B  18     7628   7759  11432    768    -65   3126       N  
ATOM   1203  CA  VAL B  18       5.905  17.314  35.010  1.00 69.98           C  
ANISOU 1203  CA  VAL B  18     7586   7646  11357    773    -90   3088       C  
ATOM   1204  C   VAL B  18       6.899  17.953  35.991  1.00 70.31           C  
ANISOU 1204  C   VAL B  18     7664   7640  11410    770   -101   3073       C  
ATOM   1205  O   VAL B  18       7.977  18.391  35.587  1.00 72.86           O  
ANISOU 1205  O   VAL B  18     7969   7976  11737    758   -111   3063       O  
ATOM   1206  CB  VAL B  18       6.548  16.028  34.433  1.00 69.92           C  
ANISOU 1206  CB  VAL B  18     7546   7677  11343    768   -119   3047       C  
ATOM   1207  CG1 VAL B  18       7.176  15.180  35.547  1.00 69.83           C  
ANISOU 1207  CG1 VAL B  18     7570   7627  11335    772   -147   3005       C  
ATOM   1208  CG2 VAL B  18       5.523  15.218  33.647  1.00 69.85           C  
ANISOU 1208  CG2 VAL B  18     7507   7709  11322    773   -111   3057       C  
ATOM   1209  N   ASN B  19       6.558  17.963  37.281  1.00 68.49           N  
ANISOU 1209  N   ASN B  19     7485   7354  11185    781   -100   3071       N  
ATOM   1210  CA  ASN B  19       7.452  18.553  38.273  1.00 68.54           C  
ANISOU 1210  CA  ASN B  19     7528   7312  11201    778   -110   3058       C  
ATOM   1211  C   ASN B  19       8.733  17.731  38.438  1.00 68.51           C  
ANISOU 1211  C   ASN B  19     7520   7311  11199    771   -146   3009       C  
ATOM   1212  O   ASN B  19       8.712  16.608  38.899  1.00 68.40           O  
ANISOU 1212  O   ASN B  19     7518   7289  11181    777   -165   2980       O  
ATOM   1213  CB  ASN B  19       6.727  18.665  39.616  1.00 68.48           C  
ANISOU 1213  CB  ASN B  19     7576   7245  11197    792   -102   3066       C  
ATOM   1214  CG  ASN B  19       7.616  19.208  40.720  1.00 68.52           C  
ANISOU 1214  CG  ASN B  19     7622   7198  11213    791   -113   3050       C  
ATOM   1215  OD1 ASN B  19       8.714  19.690  40.470  1.00 68.60           O  
ANISOU 1215  OD1 ASN B  19     7621   7215  11229    779   -123   3039       O  
ATOM   1216  ND2 ASN B  19       7.129  19.148  41.952  1.00 68.46           N  
ANISOU 1216  ND2 ASN B  19     7664   7138  11208    802   -110   3050       N  
ATOM   1217  N   VAL B  20       9.875  18.326  38.149  1.00 68.61           N  
ANISOU 1217  N   VAL B  20     7520   7330  11218    759   -155   3000       N  
ATOM   1218  CA  VAL B  20      11.109  17.555  38.107  1.00 68.59           C  
ANISOU 1218  CA  VAL B  20     7506   7338  11216    751   -187   2956       C  
ATOM   1219  C   VAL B  20      11.774  17.481  39.461  1.00 68.56           C  
ANISOU 1219  C   VAL B  20     7551   7278  11221    754   -206   2929       C  
ATOM   1220  O   VAL B  20      12.806  16.843  39.606  1.00 68.54           O  
ANISOU 1220  O   VAL B  20     7546   7276  11220    748   -234   2891       O  
ATOM   1221  CB  VAL B  20      12.119  18.139  37.118  1.00 68.71           C  
ANISOU 1221  CB  VAL B  20     7482   7390  11234    735   -191   2955       C  
ATOM   1222  CG1 VAL B  20      11.500  18.293  35.737  1.00 68.75           C  
ANISOU 1222  CG1 VAL B  20     7438   7452  11231    731   -172   2983       C  
ATOM   1223  CG2 VAL B  20      12.604  19.454  37.628  1.00 68.81           C  
ANISOU 1223  CG2 VAL B  20     7520   7368  11258    731   -181   2972       C  
ATOM   1224  N   ASP B  21      11.223  18.164  40.450  1.00 68.57           N  
ANISOU 1224  N   ASP B  21     7596   7229  11227    762   -190   2950       N  
ATOM   1225  CA  ASP B  21      11.796  18.062  41.781  1.00 68.53           C  
ANISOU 1225  CA  ASP B  21     7640   7170  11230    766   -207   2925       C  
ATOM   1226  C   ASP B  21      11.020  17.073  42.620  1.00 68.40           C  
ANISOU 1226  C   ASP B  21     7653   7127  11208    780   -213   2912       C  
ATOM   1227  O   ASP B  21      11.448  16.760  43.744  1.00 68.35           O  
ANISOU 1227  O   ASP B  21     7686   7077  11207    784   -230   2887       O  
ATOM   1228  CB  ASP B  21      11.826  19.424  42.487  1.00 68.63           C  
ANISOU 1228  CB  ASP B  21     7687   7137  11251    766   -189   2950       C  
ATOM   1229  CG  ASP B  21      12.866  20.376  41.903  1.00 68.92           C  
ANISOU 1229  CG  ASP B  21     7702   7190  11296    752   -190   2954       C  
ATOM   1230  OD1 ASP B  21      13.961  19.928  41.487  1.00 68.83           O  
ANISOU 1230  OD1 ASP B  21     7667   7201  11284    742   -214   2924       O  
ATOM   1231  OD2 ASP B  21      12.588  21.591  41.867  1.00 72.26           O  
ANISOU 1231  OD2 ASP B  21     8132   7601  11723    751   -166   2989       O  
ATOM   1232  N   GLU B  22       9.905  16.560  42.077  1.00 68.33           N  
ANISOU 1232  N   GLU B  22     7626   7146  11191    787   -199   2928       N  
ATOM   1233  CA  GLU B  22       9.038  15.644  42.847  1.00 68.20           C  
ANISOU 1233  CA  GLU B  22     7637   7106  11170    801   -202   2920       C  
ATOM   1234  C   GLU B  22       8.681  14.281  42.215  1.00 68.10           C  
ANISOU 1234  C   GLU B  22     7593   7134  11146    803   -215   2901       C  
ATOM   1235  O   GLU B  22       8.894  13.242  42.833  1.00 68.00           O  
ANISOU 1235  O   GLU B  22     7598   7106  11132    808   -237   2867       O  
ATOM   1236  CB  GLU B  22       7.753  16.359  43.248  1.00 68.20           C  
ANISOU 1236  CB  GLU B  22     7663   7081  11170    812   -170   2961       C  
ATOM   1237  CG  GLU B  22       7.725  16.703  44.736  1.00 68.18           C  
ANISOU 1237  CG  GLU B  22     7720   7012  11175    820   -171   2959       C  
ATOM   1238  CD  GLU B  22       8.562  15.715  45.593  1.00 68.11           C  
ANISOU 1238  CD  GLU B  22     7733   6977  11167    821   -204   2911       C  
ATOM   1239  OE1 GLU B  22       8.382  14.466  45.502  1.00 68.00           O  
ANISOU 1239  OE1 GLU B  22     7710   6980  11146    825   -221   2887       O  
ATOM   1240  OE2 GLU B  22       9.426  16.201  46.365  1.00 68.15           O  
ANISOU 1240  OE2 GLU B  22     7768   6945  11181    817   -215   2898       O  
ATOM   1241  N   VAL B  23       8.081  14.310  41.029  1.00 61.56           N  
ANISOU 1241  N   VAL B  23     9208   8341   5841    902   -720   -452       N  
ATOM   1242  CA  VAL B  23       7.540  13.131  40.365  1.00 58.85           C  
ANISOU 1242  CA  VAL B  23     8851   7997   5511    921   -709   -450       C  
ATOM   1243  C   VAL B  23       8.457  11.925  40.376  1.00 56.83           C  
ANISOU 1243  C   VAL B  23     8580   7755   5256    911   -707   -432       C  
ATOM   1244  O   VAL B  23       8.042  10.840  40.786  1.00 54.52           O  
ANISOU 1244  O   VAL B  23     8278   7471   4966    913   -700   -432       O  
ATOM   1245  CB  VAL B  23       7.213  13.434  38.910  1.00 59.70           C  
ANISOU 1245  CB  VAL B  23     8959   8091   5635    943   -705   -452       C  
ATOM   1246  CG1 VAL B  23       7.060  12.167  38.121  1.00 57.39           C  
ANISOU 1246  CG1 VAL B  23     8650   7800   5355    957   -696   -445       C  
ATOM   1247  CG2 VAL B  23       5.968  14.223  38.839  1.00 61.06           C  
ANISOU 1247  CG2 VAL B  23     9141   8250   5810    959   -702   -470       C  
ATOM   1248  N   GLY B  24       9.701  12.093  39.946  1.00 57.94           N  
ANISOU 1248  N   GLY B  24     8720   7899   5395    899   -715   -418       N  
ATOM   1249  CA  GLY B  24      10.596  10.955  39.875  1.00 56.20           C  
ANISOU 1249  CA  GLY B  24     8485   7691   5176    890   -713   -400       C  
ATOM   1250  C   GLY B  24      10.744  10.276  41.219  1.00 54.52           C  
ANISOU 1250  C   GLY B  24     8268   7495   4951    873   -714   -397       C  
ATOM   1251  O   GLY B  24      10.751   9.062  41.310  1.00 52.18           O  
ANISOU 1251  O   GLY B  24     7960   7208   4659    875   -707   -390       O  
ATOM   1252  N   GLY B  25      10.826  11.077  42.272  1.00 56.19           N  
ANISOU 1252  N   GLY B  25     8491   7711   5148    858   -721   -403       N  
ATOM   1253  CA  GLY B  25      11.065  10.561  43.602  1.00 55.28           C  
ANISOU 1253  CA  GLY B  25     8372   7611   5019    839   -723   -400       C  
ATOM   1254  C   GLY B  25       9.820   9.887  44.098  1.00 54.05           C  
ANISOU 1254  C   GLY B  25     8213   7455   4867    852   -712   -411       C  
ATOM   1255  O   GLY B  25       9.880   8.964  44.895  1.00 53.40           O  
ANISOU 1255  O   GLY B  25     8124   7386   4780    844   -709   -406       O  
ATOM   1256  N   GLU B  26       8.673  10.344  43.624  1.00 55.36           N  
ANISOU 1256  N   GLU B  26     8386   7607   5042    872   -707   -427       N  
ATOM   1257  CA  GLU B  26       7.437   9.721  44.056  1.00 54.11           C  
ANISOU 1257  CA  GLU B  26     8225   7448   4888    884   -697   -439       C  
ATOM   1258  C   GLU B  26       7.260   8.387  43.368  1.00 51.69           C  
ANISOU 1258  C   GLU B  26     7902   7143   4594    898   -687   -432       C  
ATOM   1259  O   GLU B  26       6.766   7.452  44.000  1.00 50.42           O  
ANISOU 1259  O   GLU B  26     7734   6989   4433    899   -679   -434       O  
ATOM   1260  CB  GLU B  26       6.243  10.604  43.783  1.00 55.29           C  
ANISOU 1260  CB  GLU B  26     8384   7581   5042    901   -695   -457       C  
ATOM   1261  CG  GLU B  26       5.012  10.120  44.505  1.00 55.21           C  
ANISOU 1261  CG  GLU B  26     8373   7572   5032    910   -687   -470       C  
ATOM   1262  CD  GLU B  26       3.796  11.031  44.327  1.00 56.81           C  
ANISOU 1262  CD  GLU B  26     8586   7759   5239    926   -685   -489       C  
ATOM   1263  OE1 GLU B  26       3.980  12.265  44.071  1.00 57.37           O  
ANISOU 1263  OE1 GLU B  26     8669   7822   5307    924   -692   -493       O  
ATOM   1264  OE2 GLU B  26       2.666  10.482  44.445  1.00 57.74           O  
ANISOU 1264  OE2 GLU B  26     8700   7876   5364    940   -675   -499       O  
ATOM   1265  N   ALA B  27       7.676   8.294  42.095  1.00 50.84           N  
ANISOU 1265  N   ALA B  27     7790   7029   4498    908   -686   -424       N  
ATOM   1266  CA  ALA B  27       7.625   7.031  41.358  1.00 48.91           C  
ANISOU 1266  CA  ALA B  27     7530   6786   4266    920   -676   -417       C  
ATOM   1267  C   ALA B  27       8.549   6.043  42.055  1.00 47.66           C  
ANISOU 1267  C   ALA B  27     7363   6646   4101    902   -677   -401       C  
ATOM   1268  O   ALA B  27       8.213   4.870  42.219  1.00 46.11           O  
ANISOU 1268  O   ALA B  27     7156   6456   3909    908   -667   -399       O  
ATOM   1269  CB  ALA B  27       8.006   7.204  39.885  1.00 49.45           C  
ANISOU 1269  CB  ALA B  27     7596   6845   4348    933   -676   -411       C  
ATOM   1270  N   LEU B  28       9.697   6.509  42.515  1.00 47.92           N  
ANISOU 1270  N   LEU B  28     7399   6686   4122    881   -687   -390       N  
ATOM   1271  CA  LEU B  28      10.646   5.571  43.104  1.00 46.96           C  
ANISOU 1271  CA  LEU B  28     7268   6582   3993    864   -689   -373       C  
ATOM   1272  C   LEU B  28      10.116   4.996  44.408  1.00 46.62           C  
ANISOU 1272  C   LEU B  28     7224   6549   3941    857   -685   -378       C  
ATOM   1273  O   LEU B  28      10.098   3.790  44.588  1.00 45.45           O  
ANISOU 1273  O   LEU B  28     7065   6410   3795    859   -677   -372       O  
ATOM   1274  CB  LEU B  28      12.010   6.225  43.350  1.00 48.43           C  
ANISOU 1274  CB  LEU B  28     7459   6776   4168    842   -702   -360       C  
ATOM   1275  CG  LEU B  28      12.926   5.475  44.303  1.00 48.52           C  
ANISOU 1275  CG  LEU B  28     7463   6806   4167    821   -705   -345       C  
ATOM   1276  CD1 LEU B  28      13.330   4.190  43.673  1.00 46.80           C  
ANISOU 1276  CD1 LEU B  28     7230   6594   3959    826   -697   -331       C  
ATOM   1277  CD2 LEU B  28      14.123   6.302  44.597  1.00 50.80           C  
ANISOU 1277  CD2 LEU B  28     7756   7101   4443    799   -718   -335       C  
ATOM   1278  N   GLY B  29       9.693   5.856  45.320  1.00 46.50           N  
ANISOU 1278  N   GLY B  29     7220   6533   3914    850   -690   -390       N  
ATOM   1279  CA  GLY B  29       9.234   5.400  46.621  1.00 46.64           C  
ANISOU 1279  CA  GLY B  29     7238   6562   3922    842   -687   -395       C  
ATOM   1280  C   GLY B  29       7.958   4.559  46.569  1.00 45.22           C  
ANISOU 1280  C   GLY B  29     7052   6377   3752    862   -674   -406       C  
ATOM   1281  O   GLY B  29       7.596   3.883  47.547  1.00 45.07           O  
ANISOU 1281  O   GLY B  29     7030   6368   3727    857   -669   -407       O  
ATOM   1282  N   ARG B  30       7.239   4.604  45.448  1.00 45.19           N  
ANISOU 1282  N   ARG B  30     7047   6359   3763    884   -667   -414       N  
ATOM   1283  CA  ARG B  30       6.047   3.791  45.378  1.00 44.83           C  
ANISOU 1283  CA  ARG B  30     6995   6310   3728    902   -655   -424       C  
ATOM   1284  C   ARG B  30       6.502   2.396  45.041  1.00 44.19           C  
ANISOU 1284  C   ARG B  30     6899   6238   3653    904   -647   -410       C  
ATOM   1285  O   ARG B  30       6.125   1.428  45.702  1.00 43.81           O  
ANISOU 1285  O   ARG B  30     6844   6198   3603    903   -640   -409       O  
ATOM   1286  CB  ARG B  30       5.018   4.362  44.382  1.00 45.06           C  
ANISOU 1286  CB  ARG B  30     7028   6322   3770    925   -650   -438       C  
ATOM   1287  CG  ARG B  30       4.029   5.359  45.055  1.00 45.61           C  
ANISOU 1287  CG  ARG B  30     7112   6385   3834    927   -653   -456       C  
ATOM   1288  CD  ARG B  30       3.129   6.115  44.085  1.00 45.91           C  
ANISOU 1288  CD  ARG B  30     7154   6405   3883    948   -650   -469       C  
ATOM   1289  NE  ARG B  30       2.381   7.196  44.753  1.00 46.47           N  
ANISOU 1289  NE  ARG B  30     7240   6470   3947    947   -655   -485       N  
ATOM   1290  CZ  ARG B  30       1.210   7.049  45.387  1.00 46.49           C  
ANISOU 1290  CZ  ARG B  30     7243   6471   3949    955   -649   -499       C  
ATOM   1291  NH1 ARG B  30       0.592   5.876  45.458  1.00 45.98           N  
ANISOU 1291  NH1 ARG B  30     7167   6411   3891    965   -638   -500       N  
ATOM   1292  NH2 ARG B  30       0.638   8.088  45.957  1.00 47.04           N  
ANISOU 1292  NH2 ARG B  30     7326   6535   4012    953   -653   -511       N  
ATOM   1293  N   LEU B  31       7.396   2.303  44.076  1.00 44.74           N  
ANISOU 1293  N   LEU B  31     6964   6306   3729    903   -649   -397       N  
ATOM   1294  CA  LEU B  31       8.093   1.027  43.815  1.00 43.47           C  
ANISOU 1294  CA  LEU B  31     6789   6156   3573    901   -644   -380       C  
ATOM   1295  C   LEU B  31       8.665   0.335  45.067  1.00 43.23           C  
ANISOU 1295  C   LEU B  31     6754   6142   3528    882   -645   -370       C  
ATOM   1296  O   LEU B  31       8.460  -0.835  45.281  1.00 42.33           O  
ANISOU 1296  O   LEU B  31     6631   6036   3417    885   -636   -366       O  
ATOM   1297  CB  LEU B  31       9.232   1.243  42.827  1.00 43.63           C  
ANISOU 1297  CB  LEU B  31     6806   6174   3597    897   -650   -366       C  
ATOM   1298  CG  LEU B  31      10.023  -0.018  42.541  1.00 42.57           C  
ANISOU 1298  CG  LEU B  31     6658   6051   3467    893   -645   -348       C  
ATOM   1299  CD1 LEU B  31      10.052  -0.194  41.072  1.00 42.36           C  
ANISOU 1299  CD1 LEU B  31     6624   6013   3456    910   -641   -346       C  
ATOM   1300  CD2 LEU B  31      11.403   0.154  43.062  1.00 43.10           C  
ANISOU 1300  CD2 LEU B  31     6725   6129   3521    870   -656   -331       C  
ATOM   1301  N   LEU B  32       9.384   1.063  45.890  1.00 41.79           N  
ANISOU 1301  N   LEU B  32     6580   5967   3331    861   -657   -365       N  
ATOM   1302  CA  LEU B  32       9.829   0.502  47.149  1.00 41.93           C  
ANISOU 1302  CA  LEU B  32     6595   6002   3335    843   -659   -357       C  
ATOM   1303  C   LEU B  32       8.677  -0.074  47.964  1.00 41.94           C  
ANISOU 1303  C   LEU B  32     6596   6006   3335    851   -649   -369       C  
ATOM   1304  O   LEU B  32       8.846  -1.091  48.636  1.00 41.91           O  
ANISOU 1304  O   LEU B  32     6583   6013   3326    845   -644   -361       O  
ATOM   1305  CB  LEU B  32      10.567   1.559  47.982  1.00 42.27           C  
ANISOU 1305  CB  LEU B  32     6648   6051   3361    821   -673   -355       C  
ATOM   1306  CG  LEU B  32      11.821   2.099  47.318  1.00 42.28           C  
ANISOU 1306  CG  LEU B  32     6650   6054   3362    811   -683   -341       C  
ATOM   1307  CD1 LEU B  32      12.458   3.128  48.214  1.00 42.63           C  
ANISOU 1307  CD1 LEU B  32     6704   6105   3389    789   -696   -340       C  
ATOM   1308  CD2 LEU B  32      12.744   0.941  47.056  1.00 42.08           C  
ANISOU 1308  CD2 LEU B  32     6611   6039   3339    806   -680   -321       C  
ATOM   1309  N   VAL B  33       7.524   0.597  47.929  1.00 42.67           N  
ANISOU 1309  N   VAL B  33     6696   6085   3431    864   -647   -389       N  
ATOM   1310  CA  VAL B  33       6.391   0.229  48.782  1.00 42.73           C  
ANISOU 1310  CA  VAL B  33     6705   6094   3436    869   -639   -402       C  
ATOM   1311  C   VAL B  33       5.534  -0.907  48.212  1.00 42.43           C  
ANISOU 1311  C   VAL B  33     6656   6052   3413    890   -625   -406       C  
ATOM   1312  O   VAL B  33       5.157  -1.852  48.937  1.00 42.40           O  
ANISOU 1312  O   VAL B  33     6646   6057   3406    889   -617   -405       O  
ATOM   1313  CB  VAL B  33       5.510   1.416  49.028  1.00 42.94           C  
ANISOU 1313  CB  VAL B  33     6745   6110   3461    874   -643   -420       C  
ATOM   1314  CG1 VAL B  33       4.142   0.956  49.478  1.00 42.92           C  
ANISOU 1314  CG1 VAL B  33     6741   6104   3462    888   -633   -435       C  
ATOM   1315  CG2 VAL B  33       6.161   2.339  50.057  1.00 43.28           C  
ANISOU 1315  CG2 VAL B  33     6798   6161   3486    851   -656   -419       C  
ATOM   1316  N   VAL B  34       5.259  -0.812  46.902  1.00 44.97           N  
ANISOU 1316  N   VAL B  34     6975   6361   3749    907   -621   -409       N  
ATOM   1317  CA  VAL B  34       4.410  -1.764  46.172  1.00 44.39           C  
ANISOU 1317  CA  VAL B  34     6892   6284   3692    928   -607   -414       C  
ATOM   1318  C   VAL B  34       5.086  -3.110  45.909  1.00 43.18           C  
ANISOU 1318  C   VAL B  34     6724   6140   3543    927   -600   -397       C  
ATOM   1319  O   VAL B  34       4.447  -4.158  46.030  1.00 43.23           O  
ANISOU 1319  O   VAL B  34     6722   6149   3554    936   -589   -400       O  
ATOM   1320  CB  VAL B  34       3.972  -1.167  44.847  1.00 44.47           C  
ANISOU 1320  CB  VAL B  34     6904   6278   3716    947   -606   -421       C  
ATOM   1321  CG1 VAL B  34       3.403  -2.230  43.919  1.00 44.27           C  
ANISOU 1321  CG1 VAL B  34     6865   6249   3706    966   -593   -422       C  
ATOM   1322  CG2 VAL B  34       2.946  -0.061  45.113  1.00 44.17           C  
ANISOU 1322  CG2 VAL B  34     6877   6229   3676    953   -609   -440       C  
ATOM   1323  N   TYR B  35       6.374  -3.077  45.563  1.00 42.64           N  
ANISOU 1323  N   TYR B  35     6654   6077   3472    915   -607   -381       N  
ATOM   1324  CA  TYR B  35       7.168  -4.263  45.316  1.00 41.63           C  
ANISOU 1324  CA  TYR B  35     6513   5959   3347    911   -602   -363       C  
ATOM   1325  C   TYR B  35       8.330  -4.300  46.267  1.00 42.06           C  
ANISOU 1325  C   TYR B  35     6568   6027   3385    887   -611   -348       C  
ATOM   1326  O   TYR B  35       9.453  -4.089  45.845  1.00 41.60           O  
ANISOU 1326  O   TYR B  35     6508   5972   3325    877   -619   -333       O  
ATOM   1327  CB  TYR B  35       7.681  -4.253  43.890  1.00 40.59           C  
ANISOU 1327  CB  TYR B  35     6376   5819   3227    920   -602   -356       C  
ATOM   1328  CG  TYR B  35       6.599  -3.975  42.897  1.00 40.52           C  
ANISOU 1328  CG  TYR B  35     6368   5796   3233    943   -596   -372       C  
ATOM   1329  CD1 TYR B  35       5.561  -4.888  42.689  1.00 40.60           C  
ANISOU 1329  CD1 TYR B  35     6369   5803   3253    960   -582   -380       C  
ATOM   1330  CD2 TYR B  35       6.594  -2.795  42.169  1.00 40.72           C  
ANISOU 1330  CD2 TYR B  35     6401   5809   3262    948   -603   -378       C  
ATOM   1331  CE1 TYR B  35       4.544  -4.635  41.779  1.00 40.82           C  
ANISOU 1331  CE1 TYR B  35     6396   5818   3294    981   -577   -394       C  
ATOM   1332  CE2 TYR B  35       5.587  -2.518  41.254  1.00 40.88           C  
ANISOU 1332  CE2 TYR B  35     6422   5816   3296    969   -598   -392       C  
ATOM   1333  CZ  TYR B  35       4.560  -3.438  41.064  1.00 40.90           C  
ANISOU 1333  CZ  TYR B  35     6415   5817   3307    986   -584   -400       C  
ATOM   1334  OH  TYR B  35       3.570  -3.152  40.143  1.00 41.29           O  
ANISOU 1334  OH  TYR B  35     6464   5854   3369   1007   -579   -413       O  
ATOM   1335  N   PRO B  36       8.084  -4.618  47.546  1.00 41.00           N  
ANISOU 1335  N   PRO B  36     6436   5903   3239    877   -610   -349       N  
ATOM   1336  CA  PRO B  36       9.089  -4.393  48.601  1.00 42.12           C  
ANISOU 1336  CA  PRO B  36     6581   6060   3364    853   -621   -337       C  
ATOM   1337  C   PRO B  36      10.461  -5.024  48.392  1.00 41.41           C  
ANISOU 1337  C   PRO B  36     6482   5981   3272    841   -624   -314       C  
ATOM   1338  O   PRO B  36      11.358  -4.673  49.140  1.00 42.58           O  
ANISOU 1338  O   PRO B  36     6633   6140   3406    820   -634   -304       O  
ATOM   1339  CB  PRO B  36       8.440  -4.987  49.856  1.00 43.67           C  
ANISOU 1339  CB  PRO B  36     6777   6265   3552    850   -615   -343       C  
ATOM   1340  CG  PRO B  36       7.192  -5.653  49.403  1.00 43.11           C  
ANISOU 1340  CG  PRO B  36     6701   6185   3494    872   -601   -356       C  
ATOM   1341  CD  PRO B  36       6.793  -5.030  48.107  1.00 41.81           C  
ANISOU 1341  CD  PRO B  36     6538   6004   3343    888   -600   -365       C  
ATOM   1342  N   TRP B  37      10.646  -5.934  47.446  1.00 40.21           N  
ANISOU 1342  N   TRP B  37     6319   5827   3133    851   -615   -306       N  
ATOM   1343  CA  TRP B  37      11.951  -6.563  47.333  1.00 40.11           C  
ANISOU 1343  CA  TRP B  37     6298   5826   3117    839   -618   -283       C  
ATOM   1344  C   TRP B  37      13.002  -5.651  46.704  1.00 40.38           C  
ANISOU 1344  C   TRP B  37     6336   5858   3150    829   -631   -274       C  
ATOM   1345  O   TRP B  37      14.193  -5.925  46.806  1.00 40.46           O  
ANISOU 1345  O   TRP B  37     6341   5878   3154    814   -637   -255       O  
ATOM   1346  CB  TRP B  37      11.848  -7.846  46.541  1.00 39.46           C  
ANISOU 1346  CB  TRP B  37     6202   5743   3048    853   -605   -277       C  
ATOM   1347  CG  TRP B  37      11.263  -7.668  45.208  1.00 39.10           C  
ANISOU 1347  CG  TRP B  37     6156   5682   3020    873   -600   -286       C  
ATOM   1348  CD1 TRP B  37      11.900  -7.250  44.063  1.00 39.03           C  
ANISOU 1348  CD1 TRP B  37     6145   5665   3018    875   -604   -280       C  
ATOM   1349  CD2 TRP B  37       9.910  -7.909  44.848  1.00 38.92           C  
ANISOU 1349  CD2 TRP B  37     6132   5648   3008    894   -588   -304       C  
ATOM   1350  NE1 TRP B  37      11.014  -7.220  43.006  1.00 38.74           N  
ANISOU 1350  NE1 TRP B  37     6107   5615   2997    897   -597   -293       N  
ATOM   1351  CE2 TRP B  37       9.784  -7.619  43.462  1.00 38.72           C  
ANISOU 1351  CE2 TRP B  37     6105   5611   2997    908   -587   -308       C  
ATOM   1352  CE3 TRP B  37       8.783  -8.330  45.559  1.00 38.95           C  
ANISOU 1352  CE3 TRP B  37     6136   5652   3010    901   -579   -318       C  
ATOM   1353  CZ2 TRP B  37       8.576  -7.749  42.783  1.00 38.56           C  
ANISOU 1353  CZ2 TRP B  37     6082   5579   2990    930   -577   -324       C  
ATOM   1354  CZ3 TRP B  37       7.601  -8.457  44.885  1.00 38.78           C  
ANISOU 1354  CZ3 TRP B  37     6113   5620   3003    923   -570   -334       C  
ATOM   1355  CH2 TRP B  37       7.504  -8.175  43.502  1.00 38.59           C  
ANISOU 1355  CH2 TRP B  37     6087   5584   2993    937   -568   -337       C  
ATOM   1356  N   THR B  38      12.593  -4.565  46.062  1.00 40.75           N  
ANISOU 1356  N   THR B  38     6390   5890   3202    837   -635   -287       N  
ATOM   1357  CA  THR B  38      13.594  -3.659  45.537  1.00 40.83           C  
ANISOU 1357  CA  THR B  38     6405   5899   3210    827   -647   -278       C  
ATOM   1358  C   THR B  38      14.245  -2.881  46.664  1.00 41.18           C  
ANISOU 1358  C   THR B  38     6457   5953   3236    804   -660   -274       C  
ATOM   1359  O   THR B  38      15.351  -2.346  46.506  1.00 41.28           O  
ANISOU 1359  O   THR B  38     6472   5970   3243    790   -671   -262       O  
ATOM   1360  CB  THR B  38      13.020  -2.692  44.584  1.00 40.79           C  
ANISOU 1360  CB  THR B  38     6407   5876   3215    841   -649   -292       C  
ATOM   1361  OG1 THR B  38      11.814  -2.192  45.163  1.00 40.93           O  
ANISOU 1361  OG1 THR B  38     6434   5887   3230    849   -646   -312       O  
ATOM   1362  CG2 THR B  38      12.757  -3.369  43.248  1.00 40.44           C  
ANISOU 1362  CG2 THR B  38     6354   5823   3189    861   -639   -291       C  
ATOM   1363  N   GLN B  39      13.577  -2.830  47.811  1.00 40.79           N  
ANISOU 1363  N   GLN B  39     6414   5909   3177    800   -659   -284       N  
ATOM   1364  CA  GLN B  39      14.147  -2.133  48.954  1.00 42.65           C  
ANISOU 1364  CA  GLN B  39     6656   6156   3394    778   -671   -281       C  
ATOM   1365  C   GLN B  39      15.566  -2.588  49.231  1.00 43.03           C  
ANISOU 1365  C   GLN B  39     6696   6219   3433    759   -678   -258       C  
ATOM   1366  O   GLN B  39      16.379  -1.852  49.781  1.00 44.64           O  
ANISOU 1366  O   GLN B  39     6905   6432   3623    740   -690   -252       O  
ATOM   1367  CB  GLN B  39      13.306  -2.358  50.188  1.00 43.66           C  
ANISOU 1367  CB  GLN B  39     6787   6289   3512    776   -667   -292       C  
ATOM   1368  CG  GLN B  39      11.961  -1.844  50.026  1.00 43.93           C  
ANISOU 1368  CG  GLN B  39     6829   6309   3553    793   -662   -315       C  
ATOM   1369  CD  GLN B  39      11.207  -1.897  51.303  1.00 45.83           C  
ANISOU 1369  CD  GLN B  39     7075   6556   3784    789   -660   -325       C  
ATOM   1370  OE1 GLN B  39      11.622  -2.569  52.246  1.00 46.86           O  
ANISOU 1370  OE1 GLN B  39     7200   6701   3903    776   -659   -315       O  
ATOM   1371  NE2 GLN B  39      10.079  -1.172  51.359  1.00 46.65           N  
ANISOU 1371  NE2 GLN B  39     7188   6648   3890    800   -658   -346       N  
ATOM   1372  N   ARG B  40      15.836  -3.818  48.842  1.00 45.60           N  
ANISOU 1372  N   ARG B  40     7010   6550   3767    764   -669   -245       N  
ATOM   1373  CA  ARG B  40      17.107  -4.477  49.065  1.00 45.92           C  
ANISOU 1373  CA  ARG B  40     7042   6606   3801    748   -673   -222       C  
ATOM   1374  C   ARG B  40      18.319  -3.698  48.543  1.00 46.86           C  
ANISOU 1374  C   ARG B  40     7162   6726   3917    735   -686   -209       C  
ATOM   1375  O   ARG B  40      19.400  -3.739  49.134  1.00 48.06           O  
ANISOU 1375  O   ARG B  40     7310   6893   4057    715   -695   -193       O  
ATOM   1376  CB  ARG B  40      17.038  -5.850  48.398  1.00 44.29           C  
ANISOU 1376  CB  ARG B  40     6822   6399   3607    762   -660   -213       C  
ATOM   1377  CG  ARG B  40      18.144  -6.769  48.731  1.00 44.62           C  
ANISOU 1377  CG  ARG B  40     6853   6456   3643    748   -661   -189       C  
ATOM   1378  CD  ARG B  40      17.635  -8.171  48.656  1.00 43.56           C  
ANISOU 1378  CD  ARG B  40     6709   6323   3517    761   -646   -187       C  
ATOM   1379  NE  ARG B  40      17.182  -8.526  47.328  1.00 42.12           N  
ANISOU 1379  NE  ARG B  40     6522   6127   3354    782   -636   -192       N  
ATOM   1380  CZ  ARG B  40      16.246  -9.439  47.127  1.00 41.43           C  
ANISOU 1380  CZ  ARG B  40     6429   6036   3276    799   -622   -200       C  
ATOM   1381  NH1 ARG B  40      15.688 -10.029  48.185  1.00 42.06           N  
ANISOU 1381  NH1 ARG B  40     6509   6123   3348    798   -616   -204       N  
ATOM   1382  NH2 ARG B  40      15.849  -9.746  45.895  1.00 40.45           N  
ANISOU 1382  NH2 ARG B  40     6301   5900   3170    817   -613   -205       N  
ATOM   1383  N   PHE B  41      18.117  -3.020  47.418  1.00 45.18           N  
ANISOU 1383  N   PHE B  41     6953   6497   3716    747   -687   -217       N  
ATOM   1384  CA  PHE B  41      19.152  -2.253  46.758  1.00 46.34           C  
ANISOU 1384  CA  PHE B  41     7102   6643   3863    738   -698   -207       C  
ATOM   1385  C   PHE B  41      19.347  -0.873  47.397  1.00 48.53           C  
ANISOU 1385  C   PHE B  41     7391   6921   4126    723   -711   -215       C  
ATOM   1386  O   PHE B  41      20.404  -0.276  47.292  1.00 50.29           O  
ANISOU 1386  O   PHE B  41     7615   7149   4343    709   -722   -203       O  
ATOM   1387  CB  PHE B  41      18.798  -2.109  45.280  1.00 45.38           C  
ANISOU 1387  CB  PHE B  41     6980   6504   3760    758   -693   -213       C  
ATOM   1388  CG  PHE B  41      19.106  -3.333  44.459  1.00 43.86           C  
ANISOU 1388  CG  PHE B  41     6773   6312   3580    767   -684   -200       C  
ATOM   1389  CD1 PHE B  41      18.826  -4.593  44.923  1.00 44.24           C  
ANISOU 1389  CD1 PHE B  41     6812   6368   3628    771   -673   -195       C  
ATOM   1390  CD2 PHE B  41      19.687  -3.226  43.196  1.00 42.41           C  
ANISOU 1390  CD2 PHE B  41     6586   6120   3408    773   -685   -192       C  
ATOM   1391  CE1 PHE B  41      19.120  -5.688  44.152  1.00 43.17           C  
ANISOU 1391  CE1 PHE B  41     6665   6233   3505    779   -664   -183       C  
ATOM   1392  CE2 PHE B  41      19.974  -4.364  42.429  1.00 41.36           C  
ANISOU 1392  CE2 PHE B  41     6440   5988   3286    781   -676   -180       C  
ATOM   1393  CZ  PHE B  41      19.688  -5.562  42.902  1.00 41.73           C  
ANISOU 1393  CZ  PHE B  41     6478   6043   3333    784   -666   -176       C  
ATOM   1394  N   PHE B  42      18.280  -0.339  47.980  1.00 45.34           N  
ANISOU 1394  N   PHE B  42     6997   6512   3719    729   -709   -234       N  
ATOM   1395  CA  PHE B  42      18.253   1.017  48.513  1.00 46.20           C  
ANISOU 1395  CA  PHE B  42     7119   6619   3817    718   -720   -245       C  
ATOM   1396  C   PHE B  42      18.329   1.165  50.043  1.00 47.91           C  
ANISOU 1396  C   PHE B  42     7340   6851   4014    700   -726   -246       C  
ATOM   1397  O   PHE B  42      18.236   2.287  50.534  1.00 49.93           O  
ANISOU 1397  O   PHE B  42     7606   7105   4259    691   -734   -256       O  
ATOM   1398  CB  PHE B  42      16.992   1.745  48.010  1.00 46.22           C  
ANISOU 1398  CB  PHE B  42     7132   6602   3828    737   -716   -268       C  
ATOM   1399  CG  PHE B  42      16.900   1.863  46.512  1.00 45.74           C  
ANISOU 1399  CG  PHE B  42     7069   6525   3784    755   -712   -269       C  
ATOM   1400  CD1 PHE B  42      17.638   2.795  45.825  1.00 46.03           C  
ANISOU 1400  CD1 PHE B  42     7111   6557   3823    750   -721   -265       C  
ATOM   1401  CD2 PHE B  42      16.046   1.060  45.790  1.00 44.99           C  
ANISOU 1401  CD2 PHE B  42     6968   6421   3705    777   -699   -275       C  
ATOM   1402  CE1 PHE B  42      17.543   2.921  44.435  1.00 45.59           C  
ANISOU 1402  CE1 PHE B  42     7054   6486   3782    766   -718   -266       C  
ATOM   1403  CE2 PHE B  42      15.958   1.186  44.405  1.00 44.56           C  
ANISOU 1403  CE2 PHE B  42     6911   6352   3666    793   -696   -276       C  
ATOM   1404  CZ  PHE B  42      16.718   2.124  43.738  1.00 44.86           C  
ANISOU 1404  CZ  PHE B  42     6955   6385   3705    788   -705   -271       C  
ATOM   1405  N   GLU B  43      18.451   0.096  50.819  1.00 46.92           N  
ANISOU 1405  N   GLU B  43     7205   6739   3882    694   -721   -236       N  
ATOM   1406  CA  GLU B  43      18.269   0.273  52.266  1.00 49.01           C  
ANISOU 1406  CA  GLU B  43     7474   7017   4129    679   -725   -241       C  
ATOM   1407  C   GLU B  43      19.294   1.189  52.915  1.00 51.98           C  
ANISOU 1407  C   GLU B  43     7855   7405   4489    655   -740   -234       C  
ATOM   1408  O   GLU B  43      19.180   1.515  54.092  1.00 54.34           O  
ANISOU 1408  O   GLU B  43     8159   7714   4772    642   -744   -239       O  
ATOM   1409  CB  GLU B  43      18.304  -1.052  52.983  1.00 48.20           C  
ANISOU 1409  CB  GLU B  43     7362   6929   4024    677   -717   -231       C  
ATOM   1410  CG  GLU B  43      16.993  -1.783  53.004  1.00 45.58           C  
ANISOU 1410  CG  GLU B  43     7029   6589   3701    697   -703   -244       C  
ATOM   1411  CD  GLU B  43      17.203  -3.279  53.148  1.00 44.91           C  
ANISOU 1411  CD  GLU B  43     6931   6514   3619    699   -694   -229       C  
ATOM   1412  OE1 GLU B  43      18.216  -3.695  53.807  1.00 45.17           O  
ANISOU 1412  OE1 GLU B  43     6959   6564   3640    681   -699   -211       O  
ATOM   1413  OE2 GLU B  43      16.360  -4.023  52.580  1.00 44.44           O  
ANISOU 1413  OE2 GLU B  43     6867   6444   3573    719   -681   -236       O  
ATOM   1414  N   SER B  44      20.302   1.577  52.139  1.00 48.88           N  
ANISOU 1414  N   SER B  44     7461   7013   4100    649   -748   -222       N  
ATOM   1415  CA  SER B  44      21.277   2.601  52.513  1.00 52.02           C  
ANISOU 1415  CA  SER B  44     7863   7419   4483    627   -762   -217       C  
ATOM   1416  C   SER B  44      20.636   3.962  52.757  1.00 54.03           C  
ANISOU 1416  C   SER B  44     8133   7664   4732    627   -767   -237       C  
ATOM   1417  O   SER B  44      21.274   4.859  53.326  1.00 57.11           O  
ANISOU 1417  O   SER B  44     8528   8062   5108    609   -779   -236       O  
ATOM   1418  CB  SER B  44      22.337   2.748  51.412  1.00 51.84           C  
ANISOU 1418  CB  SER B  44     7836   7394   4468    625   -768   -201       C  
ATOM   1419  OG  SER B  44      21.801   3.207  50.171  1.00 49.72           O  
ANISOU 1419  OG  SER B  44     7573   7104   4216    644   -764   -212       O  
ATOM   1420  N   PHE B  45      19.388   4.121  52.301  1.00 52.80           N  
ANISOU 1420  N   PHE B  45     7984   7490   4589    648   -759   -256       N  
ATOM   1421  CA  PHE B  45      18.678   5.399  52.389  1.00 54.43           C  
ANISOU 1421  CA  PHE B  45     8204   7684   4792    652   -762   -277       C  
ATOM   1422  C   PHE B  45      18.367   5.784  53.809  1.00 57.09           C  
ANISOU 1422  C   PHE B  45     8547   8032   5112    638   -766   -286       C  
ATOM   1423  O   PHE B  45      18.537   6.932  54.189  1.00 59.76           O  
ANISOU 1423  O   PHE B  45     8896   8371   5440    626   -775   -294       O  
ATOM   1424  CB  PHE B  45      17.373   5.363  51.612  1.00 51.88           C  
ANISOU 1424  CB  PHE B  45     7886   7341   4486    678   -751   -293       C  
ATOM   1425  CG  PHE B  45      17.551   5.487  50.143  1.00 50.19           C  
ANISOU 1425  CG  PHE B  45     7670   7112   4288    692   -749   -290       C  
ATOM   1426  CD1 PHE B  45      16.451   5.515  49.302  1.00 48.15           C  
ANISOU 1426  CD1 PHE B  45     7415   6835   4046    716   -740   -304       C  
ATOM   1427  CD2 PHE B  45      18.824   5.563  49.593  1.00 50.99           C  
ANISOU 1427  CD2 PHE B  45     7766   7219   4389    681   -757   -273       C  
ATOM   1428  CE1 PHE B  45      16.616   5.641  47.944  1.00 47.03           C  
ANISOU 1428  CE1 PHE B  45     7271   6680   3918    729   -739   -301       C  
ATOM   1429  CE2 PHE B  45      18.998   5.677  48.229  1.00 49.94           C  
ANISOU 1429  CE2 PHE B  45     7631   7072   4271    694   -755   -269       C  
ATOM   1430  CZ  PHE B  45      17.903   5.725  47.405  1.00 48.00           C  
ANISOU 1430  CZ  PHE B  45     7389   6808   4040    718   -746   -284       C  
ATOM   1431  N   GLY B  46      17.867   4.832  54.584  1.00 55.10           N  
ANISOU 1431  N   GLY B  46     8290   7788   4856    639   -759   -286       N  
ATOM   1432  CA  GLY B  46      17.387   5.137  55.916  1.00 57.45           C  
ANISOU 1432  CA  GLY B  46     8594   8096   5140    629   -761   -297       C  
ATOM   1433  C   GLY B  46      16.276   4.151  56.145  1.00 55.29           C  
ANISOU 1433  C   GLY B  46     8317   7818   4873    645   -747   -304       C  
ATOM   1434  O   GLY B  46      16.308   3.083  55.546  1.00 52.08           O  
ANISOU 1434  O   GLY B  46     7900   7410   4478    656   -739   -294       O  
ATOM   1435  N   ASP B  47      15.293   4.496  56.981  1.00 57.34           N  
ANISOU 1435  N   ASP B  47     8585   8076   5127    647   -745   -322       N  
ATOM   1436  CA  ASP B  47      14.136   3.613  57.174  1.00 56.20           C  
ANISOU 1436  CA  ASP B  47     8437   7926   4990    664   -732   -330       C  
ATOM   1437  C   ASP B  47      13.281   3.540  55.907  1.00 53.21           C  
ANISOU 1437  C   ASP B  47     8059   7527   4633    690   -723   -340       C  
ATOM   1438  O   ASP B  47      12.777   4.548  55.422  1.00 53.21           O  
ANISOU 1438  O   ASP B  47     8069   7511   4637    698   -725   -354       O  
ATOM   1439  CB  ASP B  47      13.279   4.099  58.348  1.00 59.62           C  
ANISOU 1439  CB  ASP B  47     8879   8362   5412    660   -732   -347       C  
ATOM   1440  CG  ASP B  47      12.026   3.252  58.547  1.00 59.25           C  
ANISOU 1440  CG  ASP B  47     8830   8309   5373    677   -719   -358       C  
ATOM   1441  OD1 ASP B  47      11.971   2.131  58.001  1.00 60.30           O  
ANISOU 1441  OD1 ASP B  47     8952   8441   5517    689   -709   -349       O  
ATOM   1442  OD2 ASP B  47      11.102   3.712  59.259  1.00 58.12           O  
ANISOU 1442  OD2 ASP B  47     8695   8162   5225    679   -717   -375       O  
ATOM   1443  N   LEU B  48      13.170   2.342  55.358  1.00 52.40           N  
ANISOU 1443  N   LEU B  48     7946   7423   4542    702   -712   -332       N  
ATOM   1444  CA  LEU B  48      12.271   2.076  54.246  1.00 51.46           C  
ANISOU 1444  CA  LEU B  48     7825   7286   4442    728   -702   -341       C  
ATOM   1445  C   LEU B  48      10.988   1.264  54.585  1.00 51.07           C  
ANISOU 1445  C   LEU B  48     7774   7233   4399    743   -689   -353       C  
ATOM   1446  O   LEU B  48      10.333   0.742  53.681  1.00 50.45           O  
ANISOU 1446  O   LEU B  48     7690   7143   4336    764   -679   -357       O  
ATOM   1447  CB  LEU B  48      13.053   1.414  53.128  1.00 50.86           C  
ANISOU 1447  CB  LEU B  48     7739   7209   4377    733   -700   -324       C  
ATOM   1448  CG  LEU B  48      13.938   2.449  52.459  1.00 51.16           C  
ANISOU 1448  CG  LEU B  48     7782   7243   4415    725   -711   -319       C  
ATOM   1449  CD1 LEU B  48      14.754   1.804  51.358  1.00 50.59           C  
ANISOU 1449  CD1 LEU B  48     7699   7169   4353    729   -709   -302       C  
ATOM   1450  CD2 LEU B  48      13.067   3.564  51.912  1.00 51.36           C  
ANISOU 1450  CD2 LEU B  48     7819   7248   4446    738   -712   -339       C  
ATOM   1451  N   SER B  49      10.686   1.078  55.868  1.00 54.70           N  
ANISOU 1451  N   SER B  49     8235   7704   4846    734   -689   -357       N  
ATOM   1452  CA  SER B  49       9.653   0.122  56.300  1.00 55.02           C  
ANISOU 1452  CA  SER B  49     8271   7744   4890    746   -676   -364       C  
ATOM   1453  C   SER B  49       8.204   0.550  56.018  1.00 54.47           C  
ANISOU 1453  C   SER B  49     8208   7657   4830    766   -669   -386       C  
ATOM   1454  O   SER B  49       7.446  -0.184  55.360  1.00 52.58           O  
ANISOU 1454  O   SER B  49     7963   7409   4605    786   -658   -391       O  
ATOM   1455  CB  SER B  49       9.799  -0.157  57.798  1.00 58.70           C  
ANISOU 1455  CB  SER B  49     8737   8228   5339    729   -678   -361       C  
ATOM   1456  OG  SER B  49       9.523   1.016  58.558  1.00 61.26           O  
ANISOU 1456  OG  SER B  49     9074   8552   5651    719   -687   -374       O  
ATOM   1457  N   THR B  50       7.803   1.684  56.595  1.00 51.54           N  
ANISOU 1457  N   THR B  50     7850   7283   4451    760   -676   -400       N  
ATOM   1458  CA  THR B  50       6.477   2.269  56.386  1.00 51.68           C  
ANISOU 1458  CA  THR B  50     7875   7284   4476    777   -671   -421       C  
ATOM   1459  C   THR B  50       6.447   3.002  55.049  1.00 49.62           C  
ANISOU 1459  C   THR B  50     7618   7007   4229    789   -673   -425       C  
ATOM   1460  O   THR B  50       7.499   3.333  54.511  1.00 49.63           O  
ANISOU 1460  O   THR B  50     7619   7009   4229    781   -681   -414       O  
ATOM   1461  CB  THR B  50       6.132   3.242  57.505  1.00 55.56           C  
ANISOU 1461  CB  THR B  50     8379   7779   4954    765   -678   -434       C  
ATOM   1462  OG1 THR B  50       6.090   4.573  56.974  1.00 56.00           O  
ANISOU 1462  OG1 THR B  50     8446   7822   5011    766   -685   -443       O  
ATOM   1463  CG2 THR B  50       7.180   3.165  58.620  1.00 58.23           C  
ANISOU 1463  CG2 THR B  50     8715   8137   5272    739   -687   -421       C  
ATOM   1464  N   PRO B  51       5.251   3.248  54.488  1.00 52.74           N  
ANISOU 1464  N   PRO B  51     8017   7386   4636    810   -666   -441       N  
ATOM   1465  CA  PRO B  51       5.190   4.051  53.253  1.00 50.64           C  
ANISOU 1465  CA  PRO B  51     7756   7104   4381    822   -668   -446       C  
ATOM   1466  C   PRO B  51       5.506   5.555  53.509  1.00 51.91           C  
ANISOU 1466  C   PRO B  51     7931   7261   4532    810   -681   -452       C  
ATOM   1467  O   PRO B  51       6.011   6.268  52.619  1.00 50.64           O  
ANISOU 1467  O   PRO B  51     7774   7092   4376    811   -686   -449       O  
ATOM   1468  CB  PRO B  51       3.755   3.858  52.797  1.00 50.20           C  
ANISOU 1468  CB  PRO B  51     7700   7034   4339    846   -658   -462       C  
ATOM   1469  CG  PRO B  51       3.013   3.714  54.092  1.00 51.59           C  
ANISOU 1469  CG  PRO B  51     7879   7217   4505    841   -655   -472       C  
ATOM   1470  CD  PRO B  51       3.906   2.884  54.964  1.00 53.98           C  
ANISOU 1470  CD  PRO B  51     8175   7539   4797    823   -656   -456       C  
ATOM   1471  N   ASP B  52       5.228   6.036  54.722  1.00 50.34           N  
ANISOU 1471  N   ASP B  52     7740   7068   4319    798   -685   -461       N  
ATOM   1472  CA  ASP B  52       5.486   7.438  55.028  1.00 51.97           C  
ANISOU 1472  CA  ASP B  52     7959   7271   4515    786   -696   -468       C  
ATOM   1473  C   ASP B  52       6.974   7.712  55.127  1.00 52.32           C  
ANISOU 1473  C   ASP B  52     8003   7328   4549    764   -707   -452       C  
ATOM   1474  O   ASP B  52       7.461   8.732  54.629  1.00 52.31           O  
ANISOU 1474  O   ASP B  52     8009   7319   4547    760   -715   -452       O  
ATOM   1475  CB  ASP B  52       4.781   7.849  56.312  1.00 55.34           C  
ANISOU 1475  CB  ASP B  52     8395   7703   4930    778   -697   -481       C  
ATOM   1476  CG  ASP B  52       3.295   8.056  56.100  1.00 55.41           C  
ANISOU 1476  CG  ASP B  52     8408   7696   4949    799   -689   -500       C  
ATOM   1477  OD1 ASP B  52       2.876   8.181  54.911  1.00 53.04           O  
ANISOU 1477  OD1 ASP B  52     8107   7381   4664    818   -684   -504       O  
ATOM   1478  OD2 ASP B  52       2.557   8.097  57.115  1.00 58.08           O  
ANISOU 1478  OD2 ASP B  52     8751   8038   5280    797   -687   -511       O  
ATOM   1479  N   ALA B  53       7.693   6.799  55.767  1.00 51.29           N  
ANISOU 1479  N   ALA B  53     7863   7215   4411    751   -707   -437       N  
ATOM   1480  CA  ALA B  53       9.137   6.907  55.850  1.00 51.57           C  
ANISOU 1480  CA  ALA B  53     7896   7263   4437    731   -717   -420       C  
ATOM   1481  C   ALA B  53       9.711   6.932  54.454  1.00 48.57           C  
ANISOU 1481  C   ALA B  53     7512   6874   4070    740   -718   -411       C  
ATOM   1482  O   ALA B  53      10.458   7.827  54.117  1.00 48.81           O  
ANISOU 1482  O   ALA B  53     7547   6902   4096    730   -727   -407       O  
ATOM   1483  CB  ALA B  53       9.720   5.771  56.645  1.00 52.72           C  
ANISOU 1483  CB  ALA B  53     8030   7428   4573    718   -715   -405       C  
ATOM   1484  N   VAL B  54       9.348   5.962  53.637  1.00 48.63           N  
ANISOU 1484  N   VAL B  54     7510   6876   4092    757   -707   -407       N  
ATOM   1485  CA  VAL B  54       9.837   5.922  52.265  1.00 48.39           C  
ANISOU 1485  CA  VAL B  54     7475   6836   4075    767   -707   -399       C  
ATOM   1486  C   VAL B  54       9.547   7.214  51.526  1.00 48.38           C  
ANISOU 1486  C   VAL B  54     7486   6818   4079    775   -712   -410       C  
ATOM   1487  O   VAL B  54      10.441   7.834  50.955  1.00 48.36           O  
ANISOU 1487  O   VAL B  54     7485   6814   4076    768   -720   -402       O  
ATOM   1488  CB  VAL B  54       9.202   4.765  51.457  1.00 48.11           C  
ANISOU 1488  CB  VAL B  54     7429   6794   4057    789   -694   -398       C  
ATOM   1489  CG1 VAL B  54       9.608   4.849  49.984  1.00 47.86           C  
ANISOU 1489  CG1 VAL B  54     7394   6752   4039    800   -694   -391       C  
ATOM   1490  CG2 VAL B  54       9.598   3.445  52.046  1.00 48.09           C  
ANISOU 1490  CG2 VAL B  54     7414   6807   4050    781   -689   -384       C  
ATOM   1491  N   MET B  55       8.280   7.612  51.538  1.00 47.02           N  
ANISOU 1491  N   MET B  55     7321   6634   3912    790   -706   -429       N  
ATOM   1492  CA  MET B  55       7.873   8.794  50.806  1.00 47.03           C  
ANISOU 1492  CA  MET B  55     7333   6618   3919    800   -709   -440       C  
ATOM   1493  C   MET B  55       8.557  10.067  51.365  1.00 47.23           C  
ANISOU 1493  C   MET B  55     7369   6646   3929    780   -722   -442       C  
ATOM   1494  O   MET B  55       8.914  10.986  50.614  1.00 47.23           O  
ANISOU 1494  O   MET B  55     7377   6637   3932    782   -728   -442       O  
ATOM   1495  CB  MET B  55       6.363   8.923  50.840  1.00 47.01           C  
ANISOU 1495  CB  MET B  55     7335   6604   3924    819   -701   -460       C  
ATOM   1496  CG  MET B  55       5.607   7.855  50.095  1.00 46.82           C  
ANISOU 1496  CG  MET B  55     7301   6573   3916    841   -688   -460       C  
ATOM   1497  SD  MET B  55       6.079   7.457  48.395  1.00 46.61           S  
ANISOU 1497  SD  MET B  55     7265   6538   3907    856   -685   -449       S  
ATOM   1498  CE  MET B  55       6.566   9.002  47.638  1.00 46.68           C  
ANISOU 1498  CE  MET B  55     7286   6534   3915    854   -696   -452       C  
ATOM   1499  N   GLY B  56       8.748  10.083  52.686  1.00 49.89           N  
ANISOU 1499  N   GLY B  56     7709   6997   4250    762   -727   -442       N  
ATOM   1500  CA  GLY B  56       9.401  11.171  53.379  1.00 52.71           C  
ANISOU 1500  CA  GLY B  56     8075   7360   4591    741   -738   -444       C  
ATOM   1501  C   GLY B  56      10.913  11.204  53.269  1.00 53.04           C  
ANISOU 1501  C   GLY B  56     8113   7415   4626    722   -748   -425       C  
ATOM   1502  O   GLY B  56      11.489  12.296  53.174  1.00 55.18           O  
ANISOU 1502  O   GLY B  56     8393   7683   4890    712   -757   -426       O  
ATOM   1503  N   ASN B  57      11.554  10.031  53.275  1.00 56.45           N  
ANISOU 1503  N   ASN B  57     8531   7859   5059    718   -745   -408       N  
ATOM   1504  CA  ASN B  57      13.010   9.946  53.382  1.00 56.97           C  
ANISOU 1504  CA  ASN B  57     8591   7939   5115    698   -754   -390       C  
ATOM   1505  C   ASN B  57      13.704  10.769  52.296  1.00 57.10           C  
ANISOU 1505  C   ASN B  57     8612   7946   5138    698   -761   -385       C  
ATOM   1506  O   ASN B  57      13.558  10.458  51.098  1.00 55.10           O  
ANISOU 1506  O   ASN B  57     8354   7680   4900    716   -755   -382       O  
ATOM   1507  CB  ASN B  57      13.487   8.495  53.292  1.00 54.87           C  
ANISOU 1507  CB  ASN B  57     8310   7685   4853    698   -749   -372       C  
ATOM   1508  CG  ASN B  57      15.002   8.389  53.281  1.00 55.06           C  
ANISOU 1508  CG  ASN B  57     8328   7724   4870    678   -758   -352       C  
ATOM   1509  OD1 ASN B  57      15.656   8.724  52.279  1.00 54.26           O  
ANISOU 1509  OD1 ASN B  57     8225   7616   4775    680   -762   -344       O  
ATOM   1510  ND2 ASN B  57      15.580   7.960  54.417  1.00 56.47           N  
ANISOU 1510  ND2 ASN B  57     8501   7922   5033    659   -762   -342       N  
ATOM   1511  N   PRO B  58      14.478  11.808  52.716  1.00 58.80           N  
ANISOU 1511  N   PRO B  58     7105   4216  11022   1084    695   1015       N  
ATOM   1512  CA  PRO B  58      15.037  12.816  51.800  1.00 58.90           C  
ANISOU 1512  CA  PRO B  58     7081   4245  11055   1068    717   1020       C  
ATOM   1513  C   PRO B  58      15.982  12.230  50.778  1.00 58.81           C  
ANISOU 1513  C   PRO B  58     7034   4282  11031   1060    677    993       C  
ATOM   1514  O   PRO B  58      16.202  12.878  49.764  1.00 58.86           O  
ANISOU 1514  O   PRO B  58     7002   4308  11053   1048    693   1009       O  
ATOM   1515  CB  PRO B  58      15.783  13.784  52.730  1.00 59.09           C  
ANISOU 1515  CB  PRO B  58     7129   4235  11086   1061    738    985       C  
ATOM   1516  CG  PRO B  58      15.156  13.623  54.051  1.00 59.11           C  
ANISOU 1516  CG  PRO B  58     7179   4196  11083   1074    747    985       C  
ATOM   1517  CD  PRO B  58      14.760  12.149  54.126  1.00 58.92           C  
ANISOU 1517  CD  PRO B  58     7165   4189  11033   1087    704    984       C  
ATOM   1518  N   LYS B  59      16.533  11.041  51.025  1.00 58.70           N  
ANISOU 1518  N   LYS B  59     7029   4285  10988   1067    625    953       N  
ATOM   1519  CA  LYS B  59      17.462  10.474  50.050  1.00 58.61           C  
ANISOU 1519  CA  LYS B  59     6984   4320  10966   1060    586    926       C  
ATOM   1520  C   LYS B  59      16.695   9.822  48.925  1.00 58.46           C  
ANISOU 1520  C   LYS B  59     6932   4335  10946   1063    577    969       C  
ATOM   1521  O   LYS B  59      17.258   9.589  47.850  1.00 58.40           O  
ANISOU 1521  O   LYS B  59     6887   4368  10936   1055    556    962       O  
ATOM   1522  CB  LYS B  59      18.410   9.476  50.687  1.00 58.55           C  
ANISOU 1522  CB  LYS B  59     6997   4320  10929   1065    534    866       C  
ATOM   1523  CG  LYS B  59      19.478  10.098  51.527  1.00 58.69           C  
ANISOU 1523  CG  LYS B  59     7037   4316  10946   1059    536    815       C  
ATOM   1524  CD  LYS B  59      20.153   9.054  52.344  1.00 58.62           C  
ANISOU 1524  CD  LYS B  59     7057   4308  10909   1067    487    763       C  
ATOM   1525  CE  LYS B  59      20.891   9.630  53.525  1.00 58.76           C  
ANISOU 1525  CE  LYS B  59     7110   4292  10926   1065    495    719       C  
ATOM   1526  NZ  LYS B  59      21.526   8.545  54.327  1.00 58.69           N  
ANISOU 1526  NZ  LYS B  59     7129   4283  10888   1074    446    668       N  
ATOM   1527  N   VAL B  60      15.408   9.548  49.172  1.00 58.40           N  
ANISOU 1527  N   VAL B  60     6938   4310  10941   1074    593   1013       N  
ATOM   1528  CA  VAL B  60      14.556   8.916  48.167  1.00 58.25           C  
ANISOU 1528  CA  VAL B  60     6891   4321  10922   1078    586   1058       C  
ATOM   1529  C   VAL B  60      14.193   9.866  47.035  1.00 58.31           C  
ANISOU 1529  C   VAL B  60     6858   4342  10956   1066    624   1103       C  
ATOM   1530  O   VAL B  60      14.360   9.515  45.860  1.00 58.23           O  
ANISOU 1530  O   VAL B  60     6808   4372  10944   1060    607   1112       O  
ATOM   1531  CB  VAL B  60      13.273   8.383  48.747  1.00 58.18           C  
ANISOU 1531  CB  VAL B  60     6907   4289  10908   1093    594   1093       C  
ATOM   1532  CG1 VAL B  60      12.593   7.556  47.702  1.00 58.01           C  
ANISOU 1532  CG1 VAL B  60     6856   4303  10882   1097    577   1129       C  
ATOM   1533  CG2 VAL B  60      13.561   7.562  49.952  1.00 58.14           C  
ANISOU 1533  CG2 VAL B  60     6945   4266  10879   1104    562   1052       C  
ATOM   1534  N   LYS B  61      13.701  11.061  47.361  1.00 58.46           N  
ANISOU 1534  N   LYS B  61     6885   4327  10999   1062    675   1131       N  
ATOM   1535  CA  LYS B  61      13.310  11.952  46.281  1.00 58.51           C  
ANISOU 1535  CA  LYS B  61     6854   4346  11031   1052    711   1176       C  
ATOM   1536  C   LYS B  61      14.563  12.477  45.639  1.00 58.59           C  
ANISOU 1536  C   LYS B  61     6835   4380  11045   1036    704   1142       C  
ATOM   1537  O   LYS B  61      14.593  12.763  44.429  1.00 58.57           O  
ANISOU 1537  O   LYS B  61     6791   4409  11055   1026    711   1165       O  
ATOM   1538  CB  LYS B  61      12.428  13.101  46.760  1.00 58.65           C  
ANISOU 1538  CB  LYS B  61     6887   4322  11075   1051    769   1216       C  
ATOM   1539  CG  LYS B  61      12.793  13.695  48.103  1.00 58.79           C  
ANISOU 1539  CG  LYS B  61     6946   4297  11094   1053    785   1185       C  
ATOM   1540  CD  LYS B  61      11.843  14.849  48.458  1.00 58.92           C  
ANISOU 1540  CD  LYS B  61     6974   4275  11139   1053    843   1230       C  
ATOM   1541  CE  LYS B  61      10.395  14.377  48.724  1.00 58.83           C  
ANISOU 1541  CE  LYS B  61     6979   4247  11128   1066    856   1279       C  
ATOM   1542  NZ  LYS B  61      10.254  13.805  50.095  1.00 58.82           N  
ANISOU 1542  NZ  LYS B  61     7026   4214  11108   1080    842   1254       N  
ATOM   1543  N   ALA B  62      15.604  12.583  46.464  1.00 58.66           N  
ANISOU 1543  N   ALA B  62     6869   4376  11045   1034    688   1087       N  
ATOM   1544  CA  ALA B  62      16.914  13.043  46.016  1.00 58.74           C  
ANISOU 1544  CA  ALA B  62     6857   4406  11056   1020    678   1047       C  
ATOM   1545  C   ALA B  62      17.365  12.108  44.929  1.00 58.59           C  
ANISOU 1545  C   ALA B  62     6803   4438  11022   1017    635   1037       C  
ATOM   1546  O   ALA B  62      17.884  12.537  43.892  1.00 58.62           O  
ANISOU 1546  O   ALA B  62     6768   4470  11035   1004    638   1038       O  
ATOM   1547  CB  ALA B  62      17.906  13.064  47.163  1.00 58.82           C  
ANISOU 1547  CB  ALA B  62     6902   4393  11053   1021    661    987       C  
ATOM   1548  N   HIS B  63      17.139  10.819  45.186  1.00 58.44           N  
ANISOU 1548  N   HIS B  63     6797   4428  10979   1030    596   1026       N  
ATOM   1549  CA  HIS B  63      17.457   9.773  44.236  1.00 58.28           C  
ANISOU 1549  CA  HIS B  63     6747   4455  10942   1029    552   1017       C  
ATOM   1550  C   HIS B  63      16.502   9.791  43.052  1.00 58.21           C  
ANISOU 1550  C   HIS B  63     6702   4469  10946   1027    569   1076       C  
ATOM   1551  O   HIS B  63      16.935   9.807  41.907  1.00 58.18           O  
ANISOU 1551  O   HIS B  63     6657   4503  10945   1017    560   1079       O  
ATOM   1552  CB  HIS B  63      17.426   8.402  44.903  1.00 58.14           C  
ANISOU 1552  CB  HIS B  63     6757   4439  10895   1044    507    991       C  
ATOM   1553  CG  HIS B  63      18.056   7.330  44.073  1.00 58.00           C  
ANISOU 1553  CG  HIS B  63     6711   4468  10857   1043    457    967       C  
ATOM   1554  ND1 HIS B  63      18.949   6.415  44.585  1.00 57.94           N  
ANISOU 1554  ND1 HIS B  63     6720   4469  10824   1047    409    911       N  
ATOM   1555  CD2 HIS B  63      17.940   7.049  42.755  1.00 57.91           C  
ANISOU 1555  CD2 HIS B  63     6657   4498  10848   1037    447    990       C  
ATOM   1556  CE1 HIS B  63      19.349   5.612  43.615  1.00 57.81           C  
ANISOU 1556  CE1 HIS B  63     6673   4498  10796   1045    372    901       C  
ATOM   1557  NE2 HIS B  63      18.752   5.977  42.494  1.00 57.79           N  
ANISOU 1557  NE2 HIS B  63     6633   4516  10810   1038    394    949       N  
ATOM   1558  N   GLY B  64      15.206   9.794  43.322  1.00 58.18           N  
ANISOU 1558  N   GLY B  64     6712   4444  10950   1037    595   1125       N  
ATOM   1559  CA  GLY B  64      14.233   9.799  42.249  1.00 58.11           C  
ANISOU 1559  CA  GLY B  64     6670   4455  10954   1036    612   1183       C  
ATOM   1560  C   GLY B  64      14.531  10.831  41.173  1.00 58.20           C  
ANISOU 1560  C   GLY B  64     6641   4485  10988   1019    640   1201       C  
ATOM   1561  O   GLY B  64      14.356  10.554  39.981  1.00 58.12           O  
ANISOU 1561  O   GLY B  64     6592   4511  10979   1015    632   1226       O  
ATOM   1562  N   LYS B  65      14.998  12.008  41.599  1.00 58.38           N  
ANISOU 1562  N   LYS B  65     6672   4482  11027   1011    672   1189       N  
ATOM   1563  CA  LYS B  65      15.274  13.107  40.689  1.00 58.49           C  
ANISOU 1563  CA  LYS B  65     6650   4508  11064    995    702   1207       C  
ATOM   1564  C   LYS B  65      16.221  12.640  39.604  1.00 58.42           C  
ANISOU 1564  C   LYS B  65     6603   4548  11045    985    666   1181       C  
ATOM   1565  O   LYS B  65      15.927  12.765  38.413  1.00 58.38           O  
ANISOU 1565  O   LYS B  65     6558   4573  11050    978    674   1215       O  
ATOM   1566  CB  LYS B  65      15.865  14.295  41.446  1.00 58.68           C  
ANISOU 1566  CB  LYS B  65     6694   4498  11103    988    732   1184       C  
ATOM   1567  CG  LYS B  65      15.747  15.641  40.713  1.00 58.81           C  
ANISOU 1567  CG  LYS B  65     6682   4514  11151    973    779   1218       C  
ATOM   1568  CD  LYS B  65      15.889  16.833  41.679  1.00 59.00           C  
ANISOU 1568  CD  LYS B  65     6734   4493  11192    970    819   1209       C  
ATOM   1569  CE  LYS B  65      16.389  18.075  40.944  1.00 59.15           C  
ANISOU 1569  CE  LYS B  65     6721   4518  11234    953    850   1217       C  
ATOM   1570  NZ  LYS B  65      16.679  19.217  41.849  1.00 59.33           N  
ANISOU 1570  NZ  LYS B  65     6770   4501  11273    949    885   1203       N  
ATOM   1571  N   LYS B  66      17.347  12.068  40.039  1.00 58.39           N  
ANISOU 1571  N   LYS B  66     6612   4554  11021    985    625   1121       N  
ATOM   1572  CA  LYS B  66      18.388  11.565  39.148  1.00 58.33           C  
ANISOU 1572  CA  LYS B  66     6572   4591  11000    977    587   1088       C  
ATOM   1573  C   LYS B  66      17.805  10.533  38.193  1.00 58.15           C  
ANISOU 1573  C   LYS B  66     6522   4606  10967    981    561   1115       C  
ATOM   1574  O   LYS B  66      18.177  10.499  37.012  1.00 58.11           O  
ANISOU 1574  O   LYS B  66     6476   4640  10964    971    551   1120       O  
ATOM   1575  CB  LYS B  66      19.530  10.978  39.959  1.00 58.32           C  
ANISOU 1575  CB  LYS B  66     6596   4588  10976    980    546   1020       C  
ATOM   1576  CG  LYS B  66      20.471  12.015  40.486  1.00 58.50           C  
ANISOU 1576  CG  LYS B  66     6629   4590  11008    970    564    985       C  
ATOM   1577  CD  LYS B  66      21.621  11.425  41.300  1.00 58.49           C  
ANISOU 1577  CD  LYS B  66     6653   4587  10984    973    523    917       C  
ATOM   1578  CE  LYS B  66      21.092  10.688  42.535  1.00 58.43           C  
ANISOU 1578  CE  LYS B  66     6692   4549  10961    989    510    909       C  
ATOM   1579  NZ  LYS B  66      22.176   9.927  43.251  1.00 58.40           N  
ANISOU 1579  NZ  LYS B  66     6711   4548  10932    993    464    844       N  
ATOM   1580  N   VAL B  67      16.864   9.725  38.708  1.00 58.04           N  
ANISOU 1580  N   VAL B  67     6532   4579  10942    997    553   1135       N  
ATOM   1581  CA  VAL B  67      16.181   8.686  37.935  1.00 57.87           C  
ANISOU 1581  CA  VAL B  67     6490   4588  10909   1003    530   1163       C  
ATOM   1582  C   VAL B  67      15.237   9.299  36.941  1.00 57.88           C  
ANISOU 1582  C   VAL B  67     6459   4598  10933    997    567   1227       C  
ATOM   1583  O   VAL B  67      15.160   8.880  35.787  1.00 57.78           O  
ANISOU 1583  O   VAL B  67     6409   4626  10919    993    552   1244       O  
ATOM   1584  CB  VAL B  67      15.357   7.757  38.808  1.00 57.76           C  
ANISOU 1584  CB  VAL B  67     6512   4555  10880   1021    515   1171       C  
ATOM   1585  CG1 VAL B  67      15.033   6.516  38.041  1.00 57.57           C  
ANISOU 1585  CG1 VAL B  67     6467   4568  10839   1027    478   1182       C  
ATOM   1586  CG2 VAL B  67      16.082   7.418  40.049  1.00 57.79           C  
ANISOU 1586  CG2 VAL B  67     6556   4535  10866   1028    492   1116       C  
ATOM   1587  N   LEU B  68      14.488  10.278  37.433  1.00 57.99           N  
ANISOU 1587  N   LEU B  68     6490   4575  10969    998    615   1261       N  
ATOM   1588  CA  LEU B  68      13.550  11.023  36.618  1.00 58.02           C  
ANISOU 1588  CA  LEU B  68     6467   4581  10998    993    657   1322       C  
ATOM   1589  C   LEU B  68      14.292  11.725  35.511  1.00 58.09           C  
ANISOU 1589  C   LEU B  68     6433   4620  11020    975    665   1320       C  
ATOM   1590  O   LEU B  68      13.835  11.757  34.357  1.00 58.04           O  
ANISOU 1590  O   LEU B  68     6389   4641  11023    969    672   1359       O  
ATOM   1591  CB  LEU B  68      12.789  12.036  37.468  1.00 58.16           C  
ANISOU 1591  CB  LEU B  68     6513   4549  11036    996    708   1351       C  
ATOM   1592  CG  LEU B  68      11.887  13.098  36.846  1.00 58.24           C  
ANISOU 1592  CG  LEU B  68     6502   4551  11077    989    760   1412       C  
ATOM   1593  CD1 LEU B  68      10.718  12.484  36.107  1.00 58.11           C  
ANISOU 1593  CD1 LEU B  68     6466   4552  11060    996    760   1465       C  
ATOM   1594  CD2 LEU B  68      11.439  13.932  38.005  1.00 58.38           C  
ANISOU 1594  CD2 LEU B  68     6557   4516  11108    994    799   1420       C  
ATOM   1595  N   GLY B  69      15.436  12.297  35.881  1.00 60.79           N  
ANISOU 1595  N   GLY B  69     6782   4954  11362    966    663   1274       N  
ATOM   1596  CA  GLY B  69      16.303  12.911  34.912  1.00 60.88           C  
ANISOU 1596  CA  GLY B  69     6755   4994  11384    949    665   1262       C  
ATOM   1597  C   GLY B  69      16.654  11.856  33.892  1.00 60.42           C  
ANISOU 1597  C   GLY B  69     6664   4986  11307    948    621   1252       C  
ATOM   1598  O   GLY B  69      16.428  12.044  32.696  1.00 61.22           O  
ANISOU 1598  O   GLY B  69     6725   5117  11419    939    629   1285       O  
ATOM   1599  N   ALA B  70      17.170  10.728  34.369  1.00 64.81           N  
ANISOU 1599  N   ALA B  70     7238   5551  11836    956    574   1209       N  
ATOM   1600  CA  ALA B  70      17.516   9.634  33.479  1.00 63.57           C  
ANISOU 1600  CA  ALA B  70     7052   5441  11660    956    529   1196       C  
ATOM   1601  C   ALA B  70      16.380   9.350  32.476  1.00 62.40           C  
ANISOU 1601  C   ALA B  70     6875   5314  11519    957    539   1256       C  
ATOM   1602  O   ALA B  70      16.636   9.132  31.292  1.00 63.99           O  
ANISOU 1602  O   ALA B  70     7037   5558  11720    948    525   1263       O  
ATOM   1603  CB  ALA B  70      17.849   8.397  34.277  1.00 60.56           C  
ANISOU 1603  CB  ALA B  70     6701   5059  11250    969    482   1153       C  
ATOM   1604  N   PHE B  71      15.127   9.397  32.932  1.00 63.00           N  
ANISOU 1604  N   PHE B  71     6972   5362  11603    968    566   1301       N  
ATOM   1605  CA  PHE B  71      13.989   9.263  32.011  1.00 62.45           C  
ANISOU 1605  CA  PHE B  71     6876   5310  11544    969    581   1362       C  
ATOM   1606  C   PHE B  71      13.851  10.478  31.071  1.00 66.07           C  
ANISOU 1606  C   PHE B  71     7299   5775  12030    954    623   1399       C  
ATOM   1607  O   PHE B  71      13.468  10.319  29.909  1.00 67.61           O  
ANISOU 1607  O   PHE B  71     7456   6003  12229    949    623   1433       O  
ATOM   1608  CB  PHE B  71      12.668   9.043  32.773  1.00 59.87           C  
ANISOU 1608  CB  PHE B  71     6580   4949  11218    985    601   1400       C  
ATOM   1609  CG  PHE B  71      12.342   7.589  33.037  1.00 58.59           C  
ANISOU 1609  CG  PHE B  71     6433   4798  11030   1000    558   1391       C  
ATOM   1610  CD1 PHE B  71      12.376   7.067  34.333  1.00 58.57           C  
ANISOU 1610  CD1 PHE B  71     6476   4766  11012   1013    542   1361       C  
ATOM   1611  CD2 PHE B  71      12.005   6.740  31.994  1.00 58.44           C  
ANISOU 1611  CD2 PHE B  71     6382   4819  11002   1000    534   1412       C  
ATOM   1612  CE1 PHE B  71      12.084   5.738  34.571  1.00 58.40           C  
ANISOU 1612  CE1 PHE B  71     6469   4755  10967   1026    503   1352       C  
ATOM   1613  CE2 PHE B  71      11.718   5.400  32.239  1.00 58.27           C  
ANISOU 1613  CE2 PHE B  71     6375   4808  10957   1014    495   1403       C  
ATOM   1614  CZ  PHE B  71      11.763   4.910  33.525  1.00 58.26           C  
ANISOU 1614  CZ  PHE B  71     6418   4777  10940   1027    480   1373       C  
ATOM   1615  N   SER B  72      14.152  11.683  31.552  1.00 67.40           N  
ANISOU 1615  N   SER B  72     7479   5914  12217    947    659   1393       N  
ATOM   1616  CA  SER B  72      14.061  12.870  30.687  1.00 67.67           C  
ANISOU 1616  CA  SER B  72     7480   5955  12278    932    699   1427       C  
ATOM   1617  C   SER B  72      14.974  12.714  29.466  1.00 67.40           C  
ANISOU 1617  C   SER B  72     7401   5969  12239    918    674   1409       C  
ATOM   1618  O   SER B  72      14.631  13.146  28.361  1.00 69.69           O  
ANISOU 1618  O   SER B  72     7654   6281  12544    908    693   1448       O  
ATOM   1619  CB  SER B  72      14.429  14.140  31.447  1.00 68.33           C  
ANISOU 1619  CB  SER B  72     7584   6000  12380    926    736   1415       C  
ATOM   1620  OG  SER B  72      13.671  14.273  32.624  1.00 68.60           O  
ANISOU 1620  OG  SER B  72     7660   5988  12417    938    757   1427       O  
ATOM   1621  N   ASP B  73      16.130  12.079  29.682  1.00 72.88           N  
ANISOU 1621  N   ASP B  73     8100   6679  12911    917    631   1349       N  
ATOM   1622  CA  ASP B  73      17.135  11.910  28.639  1.00 76.52           C  
ANISOU 1622  CA  ASP B  73     8522   7185  13366    904    604   1324       C  
ATOM   1623  C   ASP B  73      16.577  11.003  27.552  1.00 76.02           C  
ANISOU 1623  C   ASP B  73     8427   7162  13294    906    583   1354       C  
ATOM   1624  O   ASP B  73      16.945  11.112  26.375  1.00 79.63           O  
ANISOU 1624  O   ASP B  73     8842   7657  13755    893    577   1360       O  
ATOM   1625  CB  ASP B  73      18.428  11.329  29.227  1.00 76.49           C  
ANISOU 1625  CB  ASP B  73     8536   7188  13340    905    561   1253       C  
ATOM   1626  CG  ASP B  73      19.680  11.819  28.500  1.00 81.15           C  
ANISOU 1626  CG  ASP B  73     9094   7806  13932    888    552   1220       C  
ATOM   1627  OD1 ASP B  73      19.551  12.804  27.730  1.00 85.25           O  
ANISOU 1627  OD1 ASP B  73     9585   8331  14474    875    586   1251       O  
ATOM   1628  OD2 ASP B  73      20.784  11.239  28.708  1.00 80.85           O  
ANISOU 1628  OD2 ASP B  73     9061   7782  13875    887    512   1163       O  
ATOM   1629  N   GLY B  74      15.679  10.111  27.963  1.00 76.65           N  
ANISOU 1629  N   GLY B  74     8528   7234  13362    921    571   1372       N  
ATOM   1630  CA  GLY B  74      15.054   9.180  27.044  1.00 75.96           C  
ANISOU 1630  CA  GLY B  74     8414   7181  13265    925    550   1402       C  
ATOM   1631  C   GLY B  74      14.191   9.942  26.061  1.00 78.07           C  
ANISOU 1631  C   GLY B  74     8649   7457  13557    916    590   1464       C  
ATOM   1632  O   GLY B  74      14.364   9.823  24.848  1.00 81.06           O  
ANISOU 1632  O   GLY B  74     8986   7876  13937    906    581   1476       O  
ATOM   1633  N   LEU B  75      13.270  10.743  26.590  1.00 75.77           N  
ANISOU 1633  N   LEU B  75     8376   7127  13286    920    635   1504       N  
ATOM   1634  CA  LEU B  75      12.371  11.529  25.758  1.00 77.27           C  
ANISOU 1634  CA  LEU B  75     8539   7319  13501    913    677   1566       C  
ATOM   1635  C   LEU B  75      13.161  12.462  24.860  1.00 82.48           C  
ANISOU 1635  C   LEU B  75     9162   8000  14175    894    691   1561       C  
ATOM   1636  O   LEU B  75      12.702  12.822  23.773  1.00 84.34           O  
ANISOU 1636  O   LEU B  75     9361   8257  14426    885    710   1603       O  
ATOM   1637  CB  LEU B  75      11.400  12.325  26.626  1.00 75.18           C  
ANISOU 1637  CB  LEU B  75     8305   7005  13256    920    723   1601       C  
ATOM   1638  CG  LEU B  75      10.557  11.384  27.469  1.00 70.55           C  
ANISOU 1638  CG  LEU B  75     7754   6399  12654    939    710   1609       C  
ATOM   1639  CD1 LEU B  75       9.623  12.135  28.371  1.00 69.26           C  
ANISOU 1639  CD1 LEU B  75     7621   6185  12508    947    754   1641       C  
ATOM   1640  CD2 LEU B  75       9.796  10.458  26.534  1.00 70.10           C  
ANISOU 1640  CD2 LEU B  75     7671   6376  12589    944    691   1645       C  
ATOM   1641  N   ALA B  76      14.345  12.862  25.326  1.00 76.55           N  
ANISOU 1641  N   ALA B  76     8421   7242  13422    887    683   1509       N  
ATOM   1642  CA  ALA B  76      15.213  13.720  24.537  1.00 81.62           C  
ANISOU 1642  CA  ALA B  76     9031   7905  14077    869    693   1498       C  
ATOM   1643  C   ALA B  76      15.642  13.001  23.270  1.00 83.93           C  
ANISOU 1643  C   ALA B  76     9281   8251  14357    861    659   1492       C  
ATOM   1644  O   ALA B  76      15.368  13.459  22.166  1.00 87.51           O  
ANISOU 1644  O   ALA B  76     9696   8728  14826    850    677   1529       O  
ATOM   1645  CB  ALA B  76      16.419  14.149  25.347  1.00 83.25           C  
ANISOU 1645  CB  ALA B  76     9258   8093  14279    865    686   1439       C  
ATOM   1646  N   HIS B  77      16.319  11.871  23.418  1.00 82.49           N  
ANISOU 1646  N   HIS B  77    10316  11153   9875   1875    161   2011       N  
ATOM   1647  CA  HIS B  77      16.688  11.109  22.235  1.00 86.42           C  
ANISOU 1647  CA  HIS B  77    10816  11685  10335   1899    178   2018       C  
ATOM   1648  C   HIS B  77      16.061   9.711  22.242  1.00 82.22           C  
ANISOU 1648  C   HIS B  77    10312  11159   9770   1909    174   1982       C  
ATOM   1649  O   HIS B  77      16.599   8.785  22.847  1.00 79.00           O  
ANISOU 1649  O   HIS B  77     9916  10752   9350   1911    181   1958       O  
ATOM   1650  CB  HIS B  77      18.212  11.046  22.161  1.00 90.21           C  
ANISOU 1650  CB  HIS B  77    11283  12182  10812   1908    200   2035       C  
ATOM   1651  CG  HIS B  77      18.880  12.256  22.742  1.00 91.91           C  
ANISOU 1651  CG  HIS B  77    11476  12380  11067   1892    200   2060       C  
ATOM   1652  ND1 HIS B  77      19.147  12.386  24.089  1.00 87.55           N  
ANISOU 1652  ND1 HIS B  77    10926  11800  10540   1874    192   2043       N  
ATOM   1653  CD2 HIS B  77      19.302  13.407  22.165  1.00 97.62           C  
ANISOU 1653  CD2 HIS B  77    12173  13108  11809   1891    205   2099       C  
ATOM   1654  CE1 HIS B  77      19.720  13.555  24.314  1.00 90.54           C  
ANISOU 1654  CE1 HIS B  77    11282  12167  10951   1862    191   2071       C  
ATOM   1655  NE2 HIS B  77      19.824  14.194  23.163  1.00 96.57           N  
ANISOU 1655  NE2 HIS B  77    12028  12950  11713   1872    199   2106       N  
ATOM   1656  N   LEU B  78      14.970   9.554  21.491  1.00 89.69           N  
ANISOU 1656  N   LEU B  78    11267  12111  10701   1915    163   1979       N  
ATOM   1657  CA  LEU B  78      14.179   8.322  21.503  1.00 85.91           C  
ANISOU 1657  CA  LEU B  78    10814  11634  10195   1922    155   1944       C  
ATOM   1658  C   LEU B  78      14.618   7.370  20.404  1.00 88.97           C  
ANISOU 1658  C   LEU B  78    11209  12055  10541   1948    170   1945       C  
ATOM   1659  O   LEU B  78      14.210   6.209  20.367  1.00 86.08           O  
ANISOU 1659  O   LEU B  78    10864  11693  10148   1957    166   1916       O  
ATOM   1660  CB  LEU B  78      12.687   8.640  21.343  1.00 84.44           C  
ANISOU 1660  CB  LEU B  78    10635  11434  10016   1914    133   1939       C  
ATOM   1661  CG  LEU B  78      11.917   9.409  22.429  1.00 80.56           C  
ANISOU 1661  CG  LEU B  78    10142  10908   9561   1889    114   1931       C  
ATOM   1662  CD1 LEU B  78      10.539   9.819  21.922  1.00 79.98           C  
ANISOU 1662  CD1 LEU B  78    10071  10828   9490   1886     96   1934       C  
ATOM   1663  CD2 LEU B  78      11.755   8.577  23.681  1.00 74.95           C  
ANISOU 1663  CD2 LEU B  78     9449  10178   8852   1879    107   1894       C  
ATOM   1664  N   ASP B  79      15.431   7.881  19.489  1.00 88.20           N  
ANISOU 1664  N   ASP B  79    11093  11981  10439   1962    186   1978       N  
ATOM   1665  CA  ASP B  79      15.978   7.057  18.426  1.00 91.64           C  
ANISOU 1665  CA  ASP B  79    11533  12450  10835   1989    203   1982       C  
ATOM   1666  C   ASP B  79      17.226   6.304  18.873  1.00 92.16           C  
ANISOU 1666  C   ASP B  79    11602  12526  10890   1996    221   1971       C  
ATOM   1667  O   ASP B  79      17.405   5.130  18.533  1.00 93.42           O  
ANISOU 1667  O   ASP B  79    11778  12702  11015   2014    228   1952       O  
ATOM   1668  CB  ASP B  79      16.273   7.904  17.197  1.00 98.26           C  
ANISOU 1668  CB  ASP B  79    12351  13312  11671   2002    213   2022       C  
ATOM   1669  CG  ASP B  79      15.010   8.313  16.470  1.00 97.27           C  
ANISOU 1669  CG  ASP B  79    12229  13186  11545   2002    197   2029       C  
ATOM   1670  OD1 ASP B  79      13.949   7.680  16.701  1.00 92.95           O  
ANISOU 1670  OD1 ASP B  79    11703  12626  10988   1998    179   2000       O  
ATOM   1671  OD2 ASP B  79      15.080   9.266  15.663  1.00100.79           O  
ANISOU 1671  OD2 ASP B  79    12655  13642  11997   2007    202   2063       O  
ATOM   1672  N   ASN B  80      18.105   6.966  19.623  1.00 91.55           N  
ANISOU 1672  N   ASN B  80    11507  12437  10839   1983    229   1984       N  
ATOM   1673  CA  ASN B  80      19.158   6.199  20.259  1.00 89.35           C  
ANISOU 1673  CA  ASN B  80    11234  12163  10553   1987    243   1969       C  
ATOM   1674  C   ASN B  80      18.849   6.058  21.748  1.00 83.03           C  
ANISOU 1674  C   ASN B  80    10444  11329   9775   1964    229   1940       C  
ATOM   1675  O   ASN B  80      19.422   6.761  22.593  1.00 82.63           O  
ANISOU 1675  O   ASN B  80    10380  11261   9754   1948    230   1948       O  
ATOM   1676  CB  ASN B  80      20.502   6.912  20.043  1.00 94.04           C  
ANISOU 1676  CB  ASN B  80    11802  12771  11159   1991    263   2004       C  
ATOM   1677  CG  ASN B  80      21.688   6.106  20.540  1.00 93.73           C  
ANISOU 1677  CG  ASN B  80    11766  12740  11107   1998    280   1991       C  
ATOM   1678  OD1 ASN B  80      21.584   4.902  20.773  1.00 91.02           O  
ANISOU 1678  OD1 ASN B  80    11445  12400  10739   2006    280   1959       O  
ATOM   1679  ND2 ASN B  80      22.831   6.768  20.693  1.00 96.72           N  
ANISOU 1679  ND2 ASN B  80    12122  13122  11504   1995    294   2017       N  
ATOM   1680  N   LEU B  81      18.048   5.043  22.063  1.00 88.59           N  
ANISOU 1680  N   LEU B  81    11173  12025  10461   1965    218   1904       N  
ATOM   1681  CA  LEU B  81      17.689   4.729  23.439  1.00 82.67           C  
ANISOU 1681  CA  LEU B  81    10436  11247   9728   1946    206   1873       C  
ATOM   1682  C   LEU B  81      18.767   3.837  24.015  1.00 81.52           C  
ANISOU 1682  C   LEU B  81    10298  11108   9569   1952    221   1856       C  
ATOM   1683  O   LEU B  81      19.160   3.977  25.182  1.00 78.77           O  
ANISOU 1683  O   LEU B  81     9948  10739   9242   1937    220   1845       O  
ATOM   1684  CB  LEU B  81      16.322   4.052  23.519  1.00 78.83           C  
ANISOU 1684  CB  LEU B  81     9972  10749   9229   1943    187   1844       C  
ATOM   1685  CG  LEU B  81      15.107   4.968  23.390  1.00 78.57           C  
ANISOU 1685  CG  LEU B  81     9935  10700   9218   1930    167   1854       C  
ATOM   1686  CD1 LEU B  81      13.825   4.152  23.419  1.00 76.73           C  
ANISOU 1686  CD1 LEU B  81     9724  10459   8970   1930    149   1825       C  
ATOM   1687  CD2 LEU B  81      15.117   6.021  24.494  1.00 74.94           C  
ANISOU 1687  CD2 LEU B  81     9462  10212   8800   1906    159   1860       C  
ATOM   1688  N   LYS B  82      19.214   2.899  23.177  1.00 78.67           N  
ANISOU 1688  N   LYS B  82     9945  10774   9171   1976    235   1852       N  
ATOM   1689  CA  LYS B  82      20.249   1.957  23.544  1.00 78.10           C  
ANISOU 1689  CA  LYS B  82     9880  10712   9081   1986    251   1836       C  
ATOM   1690  C   LYS B  82      21.428   2.739  24.049  1.00 79.34           C  
ANISOU 1690  C   LYS B  82    10016  10867   9264   1978    264   1858       C  
ATOM   1691  O   LYS B  82      21.865   2.556  25.183  1.00 76.39           O  
ANISOU 1691  O   LYS B  82     9645  10476   8903   1966    264   1842       O  
ATOM   1692  CB  LYS B  82      20.657   1.086  22.354  1.00 82.72           C  
ANISOU 1692  CB  LYS B  82    10472  11332   9625   2016    266   1838       C  
ATOM   1693  CG  LYS B  82      21.618  -0.033  22.731  1.00 84.58           C  
ANISOU 1693  CG  LYS B  82    10719  11578   9839   2028    281   1817       C  
ATOM   1694  CD  LYS B  82      22.234  -0.699  21.502  1.00 90.37           C  
ANISOU 1694  CD  LYS B  82    11454  12347  10534   2058    299   1826       C  
ATOM   1695  CE  LYS B  82      21.282  -1.683  20.821  1.00 91.40           C  
ANISOU 1695  CE  LYS B  82    11609  12486  10633   2073    288   1803       C  
ATOM   1696  NZ  LYS B  82      21.956  -2.417  19.699  1.00 96.13           N  
ANISOU 1696  NZ  LYS B  82    12212  13120  11194   2105    305   1808       N  
ATOM   1697  N   GLY B  83      21.905   3.654  23.212  1.00 77.91           N  
ANISOU 1697  N   GLY B  83     9812  10701   9089   1984    273   1896       N  
ATOM   1698  CA  GLY B  83      23.116   4.405  23.494  1.00 80.16           C  
ANISOU 1698  CA  GLY B  83    10074  10988   9396   1979    287   1922       C  
ATOM   1699  C   GLY B  83      23.032   5.327  24.695  1.00 77.71           C  
ANISOU 1699  C   GLY B  83     9754  10643   9128   1951    273   1923       C  
ATOM   1700  O   GLY B  83      23.971   5.424  25.487  1.00 77.03           O  
ANISOU 1700  O   GLY B  83     9661  10549   9056   1944    281   1923       O  
ATOM   1701  N   THR B  84      21.909   6.020  24.821  1.00 77.47           N  
ANISOU 1701  N   THR B  84     9724  10593   9117   1937    254   1924       N  
ATOM   1702  CA  THR B  84      21.736   6.972  25.902  1.00 75.01           C  
ANISOU 1702  CA  THR B  84     9405  10249   8846   1912    239   1926       C  
ATOM   1703  C   THR B  84      21.877   6.260  27.247  1.00 70.26           C  
ANISOU 1703  C   THR B  84     8820   9628   8249   1901    235   1890       C  
ATOM   1704  O   THR B  84      22.530   6.755  28.174  1.00 69.85           O  
ANISOU 1704  O   THR B  84     8758   9558   8222   1888    235   1893       O  
ATOM   1705  CB  THR B  84      20.387   7.666  25.789  1.00 73.54           C  
ANISOU 1705  CB  THR B  84     9220  10046   8676   1900    219   1928       C  
ATOM   1706  OG1 THR B  84      20.313   8.314  24.516  1.00 78.41           O  
ANISOU 1706  OG1 THR B  84     9821  10682   9288   1911    224   1962       O  
ATOM   1707  CG2 THR B  84      20.218   8.682  26.898  1.00 69.52           C  
ANISOU 1707  CG2 THR B  84     8702   9503   8209   1876    203   1930       C  
ATOM   1708  N   PHE B  85      21.289   5.071  27.324  1.00 68.63           N  
ANISOU 1708  N   PHE B  85     8637   9425   8015   1909    233   1858       N  
ATOM   1709  CA  PHE B  85      21.324   4.259  28.535  1.00 67.87           C  
ANISOU 1709  CA  PHE B  85     8559   9312   7918   1901    230   1822       C  
ATOM   1710  C   PHE B  85      22.441   3.205  28.522  1.00 67.83           C  
ANISOU 1710  C   PHE B  85     8560   9327   7887   1917    250   1811       C  
ATOM   1711  O   PHE B  85      22.549   2.386  29.439  1.00 67.23           O  
ANISOU 1711  O   PHE B  85     8499   9241   7804   1914    250   1780       O  
ATOM   1712  CB  PHE B  85      19.970   3.579  28.735  1.00 67.39           C  
ANISOU 1712  CB  PHE B  85     8520   9240   7846   1898    213   1791       C  
ATOM   1713  CG  PHE B  85      18.854   4.533  29.021  1.00 67.29           C  
ANISOU 1713  CG  PHE B  85     8503   9203   7861   1881    192   1796       C  
ATOM   1714  CD1 PHE B  85      18.067   5.023  28.000  1.00 67.76           C  
ANISOU 1714  CD1 PHE B  85     8557   9270   7917   1885    185   1815       C  
ATOM   1715  CD2 PHE B  85      18.597   4.939  30.314  1.00 66.74           C  
ANISOU 1715  CD2 PHE B  85     8435   9104   7821   1860    180   1783       C  
ATOM   1716  CE1 PHE B  85      17.052   5.884  28.266  1.00 67.66           C  
ANISOU 1716  CE1 PHE B  85     8541   9237   7931   1869    166   1819       C  
ATOM   1717  CE2 PHE B  85      17.581   5.811  30.584  1.00 66.67           C  
ANISOU 1717  CE2 PHE B  85     8422   9073   7837   1845    161   1787       C  
ATOM   1718  CZ  PHE B  85      16.805   6.279  29.560  1.00 67.12           C  
ANISOU 1718  CZ  PHE B  85     8474   9138   7891   1850    154   1805       C  
ATOM   1719  N   ALA B  86      23.258   3.219  27.476  1.00 70.70           N  
ANISOU 1719  N   ALA B  86     8911   9719   8233   1935    268   1835       N  
ATOM   1720  CA  ALA B  86      24.292   2.206  27.316  1.00 71.96           C  
ANISOU 1720  CA  ALA B  86     9076   9900   8364   1953    288   1826       C  
ATOM   1721  C   ALA B  86      25.146   2.106  28.574  1.00 69.72           C  
ANISOU 1721  C   ALA B  86     8792   9601   8096   1942    292   1814       C  
ATOM   1722  O   ALA B  86      25.405   1.006  29.070  1.00 67.69           O  
ANISOU 1722  O   ALA B  86     8553   9346   7820   1948    298   1784       O  
ATOM   1723  CB  ALA B  86      25.153   2.507  26.099  1.00 77.95           C  
ANISOU 1723  CB  ALA B  86     9817  10691   9110   1972    306   1861       C  
ATOM   1724  N   THR B  87      25.555   3.248  29.113  1.00 70.86           N  
ANISOU 1724  N   THR B  87     8918   9729   8277   1925    288   1835       N  
ATOM   1725  CA  THR B  87      26.334   3.219  30.344  1.00 69.14           C  
ANISOU 1725  CA  THR B  87     8699   9494   8076   1913    290   1823       C  
ATOM   1726  C   THR B  87      25.458   2.836  31.522  1.00 63.76           C  
ANISOU 1726  C   THR B  87     8038   8785   7404   1898    273   1786       C  
ATOM   1727  O   THR B  87      25.816   1.966  32.299  1.00 61.42           O  
ANISOU 1727  O   THR B  87     7755   8484   7097   1899    278   1759       O  
ATOM   1728  CB  THR B  87      27.024   4.561  30.646  1.00 72.36           C  
ANISOU 1728  CB  THR B  87     9082   9890   8523   1899    288   1855       C  
ATOM   1729  OG1 THR B  87      26.868   4.862  32.043  1.00 69.34           O  
ANISOU 1729  OG1 THR B  87     8704   9474   8168   1878    274   1836       O  
ATOM   1730  CG2 THR B  87      26.427   5.684  29.793  1.00 76.76           C  
ANISOU 1730  CG2 THR B  87     9622  10447   9095   1895    280   1887       C  
ATOM   1731  N   LEU B  88      24.305   3.475  31.655  1.00 68.13           N  
ANISOU 1731  N   LEU B  88     8592   9318   7975   1885    253   1786       N  
ATOM   1732  CA  LEU B  88      23.389   3.120  32.743  1.00 63.48           C  
ANISOU 1732  CA  LEU B  88     8022   8704   7394   1871    237   1753       C  
ATOM   1733  C   LEU B  88      23.114   1.614  32.744  1.00 60.95           C  
ANISOU 1733  C   LEU B  88     7726   8394   7038   1884    243   1719       C  
ATOM   1734  O   LEU B  88      23.026   0.994  33.803  1.00 58.03           O  
ANISOU 1734  O   LEU B  88     7370   8009   6669   1877    240   1689       O  
ATOM   1735  CB  LEU B  88      22.074   3.903  32.644  1.00 62.58           C  
ANISOU 1735  CB  LEU B  88     7906   8572   7299   1859    217   1758       C  
ATOM   1736  CG  LEU B  88      21.950   5.169  33.496  1.00 62.91           C  
ANISOU 1736  CG  LEU B  88     7935   8585   7383   1837    202   1769       C  
ATOM   1737  CD1 LEU B  88      22.564   6.373  32.802  1.00 63.18           C  
ANISOU 1737  CD1 LEU B  88     7943   8625   7437   1837    205   1810       C  
ATOM   1738  CD2 LEU B  88      20.498   5.441  33.775  1.00 60.28           C  
ANISOU 1738  CD2 LEU B  88     7611   8232   7062   1826    181   1756       C  
ATOM   1739  N   SER B  89      23.025   1.035  31.551  1.00 64.59           N  
ANISOU 1739  N   SER B  89     8191   8882   7468   1903    251   1724       N  
ATOM   1740  CA  SER B  89      22.793  -0.393  31.403  1.00 63.05           C  
ANISOU 1740  CA  SER B  89     8019   8699   7238   1918    256   1694       C  
ATOM   1741  C   SER B  89      23.922  -1.185  32.070  1.00 62.57           C  
ANISOU 1741  C   SER B  89     7964   8643   7166   1924    272   1677       C  
ATOM   1742  O   SER B  89      23.702  -2.274  32.624  1.00 59.65           O  
ANISOU 1742  O   SER B  89     7615   8269   6779   1926    272   1644       O  
ATOM   1743  CB  SER B  89      22.668  -0.767  29.915  1.00 66.27           C  
ANISOU 1743  CB  SER B  89     8428   9136   7615   1940    263   1707       C  
ATOM   1744  OG  SER B  89      22.470  -2.170  29.733  1.00 65.01           O  
ANISOU 1744  OG  SER B  89     8292   8988   7422   1955    267   1677       O  
ATOM   1745  N   GLU B  90      25.132  -0.623  32.018  1.00 60.58           N  
ANISOU 1745  N   GLU B  90     7694   8400   6925   1925    285   1701       N  
ATOM   1746  CA  GLU B  90      26.287  -1.254  32.627  1.00 60.71           C  
ANISOU 1746  CA  GLU B  90     7713   8422   6933   1930    301   1689       C  
ATOM   1747  C   GLU B  90      26.172  -1.208  34.146  1.00 57.08           C  
ANISOU 1747  C   GLU B  90     7260   7931   6496   1911    291   1666       C  
ATOM   1748  O   GLU B  90      26.496  -2.184  34.822  1.00 55.20           O  
ANISOU 1748  O   GLU B  90     7037   7692   6243   1915    297   1638       O  
ATOM   1749  CB  GLU B  90      27.566  -0.578  32.160  1.00 65.13           C  
ANISOU 1749  CB  GLU B  90     8249   8996   7500   1936    317   1724       C  
ATOM   1750  CG  GLU B  90      28.742  -0.718  33.128  1.00 65.75           C  
ANISOU 1750  CG  GLU B  90     8324   9069   7588   1932    327   1718       C  
ATOM   1751  CD  GLU B  90      30.091  -0.464  32.463  1.00 70.89           C  
ANISOU 1751  CD  GLU B  90     8956   9745   8235   1944    347   1748       C  
ATOM   1752  OE1 GLU B  90      30.243   0.614  31.830  1.00 74.20           O  
ANISOU 1752  OE1 GLU B  90     9352  10168   8672   1942    347   1784       O  
ATOM   1753  OE2 GLU B  90      30.982  -1.354  32.568  1.00 71.90           O  
ANISOU 1753  OE2 GLU B  90     9090   9888   8342   1958    364   1736       O  
ATOM   1754  N   LEU B  91      25.685  -0.093  34.685  1.00 54.99           N  
ANISOU 1754  N   LEU B  91     6985   7642   6266   1891    275   1677       N  
ATOM   1755  CA  LEU B  91      25.614   0.037  36.132  1.00 52.06           C  
ANISOU 1755  CA  LEU B  91     6619   7243   5918   1873    265   1657       C  
ATOM   1756  C   LEU B  91      24.708  -1.062  36.712  1.00 50.87           C  
ANISOU 1756  C   LEU B  91     6494   7083   5750   1873    258   1617       C  
ATOM   1757  O   LEU B  91      25.088  -1.765  37.661  1.00 50.30           O  
ANISOU 1757  O   LEU B  91     6434   7004   5672   1872    263   1592       O  
ATOM   1758  CB  LEU B  91      25.128   1.431  36.550  1.00 52.24           C  
ANISOU 1758  CB  LEU B  91     6628   7241   5981   1853    247   1675       C  
ATOM   1759  CG  LEU B  91      24.943   1.570  38.073  1.00 51.03           C  
ANISOU 1759  CG  LEU B  91     6482   7057   5851   1835    235   1652       C  
ATOM   1760  CD1 LEU B  91      26.077   0.964  38.831  1.00 50.67           C  
ANISOU 1760  CD1 LEU B  91     6441   7013   5799   1838    248   1638       C  
ATOM   1761  CD2 LEU B  91      24.778   2.989  38.540  1.00 51.23           C  
ANISOU 1761  CD2 LEU B  91     6491   7057   5917   1817    219   1671       C  
ATOM   1762  N   HIS B  92      23.521  -1.217  36.134  1.00 55.85           N  
ANISOU 1762  N   HIS B  92     7133   7715   6371   1875    248   1613       N  
ATOM   1763  CA  HIS B  92      22.525  -2.140  36.672  1.00 52.67           C  
ANISOU 1763  CA  HIS B  92     6754   7302   5957   1873    238   1578       C  
ATOM   1764  C   HIS B  92      22.806  -3.605  36.316  1.00 52.33           C  
ANISOU 1764  C   HIS B  92     6729   7279   5875   1892    252   1556       C  
ATOM   1765  O   HIS B  92      22.685  -4.486  37.167  1.00 49.88           O  
ANISOU 1765  O   HIS B  92     6435   6960   5556   1890    252   1525       O  
ATOM   1766  CB  HIS B  92      21.129  -1.782  36.173  1.00 52.45           C  
ANISOU 1766  CB  HIS B  92     6728   7268   5934   1868    221   1582       C  
ATOM   1767  CG  HIS B  92      20.763  -0.339  36.337  1.00 52.81           C  
ANISOU 1767  CG  HIS B  92     6756   7295   6015   1851    208   1606       C  
ATOM   1768  ND1 HIS B  92      21.437   0.676  35.697  1.00 55.74           N  
ANISOU 1768  ND1 HIS B  92     7104   7674   6399   1852    212   1640       N  
ATOM   1769  CD2 HIS B  92      19.772   0.256  37.039  1.00 50.91           C  
ANISOU 1769  CD2 HIS B  92     6515   7029   5798   1834    189   1599       C  
ATOM   1770  CE1 HIS B  92      20.880   1.836  35.999  1.00 55.58           C  
ANISOU 1770  CE1 HIS B  92     7073   7634   6411   1836    197   1654       C  
ATOM   1771  NE2 HIS B  92      19.863   1.608  36.806  1.00 52.65           N  
ANISOU 1771  NE2 HIS B  92     6715   7242   6046   1826    183   1630       N  
ATOM   1772  N   CYS B  93      23.146  -3.880  35.057  1.00 58.06           N  
ANISOU 1772  N   CYS B  93     7451   8032   6576   1910    262   1571       N  
ATOM   1773  CA  CYS B  93      23.311  -5.266  34.620  1.00 58.32           C  
ANISOU 1773  CA  CYS B  93     7503   8084   6572   1930    273   1550       C  
ATOM   1774  C   CYS B  93      24.667  -5.870  34.993  1.00 59.08           C  
ANISOU 1774  C   CYS B  93     7601   8192   6656   1940    292   1542       C  
ATOM   1775  O   CYS B  93      24.736  -6.972  35.558  1.00 57.26           O  
ANISOU 1775  O   CYS B  93     7389   7960   6408   1945    297   1511       O  
ATOM   1776  CB  CYS B  93      23.104  -5.353  33.112  1.00 61.12           C  
ANISOU 1776  CB  CYS B  93     7855   8462   6904   1948    275   1567       C  
ATOM   1777  SG  CYS B  93      21.602  -4.417  32.511  1.00 60.60           S  
ANISOU 1777  SG  CYS B  93     7783   8386   6856   1937    253   1584       S  
ATOM   1778  N   ASP B  94      25.751  -5.155  34.682  1.00 55.81           N  
ANISOU 1778  N   ASP B  94     7166   7788   6250   1943    305   1570       N  
ATOM   1779  CA  ASP B  94      27.104  -5.693  34.874  1.00 57.31           C  
ANISOU 1779  CA  ASP B  94     7356   7993   6428   1954    325   1567       C  
ATOM   1780  C   ASP B  94      27.622  -5.546  36.309  1.00 55.54           C  
ANISOU 1780  C   ASP B  94     7131   7747   6225   1938    325   1554       C  
ATOM   1781  O   ASP B  94      28.246  -6.486  36.843  1.00 54.87           O  
ANISOU 1781  O   ASP B  94     7058   7667   6124   1946    336   1531       O  
ATOM   1782  CB  ASP B  94      28.083  -5.043  33.895  1.00 61.83           C  
ANISOU 1782  CB  ASP B  94     7905   8587   6999   1965    339   1604       C  
ATOM   1783  CG  ASP B  94      27.978  -5.630  32.493  1.00 64.23           C  
ANISOU 1783  CG  ASP B  94     8214   8921   7270   1989    347   1611       C  
ATOM   1784  OD1 ASP B  94      28.519  -5.021  31.538  1.00 68.21           O  
ANISOU 1784  OD1 ASP B  94     8700   9444   7773   1999    356   1643       O  
ATOM   1785  OD2 ASP B  94      27.336  -6.702  32.339  1.00 62.44           O  
ANISOU 1785  OD2 ASP B  94     8010   8698   7018   1999    343   1583       O  
ATOM   1786  N   LYS B  95      27.416  -4.371  36.916  1.00 49.47           N  
ANISOU 1786  N   LYS B  95     6348   6956   5492   1918    312   1569       N  
ATOM   1787  CA  LYS B  95      27.882  -4.154  38.285  1.00 48.20           C  
ANISOU 1787  CA  LYS B  95     6187   6774   5354   1903    310   1557       C  
ATOM   1788  C   LYS B  95      26.898  -4.599  39.348  1.00 44.42           C  
ANISOU 1788  C   LYS B  95     5726   6271   4879   1891    296   1524       C  
ATOM   1789  O   LYS B  95      27.287  -5.187  40.347  1.00 43.24           O  
ANISOU 1789  O   LYS B  95     5588   6114   4728   1889    301   1500       O  
ATOM   1790  CB  LYS B  95      28.233  -2.683  38.507  1.00 50.00           C  
ANISOU 1790  CB  LYS B  95     6391   6988   5619   1887    303   1587       C  
ATOM   1791  CG  LYS B  95      29.004  -2.051  37.356  1.00 53.35           C  
ANISOU 1791  CG  LYS B  95     6794   7434   6043   1897    314   1626       C  
ATOM   1792  CD  LYS B  95      30.406  -1.622  37.759  1.00 57.00           C  
ANISOU 1792  CD  LYS B  95     7240   7897   6519   1895    325   1642       C  
ATOM   1793  CE  LYS B  95      31.466  -2.271  36.876  1.00 58.63           C  
ANISOU 1793  CE  LYS B  95     7443   8137   6697   1917    348   1652       C  
ATOM   1794  NZ  LYS B  95      31.774  -3.692  37.262  1.00 57.54           N  
ANISOU 1794  NZ  LYS B  95     7327   8008   6529   1930    360   1618       N  
ATOM   1795  N   LEU B  96      25.634  -4.231  39.158  1.00 48.67           N  
ANISOU 1795  N   LEU B  96     6267   6798   5427   1883    279   1524       N  
ATOM   1796  CA  LEU B  96      24.539  -4.439  40.140  1.00 45.51           C  
ANISOU 1796  CA  LEU B  96     5881   6374   5036   1869    264   1497       C  
ATOM   1797  C   LEU B  96      23.756  -5.767  40.072  1.00 44.84           C  
ANISOU 1797  C   LEU B  96     5820   6294   4922   1878    263   1466       C  
ATOM   1798  O   LEU B  96      23.349  -6.322  41.104  1.00 44.55           O  
ANISOU 1798  O   LEU B  96     5798   6243   4887   1872    259   1438       O  
ATOM   1799  CB  LEU B  96      23.555  -3.275  40.023  1.00 45.11           C  
ANISOU 1799  CB  LEU B  96     5820   6307   5013   1855    245   1515       C  
ATOM   1800  CG  LEU B  96      23.917  -1.952  40.677  1.00 45.81           C  
ANISOU 1800  CG  LEU B  96     5890   6376   5140   1838    237   1534       C  
ATOM   1801  CD1 LEU B  96      22.848  -0.949  40.312  1.00 45.96           C  
ANISOU 1801  CD1 LEU B  96     5900   6383   5179   1828    219   1551       C  
ATOM   1802  CD2 LEU B  96      23.988  -2.109  42.184  1.00 44.84           C  
ANISOU 1802  CD2 LEU B  96     5776   6230   5030   1826    233   1509       C  
ATOM   1803  N   HIS B  97      23.504  -6.216  38.842  1.00 46.45           N  
ANISOU 1803  N   HIS B  97     6027   6519   5102   1894    267   1473       N  
ATOM   1804  CA  HIS B  97      22.693  -7.399  38.554  1.00 45.22           C  
ANISOU 1804  CA  HIS B  97     5894   6369   4920   1903    263   1448       C  
ATOM   1805  C   HIS B  97      21.249  -7.226  38.998  1.00 42.92           C  
ANISOU 1805  C   HIS B  97     5609   6056   4642   1889    243   1436       C  
ATOM   1806  O   HIS B  97      20.658  -8.123  39.592  1.00 41.29           O  
ANISOU 1806  O   HIS B  97     5421   5842   4427   1888    239   1407       O  
ATOM   1807  CB  HIS B  97      23.296  -8.664  39.209  1.00 44.94           C  
ANISOU 1807  CB  HIS B  97     5875   6337   4862   1912    276   1417       C  
ATOM   1808  CG  HIS B  97      24.763  -8.832  38.950  1.00 47.31           C  
ANISOU 1808  CG  HIS B  97     6168   6656   5150   1926    296   1427       C  
ATOM   1809  ND1 HIS B  97      25.294  -8.872  37.676  1.00 49.85           N  
ANISOU 1809  ND1 HIS B  97     6483   7004   5453   1943    307   1447       N  
ATOM   1810  CD2 HIS B  97      25.804  -8.924  39.801  1.00 47.88           C  
ANISOU 1810  CD2 HIS B  97     6239   6726   5227   1924    308   1420       C  
ATOM   1811  CE1 HIS B  97      26.601  -8.979  37.758  1.00 51.91           C  
ANISOU 1811  CE1 HIS B  97     6737   7277   5708   1952    324   1452       C  
ATOM   1812  NE2 HIS B  97      26.936  -9.015  39.035  1.00 50.68           N  
ANISOU 1812  NE2 HIS B  97     6585   7104   5567   1940    325   1436       N  
ATOM   1813  N   VAL B  98      20.682  -6.061  38.714  1.00 46.31           N  
ANISOU 1813  N   VAL B  98     6023   6477   5095   1878    230   1459       N  
ATOM   1814  CA  VAL B  98      19.253  -5.844  38.834  1.00 44.56           C  
ANISOU 1814  CA  VAL B  98     5806   6239   4885   1867    211   1453       C  
ATOM   1815  C   VAL B  98      18.547  -6.743  37.822  1.00 45.07           C  
ANISOU 1815  C   VAL B  98     5885   6319   4921   1881    208   1446       C  
ATOM   1816  O   VAL B  98      18.980  -6.805  36.661  1.00 47.07           O  
ANISOU 1816  O   VAL B  98     6134   6595   5157   1896    216   1462       O  
ATOM   1817  CB  VAL B  98      18.908  -4.388  38.551  1.00 44.53           C  
ANISOU 1817  CB  VAL B  98     5783   6226   4910   1855    200   1483       C  
ATOM   1818  CG1 VAL B  98      17.418  -4.090  38.817  1.00 44.42           C  
ANISOU 1818  CG1 VAL B  98     5773   6194   4911   1842    180   1476       C  
ATOM   1819  CG2 VAL B  98      19.801  -3.510  39.371  1.00 45.80           C  
ANISOU 1819  CG2 VAL B  98     5929   6375   5097   1844    204   1494       C  
ATOM   1820  N   ASP B  99      17.480  -7.431  38.243  1.00 42.06           N  
ANISOU 1820  N   ASP B  99     5520   5926   4535   1876    196   1421       N  
ATOM   1821  CA  ASP B  99      16.682  -8.203  37.308  1.00 42.83           C  
ANISOU 1821  CA  ASP B  99     5630   6034   4608   1887    189   1414       C  
ATOM   1822  C   ASP B  99      15.865  -7.261  36.445  1.00 43.44           C  
ANISOU 1822  C   ASP B  99     5696   6112   4698   1883    175   1439       C  
ATOM   1823  O   ASP B  99      15.112  -6.450  36.983  1.00 42.14           O  
ANISOU 1823  O   ASP B  99     5524   5928   4560   1866    162   1444       O  
ATOM   1824  CB  ASP B  99      15.771  -9.166  38.049  1.00 41.49           C  
ANISOU 1824  CB  ASP B  99     5480   5851   4434   1882    179   1383       C  
ATOM   1825  CG  ASP B  99      14.767  -9.844  37.119  1.00 42.69           C  
ANISOU 1825  CG  ASP B  99     5644   6010   4566   1890    167   1378       C  
ATOM   1826  OD1 ASP B  99      15.204 -10.500  36.148  1.00 44.54           O  
ANISOU 1826  OD1 ASP B  99     5885   6265   4773   1909    174   1378       O  
ATOM   1827  OD2 ASP B  99      13.535  -9.710  37.353  1.00 42.08           O  
ANISOU 1827  OD2 ASP B  99     5570   5917   4501   1879    149   1373       O  
ATOM   1828  N   PRO B 100      15.985  -7.370  35.108  1.00 42.94           N  
ANISOU 1828  N   PRO B 100     5631   6071   4615   1899    178   1454       N  
ATOM   1829  CA  PRO B 100      15.449  -6.412  34.128  1.00 43.62           C  
ANISOU 1829  CA  PRO B 100     5704   6161   4709   1898    169   1482       C  
ATOM   1830  C   PRO B 100      13.951  -6.211  34.246  1.00 43.79           C  
ANISOU 1830  C   PRO B 100     5729   6165   4743   1885    147   1477       C  
ATOM   1831  O   PRO B 100      13.382  -5.314  33.649  1.00 44.52           O  
ANISOU 1831  O   PRO B 100     5810   6257   4848   1881    138   1499       O  
ATOM   1832  CB  PRO B 100      15.801  -7.047  32.773  1.00 44.22           C  
ANISOU 1832  CB  PRO B 100     5785   6265   4752   1921    177   1489       C  
ATOM   1833  CG  PRO B 100      16.119  -8.436  33.068  1.00 43.68           C  
ANISOU 1833  CG  PRO B 100     5737   6202   4659   1932    184   1460       C  
ATOM   1834  CD  PRO B 100      16.717  -8.442  34.437  1.00 43.11           C  
ANISOU 1834  CD  PRO B 100     5664   6115   4602   1920    192   1446       C  
ATOM   1835  N   GLU B 101      13.305  -7.094  34.989  1.00 45.87           N  
ANISOU 1835  N   GLU B 101     6009   6416   5002   1881    140   1448       N  
ATOM   1836  CA  GLU B 101      11.884  -6.974  35.207  1.00 45.69           C  
ANISOU 1836  CA  GLU B 101     5992   6377   4993   1868    120   1442       C  
ATOM   1837  C   GLU B 101      11.560  -5.814  36.103  1.00 44.44           C  
ANISOU 1837  C   GLU B 101     5820   6197   4870   1849    113   1451       C  
ATOM   1838  O   GLU B 101      10.462  -5.293  36.032  1.00 45.28           O  
ANISOU 1838  O   GLU B 101     5922   6291   4990   1839     96   1457       O  
ATOM   1839  CB  GLU B 101      11.314  -8.259  35.813  1.00 44.34           C  
ANISOU 1839  CB  GLU B 101     5842   6198   4808   1869    114   1409       C  
ATOM   1840  CG  GLU B 101       9.810  -8.351  35.722  1.00 45.61           C  
ANISOU 1840  CG  GLU B 101     6009   6347   4975   1860     93   1404       C  
ATOM   1841  CD  GLU B 101       9.321  -8.511  34.292  1.00 48.95           C  
ANISOU 1841  CD  GLU B 101     6434   6785   5378   1873     84   1416       C  
ATOM   1842  OE1 GLU B 101       9.872  -7.906  33.347  1.00 50.30           O  
ANISOU 1842  OE1 GLU B 101     6595   6973   5545   1882     91   1439       O  
ATOM   1843  OE2 GLU B 101       8.364  -9.270  34.104  1.00 50.49           O  
ANISOU 1843  OE2 GLU B 101     6644   6977   5564   1873     70   1401       O  
ATOM   1844  N   ASN B 102      12.496  -5.414  36.954  1.00 42.45           N  
ANISOU 1844  N   ASN B 102     5559   5938   4631   1843    124   1452       N  
ATOM   1845  CA  ASN B 102      12.210  -4.290  37.826  1.00 41.91           C  
ANISOU 1845  CA  ASN B 102     5478   5848   4597   1825    116   1460       C  
ATOM   1846  C   ASN B 102      12.343  -2.905  37.138  1.00 43.69           C  
ANISOU 1846  C   ASN B 102     5683   6076   4841   1822    113   1494       C  
ATOM   1847  O   ASN B 102      11.884  -1.896  37.661  1.00 43.69           O  
ANISOU 1847  O   ASN B 102     5673   6058   4870   1808    103   1503       O  
ATOM   1848  CB  ASN B 102      13.073  -4.380  39.070  1.00 40.29           C  
ANISOU 1848  CB  ASN B 102     5273   5633   4401   1820    127   1446       C  
ATOM   1849  CG  ASN B 102      12.567  -5.418  40.033  1.00 39.07           C  
ANISOU 1849  CG  ASN B 102     5137   5468   4240   1816    124   1414       C  
ATOM   1850  OD1 ASN B 102      11.424  -5.800  39.957  1.00 39.49           O  
ANISOU 1850  OD1 ASN B 102     5199   5515   4291   1814    111   1404       O  
ATOM   1851  ND2 ASN B 102      13.404  -5.866  40.951  1.00 37.60           N  
ANISOU 1851  ND2 ASN B 102     4955   5278   4052   1817    136   1397       N  
ATOM   1852  N   PHE B 103      12.907  -2.878  35.938  1.00 43.48           N  
ANISOU 1852  N   PHE B 103     5651   6072   4798   1836    122   1512       N  
ATOM   1853  CA  PHE B 103      12.905  -1.668  35.142  1.00 46.08           C  
ANISOU 1853  CA  PHE B 103     5962   6405   5141   1835    118   1545       C  
ATOM   1854  C   PHE B 103      11.506  -1.358  34.692  1.00 47.29           C  
ANISOU 1854  C   PHE B 103     6116   6552   5300   1829    100   1549       C  
ATOM   1855  O   PHE B 103      11.053  -0.227  34.755  1.00 48.20           O  
ANISOU 1855  O   PHE B 103     6218   6654   5440   1818     90   1566       O  
ATOM   1856  CB  PHE B 103      13.791  -1.792  33.913  1.00 48.77           C  
ANISOU 1856  CB  PHE B 103     6297   6773   5459   1853    133   1564       C  
ATOM   1857  CG  PHE B 103      15.197  -2.207  34.221  1.00 48.00           C  
ANISOU 1857  CG  PHE B 103     6198   6686   5352   1860    152   1560       C  
ATOM   1858  CD1 PHE B 103      15.710  -2.068  35.501  1.00 45.57           C  
ANISOU 1858  CD1 PHE B 103     5890   6362   5063   1849    156   1549       C  
ATOM   1859  CD2 PHE B 103      16.006  -2.751  33.226  1.00 50.07           C  
ANISOU 1859  CD2 PHE B 103     6462   6976   5587   1880    167   1568       C  
ATOM   1860  CE1 PHE B 103      16.981  -2.475  35.783  1.00 45.10           C  
ANISOU 1860  CE1 PHE B 103     5830   6312   4994   1856    173   1545       C  
ATOM   1861  CE2 PHE B 103      17.283  -3.160  33.496  1.00 49.67           C  
ANISOU 1861  CE2 PHE B 103     6410   6935   5527   1888    186   1565       C  
ATOM   1862  CZ  PHE B 103      17.777  -3.022  34.774  1.00 47.11           C  
ANISOU 1862  CZ  PHE B 103     6085   6594   5222   1876    188   1554       C  
ATOM   1863  N   ARG B 104      10.819  -2.366  34.203  1.00 45.94           N  
ANISOU 1863  N   ARG B 104     5962   6389   5106   1838     94   1533       N  
ATOM   1864  CA  ARG B 104       9.484  -2.158  33.700  1.00 47.45           C  
ANISOU 1864  CA  ARG B 104     6155   6575   5300   1834     76   1537       C  
ATOM   1865  C   ARG B 104       8.512  -1.945  34.854  1.00 45.52           C  
ANISOU 1865  C   ARG B 104     5913   6304   5079   1816     62   1522       C  
ATOM   1866  O   ARG B 104       7.614  -1.067  34.782  1.00 46.67           O  
ANISOU 1866  O   ARG B 104     6049   6438   5244   1806     48   1534       O  
ATOM   1867  CB  ARG B 104       9.059  -3.332  32.843  1.00 48.71           C  
ANISOU 1867  CB  ARG B 104     6331   6750   5427   1849     73   1525       C  
ATOM   1868  CG  ARG B 104      10.028  -4.455  32.866  1.00 49.12           C  
ANISOU 1868  CG  ARG B 104     6395   6816   5453   1862     89   1508       C  
ATOM   1869  CD  ARG B 104       9.852  -5.300  31.633  1.00 51.61           C  
ANISOU 1869  CD  ARG B 104     6722   7153   5736   1881     87   1507       C  
ATOM   1870  NE  ARG B 104       9.769  -4.478  30.426  1.00 55.20           N  
ANISOU 1870  NE  ARG B 104     7164   7621   6190   1887     86   1536       N  
ATOM   1871  CZ  ARG B 104      10.392  -4.763  29.282  1.00 58.23           C  
ANISOU 1871  CZ  ARG B 104     7547   8029   6548   1907     96   1548       C  
ATOM   1872  NH1 ARG B 104      11.160  -5.862  29.180  1.00 58.04           N  
ANISOU 1872  NH1 ARG B 104     7537   8020   6497   1922    108   1532       N  
ATOM   1873  NH2 ARG B 104      10.247  -3.947  28.235  1.00 61.71           N  
ANISOU 1873  NH2 ARG B 104     7976   8482   6990   1912     94   1575       N  
ATOM   1874  N   LEU B 105       8.712  -2.734  35.911  1.00 45.96           N  
ANISOU 1874  N   LEU B 105     5980   6350   5132   1813     66   1496       N  
ATOM   1875  CA  LEU B 105       7.952  -2.552  37.130  1.00 44.35           C  
ANISOU 1875  CA  LEU B 105     5778   6122   4951   1797     56   1481       C  
ATOM   1876  C   LEU B 105       8.049  -1.107  37.566  1.00 44.61           C  
ANISOU 1876  C   LEU B 105     5793   6141   5017   1785     52   1500       C  
ATOM   1877  O   LEU B 105       7.050  -0.501  37.913  1.00 45.22           O  
ANISOU 1877  O   LEU B 105     5866   6202   5113   1774     38   1502       O  
ATOM   1878  CB  LEU B 105       8.429  -3.474  38.244  1.00 41.79           C  
ANISOU 1878  CB  LEU B 105     5465   5792   4620   1796     65   1454       C  
ATOM   1879  CG  LEU B 105       7.864  -4.913  38.260  1.00 41.50           C  
ANISOU 1879  CG  LEU B 105     5450   5759   4560   1803     62   1427       C  
ATOM   1880  CD1 LEU B 105       8.113  -5.618  39.586  1.00 39.20           C  
ANISOU 1880  CD1 LEU B 105     5169   5456   4270   1798     68   1401       C  
ATOM   1881  CD2 LEU B 105       6.377  -4.953  37.944  1.00 42.87           C  
ANISOU 1881  CD2 LEU B 105     5627   5925   4737   1797     42   1426       C  
ATOM   1882  N   LEU B 106       9.242  -0.536  37.498  1.00 42.80           N  
ANISOU 1882  N   LEU B 106     5552   5918   4792   1787     65   1516       N  
ATOM   1883  CA  LEU B 106       9.406   0.888  37.829  1.00 43.63           C  
ANISOU 1883  CA  LEU B 106     5639   6009   4929   1776     61   1537       C  
ATOM   1884  C   LEU B 106       8.827   1.862  36.801  1.00 46.55           C  
ANISOU 1884  C   LEU B 106     5996   6382   5307   1776     51   1564       C  
ATOM   1885  O   LEU B 106       8.223   2.856  37.188  1.00 47.31           O  
ANISOU 1885  O   LEU B 106     6084   6462   5431   1764     39   1573       O  
ATOM   1886  CB  LEU B 106      10.882   1.225  38.026  1.00 43.33           C  
ANISOU 1886  CB  LEU B 106     5591   5977   4895   1779     76   1547       C  
ATOM   1887  CG  LEU B 106      11.154   2.704  38.219  1.00 44.99           C  
ANISOU 1887  CG  LEU B 106     5783   6174   5138   1768     71   1571       C  
ATOM   1888  CD1 LEU B 106      10.652   3.126  39.596  1.00 43.93           C  
ANISOU 1888  CD1 LEU B 106     5650   6013   5030   1753     60   1557       C  
ATOM   1889  CD2 LEU B 106      12.619   2.934  38.061  1.00 45.85           C  
ANISOU 1889  CD2 LEU B 106     5882   6294   5246   1774     87   1586       C  
ATOM   1890  N   GLY B 107       9.038   1.587  35.511  1.00 43.97           N  
ANISOU 1890  N   GLY B 107     5669   6079   4959   1789     56   1577       N  
ATOM   1891  CA  GLY B 107       8.507   2.410  34.437  1.00 45.86           C  
ANISOU 1891  CA  GLY B 107     5898   6325   5203   1791     48   1603       C  
ATOM   1892  C   GLY B 107       6.998   2.495  34.525  1.00 46.66           C  
ANISOU 1892  C   GLY B 107     6005   6413   5312   1783     29   1596       C  
ATOM   1893  O   GLY B 107       6.400   3.532  34.263  1.00 47.90           O  
ANISOU 1893  O   GLY B 107     6150   6562   5488   1776     18   1614       O  
ATOM   1894  N   ASN B 108       6.378   1.385  34.920  1.00 45.92           N  
ANISOU 1894  N   ASN B 108     5928   6316   5204   1784     25   1569       N  
ATOM   1895  CA  ASN B 108       4.931   1.349  35.134  1.00 46.45           C  
ANISOU 1895  CA  ASN B 108     6001   6369   5279   1775      6   1559       C  
ATOM   1896  C   ASN B 108       4.470   2.135  36.349  1.00 45.36           C  
ANISOU 1896  C   ASN B 108     5856   6205   5173   1759     -2   1555       C  
ATOM   1897  O   ASN B 108       3.454   2.794  36.270  1.00 46.92           O  
ANISOU 1897  O   ASN B 108     6050   6393   5386   1752    -17   1563       O  
ATOM   1898  CB  ASN B 108       4.448  -0.084  35.271  1.00 45.53           C  
ANISOU 1898  CB  ASN B 108     5904   6255   5139   1780      4   1532       C  
ATOM   1899  CG  ASN B 108       3.858  -0.612  33.999  1.00 48.17           C  
ANISOU 1899  CG  ASN B 108     6245   6606   5450   1791     -3   1537       C  
ATOM   1900  OD1 ASN B 108       3.883   0.058  32.958  1.00 50.80           O  
ANISOU 1900  OD1 ASN B 108     6568   6950   5782   1797     -4   1561       O  
ATOM   1901  ND2 ASN B 108       3.320  -1.828  34.063  1.00 47.87           N  
ANISOU 1901  ND2 ASN B 108     6225   6570   5395   1795     -9   1514       N  
ATOM   1902  N   VAL B 109       5.173   2.044  37.476  1.00 43.97           N  
ANISOU 1902  N   VAL B 109     5682   6019   5006   1754      6   1542       N  
ATOM   1903  CA  VAL B 109       4.792   2.808  38.654  1.00 43.70           C  
ANISOU 1903  CA  VAL B 109     5642   5960   5002   1739     -2   1537       C  
ATOM   1904  C   VAL B 109       4.958   4.276  38.301  1.00 44.29           C  
ANISOU 1904  C   VAL B 109     5698   6030   5100   1735     -7   1566       C  
ATOM   1905  O   VAL B 109       4.193   5.147  38.774  1.00 44.43           O  
ANISOU 1905  O   VAL B 109     5709   6029   5142   1724    -20   1570       O  
ATOM   1906  CB  VAL B 109       5.619   2.432  39.882  1.00 42.92           C  
ANISOU 1906  CB  VAL B 109     5548   5853   4907   1736      8   1519       C  
ATOM   1907  CG1 VAL B 109       5.471   3.401  40.993  1.00 42.75           C  
ANISOU 1907  CG1 VAL B 109     5518   5808   4917   1723      1   1519       C  
ATOM   1908  CG2 VAL B 109       5.163   1.126  40.373  1.00 42.37           C  
ANISOU 1908  CG2 VAL B 109     5495   5783   4820   1738      9   1490       C  
ATOM   1909  N   LEU B 110       5.913   4.570  37.421  1.00 44.42           N  
ANISOU 1909  N   LEU B 110     5706   6064   5109   1743      4   1587       N  
ATOM   1910  CA  LEU B 110       6.027   5.943  36.936  1.00 45.22           C  
ANISOU 1910  CA  LEU B 110     5789   6161   5230   1739     -1   1616       C  
ATOM   1911  C   LEU B 110       4.719   6.351  36.220  1.00 46.11           C  
ANISOU 1911  C   LEU B 110     5900   6272   5346   1738    -16   1626       C  
ATOM   1912  O   LEU B 110       4.073   7.320  36.626  1.00 46.43           O  
ANISOU 1912  O   LEU B 110     5934   6296   5413   1727    -29   1632       O  
ATOM   1913  CB  LEU B 110       7.224   6.110  36.012  1.00 45.53           C  
ANISOU 1913  CB  LEU B 110     5820   6221   5259   1749     14   1638       C  
ATOM   1914  CG  LEU B 110       7.330   7.468  35.350  1.00 47.34           C  
ANISOU 1914  CG  LEU B 110     6030   6450   5507   1747     10   1670       C  
ATOM   1915  CD1 LEU B 110       7.768   8.470  36.388  1.00 47.01           C  
ANISOU 1915  CD1 LEU B 110     5978   6386   5498   1735      6   1675       C  
ATOM   1916  CD2 LEU B 110       8.287   7.409  34.189  1.00 49.46           C  
ANISOU 1916  CD2 LEU B 110     6291   6744   5758   1761     25   1692       C  
ATOM   1917  N   VAL B 111       4.317   5.587  35.198  1.00 44.60           N  
ANISOU 1917  N   VAL B 111     5717   6101   5129   1748    -16   1625       N  
ATOM   1918  CA  VAL B 111       3.065   5.833  34.455  1.00 47.02           C  
ANISOU 1918  CA  VAL B 111     6024   6408   5435   1748    -31   1633       C  
ATOM   1919  C   VAL B 111       1.857   5.935  35.378  1.00 46.35           C  
ANISOU 1919  C   VAL B 111     5944   6301   5367   1736    -47   1617       C  
ATOM   1920  O   VAL B 111       0.975   6.750  35.143  1.00 48.49           O  
ANISOU 1920  O   VAL B 111     6207   6563   5653   1730    -60   1629       O  
ATOM   1921  CB  VAL B 111       2.795   4.743  33.378  1.00 47.98           C  
ANISOU 1921  CB  VAL B 111     6158   6551   5523   1762    -30   1628       C  
ATOM   1922  CG1 VAL B 111       1.335   4.458  33.260  1.00 48.80           C  
ANISOU 1922  CG1 VAL B 111     6269   6647   5625   1758    -47   1619       C  
ATOM   1923  CG2 VAL B 111       3.382   5.156  32.018  1.00 51.12           C  
ANISOU 1923  CG2 VAL B 111     6545   6970   5908   1774    -22   1656       C  
ATOM   1924  N   CYS B 112       1.836   5.158  36.446  1.00 48.02           N  
ANISOU 1924  N   CYS B 112     6166   6502   5578   1732    -45   1591       N  
ATOM   1925  CA  CYS B 112       0.832   5.360  37.473  1.00 47.62           C  
ANISOU 1925  CA  CYS B 112     6118   6430   5546   1720    -57   1577       C  
ATOM   1926  C   CYS B 112       0.880   6.735  38.117  1.00 48.37           C  
ANISOU 1926  C   CYS B 112     6199   6506   5674   1710    -63   1590       C  
ATOM   1927  O   CYS B 112      -0.136   7.421  38.208  1.00 50.00           O  
ANISOU 1927  O   CYS B 112     6401   6700   5898   1703    -77   1595       O  
ATOM   1928  CB  CYS B 112       0.971   4.318  38.556  1.00 44.97           C  
ANISOU 1928  CB  CYS B 112     5795   6088   5204   1718    -52   1548       C  
ATOM   1929  SG  CYS B 112      -0.167   2.970  38.334  1.00 45.25           S  
ANISOU 1929  SG  CYS B 112     5848   6128   5217   1722    -60   1528       S  
ATOM   1930  N   VAL B 113       2.063   7.130  38.572  1.00 48.61           N  
ANISOU 1930  N   VAL B 113     6222   6533   5713   1709    -52   1594       N  
ATOM   1931  CA  VAL B 113       2.247   8.457  39.174  1.00 49.73           C  
ANISOU 1931  CA  VAL B 113     6352   6657   5887   1699    -58   1607       C  
ATOM   1932  C   VAL B 113       1.938   9.620  38.200  1.00 53.02           C  
ANISOU 1932  C   VAL B 113     6754   7076   6315   1699    -66   1636       C  
ATOM   1933  O   VAL B 113       1.331  10.620  38.600  1.00 54.57           O  
ANISOU 1933  O   VAL B 113     6943   7255   6538   1691    -79   1643       O  
ATOM   1934  CB  VAL B 113       3.669   8.599  39.715  1.00 48.53           C  
ANISOU 1934  CB  VAL B 113     6196   6504   5741   1700    -46   1608       C  
ATOM   1935  CG1 VAL B 113       3.862   9.975  40.356  1.00 50.36           C  
ANISOU 1935  CG1 VAL B 113     6414   6714   6006   1690    -54   1620       C  
ATOM   1936  CG2 VAL B 113       3.941   7.456  40.718  1.00 45.75           C  
ANISOU 1936  CG2 VAL B 113     5857   6149   5376   1700    -38   1578       C  
ATOM   1937  N   LEU B 114       2.356   9.468  36.938  1.00 47.70           N  
ANISOU 1937  N   LEU B 114     6076   6423   5623   1709    -59   1653       N  
ATOM   1938  CA  LEU B 114       1.942  10.356  35.857  1.00 51.12           C  
ANISOU 1938  CA  LEU B 114     6499   6863   6061   1711    -65   1680       C  
ATOM   1939  C   LEU B 114       0.415  10.533  35.791  1.00 52.43           C  
ANISOU 1939  C   LEU B 114     6668   7020   6233   1706    -83   1676       C  
ATOM   1940  O   LEU B 114      -0.129  11.651  35.771  1.00 54.82           O  
ANISOU 1940  O   LEU B 114     6960   7311   6558   1700    -94   1691       O  
ATOM   1941  CB  LEU B 114       2.429   9.821  34.515  1.00 52.32           C  
ANISOU 1941  CB  LEU B 114     6652   7043   6186   1725    -55   1693       C  
ATOM   1942  CG  LEU B 114       3.828  10.178  34.051  1.00 52.72           C  
ANISOU 1942  CG  LEU B 114     6690   7106   6234   1731    -39   1713       C  
ATOM   1943  CD1 LEU B 114       3.881  10.221  32.534  1.00 55.80           C  
ANISOU 1943  CD1 LEU B 114     7076   7521   6606   1743    -35   1736       C  
ATOM   1944  CD2 LEU B 114       4.269  11.491  34.629  1.00 53.77           C  
ANISOU 1944  CD2 LEU B 114     6809   7221   6400   1721    -43   1728       C  
ATOM   1945  N   ALA B 115      -0.271   9.403  35.730  1.00 53.82           N  
ANISOU 1945  N   ALA B 115     6858   7202   6389   1710    -85   1657       N  
ATOM   1946  CA  ALA B 115      -1.705   9.424  35.672  1.00 55.09           C  
ANISOU 1946  CA  ALA B 115     7023   7356   6554   1706   -101   1652       C  
ATOM   1947  C   ALA B 115      -2.242  10.063  36.972  1.00 54.77           C  
ANISOU 1947  C   ALA B 115     6979   7289   6541   1694   -110   1642       C  
ATOM   1948  O   ALA B 115      -3.255  10.751  36.943  1.00 56.95           O  
ANISOU 1948  O   ALA B 115     7252   7555   6833   1688   -124   1648       O  
ATOM   1949  CB  ALA B 115      -2.236   8.012  35.457  1.00 53.93           C  
ANISOU 1949  CB  ALA B 115     6892   7219   6381   1711   -101   1632       C  
ATOM   1950  N   HIS B 116      -1.549   9.882  38.095  1.00 53.27           N  
ANISOU 1950  N   HIS B 116     6792   7088   6359   1690   -103   1627       N  
ATOM   1951  CA  HIS B 116      -2.010  10.454  39.355  1.00 53.32           C  
ANISOU 1951  CA  HIS B 116     6797   7070   6391   1679   -112   1616       C  
ATOM   1952  C   HIS B 116      -2.016  11.950  39.336  1.00 55.69           C  
ANISOU 1952  C   HIS B 116     7083   7358   6719   1674   -120   1638       C  
ATOM   1953  O   HIS B 116      -2.985  12.564  39.771  1.00 57.03           O  
ANISOU 1953  O   HIS B 116     7249   7512   6906   1668   -134   1636       O  
ATOM   1954  CB  HIS B 116      -1.150  10.026  40.513  1.00 50.74           C  
ANISOU 1954  CB  HIS B 116     6475   6736   6067   1677   -102   1598       C  
ATOM   1955  CG  HIS B 116      -1.662  10.465  41.849  1.00 51.09           C  
ANISOU 1955  CG  HIS B 116     6520   6757   6135   1668   -111   1584       C  
ATOM   1956  ND1 HIS B 116      -0.907  10.375  42.996  1.00 50.23           N  
ANISOU 1956  ND1 HIS B 116     6414   6637   6034   1665   -105   1570       N  
ATOM   1957  CD2 HIS B 116      -2.859  10.961  42.233  1.00 52.57           C  
ANISOU 1957  CD2 HIS B 116     6706   6930   6338   1663   -125   1582       C  
ATOM   1958  CE1 HIS B 116      -1.607  10.801  44.028  1.00 51.21           C  
ANISOU 1958  CE1 HIS B 116     6539   6742   6178   1659   -115   1559       C  
ATOM   1959  NE2 HIS B 116      -2.796  11.168  43.591  1.00 52.64           N  
ANISOU 1959  NE2 HIS B 116     6717   6920   6364   1657   -127   1567       N  
ATOM   1960  N   HIS B 117      -0.938  12.558  38.858  1.00 57.06           N  
ANISOU 1960  N   HIS B 117     7246   7537   6896   1677   -113   1657       N  
ATOM   1961  CA  HIS B 117      -0.878  14.020  38.851  1.00 59.74           C  
ANISOU 1961  CA  HIS B 117     7572   7864   7264   1671   -121   1678       C  
ATOM   1962  C   HIS B 117      -1.789  14.615  37.768  1.00 62.90           C  
ANISOU 1962  C   HIS B 117     7965   8270   7665   1673   -131   1698       C  
ATOM   1963  O   HIS B 117      -2.501  15.565  38.032  1.00 65.21           O  
ANISOU 1963  O   HIS B 117     8251   8547   7979   1667   -144   1704       O  
ATOM   1964  CB  HIS B 117       0.569  14.510  38.672  1.00 59.81           C  
ANISOU 1964  CB  HIS B 117     7570   7876   7278   1673   -111   1695       C  
ATOM   1965  CG  HIS B 117       1.424  14.348  39.896  1.00 58.04           C  
ANISOU 1965  CG  HIS B 117     7349   7639   7064   1669   -106   1679       C  
ATOM   1966  ND1 HIS B 117       2.484  15.180  40.183  1.00 59.05           N  
ANISOU 1966  ND1 HIS B 117     7467   7758   7210   1666   -104   1692       N  
ATOM   1967  CD2 HIS B 117       1.376  13.446  40.906  1.00 55.76           C  
ANISOU 1967  CD2 HIS B 117     7074   7345   6769   1667   -103   1651       C  
ATOM   1968  CE1 HIS B 117       3.048  14.803  41.318  1.00 57.37           C  
ANISOU 1968  CE1 HIS B 117     7261   7535   7003   1663   -101   1672       C  
ATOM   1969  NE2 HIS B 117       2.397  13.751  41.778  1.00 55.36           N  
ANISOU 1969  NE2 HIS B 117     7020   7283   6733   1664    -99   1647       N  
ATOM   1970  N   PHE B 118      -1.803  14.030  36.575  1.00 59.48           N  
ANISOU 1970  N   PHE B 118     7533   7859   7206   1682   -125   1707       N  
ATOM   1971  CA  PHE B 118      -2.497  14.644  35.446  1.00 62.79           C  
ANISOU 1971  CA  PHE B 118     7946   8287   7625   1685   -132   1728       C  
ATOM   1972  C   PHE B 118      -3.945  14.240  35.184  1.00 63.64           C  
ANISOU 1972  C   PHE B 118     8061   8394   7724   1685   -145   1719       C  
ATOM   1973  O   PHE B 118      -4.493  14.645  34.167  1.00 66.44           O  
ANISOU 1973  O   PHE B 118     8410   8758   8075   1688   -150   1737       O  
ATOM   1974  CB  PHE B 118      -1.723  14.390  34.173  1.00 63.90           C  
ANISOU 1974  CB  PHE B 118     8082   8452   7744   1695   -120   1746       C  
ATOM   1975  CG  PHE B 118      -0.439  15.105  34.130  1.00 64.41           C  
ANISOU 1975  CG  PHE B 118     8135   8518   7820   1696   -110   1765       C  
ATOM   1976  CD1 PHE B 118       0.713  14.523  34.638  1.00 62.42           C  
ANISOU 1976  CD1 PHE B 118     7886   8269   7561   1697    -97   1755       C  
ATOM   1977  CD2 PHE B 118      -0.370  16.374  33.606  1.00 67.16           C  
ANISOU 1977  CD2 PHE B 118     8468   8862   8186   1694   -115   1792       C  
ATOM   1978  CE1 PHE B 118       1.907  15.197  34.605  1.00 63.24           C  
ANISOU 1978  CE1 PHE B 118     7978   8373   7677   1697    -89   1773       C  
ATOM   1979  CE2 PHE B 118       0.820  17.053  33.569  1.00 68.04           C  
ANISOU 1979  CE2 PHE B 118     8567   8974   8310   1694   -106   1811       C  
ATOM   1980  CZ  PHE B 118       1.958  16.468  34.068  1.00 66.09           C  
ANISOU 1980  CZ  PHE B 118     8323   8730   8057   1695    -94   1801       C  
ATOM   1981  N   GLY B 119      -4.553  13.426  36.046  1.00 61.45           N  
ANISOU 1981  N   GLY B 119     7796   8110   7444   1681   -148   1693       N  
ATOM   1982  CA  GLY B 119      -5.981  13.143  35.953  1.00 62.63           C  
ANISOU 1982  CA  GLY B 119     7950   8255   7590   1679   -162   1685       C  
ATOM   1983  C   GLY B 119      -6.463  12.774  34.557  1.00 64.60           C  
ANISOU 1983  C   GLY B 119     8202   8524   7818   1688   -164   1696       C  
ATOM   1984  O   GLY B 119      -5.746  12.091  33.801  1.00 63.87           O  
ANISOU 1984  O   GLY B 119     8113   8451   7702   1696   -153   1699       O  
ATOM   1985  N   LYS B 120      -7.656  13.273  34.209  1.00 60.57           N  
ANISOU 1985  N   LYS B 120     7688   8009   7315   1685   -179   1704       N  
ATOM   1986  CA  LYS B 120      -8.317  12.996  32.928  1.00 63.17           C  
ANISOU 1986  CA  LYS B 120     8020   8355   7627   1692   -184   1714       C  
ATOM   1987  C   LYS B 120      -7.470  13.373  31.728  1.00 64.75           C  
ANISOU 1987  C   LYS B 120     8213   8574   7816   1701   -175   1738       C  
ATOM   1988  O   LYS B 120      -7.666  12.881  30.623  1.00 66.30           O  
ANISOU 1988  O   LYS B 120     8413   8788   7990   1710   -176   1745       O  
ATOM   1989  CB  LYS B 120      -9.651  13.751  32.850  1.00 66.39           C  
ANISOU 1989  CB  LYS B 120     8423   8751   8050   1687   -201   1721       C  
ATOM   1990  CG  LYS B 120      -9.611  15.139  33.460  1.00 67.42           C  
ANISOU 1990  CG  LYS B 120     8541   8864   8211   1680   -205   1732       C  
ATOM   1991  CD  LYS B 120     -10.953  15.857  33.361  1.00 70.97           C  
ANISOU 1991  CD  LYS B 120     8986   9303   8675   1676   -222   1739       C  
ATOM   1992  CE  LYS B 120     -10.981  16.853  32.190  1.00 74.26           C  
ANISOU 1992  CE  LYS B 120     9392   9729   9096   1680   -224   1767       C  
ATOM   1993  NZ  LYS B 120     -12.088  17.857  32.296  1.00 76.74           N  
ANISOU 1993  NZ  LYS B 120     9699  10028   9430   1675   -239   1775       N  
ATOM   1994  N   GLU B 121      -6.524  14.263  31.971  1.00 65.51           N  
ANISOU 1994  N   GLU B 121     8297   8665   7928   1699   -167   1752       N  
ATOM   1995  CA  GLU B 121      -5.647  14.805  30.950  1.00 67.54           C  
ANISOU 1995  CA  GLU B 121     8544   8938   8180   1707   -158   1778       C  
ATOM   1996  C   GLU B 121      -4.591  13.774  30.542  1.00 65.61           C  
ANISOU 1996  C   GLU B 121     8306   8713   7908   1716   -142   1773       C  
ATOM   1997  O   GLU B 121      -3.968  13.917  29.481  1.00 67.66           O  
ANISOU 1997  O   GLU B 121     8560   8992   8156   1726   -133   1793       O  
ATOM   1998  CB  GLU B 121      -5.020  16.106  31.484  1.00 68.25           C  
ANISOU 1998  CB  GLU B 121     8619   9012   8299   1700   -156   1793       C  
ATOM   1999  CG  GLU B 121      -3.902  16.780  30.690  1.00 71.06           C  
ANISOU 1999  CG  GLU B 121     8962   9381   8655   1705   -145   1821       C  
ATOM   2000  CD  GLU B 121      -3.380  18.009  31.441  1.00 71.59           C  
ANISOU 2000  CD  GLU B 121     9017   9428   8756   1696   -147   1831       C  
ATOM   2001  OE1 GLU B 121      -4.022  18.385  32.456  1.00 70.59           O  
ANISOU 2001  OE1 GLU B 121     8893   9279   8650   1687   -159   1818       O  
ATOM   2002  OE2 GLU B 121      -2.339  18.585  31.041  1.00 73.32           O  
ANISOU 2002  OE2 GLU B 121     9225   9654   8980   1699   -137   1853       O  
ATOM   2003  N   PHE B 122      -4.415  12.723  31.356  1.00 66.29           N  
ANISOU 2003  N   PHE B 122     8405   8796   7986   1715   -138   1747       N  
ATOM   2004  CA  PHE B 122      -3.557  11.614  30.954  1.00 64.61           C  
ANISOU 2004  CA  PHE B 122     8201   8603   7746   1725   -124   1739       C  
ATOM   2005  C   PHE B 122      -4.489  10.623  30.270  1.00 65.61           C  
ANISOU 2005  C   PHE B 122     8340   8740   7848   1731   -132   1729       C  
ATOM   2006  O   PHE B 122      -5.073   9.741  30.906  1.00 63.58           O  
ANISOU 2006  O   PHE B 122     8096   8476   7586   1728   -138   1705       O  
ATOM   2007  CB  PHE B 122      -2.861  10.999  32.193  1.00 60.42           C  
ANISOU 2007  CB  PHE B 122     7677   8062   7217   1720   -116   1717       C  
ATOM   2008  CG  PHE B 122      -1.777   9.981  31.882  1.00 58.55           C  
ANISOU 2008  CG  PHE B 122     7447   7844   6955   1731    -99   1710       C  
ATOM   2009  CD1 PHE B 122      -0.470  10.385  31.630  1.00 59.39           C  
ANISOU 2009  CD1 PHE B 122     7544   7960   7062   1735    -85   1726       C  
ATOM   2010  CD2 PHE B 122      -2.064   8.626  31.874  1.00 56.28           C  
ANISOU 2010  CD2 PHE B 122     7176   7564   6643   1736    -99   1688       C  
ATOM   2011  CE1 PHE B 122       0.524   9.458  31.343  1.00 57.99           C  
ANISOU 2011  CE1 PHE B 122     7373   7800   6860   1745    -69   1721       C  
ATOM   2012  CE2 PHE B 122      -1.083   7.696  31.587  1.00 54.78           C  
ANISOU 2012  CE2 PHE B 122     6993   7391   6429   1746    -84   1681       C  
ATOM   2013  CZ  PHE B 122       0.217   8.115  31.318  1.00 55.60           C  
ANISOU 2013  CZ  PHE B 122     7087   7505   6532   1751    -69   1698       C  
ATOM   2014  N   THR B 123      -4.532  10.724  28.944  1.00 61.65           N  
ANISOU 2014  N   THR B 123     7836   8258   7331   1742   -132   1747       N  
ATOM   2015  CA  THR B 123      -5.572  10.084  28.144  1.00 64.01           C  
ANISOU 2015  CA  THR B 123     8145   8566   7611   1748   -144   1743       C  
ATOM   2016  C   THR B 123      -5.101   8.744  27.638  1.00 63.25           C  
ANISOU 2016  C   THR B 123     8062   8488   7482   1760   -136   1730       C  
ATOM   2017  O   THR B 123      -3.896   8.524  27.531  1.00 62.54           O  
ANISOU 2017  O   THR B 123     7971   8410   7382   1767   -120   1734       O  
ATOM   2018  CB  THR B 123      -5.992  10.968  26.967  1.00 68.78           C  
ANISOU 2018  CB  THR B 123     8738   9179   8215   1753   -150   1770       C  
ATOM   2019  OG1 THR B 123      -5.116  10.759  25.864  1.00 70.86           O  
ANISOU 2019  OG1 THR B 123     9001   9468   8456   1767   -137   1785       O  
ATOM   2020  CG2 THR B 123      -5.924  12.413  27.362  1.00 69.55           C  
ANISOU 2020  CG2 THR B 123     8819   9262   8343   1744   -151   1788       C  
ATOM   2021  N   PRO B 124      -6.038   7.839  27.320  1.00 63.79           N  
ANISOU 2021  N   PRO B 124     8144   8560   7535   1763   -149   1716       N  
ATOM   2022  CA  PRO B 124      -5.643   6.517  26.818  1.00 64.37           C  
ANISOU 2022  CA  PRO B 124     8231   8649   7576   1775   -144   1703       C  
ATOM   2023  C   PRO B 124      -4.636   6.560  25.654  1.00 67.18           C  
ANISOU 2023  C   PRO B 124     8584   9032   7911   1791   -130   1722       C  
ATOM   2024  O   PRO B 124      -3.703   5.764  25.682  1.00 66.99           O  
ANISOU 2024  O   PRO B 124     8567   9018   7869   1799   -116   1712       O  
ATOM   2025  CB  PRO B 124      -6.974   5.905  26.395  1.00 65.46           C  
ANISOU 2025  CB  PRO B 124     8381   8787   7705   1775   -163   1694       C  
ATOM   2026  CG  PRO B 124      -7.953   6.508  27.351  1.00 63.79           C  
ANISOU 2026  CG  PRO B 124     8165   8551   7522   1759   -176   1688       C  
ATOM   2027  CD  PRO B 124      -7.483   7.908  27.595  1.00 63.66           C  
ANISOU 2027  CD  PRO B 124     8131   8528   7530   1754   -169   1709       C  
ATOM   2028  N   PRO B 125      -4.785   7.482  24.681  1.00 63.95           N  
ANISOU 2028  N   PRO B 125     8163   8631   7504   1796   -131   1748       N  
ATOM   2029  CA  PRO B 125      -3.707   7.574  23.685  1.00 66.75           C  
ANISOU 2029  CA  PRO B 125     8512   9009   7840   1811   -115   1767       C  
ATOM   2030  C   PRO B 125      -2.347   8.021  24.262  1.00 65.50           C  
ANISOU 2030  C   PRO B 125     8343   8851   7693   1809    -96   1774       C  
ATOM   2031  O   PRO B 125      -1.302   7.531  23.805  1.00 66.46           O  
ANISOU 2031  O   PRO B 125     8466   8990   7794   1821    -80   1777       O  
ATOM   2032  CB  PRO B 125      -4.236   8.620  22.695  1.00 70.09           C  
ANISOU 2032  CB  PRO B 125     8924   9439   8269   1814   -122   1794       C  
ATOM   2033  CG  PRO B 125      -5.687   8.579  22.845  1.00 69.75           C  
ANISOU 2033  CG  PRO B 125     8886   9381   8233   1806   -144   1784       C  
ATOM   2034  CD  PRO B 125      -5.940   8.308  24.295  1.00 65.56           C  
ANISOU 2034  CD  PRO B 125     8361   8828   7722   1790   -148   1761       C  
ATOM   2035  N   VAL B 126      -2.361   8.935  25.233  1.00 66.02           N  
ANISOU 2035  N   VAL B 126     8399   8896   7791   1794    -97   1777       N  
ATOM   2036  CA  VAL B 126      -1.128   9.433  25.816  1.00 65.17           C  
ANISOU 2036  CA  VAL B 126     8280   8786   7696   1790    -81   1785       C  
ATOM   2037  C   VAL B 126      -0.418   8.345  26.636  1.00 63.64           C  
ANISOU 2037  C   VAL B 126     8098   8591   7492   1791    -71   1760       C  
ATOM   2038  O   VAL B 126       0.802   8.180  26.525  1.00 64.16           O  
ANISOU 2038  O   VAL B 126     8160   8668   7548   1798    -54   1765       O  
ATOM   2039  CB  VAL B 126      -1.382  10.673  26.676  1.00 64.00           C  
ANISOU 2039  CB  VAL B 126     8119   8614   7585   1775    -88   1793       C  
ATOM   2040  CG1 VAL B 126      -0.198  10.931  27.624  1.00 63.30           C  
ANISOU 2040  CG1 VAL B 126     8023   8516   7511   1769    -75   1791       C  
ATOM   2041  CG2 VAL B 126      -1.623  11.865  25.776  1.00 67.38           C  
ANISOU 2041  CG2 VAL B 126     8531   9046   8023   1776    -91   1824       C  
ATOM   2042  N   GLN B 127      -1.163   7.598  27.447  1.00 64.11           N  
ANISOU 2042  N   GLN B 127     8171   8636   7552   1784    -82   1733       N  
ATOM   2043  CA  GLN B 127      -0.582   6.438  28.123  1.00 62.14           C  
ANISOU 2043  CA  GLN B 127     7935   8388   7289   1786    -73   1708       C  
ATOM   2044  C   GLN B 127       0.021   5.478  27.088  1.00 64.48           C  
ANISOU 2044  C   GLN B 127     8239   8710   7549   1804    -63   1707       C  
ATOM   2045  O   GLN B 127       1.201   5.115  27.175  1.00 64.29           O  
ANISOU 2045  O   GLN B 127     8216   8697   7516   1811    -46   1706       O  
ATOM   2046  CB  GLN B 127      -1.627   5.701  28.965  1.00 59.82           C  
ANISOU 2046  CB  GLN B 127     7654   8076   6997   1777    -87   1680       C  
ATOM   2047  CG  GLN B 127      -1.263   4.244  29.269  1.00 59.32           C  
ANISOU 2047  CG  GLN B 127     7608   8020   6911   1783    -81   1654       C  
ATOM   2048  CD  GLN B 127      -2.191   3.608  30.283  1.00 57.04           C  
ANISOU 2048  CD  GLN B 127     7330   7712   6629   1772    -93   1628       C  
ATOM   2049  OE1 GLN B 127      -3.191   4.195  30.665  1.00 55.48           O  
ANISOU 2049  OE1 GLN B 127     7129   7499   6453   1761   -107   1629       O  
ATOM   2050  NE2 GLN B 127      -1.859   2.405  30.725  1.00 57.19           N  
ANISOU 2050  NE2 GLN B 127     7364   7734   6633   1776    -87   1605       N  
ATOM   2051  N   ALA B 128      -0.791   5.088  26.104  1.00 61.65           N  
ANISOU 2051  N   ALA B 128     7889   8363   7173   1812    -74   1709       N  
ATOM   2052  CA  ALA B 128      -0.347   4.194  25.042  1.00 64.35           C  
ANISOU 2052  CA  ALA B 128     8240   8729   7481   1831    -67   1709       C  
ATOM   2053  C   ALA B 128       0.934   4.702  24.382  1.00 67.21           C  
ANISOU 2053  C   ALA B 128     8590   9111   7836   1842    -47   1733       C  
ATOM   2054  O   ALA B 128       1.774   3.913  23.973  1.00 69.85           O  
ANISOU 2054  O   ALA B 128     8930   9463   8145   1857    -34   1728       O  
ATOM   2055  CB  ALA B 128      -1.434   4.013  24.017  1.00 66.74           C  
ANISOU 2055  CB  ALA B 128     8549   9039   7769   1838    -83   1713       C  
ATOM   2056  N   ALA B 129       1.100   6.012  24.293  1.00 68.00           N  
ANISOU 2056  N   ALA B 129     8671   9207   7958   1837    -45   1758       N  
ATOM   2057  CA  ALA B 129       2.370   6.546  23.825  1.00 70.26           C  
ANISOU 2057  CA  ALA B 129     8944   9510   8243   1845    -26   1781       C  
ATOM   2058  C   ALA B 129       3.459   6.377  24.900  1.00 67.61           C  
ANISOU 2058  C   ALA B 129     8606   9166   7917   1839    -12   1771       C  
ATOM   2059  O   ALA B 129       4.591   5.953  24.602  1.00 69.04           O  
ANISOU 2059  O   ALA B 129     8787   9365   8081   1851      6   1774       O  
ATOM   2060  CB  ALA B 129       2.225   8.010  23.425  1.00 71.45           C  
ANISOU 2060  CB  ALA B 129     9074   9657   8416   1840    -28   1812       C  
ATOM   2061  N   TYR B 130       3.126   6.690  26.150  1.00 67.65           N  
ANISOU 2061  N   TYR B 130     8610   9145   7948   1822    -19   1758       N  
ATOM   2062  CA  TYR B 130       4.116   6.579  27.215  1.00 65.32           C  
ANISOU 2062  CA  TYR B 130     8313   8841   7663   1816     -7   1748       C  
ATOM   2063  C   TYR B 130       4.499   5.139  27.468  1.00 64.19           C  
ANISOU 2063  C   TYR B 130     8189   8707   7495   1824      0   1721       C  
ATOM   2064  O   TYR B 130       5.636   4.850  27.864  1.00 63.99           O  
ANISOU 2064  O   TYR B 130     8162   8686   7465   1827     16   1717       O  
ATOM   2065  CB  TYR B 130       3.613   7.217  28.498  1.00 62.15           C  
ANISOU 2065  CB  TYR B 130     7909   8411   7296   1796    -18   1739       C  
ATOM   2066  CG  TYR B 130       4.030   8.654  28.589  1.00 63.40           C  
ANISOU 2066  CG  TYR B 130     8047   8561   7482   1788    -17   1765       C  
ATOM   2067  CD1 TYR B 130       5.021   9.054  29.472  1.00 62.06           C  
ANISOU 2067  CD1 TYR B 130     7869   8380   7330   1781     -7   1766       C  
ATOM   2068  CD2 TYR B 130       3.450   9.620  27.759  1.00 66.35           C  
ANISOU 2068  CD2 TYR B 130     8409   8937   7864   1789    -24   1790       C  
ATOM   2069  CE1 TYR B 130       5.416  10.379  29.549  1.00 63.69           C  
ANISOU 2069  CE1 TYR B 130     8057   8578   7564   1774     -8   1791       C  
ATOM   2070  CE2 TYR B 130       3.836  10.961  27.833  1.00 67.91           C  
ANISOU 2070  CE2 TYR B 130     8588   9126   8089   1781    -24   1815       C  
ATOM   2071  CZ  TYR B 130       4.826  11.335  28.725  1.00 66.64           C  
ANISOU 2071  CZ  TYR B 130     8420   8955   7947   1774    -15   1816       C  
ATOM   2072  OH  TYR B 130       5.224  12.653  28.798  1.00 68.71           O  
ANISOU 2072  OH  TYR B 130     8663   9206   8236   1767    -16   1840       O  
ATOM   2073  N   GLN B 131       3.557   4.233  27.229  1.00 61.45           N  
ANISOU 2073  N   GLN B 131     7858   8361   7130   1827    -12   1703       N  
ATOM   2074  CA  GLN B 131       3.850   2.812  27.389  1.00 60.91           C  
ANISOU 2074  CA  GLN B 131     7807   8300   7035   1836     -6   1677       C  
ATOM   2075  C   GLN B 131       4.993   2.437  26.472  1.00 63.95           C  
ANISOU 2075  C   GLN B 131     8191   8712   7394   1855     12   1688       C  
ATOM   2076  O   GLN B 131       5.902   1.733  26.893  1.00 63.20           O  
ANISOU 2076  O   GLN B 131     8102   8622   7288   1860     25   1675       O  
ATOM   2077  CB  GLN B 131       2.620   1.937  27.121  1.00 61.14           C  
ANISOU 2077  CB  GLN B 131     7853   8327   7049   1838    -24   1658       C  
ATOM   2078  CG  GLN B 131       1.569   2.019  28.229  1.00 59.18           C  
ANISOU 2078  CG  GLN B 131     7609   8053   6825   1820    -39   1642       C  
ATOM   2079  CD  GLN B 131       2.090   1.567  29.602  1.00 58.37           C  
ANISOU 2079  CD  GLN B 131     7511   7936   6731   1811    -32   1619       C  
ATOM   2080  OE1 GLN B 131       1.475   1.861  30.629  1.00 57.41           O  
ANISOU 2080  OE1 GLN B 131     7389   7793   6633   1796    -40   1609       O  
ATOM   2081  NE2 GLN B 131       3.218   0.837  29.619  1.00 58.79           N  
ANISOU 2081  NE2 GLN B 131     7570   8002   6765   1821    -15   1612       N  
ATOM   2082  N   LYS B 132       4.970   2.944  25.240  1.00 62.95           N  
ANISOU 2082  N   LYS B 132     8056   8603   7259   1866     13   1713       N  
ATOM   2083  CA  LYS B 132       6.064   2.697  24.314  1.00 66.57           C  
ANISOU 2083  CA  LYS B 132     8511   9088   7693   1885     31   1726       C  
ATOM   2084  C   LYS B 132       7.382   3.183  24.930  1.00 66.09           C  
ANISOU 2084  C   LYS B 132     8438   9028   7647   1881     49   1736       C  
ATOM   2085  O   LYS B 132       8.437   2.535  24.801  1.00 67.88           O  
ANISOU 2085  O   LYS B 132     8667   9270   7855   1894     66   1733       O  
ATOM   2086  CB  LYS B 132       5.796   3.375  22.973  1.00 70.80           C  
ANISOU 2086  CB  LYS B 132     9037   9641   8222   1896     29   1755       C  
ATOM   2087  CG  LYS B 132       4.791   2.620  22.124  1.00 72.44           C  
ANISOU 2087  CG  LYS B 132     9260   9857   8405   1906     15   1745       C  
ATOM   2088  CD  LYS B 132       4.460   3.337  20.824  1.00 76.92           C  
ANISOU 2088  CD  LYS B 132     9819  10441   8967   1916     12   1773       C  
ATOM   2089  CE  LYS B 132       3.148   2.810  20.237  1.00 78.87           C  
ANISOU 2089  CE  LYS B 132    10080  10687   9199   1919     -9   1762       C  
ATOM   2090  NZ  LYS B 132       2.710   3.565  19.033  1.00 84.09           N  
ANISOU 2090  NZ  LYS B 132    10732  11361   9856   1928    -14   1788       N  
ATOM   2091  N   VAL B 133       7.294   4.305  25.638  1.00 65.57           N  
ANISOU 2091  N   VAL B 133     8357   8942   7615   1864     45   1748       N  
ATOM   2092  CA  VAL B 133       8.462   4.934  26.216  1.00 65.34           C  
ANISOU 2092  CA  VAL B 133     8313   8909   7604   1859     59   1760       C  
ATOM   2093  C   VAL B 133       9.040   4.185  27.385  1.00 62.15           C  
ANISOU 2093  C   VAL B 133     7919   8496   7201   1854     66   1734       C  
ATOM   2094  O   VAL B 133      10.223   3.919  27.386  1.00 63.27           O  
ANISOU 2094  O   VAL B 133     8057   8649   7332   1862     83   1737       O  
ATOM   2095  CB  VAL B 133       8.157   6.337  26.682  1.00 64.61           C  
ANISOU 2095  CB  VAL B 133     8204   8796   7548   1842     51   1778       C  
ATOM   2096  CG1 VAL B 133       9.446   7.009  27.137  1.00 64.45           C  
ANISOU 2096  CG1 VAL B 133     8167   8774   7546   1838     65   1794       C  
ATOM   2097  CG2 VAL B 133       7.467   7.121  25.564  1.00 68.30           C  
ANISOU 2097  CG2 VAL B 133     8662   9273   8017   1846     43   1803       C  
ATOM   2098  N   VAL B 134       8.244   3.846  28.394  1.00 61.31           N  
ANISOU 2098  N   VAL B 134     7824   8367   7105   1841     53   1708       N  
ATOM   2099  CA  VAL B 134       8.856   3.214  29.574  1.00 60.68           C  
ANISOU 2099  CA  VAL B 134     7752   8277   7027   1835     60   1685       C  
ATOM   2100  C   VAL B 134       9.300   1.801  29.251  1.00 61.04           C  
ANISOU 2100  C   VAL B 134     7814   8341   7038   1851     70   1666       C  
ATOM   2101  O   VAL B 134      10.104   1.216  29.981  1.00 60.78           O  
ANISOU 2101  O   VAL B 134     7786   8307   7001   1852     81   1650       O  
ATOM   2102  CB  VAL B 134       7.933   3.186  30.802  1.00 59.77           C  
ANISOU 2102  CB  VAL B 134     7645   8134   6932   1818     45   1662       C  
ATOM   2103  CG1 VAL B 134       7.485   4.605  31.127  1.00 59.53           C  
ANISOU 2103  CG1 VAL B 134     7598   8085   6937   1803     34   1680       C  
ATOM   2104  CG2 VAL B 134       6.743   2.284  30.575  1.00 59.62           C  
ANISOU 2104  CG2 VAL B 134     7642   8114   6896   1821     32   1642       C  
ATOM   2105  N   ALA B 135       8.802   1.278  28.132  1.00 61.93           N  
ANISOU 2105  N   ALA B 135     7935   8471   7126   1865     66   1667       N  
ATOM   2106  CA  ALA B 135       9.288   0.010  27.614  1.00 62.65           C  
ANISOU 2106  CA  ALA B 135     8041   8582   7181   1883     76   1653       C  
ATOM   2107  C   ALA B 135      10.672   0.237  27.032  1.00 63.74           C  
ANISOU 2107  C   ALA B 135     8167   8742   7309   1897     97   1674       C  
ATOM   2108  O   ALA B 135      11.659  -0.269  27.564  1.00 63.68           O  
ANISOU 2108  O   ALA B 135     8162   8738   7296   1900    112   1663       O  
ATOM   2109  CB  ALA B 135       8.353  -0.554  26.573  1.00 63.16           C  
ANISOU 2109  CB  ALA B 135     8117   8657   7223   1894     64   1650       C  
ATOM   2110  N   GLY B 136      10.736   1.038  25.969  1.00 61.20           N  
ANISOU 2110  N   GLY B 136     7832   8435   6988   1904    100   1704       N  
ATOM   2111  CA  GLY B 136      11.984   1.306  25.268  1.00 65.07           C  
ANISOU 2111  CA  GLY B 136     8308   8948   7468   1918    120   1727       C  
ATOM   2112  C   GLY B 136      13.108   1.615  26.231  1.00 64.06           C  
ANISOU 2112  C   GLY B 136     8170   8812   7357   1910    133   1729       C  
ATOM   2113  O   GLY B 136      14.220   1.118  26.072  1.00 66.33           O  
ANISOU 2113  O   GLY B 136     8457   9116   7629   1923    151   1729       O  
ATOM   2114  N   VAL B 137      12.796   2.393  27.261  1.00 64.48           N  
ANISOU 2114  N   VAL B 137     8216   8839   7444   1889    124   1728       N  
ATOM   2115  CA  VAL B 137      13.749   2.656  28.325  1.00 63.28           C  
ANISOU 2115  CA  VAL B 137     8057   8675   7312   1879    133   1725       C  
ATOM   2116  C   VAL B 137      14.147   1.372  29.046  1.00 61.21           C  
ANISOU 2116  C   VAL B 137     7813   8413   7031   1883    140   1693       C  
ATOM   2117  O   VAL B 137      15.337   1.065  29.149  1.00 62.80           O  
ANISOU 2117  O   VAL B 137     8012   8626   7225   1891    157   1694       O  
ATOM   2118  CB  VAL B 137      13.199   3.657  29.357  1.00 60.57           C  
ANISOU 2118  CB  VAL B 137     7706   8302   7007   1856    118   1726       C  
ATOM   2119  CG1 VAL B 137      14.079   3.664  30.594  1.00 58.36           C  
ANISOU 2119  CG1 VAL B 137     7425   8008   6743   1847    126   1715       C  
ATOM   2120  CG2 VAL B 137      13.168   5.019  28.760  1.00 63.63           C  
ANISOU 2120  CG2 VAL B 137     8073   8689   7415   1852    115   1761       C  
ATOM   2121  N   ALA B 138      13.154   0.630  29.540  1.00 62.59           N  
ANISOU 2121  N   ALA B 138     8006   8575   7201   1878    127   1665       N  
ATOM   2122  CA  ALA B 138      13.418  -0.601  30.308  1.00 60.46           C  
ANISOU 2122  CA  ALA B 138     7755   8302   6916   1880    132   1632       C  
ATOM   2123  C   ALA B 138      14.290  -1.597  29.515  1.00 63.22           C  
ANISOU 2123  C   ALA B 138     8112   8680   7230   1903    149   1629       C  
ATOM   2124  O   ALA B 138      15.227  -2.196  30.058  1.00 62.83           O  
ANISOU 2124  O   ALA B 138     8067   8634   7172   1907    162   1616       O  
ATOM   2125  CB  ALA B 138      12.086  -1.264  30.751  1.00 57.78           C  
ANISOU 2125  CB  ALA B 138     7433   7948   6574   1873    114   1605       C  
ATOM   2126  N   ASN B 139      13.994  -1.738  28.224  1.00 60.63           N  
ANISOU 2126  N   ASN B 139     7785   8372   6880   1918    147   1641       N  
ATOM   2127  CA  ASN B 139      14.791  -2.575  27.345  1.00 63.93           C  
ANISOU 2127  CA  ASN B 139     8209   8817   7264   1942    163   1641       C  
ATOM   2128  C   ASN B 139      16.197  -2.056  27.154  1.00 66.61           C  
ANISOU 2128  C   ASN B 139     8530   9171   7606   1949    184   1665       C  
ATOM   2129  O   ASN B 139      17.159  -2.772  27.410  1.00 66.87           O  
ANISOU 2129  O   ASN B 139     8569   9214   7624   1958    199   1654       O  
ATOM   2130  CB  ASN B 139      14.117  -2.704  25.996  1.00 67.17           C  
ANISOU 2130  CB  ASN B 139     8624   9245   7654   1956    156   1652       C  
ATOM   2131  CG  ASN B 139      12.853  -3.498  26.080  1.00 65.08           C  
ANISOU 2131  CG  ASN B 139     8380   8969   7379   1954    136   1626       C  
ATOM   2132  OD1 ASN B 139      12.850  -4.605  26.629  1.00 62.39           O  
ANISOU 2132  OD1 ASN B 139     8057   8624   7025   1956    136   1597       O  
ATOM   2133  ND2 ASN B 139      11.745  -2.927  25.573  1.00 66.40           N  
ANISOU 2133  ND2 ASN B 139     8544   9131   7555   1948    119   1637       N  
ATOM   2134  N   ALA B 140      16.318  -0.811  26.702  1.00 64.64           N  
ANISOU 2134  N   ALA B 140     8260   8924   7376   1944    185   1697       N  
ATOM   2135  CA  ALA B 140      17.633  -0.224  26.488  1.00 67.81           C  
ANISOU 2135  CA  ALA B 140     8642   9339   7783   1950    204   1723       C  
ATOM   2136  C   ALA B 140      18.453  -0.330  27.771  1.00 65.20           C  
ANISOU 2136  C   ALA B 140     8311   8994   7468   1939    211   1710       C  
ATOM   2137  O   ALA B 140      19.642  -0.629  27.743  1.00 67.43           O  
ANISOU 2137  O   ALA B 140     8589   9292   7740   1949    229   1714       O  
ATOM   2138  CB  ALA B 140      17.510   1.215  26.041  1.00 70.02           C  
ANISOU 2138  CB  ALA B 140     8899   9617   8088   1942    200   1759       C  
ATOM   2139  N   LEU B 141      17.802  -0.117  28.900  1.00 65.06           N  
ANISOU 2139  N   LEU B 141     8298   8948   7474   1918    197   1693       N  
ATOM   2140  CA  LEU B 141      18.483  -0.203  30.164  1.00 62.56           C  
ANISOU 2140  CA  LEU B 141     7981   8616   7172   1907    202   1679       C  
ATOM   2141  C   LEU B 141      18.945  -1.638  30.406  1.00 61.73           C  
ANISOU 2141  C   LEU B 141     7896   8522   7038   1920    212   1650       C  
ATOM   2142  O   LEU B 141      19.897  -1.891  31.175  1.00 60.94           O  
ANISOU 2142  O   LEU B 141     7795   8418   6940   1919    224   1641       O  
ATOM   2143  CB  LEU B 141      17.570   0.261  31.288  1.00 58.51           C  
ANISOU 2143  CB  LEU B 141     7471   8071   6688   1885    183   1665       C  
ATOM   2144  CG  LEU B 141      18.261   0.296  32.642  1.00 56.13           C  
ANISOU 2144  CG  LEU B 141     7169   7752   6405   1873    187   1652       C  
ATOM   2145  CD1 LEU B 141      19.473   1.211  32.555  1.00 58.68           C  
ANISOU 2145  CD1 LEU B 141     7470   8080   6744   1872    199   1681       C  
ATOM   2146  CD2 LEU B 141      17.320   0.749  33.710  1.00 52.44           C  
ANISOU 2146  CD2 LEU B 141     6705   7254   5965   1852    169   1639       C  
ATOM   2147  N   ALA B 142      18.259  -2.582  29.756  1.00 64.64           N  
ANISOU 2147  N   ALA B 142     8282   8901   7378   1933    208   1634       N  
ATOM   2148  CA  ALA B 142      18.547  -4.021  29.913  1.00 64.23           C  
ANISOU 2148  CA  ALA B 142     8250   8857   7296   1946    215   1604       C  
ATOM   2149  C   ALA B 142      19.464  -4.620  28.805  1.00 68.70           C  
ANISOU 2149  C   ALA B 142     8817   9455   7829   1972    234   1613       C  
ATOM   2150  O   ALA B 142      19.716  -5.830  28.757  1.00 69.17           O  
ANISOU 2150  O   ALA B 142     8894   9525   7861   1986    240   1590       O  
ATOM   2151  CB  ALA B 142      17.222  -4.792  29.986  1.00 62.25           C  
ANISOU 2151  CB  ALA B 142     8020   8596   7035   1944    198   1578       C  
ATOM   2152  N   HIS B 143      19.944  -3.766  27.914  1.00 68.00           N  
ANISOU 2152  N   HIS B 143     8709   9384   7744   1979    242   1647       N  
ATOM   2153  CA  HIS B 143      20.632  -4.218  26.716  1.00 72.99           C  
ANISOU 2153  CA  HIS B 143     9340  10047   8345   2005    257   1659       C  
ATOM   2154  C   HIS B 143      21.974  -4.908  26.959  1.00 74.31           C  
ANISOU 2154  C   HIS B 143     9509  10229   8496   2018    279   1652       C  
ATOM   2155  O   HIS B 143      22.341  -5.817  26.210  1.00 77.61           O  
ANISOU 2155  O   HIS B 143     9937  10670   8880   2041    289   1645       O  
ATOM   2156  CB  HIS B 143      20.858  -3.037  25.772  1.00 76.84           C  
ANISOU 2156  CB  HIS B 143     9805  10549   8843   2008    262   1700       C  
ATOM   2157  CG  HIS B 143      21.724  -3.368  24.594  1.00 82.58           C  
ANISOU 2157  CG  HIS B 143    10527  11310   9541   2035    281   1716       C  
ATOM   2158  ND1 HIS B 143      21.449  -4.415  23.738  1.00 85.43           N  
ANISOU 2158  ND1 HIS B 143    10906  11689   9865   2057    281   1702       N  
ATOM   2159  CD2 HIS B 143      22.866  -2.802  24.138  1.00 86.40           C  
ANISOU 2159  CD2 HIS B 143    10989  11812  10026   2044    300   1746       C  
ATOM   2160  CE1 HIS B 143      22.374  -4.468  22.795  1.00 90.80           C  
ANISOU 2160  CE1 HIS B 143    11576  12398  10524   2080    300   1722       C  
ATOM   2161  NE2 HIS B 143      23.247  -3.501  23.016  1.00 91.52           N  
ANISOU 2161  NE2 HIS B 143    11643  12491  10639   2072    312   1749       N  
ATOM   2162  N   LYS B 144      22.707  -4.473  27.986  1.00 69.94           N  
ANISOU 2162  N   LYS B 144     8946   9662   7966   2004    285   1654       N  
ATOM   2163  CA  LYS B 144      24.014  -5.055  28.318  1.00 71.39           C  
ANISOU 2163  CA  LYS B 144     9129   9858   8138   2014    305   1647       C  
ATOM   2164  C   LYS B 144      23.877  -6.443  28.999  1.00 69.10           C  
ANISOU 2164  C   LYS B 144     8865   9561   7827   2018    304   1606       C  
ATOM   2165  O   LYS B 144      24.878  -7.071  29.381  1.00 70.06           O  
ANISOU 2165  O   LYS B 144     8990   9691   7937   2027    320   1595       O  
ATOM   2166  CB  LYS B 144      24.827  -4.092  29.193  1.00 70.62           C  
ANISOU 2166  CB  LYS B 144     9012   9747   8074   1997    310   1664       C  
ATOM   2167  CG  LYS B 144      25.292  -2.818  28.471  1.00 74.32           C  
ANISOU 2167  CG  LYS B 144     9453  10226   8560   1996    316   1707       C  
ATOM   2168  CD  LYS B 144      26.464  -3.039  27.503  1.00 78.79           C  
ANISOU 2168  CD  LYS B 144    10008  10825   9102   2020    339   1728       C  
ATOM   2169  CE  LYS B 144      27.805  -3.082  28.242  1.00 81.59           C  
ANISOU 2169  CE  LYS B 144    10354  11180   9465   2019    355   1729       C  
ATOM   2170  NZ  LYS B 144      28.858  -3.924  27.566  1.00 85.69           N  
ANISOU 2170  NZ  LYS B 144    10875  11731   9952   2045    378   1730       N  
ATOM   2171  N   TYR B 145      22.633  -6.883  29.192  1.00 70.52           N  
ANISOU 2171  N   TYR B 145     9062   9726   8005   2012    286   1584       N  
ATOM   2172  CA  TYR B 145      22.335  -8.215  29.717  1.00 68.66           C  
ANISOU 2172  CA  TYR B 145     8852   9485   7749   2016    283   1545       C  
ATOM   2173  C   TYR B 145      22.504  -9.305  28.656  1.00 72.49           C  
ANISOU 2173  C   TYR B 145     9353   9996   8195   2044    290   1537       C  
ATOM   2174  O   TYR B 145      22.558 -10.500  28.974  1.00 72.26           O  
ANISOU 2174  O   TYR B 145     9344   9967   8144   2052    292   1506       O  
ATOM   2175  CB  TYR B 145      20.910  -8.251  30.286  1.00 64.71           C  
ANISOU 2175  CB  TYR B 145     8364   8960   7263   1998    260   1527       C  
ATOM   2176  CG  TYR B 145      20.875  -8.103  31.781  1.00 60.57           C  
ANISOU 2176  CG  TYR B 145     7841   8409   6764   1977    256   1511       C  
ATOM   2177  CD1 TYR B 145      21.779  -8.792  32.569  1.00 60.02           C  
ANISOU 2177  CD1 TYR B 145     7778   8339   6687   1980    269   1492       C  
ATOM   2178  CD2 TYR B 145      19.959  -7.270  32.401  1.00 57.58           C  
ANISOU 2178  CD2 TYR B 145     7456   8006   6415   1955    239   1514       C  
ATOM   2179  CE1 TYR B 145      21.773  -8.661  33.942  1.00 56.67           C  
ANISOU 2179  CE1 TYR B 145     7355   7892   6285   1962    266   1477       C  
ATOM   2180  CE2 TYR B 145      19.947  -7.124  33.774  1.00 54.27           C  
ANISOU 2180  CE2 TYR B 145     7038   7564   6019   1937    235   1499       C  
ATOM   2181  CZ  TYR B 145      20.861  -7.825  34.547  1.00 53.87           C  
ANISOU 2181  CZ  TYR B 145     6994   7513   5960   1940    249   1480       C  
ATOM   2182  OH  TYR B 145      20.882  -7.716  35.931  1.00 51.01           O  
ANISOU 2182  OH  TYR B 145     6634   7128   5618   1924    246   1465       O  
ATOM   2183  N   HIS B 146      22.556  -8.879  27.396  1.00 69.95           N  
ANISOU 2183  N   HIS B 146     9021   9696   7862   2058    293   1563       N  
ATOM   2184  CA  HIS B 146      22.957  -9.741  26.290  1.00 74.49           C  
ANISOU 2184  CA  HIS B 146     9605  10298   8399   2087    304   1560       C  
ATOM   2185  C   HIS B 146      23.993  -8.995  25.399  1.00 79.47           C  
ANISOU 2185  C   HIS B 146    10212  10955   9027   2101    323   1597       C  
ATOM   2186  O   HIS B 146      24.765  -8.131  25.849  1.00 79.37           O  
ANISOU 2186  O   HIS B 146    10179  10940   9038   2090    333   1618       O  
ATOM   2187  CB  HIS B 146      21.736 -10.201  25.469  1.00 75.26           C  
ANISOU 2187  CB  HIS B 146     9719  10398   8479   2095    285   1551       C  
ATOM   2188  CG  HIS B 146      20.418  -9.658  25.950  1.00 77.63           C  
ANISOU 2188  CG  HIS B 146    10020  10672   8805   2071    262   1548       C  
ATOM   2189  ND1 HIS B 146      19.763 -10.152  27.064  1.00 78.76           N  
ANISOU 2189  ND1 HIS B 146    10178  10790   8959   2054    250   1519       N  
ATOM   2190  CD2 HIS B 146      19.608  -8.695  25.442  1.00 79.44           C  
ANISOU 2190  CD2 HIS B 146    10238  10897   9049   2062    249   1570       C  
ATOM   2191  CE1 HIS B 146      18.619  -9.506  27.231  1.00 81.28           C  
ANISOU 2191  CE1 HIS B 146    10494  11090   9299   2036    230   1523       C  
ATOM   2192  NE2 HIS B 146      18.501  -8.615  26.260  1.00 81.72           N  
ANISOU 2192  NE2 HIS B 146    10534  11158   9358   2040    230   1554       N  
ATOM   2193  OXT HIS B 146      24.122  -9.224  24.193  1.00 84.21           O  
ANISOU 2193  OXT HIS B 146    10814  11581   9602   2124    329   1609       O  
TER    2194      HIS B 146                                                      
ATOM   2195  N   CYS C  92      54.156 -40.417  27.516  1.00 80.30           N  
ANISOU 2195  N   CYS C  92     7925   8247  14338    896    543    156       N  
ATOM   2196  CA  CYS C  92      55.526 -40.089  27.860  1.00 84.27           C  
ANISOU 2196  CA  CYS C  92     8391   8789  14838    928    489    175       C  
ATOM   2197  C   CYS C  92      56.255 -39.358  26.746  1.00 86.32           C  
ANISOU 2197  C   CYS C  92     8600   9086  15110    883    463    136       C  
ATOM   2198  O   CYS C  92      56.595 -39.968  25.720  1.00 86.79           O  
ANISOU 2198  O   CYS C  92     8631   9130  15217    867    505    113       O  
ATOM   2199  CB  CYS C  92      56.321 -41.342  28.195  1.00 87.02           C  
ANISOU 2199  CB  CYS C  92     8730   9110  15225    989    521    209       C  
ATOM   2200  SG  CYS C  92      56.362 -42.571  26.853  1.00 89.04           S  
ANISOU 2200  SG  CYS C  92     8961   9320  15549    972    605    182       S  
ATOM   2201  N   PRO C  93      56.523 -38.051  26.960  1.00 82.76           N  
ANISOU 2201  N   PRO C  93     8140   8687  14619    862    393    128       N  
ATOM   2202  CA  PRO C  93      57.607 -37.316  26.280  1.00 86.30           C  
ANISOU 2202  CA  PRO C  93     8537   9181  15073    838    350    105       C  
ATOM   2203  C   PRO C  93      58.939 -37.899  26.736  1.00 89.07           C  
ANISOU 2203  C   PRO C  93     8857   9541  15446    897    337    138       C  
ATOM   2204  O   PRO C  93      59.550 -37.315  27.646  1.00 90.54           O  
ANISOU 2204  O   PRO C  93     9040   9762  15600    927    277    164       O  
ATOM   2205  CB  PRO C  93      57.446 -35.881  26.779  1.00 86.68           C  
ANISOU 2205  CB  PRO C  93     8595   9275  15064    817    278    101       C  
ATOM   2206  CG  PRO C  93      55.949 -35.778  27.086  1.00 82.61           C  
ANISOU 2206  CG  PRO C  93     8132   8734  14521    797    299     98       C  
ATOM   2207  CD  PRO C  93      55.517 -37.146  27.555  1.00 80.71           C  
ANISOU 2207  CD  PRO C  93     7920   8439  14306    842    361    127       C  
ATOM   2208  N   LYS C  94      59.380 -38.991  26.082  1.00 76.77           N  
ANISOU 2208  N   LYS C  94     7276   7953  13941    910    391    134       N  
ATOM   2209  CA  LYS C  94      60.277 -40.029  26.628  1.00 78.28           C  
ANISOU 2209  CA  LYS C  94     7454   8128  14160    976    405    171       C  
ATOM   2210  C   LYS C  94      61.420 -39.510  27.470  1.00 80.74           C  
ANISOU 2210  C   LYS C  94     7744   8484  14449   1017    338    199       C  
ATOM   2211  O   LYS C  94      62.100 -38.580  27.066  1.00 83.29           O  
ANISOU 2211  O   LYS C  94     8031   8853  14762    989    290    179       O  
ATOM   2212  CB  LYS C  94      60.894 -40.831  25.476  1.00 80.66           C  
ANISOU 2212  CB  LYS C  94     7715   8413  14520    966    452    148       C  
ATOM   2213  CG  LYS C  94      60.002 -41.880  24.802  1.00 81.01           C  
ANISOU 2213  CG  LYS C  94     7779   8400  14602    951    534    134       C  
ATOM   2214  CD  LYS C  94      60.895 -42.897  24.021  1.00 84.53           C  
ANISOU 2214  CD  LYS C  94     8184   8828  15106    967    576    127       C  
ATOM   2215  CE  LYS C  94      60.118 -44.088  23.428  1.00 84.76           C  
ANISOU 2215  CE  LYS C  94     8233   8797  15176    962    660    118       C  
ATOM   2216  NZ  LYS C  94      59.541 -44.995  24.463  1.00 85.00           N  
ANISOU 2216  NZ  LYS C  94     8310   8784  15202   1013    691    159       N  
ATOM   2217  N   PRO C  95      61.633 -40.119  28.647  1.00 72.74           N  
ANISOU 2217  N   PRO C  95     6753   7457  13429   1083    334    246       N  
ATOM   2218  CA  PRO C  95      62.690 -39.687  29.555  1.00 75.29           C  
ANISOU 2218  CA  PRO C  95     7058   7819  13729   1127    271    277       C  
ATOM   2219  C   PRO C  95      64.052 -39.956  28.928  1.00 79.02           C  
ANISOU 2219  C   PRO C  95     7473   8312  14240   1138    265    268       C  
ATOM   2220  O   PRO C  95      64.180 -40.872  28.112  1.00 79.06           O  
ANISOU 2220  O   PRO C  95     7461   8286  14292   1135    321    253       O  
ATOM   2221  CB  PRO C  95      62.465 -40.557  30.793  1.00 73.80           C  
ANISOU 2221  CB  PRO C  95     6910   7597  13534   1194    287    326       C  
ATOM   2222  CG  PRO C  95      61.983 -41.818  30.233  1.00 72.11           C  
ANISOU 2222  CG  PRO C  95     6708   7327  13365   1197    367    322       C  
ATOM   2223  CD  PRO C  95      61.084 -41.415  29.069  1.00 70.62           C  
ANISOU 2223  CD  PRO C  95     6519   7131  13182   1123    395    273       C  
ATOM   2224  N   PRO C  96      65.057 -39.156  29.279  1.00 71.72           N  
ANISOU 2224  N   PRO C  96     6518   7439  13294   1149    199    274       N  
ATOM   2225  CA  PRO C  96      66.378 -39.419  28.721  1.00 75.61           C  
ANISOU 2225  CA  PRO C  96     6954   7951  13822   1162    193    266       C  
ATOM   2226  C   PRO C  96      66.958 -40.678  29.349  1.00 76.06           C  
ANISOU 2226  C   PRO C  96     7013   7979  13908   1235    221    304       C  
ATOM   2227  O   PRO C  96      66.556 -41.032  30.469  1.00 74.39           O  
ANISOU 2227  O   PRO C  96     6842   7747  13675   1281    220    343       O  
ATOM   2228  CB  PRO C  96      67.183 -38.171  29.106  1.00 78.64           C  
ANISOU 2228  CB  PRO C  96     7312   8398  14168   1157    112    266       C  
ATOM   2229  CG  PRO C  96      66.498 -37.651  30.326  1.00 77.49           C  
ANISOU 2229  CG  PRO C  96     7215   8257  13972   1176     76    295       C  
ATOM   2230  CD  PRO C  96      65.044 -38.002  30.189  1.00 72.11           C  
ANISOU 2230  CD  PRO C  96     6581   7529  13288   1152    128    288       C  
ATOM   2231  N   GLU C  97      67.864 -41.346  28.632  1.00 73.59           N  
ANISOU 2231  N   GLU C  97     6657   7663  13642   1245    245    293       N  
ATOM   2232  CA  GLU C  97      68.554 -42.524  29.147  1.00 74.57           C  
ANISOU 2232  CA  GLU C  97     6775   7762  13795   1314    268    327       C  
ATOM   2233  C   GLU C  97      69.706 -42.122  30.044  1.00 77.84           C  
ANISOU 2233  C   GLU C  97     7167   8220  14188   1362    203    355       C  
ATOM   2234  O   GLU C  97      70.308 -41.057  29.866  1.00 80.46           O  
ANISOU 2234  O   GLU C  97     7466   8604  14500   1336    147    338       O  
ATOM   2235  CB  GLU C  97      69.076 -43.393  28.007  1.00 76.10           C  
ANISOU 2235  CB  GLU C  97     6931   7937  14047   1306    319    303       C  
ATOM   2236  CG  GLU C  97      68.537 -43.029  26.634  1.00 73.29           C  
ANISOU 2236  CG  GLU C  97     6561   7579  13708   1230    348    253       C  
ATOM   2237  CD  GLU C  97      68.090 -44.265  25.870  1.00 70.71           C  
ANISOU 2237  CD  GLU C  97     6240   7197  13430   1227    429    242       C  
ATOM   2238  OE1 GLU C  97      68.983 -45.067  25.456  1.00 71.39           O  
ANISOU 2238  OE1 GLU C  97     6291   7276  13559   1253    452    241       O  
ATOM   2239  OE2 GLU C  97      66.841 -44.439  25.715  1.00 68.23           O  
ANISOU 2239  OE2 GLU C  97     5966   6846  13111   1199    469    234       O  
ATOM   2240  N   ILE C  98      70.016 -42.972  31.011  1.00 68.80           N  
ANISOU 2240  N   ILE C  98     6040   7053  13048   1433    210    398       N  
ATOM   2241  CA  ILE C  98      71.288 -42.845  31.700  1.00 70.17           C  
ANISOU 2241  CA  ILE C  98     6183   7264  13215   1484    158    422       C  
ATOM   2242  C   ILE C  98      72.160 -44.071  31.409  1.00 71.78           C  
ANISOU 2242  C   ILE C  98     6359   7445  13471   1529    196    430       C  
ATOM   2243  O   ILE C  98      71.655 -45.155  31.095  1.00 72.06           O  
ANISOU 2243  O   ILE C  98     6413   7428  13538   1538    262    433       O  
ATOM   2244  CB  ILE C  98      71.121 -42.657  33.214  1.00 70.77           C  
ANISOU 2244  CB  ILE C  98     6300   7344  13247   1535    119    468       C  
ATOM   2245  CG1 ILE C  98      70.654 -43.935  33.883  1.00 71.87           C  
ANISOU 2245  CG1 ILE C  98     6481   7425  13400   1590    169    505       C  
ATOM   2246  CG2 ILE C  98      70.158 -41.562  33.490  1.00 69.18           C  
ANISOU 2246  CG2 ILE C  98     6131   7158  12998   1493     89    461       C  
ATOM   2247  CD1 ILE C  98      70.459 -43.782  35.374  1.00 72.49           C  
ANISOU 2247  CD1 ILE C  98     6601   7505  13435   1641    133    551       C  
ATOM   2248  N   ALA C  99      73.476 -43.873  31.490  1.00 71.56           N  
ANISOU 2248  N   ALA C  99     6284   7458  13449   1555    154    433       N  
ATOM   2249  CA  ALA C  99      74.447 -44.928  31.250  1.00 74.30           C  
ANISOU 2249  CA  ALA C  99     6598   7791  13842   1600    181    440       C  
ATOM   2250  C   ALA C  99      74.212 -46.137  32.161  1.00 73.01           C  
ANISOU 2250  C   ALA C  99     6475   7577  13687   1669    216    484       C  
ATOM   2251  O   ALA C  99      74.158 -45.997  33.389  1.00 73.08           O  
ANISOU 2251  O   ALA C  99     6515   7591  13662   1713    182    522       O  
ATOM   2252  CB  ALA C  99      75.834 -44.385  31.439  1.00 78.90           C  
ANISOU 2252  CB  ALA C  99     7130   8430  14420   1621    120    441       C  
ATOM   2253  N   HIS C 100      74.072 -47.310  31.541  1.00 75.07           N  
ANISOU 2253  N   HIS C 100     6737   7791  13995   1677    283    479       N  
ATOM   2254  CA  HIS C 100      73.863 -48.587  32.238  1.00 74.18           C  
ANISOU 2254  CA  HIS C 100     6662   7626  13898   1740    325    517       C  
ATOM   2255  C   HIS C 100      72.633 -48.598  33.149  1.00 70.63           C  
ANISOU 2255  C   HIS C 100     6279   7144  13412   1748    335    545       C  
ATOM   2256  O   HIS C 100      72.636 -49.201  34.220  1.00 70.95           O  
ANISOU 2256  O   HIS C 100     6353   7163  13443   1810    335    587       O  
ATOM   2257  CB  HIS C 100      75.116 -48.967  33.056  1.00 77.81           C  
ANISOU 2257  CB  HIS C 100     7100   8104  14361   1815    290    550       C  
ATOM   2258  CG  HIS C 100      76.296 -49.349  32.215  1.00 81.03           C  
ANISOU 2258  CG  HIS C 100     7446   8528  14812   1821    296    528       C  
ATOM   2259  ND1 HIS C 100      76.545 -50.650  31.822  1.00 81.86           N  
ANISOU 2259  ND1 HIS C 100     7546   8591  14965   1853    353    531       N  
ATOM   2260  CD2 HIS C 100      77.282 -48.596  31.674  1.00 83.76           C  
ANISOU 2260  CD2 HIS C 100     7734   8929  15161   1799    253    501       C  
ATOM   2261  CE1 HIS C 100      77.636 -50.682  31.081  1.00 84.89           C  
ANISOU 2261  CE1 HIS C 100     7870   9003  15380   1850    344    508       C  
ATOM   2262  NE2 HIS C 100      78.105 -49.450  30.979  1.00 86.14           N  
ANISOU 2262  NE2 HIS C 100     7996   9220  15512   1817    285    489       N  
ATOM   2263  N   GLY C 101      71.556 -47.966  32.718  1.00 78.34           N  
ANISOU 2263  N   GLY C 101     7277   8117  14371   1686    345    520       N  
ATOM   2264  CA  GLY C 101      70.419 -47.897  33.608  1.00 75.05           C  
ANISOU 2264  CA  GLY C 101     6923   7676  13918   1693    350    546       C  
ATOM   2265  C   GLY C 101      69.089 -47.859  32.913  1.00 71.48           C  
ANISOU 2265  C   GLY C 101     6500   7193  13468   1632    398    519       C  
ATOM   2266  O   GLY C 101      69.008 -47.478  31.747  1.00 71.55           O  
ANISOU 2266  O   GLY C 101     6479   7213  13494   1573    410    476       O  
ATOM   2267  N   TYR C 102      68.043 -48.243  33.639  1.00 71.97           N  
ANISOU 2267  N   TYR C 102     6620   7215  13511   1648    424    544       N  
ATOM   2268  CA  TYR C 102      66.731 -48.361  33.037  1.00 68.77           C  
ANISOU 2268  CA  TYR C 102     6245   6774  13110   1596    475    521       C  
ATOM   2269  C   TYR C 102      65.704 -47.693  33.870  1.00 66.11           C  
ANISOU 2269  C   TYR C 102     5958   6439  12723   1585    453    535       C  
ATOM   2270  O   TYR C 102      65.931 -47.346  35.031  1.00 66.82           O  
ANISOU 2270  O   TYR C 102     6065   6547  12775   1626    407    569       O  
ATOM   2271  CB  TYR C 102      66.326 -49.814  32.823  1.00 68.14           C  
ANISOU 2271  CB  TYR C 102     6189   6630  13071   1620    553    531       C  
ATOM   2272  CG  TYR C 102      66.120 -50.646  34.080  1.00 67.96           C  
ANISOU 2272  CG  TYR C 102     6214   6571  13036   1688    566    582       C  
ATOM   2273  CD1 TYR C 102      64.916 -50.630  34.764  1.00 65.39           C  
ANISOU 2273  CD1 TYR C 102     5947   6219  12680   1684    580    599       C  
ATOM   2274  CD2 TYR C 102      67.111 -51.503  34.541  1.00 70.57           C  
ANISOU 2274  CD2 TYR C 102     6533   6892  13390   1755    567    612       C  
ATOM   2275  CE1 TYR C 102      64.715 -51.409  35.899  1.00 65.58           C  
ANISOU 2275  CE1 TYR C 102     6016   6208  12693   1745    594    645       C  
ATOM   2276  CE2 TYR C 102      66.917 -52.293  35.673  1.00 70.73           C  
ANISOU 2276  CE2 TYR C 102     6599   6877  13400   1817    580    658       C  
ATOM   2277  CZ  TYR C 102      65.714 -52.244  36.353  1.00 68.30           C  
ANISOU 2277  CZ  TYR C 102     6349   6543  13060   1811    594    675       C  
ATOM   2278  OH  TYR C 102      65.508 -53.030  37.479  1.00 68.79           O  
ANISOU 2278  OH  TYR C 102     6457   6569  13110   1872    608    721       O  
ATOM   2279  N   VAL C 103      64.549 -47.565  33.237  1.00 72.10           N  
ANISOU 2279  N   VAL C 103     6739   7176  13481   1530    491    507       N  
ATOM   2280  CA  VAL C 103      63.409 -46.805  33.703  1.00 69.05           C  
ANISOU 2280  CA  VAL C 103     6394   6792  13049   1500    476    507       C  
ATOM   2281  C   VAL C 103      62.234 -47.711  34.094  1.00 66.49           C  
ANISOU 2281  C   VAL C 103     6128   6409  12727   1512    536    525       C  
ATOM   2282  O   VAL C 103      61.917 -48.686  33.394  1.00 66.14           O  
ANISOU 2282  O   VAL C 103     6086   6320  12723   1504    602    513       O  
ATOM   2283  CB  VAL C 103      62.994 -45.843  32.595  1.00 67.72           C  
ANISOU 2283  CB  VAL C 103     6205   6650  12877   1421    468    456       C  
ATOM   2284  CG1 VAL C 103      61.484 -45.710  32.503  1.00 67.11           C  
ANISOU 2284  CG1 VAL C 103     6173   6543  12781   1379    501    443       C  
ATOM   2285  CG2 VAL C 103      63.709 -44.506  32.777  1.00 67.74           C  
ANISOU 2285  CG2 VAL C 103     6176   6718  12845   1407    388    449       C  
ATOM   2286  N   GLU C 104      61.608 -47.416  35.229  1.00 73.17           N  
ANISOU 2286  N   GLU C 104     7019   7253  13529   1532    514    555       N  
ATOM   2287  CA  GLU C 104      60.349 -48.075  35.584  1.00 70.62           C  
ANISOU 2287  CA  GLU C 104     6752   6878  13201   1533    567    567       C  
ATOM   2288  C   GLU C 104      59.130 -47.122  35.545  1.00 67.57           C  
ANISOU 2288  C   GLU C 104     6395   6503  12776   1478    556    545       C  
ATOM   2289  O   GLU C 104      58.994 -46.221  36.377  1.00 67.02           O  
ANISOU 2289  O   GLU C 104     6341   6465  12659   1482    501    560       O  
ATOM   2290  CB  GLU C 104      60.442 -48.702  36.965  1.00 71.47           C  
ANISOU 2290  CB  GLU C 104     6899   6965  13291   1605    562    621       C  
ATOM   2291  CG  GLU C 104      59.116 -49.320  37.358  1.00 69.05           C  
ANISOU 2291  CG  GLU C 104     6652   6608  12977   1603    615    634       C  
ATOM   2292  CD  GLU C 104      59.058 -49.730  38.809  1.00 70.02           C  
ANISOU 2292  CD  GLU C 104     6818   6714  13072   1668    604    687       C  
ATOM   2293  OE1 GLU C 104      59.162 -48.833  39.677  1.00 70.22           O  
ANISOU 2293  OE1 GLU C 104     6853   6777  13052   1680    543    704       O  
ATOM   2294  OE2 GLU C 104      58.897 -50.950  39.072  1.00 70.78           O  
ANISOU 2294  OE2 GLU C 104     6942   6760  13193   1705    657    710       O  
ATOM   2295  N   HIS C 105      58.233 -47.328  34.595  1.00 72.81           N  
ANISOU 2295  N   HIS C 105     7066   7140  13460   1426    608    511       N  
ATOM   2296  CA  HIS C 105      57.156 -46.364  34.404  1.00 69.97           C  
ANISOU 2296  CA  HIS C 105     6726   6794  13066   1368    596    484       C  
ATOM   2297  C   HIS C 105      55.985 -46.440  35.403  1.00 67.57           C  
ANISOU 2297  C   HIS C 105     6483   6465  12725   1380    607    508       C  
ATOM   2298  O   HIS C 105      55.477 -47.523  35.726  1.00 67.16           O  
ANISOU 2298  O   HIS C 105     6466   6362  12689   1407    662    529       O  
ATOM   2299  CB  HIS C 105      56.593 -46.511  32.997  1.00 68.91           C  
ANISOU 2299  CB  HIS C 105     6577   6641  12965   1306    647    435       C  
ATOM   2300  CG  HIS C 105      57.291 -45.675  31.985  1.00 70.31           C  
ANISOU 2300  CG  HIS C 105     6700   6862  13151   1263    613    397       C  
ATOM   2301  ND1 HIS C 105      58.440 -46.084  31.354  1.00 73.04           N  
ANISOU 2301  ND1 HIS C 105     6999   7216  13538   1276    617    390       N  
ATOM   2302  CD2 HIS C 105      57.006 -44.445  31.503  1.00 69.53           C  
ANISOU 2302  CD2 HIS C 105     6589   6802  13027   1207    575    363       C  
ATOM   2303  CE1 HIS C 105      58.833 -45.143  30.515  1.00 74.05           C  
ANISOU 2303  CE1 HIS C 105     7086   7385  13664   1229    584    353       C  
ATOM   2304  NE2 HIS C 105      57.984 -44.136  30.591  1.00 71.93           N  
ANISOU 2304  NE2 HIS C 105     6838   7136  13355   1186    557    336       N  
ATOM   2305  N   SER C 106      55.529 -45.282  35.861  1.00 69.77           N  
ANISOU 2305  N   SER C 106     6777   6779  12955   1357    557    504       N  
ATOM   2306  CA  SER C 106      54.289 -45.219  36.625  1.00 67.27           C  
ANISOU 2306  CA  SER C 106     6515   6441  12602   1355    569    518       C  
ATOM   2307  C   SER C 106      53.383 -44.176  36.007  1.00 64.95           C  
ANISOU 2307  C   SER C 106     6225   6168  12285   1285    556    476       C  
ATOM   2308  O   SER C 106      53.870 -43.246  35.356  1.00 65.65           O  
ANISOU 2308  O   SER C 106     6275   6300  12369   1250    515    446       O  
ATOM   2309  CB  SER C 106      54.547 -44.880  38.096  1.00 67.99           C  
ANISOU 2309  CB  SER C 106     6631   6552  12649   1407    516    564       C  
ATOM   2310  OG  SER C 106      54.829 -46.033  38.865  1.00 70.10           O  
ANISOU 2310  OG  SER C 106     6920   6782  12931   1471    545    607       O  
ATOM   2311  N   VAL C 107      52.075 -44.343  36.177  1.00 69.01           N  
ANISOU 2311  N   VAL C 107     6784   6652  12784   1266    593    471       N  
ATOM   2312  CA  VAL C 107      51.135 -43.255  35.935  1.00 66.66           C  
ANISOU 2312  CA  VAL C 107     6499   6378  12451   1209    570    440       C  
ATOM   2313  C   VAL C 107      50.257 -43.117  37.158  1.00 65.11           C  
ANISOU 2313  C   VAL C 107     6356   6173  12209   1231    560    469       C  
ATOM   2314  O   VAL C 107      49.986 -44.112  37.837  1.00 65.27           O  
ANISOU 2314  O   VAL C 107     6409   6152  12237   1272    600    502       O  
ATOM   2315  CB  VAL C 107      50.245 -43.473  34.707  1.00 65.24           C  
ANISOU 2315  CB  VAL C 107     6318   6172  12298   1150    627    393       C  
ATOM   2316  CG1 VAL C 107      51.077 -43.485  33.456  1.00 66.86           C  
ANISOU 2316  CG1 VAL C 107     6470   6389  12545   1123    633    361       C  
ATOM   2317  CG2 VAL C 107      49.467 -44.737  34.846  1.00 64.67           C  
ANISOU 2317  CG2 VAL C 107     6283   6040  12250   1166    702    407       C  
ATOM   2318  N   ARG C 108      49.857 -41.883  37.459  1.00 67.91           N  
ANISOU 2318  N   ARG C 108     6719   6566  12516   1204    506    458       N  
ATOM   2319  CA  ARG C 108      48.887 -41.609  38.506  1.00 66.30           C  
ANISOU 2319  CA  ARG C 108     6566   6358  12267   1213    496    478       C  
ATOM   2320  C   ARG C 108      47.667 -41.005  37.838  1.00 63.67           C  
ANISOU 2320  C   ARG C 108     6247   6025  11919   1148    511    434       C  
ATOM   2321  O   ARG C 108      47.765 -39.999  37.147  1.00 63.38           O  
ANISOU 2321  O   ARG C 108     6183   6025  11872   1102    475    399       O  
ATOM   2322  CB  ARG C 108      49.454 -40.672  39.574  1.00 67.62           C  
ANISOU 2322  CB  ARG C 108     6734   6572  12387   1243    416    506       C  
ATOM   2323  CG  ARG C 108      48.423 -40.097  40.578  1.00 65.95           C  
ANISOU 2323  CG  ARG C 108     6571   6366  12121   1244    394    519       C  
ATOM   2324  CD  ARG C 108      49.050 -39.081  41.595  1.00 67.43           C  
ANISOU 2324  CD  ARG C 108     6755   6603  12261   1271    310    545       C  
ATOM   2325  NE  ARG C 108      49.589 -39.722  42.813  1.00 69.52           N  
ANISOU 2325  NE  ARG C 108     7038   6856  12519   1343    302    600       N  
ATOM   2326  CZ  ARG C 108      50.893 -39.888  43.126  1.00 72.86           C  
ANISOU 2326  CZ  ARG C 108     7433   7297  12955   1388    271    625       C  
ATOM   2327  NH1 ARG C 108      51.875 -39.441  42.330  1.00 74.76           N  
ANISOU 2327  NH1 ARG C 108     7622   7570  13215   1371    242    603       N  
ATOM   2328  NH2 ARG C 108      51.230 -40.503  44.267  1.00 74.58           N  
ANISOU 2328  NH2 ARG C 108     7673   7499  13164   1453    268    674       N  
ATOM   2329  N   TYR C 109      46.517 -41.649  38.009  1.00 63.31           N  
ANISOU 2329  N   TYR C 109     6243   5938  11874   1143    566    436       N  
ATOM   2330  CA  TYR C 109      45.291 -41.189  37.385  1.00 60.96           C  
ANISOU 2330  CA  TYR C 109     5962   5636  11565   1083    586    394       C  
ATOM   2331  C   TYR C 109      44.711 -40.091  38.233  1.00 59.67           C  
ANISOU 2331  C   TYR C 109     5825   5505  11342   1076    531    400       C  
ATOM   2332  O   TYR C 109      44.712 -40.187  39.458  1.00 60.12           O  
ANISOU 2332  O   TYR C 109     5911   5561  11370   1122    511    441       O  
ATOM   2333  CB  TYR C 109      44.292 -42.325  37.225  1.00 60.15           C  
ANISOU 2333  CB  TYR C 109     5892   5475  11487   1079    668    392       C  
ATOM   2334  CG  TYR C 109      44.494 -43.126  35.975  1.00 60.96           C  
ANISOU 2334  CG  TYR C 109     5966   5548  11647   1057    726    365       C  
ATOM   2335  CD1 TYR C 109      45.125 -44.348  36.018  1.00 63.01           C  
ANISOU 2335  CD1 TYR C 109     6220   5773  11948   1100    768    391       C  
ATOM   2336  CD2 TYR C 109      44.061 -42.663  34.750  1.00 59.94           C  
ANISOU 2336  CD2 TYR C 109     5818   5427  11531    994    738    313       C  
ATOM   2337  CE1 TYR C 109      45.325 -45.104  34.870  1.00 64.07           C  
ANISOU 2337  CE1 TYR C 109     6329   5880  12136   1080    821    366       C  
ATOM   2338  CE2 TYR C 109      44.250 -43.404  33.597  1.00 61.05           C  
ANISOU 2338  CE2 TYR C 109     5932   5541  11725    974    792    288       C  
ATOM   2339  CZ  TYR C 109      44.886 -44.632  33.664  1.00 63.14           C  
ANISOU 2339  CZ  TYR C 109     6190   5770  12030   1017    833    315       C  
ATOM   2340  OH  TYR C 109      45.095 -45.410  32.542  1.00 64.51           O  
ANISOU 2340  OH  TYR C 109     6338   5916  12256   1000    887    291       O  
ATOM   2341  N   GLN C 110      44.246 -39.031  37.584  1.00 65.07           N  
ANISOU 2341  N   GLN C 110     6499   6218  12005   1020    504    358       N  
ATOM   2342  CA  GLN C 110      43.557 -37.952  38.280  1.00 63.69           C  
ANISOU 2342  CA  GLN C 110     6351   6074  11773   1007    455    357       C  
ATOM   2343  C   GLN C 110      42.388 -37.511  37.442  1.00 61.40           C  
ANISOU 2343  C   GLN C 110     6071   5780  11477    943    478    308       C  
ATOM   2344  O   GLN C 110      42.484 -37.505  36.214  1.00 61.30           O  
ANISOU 2344  O   GLN C 110     6029   5765  11496    902    499    269       O  
ATOM   2345  CB  GLN C 110      44.477 -36.766  38.546  1.00 65.05           C  
ANISOU 2345  CB  GLN C 110     6497   6304  11916   1010    371    361       C  
ATOM   2346  CG  GLN C 110      45.693 -37.091  39.389  1.00 67.35           C  
ANISOU 2346  CG  GLN C 110     6775   6605  12210   1073    341    407       C  
ATOM   2347  CD  GLN C 110      46.503 -35.859  39.695  1.00 69.17           C  
ANISOU 2347  CD  GLN C 110     6982   6894  12407   1075    256    410       C  
ATOM   2348  OE1 GLN C 110      45.981 -34.743  39.619  1.00 68.81           O  
ANISOU 2348  OE1 GLN C 110     6942   6879  12324   1036    217    386       O  
ATOM   2349  NE2 GLN C 110      47.787 -36.041  40.033  1.00 71.54           N  
ANISOU 2349  NE2 GLN C 110     7254   7210  12719   1118    228    438       N  
ATOM   2350  N   CYS C 111      41.296 -37.141  38.109  1.00 64.13           N  
ANISOU 2350  N   CYS C 111     6459   6125  11782    936    473    310       N  
ATOM   2351  CA  CYS C 111      40.067 -36.778  37.435  1.00 62.01           C  
ANISOU 2351  CA  CYS C 111     6206   5850  11505    879    497    265       C  
ATOM   2352  C   CYS C 111      40.044 -35.265  37.218  1.00 61.49           C  
ANISOU 2352  C   CYS C 111     6128   5837  11400    840    427    237       C  
ATOM   2353  O   CYS C 111      40.442 -34.499  38.100  1.00 62.16           O  
ANISOU 2353  O   CYS C 111     6216   5957  11444    864    363    260       O  
ATOM   2354  CB  CYS C 111      38.853 -37.249  38.248  1.00 60.62           C  
ANISOU 2354  CB  CYS C 111     6082   5642  11308    891    533    281       C  
ATOM   2355  SG  CYS C 111      38.556 -39.055  38.266  1.00 61.12           S  
ANISOU 2355  SG  CYS C 111     6167   5637  11420    921    629    303       S  
ATOM   2356  N   LYS C 112      39.566 -34.830  36.055  1.00 60.69           N  
ANISOU 2356  N   LYS C 112     6012   5740  11309    781    439    186       N  
ATOM   2357  CA  LYS C 112      39.606 -33.417  35.721  1.00 60.61           C  
ANISOU 2357  CA  LYS C 112     5986   5778  11264    742    375    156       C  
ATOM   2358  C   LYS C 112      38.633 -32.599  36.559  1.00 59.11           C  
ANISOU 2358  C   LYS C 112     5836   5606  11017    736    341    157       C  
ATOM   2359  O   LYS C 112      37.929 -33.130  37.429  1.00 58.16           O  
ANISOU 2359  O   LYS C 112     5754   5461  10883    763    366    182       O  
ATOM   2360  CB  LYS C 112      39.277 -33.198  34.259  1.00 60.17           C  
ANISOU 2360  CB  LYS C 112     5908   5720  11233    681    400    100       C  
ATOM   2361  CG  LYS C 112      39.967 -34.076  33.291  1.00 61.80           C  
ANISOU 2361  CG  LYS C 112     6080   5903  11499    678    446     91       C  
ATOM   2362  CD  LYS C 112      39.904 -33.441  31.929  1.00 62.18           C  
ANISOU 2362  CD  LYS C 112     6100   5967  11560    617    443     37       C  
ATOM   2363  CE  LYS C 112      40.506 -34.327  30.865  1.00 63.55           C  
ANISOU 2363  CE  LYS C 112     6239   6115  11793    609    493     24       C  
ATOM   2364  NZ  LYS C 112      40.411 -33.652  29.550  1.00 63.74           N  
ANISOU 2364  NZ  LYS C 112     6236   6155  11826    548    488    -30       N  
ATOM   2365  N   ASN C 113      38.578 -31.306  36.257  1.00 62.68           N  
ANISOU 2365  N   ASN C 113     6277   6101  11436    699    284    128       N  
ATOM   2366  CA  ASN C 113      37.774 -30.348  37.006  1.00 61.57           C  
ANISOU 2366  CA  ASN C 113     6170   5986  11239    691    239    127       C  
ATOM   2367  C   ASN C 113      36.314 -30.734  37.131  1.00 59.13           C  
ANISOU 2367  C   ASN C 113     5902   5645  10921    675    289    114       C  
ATOM   2368  O   ASN C 113      35.710 -31.186  36.160  1.00 58.12           O  
ANISOU 2368  O   ASN C 113     5771   5489  10822    639    343     79       O  
ATOM   2369  CB  ASN C 113      37.886 -28.975  36.354  1.00 61.92           C  
ANISOU 2369  CB  ASN C 113     6194   6075  11258    643    181     88       C  
ATOM   2370  CG  ASN C 113      39.331 -28.537  36.174  1.00 64.74           C  
ANISOU 2370  CG  ASN C 113     6509   6467  11624    655    131     98       C  
ATOM   2371  OD1 ASN C 113      40.273 -29.311  36.416  1.00 67.07           O  
ANISOU 2371  OD1 ASN C 113     6786   6750  11949    696    144    130       O  
ATOM   2372  ND2 ASN C 113      39.519 -27.300  35.740  1.00 64.86           N  
ANISOU 2372  ND2 ASN C 113     6507   6523  11613    618     74     69       N  
ATOM   2373  N   TYR C 114      35.776 -30.539  38.341  1.00 58.84           N  
ANISOU 2373  N   TYR C 114     5903   5613  10842    702    268    141       N  
ATOM   2374  CA  TYR C 114      34.397 -30.892  38.715  1.00 58.44           C  
ANISOU 2374  CA  TYR C 114     5895   5534  10775    695    310    136       C  
ATOM   2375  C   TYR C 114      34.134 -32.416  38.791  1.00 59.42           C  
ANISOU 2375  C   TYR C 114     6033   5602  10940    721    392    156       C  
ATOM   2376  O   TYR C 114      32.977 -32.828  38.932  1.00 59.09           O  
ANISOU 2376  O   TYR C 114     6025   5533  10892    710    436    147       O  
ATOM   2377  CB  TYR C 114      33.378 -30.212  37.788  1.00 56.74           C  
ANISOU 2377  CB  TYR C 114     5683   5326  10548    632    316     79       C  
ATOM   2378  CG  TYR C 114      33.738 -28.778  37.448  1.00 55.74           C  
ANISOU 2378  CG  TYR C 114     5537   5252  10391    601    241     54       C  
ATOM   2379  CD1 TYR C 114      33.702 -27.764  38.414  1.00 55.62           C  
ANISOU 2379  CD1 TYR C 114     5538   5274  10320    615    173     70       C  
ATOM   2380  CD2 TYR C 114      34.135 -28.443  36.161  1.00 55.18           C  
ANISOU 2380  CD2 TYR C 114     5429   5190  10345    558    239     14       C  
ATOM   2381  CE1 TYR C 114      34.073 -26.454  38.099  1.00 55.76           C  
ANISOU 2381  CE1 TYR C 114     5537   5339  10310    587    104     47       C  
ATOM   2382  CE2 TYR C 114      34.480 -27.142  35.834  1.00 55.94           C  
ANISOU 2382  CE2 TYR C 114     5508   5334  10414    529    172     -9       C  
ATOM   2383  CZ  TYR C 114      34.453 -26.148  36.801  1.00 56.22           C  
ANISOU 2383  CZ  TYR C 114     5561   5406  10395    543    104      7       C  
ATOM   2384  OH  TYR C 114      34.810 -24.861  36.450  1.00 57.33           O  
ANISOU 2384  OH  TYR C 114     5684   5592  10508    514     38    -16       O  
ATOM   2385  N   TYR C 115      35.185 -33.235  38.636  1.00 61.15           N  
ANISOU 2385  N   TYR C 115     6228   5806  11202    751    412    180       N  
ATOM   2386  CA  TYR C 115      35.076 -34.695  38.783  1.00 61.47           C  
ANISOU 2386  CA  TYR C 115     6282   5794  11280    781    485    204       C  
ATOM   2387  C   TYR C 115      35.898 -35.310  39.936  1.00 63.13           C  
ANISOU 2387  C   TYR C 115     6500   5996  11489    849    475    264       C  
ATOM   2388  O   TYR C 115      36.603 -34.600  40.663  1.00 64.08           O  
ANISOU 2388  O   TYR C 115     6615   6154  11580    875    409    288       O  
ATOM   2389  CB  TYR C 115      35.465 -35.371  37.470  1.00 61.96           C  
ANISOU 2389  CB  TYR C 115     6310   5832  11400    757    534    177       C  
ATOM   2390  CG  TYR C 115      34.407 -35.220  36.398  1.00 60.49           C  
ANISOU 2390  CG  TYR C 115     6127   5634  11223    697    571    123       C  
ATOM   2391  CD1 TYR C 115      33.390 -36.158  36.261  1.00 59.64           C  
ANISOU 2391  CD1 TYR C 115     6046   5481  11135    688    644    115       C  
ATOM   2392  CD2 TYR C 115      34.419 -34.129  35.537  1.00 60.19           C  
ANISOU 2392  CD2 TYR C 115     6065   5631  11174    648    532     79       C  
ATOM   2393  CE1 TYR C 115      32.427 -36.011  35.289  1.00 58.49           C  
ANISOU 2393  CE1 TYR C 115     5902   5325  10997    634    677     65       C  
ATOM   2394  CE2 TYR C 115      33.467 -33.977  34.567  1.00 59.03           C  
ANISOU 2394  CE2 TYR C 115     5920   5474  11034    593    564     30       C  
ATOM   2395  CZ  TYR C 115      32.479 -34.917  34.439  1.00 58.17           C  
ANISOU 2395  CZ  TYR C 115     5837   5320  10945    587    636     22       C  
ATOM   2396  OH  TYR C 115      31.523 -34.775  33.460  1.00 57.22           O  
ANISOU 2396  OH  TYR C 115     5719   5190  10832    533    668    -28       O  
ATOM   2397  N   LYS C 116      35.806 -36.633  40.090  1.00 61.93           N  
ANISOU 2397  N   LYS C 116     6363   5797  11372    877    540    286       N  
ATOM   2398  CA  LYS C 116      36.360 -37.279  41.273  1.00 63.64           C  
ANISOU 2398  CA  LYS C 116     6596   6000  11583    942    537    343       C  
ATOM   2399  C   LYS C 116      36.820 -38.727  41.009  1.00 65.01           C  
ANISOU 2399  C   LYS C 116     6763   6126  11811    970    603    362       C  
ATOM   2400  O   LYS C 116      36.209 -39.436  40.209  1.00 64.42           O  
ANISOU 2400  O   LYS C 116     6691   6015  11770    943    668    337       O  
ATOM   2401  CB  LYS C 116      35.306 -37.218  42.377  1.00 63.02           C  
ANISOU 2401  CB  LYS C 116     6568   5914  11462    955    539    362       C  
ATOM   2402  CG  LYS C 116      35.703 -37.713  43.751  1.00 65.06           C  
ANISOU 2402  CG  LYS C 116     6852   6163  11704   1020    528    420       C  
ATOM   2403  CD  LYS C 116      34.554 -37.425  44.733  1.00 64.34           C  
ANISOU 2403  CD  LYS C 116     6810   6072  11565   1023    524    430       C  
ATOM   2404  CE  LYS C 116      33.185 -37.814  44.126  1.00 62.52           C  
ANISOU 2404  CE  LYS C 116     6601   5809  11344    978    588    393       C  
ATOM   2405  NZ  LYS C 116      32.027 -37.698  45.070  1.00 62.07           N  
ANISOU 2405  NZ  LYS C 116     6593   5747  11245    982    594    403       N  
ATOM   2406  N   LEU C 117      37.902 -39.166  41.652  1.00 61.08           N  
ANISOU 2406  N   LEU C 117     6256   5629  11324   1025    586    406       N  
ATOM   2407  CA  LEU C 117      38.337 -40.560  41.505  1.00 62.58           C  
ANISOU 2407  CA  LEU C 117     6443   5772  11562   1057    646    427       C  
ATOM   2408  C   LEU C 117      37.382 -41.530  42.199  1.00 62.73           C  
ANISOU 2408  C   LEU C 117     6512   5744  11579   1078    705    450       C  
ATOM   2409  O   LEU C 117      37.023 -41.328  43.366  1.00 62.87           O  
ANISOU 2409  O   LEU C 117     6564   5768  11556   1105    682    480       O  
ATOM   2410  CB  LEU C 117      39.744 -40.776  42.071  1.00 64.88           C  
ANISOU 2410  CB  LEU C 117     6713   6076  11862   1113    611    469       C  
ATOM   2411  CG  LEU C 117      40.914 -40.554  41.124  1.00 65.85           C  
ANISOU 2411  CG  LEU C 117     6781   6221  12017   1103    590    451       C  
ATOM   2412  CD1 LEU C 117      42.223 -40.711  41.881  1.00 68.27           C  
ANISOU 2412  CD1 LEU C 117     7072   6542  12324   1162    550    496       C  
ATOM   2413  CD2 LEU C 117      40.859 -41.470  39.925  1.00 65.93           C  
ANISOU 2413  CD2 LEU C 117     6773   6193  12084   1078    659    424       C  
ATOM   2414  N   ARG C 118      36.955 -42.571  41.488  1.00 69.52           N  
ANISOU 2414  N   ARG C 118     7375   6557  12482   1063    780    435       N  
ATOM   2415  CA  ARG C 118      36.313 -43.707  42.148  1.00 70.56           C  
ANISOU 2415  CA  ARG C 118     7549   6639  12620   1092    840    464       C  
ATOM   2416  C   ARG C 118      37.087 -45.018  41.971  1.00 72.83           C  
ANISOU 2416  C   ARG C 118     7827   6887  12959   1130    888    488       C  
ATOM   2417  O   ARG C 118      37.068 -45.581  40.875  1.00 72.93           O  
ANISOU 2417  O   ARG C 118     7819   6875  13016   1103    936    460       O  
ATOM   2418  CB  ARG C 118      34.895 -43.881  41.616  1.00 69.12           C  
ANISOU 2418  CB  ARG C 118     7391   6432  12440   1043    894    427       C  
ATOM   2419  CG  ARG C 118      34.162 -45.046  42.250  1.00 70.27           C  
ANISOU 2419  CG  ARG C 118     7581   6525  12592   1068    959    453       C  
ATOM   2420  CD  ARG C 118      32.858 -45.357  41.531  1.00 69.18           C  
ANISOU 2420  CD  ARG C 118     7460   6358  12466   1018   1021    412       C  
ATOM   2421  NE  ARG C 118      32.046 -46.271  42.325  1.00 70.54           N  
ANISOU 2421  NE  ARG C 118     7682   6488  12633   1040   1073    439       N  
ATOM   2422  CZ  ARG C 118      31.145 -45.867  43.214  1.00 70.41           C  
ANISOU 2422  CZ  ARG C 118     7704   6478  12569   1040   1060    447       C  
ATOM   2423  NH1 ARG C 118      30.927 -44.564  43.408  1.00 68.95           N  
ANISOU 2423  NH1 ARG C 118     7515   6342  12341   1019    997    430       N  
ATOM   2424  NH2 ARG C 118      30.456 -46.764  43.903  1.00 72.03           N  
ANISOU 2424  NH2 ARG C 118     7953   6644  12773   1061   1111    471       N  
ATOM   2425  N   THR C 119      37.752 -45.470  43.044  1.00 70.48           N  
ANISOU 2425  N   THR C 119     7544   6583  12654   1191    873    540       N  
ATOM   2426  CA  THR C 119      38.381 -46.803  43.148  1.00 72.97           C  
ANISOU 2426  CA  THR C 119     7861   6855  13010   1236    920    572       C  
ATOM   2427  C   THR C 119      39.244 -46.960  44.430  1.00 75.15           C  
ANISOU 2427  C   THR C 119     8149   7139  13266   1305    880    629       C  
ATOM   2428  O   THR C 119      39.653 -45.971  45.049  1.00 74.82           O  
ANISOU 2428  O   THR C 119     8100   7142  13185   1318    810    641       O  
ATOM   2429  CB  THR C 119      39.262 -47.124  41.917  1.00 73.50           C  
ANISOU 2429  CB  THR C 119     7877   6919  13129   1222    935    548       C  
ATOM   2430  OG1 THR C 119      39.643 -48.513  41.930  1.00 75.00           O  
ANISOU 2430  OG1 THR C 119     8074   7061  13362   1260    992    574       O  
ATOM   2431  CG2 THR C 119      40.477 -46.179  41.862  1.00 73.78           C  
ANISOU 2431  CG2 THR C 119     7870   7009  13155   1232    859    550       C  
ATOM   2432  N   GLU C 120      39.557 -48.206  44.792  1.00 72.74           N  
ANISOU 2432  N   GLU C 120     7860   6790  12989   1350    926    663       N  
ATOM   2433  CA  GLU C 120      40.216 -48.519  46.075  1.00 75.16           C  
ANISOU 2433  CA  GLU C 120     8186   7095  13276   1418    899    719       C  
ATOM   2434  C   GLU C 120      41.763 -48.774  46.182  1.00 77.27           C  
ANISOU 2434  C   GLU C 120     8419   7374  13565   1468    867    747       C  
ATOM   2435  O   GLU C 120      42.254 -48.953  47.300  1.00 79.38           O  
ANISOU 2435  O   GLU C 120     8705   7642  13812   1524    841    793       O  
ATOM   2436  CB  GLU C 120      39.502 -49.754  46.659  1.00 76.91           C  
ANISOU 2436  CB  GLU C 120     8458   7258  13505   1444    967    747       C  
ATOM   2437  CG  GLU C 120      38.239 -50.156  45.876  1.00 76.16           C  
ANISOU 2437  CG  GLU C 120     8380   7129  13428   1391   1035    709       C  
ATOM   2438  CD  GLU C 120      37.420 -51.271  46.549  1.00 78.22           C  
ANISOU 2438  CD  GLU C 120     8695   7336  13690   1413   1099    736       C  
ATOM   2439  OE1 GLU C 120      37.987 -52.373  46.768  1.00 80.89           O  
ANISOU 2439  OE1 GLU C 120     9040   7636  14057   1458   1132    767       O  
ATOM   2440  OE2 GLU C 120      36.212 -51.038  46.856  1.00 77.35           O  
ANISOU 2440  OE2 GLU C 120     8619   7219  13550   1387   1115    725       O  
ATOM   2441  N   GLY C 121      42.549 -48.729  45.104  1.00 73.23           N  
ANISOU 2441  N   GLY C 121     7858   6874  13091   1450    865    721       N  
ATOM   2442  CA  GLY C 121      42.422 -47.771  44.034  1.00 70.86           C  
ANISOU 2442  CA  GLY C 121     7522   6608  12793   1389    843    670       C  
ATOM   2443  C   GLY C 121      43.070 -46.473  44.474  1.00 70.34           C  
ANISOU 2443  C   GLY C 121     7434   6603  12688   1394    756    674       C  
ATOM   2444  O   GLY C 121      42.437 -45.427  44.437  1.00 68.22           O  
ANISOU 2444  O   GLY C 121     7170   6366  12385   1355    723    650       O  
ATOM   2445  N   ASP C 122      44.322 -46.554  44.943  1.00 66.85           N  
ANISOU 2445  N   ASP C 122     6971   6178  12251   1444    717    706       N  
ATOM   2446  CA  ASP C 122      45.105 -45.384  45.347  1.00 66.90           C  
ANISOU 2446  CA  ASP C 122     6953   6242  12224   1453    633    712       C  
ATOM   2447  C   ASP C 122      45.510 -44.597  44.115  1.00 65.42           C  
ANISOU 2447  C   ASP C 122     6714   6089  12052   1402    610    665       C  
ATOM   2448  O   ASP C 122      46.096 -43.518  44.214  1.00 65.39           O  
ANISOU 2448  O   ASP C 122     6685   6136  12024   1397    541    660       O  
ATOM   2449  CB  ASP C 122      46.338 -45.790  46.156  1.00 70.00           C  
ANISOU 2449  CB  ASP C 122     7336   6639  12620   1522    604    759       C  
ATOM   2450  CG  ASP C 122      47.606 -45.964  45.288  1.00 71.08           C  
ANISOU 2450  CG  ASP C 122     7418   6790  12801   1527    597    747       C  
ATOM   2451  OD1 ASP C 122      47.637 -46.871  44.424  1.00 70.96           O  
ANISOU 2451  OD1 ASP C 122     7390   6738  12833   1516    656    732       O  
ATOM   2452  OD2 ASP C 122      48.597 -45.217  45.495  1.00 72.59           O  
ANISOU 2452  OD2 ASP C 122     7577   7025  12977   1542    531    754       O  
ATOM   2453  N   GLY C 123      45.203 -45.152  42.948  1.00 66.56           N  
ANISOU 2453  N   GLY C 123     6845   6206  12240   1365    667    631       N  
ATOM   2454  CA  GLY C 123      45.304 -44.412  41.705  1.00 65.01           C  
ANISOU 2454  CA  GLY C 123     6607   6037  12057   1307    654    581       C  
ATOM   2455  C   GLY C 123      46.546 -44.639  40.856  1.00 66.64           C  
ANISOU 2455  C   GLY C 123     6760   6254  12307   1312    650    571       C  
ATOM   2456  O   GLY C 123      46.504 -44.384  39.653  1.00 65.91           O  
ANISOU 2456  O   GLY C 123     6637   6168  12239   1262    663    527       O  
ATOM   2457  N   VAL C 124      47.644 -45.112  41.454  1.00 63.83           N  
ANISOU 2457  N   VAL C 124     6392   5898  11961   1370    632    609       N  
ATOM   2458  CA  VAL C 124      48.897 -45.275  40.712  1.00 64.98           C  
ANISOU 2458  CA  VAL C 124     6486   6058  12146   1378    623    601       C  
ATOM   2459  C   VAL C 124      48.910 -46.597  39.964  1.00 65.97           C  
ANISOU 2459  C   VAL C 124     6606   6131  12327   1381    699    595       C  
ATOM   2460  O   VAL C 124      48.275 -47.568  40.399  1.00 66.86           O  
ANISOU 2460  O   VAL C 124     6758   6197  12447   1403    752    616       O  
ATOM   2461  CB  VAL C 124      50.104 -45.201  41.619  1.00 67.53           C  
ANISOU 2461  CB  VAL C 124     6796   6406  12457   1438    570    642       C  
ATOM   2462  CG1 VAL C 124      51.339 -45.095  40.782  1.00 68.22           C  
ANISOU 2462  CG1 VAL C 124     6825   6518  12578   1435    551    625       C  
ATOM   2463  CG2 VAL C 124      49.981 -43.996  42.526  1.00 66.99           C  
ANISOU 2463  CG2 VAL C 124     6741   6383  12331   1440    499    654       C  
ATOM   2464  N   TYR C 125      49.557 -46.612  38.799  1.00 66.08           N  
ANISOU 2464  N   TYR C 125     6573   6155  12380   1355    707    563       N  
ATOM   2465  CA  TYR C 125      49.666 -47.837  38.016  1.00 67.25           C  
ANISOU 2465  CA  TYR C 125     6711   6257  12583   1358    777    555       C  
ATOM   2466  C   TYR C 125      51.056 -47.993  37.401  1.00 68.86           C  
ANISOU 2466  C   TYR C 125     6861   6479  12824   1373    761    551       C  
ATOM   2467  O   TYR C 125      51.449 -47.154  36.585  1.00 68.14           O  
ANISOU 2467  O   TYR C 125     6729   6426  12735   1333    729    517       O  
ATOM   2468  CB  TYR C 125      48.592 -47.861  36.928  1.00 65.64           C  
ANISOU 2468  CB  TYR C 125     6512   6033  12397   1293    828    509       C  
ATOM   2469  CG  TYR C 125      47.185 -47.982  37.454  1.00 64.51           C  
ANISOU 2469  CG  TYR C 125     6422   5861  12226   1280    859    512       C  
ATOM   2470  CD1 TYR C 125      46.550 -46.911  38.028  1.00 62.68           C  
ANISOU 2470  CD1 TYR C 125     6212   5661  11942   1261    813    509       C  
ATOM   2471  CD2 TYR C 125      46.483 -49.173  37.360  1.00 65.45           C  
ANISOU 2471  CD2 TYR C 125     6572   5923  12372   1286    934    518       C  
ATOM   2472  CE1 TYR C 125      45.240 -47.020  38.521  1.00 61.72           C  
ANISOU 2472  CE1 TYR C 125     6141   5515  11796   1249    842    512       C  
ATOM   2473  CE2 TYR C 125      45.167 -49.299  37.839  1.00 64.63           C  
ANISOU 2473  CE2 TYR C 125     6519   5794  12245   1273    965    520       C  
ATOM   2474  CZ  TYR C 125      44.548 -48.217  38.418  1.00 62.72           C  
ANISOU 2474  CZ  TYR C 125     6296   5584  11950   1255    918    517       C  
ATOM   2475  OH  TYR C 125      43.258 -48.299  38.906  1.00 61.99           O  
ANISOU 2475  OH  TYR C 125     6252   5470  11832   1242    946    518       O  
ATOM   2476  N   THR C 126      51.769 -49.073  37.774  1.00 62.05           N  
ANISOU 2476  N   THR C 126     5998   5588  11989   1430    785    585       N  
ATOM   2477  CA  THR C 126      53.167 -49.323  37.355  1.00 63.55           C  
ANISOU 2477  CA  THR C 126     6139   5794  12213   1456    769    587       C  
ATOM   2478  C   THR C 126      53.277 -50.276  36.171  1.00 64.35           C  
ANISOU 2478  C   THR C 126     6217   5859  12373   1438    834    562       C  
ATOM   2479  O   THR C 126      52.570 -51.278  36.124  1.00 64.77           O  
ANISOU 2479  O   THR C 126     6302   5860  12446   1443    899    568       O  
ATOM   2480  CB  THR C 126      54.018 -49.929  38.483  1.00 66.05           C  
ANISOU 2480  CB  THR C 126     6466   6104  12526   1533    751    640       C  
ATOM   2481  OG1 THR C 126      53.733 -49.297  39.736  1.00 66.08           O  
ANISOU 2481  OG1 THR C 126     6502   6128  12476   1557    704    670       O  
ATOM   2482  CG2 THR C 126      55.481 -49.759  38.157  1.00 66.98           C  
ANISOU 2482  CG2 THR C 126     6528   6256  12664   1554    712    639       C  
ATOM   2483  N   LEU C 127      54.168 -49.983  35.229  1.00 64.41           N  
ANISOU 2483  N   LEU C 127     6171   5894  12406   1418    817    535       N  
ATOM   2484  CA  LEU C 127      54.323 -50.836  34.046  1.00 64.98           C  
ANISOU 2484  CA  LEU C 127     6218   5936  12534   1400    877    509       C  
ATOM   2485  C   LEU C 127      55.107 -52.111  34.373  1.00 67.72           C  
ANISOU 2485  C   LEU C 127     6564   6249  12917   1463    907    543       C  
ATOM   2486  O   LEU C 127      55.990 -52.102  35.225  1.00 68.99           O  
ANISOU 2486  O   LEU C 127     6719   6428  13065   1517    866    578       O  
ATOM   2487  CB  LEU C 127      55.000 -50.058  32.914  1.00 63.95           C  
ANISOU 2487  CB  LEU C 127     6030   5848  12420   1355    848    467       C  
ATOM   2488  CG  LEU C 127      54.853 -50.523  31.461  1.00 63.96           C  
ANISOU 2488  CG  LEU C 127     6004   5827  12469   1310    903    424       C  
ATOM   2489  CD1 LEU C 127      55.927 -51.499  31.064  1.00 66.25           C  
ANISOU 2489  CD1 LEU C 127     6262   6101  12809   1346    928    433       C  
ATOM   2490  CD2 LEU C 127      53.478 -51.106  31.209  1.00 63.48           C  
ANISOU 2490  CD2 LEU C 127     5985   5717  12416   1282    969    412       C  
ATOM   2491  N   ASN C 128      54.758 -53.202  33.691  1.00 65.70           N  
ANISOU 2491  N   ASN C 128     6314   5944  12705   1457    979    532       N  
ATOM   2492  CA  ASN C 128      55.257 -54.558  33.986  1.00 68.39           C  
ANISOU 2492  CA  ASN C 128     6663   6241  13080   1514   1021    564       C  
ATOM   2493  C   ASN C 128      56.448 -54.973  33.146  1.00 70.44           C  
ANISOU 2493  C   ASN C 128     6869   6508  13386   1525   1026    551       C  
ATOM   2494  O   ASN C 128      56.788 -54.318  32.172  1.00 69.94           O  
ANISOU 2494  O   ASN C 128     6762   6477  13335   1481   1008    513       O  
ATOM   2495  CB  ASN C 128      54.145 -55.584  33.728  1.00 68.79           C  
ANISOU 2495  CB  ASN C 128     6755   6230  13153   1502   1102    560       C  
ATOM   2496  CG  ASN C 128      53.515 -56.101  34.985  1.00 69.24           C  
ANISOU 2496  CG  ASN C 128     6871   6255  13183   1544   1116    604       C  
ATOM   2497  OD1 ASN C 128      53.784 -55.609  36.077  1.00 68.87           O  
ANISOU 2497  OD1 ASN C 128     6838   6232  13096   1578   1064    635       O  
ATOM   2498  ND2 ASN C 128      52.659 -57.105  34.843  1.00 70.31           N  
ANISOU 2498  ND2 ASN C 128     7042   6334  13340   1540   1187    605       N  
ATOM   2499  N   ASN C 129      57.035 -56.115  33.456  1.00 70.07           N  
ANISOU 2499  N   ASN C 129     6827   6428  13368   1581   1054    581       N  
ATOM   2500  CA  ASN C 129      57.915 -56.725  32.476  1.00 72.13           C  
ANISOU 2500  CA  ASN C 129     7043   6683  13681   1583   1079    563       C  
ATOM   2501  C   ASN C 129      57.002 -57.424  31.479  1.00 72.42           C  
ANISOU 2501  C   ASN C 129     7090   6673  13752   1541   1155    532       C  
ATOM   2502  O   ASN C 129      57.385 -57.711  30.338  1.00 73.48           O  
ANISOU 2502  O   ASN C 129     7186   6804  13929   1516   1181    501       O  
ATOM   2503  CB  ASN C 129      58.907 -57.680  33.128  1.00 74.87           C  
ANISOU 2503  CB  ASN C 129     7388   7013  14047   1659   1080    604       C  
ATOM   2504  CG  ASN C 129      60.024 -56.941  33.836  1.00 75.04           C  
ANISOU 2504  CG  ASN C 129     7383   7086  14042   1696   1003    624       C  
ATOM   2505  OD1 ASN C 129      60.417 -55.860  33.406  1.00 73.19           O  
ANISOU 2505  OD1 ASN C 129     7110   6904  13795   1661    955    598       O  
ATOM   2506  ND2 ASN C 129      60.529 -57.508  34.933  1.00 77.47           N  
ANISOU 2506  ND2 ASN C 129     7712   7382  14341   1766    991    671       N  
ATOM   2507  N   GLU C 130      55.774 -57.667  31.951  1.00 71.97           N  
ANISOU 2507  N   GLU C 130     7087   6582  13676   1532   1188    542       N  
ATOM   2508  CA  GLU C 130      54.657 -58.180  31.169  1.00 72.16           C  
ANISOU 2508  CA  GLU C 130     7132   6564  13723   1487   1257    514       C  
ATOM   2509  C   GLU C 130      54.020 -57.027  30.399  1.00 69.61           C  
ANISOU 2509  C   GLU C 130     6793   6274  13382   1413   1238    468       C  
ATOM   2510  O   GLU C 130      53.040 -57.219  29.680  1.00 69.37           O  
ANISOU 2510  O   GLU C 130     6776   6217  13365   1366   1288    438       O  
ATOM   2511  CB  GLU C 130      53.631 -58.840  32.096  1.00 72.94           C  
ANISOU 2511  CB  GLU C 130     7295   6616  13803   1509   1295    545       C  
ATOM   2512  CG  GLU C 130      53.899 -60.277  32.521  1.00 73.63           C  
ANISOU 2512  CG  GLU C 130     7406   6651  13920   1568   1343    581       C  
ATOM   2513  CD  GLU C 130      55.269 -60.520  33.182  1.00 76.08           C  
ANISOU 2513  CD  GLU C 130     7696   6977  14233   1635   1303    617       C  
ATOM   2514  OE1 GLU C 130      56.189 -59.676  33.073  1.00 77.01           O  
ANISOU 2514  OE1 GLU C 130     7770   7147  14342   1635   1243    609       O  
ATOM   2515  OE2 GLU C 130      55.431 -61.596  33.819  1.00 77.30           O  
ANISOU 2515  OE2 GLU C 130     7880   7091  14401   1690   1332    654       O  
ATOM   2516  N   LYS C 131      54.576 -55.828  30.573  1.00 72.18           N  
ANISOU 2516  N   LYS C 131     7092   6658  13677   1404   1167    462       N  
ATOM   2517  CA  LYS C 131      54.094 -54.601  29.913  1.00 69.91           C  
ANISOU 2517  CA  LYS C 131     6787   6409  13368   1337   1138    420       C  
ATOM   2518  C   LYS C 131      52.581 -54.393  30.117  1.00 67.66           C  
ANISOU 2518  C   LYS C 131     6551   6103  13055   1301   1163    411       C  
ATOM   2519  O   LYS C 131      51.835 -53.943  29.242  1.00 66.49           O  
ANISOU 2519  O   LYS C 131     6398   5957  12909   1240   1180    369       O  
ATOM   2520  CB  LYS C 131      54.505 -54.614  28.440  1.00 71.13           C  
ANISOU 2520  CB  LYS C 131     6892   6570  13565   1294   1159    375       C  
ATOM   2521  CG  LYS C 131      56.049 -54.589  28.328  1.00 73.28           C  
ANISOU 2521  CG  LYS C 131     7113   6873  13856   1328   1120    384       C  
ATOM   2522  CD  LYS C 131      56.569 -54.486  26.905  1.00 74.47           C  
ANISOU 2522  CD  LYS C 131     7211   7039  14047   1286   1132    339       C  
ATOM   2523  CE  LYS C 131      56.383 -55.800  26.170  1.00 76.88           C  
ANISOU 2523  CE  LYS C 131     7517   7288  14404   1288   1211    330       C  
ATOM   2524  NZ  LYS C 131      57.243 -55.933  24.962  1.00 78.05           N  
ANISOU 2524  NZ  LYS C 131     7609   7450  14597   1269   1220    299       N  
ATOM   2525  N   GLN C 132      52.181 -54.700  31.343  1.00 66.92           N  
ANISOU 2525  N   GLN C 132     6503   5990  12933   1343   1162    452       N  
ATOM   2526  CA  GLN C 132      50.839 -54.528  31.833  1.00 65.21           C  
ANISOU 2526  CA  GLN C 132     6337   5755  12683   1322   1180    453       C  
ATOM   2527  C   GLN C 132      50.804 -53.331  32.788  1.00 63.05           C  
ANISOU 2527  C   GLN C 132     6075   5528  12352   1327   1107    469       C  
ATOM   2528  O   GLN C 132      51.828 -52.999  33.394  1.00 63.57           O  
ANISOU 2528  O   GLN C 132     6123   5627  12405   1367   1053    494       O  
ATOM   2529  CB  GLN C 132      50.385 -55.813  32.525  1.00 67.01           C  
ANISOU 2529  CB  GLN C 132     6612   5924  12923   1366   1236    489       C  
ATOM   2530  CG  GLN C 132      50.534 -57.052  31.665  1.00 69.68           C  
ANISOU 2530  CG  GLN C 132     6939   6216  13320   1368   1306    479       C  
ATOM   2531  CD  GLN C 132      50.207 -58.324  32.403  1.00 71.92           C  
ANISOU 2531  CD  GLN C 132     7268   6443  13614   1416   1357    517       C  
ATOM   2532  OE1 GLN C 132      50.037 -58.340  33.624  1.00 71.78           O  
ANISOU 2532  OE1 GLN C 132     7289   6422  13562   1455   1338    557       O  
ATOM   2533  NE2 GLN C 132      50.123 -59.408  31.660  1.00 74.31           N  
ANISOU 2533  NE2 GLN C 132     7569   6701  13965   1413   1423    506       N  
ATOM   2534  N   TRP C 133      49.655 -52.654  32.884  1.00 70.32           N  
ANISOU 2534  N   TRP C 133     7025   6455  13240   1285   1103    451       N  
ATOM   2535  CA  TRP C 133      49.531 -51.480  33.753  1.00 68.40           C  
ANISOU 2535  CA  TRP C 133     6793   6255  12939   1286   1035    463       C  
ATOM   2536  C   TRP C 133      48.845 -51.851  35.046  1.00 68.39           C  
ANISOU 2536  C   TRP C 133     6849   6229  12906   1324   1044    504       C  
ATOM   2537  O   TRP C 133      47.635 -52.059  35.056  1.00 67.66           O  
ANISOU 2537  O   TRP C 133     6794   6108  12806   1298   1085    494       O  
ATOM   2538  CB  TRP C 133      48.753 -50.375  33.054  1.00 66.04           C  
ANISOU 2538  CB  TRP C 133     6488   5986  12620   1216   1018    417       C  
ATOM   2539  CG  TRP C 133      49.576 -49.606  32.112  1.00 65.98           C  
ANISOU 2539  CG  TRP C 133     6425   6020  12624   1185    981    384       C  
ATOM   2540  CD1 TRP C 133      49.601 -49.738  30.765  1.00 66.53           C  
ANISOU 2540  CD1 TRP C 133     6462   6083  12732   1140   1013    342       C  
ATOM   2541  CD2 TRP C 133      50.514 -48.576  32.436  1.00 65.69           C  
ANISOU 2541  CD2 TRP C 133     6359   6040  12561   1194    903    390       C  
ATOM   2542  NE1 TRP C 133      50.491 -48.851  30.221  1.00 66.57           N  
ANISOU 2542  NE1 TRP C 133     6420   6138  12737   1121    962    321       N  
ATOM   2543  CE2 TRP C 133      51.067 -48.125  31.228  1.00 66.08           C  
ANISOU 2543  CE2 TRP C 133     6358   6114  12634   1153    893    350       C  
ATOM   2544  CE3 TRP C 133      50.934 -47.988  33.630  1.00 65.42           C  
ANISOU 2544  CE3 TRP C 133     6335   6037  12484   1233    841    426       C  
ATOM   2545  CZ2 TRP C 133      52.021 -47.110  31.173  1.00 66.23           C  
ANISOU 2545  CZ2 TRP C 133     6338   6189  12637   1149    824    344       C  
ATOM   2546  CZ3 TRP C 133      51.883 -46.988  33.574  1.00 65.56           C  
ANISOU 2546  CZ3 TRP C 133     6314   6110  12486   1230    773    420       C  
ATOM   2547  CH2 TRP C 133      52.420 -46.560  32.354  1.00 65.99           C  
ANISOU 2547  CH2 TRP C 133     6319   6188  12565   1187    765    379       C  
ATOM   2548  N   ILE C 134      49.599 -51.892  36.143  1.00 64.36           N  
ANISOU 2548  N   ILE C 134     6345   5731  12376   1383   1004    548       N  
ATOM   2549  CA  ILE C 134      49.124 -52.593  37.337  1.00 65.47           C  
ANISOU 2549  CA  ILE C 134     6539   5837  12500   1430   1025    593       C  
ATOM   2550  C   ILE C 134      49.134 -51.833  38.667  1.00 64.91           C  
ANISOU 2550  C   ILE C 134     6493   5797  12372   1460    963    626       C  
ATOM   2551  O   ILE C 134      50.199 -51.494  39.191  1.00 65.76           O  
ANISOU 2551  O   ILE C 134     6580   5937  12469   1499    908    650       O  
ATOM   2552  CB  ILE C 134      49.947 -53.878  37.563  1.00 68.53           C  
ANISOU 2552  CB  ILE C 134     6926   6189  12925   1489   1057    626       C  
ATOM   2553  CG1 ILE C 134      50.162 -54.600  36.240  1.00 69.49           C  
ANISOU 2553  CG1 ILE C 134     7015   6285  13104   1464   1111    594       C  
ATOM   2554  CG2 ILE C 134      49.248 -54.785  38.571  1.00 70.04           C  
ANISOU 2554  CG2 ILE C 134     7175   6332  13105   1528   1097    665       C  
ATOM   2555  CD1 ILE C 134      48.911 -55.147  35.675  1.00 69.15           C  
ANISOU 2555  CD1 ILE C 134     7000   6197  13076   1424   1181    570       C  
ATOM   2556  N   ASN C 135      47.945 -51.625  39.238  1.00 68.41           N  
ANISOU 2556  N   ASN C 135     6983   6229  12781   1445    973    630       N  
ATOM   2557  CA  ASN C 135      47.853 -51.094  40.599  1.00 68.45           C  
ANISOU 2557  CA  ASN C 135     7019   6254  12734   1479    924    667       C  
ATOM   2558  C   ASN C 135      47.857 -52.167  41.652  1.00 71.13           C  
ANISOU 2558  C   ASN C 135     7400   6552  13074   1541    952    717       C  
ATOM   2559  O   ASN C 135      46.957 -52.999  41.677  1.00 71.83           O  
ANISOU 2559  O   ASN C 135     7527   6593  13174   1537   1015    719       O  
ATOM   2560  CB  ASN C 135      46.596 -50.267  40.821  1.00 66.14           C  
ANISOU 2560  CB  ASN C 135     6757   5974  12399   1436    914    649       C  
ATOM   2561  CG  ASN C 135      46.388 -49.943  42.294  1.00 66.81           C  
ANISOU 2561  CG  ASN C 135     6882   6069  12433   1476    875    691       C  
ATOM   2562  OD1 ASN C 135      45.358 -50.257  42.861  1.00 67.20           O  
ANISOU 2562  OD1 ASN C 135     6979   6090  12463   1476    906    702       O  
ATOM   2563  ND2 ASN C 135      47.396 -49.341  42.926  1.00 67.33           N  
ANISOU 2563  ND2 ASN C 135     6928   6176  12477   1512    808    714       N  
ATOM   2564  N   LYS C 136      48.809 -52.082  42.581  1.00 75.43           N  
ANISOU 2564  N   LYS C 136     7941   7117  13602   1598    904    756       N  
ATOM   2565  CA  LYS C 136      49.059 -53.176  43.519  1.00 78.51           C  
ANISOU 2565  CA  LYS C 136     8364   7467  13998   1664    929    805       C  
ATOM   2566  C   LYS C 136      47.856 -53.463  44.445  1.00 78.96           C  
ANISOU 2566  C   LYS C 136     8485   7494  14023   1670    957    827       C  
ATOM   2567  O   LYS C 136      47.860 -54.434  45.201  1.00 81.45           O  
ANISOU 2567  O   LYS C 136     8835   7770  14342   1719    987    866       O  
ATOM   2568  CB  LYS C 136      50.333 -52.912  44.337  1.00 80.28           C  
ANISOU 2568  CB  LYS C 136     8571   7725  14208   1722    866    841       C  
ATOM   2569  CG  LYS C 136      50.319 -51.726  45.285  1.00 79.35           C  
ANISOU 2569  CG  LYS C 136     8462   7655  14032   1728    792    856       C  
ATOM   2570  CD  LYS C 136      51.653 -51.693  46.056  1.00 81.42           C  
ANISOU 2570  CD  LYS C 136     8706   7943  14288   1792    739    893       C  
ATOM   2571  CE  LYS C 136      51.882 -50.378  46.813  1.00 80.52           C  
ANISOU 2571  CE  LYS C 136     8587   7885  14121   1795    656    902       C  
ATOM   2572  NZ  LYS C 136      50.693 -49.935  47.634  1.00 79.54           N  
ANISOU 2572  NZ  LYS C 136     8514   7759  13950   1783    652    912       N  
ATOM   2573  N   ALA C 137      46.818 -52.653  44.362  1.00 69.80           N  
ANISOU 2573  N   ALA C 137     7340   6349  12832   1621    949    802       N  
ATOM   2574  CA  ALA C 137      45.628 -52.888  45.152  1.00 70.17           C  
ANISOU 2574  CA  ALA C 137     7445   6368  12849   1622    977    818       C  
ATOM   2575  C   ALA C 137      44.506 -53.550  44.318  1.00 69.53           C  
ANISOU 2575  C   ALA C 137     7381   6241  12795   1576   1056    787       C  
ATOM   2576  O   ALA C 137      43.910 -54.555  44.701  1.00 71.54           O  
ANISOU 2576  O   ALA C 137     7677   6446  13058   1594   1112    807       O  
ATOM   2577  CB  ALA C 137      45.153 -51.580  45.767  1.00 68.20           C  
ANISOU 2577  CB  ALA C 137     7206   6164  12542   1603    917    815       C  
ATOM   2578  N   VAL C 138      44.127 -52.887  43.241  1.00 70.81           N  
ANISOU 2578  N   VAL C 138     7515   6423  12965   1513   1056    737       N  
ATOM   2579  CA  VAL C 138      43.088 -53.374  42.347  1.00 70.15           C  
ANISOU 2579  CA  VAL C 138     7442   6304  12907   1464   1124    702       C  
ATOM   2580  C   VAL C 138      43.621 -54.054  41.089  1.00 70.59           C  
ANISOU 2580  C   VAL C 138     7460   6340  13022   1449   1166    676       C  
ATOM   2581  O   VAL C 138      42.848 -54.471  40.245  1.00 70.32           O  
ANISOU 2581  O   VAL C 138     7430   6277  13013   1408   1223    644       O  
ATOM   2582  CB  VAL C 138      42.168 -52.211  41.919  1.00 66.92           C  
ANISOU 2582  CB  VAL C 138     7031   5928  12469   1401   1102    660       C  
ATOM   2583  CG1 VAL C 138      41.798 -51.369  43.131  1.00 66.27           C  
ANISOU 2583  CG1 VAL C 138     6979   5875  12326   1415   1049    683       C  
ATOM   2584  CG2 VAL C 138      42.857 -51.337  40.891  1.00 64.73           C  
ANISOU 2584  CG2 VAL C 138     6697   5695  12204   1365   1062    622       C  
ATOM   2585  N   GLY C 139      44.937 -54.129  40.927  1.00 71.76           N  
ANISOU 2585  N   GLY C 139     7569   6506  13192   1481   1137    687       N  
ATOM   2586  CA  GLY C 139      45.471 -54.775  39.738  1.00 72.48           C  
ANISOU 2586  CA  GLY C 139     7622   6578  13338   1467   1176    663       C  
ATOM   2587  C   GLY C 139      45.263 -54.116  38.380  1.00 70.26           C  
ANISOU 2587  C   GLY C 139     7302   6320  13075   1400   1177    606       C  
ATOM   2588  O   GLY C 139      45.839 -53.063  38.053  1.00 68.61           O  
ANISOU 2588  O   GLY C 139     7054   6161  12852   1380   1119    587       O  
ATOM   2589  N   ASP C 140      44.518 -54.841  37.554  1.00 73.88           N  
ANISOU 2589  N   ASP C 140     7768   6736  13566   1367   1247    580       N  
ATOM   2590  CA  ASP C 140      44.241 -54.504  36.167  1.00 72.41           C  
ANISOU 2590  CA  ASP C 140     7549   6559  13406   1304   1266    526       C  
ATOM   2591  C   ASP C 140      43.126 -53.452  36.008  1.00 69.71           C  
ANISOU 2591  C   ASP C 140     7219   6240  13026   1247   1249    492       C  
ATOM   2592  O   ASP C 140      42.932 -52.886  34.923  1.00 68.28           O  
ANISOU 2592  O   ASP C 140     7009   6078  12857   1192   1248    446       O  
ATOM   2593  CB  ASP C 140      43.864 -55.801  35.432  1.00 74.46           C  
ANISOU 2593  CB  ASP C 140     7816   6760  13715   1296   1351    515       C  
ATOM   2594  CG  ASP C 140      43.796 -55.635  33.929  1.00 74.20           C  
ANISOU 2594  CG  ASP C 140     7743   6731  13717   1239   1374    461       C  
ATOM   2595  OD1 ASP C 140      44.532 -54.773  33.402  1.00 73.47           O  
ANISOU 2595  OD1 ASP C 140     7607   6685  13625   1221   1324    441       O  
ATOM   2596  OD2 ASP C 140      43.009 -56.373  33.281  1.00 75.01           O  
ANISOU 2596  OD2 ASP C 140     7860   6792  13849   1212   1442    440       O  
ATOM   2597  N   LYS C 141      42.389 -53.190  37.080  1.00 71.97           N  
ANISOU 2597  N   LYS C 141     7551   6527  13269   1259   1236    515       N  
ATOM   2598  CA  LYS C 141      41.173 -52.389  36.948  1.00 69.66           C  
ANISOU 2598  CA  LYS C 141     7277   6248  12943   1206   1232    484       C  
ATOM   2599  C   LYS C 141      41.438 -50.897  37.043  1.00 67.00           C  
ANISOU 2599  C   LYS C 141     6918   5974  12566   1186   1153    470       C  
ATOM   2600  O   LYS C 141      42.032 -50.411  38.003  1.00 66.98           O  
ANISOU 2600  O   LYS C 141     6918   5999  12531   1224   1096    502       O  
ATOM   2601  CB  LYS C 141      40.151 -52.781  38.003  1.00 70.48           C  
ANISOU 2601  CB  LYS C 141     7439   6322  13017   1224   1258    511       C  
ATOM   2602  CG  LYS C 141      38.859 -52.024  37.866  1.00 68.05           C  
ANISOU 2602  CG  LYS C 141     7152   6025  12677   1171   1258    478       C  
ATOM   2603  CD  LYS C 141      37.764 -52.577  38.796  1.00 68.95           C  
ANISOU 2603  CD  LYS C 141     7325   6104  12769   1185   1297    501       C  
ATOM   2604  CE  LYS C 141      38.132 -52.442  40.283  1.00 69.65           C  
ANISOU 2604  CE  LYS C 141     7441   6205  12817   1242   1253    554       C  
ATOM   2605  NZ  LYS C 141      37.020 -52.887  41.186  1.00 69.49           N  
ANISOU 2605  NZ  LYS C 141     7479   6153  12771   1252   1287    574       N  
ATOM   2606  N   LEU C 142      40.987 -50.159  36.043  1.00 67.68           N  
ANISOU 2606  N   LEU C 142     6982   6080  12653   1125   1148    420       N  
ATOM   2607  CA  LEU C 142      41.200 -48.722  36.034  1.00 65.02           C  
ANISOU 2607  CA  LEU C 142     6623   5801  12279   1100   1074    402       C  
ATOM   2608  C   LEU C 142      40.233 -48.032  36.996  1.00 62.93           C  
ANISOU 2608  C   LEU C 142     6401   5550  11958   1095   1047    412       C  
ATOM   2609  O   LEU C 142      39.298 -48.673  37.498  1.00 63.41           O  
ANISOU 2609  O   LEU C 142     6506   5575  12013   1103   1093    424       O  
ATOM   2610  CB  LEU C 142      41.031 -48.186  34.620  1.00 63.68           C  
ANISOU 2610  CB  LEU C 142     6418   5647  12129   1036   1080    346       C  
ATOM   2611  CG  LEU C 142      42.090 -48.625  33.619  1.00 65.83           C  
ANISOU 2611  CG  LEU C 142     6642   5917  12452   1036   1093    333       C  
ATOM   2612  CD1 LEU C 142      41.647 -48.211  32.242  1.00 64.97           C  
ANISOU 2612  CD1 LEU C 142     6508   5815  12362    970   1111    276       C  
ATOM   2613  CD2 LEU C 142      43.447 -48.037  33.962  1.00 66.66           C  
ANISOU 2613  CD2 LEU C 142     6713   6066  12548   1068   1025    354       C  
ATOM   2614  N   PRO C 143      40.481 -46.738  37.299  1.00 66.48           N  
ANISOU 2614  N   PRO C 143     6838   6054  12366   1086    973    407       N  
ATOM   2615  CA  PRO C 143      39.429 -45.970  37.974  1.00 64.22           C  
ANISOU 2615  CA  PRO C 143     6588   5783  12028   1068    950    404       C  
ATOM   2616  C   PRO C 143      38.506 -45.312  36.975  1.00 61.82           C  
ANISOU 2616  C   PRO C 143     6278   5489  11721    999    960    348       C  
ATOM   2617  O   PRO C 143      38.802 -45.326  35.781  1.00 61.94           O  
ANISOU 2617  O   PRO C 143     6258   5506  11772    965    976    313       O  
ATOM   2618  CB  PRO C 143      40.202 -44.917  38.749  1.00 63.71           C  
ANISOU 2618  CB  PRO C 143     6512   5771  11924   1092    865    425       C  
ATOM   2619  CG  PRO C 143      41.441 -44.725  37.953  1.00 64.58           C  
ANISOU 2619  CG  PRO C 143     6569   5905  12064   1090    840    413       C  
ATOM   2620  CD  PRO C 143      41.782 -46.041  37.327  1.00 66.81           C  
ANISOU 2620  CD  PRO C 143     6840   6141  12404   1103    906    415       C  
ATOM   2621  N   GLU C 144      37.424 -44.711  37.467  1.00 66.52           N  
ANISOU 2621  N   GLU C 144     6907   6093  12273    978    948    340       N  
ATOM   2622  CA  GLU C 144      36.493 -43.974  36.618  1.00 64.07           C  
ANISOU 2622  CA  GLU C 144     6593   5796  11953    914    951    288       C  
ATOM   2623  C   GLU C 144      36.264 -42.629  37.261  1.00 62.03           C  
ANISOU 2623  C   GLU C 144     6345   5587  11637    905    879    286       C  
ATOM   2624  O   GLU C 144      36.417 -42.489  38.473  1.00 62.42           O  
ANISOU 2624  O   GLU C 144     6417   5646  11652    947    846    326       O  
ATOM   2625  CB  GLU C 144      35.190 -44.720  36.453  1.00 63.69           C  
ANISOU 2625  CB  GLU C 144     6581   5703  11915    892   1023    272       C  
ATOM   2626  CG  GLU C 144      34.556 -45.114  37.783  1.00 66.27           C  
ANISOU 2626  CG  GLU C 144     6959   6011  12211    929   1034    312       C  
ATOM   2627  CD  GLU C 144      33.434 -46.178  37.652  1.00 66.48           C  
ANISOU 2627  CD  GLU C 144     7020   5983  12258    918   1117    305       C  
ATOM   2628  OE1 GLU C 144      32.242 -45.805  37.854  1.00 67.47           O  
ANISOU 2628  OE1 GLU C 144     7174   6108  12352    889   1125    287       O  
ATOM   2629  OE2 GLU C 144      33.757 -47.368  37.372  1.00 65.88           O  
ANISOU 2629  OE2 GLU C 144     6941   5865  12227    938   1173    318       O  
ATOM   2630  N   CYS C 145      35.938 -41.619  36.468  1.00 63.61           N  
ANISOU 2630  N   CYS C 145     6526   5818  11824    851    852    241       N  
ATOM   2631  CA  CYS C 145      35.735 -40.310  37.061  1.00 61.80           C  
ANISOU 2631  CA  CYS C 145     6306   5636  11540    842    781    238       C  
ATOM   2632  C   CYS C 145      34.238 -39.950  37.232  1.00 59.80           C  
ANISOU 2632  C   CYS C 145     6091   5378  11253    808    796    215       C  
ATOM   2633  O   CYS C 145      33.453 -39.881  36.273  1.00 58.73           O  
ANISOU 2633  O   CYS C 145     5953   5232  11131    758    829    170       O  
ATOM   2634  CB  CYS C 145      36.454 -39.253  36.243  1.00 61.19           C  
ANISOU 2634  CB  CYS C 145     6185   5604  11461    810    727    208       C  
ATOM   2635  SG  CYS C 145      38.262 -39.340  36.276  1.00 63.46           S  
ANISOU 2635  SG  CYS C 145     6427   5912  11772    852    687    237       S  
ATOM   2636  N   GLU C 146      33.863 -39.723  38.484  1.00 65.49           N  
ANISOU 2636  N   GLU C 146     6848   6106  11930    838    771    247       N  
ATOM   2637  CA  GLU C 146      32.480 -39.499  38.879  1.00 64.01           C  
ANISOU 2637  CA  GLU C 146     6700   5911  11708    817    786    233       C  
ATOM   2638  C   GLU C 146      32.238 -38.030  39.287  1.00 62.13           C  
ANISOU 2638  C   GLU C 146     6467   5726  11415    799    710    222       C  
ATOM   2639  O   GLU C 146      33.015 -37.439  40.058  1.00 62.62           O  
ANISOU 2639  O   GLU C 146     6523   5820  11448    831    648    251       O  
ATOM   2640  CB  GLU C 146      32.145 -40.456  40.012  1.00 65.51           C  
ANISOU 2640  CB  GLU C 146     6931   6065  11893    864    821    279       C  
ATOM   2641  CG  GLU C 146      30.995 -40.105  40.907  1.00 64.72           C  
ANISOU 2641  CG  GLU C 146     6877   5969  11746    861    816    284       C  
ATOM   2642  CD  GLU C 146      30.947 -41.038  42.121  1.00 66.87           C  
ANISOU 2642  CD  GLU C 146     7186   6209  12012    917    842    336       C  
ATOM   2643  OE1 GLU C 146      31.292 -40.544  43.227  1.00 67.54           O  
ANISOU 2643  OE1 GLU C 146     7284   6319  12058    953    789    372       O  
ATOM   2644  OE2 GLU C 146      30.599 -42.250  41.969  1.00 68.19           O  
ANISOU 2644  OE2 GLU C 146     7369   6327  12214    924    915    343       O  
ATOM   2645  N   ALA C 147      31.178 -37.436  38.745  1.00 62.24           N  
ANISOU 2645  N   ALA C 147     6490   5747  11411    748    715    177       N  
ATOM   2646  CA  ALA C 147      30.882 -36.034  38.993  1.00 60.49           C  
ANISOU 2646  CA  ALA C 147     6272   5574  11139    725    647    160       C  
ATOM   2647  C   ALA C 147      30.665 -35.717  40.474  1.00 60.59           C  
ANISOU 2647  C   ALA C 147     6320   5600  11101    764    609    200       C  
ATOM   2648  O   ALA C 147      30.093 -36.492  41.216  1.00 61.21           O  
ANISOU 2648  O   ALA C 147     6433   5648  11177    790    649    225       O  
ATOM   2649  CB  ALA C 147      29.672 -35.621  38.202  1.00 58.64           C  
ANISOU 2649  CB  ALA C 147     6047   5338  10897    667    668    106       C  
ATOM   2650  N   VAL C 148      31.157 -34.565  40.900  1.00 61.21           N  
ANISOU 2650  N   VAL C 148     6388   5727  11141    769    531    205       N  
ATOM   2651  CA  VAL C 148      30.898 -34.073  42.246  1.00 61.44           C  
ANISOU 2651  CA  VAL C 148     6450   5776  11118    800    488    238       C  
ATOM   2652  C   VAL C 148      29.516 -33.477  42.233  1.00 59.47           C  
ANISOU 2652  C   VAL C 148     6229   5533  10833    761    490    204       C  
ATOM   2653  O   VAL C 148      29.037 -33.099  41.162  1.00 57.92           O  
ANISOU 2653  O   VAL C 148     6018   5341  10647    709    501    154       O  
ATOM   2654  CB  VAL C 148      31.923 -33.015  42.683  1.00 62.22           C  
ANISOU 2654  CB  VAL C 148     6528   5925  11187    818    402    254       C  
ATOM   2655  CG1 VAL C 148      32.131 -33.066  44.195  1.00 64.08           C  
ANISOU 2655  CG1 VAL C 148     6792   6168  11389    874    372    308       C  
ATOM   2656  CG2 VAL C 148      33.224 -33.258  41.977  1.00 63.43           C  
ANISOU 2656  CG2 VAL C 148     6636   6082  11382    825    397    257       C  
ATOM   2657  N   CYS C 149      28.878 -33.405  43.400  1.00 56.17           N  
ANISOU 2657  N   CYS C 149     5850   5116  10375    785    481    229       N  
ATOM   2658  CA  CYS C 149      27.586 -32.716  43.528  1.00 54.45           C  
ANISOU 2658  CA  CYS C 149     5661   4911  10118    751    473    199       C  
ATOM   2659  C   CYS C 149      27.564 -31.755  44.742  1.00 54.93           C  
ANISOU 2659  C   CYS C 149     5742   5011  10119    775    403    224       C  
ATOM   2660  O   CYS C 149      28.129 -32.051  45.785  1.00 56.98           O  
ANISOU 2660  O   CYS C 149     6014   5269  10368    826    386    273       O  
ATOM   2661  CB  CYS C 149      26.446 -33.748  43.629  1.00 54.46           C  
ANISOU 2661  CB  CYS C 149     5696   4865  10133    747    552    196       C  
ATOM   2662  SG  CYS C 149      26.421 -34.684  45.177  1.00 57.04           S  
ANISOU 2662  SG  CYS C 149     6063   5163  10446    812    574    260       S  
ATOM   2663  N   GLY C 150      26.927 -30.604  44.616  1.00 51.72           N  
ANISOU 2663  N   GLY C 150     5341   4638   9673    740    360    191       N  
ATOM   2664  CA  GLY C 150      26.788 -29.725  45.763  1.00 51.84           C  
ANISOU 2664  CA  GLY C 150     5378   4688   9630    761    297    212       C  
ATOM   2665  C   GLY C 150      27.991 -28.829  45.959  1.00 51.60           C  
ANISOU 2665  C   GLY C 150     5321   4701   9584    777    219    228       C  
ATOM   2666  O   GLY C 150      28.299 -28.374  47.072  1.00 52.54           O  
ANISOU 2666  O   GLY C 150     5454   4845   9665    813    169    263       O  
ATOM   2667  N   LYS C 151      28.691 -28.597  44.856  1.00 50.64           N  
ANISOU 2667  N   LYS C 151     5159   4589   9492    751    211    202       N  
ATOM   2668  CA  LYS C 151      29.895 -27.780  44.829  1.00 50.36           C  
ANISOU 2668  CA  LYS C 151     5092   4594   9448    760    141    211       C  
ATOM   2669  C   LYS C 151      29.787 -26.933  43.584  1.00 49.46           C  
ANISOU 2669  C   LYS C 151     4952   4503   9339    702    122    156       C  
ATOM   2670  O   LYS C 151      30.351 -27.271  42.559  1.00 49.45           O  
ANISOU 2670  O   LYS C 151     4918   4491   9380    684    146    138       O  
ATOM   2671  CB  LYS C 151      31.165 -28.628  44.785  1.00 50.79           C  
ANISOU 2671  CB  LYS C 151     5120   4633   9546    798    157    245       C  
ATOM   2672  CG  LYS C 151      31.220 -29.775  45.766  1.00 51.72           C  
ANISOU 2672  CG  LYS C 151     5262   4715   9674    851    197    295       C  
ATOM   2673  CD  LYS C 151      31.387 -29.306  47.203  1.00 52.15           C  
ANISOU 2673  CD  LYS C 151     5341   4794   9680    895    142    337       C  
ATOM   2674  CE  LYS C 151      31.367 -30.502  48.168  1.00 53.10           C  
ANISOU 2674  CE  LYS C 151     5490   4876   9811    948    187    386       C  
ATOM   2675  NZ  LYS C 151      31.484 -30.087  49.592  1.00 53.96           N  
ANISOU 2675  NZ  LYS C 151     5624   5007   9872    992    137    428       N  
ATOM   2676  N   PRO C 152      28.986 -25.866  43.634  1.00 52.17           N  
ANISOU 2676  N   PRO C 152     5311   4875   9638    671     84    127       N  
ATOM   2677  CA  PRO C 152      29.015 -25.027  42.436  1.00 51.34           C  
ANISOU 2677  CA  PRO C 152     5178   4792   9535    617     61     77       C  
ATOM   2678  C   PRO C 152      30.277 -24.161  42.423  1.00 51.07           C  
ANISOU 2678  C   PRO C 152     5113   4800   9491    625    -11     87       C  
ATOM   2679  O   PRO C 152      30.740 -23.669  43.470  1.00 51.34           O  
ANISOU 2679  O   PRO C 152     5155   4860   9491    660    -66    122       O  
ATOM   2680  CB  PRO C 152      27.737 -24.188  42.559  1.00 50.97           C  
ANISOU 2680  CB  PRO C 152     5162   4762   9444    585     43     44       C  
ATOM   2681  CG  PRO C 152      27.442 -24.175  44.009  1.00 51.56           C  
ANISOU 2681  CG  PRO C 152     5271   4841   9478    627     23     85       C  
ATOM   2682  CD  PRO C 152      28.052 -25.366  44.659  1.00 52.35           C  
ANISOU 2682  CD  PRO C 152     5373   4910   9606    679     60    136       C  
ATOM   2683  N   LYS C 153      30.813 -23.971  41.223  1.00 59.43           N  
ANISOU 2683  N   LYS C 153     6135   5864  10580    591    -11     55       N  
ATOM   2684  CA  LYS C 153      32.030 -23.208  41.044  1.00 59.74           C  
ANISOU 2684  CA  LYS C 153     6141   5941  10615    593    -73     60       C  
ATOM   2685  C   LYS C 153      31.913 -21.784  41.582  1.00 59.57           C  
ANISOU 2685  C   LYS C 153     6131   5968  10535    584   -154     54       C  
ATOM   2686  O   LYS C 153      32.841 -21.303  42.233  1.00 59.88           O  
ANISOU 2686  O   LYS C 153     6159   6037  10555    614   -211     85       O  
ATOM   2687  CB  LYS C 153      32.413 -23.166  39.578  1.00 61.65           C  
ANISOU 2687  CB  LYS C 153     6346   6181  10896    549    -57     19       C  
ATOM   2688  CG  LYS C 153      33.705 -22.430  39.336  1.00 62.48           C  
ANISOU 2688  CG  LYS C 153     6414   6324  11000    549   -117     23       C  
ATOM   2689  CD  LYS C 153      34.841 -23.017  40.184  1.00 61.66           C  
ANISOU 2689  CD  LYS C 153     6299   6219  10909    608   -127     78       C  
ATOM   2690  CE  LYS C 153      36.115 -23.283  39.356  1.00 63.90           C  
ANISOU 2690  CE  LYS C 153     6536   6506  11237    606   -125     76       C  
ATOM   2691  NZ  LYS C 153      37.001 -22.077  39.188  1.00 61.64           N  
ANISOU 2691  NZ  LYS C 153     6223   6269  10928    593   -202     67       N  
ATOM   2692  N   ASN C 154      30.802 -21.102  41.294  1.00 61.05           N  
ANISOU 2692  N   ASN C 154     6338   6164  10693    544   -161     15       N  
ATOM   2693  CA  ASN C 154      30.537 -19.778  41.884  1.00 60.15           C  
ANISOU 2693  CA  ASN C 154     6240   6094  10520    537   -235     10       C  
ATOM   2694  C   ASN C 154      29.186 -19.791  42.582  1.00 59.91           C  
ANISOU 2694  C   ASN C 154     6254   6053  10456    538   -219      7       C  
ATOM   2695  O   ASN C 154      28.157 -19.661  41.928  1.00 59.88           O  
ANISOU 2695  O   ASN C 154     6262   6039  10450    497   -192    -35       O  
ATOM   2696  CB  ASN C 154      30.579 -18.628  40.855  1.00 61.63           C  
ANISOU 2696  CB  ASN C 154     6408   6313  10695    483   -277    -39       C  
ATOM   2697  CG  ASN C 154      31.028 -19.074  39.468  1.00 63.25           C  
ANISOU 2697  CG  ASN C 154     6578   6501  10953    451   -238    -69       C  
ATOM   2698  OD1 ASN C 154      30.191 -19.420  38.633  1.00 61.97           O  
ANISOU 2698  OD1 ASN C 154     6421   6313  10810    415   -187   -106       O  
ATOM   2699  ND2 ASN C 154      32.338 -19.046  39.207  1.00 66.47           N  
ANISOU 2699  ND2 ASN C 154     6950   6922  11383    462   -261    -54       N  
ATOM   2700  N   PRO C 155      29.192 -20.000  43.909  1.00 60.45           N  
ANISOU 2700  N   PRO C 155     6347   6122  10500    587   -231     53       N  
ATOM   2701  CA  PRO C 155      27.980 -20.051  44.748  1.00 60.74           C  
ANISOU 2701  CA  PRO C 155     6428   6150  10501    596   -219     59       C  
ATOM   2702  C   PRO C 155      27.403 -18.649  44.988  1.00 60.70           C  
ANISOU 2702  C   PRO C 155     6438   6186  10438    572   -285     34       C  
ATOM   2703  O   PRO C 155      27.973 -17.667  44.510  1.00 61.24           O  
ANISOU 2703  O   PRO C 155     6485   6290  10492    554   -344     20       O  
ATOM   2704  CB  PRO C 155      28.482 -20.692  46.045  1.00 61.69           C  
ANISOU 2704  CB  PRO C 155     6562   6262  10617    659   -220    120       C  
ATOM   2705  CG  PRO C 155      29.954 -20.298  46.112  1.00 61.29           C  
ANISOU 2705  CG  PRO C 155     6476   6238  10572    679   -273    143       C  
ATOM   2706  CD  PRO C 155      30.438 -20.066  44.698  1.00 60.40           C  
ANISOU 2706  CD  PRO C 155     6326   6126  10497    637   -262    104       C  
ATOM   2707  N   ALA C 156      26.292 -18.532  45.701  1.00 66.72           N  
ANISOU 2707  N   ALA C 156     7238   6944  11169    570   -274     28       N  
ATOM   2708  CA  ALA C 156      25.658 -17.226  45.738  1.00 66.26           C  
ANISOU 2708  CA  ALA C 156     7193   6922  11061    539   -330     -4       C  
ATOM   2709  C   ALA C 156      25.931 -16.470  47.058  1.00 68.00           C  
ANISOU 2709  C   ALA C 156     7432   7176  11228    576   -397     32       C  
ATOM   2710  O   ALA C 156      25.172 -16.635  48.032  1.00 68.28           O  
ANISOU 2710  O   ALA C 156     7503   7205  11235    596   -388     47       O  
ATOM   2711  CB  ALA C 156      24.144 -17.395  45.514  1.00 65.88           C  
ANISOU 2711  CB  ALA C 156     7173   6853  11005    508   -283    -42       C  
ATOM   2712  N   ASN C 157      26.885 -15.526  47.016  1.00 74.31           N  
ANISOU 2712  N   ASN C 157     8209   8013  12011    578   -467     38       N  
ATOM   2713  CA  ASN C 157      27.604 -15.029  48.209  1.00 75.17           C  
ANISOU 2713  CA  ASN C 157     8327   8153  12083    622   -530     82       C  
ATOM   2714  C   ASN C 157      29.039 -14.618  47.845  1.00 75.50           C  
ANISOU 2714  C   ASN C 157     8331   8219  12138    630   -577     96       C  
ATOM   2715  O   ASN C 157      30.016 -15.142  48.399  1.00 76.37           O  
ANISOU 2715  O   ASN C 157     8431   8326  12261    676   -581    142       O  
ATOM   2716  CB  ASN C 157      27.668 -16.089  49.344  1.00 66.50           C  
ANISOU 2716  CB  ASN C 157     7250   7028  10989    677   -495    134       C  
ATOM   2717  CG  ASN C 157      27.545 -15.471  50.764  1.00 67.36           C  
ANISOU 2717  CG  ASN C 157     7389   7164  11040    709   -551    164       C  
ATOM   2718  OD1 ASN C 157      28.575 -15.157  51.406  1.00 68.20           O  
ANISOU 2718  OD1 ASN C 157     7487   7291  11134    747   -598    204       O  
ATOM   2719  ND2 ASN C 157      26.286 -15.305  51.258  1.00 67.19           N  
ANISOU 2719  ND2 ASN C 157     7402   7144  10983    694   -546    145       N  
ATOM   2720  N   ILE C 158       9.047 -16.979  40.092  1.00 43.72           N  
ANISOU 2720  N   ILE C 158     4568   3941   8104    102     85   -571       N  
ATOM   2721  CA  ILE C 158       9.502 -16.201  41.242  1.00 43.61           C  
ANISOU 2721  CA  ILE C 158     4566   3960   8042    135     14   -533       C  
ATOM   2722  C   ILE C 158       9.124 -14.734  41.060  1.00 42.75           C  
ANISOU 2722  C   ILE C 158     4463   3895   7884    109    -59   -572       C  
ATOM   2723  O   ILE C 158       9.462 -14.121  40.036  1.00 42.42           O  
ANISOU 2723  O   ILE C 158     4400   3866   7850     77    -84   -606       O  
ATOM   2724  CB  ILE C 158      11.033 -16.330  41.443  1.00 44.11           C  
ANISOU 2724  CB  ILE C 158     4606   4028   8127    166    -13   -485       C  
ATOM   2725  CG1 ILE C 158      11.467 -17.803  41.360  1.00 45.01           C  
ANISOU 2725  CG1 ILE C 158     4710   4096   8297    186     62   -454       C  
ATOM   2726  CG2 ILE C 158      11.455 -15.707  42.776  1.00 43.99           C  
ANISOU 2726  CG2 ILE C 158     4606   4043   8065    206    -77   -441       C  
ATOM   2727  CD1 ILE C 158      12.792 -18.104  41.969  1.00 45.52           C  
ANISOU 2727  CD1 ILE C 158     4761   4161   8375    229     42   -396       C  
ATOM   2728  N   LEU C 159       8.393 -14.176  42.018  1.00 45.39           N  
ANISOU 2728  N   LEU C 159     4827   4252   8168    121    -90   -569       N  
ATOM   2729  CA  LEU C 159       7.934 -12.790  41.866  1.00 44.74           C  
ANISOU 2729  CA  LEU C 159     4753   4210   8036     96   -158   -608       C  
ATOM   2730  C   LEU C 159       9.033 -11.792  42.224  1.00 44.62           C  
ANISOU 2730  C   LEU C 159     4727   4232   7994    112   -242   -583       C  
ATOM   2731  O   LEU C 159       9.296 -10.817  41.480  1.00 44.35           O  
ANISOU 2731  O   LEU C 159     4680   4222   7948     83   -290   -615       O  
ATOM   2732  CB  LEU C 159       6.689 -12.522  42.711  1.00 44.47           C  
ANISOU 2732  CB  LEU C 159     4753   4187   7955    101   -162   -619       C  
ATOM   2733  CG  LEU C 159       5.488 -13.348  42.280  1.00 44.74           C  
ANISOU 2733  CG  LEU C 159     4799   4190   8011     79    -84   -653       C  
ATOM   2734  CD1 LEU C 159       4.333 -13.112  43.224  1.00 44.64           C  
ANISOU 2734  CD1 LEU C 159     4820   4190   7952     88    -89   -659       C  
ATOM   2735  CD2 LEU C 159       5.139 -13.048  40.846  1.00 44.60           C  
ANISOU 2735  CD2 LEU C 159     4764   4169   8012     29    -73   -714       C  
ATOM   2736  N   GLY C 160       9.683 -12.051  43.349  1.00 42.46           N  
ANISOU 2736  N   GLY C 160     4459   3961   7712    158   -257   -525       N  
ATOM   2737  CA  GLY C 160      10.797 -11.229  43.768  1.00 42.42           C  
ANISOU 2737  CA  GLY C 160     4444   3989   7686    178   -332   -495       C  
ATOM   2738  C   GLY C 160      12.105 -11.538  43.049  1.00 42.84           C  
ANISOU 2738  C   GLY C 160     4462   4033   7784    178   -329   -480       C  
ATOM   2739  O   GLY C 160      12.113 -12.005  41.892  1.00 42.94           O  
ANISOU 2739  O   GLY C 160     4454   4022   7839    148   -284   -510       O  
ATOM   2740  N   GLY C 161      13.202 -11.290  43.775  1.00 41.82           N  
ANISOU 2740  N   GLY C 161     4324   3921   7645    213   -376   -433       N  
ATOM   2741  CA  GLY C 161      14.506 -10.928  43.221  1.00 42.10           C  
ANISOU 2741  CA  GLY C 161     4327   3970   7699    210   -413   -424       C  
ATOM   2742  C   GLY C 161      15.593 -11.969  43.082  1.00 42.85           C  
ANISOU 2742  C   GLY C 161     4397   4038   7847    233   -374   -386       C  
ATOM   2743  O   GLY C 161      15.320 -13.123  42.761  1.00 43.13           O  
ANISOU 2743  O   GLY C 161     4430   4033   7924    233   -299   -385       O  
ATOM   2744  N   HIS C 162      16.835 -11.524  43.306  1.00 38.19           N  
ANISOU 2744  N   HIS C 162     5390   6081   3040   1173    154   -820       N  
ATOM   2745  CA  HIS C 162      18.084 -12.292  43.144  1.00 38.15           C  
ANISOU 2745  CA  HIS C 162     5396   6048   3050   1161    164   -840       C  
ATOM   2746  C   HIS C 162      18.298 -12.783  41.711  1.00 38.64           C  
ANISOU 2746  C   HIS C 162     5473   6115   3092   1158    162   -852       C  
ATOM   2747  O   HIS C 162      18.006 -13.917  41.381  1.00 39.01           O  
ANISOU 2747  O   HIS C 162     5522   6170   3130   1145    144   -871       O  
ATOM   2748  CB  HIS C 162      18.119 -13.416  44.137  1.00 38.21           C  
ANISOU 2748  CB  HIS C 162     5396   6046   3075   1145    152   -858       C  
ATOM   2749  CG  HIS C 162      17.892 -12.970  45.542  1.00 37.76           C  
ANISOU 2749  CG  HIS C 162     5325   5984   3037   1147    154   -847       C  
ATOM   2750  ND1 HIS C 162      18.829 -12.264  46.257  1.00 37.59           N  
ANISOU 2750  ND1 HIS C 162     5304   5937   3041   1151    177   -837       N  
ATOM   2751  CD2 HIS C 162      16.823 -13.108  46.363  1.00 37.70           C  
ANISOU 2751  CD2 HIS C 162     5302   5994   3028   1146    137   -843       C  
ATOM   2752  CE1 HIS C 162      18.359 -11.995  47.462  1.00 37.46           C  
ANISOU 2752  CE1 HIS C 162     5273   5922   3037   1153    173   -828       C  
ATOM   2753  NE2 HIS C 162      17.147 -12.505  47.557  1.00 37.44           N  
ANISOU 2753  NE2 HIS C 162     5261   5947   3019   1150    149   -832       N  
ATOM   2754  N   LEU C 163      18.698 -11.863  40.834  1.00 42.58           N  
ANISOU 2754  N   LEU C 163     5982   6613   3582   1170    178   -839       N  
ATOM   2755  CA  LEU C 163      19.073 -12.174  39.454  1.00 42.97           C  
ANISOU 2755  CA  LEU C 163     6047   6664   3615   1168    180   -848       C  
ATOM   2756  C   LEU C 163      20.264 -13.120  39.506  1.00 42.65           C  
ANISOU 2756  C   LEU C 163     6016   6595   3593   1153    188   -870       C  
ATOM   2757  O   LEU C 163      21.132 -12.993  40.398  1.00 42.27           O  
ANISOU 2757  O   LEU C 163     5967   6521   3573   1150    202   -870       O  
ATOM   2758  CB  LEU C 163      19.410 -10.895  38.684  1.00 43.49           C  
ANISOU 2758  CB  LEU C 163     6122   6730   3673   1185    199   -829       C  
ATOM   2759  CG  LEU C 163      19.876 -10.821  37.232  1.00 44.09           C  
ANISOU 2759  CG  LEU C 163     6214   6806   3733   1187    207   -833       C  
ATOM   2760  CD1 LEU C 163      21.334 -11.058  37.136  1.00 44.21           C  
ANISOU 2760  CD1 LEU C 163     6241   6789   3767   1180    227   -843       C  
ATOM   2761  CD2 LEU C 163      19.171 -11.796  36.401  1.00 44.43           C  
ANISOU 2761  CD2 LEU C 163     6260   6870   3751   1179    186   -848       C  
ATOM   2762  N   ASP C 164      20.334 -14.073  38.576  1.00 48.73           N  
ANISOU 2762  N   ASP C 164     6796   7369   4350   1143    178   -888       N  
ATOM   2763  CA  ASP C 164      21.417 -15.040  38.675  1.00 48.61           C  
ANISOU 2763  CA  ASP C 164     6790   7328   4353   1128    184   -909       C  
ATOM   2764  C   ASP C 164      22.587 -14.553  37.832  1.00 48.97           C  
ANISOU 2764  C   ASP C 164     6851   7354   4402   1132    207   -907       C  
ATOM   2765  O   ASP C 164      22.637 -14.750  36.610  1.00 49.55           O  
ANISOU 2765  O   ASP C 164     6935   7435   4455   1132    206   -913       O  
ATOM   2766  CB  ASP C 164      20.933 -16.406  38.208  1.00 48.86           C  
ANISOU 2766  CB  ASP C 164     6822   7371   4370   1113    162   -932       C  
ATOM   2767  CG  ASP C 164      22.021 -17.421  38.191  1.00 48.87           C  
ANISOU 2767  CG  ASP C 164     6833   7346   4388   1098    167   -954       C  
ATOM   2768  OD1 ASP C 164      22.893 -17.326  39.082  1.00 48.36           O  
ANISOU 2768  OD1 ASP C 164     6767   7256   4352   1095    181   -954       O  
ATOM   2769  OD2 ASP C 164      21.995 -18.292  37.284  1.00 49.49           O  
ANISOU 2769  OD2 ASP C 164     6921   7431   4453   1089    157   -970       O  
ATOM   2770  N   ALA C 165      23.560 -13.965  38.508  1.00 50.61           N  
ANISOU 2770  N   ALA C 165     7059   7536   4635   1135    228   -900       N  
ATOM   2771  CA  ALA C 165      24.575 -13.238  37.801  1.00 51.02           C  
ANISOU 2771  CA  ALA C 165     7123   7571   4691   1142    252   -893       C  
ATOM   2772  C   ALA C 165      25.628 -14.202  37.311  1.00 51.28           C  
ANISOU 2772  C   ALA C 165     7169   7583   4733   1127    257   -915       C  
ATOM   2773  O   ALA C 165      26.081 -14.168  36.152  1.00 51.89           O  
ANISOU 2773  O   ALA C 165     7260   7659   4798   1129    265   -918       O  
ATOM   2774  CB  ALA C 165      25.160 -12.208  38.701  1.00 50.76           C  
ANISOU 2774  CB  ALA C 165     7085   7520   4682   1150    271   -876       C  
ATOM   2775  N   LYS C 166      26.010 -15.042  38.267  1.00 58.67           N  
ANISOU 2775  N   LYS C 166     8100   8502   5691   1114    254   -928       N  
ATOM   2776  CA  LYS C 166      27.107 -15.998  38.178  1.00 58.85           C  
ANISOU 2776  CA  LYS C 166     8132   8499   5730   1099    260   -949       C  
ATOM   2777  C   LYS C 166      26.780 -17.360  37.547  1.00 59.13           C  
ANISOU 2777  C   LYS C 166     8172   8544   5751   1085    241   -972       C  
ATOM   2778  O   LYS C 166      27.667 -18.014  36.992  1.00 59.62           O  
ANISOU 2778  O   LYS C 166     8245   8589   5817   1075    248   -988       O  
ATOM   2779  CB  LYS C 166      27.657 -16.214  39.588  1.00 58.38           C  
ANISOU 2779  CB  LYS C 166     8064   8416   5703   1091    266   -952       C  
ATOM   2780  CG  LYS C 166      27.074 -15.222  40.604  1.00 57.77           C  
ANISOU 2780  CG  LYS C 166     7972   8346   5633   1102    267   -931       C  
ATOM   2781  CD  LYS C 166      28.108 -14.844  41.663  1.00 57.72           C  
ANISOU 2781  CD  LYS C 166     7962   8308   5661   1100    286   -925       C  
ATOM   2782  CE  LYS C 166      27.507 -13.937  42.732  1.00 57.19           C  
ANISOU 2782  CE  LYS C 166     7881   8248   5602   1110    287   -905       C  
ATOM   2783  NZ  LYS C 166      28.458 -13.699  43.856  1.00 57.28           N  
ANISOU 2783  NZ  LYS C 166     7887   8228   5647   1106    303   -902       N  
ATOM   2784  N   GLY C 167      25.519 -17.779  37.623  1.00 52.60           N  
ANISOU 2784  N   GLY C 167     7337   7744   4906   1084    217   -975       N  
ATOM   2785  CA  GLY C 167      25.171 -19.169  37.412  1.00 52.87           C  
ANISOU 2785  CA  GLY C 167     7371   7785   4933   1068    197   -997       C  
ATOM   2786  C   GLY C 167      25.437 -19.988  38.656  1.00 52.32           C  
ANISOU 2786  C   GLY C 167     7293   7699   4889   1054    192  -1010       C  
ATOM   2787  O   GLY C 167      26.026 -21.047  38.568  1.00 52.52           O  
ANISOU 2787  O   GLY C 167     7323   7708   4923   1039    189  -1030       O  
ATOM   2788  N   SER C 168      25.001 -19.498  39.813  1.00 49.17           N  
ANISOU 2788  N   SER C 168     6880   7302   4502   1059    190   -998       N  
ATOM   2789  CA  SER C 168      25.150 -20.178  41.115  1.00 48.77           C  
ANISOU 2789  CA  SER C 168     6818   7235   4476   1048    184  -1007       C  
ATOM   2790  C   SER C 168      24.276 -21.423  41.318  1.00 48.97           C  
ANISOU 2790  C   SER C 168     6836   7277   4494   1034    157  -1025       C  
ATOM   2791  O   SER C 168      24.231 -21.995  42.423  1.00 48.87           O  
ANISOU 2791  O   SER C 168     6814   7255   4500   1024    149  -1032       O  
ATOM   2792  CB  SER C 168      24.863 -19.208  42.254  1.00 48.51           C  
ANISOU 2792  CB  SER C 168     6772   7202   4456   1058    190   -987       C  
ATOM   2793  OG  SER C 168      25.796 -18.154  42.235  1.00 48.35           O  
ANISOU 2793  OG  SER C 168     6758   7163   4449   1068    216   -973       O  
ATOM   2794  N   PHE C 169      23.494 -21.758  40.295  1.00 46.92           N  
ANISOU 2794  N   PHE C 169     6581   7042   4206   1034    141  -1029       N  
ATOM   2795  CA  PHE C 169      22.534 -22.852  40.405  1.00 47.20           C  
ANISOU 2795  CA  PHE C 169     6608   7095   4231   1022    114  -1044       C  
ATOM   2796  C   PHE C 169      22.640 -23.778  39.202  1.00 48.02           C  
ANISOU 2796  C   PHE C 169     6724   7203   4318   1012    106  -1062       C  
ATOM   2797  O   PHE C 169      21.751 -23.827  38.371  1.00 48.51           O  
ANISOU 2797  O   PHE C 169     6787   7291   4353   1015     92  -1061       O  
ATOM   2798  CB  PHE C 169      21.103 -22.281  40.584  1.00 47.02           C  
ANISOU 2798  CB  PHE C 169     6573   7105   4189   1032     98  -1028       C  
ATOM   2799  CG  PHE C 169      20.938 -21.540  41.869  1.00 46.36           C  
ANISOU 2799  CG  PHE C 169     6476   7017   4123   1040    103  -1013       C  
ATOM   2800  CD1 PHE C 169      20.506 -22.190  43.010  1.00 46.19           C  
ANISOU 2800  CD1 PHE C 169     6441   6995   4115   1029     88  -1021       C  
ATOM   2801  CD2 PHE C 169      21.317 -20.216  41.958  1.00 46.00           C  
ANISOU 2801  CD2 PHE C 169     6432   6965   4082   1056    124   -992       C  
ATOM   2802  CE1 PHE C 169      20.416 -21.521  44.216  1.00 45.71           C  
ANISOU 2802  CE1 PHE C 169     6368   6928   4071   1036     94  -1007       C  
ATOM   2803  CE2 PHE C 169      21.240 -19.538  43.153  1.00 45.54           C  
ANISOU 2803  CE2 PHE C 169     6362   6901   4040   1062    130   -978       C  
ATOM   2804  CZ  PHE C 169      20.778 -20.188  44.290  1.00 45.40           C  
ANISOU 2804  CZ  PHE C 169     6331   6883   4036   1052    115   -986       C  
ATOM   2805  N   PRO C 170      23.754 -24.521  39.115  1.00 51.25           N  
ANISOU 2805  N   PRO C 170     7143   7586   4744   1000    115  -1079       N  
ATOM   2806  CA  PRO C 170      24.100 -25.319  37.935  1.00 52.19           C  
ANISOU 2806  CA  PRO C 170     7275   7704   4850    991    113  -1095       C  
ATOM   2807  C   PRO C 170      23.209 -26.534  37.777  1.00 52.78           C  
ANISOU 2807  C   PRO C 170     7345   7796   4912    977     85  -1112       C  
ATOM   2808  O   PRO C 170      23.167 -27.100  36.689  1.00 53.66           O  
ANISOU 2808  O   PRO C 170     7467   7916   5007    971     79  -1123       O  
ATOM   2809  CB  PRO C 170      25.552 -25.734  38.198  1.00 52.31           C  
ANISOU 2809  CB  PRO C 170     7299   7683   4892    981    131  -1107       C  
ATOM   2810  CG  PRO C 170      26.015 -24.808  39.282  1.00 51.45           C  
ANISOU 2810  CG  PRO C 170     7183   7559   4807    990    148  -1091       C  
ATOM   2811  CD  PRO C 170      24.807 -24.618  40.135  1.00 50.86           C  
ANISOU 2811  CD  PRO C 170     7092   7505   4728    994    130  -1082       C  
ATOM   2812  N   TRP C 171      22.516 -26.914  38.844  1.00 49.53           N  
ANISOU 2812  N   TRP C 171     6919   7391   4510    971     69  -1114       N  
ATOM   2813  CA  TRP C 171      21.623 -28.052  38.825  1.00 50.15           C  
ANISOU 2813  CA  TRP C 171     6991   7486   4579    957     42  -1129       C  
ATOM   2814  C   TRP C 171      20.205 -27.694  38.390  1.00 50.33           C  
ANISOU 2814  C   TRP C 171     7007   7545   4573    965     24  -1118       C  
ATOM   2815  O   TRP C 171      19.314 -28.530  38.450  1.00 50.84           O  
ANISOU 2815  O   TRP C 171     7062   7625   4628    955      0  -1128       O  
ATOM   2816  CB  TRP C 171      21.575 -28.683  40.211  1.00 49.77           C  
ANISOU 2816  CB  TRP C 171     6929   7427   4556    946     33  -1137       C  
ATOM   2817  CG  TRP C 171      21.225 -27.713  41.299  1.00 48.81           C  
ANISOU 2817  CG  TRP C 171     6794   7307   4443    957     38  -1118       C  
ATOM   2818  CD1 TRP C 171      19.979 -27.237  41.614  1.00 48.53           C  
ANISOU 2818  CD1 TRP C 171     6747   7299   4395    965     23  -1105       C  
ATOM   2819  CD2 TRP C 171      22.135 -27.083  42.212  1.00 48.10           C  
ANISOU 2819  CD2 TRP C 171     6704   7192   4380    962     59  -1110       C  
ATOM   2820  NE1 TRP C 171      20.059 -26.353  42.674  1.00 47.72           N  
ANISOU 2820  NE1 TRP C 171     6635   7190   4308    975     34  -1089       N  
ATOM   2821  CE2 TRP C 171      21.368 -26.238  43.057  1.00 47.46           C  
ANISOU 2821  CE2 TRP C 171     6608   7124   4299    973     56  -1092       C  
ATOM   2822  CE3 TRP C 171      23.527 -27.145  42.399  1.00 48.07           C  
ANISOU 2822  CE3 TRP C 171     6708   7155   4400    958     80  -1116       C  
ATOM   2823  CZ2 TRP C 171      21.944 -25.476  44.075  1.00 46.85           C  
ANISOU 2823  CZ2 TRP C 171     6526   7028   4245    980     73  -1080       C  
ATOM   2824  CZ3 TRP C 171      24.096 -26.380  43.413  1.00 47.43           C  
ANISOU 2824  CZ3 TRP C 171     6623   7057   4343    965     97  -1103       C  
ATOM   2825  CH2 TRP C 171      23.304 -25.559  44.237  1.00 46.85           C  
ANISOU 2825  CH2 TRP C 171     6536   6997   4269    976     93  -1086       C  
ATOM   2826  N   GLN C 172      19.977 -26.442  37.999  1.00 48.03           N  
ANISOU 2826  N   GLN C 172     6717   7266   4268    984     34  -1097       N  
ATOM   2827  CA  GLN C 172      18.646 -25.975  37.617  1.00 48.29           C  
ANISOU 2827  CA  GLN C 172     6742   7332   4275    993     18  -1084       C  
ATOM   2828  C   GLN C 172      18.330 -26.233  36.133  1.00 49.48           C  
ANISOU 2828  C   GLN C 172     6904   7500   4397    993     11  -1090       C  
ATOM   2829  O   GLN C 172      19.051 -25.752  35.243  1.00 49.79           O  
ANISOU 2829  O   GLN C 172     6957   7531   4430   1000     29  -1086       O  
ATOM   2830  CB  GLN C 172      18.518 -24.485  37.912  1.00 47.56           C  
ANISOU 2830  CB  GLN C 172     6646   7244   4181   1013     33  -1059       C  
ATOM   2831  CG  GLN C 172      17.249 -23.893  37.385  1.00 47.97           C  
ANISOU 2831  CG  GLN C 172     6691   7329   4205   1024     19  -1044       C  
ATOM   2832  CD  GLN C 172      16.046 -24.521  38.032  1.00 48.10           C  
ANISOU 2832  CD  GLN C 172     6692   7365   4217   1016     -7  -1048       C  
ATOM   2833  OE1 GLN C 172      15.731 -24.231  39.193  1.00 47.47           O  
ANISOU 2833  OE1 GLN C 172     6599   7285   4152   1018    -10  -1040       O  
ATOM   2834  NE2 GLN C 172      15.371 -25.408  37.300  1.00 49.01           N  
ANISOU 2834  NE2 GLN C 172     6809   7499   4315   1006    -28  -1061       N  
ATOM   2835  N   ALA C 173      17.254 -26.980  35.863  1.00 46.82           N  
ANISOU 2835  N   ALA C 173     6561   7186   4044    984    -14  -1097       N  
ATOM   2836  CA  ALA C 173      16.813 -27.196  34.479  1.00 48.10           C  
ANISOU 2836  CA  ALA C 173     6732   7367   4177    984    -23  -1101       C  
ATOM   2837  C   ALA C 173      15.448 -26.542  34.150  1.00 48.40           C  
ANISOU 2837  C   ALA C 173     6761   7438   4190    996    -38  -1084       C  
ATOM   2838  O   ALA C 173      14.502 -26.522  34.957  1.00 47.92           O  
ANISOU 2838  O   ALA C 173     6685   7392   4130    995    -53  -1078       O  
ATOM   2839  CB  ALA C 173      16.759 -28.658  34.169  1.00 49.23           C  
ANISOU 2839  CB  ALA C 173     6878   7509   4320    964    -40  -1125       C  
ATOM   2840  N   LYS C 174      15.383 -26.004  32.936  1.00 50.17           N  
ANISOU 2840  N   LYS C 174     6997   7675   4391   1005    -32  -1077       N  
ATOM   2841  CA  LYS C 174      14.202 -25.352  32.430  1.00 50.69           C  
ANISOU 2841  CA  LYS C 174     7057   7772   4432   1016    -44  -1061       C  
ATOM   2842  C   LYS C 174      13.617 -26.245  31.386  1.00 52.30           C  
ANISOU 2842  C   LYS C 174     7266   7992   4614   1006    -63  -1074       C  
ATOM   2843  O   LYS C 174      14.202 -26.396  30.320  1.00 53.22           O  
ANISOU 2843  O   LYS C 174     7398   8104   4720   1005    -54  -1081       O  
ATOM   2844  CB  LYS C 174      14.536 -23.979  31.835  1.00 50.62           C  
ANISOU 2844  CB  LYS C 174     7056   7763   4413   1036    -23  -1040       C  
ATOM   2845  CG  LYS C 174      13.465 -23.387  30.933  1.00 51.64           C  
ANISOU 2845  CG  LYS C 174     7184   7923   4512   1047    -33  -1026       C  
ATOM   2846  CD  LYS C 174      13.904 -22.022  30.433  1.00 51.71           C  
ANISOU 2846  CD  LYS C 174     7202   7931   4516   1066    -11  -1007       C  
ATOM   2847  CE  LYS C 174      12.952 -21.492  29.367  1.00 52.32           C  
ANISOU 2847  CE  LYS C 174     7280   8037   4562   1076    -20   -994       C  
ATOM   2848  NZ  LYS C 174      13.540 -20.364  28.589  1.00 52.92           N  
ANISOU 2848  NZ  LYS C 174     7369   8108   4630   1092      2   -980       N  
ATOM   2849  N   MET C 175      12.463 -26.830  31.699  1.00 50.77           N  
ANISOU 2849  N   MET C 175     7059   7819   4413    998    -88  -1077       N  
ATOM   2850  CA  MET C 175      11.755 -27.700  30.770  1.00 52.49           C  
ANISOU 2850  CA  MET C 175     7279   8055   4609    987   -109  -1089       C  
ATOM   2851  C   MET C 175      10.491 -27.047  30.199  1.00 53.45           C  
ANISOU 2851  C   MET C 175     7395   8210   4705    998   -122  -1072       C  
ATOM   2852  O   MET C 175       9.644 -26.513  30.946  1.00 53.01           O  
ANISOU 2852  O   MET C 175     7325   8168   4650   1005   -131  -1058       O  
ATOM   2853  CB  MET C 175      11.389 -28.998  31.466  1.00 52.69           C  
ANISOU 2853  CB  MET C 175     7295   8079   4647    967   -130  -1107       C  
ATOM   2854  CG  MET C 175      10.504 -29.892  30.648  1.00 54.61           C  
ANISOU 2854  CG  MET C 175     7538   8343   4870    956   -154  -1118       C  
ATOM   2855  SD  MET C 175       9.976 -31.298  31.618  1.00 54.73           S  
ANISOU 2855  SD  MET C 175     7538   8357   4901    934   -178  -1136       S  
ATOM   2856  CE  MET C 175       9.873 -30.660  33.298  1.00 52.69           C  
ANISOU 2856  CE  MET C 175     7262   8090   4666    940   -174  -1123       C  
ATOM   2857  N   VAL C 176      10.345 -27.093  28.876  1.00 55.99           N  
ANISOU 2857  N   VAL C 176     7728   8543   5003   1000   -125  -1074       N  
ATOM   2858  CA  VAL C 176       9.151 -26.523  28.271  1.00 57.24           C  
ANISOU 2858  CA  VAL C 176     7881   8732   5135   1009   -138  -1059       C  
ATOM   2859  C   VAL C 176       8.268 -27.640  27.695  1.00 59.05           C  
ANISOU 2859  C   VAL C 176     8108   8980   5350    994   -164  -1073       C  
ATOM   2860  O   VAL C 176       8.741 -28.530  26.966  1.00 60.20           O  
ANISOU 2860  O   VAL C 176     8264   9117   5491    982   -166  -1091       O  
ATOM   2861  CB  VAL C 176       9.522 -25.445  27.197  1.00 57.82           C  
ANISOU 2861  CB  VAL C 176     7968   8809   5192   1026   -119  -1044       C  
ATOM   2862  CG1 VAL C 176      10.920 -24.926  27.427  1.00 56.44           C  
ANISOU 2862  CG1 VAL C 176     7803   8605   5035   1033    -91  -1043       C  
ATOM   2863  CG2 VAL C 176       9.396 -25.960  25.785  1.00 59.82           C  
ANISOU 2863  CG2 VAL C 176     8234   9072   5421   1021   -126  -1054       C  
ATOM   2864  N   SER C 177       6.983 -27.608  28.059  1.00 63.29           N  
ANISOU 2864  N   SER C 177     8629   9540   5878    994   -185  -1064       N  
ATOM   2865  CA  SER C 177       6.023 -28.592  27.546  1.00 65.10           C  
ANISOU 2865  CA  SER C 177     8854   9789   6092    980   -212  -1075       C  
ATOM   2866  C   SER C 177       5.705 -28.335  26.072  1.00 67.12           C  
ANISOU 2866  C   SER C 177     9121  10061   6319    986   -213  -1071       C  
ATOM   2867  O   SER C 177       6.290 -27.442  25.454  1.00 67.04           O  
ANISOU 2867  O   SER C 177     9123  10048   6302   1000   -194  -1061       O  
ATOM   2868  CB  SER C 177       4.745 -28.602  28.384  1.00 64.90           C  
ANISOU 2868  CB  SER C 177     8809   9783   6068    978   -233  -1066       C  
ATOM   2869  OG  SER C 177       4.911 -29.500  29.476  1.00 63.62           O  
ANISOU 2869  OG  SER C 177     8637   9607   5929    963   -241  -1081       O  
ATOM   2870  N   HIS C 178       4.816 -29.131  25.490  1.00 68.38           N  
ANISOU 2870  N   HIS C 178     9278  10240   6463    974   -236  -1079       N  
ATOM   2871  CA  HIS C 178       4.680 -29.075  24.044  1.00 70.52           C  
ANISOU 2871  CA  HIS C 178     9562  10523   6708    977   -237  -1079       C  
ATOM   2872  C   HIS C 178       4.174 -27.714  23.605  1.00 70.66           C  
ANISOU 2872  C   HIS C 178     9580  10560   6709    998   -231  -1055       C  
ATOM   2873  O   HIS C 178       4.576 -27.203  22.563  1.00 71.68           O  
ANISOU 2873  O   HIS C 178     9723  10690   6823   1007   -218  -1050       O  
ATOM   2874  CB  HIS C 178       3.746 -30.158  23.514  1.00 72.71           C  
ANISOU 2874  CB  HIS C 178     9835  10819   6972    961   -264  -1092       C  
ATOM   2875  CG  HIS C 178       3.824 -30.322  22.026  1.00 75.07           C  
ANISOU 2875  CG  HIS C 178    10151  11126   7248    961   -264  -1097       C  
ATOM   2876  ND1 HIS C 178       3.212 -29.452  21.146  1.00 75.96           N  
ANISOU 2876  ND1 HIS C 178    10266  11260   7336    975   -264  -1080       N  
ATOM   2877  CD2 HIS C 178       4.479 -31.230  21.264  1.00 76.87           C  
ANISOU 2877  CD2 HIS C 178    10392  11342   7472    948   -262  -1116       C  
ATOM   2878  CE1 HIS C 178       3.470 -29.831  19.906  1.00 78.21           C  
ANISOU 2878  CE1 HIS C 178    10565  11546   7604    970   -263  -1090       C  
ATOM   2879  NE2 HIS C 178       4.235 -30.908  19.950  1.00 78.80           N  
ANISOU 2879  NE2 HIS C 178    10648  11602   7692    955   -262  -1111       N  
ATOM   2880  N   HIS C 179       3.285 -27.146  24.412  1.00 70.10           N  
ANISOU 2880  N   HIS C 179     9492  10503   6640   1004   -240  -1039       N  
ATOM   2881  CA  HIS C 179       2.664 -25.847  24.157  1.00 70.27           C  
ANISOU 2881  CA  HIS C 179     9509  10542   6647   1024   -236  -1014       C  
ATOM   2882  C   HIS C 179       3.344 -24.627  24.844  1.00 68.01           C  
ANISOU 2882  C   HIS C 179     9223  10243   6375   1041   -211   -998       C  
ATOM   2883  O   HIS C 179       2.652 -23.854  25.499  1.00 67.08           O  
ANISOU 2883  O   HIS C 179     9093  10137   6259   1051   -214   -980       O  
ATOM   2884  CB  HIS C 179       1.164 -25.875  24.429  1.00 71.33           C  
ANISOU 2884  CB  HIS C 179     9627  10705   6772   1022   -261  -1005       C  
ATOM   2885  CG  HIS C 179       0.777 -26.259  25.813  1.00 70.07           C  
ANISOU 2885  CG  HIS C 179     9450  10542   6633   1014   -272  -1007       C  
ATOM   2886  ND1 HIS C 179       1.677 -26.687  26.760  1.00 68.12           N  
ANISOU 2886  ND1 HIS C 179     9202  10269   6411   1007   -262  -1018       N  
ATOM   2887  CD2 HIS C 179      -0.435 -26.271  26.413  1.00 70.58           C  
ANISOU 2887  CD2 HIS C 179     9496  10625   6696   1012   -292   -998       C  
ATOM   2888  CE1 HIS C 179       1.035 -26.946  27.885  1.00 67.49           C  
ANISOU 2888  CE1 HIS C 179     9105  10194   6345   1001   -276  -1017       C  
ATOM   2889  NE2 HIS C 179      -0.251 -26.705  27.701  1.00 68.96           N  
ANISOU 2889  NE2 HIS C 179     9280  10407   6515   1004   -294  -1005       N  
ATOM   2890  N   ASN C 180       4.675 -24.600  24.931  1.00 72.22           N  
ANISOU 2890  N   ASN C 180     9768  10748   6923   1042   -189  -1005       N  
ATOM   2891  CA  ASN C 180       5.402 -23.374  25.303  1.00 70.46           C  
ANISOU 2891  CA  ASN C 180     9549  10513   6711   1059   -164   -989       C  
ATOM   2892  C   ASN C 180       5.158 -22.985  26.756  1.00 68.62           C  
ANISOU 2892  C   ASN C 180     9299  10276   6497   1062   -164   -979       C  
ATOM   2893  O   ASN C 180       5.285 -21.806  27.138  1.00 67.63           O  
ANISOU 2893  O   ASN C 180     9171  10150   6377   1079   -149   -960       O  
ATOM   2894  CB  ASN C 180       5.004 -22.205  24.392  1.00 71.40           C  
ANISOU 2894  CB  ASN C 180     9672  10649   6807   1077   -157   -968       C  
ATOM   2895  CG  ASN C 180       6.185 -21.294  24.002  1.00 70.89           C  
ANISOU 2895  CG  ASN C 180     9623  10566   6747   1090   -128   -961       C  
ATOM   2896  OD1 ASN C 180       7.353 -21.674  24.064  1.00 70.53           O  
ANISOU 2896  OD1 ASN C 180     9587  10495   6715   1085   -113   -974       O  
ATOM   2897  ND2 ASN C 180       5.848 -20.074  23.594  1.00 71.01           N  
ANISOU 2897  ND2 ASN C 180     9638  10595   6749   1108   -120   -939       N  
ATOM   2898  N   LEU C 181       4.826 -23.987  27.568  1.00 62.85           N  
ANISOU 2898  N   LEU C 181     8557   9543   5779   1047   -181   -993       N  
ATOM   2899  CA  LEU C 181       4.677 -23.781  29.002  1.00 61.25           C  
ANISOU 2899  CA  LEU C 181     8339   9335   5598   1047   -181   -986       C  
ATOM   2900  C   LEU C 181       5.957 -24.143  29.762  1.00 59.60           C  
ANISOU 2900  C   LEU C 181     8136   9094   5417   1041   -164   -999       C  
ATOM   2901  O   LEU C 181       6.394 -25.313  29.770  1.00 59.81           O  
ANISOU 2901  O   LEU C 181     8166   9107   5451   1024   -170  -1021       O  
ATOM   2902  CB  LEU C 181       3.506 -24.589  29.537  1.00 61.98           C  
ANISOU 2902  CB  LEU C 181     8416   9444   5690   1034   -209   -992       C  
ATOM   2903  CG  LEU C 181       2.172 -23.865  29.526  1.00 62.63           C  
ANISOU 2903  CG  LEU C 181     8485   9556   5757   1044   -223   -972       C  
ATOM   2904  CD1 LEU C 181       1.184 -24.553  30.447  1.00 62.33           C  
ANISOU 2904  CD1 LEU C 181     8428   9528   5725   1032   -247   -976       C  
ATOM   2905  CD2 LEU C 181       2.386 -22.469  29.981  1.00 62.14           C  
ANISOU 2905  CD2 LEU C 181     8420   9490   5699   1064   -204   -949       C  
ATOM   2906  N   THR C 182       6.548 -23.139  30.403  1.00 53.25           N  
ANISOU 2906  N   THR C 182     7330   8276   4625   1055   -144   -985       N  
ATOM   2907  CA  THR C 182       7.851 -23.292  31.018  1.00 51.86           C  
ANISOU 2907  CA  THR C 182     7162   8069   4475   1051   -124   -994       C  
ATOM   2908  C   THR C 182       7.743 -23.888  32.427  1.00 50.70           C  
ANISOU 2908  C   THR C 182     7000   7912   4351   1040   -133  -1002       C  
ATOM   2909  O   THR C 182       6.895 -23.482  33.207  1.00 50.26           O  
ANISOU 2909  O   THR C 182     6928   7870   4297   1045   -142   -989       O  
ATOM   2910  CB  THR C 182       8.547 -21.952  31.033  1.00 51.10           C  
ANISOU 2910  CB  THR C 182     7071   7962   4383   1070    -98   -976       C  
ATOM   2911  OG1 THR C 182       8.862 -21.599  29.681  1.00 52.30           O  
ANISOU 2911  OG1 THR C 182     7238   8117   4515   1077    -88   -974       O  
ATOM   2912  CG2 THR C 182       9.801 -21.997  31.863  1.00 49.48           C  
ANISOU 2912  CG2 THR C 182     6869   7725   4206   1068    -78   -982       C  
ATOM   2913  N   THR C 183       8.584 -24.879  32.731  1.00 50.87           N  
ANISOU 2913  N   THR C 183     7026   7912   4390   1025   -131  -1023       N  
ATOM   2914  CA  THR C 183       8.463 -25.638  33.974  1.00 50.09           C  
ANISOU 2914  CA  THR C 183     6915   7805   4313   1012   -142  -1033       C  
ATOM   2915  C   THR C 183       9.804 -26.126  34.505  1.00 49.02           C  
ANISOU 2915  C   THR C 183     6786   7635   4203   1004   -125  -1048       C  
ATOM   2916  O   THR C 183      10.724 -26.386  33.721  1.00 49.31           O  
ANISOU 2916  O   THR C 183     6840   7658   4239   1002   -113  -1058       O  
ATOM   2917  CB  THR C 183       7.526 -26.861  33.785  1.00 51.37           C  
ANISOU 2917  CB  THR C 183     7070   7983   4466    995   -171  -1048       C  
ATOM   2918  OG1 THR C 183       7.699 -27.436  32.478  1.00 52.73           O  
ANISOU 2918  OG1 THR C 183     7256   8158   4620    989   -174  -1060       O  
ATOM   2919  CG2 THR C 183       6.063 -26.451  33.965  1.00 52.10           C  
ANISOU 2919  CG2 THR C 183     7147   8106   4544   1000   -190  -1032       C  
ATOM   2920  N   GLY C 184       9.906 -26.273  35.828  1.00 48.14           N  
ANISOU 2920  N   GLY C 184     6664   7512   4115    999   -126  -1049       N  
ATOM   2921  CA  GLY C 184      11.176 -26.646  36.450  1.00 47.38           C  
ANISOU 2921  CA  GLY C 184     6573   7384   4046    993   -110  -1061       C  
ATOM   2922  C   GLY C 184      11.551 -28.113  36.686  1.00 47.55           C  
ANISOU 2922  C   GLY C 184     6595   7390   4081    971   -120  -1087       C  
ATOM   2923  O   GLY C 184      10.690 -28.954  36.913  1.00 48.09           O  
ANISOU 2923  O   GLY C 184     6654   7472   4146    958   -144  -1096       O  
ATOM   2924  N   ALA C 185      12.852 -28.401  36.636  1.00 49.00           N  
ANISOU 2924  N   ALA C 185     6791   7546   4280    966   -102  -1098       N  
ATOM   2925  CA  ALA C 185      13.420 -29.730  36.945  1.00 49.08           C  
ANISOU 2925  CA  ALA C 185     6803   7537   4308    946   -108  -1122       C  
ATOM   2926  C   ALA C 185      14.849 -29.585  37.487  1.00 48.28           C  
ANISOU 2926  C   ALA C 185     6710   7402   4234    946    -84  -1126       C  
ATOM   2927  O   ALA C 185      15.610 -28.686  37.082  1.00 47.88           O  
ANISOU 2927  O   ALA C 185     6669   7340   4182    959    -61  -1116       O  
ATOM   2928  CB  ALA C 185      13.422 -30.636  35.715  1.00 49.93           C  
ANISOU 2928  CB  ALA C 185     6922   7650   4399    935   -117  -1139       C  
ATOM   2929  N   THR C 186      15.245 -30.454  38.401  1.00 47.92           N  
ANISOU 2929  N   THR C 186     6658   7337   4211    932    -88  -1141       N  
ATOM   2930  CA  THR C 186      16.591 -30.312  38.919  1.00 47.12           C  
ANISOU 2930  CA  THR C 186     6565   7204   4136    932    -65  -1144       C  
ATOM   2931  C   THR C 186      17.454 -31.565  38.692  1.00 47.93           C  
ANISOU 2931  C   THR C 186     6675   7284   4251    913    -64  -1169       C  
ATOM   2932  O   THR C 186      16.970 -32.674  38.701  1.00 48.88           O  
ANISOU 2932  O   THR C 186     6792   7412   4370    898    -84  -1184       O  
ATOM   2933  CB  THR C 186      16.538 -29.919  40.413  1.00 46.10           C  
ANISOU 2933  CB  THR C 186     6421   7066   4029    934    -62  -1136       C  
ATOM   2934  OG1 THR C 186      15.984 -30.985  41.182  1.00 46.60           O  
ANISOU 2934  OG1 THR C 186     6471   7131   4102    918    -84  -1150       O  
ATOM   2935  CG2 THR C 186      15.664 -28.712  40.585  1.00 45.61           C  
ANISOU 2935  CG2 THR C 186     6350   7027   3954    952    -63  -1112       C  
ATOM   2936  N   LEU C 187      18.744 -31.357  38.488  1.00 48.84           N  
ANISOU 2936  N   LEU C 187     6804   7374   4379    916    -41  -1171       N  
ATOM   2937  CA  LEU C 187      19.659 -32.416  38.062  1.00 49.69           C  
ANISOU 2937  CA  LEU C 187     6922   7461   4496    900    -37  -1193       C  
ATOM   2938  C   LEU C 187      20.291 -33.127  39.232  1.00 49.46           C  
ANISOU 2938  C   LEU C 187     6888   7407   4499    887    -36  -1205       C  
ATOM   2939  O   LEU C 187      21.109 -32.546  39.960  1.00 48.51           O  
ANISOU 2939  O   LEU C 187     6767   7265   4399    893    -17  -1198       O  
ATOM   2940  CB  LEU C 187      20.763 -31.832  37.200  1.00 49.63           C  
ANISOU 2940  CB  LEU C 187     6932   7438   4487    909    -12  -1189       C  
ATOM   2941  CG  LEU C 187      21.897 -32.710  36.741  1.00 50.55           C  
ANISOU 2941  CG  LEU C 187     7063   7530   4615    896     -3  -1209       C  
ATOM   2942  CD1 LEU C 187      21.449 -33.445  35.524  1.00 51.97           C  
ANISOU 2942  CD1 LEU C 187     7250   7726   4770    888    -17  -1220       C  
ATOM   2943  CD2 LEU C 187      23.044 -31.804  36.411  1.00 50.24           C  
ANISOU 2943  CD2 LEU C 187     7035   7471   4582    907     26  -1199       C  
ATOM   2944  N   ILE C 188      19.881 -34.380  39.406  1.00 50.04           N  
ANISOU 2944  N   ILE C 188     6955   7482   4575    869    -56  -1223       N  
ATOM   2945  CA  ILE C 188      20.244 -35.165  40.563  1.00 50.03           C  
ANISOU 2945  CA  ILE C 188     6946   7461   4602    855    -60  -1235       C  
ATOM   2946  C   ILE C 188      21.542 -36.031  40.375  1.00 50.71           C  
ANISOU 2946  C   ILE C 188     7044   7516   4706    841    -49  -1254       C  
ATOM   2947  O   ILE C 188      22.230 -36.393  41.356  1.00 50.40           O  
ANISOU 2947  O   ILE C 188     7001   7453   4695    833    -42  -1260       O  
ATOM   2948  CB  ILE C 188      19.016 -36.004  40.927  1.00 50.76           C  
ANISOU 2948  CB  ILE C 188     7024   7574   4688    843    -90  -1242       C  
ATOM   2949  CG1 ILE C 188      19.211 -36.767  42.241  1.00 50.58           C  
ANISOU 2949  CG1 ILE C 188     6990   7533   4694    828    -97  -1253       C  
ATOM   2950  CG2 ILE C 188      18.596 -36.902  39.739  1.00 52.42           C  
ANISOU 2950  CG2 ILE C 188     7242   7798   4877    832   -105  -1256       C  
ATOM   2951  CD1 ILE C 188      18.277 -37.972  42.373  1.00 50.82           C  
ANISOU 2951  CD1 ILE C 188     7011   7578   4721    811   -125  -1267       C  
ATOM   2952  N   ASN C 189      21.899 -36.301  39.118  1.00 52.11           N  
ANISOU 2952  N   ASN C 189     7236   7695   4869    839    -44  -1261       N  
ATOM   2953  CA  ASN C 189      23.215 -36.867  38.765  1.00 52.80           C  
ANISOU 2953  CA  ASN C 189     7337   7753   4970    830    -28  -1275       C  
ATOM   2954  C   ASN C 189      23.495 -36.721  37.267  1.00 53.60           C  
ANISOU 2954  C   ASN C 189     7455   7860   5049    835    -20  -1277       C  
ATOM   2955  O   ASN C 189      22.771 -36.062  36.563  1.00 53.35           O  
ANISOU 2955  O   ASN C 189     7425   7854   4993    847    -24  -1265       O  
ATOM   2956  CB  ASN C 189      23.363 -38.343  39.214  1.00 53.94           C  
ANISOU 2956  CB  ASN C 189     7477   7884   5132    808    -42  -1298       C  
ATOM   2957  CG  ASN C 189      22.531 -39.338  38.392  1.00 55.43           C  
ANISOU 2957  CG  ASN C 189     7667   8093   5300    796    -65  -1311       C  
ATOM   2958  OD1 ASN C 189      22.321 -39.188  37.175  1.00 56.21           O  
ANISOU 2958  OD1 ASN C 189     7776   8207   5375    801    -66  -1310       O  
ATOM   2959  ND2 ASN C 189      22.079 -40.391  39.072  1.00 55.98           N  
ANISOU 2959  ND2 ASN C 189     7726   8163   5382    779    -85  -1324       N  
ATOM   2960  N   GLU C 190      24.548 -37.338  36.770  1.00 56.96           N  
ANISOU 2960  N   GLU C 190     7894   8264   5484    826     -9  -1291       N  
ATOM   2961  CA  GLU C 190      24.964 -37.048  35.402  1.00 57.62           C  
ANISOU 2961  CA  GLU C 190     7994   8351   5549    832      3  -1290       C  
ATOM   2962  C   GLU C 190      23.890 -37.405  34.365  1.00 58.72           C  
ANISOU 2962  C   GLU C 190     8134   8520   5657    830    -17  -1294       C  
ATOM   2963  O   GLU C 190      23.913 -36.874  33.264  1.00 59.03           O  
ANISOU 2963  O   GLU C 190     8184   8569   5674    840    -10  -1287       O  
ATOM   2964  CB  GLU C 190      26.296 -37.771  35.072  1.00 58.67           C  
ANISOU 2964  CB  GLU C 190     8140   8453   5698    820     18  -1307       C  
ATOM   2965  CG  GLU C 190      27.549 -37.181  35.750  1.00 57.75           C  
ANISOU 2965  CG  GLU C 190     8026   8306   5609    825     43  -1301       C  
ATOM   2966  CD  GLU C 190      28.864 -37.763  35.208  1.00 58.87           C  
ANISOU 2966  CD  GLU C 190     8183   8421   5764    815     60  -1315       C  
ATOM   2967  OE1 GLU C 190      29.455 -37.197  34.252  1.00 59.20           O  
ANISOU 2967  OE1 GLU C 190     8239   8460   5795    823     77  -1310       O  
ATOM   2968  OE2 GLU C 190      29.317 -38.799  35.737  1.00 59.54           O  
ANISOU 2968  OE2 GLU C 190     8266   8487   5869    798     56  -1331       O  
ATOM   2969  N   GLN C 191      23.028 -38.371  34.664  1.00 58.46           N  
ANISOU 2969  N   GLN C 191     8092   8500   5622    817    -42  -1304       N  
ATOM   2970  CA  GLN C 191      22.004 -38.762  33.696  1.00 59.59           C  
ANISOU 2970  CA  GLN C 191     8236   8670   5736    814    -62  -1308       C  
ATOM   2971  C   GLN C 191      20.543 -38.408  33.991  1.00 59.20           C  
ANISOU 2971  C   GLN C 191     8171   8652   5670    820    -83  -1296       C  
ATOM   2972  O   GLN C 191      19.667 -38.603  33.135  1.00 60.25           O  
ANISOU 2972  O   GLN C 191     8305   8809   5778    819    -98  -1296       O  
ATOM   2973  CB  GLN C 191      22.079 -40.260  33.469  1.00 61.55           C  
ANISOU 2973  CB  GLN C 191     8486   8912   5989    792    -76  -1331       C  
ATOM   2974  CG  GLN C 191      22.167 -40.645  31.999  1.00 63.07           C  
ANISOU 2974  CG  GLN C 191     8693   9111   6158    789    -76  -1340       C  
ATOM   2975  CD  GLN C 191      23.101 -41.819  31.769  1.00 64.82           C  
ANISOU 2975  CD  GLN C 191     8925   9310   6395    771    -72  -1361       C  
ATOM   2976  OE1 GLN C 191      23.926 -42.179  32.640  1.00 65.12           O  
ANISOU 2976  OE1 GLN C 191     8960   9321   6461    764    -64  -1368       O  
ATOM   2977  NE2 GLN C 191      22.977 -42.427  30.593  1.00 66.12           N  
ANISOU 2977  NE2 GLN C 191     9099   9482   6540    764    -79  -1372       N  
ATOM   2978  N   TRP C 192      20.264 -37.893  35.182  1.00 57.70           N  
ANISOU 2978  N   TRP C 192     7967   8461   5494    826    -83  -1285       N  
ATOM   2979  CA  TRP C 192      18.875 -37.809  35.634  1.00 57.36           C  
ANISOU 2979  CA  TRP C 192     7909   8445   5441    827   -106  -1277       C  
ATOM   2980  C   TRP C 192      18.522 -36.488  36.276  1.00 55.63           C  
ANISOU 2980  C   TRP C 192     7681   8234   5221    846    -98  -1254       C  
ATOM   2981  O   TRP C 192      19.375 -35.826  36.899  1.00 54.44           O  
ANISOU 2981  O   TRP C 192     7532   8064   5090    853    -78  -1247       O  
ATOM   2982  CB  TRP C 192      18.560 -38.912  36.652  1.00 57.63           C  
ANISOU 2982  CB  TRP C 192     7930   8473   5494    809   -124  -1291       C  
ATOM   2983  CG  TRP C 192      18.738 -40.329  36.158  1.00 59.47           C  
ANISOU 2983  CG  TRP C 192     8168   8699   5729    789   -135  -1314       C  
ATOM   2984  CD1 TRP C 192      19.916 -41.008  35.998  1.00 60.21           C  
ANISOU 2984  CD1 TRP C 192     8273   8766   5839    778   -123  -1329       C  
ATOM   2985  CD2 TRP C 192      17.689 -41.246  35.797  1.00 60.94           C  
ANISOU 2985  CD2 TRP C 192     8348   8906   5900    776   -162  -1323       C  
ATOM   2986  NE1 TRP C 192      19.663 -42.280  35.545  1.00 62.06           N  
ANISOU 2986  NE1 TRP C 192     8509   9003   6069    760   -140  -1348       N  
ATOM   2987  CE2 TRP C 192      18.308 -42.450  35.408  1.00 62.57           C  
ANISOU 2987  CE2 TRP C 192     8562   9096   6114    759   -163  -1344       C  
ATOM   2988  CE3 TRP C 192      16.291 -41.157  35.750  1.00 61.17           C  
ANISOU 2988  CE3 TRP C 192     8366   8965   5911    778   -184  -1315       C  
ATOM   2989  CZ2 TRP C 192      17.576 -43.557  34.986  1.00 64.38           C  
ANISOU 2989  CZ2 TRP C 192     8789   9339   6334    743   -186  -1358       C  
ATOM   2990  CZ3 TRP C 192      15.577 -42.243  35.330  1.00 62.95           C  
ANISOU 2990  CZ3 TRP C 192     8588   9203   6126    762   -206  -1329       C  
ATOM   2991  CH2 TRP C 192      16.215 -43.430  34.955  1.00 64.54           C  
ANISOU 2991  CH2 TRP C 192     8798   9388   6337    745   -207  -1350       C  
ATOM   2992  N   LEU C 193      17.243 -36.137  36.152  1.00 51.01           N  
ANISOU 2992  N   LEU C 193     7086   7679   4615    852   -115  -1243       N  
ATOM   2993  CA  LEU C 193      16.680 -34.970  36.796  1.00 49.63           C  
ANISOU 2993  CA  LEU C 193     6901   7517   4439    868   -113  -1222       C  
ATOM   2994  C   LEU C 193      15.360 -35.293  37.474  1.00 49.74           C  
ANISOU 2994  C   LEU C 193     6897   7553   4450    863   -138  -1220       C  
ATOM   2995  O   LEU C 193      14.490 -35.952  36.896  1.00 51.06           O  
ANISOU 2995  O   LEU C 193     7061   7739   4599    854   -159  -1226       O  
ATOM   2996  CB  LEU C 193      16.474 -33.870  35.783  1.00 49.63           C  
ANISOU 2996  CB  LEU C 193     6909   7533   4414    886   -103  -1205       C  
ATOM   2997  CG  LEU C 193      17.632 -33.637  34.841  1.00 50.00           C  
ANISOU 2997  CG  LEU C 193     6975   7563   4458    891    -81  -1208       C  
ATOM   2998  CD1 LEU C 193      17.208 -33.962  33.447  1.00 51.50           C  
ANISOU 2998  CD1 LEU C 193     7174   7771   4621    889    -90  -1213       C  
ATOM   2999  CD2 LEU C 193      18.108 -32.205  34.953  1.00 48.65           C  
ANISOU 2999  CD2 LEU C 193     6808   7387   4290    911    -57  -1187       C  
ATOM   3000  N   LEU C 194      15.205 -34.842  38.708  1.00 50.40           N  
ANISOU 3000  N   LEU C 194     6967   7632   4550    867   -137  -1210       N  
ATOM   3001  CA  LEU C 194      13.890 -34.818  39.320  1.00 50.47           C  
ANISOU 3001  CA  LEU C 194     6959   7664   4552    866   -159  -1203       C  
ATOM   3002  C   LEU C 194      12.965 -33.753  38.681  1.00 50.45           C  
ANISOU 3002  C   LEU C 194     6955   7691   4524    884   -162  -1182       C  
ATOM   3003  O   LEU C 194      13.414 -32.769  38.079  1.00 50.18           O  
ANISOU 3003  O   LEU C 194     6931   7656   4480    899   -143  -1170       O  
ATOM   3004  CB  LEU C 194      14.008 -34.561  40.822  1.00 49.30           C  
ANISOU 3004  CB  LEU C 194     6797   7503   4430    867   -156  -1197       C  
ATOM   3005  CG  LEU C 194      14.101 -35.801  41.711  1.00 49.67           C  
ANISOU 3005  CG  LEU C 194     6836   7536   4499    846   -169  -1216       C  
ATOM   3006  CD1 LEU C 194      14.308 -35.375  43.157  1.00 48.77           C  
ANISOU 3006  CD1 LEU C 194     6712   7409   4411    849   -162  -1209       C  
ATOM   3007  CD2 LEU C 194      12.834 -36.657  41.595  1.00 50.33           C  
ANISOU 3007  CD2 LEU C 194     6909   7644   4571    834   -199  -1223       C  
ATOM   3008  N   THR C 195      11.660 -33.989  38.808  1.00 51.34           N  
ANISOU 3008  N   THR C 195     7054   7829   4623    880   -186  -1179       N  
ATOM   3009  CA  THR C 195      10.619 -33.041  38.425  1.00 51.37           C  
ANISOU 3009  CA  THR C 195     7053   7862   4604    895   -192  -1159       C  
ATOM   3010  C   THR C 195       9.350 -33.483  39.121  1.00 51.71           C  
ANISOU 3010  C   THR C 195     7077   7923   4646    886   -218  -1158       C  
ATOM   3011  O   THR C 195       9.377 -34.358  39.989  1.00 51.70           O  
ANISOU 3011  O   THR C 195     7067   7911   4664    871   -228  -1171       O  
ATOM   3012  CB  THR C 195      10.403 -32.967  36.896  1.00 52.54           C  
ANISOU 3012  CB  THR C 195     7213   8025   4724    899   -194  -1159       C  
ATOM   3013  OG1 THR C 195       9.389 -32.000  36.586  1.00 52.65           O  
ANISOU 3013  OG1 THR C 195     7221   8066   4716    914   -199  -1138       O  
ATOM   3014  CG2 THR C 195       9.995 -34.308  36.358  1.00 54.15           C  
ANISOU 3014  CG2 THR C 195     7418   8236   4921    880   -215  -1178       C  
ATOM   3015  N   THR C 196       8.237 -32.867  38.752  1.00 52.60           N  
ANISOU 3015  N   THR C 196     7183   8065   4738    896   -229  -1143       N  
ATOM   3016  CA  THR C 196       6.947 -33.186  39.343  1.00 53.10           C  
ANISOU 3016  CA  THR C 196     7229   8149   4799    889   -254  -1140       C  
ATOM   3017  C   THR C 196       6.157 -34.000  38.358  1.00 54.81           C  
ANISOU 3017  C   THR C 196     7447   8384   4995    879   -275  -1149       C  
ATOM   3018  O   THR C 196       6.339 -33.857  37.134  1.00 55.50           O  
ANISOU 3018  O   THR C 196     7547   8477   5062    884   -270  -1149       O  
ATOM   3019  CB  THR C 196       6.130 -31.944  39.662  1.00 52.52           C  
ANISOU 3019  CB  THR C 196     7145   8094   4715    907   -254  -1115       C  
ATOM   3020  OG1 THR C 196       5.590 -31.422  38.438  1.00 53.26           O  
ANISOU 3020  OG1 THR C 196     7245   8210   4780    917   -256  -1105       O  
ATOM   3021  CG2 THR C 196       6.978 -30.886  40.340  1.00 51.01           C  
ANISOU 3021  CG2 THR C 196     6956   7886   4538    922   -229  -1103       C  
ATOM   3022  N   ALA C 197       5.282 -34.852  38.885  1.00 55.89           N  
ANISOU 3022  N   ALA C 197     7569   8530   5135    864   -299  -1157       N  
ATOM   3023  CA  ALA C 197       4.298 -35.550  38.051  1.00 57.71           C  
ANISOU 3023  CA  ALA C 197     7798   8783   5347    854   -322  -1163       C  
ATOM   3024  C   ALA C 197       3.451 -34.551  37.278  1.00 58.18           C  
ANISOU 3024  C   ALA C 197     7856   8869   5379    870   -325  -1143       C  
ATOM   3025  O   ALA C 197       3.241 -34.688  36.064  1.00 59.47           O  
ANISOU 3025  O   ALA C 197     8030   9045   5521    871   -329  -1145       O  
ATOM   3026  CB  ALA C 197       3.417 -36.439  38.900  1.00 58.40           C  
ANISOU 3026  CB  ALA C 197     7868   8877   5445    838   -347  -1170       C  
ATOM   3027  N   LYS C 198       2.998 -33.529  37.994  1.00 54.75           N  
ANISOU 3027  N   LYS C 198     7412   8444   4947    884   -321  -1123       N  
ATOM   3028  CA  LYS C 198       2.252 -32.444  37.385  1.00 55.14           C  
ANISOU 3028  CA  LYS C 198     7461   8517   4974    901   -321  -1102       C  
ATOM   3029  C   LYS C 198       2.911 -31.809  36.131  1.00 55.34           C  
ANISOU 3029  C   LYS C 198     7504   8541   4981    914   -302  -1098       C  
ATOM   3030  O   LYS C 198       2.299 -31.823  35.054  1.00 56.80           O  
ANISOU 3030  O   LYS C 198     7694   8746   5143    916   -312  -1095       O  
ATOM   3031  CB  LYS C 198       1.990 -31.383  38.451  1.00 53.91           C  
ANISOU 3031  CB  LYS C 198     7293   8364   4828    915   -314  -1083       C  
ATOM   3032  CG  LYS C 198       0.527 -31.369  38.892  1.00 54.79           C  
ANISOU 3032  CG  LYS C 198     7385   8501   4932    912   -338  -1073       C  
ATOM   3033  CD  LYS C 198       0.351 -31.446  40.409  1.00 53.79           C  
ANISOU 3033  CD  LYS C 198     7243   8366   4829    907   -342  -1071       C  
ATOM   3034  CE  LYS C 198      -1.089 -31.823  40.763  1.00 54.99           C  
ANISOU 3034  CE  LYS C 198     7376   8540   4976    899   -370  -1067       C  
ATOM   3035  NZ  LYS C 198      -1.320 -31.840  42.231  1.00 54.16           N  
ANISOU 3035  NZ  LYS C 198     7256   8430   4893    895   -374  -1065       N  
ATOM   3036  N   ASN C 199       4.149 -31.300  36.250  1.00 55.87           N  
ANISOU 3036  N   ASN C 199     7583   8586   5060    923   -277  -1097       N  
ATOM   3037  CA  ASN C 199       4.808 -30.593  35.131  1.00 55.90           C  
ANISOU 3037  CA  ASN C 199     7604   8588   5049    936   -258  -1091       C  
ATOM   3038  C   ASN C 199       4.807 -31.453  33.889  1.00 57.59           C  
ANISOU 3038  C   ASN C 199     7829   8806   5246    925   -266  -1106       C  
ATOM   3039  O   ASN C 199       4.607 -30.976  32.759  1.00 58.46           O  
ANISOU 3039  O   ASN C 199     7949   8931   5334    935   -264  -1099       O  
ATOM   3040  CB  ASN C 199       6.263 -30.203  35.453  1.00 54.41           C  
ANISOU 3040  CB  ASN C 199     7426   8369   4878    942   -230  -1093       C  
ATOM   3041  CG  ASN C 199       6.386 -29.251  36.633  1.00 52.81           C  
ANISOU 3041  CG  ASN C 199     7214   8160   4693    954   -218  -1077       C  
ATOM   3042  OD1 ASN C 199       5.795 -29.475  37.689  1.00 52.62           O  
ANISOU 3042  OD1 ASN C 199     7175   8139   4681    948   -230  -1076       O  
ATOM   3043  ND2 ASN C 199       7.176 -28.194  36.470  1.00 51.77           N  
ANISOU 3043  ND2 ASN C 199     7092   8017   4562    970   -193  -1064       N  
ATOM   3044  N   LEU C 200       5.056 -32.735  34.150  1.00 58.36           N  
ANISOU 3044  N   LEU C 200     7927   8892   5357    906   -277  -1128       N  
ATOM   3045  CA  LEU C 200       5.149 -33.805  33.156  1.00 60.06           C  
ANISOU 3045  CA  LEU C 200     8151   9107   5561    892   -286  -1146       C  
ATOM   3046  C   LEU C 200       3.842 -33.984  32.400  1.00 61.92           C  
ANISOU 3046  C   LEU C 200     8382   9373   5773    889   -309  -1142       C  
ATOM   3047  O   LEU C 200       3.826 -34.149  31.175  1.00 63.38           O  
ANISOU 3047  O   LEU C 200     8578   9565   5937    889   -310  -1146       O  
ATOM   3048  CB  LEU C 200       5.531 -35.114  33.855  1.00 60.20           C  
ANISOU 3048  CB  LEU C 200     8166   9107   5602    871   -294  -1168       C  
ATOM   3049  CG  LEU C 200       6.891 -35.803  33.684  1.00 59.68           C  
ANISOU 3049  CG  LEU C 200     8114   9011   5551    861   -279  -1187       C  
ATOM   3050  CD1 LEU C 200       7.902 -34.975  32.905  1.00 59.69           C  
ANISOU 3050  CD1 LEU C 200     8133   9002   5545    876   -253  -1181       C  
ATOM   3051  CD2 LEU C 200       7.405 -36.192  35.060  1.00 58.04           C  
ANISOU 3051  CD2 LEU C 200     7898   8781   5373    853   -276  -1194       C  
ATOM   3052  N   PHE C 201       2.748 -33.906  33.152  1.00 65.08           N  
ANISOU 3052  N   PHE C 201     8764   9790   6175    888   -326  -1133       N  
ATOM   3053  CA  PHE C 201       1.416 -34.156  32.620  1.00 66.88           C  
ANISOU 3053  CA  PHE C 201     8984  10046   6383    884   -350  -1129       C  
ATOM   3054  C   PHE C 201       0.795 -32.967  31.876  1.00 67.27           C  
ANISOU 3054  C   PHE C 201     9035  10118   6408    903   -347  -1107       C  
ATOM   3055  O   PHE C 201      -0.334 -33.051  31.403  1.00 68.91           O  
ANISOU 3055  O   PHE C 201     9235  10349   6597    901   -366  -1102       O  
ATOM   3056  CB  PHE C 201       0.476 -34.582  33.757  1.00 66.80           C  
ANISOU 3056  CB  PHE C 201     8953  10043   6385    874   -371  -1128       C  
ATOM   3057  CG  PHE C 201       0.440 -36.073  33.996  1.00 67.78           C  
ANISOU 3057  CG  PHE C 201     9073  10159   6521    851   -387  -1151       C  
ATOM   3058  CD1 PHE C 201      -0.031 -36.939  33.016  1.00 69.75           C  
ANISOU 3058  CD1 PHE C 201     9327  10419   6754    839   -403  -1162       C  
ATOM   3059  CD2 PHE C 201       0.873 -36.606  35.208  1.00 66.88           C  
ANISOU 3059  CD2 PHE C 201     8952  10026   6435    840   -387  -1161       C  
ATOM   3060  CE1 PHE C 201      -0.056 -38.306  33.244  1.00 70.76           C  
ANISOU 3060  CE1 PHE C 201     9453  10539   6895    817   -418  -1183       C  
ATOM   3061  CE2 PHE C 201       0.856 -37.978  35.443  1.00 67.89           C  
ANISOU 3061  CE2 PHE C 201     9076  10144   6574    818   -402  -1181       C  
ATOM   3062  CZ  PHE C 201       0.388 -38.826  34.468  1.00 69.82           C  
ANISOU 3062  CZ  PHE C 201     9325  10400   6803    807   -417  -1192       C  
ATOM   3063  N   LEU C 202       1.503 -31.852  31.788  1.00 64.88           N  
ANISOU 3063  N   LEU C 202     8740   9806   6104    921   -323  -1094       N  
ATOM   3064  CA  LEU C 202       0.943 -30.726  31.066  1.00 65.36           C  
ANISOU 3064  CA  LEU C 202     8802   9888   6142    939   -320  -1074       C  
ATOM   3065  C   LEU C 202       0.690 -31.109  29.615  1.00 67.49           C  
ANISOU 3065  C   LEU C 202     9084  10171   6388    935   -327  -1080       C  
ATOM   3066  O   LEU C 202       1.455 -31.856  29.032  1.00 68.06           O  
ANISOU 3066  O   LEU C 202     9169  10229   6461    926   -323  -1097       O  
ATOM   3067  CB  LEU C 202       1.860 -29.504  31.132  1.00 63.71           C  
ANISOU 3067  CB  LEU C 202     8603   9667   5938    958   -292  -1060       C  
ATOM   3068  CG  LEU C 202       2.017 -28.695  32.417  1.00 61.85           C  
ANISOU 3068  CG  LEU C 202     8356   9422   5721    968   -281  -1046       C  
ATOM   3069  CD1 LEU C 202       2.774 -27.453  32.041  1.00 61.57           C  
ANISOU 3069  CD1 LEU C 202     8332   9379   5681    987   -254  -1031       C  
ATOM   3070  CD2 LEU C 202       0.697 -28.342  33.071  1.00 61.93           C  
ANISOU 3070  CD2 LEU C 202     8347   9455   5728    971   -298  -1031       C  
ATOM   3071  N   ASN C 203      -0.393 -30.586  29.055  1.00 70.06           N  
ANISOU 3071  N   ASN C 203     9405  10524   6692    943   -339  -1065       N  
ATOM   3072  CA  ASN C 203      -0.808 -30.858  27.685  1.00 72.42           C  
ANISOU 3072  CA  ASN C 203     9712  10839   6966    941   -348  -1068       C  
ATOM   3073  C   ASN C 203      -0.943 -32.353  27.418  1.00 73.97           C  
ANISOU 3073  C   ASN C 203     9910  11033   7164    918   -366  -1092       C  
ATOM   3074  O   ASN C 203      -0.651 -32.824  26.319  1.00 75.58           O  
ANISOU 3074  O   ASN C 203    10127  11236   7354    913   -366  -1102       O  
ATOM   3075  CB  ASN C 203       0.161 -30.228  26.690  1.00 72.73           C  
ANISOU 3075  CB  ASN C 203     9771  10869   6994    953   -325  -1066       C  
ATOM   3076  CG  ASN C 203      -0.460 -30.015  25.323  1.00 74.78           C  
ANISOU 3076  CG  ASN C 203    10038  11151   7225    958   -332  -1060       C  
ATOM   3077  OD1 ASN C 203      -0.001 -30.571  24.330  1.00 75.73           O  
ANISOU 3077  OD1 ASN C 203    10173  11266   7335    951   -330  -1073       O  
ATOM   3078  ND2 ASN C 203      -1.515 -29.206  25.279  1.00 75.66           N  
ANISOU 3078  ND2 ASN C 203    10139  11285   7323    969   -341  -1040       N  
ATOM   3079  N   HIS C 204      -1.391 -33.095  28.430  1.00 75.23           N  
ANISOU 3079  N   HIS C 204    10055  11190   7340    905   -382  -1099       N  
ATOM   3080  CA  HIS C 204      -1.587 -34.543  28.306  1.00 76.81           C  
ANISOU 3080  CA  HIS C 204    10253  11387   7543    882   -400  -1121       C  
ATOM   3081  C   HIS C 204      -2.768 -35.032  29.150  1.00 77.26           C  
ANISOU 3081  C   HIS C 204    10290  11458   7607    872   -425  -1119       C  
ATOM   3082  O   HIS C 204      -3.094 -34.442  30.184  1.00 75.81           O  
ANISOU 3082  O   HIS C 204    10093  11276   7436    879   -424  -1107       O  
ATOM   3083  CB  HIS C 204      -0.316 -35.307  28.712  1.00 75.85           C  
ANISOU 3083  CB  HIS C 204    10141  11236   7444    872   -388  -1140       C  
ATOM   3084  CG  HIS C 204       0.724 -35.374  27.635  1.00 76.30           C  
ANISOU 3084  CG  HIS C 204    10219  11281   7492    874   -371  -1149       C  
ATOM   3085  ND1 HIS C 204       0.457 -35.851  26.368  1.00 78.61           N  
ANISOU 3085  ND1 HIS C 204    10520  11584   7763    868   -379  -1157       N  
ATOM   3086  CD2 HIS C 204       2.035 -35.030  27.640  1.00 74.84           C  
ANISOU 3086  CD2 HIS C 204    10046  11072   7316    880   -346  -1153       C  
ATOM   3087  CE1 HIS C 204       1.557 -35.790  25.638  1.00 78.54           C  
ANISOU 3087  CE1 HIS C 204    10530  11560   7751    871   -360  -1164       C  
ATOM   3088  NE2 HIS C 204       2.530 -35.297  26.385  1.00 76.26           N  
ANISOU 3088  NE2 HIS C 204    10244  11250   7482    879   -340  -1161       N  
ATOM   3089  N   SER C 205      -3.404 -36.112  28.708  1.00 84.44           N  
ANISOU 3089  N   SER C 205    11197  12377   8510    855   -446  -1132       N  
ATOM   3090  CA  SER C 205      -4.534 -36.672  29.437  1.00 85.12           C  
ANISOU 3090  CA  SER C 205    11263  12475   8603    843   -470  -1132       C  
ATOM   3091  C   SER C 205      -4.082 -37.517  30.616  1.00 83.93           C  
ANISOU 3091  C   SER C 205    11105  12303   8480    829   -472  -1147       C  
ATOM   3092  O   SER C 205      -2.971 -38.047  30.616  1.00 83.37           O  
ANISOU 3092  O   SER C 205    11045  12209   8421    822   -460  -1162       O  
ATOM   3093  CB  SER C 205      -5.409 -37.504  28.504  1.00 88.04           C  
ANISOU 3093  CB  SER C 205    11633  12862   8955    831   -492  -1140       C  
ATOM   3094  OG  SER C 205      -6.077 -36.666  27.575  1.00 89.42           O  
ANISOU 3094  OG  SER C 205    11811  13061   9105    844   -494  -1124       O  
ATOM   3095  N   GLU C 206      -4.946 -37.644  31.620  1.00 88.55           N  
ANISOU 3095  N   GLU C 206    11671  12896   9077    823   -488  -1141       N  
ATOM   3096  CA  GLU C 206      -4.676 -38.519  32.757  1.00 87.72           C  
ANISOU 3096  CA  GLU C 206    11558  12774   8999    808   -493  -1155       C  
ATOM   3097  C   GLU C 206      -4.424 -39.924  32.262  1.00 89.46           C  
ANISOU 3097  C   GLU C 206    11784  12984   9221    787   -503  -1178       C  
ATOM   3098  O   GLU C 206      -3.754 -40.700  32.925  1.00 88.91           O  
ANISOU 3098  O   GLU C 206    11715  12894   9174    775   -501  -1194       O  
ATOM   3099  CB  GLU C 206      -5.845 -38.520  33.735  1.00 87.72           C  
ANISOU 3099  CB  GLU C 206    11536  12787   9007    803   -512  -1146       C  
ATOM   3100  CG  GLU C 206      -6.682 -37.239  33.703  1.00 88.22           C  
ANISOU 3100  CG  GLU C 206    11592  12873   9056    822   -512  -1121       C  
ATOM   3101  CD  GLU C 206      -8.055 -37.401  34.355  1.00 88.84           C  
ANISOU 3101  CD  GLU C 206    11650  12969   9137    815   -536  -1112       C  
ATOM   3102  OE1 GLU C 206      -8.784 -38.361  33.999  1.00 90.63           O  
ANISOU 3102  OE1 GLU C 206    11872  13205   9359    800   -557  -1122       O  
ATOM   3103  OE2 GLU C 206      -8.406 -36.564  35.220  1.00 87.65           O  
ANISOU 3103  OE2 GLU C 206    11487  12823   8993    826   -533  -1096       O  
ATOM   3104  N   ASN C 207      -4.994 -40.236  31.099  1.00 89.49           N  
ANISOU 3104  N   ASN C 207    11794  13004   9203    784   -514  -1181       N  
ATOM   3105  CA  ASN C 207      -4.755 -41.480  30.381  1.00 91.43           C  
ANISOU 3105  CA  ASN C 207    12049  13244   9446    766   -522  -1202       C  
ATOM   3106  C   ASN C 207      -3.290 -41.715  30.049  1.00 90.70           C  
ANISOU 3106  C   ASN C 207    11975  13127   9361    765   -501  -1216       C  
ATOM   3107  O   ASN C 207      -2.803 -42.844  30.102  1.00 91.33           O  
ANISOU 3107  O   ASN C 207    12058  13191   9453    748   -505  -1235       O  
ATOM   3108  CB  ASN C 207      -5.532 -41.477  29.077  1.00 94.00           C  
ANISOU 3108  CB  ASN C 207    12380  13593   9744    767   -534  -1198       C  
ATOM   3109  CG  ASN C 207      -6.917 -42.074  29.197  1.00 95.99           C  
ANISOU 3109  CG  ASN C 207    12616  13865   9992    755   -561  -1197       C  
ATOM   3110  OD1 ASN C 207      -7.213 -42.885  30.081  1.00 95.51           O  
ANISOU 3110  OD1 ASN C 207    12543  13798   9950    740   -574  -1205       O  
ATOM   3111  ND2 ASN C 207      -7.779 -41.661  28.281  1.00 98.37           N  
ANISOU 3111  ND2 ASN C 207    12917  14189  10269    762   -570  -1186       N  
ATOM   3112  N   ALA C 208      -2.602 -40.633  29.683  1.00 84.03           N  
ANISOU 3112  N   ALA C 208    11141  12279   8508    784   -480  -1205       N  
ATOM   3113  CA  ALA C 208      -1.248 -40.703  29.131  1.00 83.63           C  
ANISOU 3113  CA  ALA C 208    11109  12206   8459    786   -458  -1216       C  
ATOM   3114  C   ALA C 208      -0.274 -41.414  30.050  1.00 82.29           C  
ANISOU 3114  C   ALA C 208    10940  12009   8318    774   -450  -1231       C  
ATOM   3115  O   ALA C 208      -0.312 -41.251  31.273  1.00 80.71           O  
ANISOU 3115  O   ALA C 208    10727  11801   8138    775   -450  -1227       O  
ATOM   3116  CB  ALA C 208      -0.733 -39.310  28.814  1.00 82.21           C  
ANISOU 3116  CB  ALA C 208    10939  12028   8270    809   -436  -1199       C  
ATOM   3117  N   THR C 209       0.579 -42.231  29.441  1.00 79.06           N  
ANISOU 3117  N   THR C 209    10545  11584   7911    764   -444  -1250       N  
ATOM   3118  CA  THR C 209       1.639 -42.907  30.171  1.00 78.31           C  
ANISOU 3118  CA  THR C 209    10453  11460   7843    753   -435  -1266       C  
ATOM   3119  C   THR C 209       2.987 -42.299  29.834  1.00 76.75           C  
ANISOU 3119  C   THR C 209    10272  11242   7647    765   -406  -1266       C  
ATOM   3120  O   THR C 209       3.089 -41.427  28.970  1.00 76.67           O  
ANISOU 3120  O   THR C 209    10272  11241   7617    780   -395  -1255       O  
ATOM   3121  CB  THR C 209       1.662 -44.424  29.872  1.00 80.65           C  
ANISOU 3121  CB  THR C 209    10752  11749   8144    730   -449  -1288       C  
ATOM   3122  OG1 THR C 209       2.544 -45.079  30.794  1.00 80.36           O  
ANISOU 3122  OG1 THR C 209    10714  11685   8135    719   -442  -1302       O  
ATOM   3123  CG2 THR C 209       2.109 -44.691  28.433  1.00 82.24           C  
ANISOU 3123  CG2 THR C 209    10972  11951   8325    729   -443  -1297       C  
ATOM   3124  N   ALA C 210       4.024 -42.800  30.496  1.00 75.91           N  
ANISOU 3124  N   ALA C 210    10169  11109   7565    757   -395  -1279       N  
ATOM   3125  CA  ALA C 210       5.357 -42.221  30.394  1.00 74.43           C  
ANISOU 3125  CA  ALA C 210     9996  10900   7385    768   -368  -1279       C  
ATOM   3126  C   ALA C 210       5.844 -42.165  28.947  1.00 75.61           C  
ANISOU 3126  C   ALA C 210    10165  11051   7514    772   -358  -1283       C  
ATOM   3127  O   ALA C 210       6.340 -41.131  28.482  1.00 74.57           O  
ANISOU 3127  O   ALA C 210    10043  10918   7372    789   -339  -1271       O  
ATOM   3128  CB  ALA C 210       6.313 -43.005  31.242  1.00 74.02           C  
ANISOU 3128  CB  ALA C 210     9944  10818   7361    755   -361  -1295       C  
ATOM   3129  N   LYS C 211       5.679 -43.284  28.244  1.00 76.49           N  
ANISOU 3129  N   LYS C 211    10281  11164   7618    755   -371  -1299       N  
ATOM   3130  CA  LYS C 211       6.084 -43.399  26.845  1.00 78.01           C  
ANISOU 3130  CA  LYS C 211    10492  11359   7791    756   -364  -1305       C  
ATOM   3131  C   LYS C 211       5.480 -42.293  25.969  1.00 78.31           C  
ANISOU 3131  C   LYS C 211    10534  11421   7801    774   -362  -1287       C  
ATOM   3132  O   LYS C 211       6.121 -41.811  25.027  1.00 78.58           O  
ANISOU 3132  O   LYS C 211    10583  11451   7822    784   -346  -1285       O  
ATOM   3133  CB  LYS C 211       5.683 -44.772  26.308  1.00 80.77           C  
ANISOU 3133  CB  LYS C 211    10842  11712   8136    735   -383  -1324       C  
ATOM   3134  CG  LYS C 211       6.158 -45.933  27.172  1.00 81.62           C  
ANISOU 3134  CG  LYS C 211    10945  11797   8270    716   -388  -1342       C  
ATOM   3135  CD  LYS C 211       7.684 -46.119  27.072  1.00 83.75           C  
ANISOU 3135  CD  LYS C 211    11230  12038   8555    715   -364  -1354       C  
ATOM   3136  CE  LYS C 211       8.211 -47.170  28.057  1.00 83.68           C  
ANISOU 3136  CE  LYS C 211    11214  12004   8575    697   -367  -1370       C  
ATOM   3137  NZ  LYS C 211       7.660 -48.534  27.771  1.00 83.55           N  
ANISOU 3137  NZ  LYS C 211    11196  11993   8558    676   -389  -1387       N  
ATOM   3138  N   ASP C 212       4.245 -41.906  26.287  1.00 75.51           N  
ANISOU 3138  N   ASP C 212    10164  11090   7438    779   -379  -1273       N  
ATOM   3139  CA  ASP C 212       3.564 -40.842  25.570  1.00 76.07           C  
ANISOU 3139  CA  ASP C 212    10236  11185   7484    796   -379  -1254       C  
ATOM   3140  C   ASP C 212       4.231 -39.499  25.805  1.00 73.80           C  
ANISOU 3140  C   ASP C 212     9953  10890   7199    817   -354  -1237       C  
ATOM   3141  O   ASP C 212       4.379 -38.696  24.879  1.00 74.26           O  
ANISOU 3141  O   ASP C 212    10022  10955   7238    830   -343  -1227       O  
ATOM   3142  CB  ASP C 212       2.106 -40.730  26.007  1.00 76.58           C  
ANISOU 3142  CB  ASP C 212    10282  11274   7542    795   -402  -1242       C  
ATOM   3143  CG  ASP C 212       1.366 -42.029  25.924  1.00 78.85           C  
ANISOU 3143  CG  ASP C 212    10561  11568   7829    774   -426  -1257       C  
ATOM   3144  OD1 ASP C 212       2.026 -43.087  25.806  1.00 79.93           O  
ANISOU 3144  OD1 ASP C 212    10706  11688   7976    759   -426  -1277       O  
ATOM   3145  OD2 ASP C 212       0.116 -41.977  25.993  1.00 79.60           O  
ANISOU 3145  OD2 ASP C 212    10644  11687   7914    774   -446  -1248       O  
ATOM   3146  N   ILE C 213       4.601 -39.250  27.059  1.00 73.54           N  
ANISOU 3146  N   ILE C 213     9911  10842   7190    819   -347  -1234       N  
ATOM   3147  CA  ILE C 213       5.040 -37.920  27.483  1.00 71.32           C  
ANISOU 3147  CA  ILE C 213     9630  10555   6912    839   -327  -1216       C  
ATOM   3148  C   ILE C 213       6.494 -37.592  27.106  1.00 70.47           C  
ANISOU 3148  C   ILE C 213     9541  10424   6811    845   -299  -1220       C  
ATOM   3149  O   ILE C 213       6.804 -36.450  26.768  1.00 69.64           O  
ANISOU 3149  O   ILE C 213     9442  10320   6697    863   -282  -1205       O  
ATOM   3150  CB  ILE C 213       4.895 -37.753  28.998  1.00 69.32           C  
ANISOU 3150  CB  ILE C 213     9361  10295   6682    839   -329  -1211       C  
ATOM   3151  CG1 ILE C 213       3.510 -38.181  29.456  1.00 70.23           C  
ANISOU 3151  CG1 ILE C 213     9458  10433   6795    830   -356  -1208       C  
ATOM   3152  CG2 ILE C 213       5.118 -36.340  29.376  1.00 67.39           C  
ANISOU 3152  CG2 ILE C 213     9116  10051   6439    860   -311  -1190       C  
ATOM   3153  CD1 ILE C 213       3.337 -38.129  30.955  1.00 68.50           C  
ANISOU 3153  CD1 ILE C 213     9222  10206   6599    828   -360  -1204       C  
ATOM   3154  N   ALA C 214       7.381 -38.583  27.164  1.00 68.10           N  
ANISOU 3154  N   ALA C 214     9248  10101   6526    831   -295  -1241       N  
ATOM   3155  CA  ALA C 214       8.798 -38.328  26.978  1.00 67.36           C  
ANISOU 3155  CA  ALA C 214     9170   9982   6443    836   -268  -1245       C  
ATOM   3156  C   ALA C 214       9.159 -37.617  25.665  1.00 68.11           C  
ANISOU 3156  C   ALA C 214     9281  10081   6515    848   -254  -1238       C  
ATOM   3157  O   ALA C 214       9.973 -36.693  25.691  1.00 66.65           O  
ANISOU 3157  O   ALA C 214     9104   9884   6335    863   -231  -1229       O  
ATOM   3158  CB  ALA C 214       9.572 -39.619  27.097  1.00 68.31           C  
ANISOU 3158  CB  ALA C 214     9295  10079   6580    816   -269  -1269       C  
ATOM   3159  N   PRO C 215       8.583 -38.026  24.515  1.00 66.06           N  
ANISOU 3159  N   PRO C 215     9028   9840   6232    844   -267  -1243       N  
ATOM   3160  CA  PRO C 215       8.978 -37.334  23.276  1.00 66.92           C  
ANISOU 3160  CA  PRO C 215     9153   9953   6320    856   -252  -1236       C  
ATOM   3161  C   PRO C 215       8.446 -35.914  23.179  1.00 66.06           C  
ANISOU 3161  C   PRO C 215     9041   9862   6197    877   -246  -1211       C  
ATOM   3162  O   PRO C 215       8.954 -35.120  22.386  1.00 66.13           O  
ANISOU 3162  O   PRO C 215     9063   9870   6195    890   -229  -1203       O  
ATOM   3163  CB  PRO C 215       8.359 -38.186  22.171  1.00 69.75           C  
ANISOU 3163  CB  PRO C 215     9516  10327   6657    844   -270  -1247       C  
ATOM   3164  CG  PRO C 215       7.962 -39.453  22.824  1.00 70.32           C  
ANISOU 3164  CG  PRO C 215     9578  10397   6743    824   -290  -1263       C  
ATOM   3165  CD  PRO C 215       7.642 -39.116  24.235  1.00 68.06           C  
ANISOU 3165  CD  PRO C 215     9275  10109   6476    827   -293  -1254       C  
ATOM   3166  N   THR C 216       7.420 -35.619  23.971  1.00 68.60           N  
ANISOU 3166  N   THR C 216     9345  10200   6521    880   -261  -1200       N  
ATOM   3167  CA  THR C 216       6.747 -34.323  23.952  1.00 67.78           C  
ANISOU 3167  CA  THR C 216     9235  10115   6403    900   -258  -1175       C  
ATOM   3168  C   THR C 216       7.633 -33.195  24.473  1.00 65.62           C  
ANISOU 3168  C   THR C 216     8965   9825   6142    916   -232  -1162       C  
ATOM   3169  O   THR C 216       7.609 -32.075  23.955  1.00 65.58           O  
ANISOU 3169  O   THR C 216     8966   9829   6124    934   -221  -1145       O  
ATOM   3170  CB  THR C 216       5.452 -34.380  24.797  1.00 67.31           C  
ANISOU 3170  CB  THR C 216     9155  10075   6345    897   -281  -1167       C  
ATOM   3171  OG1 THR C 216       4.449 -35.102  24.078  1.00 69.48           O  
ANISOU 3171  OG1 THR C 216     9427  10372   6602    886   -305  -1173       O  
ATOM   3172  CG2 THR C 216       4.935 -32.975  25.165  1.00 66.07           C  
ANISOU 3172  CG2 THR C 216     8990   9932   6183    917   -275  -1142       C  
ATOM   3173  N   LEU C 217       8.430 -33.507  25.487  0.71 62.09           N  
ANISOU 3173  N   LEU C 217     8515   9353   5722    910   -223  -1170       N  
ATOM   3174  CA  LEU C 217       9.166 -32.490  26.207  0.87 59.93           C  
ANISOU 3174  CA  LEU C 217     8241   9064   5464    925   -201  -1158       C  
ATOM   3175  C   LEU C 217      10.401 -31.989  25.476  0.86 59.76           C  
ANISOU 3175  C   LEU C 217     8239   9025   5443    933   -174  -1158       C  
ATOM   3176  O   LEU C 217      10.968 -32.667  24.620  0.84 61.00           O  
ANISOU 3176  O   LEU C 217     8410   9174   5594    924   -172  -1173       O  
ATOM   3177  CB  LEU C 217       9.567 -33.019  27.569  1.00 58.42           C  
ANISOU 3177  CB  LEU C 217     8040   8853   5303    915   -201  -1167       C  
ATOM   3178  CG  LEU C 217       8.413 -33.729  28.257  1.00 58.77           C  
ANISOU 3178  CG  LEU C 217     8067   8913   5349    903   -228  -1170       C  
ATOM   3179  CD1 LEU C 217       8.778 -34.182  29.652  1.00 57.22           C  
ANISOU 3179  CD1 LEU C 217     7861   8698   5183    894   -228  -1178       C  
ATOM   3180  CD2 LEU C 217       7.235 -32.807  28.303  1.00 58.80           C  
ANISOU 3180  CD2 LEU C 217     8059   8944   5337    916   -238  -1149       C  
ATOM   3181  N   THR C 218      10.767 -30.761  25.815  1.00 60.59           N  
ANISOU 3181  N   THR C 218     8344   9125   5552    951   -156  -1140       N  
ATOM   3182  CA  THR C 218      12.039 -30.151  25.465  1.00 60.00           C  
ANISOU 3182  CA  THR C 218     8285   9029   5485    960   -128  -1137       C  
ATOM   3183  C   THR C 218      12.708 -29.844  26.804  1.00 57.85           C  
ANISOU 3183  C   THR C 218     8005   8734   5241    962   -114  -1134       C  
ATOM   3184  O   THR C 218      12.014 -29.384  27.735  1.00 56.76           O  
ANISOU 3184  O   THR C 218     7851   8606   5109    968   -121  -1122       O  
ATOM   3185  CB  THR C 218      11.871 -28.857  24.629  1.00 60.21           C  
ANISOU 3185  CB  THR C 218     8317   9069   5490    980   -116  -1117       C  
ATOM   3186  OG1 THR C 218      11.125 -29.132  23.436  1.00 62.42           O  
ANISOU 3186  OG1 THR C 218     8602   9371   5742    977   -131  -1119       O  
ATOM   3187  CG2 THR C 218      13.222 -28.295  24.260  1.00 59.47           C  
ANISOU 3187  CG2 THR C 218     8240   8952   5405    987    -87  -1116       C  
ATOM   3188  N   LEU C 219      14.018 -30.114  26.930  1.00 59.09           N  
ANISOU 3188  N   LEU C 219     8172   8862   5417    957    -96  -1145       N  
ATOM   3189  CA  LEU C 219      14.705 -29.921  28.217  1.00 57.19           C  
ANISOU 3189  CA  LEU C 219     7925   8598   5205    958    -83  -1144       C  
ATOM   3190  C   LEU C 219      15.976 -29.107  28.072  1.00 56.35           C  
ANISOU 3190  C   LEU C 219     7831   8469   5110    969    -53  -1137       C  
ATOM   3191  O   LEU C 219      16.674 -29.202  27.057  1.00 57.34           O  
ANISOU 3191  O   LEU C 219     7973   8587   5228    968    -42  -1144       O  
ATOM   3192  CB  LEU C 219      15.027 -31.257  28.873  1.00 57.14           C  
ANISOU 3192  CB  LEU C 219     7915   8576   5219    937    -93  -1166       C  
ATOM   3193  CG  LEU C 219      15.545 -31.225  30.311  1.00 55.29           C  
ANISOU 3193  CG  LEU C 219     7671   8320   5016    935    -85  -1166       C  
ATOM   3194  CD1 LEU C 219      14.802 -30.252  31.159  1.00 55.02           C  
ANISOU 3194  CD1 LEU C 219     7623   8300   4983    948    -87  -1146       C  
ATOM   3195  CD2 LEU C 219      15.391 -32.595  30.910  1.00 55.24           C  
ANISOU 3195  CD2 LEU C 219     7657   8307   5023    914   -103  -1186       C  
ATOM   3196  N   TYR C 220      16.274 -28.316  29.107  1.00 56.09           N  
ANISOU 3196  N   TYR C 220     7791   8425   5096    978    -41  -1125       N  
ATOM   3197  CA  TYR C 220      17.415 -27.401  29.110  1.00 55.13           C  
ANISOU 3197  CA  TYR C 220     7678   8282   4986    990    -12  -1115       C  
ATOM   3198  C   TYR C 220      18.209 -27.379  30.412  1.00 53.60           C  
ANISOU 3198  C   TYR C 220     7479   8062   4825    987      0  -1117       C  
ATOM   3199  O   TYR C 220      17.636 -27.233  31.515  1.00 52.62           O  
ANISOU 3199  O   TYR C 220     7339   7942   4711    988     -8  -1110       O  
ATOM   3200  CB  TYR C 220      16.952 -25.980  28.836  1.00 54.71           C  
ANISOU 3200  CB  TYR C 220     7623   8245   4918   1010     -4  -1090       C  
ATOM   3201  CG  TYR C 220      16.438 -25.732  27.445  1.00 56.23           C  
ANISOU 3201  CG  TYR C 220     7826   8460   5080   1017     -9  -1086       C  
ATOM   3202  CD1 TYR C 220      17.318 -25.546  26.386  1.00 57.04           C  
ANISOU 3202  CD1 TYR C 220     7946   8551   5176   1020      8  -1089       C  
ATOM   3203  CD2 TYR C 220      15.084 -25.644  27.196  1.00 56.95           C  
ANISOU 3203  CD2 TYR C 220     7908   8582   5150   1020    -30  -1078       C  
ATOM   3204  CE1 TYR C 220      16.855 -25.296  25.116  1.00 58.57           C  
ANISOU 3204  CE1 TYR C 220     8148   8765   5342   1025      4  -1084       C  
ATOM   3205  CE2 TYR C 220      14.620 -25.399  25.945  1.00 58.46           C  
ANISOU 3205  CE2 TYR C 220     8107   8792   5313   1025    -34  -1073       C  
ATOM   3206  CZ  TYR C 220      15.503 -25.219  24.907  1.00 59.28           C  
ANISOU 3206  CZ  TYR C 220     8228   8884   5410   1028    -17  -1076       C  
ATOM   3207  OH  TYR C 220      15.040 -24.972  23.639  1.00 60.95           O  
ANISOU 3207  OH  TYR C 220     8448   9115   5594   1034    -22  -1072       O  
ATOM   3208  N   VAL C 221      19.536 -27.466  30.254  1.00 54.66           N  
ANISOU 3208  N   VAL C 221     7626   8168   4975    984     21  -1124       N  
ATOM   3209  CA  VAL C 221      20.485 -27.237  31.345  1.00 53.32           C  
ANISOU 3209  CA  VAL C 221     7453   7970   4835    984     39  -1123       C  
ATOM   3210  C   VAL C 221      21.384 -26.040  31.047  1.00 52.68           C  
ANISOU 3210  C   VAL C 221     7382   7876   4759    999     66  -1108       C  
ATOM   3211  O   VAL C 221      21.507 -25.612  29.892  1.00 53.48           O  
ANISOU 3211  O   VAL C 221     7495   7984   4842   1007     74  -1103       O  
ATOM   3212  CB  VAL C 221      21.370 -28.440  31.575  1.00 53.74           C  
ANISOU 3212  CB  VAL C 221     7511   7999   4908    966     40  -1146       C  
ATOM   3213  CG1 VAL C 221      20.744 -29.413  32.533  1.00 53.36           C  
ANISOU 3213  CG1 VAL C 221     7449   7954   4871    951     18  -1158       C  
ATOM   3214  CG2 VAL C 221      21.630 -29.059  30.266  1.00 55.34           C  
ANISOU 3214  CG2 VAL C 221     7728   8203   5094    959     39  -1160       C  
ATOM   3215  N   GLY C 222      21.999 -25.502  32.098  1.00 57.74           N  
ANISOU 3215  N   GLY C 222     8017   8496   5424   1004     81  -1100       N  
ATOM   3216  CA  GLY C 222      23.037 -24.514  31.916  1.00 57.23           C  
ANISOU 3216  CA  GLY C 222     7961   8413   5369   1015    109  -1088       C  
ATOM   3217  C   GLY C 222      22.519 -23.281  31.217  1.00 57.43           C  
ANISOU 3217  C   GLY C 222     7989   8459   5373   1034    114  -1067       C  
ATOM   3218  O   GLY C 222      21.613 -22.622  31.721  1.00 56.91           O  
ANISOU 3218  O   GLY C 222     7911   8410   5301   1044    106  -1051       O  
ATOM   3219  N   LYS C 223      23.095 -22.950  30.068  1.00 62.58           N  
ANISOU 3219  N   LYS C 223     8657   9107   6014   1039    128  -1066       N  
ATOM   3220  CA  LYS C 223      22.673 -21.752  29.376  1.00 62.88           C  
ANISOU 3220  CA  LYS C 223     8698   9163   6032   1057    134  -1046       C  
ATOM   3221  C   LYS C 223      21.528 -21.963  28.394  1.00 64.03           C  
ANISOU 3221  C   LYS C 223     8844   9340   6145   1058    114  -1046       C  
ATOM   3222  O   LYS C 223      20.342 -21.753  28.712  1.00 63.79           O  
ANISOU 3222  O   LYS C 223     8801   9334   6102   1063     97  -1036       O  
ATOM   3223  CB  LYS C 223      23.856 -21.187  28.611  1.00 63.37           C  
ANISOU 3223  CB  LYS C 223     8774   9205   6097   1062    159  -1043       C  
ATOM   3224  CG  LYS C 223      25.111 -21.155  29.448  1.00 62.98           C  
ANISOU 3224  CG  LYS C 223     8726   9122   6080   1058    179  -1046       C  
ATOM   3225  CD  LYS C 223      25.086 -20.008  30.457  1.00 62.39           C  
ANISOU 3225  CD  LYS C 223     8642   9043   6021   1071    190  -1025       C  
ATOM   3226  CE  LYS C 223      25.719 -18.746  29.855  1.00 61.54           C  
ANISOU 3226  CE  LYS C 223     8543   8928   5911   1086    214  -1007       C  
ATOM   3227  NZ  LYS C 223      26.942 -19.097  29.079  1.00 61.71           N  
ANISOU 3227  NZ  LYS C 223     8580   8928   5939   1079    230  -1020       N  
ATOM   3228  N   LYS C 224      21.870 -22.379  27.189  1.00 64.81           N  
ANISOU 3228  N   LYS C 224     8957   9439   6228   1053    116  -1056       N  
ATOM   3229  CA  LYS C 224      20.855 -22.821  26.246  1.00 66.16           C  
ANISOU 3229  CA  LYS C 224     9129   9638   6370   1051     95  -1061       C  
ATOM   3230  C   LYS C 224      20.855 -24.335  26.169  1.00 67.03           C  
ANISOU 3230  C   LYS C 224     9241   9744   6482   1031     79  -1086       C  
ATOM   3231  O   LYS C 224      20.121 -24.907  25.364  1.00 68.42           O  
ANISOU 3231  O   LYS C 224     9420   9941   6637   1025     62  -1093       O  
ATOM   3232  CB  LYS C 224      21.087 -22.212  24.859  1.00 67.32           C  
ANISOU 3232  CB  LYS C 224     9291   9791   6496   1061    106  -1054       C  
ATOM   3233  CG  LYS C 224      22.491 -22.456  24.310  1.00 68.11           C  
ANISOU 3233  CG  LYS C 224     9407   9864   6607   1055    127  -1066       C  
ATOM   3234  CD  LYS C 224      23.058 -21.208  23.640  1.00 68.57           C  
ANISOU 3234  CD  LYS C 224     9475   9917   6660   1071    149  -1049       C  
ATOM   3235  CE  LYS C 224      22.928 -19.982  24.541  1.00 67.56           C  
ANISOU 3235  CE  LYS C 224     9336   9788   6544   1086    159  -1026       C  
ATOM   3236  NZ  LYS C 224      23.403 -18.752  23.843  1.00 68.05           N  
ANISOU 3236  NZ  LYS C 224     9409   9848   6600   1102    180  -1010       N  
ATOM   3237  N   GLN C 225      21.708 -24.974  26.972  1.00 59.47           N  
ANISOU 3237  N   GLN C 225     8283   8761   5552   1019     86  -1099       N  
ATOM   3238  CA  GLN C 225      22.174 -26.298  26.618  1.00 60.51           C  
ANISOU 3238  CA  GLN C 225     8422   8881   5687   1001     80  -1124       C  
ATOM   3239  C   GLN C 225      21.008 -27.261  26.543  1.00 61.44           C  
ANISOU 3239  C   GLN C 225     8532   9022   5790    990     51  -1134       C  
ATOM   3240  O   GLN C 225      20.311 -27.536  27.536  1.00 60.70           O  
ANISOU 3240  O   GLN C 225     8423   8935   5704    986     35  -1134       O  
ATOM   3241  CB  GLN C 225      23.221 -26.789  27.619  1.00 59.52           C  
ANISOU 3241  CB  GLN C 225     8295   8724   5594    991     91  -1134       C  
ATOM   3242  CG  GLN C 225      24.308 -27.705  27.012  1.00 59.80           C  
ANISOU 3242  CG  GLN C 225     8346   8738   5638    977    100  -1155       C  
ATOM   3243  CD  GLN C 225      25.063 -28.526  28.066  1.00 60.52           C  
ANISOU 3243  CD  GLN C 225     8433   8802   5761    962    102  -1170       C  
ATOM   3244  OE1 GLN C 225      25.211 -28.109  29.228  1.00 60.22           O  
ANISOU 3244  OE1 GLN C 225     8384   8753   5743    966    108  -1161       O  
ATOM   3245  NE2 GLN C 225      25.535 -29.710  27.660  1.00 61.61           N  
ANISOU 3245  NE2 GLN C 225     8578   8929   5902    946     98  -1191       N  
ATOM   3246  N   LEU C 226      20.850 -27.809  25.342  1.00 59.21           N  
ANISOU 3246  N   LEU C 226     8260   8750   5487    984     43  -1144       N  
ATOM   3247  CA  LEU C 226      19.744 -28.683  25.021  1.00 60.53           C  
ANISOU 3247  CA  LEU C 226     8422   8941   5636    974     16  -1154       C  
ATOM   3248  C   LEU C 226      20.190 -30.104  25.286  1.00 61.11           C  
ANISOU 3248  C   LEU C 226     8497   8998   5724    953      8  -1178       C  
ATOM   3249  O   LEU C 226      21.063 -30.640  24.595  1.00 62.17           O  
ANISOU 3249  O   LEU C 226     8645   9117   5861    945     18  -1192       O  
ATOM   3250  CB  LEU C 226      19.334 -28.478  23.564  1.00 62.36           C  
ANISOU 3250  CB  LEU C 226     8665   9193   5837    980     13  -1151       C  
ATOM   3251  CG  LEU C 226      18.238 -29.309  22.899  1.00 64.21           C  
ANISOU 3251  CG  LEU C 226     8896   9452   6047    970    -14  -1160       C  
ATOM   3252  CD1 LEU C 226      18.822 -30.574  22.265  1.00 65.73           C  
ANISOU 3252  CD1 LEU C 226     9101   9633   6242    952    -17  -1184       C  
ATOM   3253  CD2 LEU C 226      17.136 -29.655  23.887  1.00 63.55           C  
ANISOU 3253  CD2 LEU C 226     8794   9384   5968    965    -37  -1159       C  
ATOM   3254  N   VAL C 227      19.617 -30.706  26.317  1.00 61.35           N  
ANISOU 3254  N   VAL C 227     8513   9032   5767    944     -9  -1184       N  
ATOM   3255  CA  VAL C 227      19.863 -32.118  26.573  1.00 62.08           C  
ANISOU 3255  CA  VAL C 227     8605   9112   5872    924    -19  -1207       C  
ATOM   3256  C   VAL C 227      18.697 -32.913  26.031  1.00 63.53           C  
ANISOU 3256  C   VAL C 227     8783   9321   6033    914    -47  -1215       C  
ATOM   3257  O   VAL C 227      17.546 -32.555  26.251  1.00 63.15           O  
ANISOU 3257  O   VAL C 227     8724   9297   5973    920    -62  -1203       O  
ATOM   3258  CB  VAL C 227      20.063 -32.433  28.065  1.00 60.55           C  
ANISOU 3258  CB  VAL C 227     8398   8902   5708    917    -21  -1210       C  
ATOM   3259  CG1 VAL C 227      21.380 -31.889  28.511  1.00 59.63           C  
ANISOU 3259  CG1 VAL C 227     8287   8755   5614    922      6  -1207       C  
ATOM   3260  CG2 VAL C 227      18.941 -31.877  28.911  1.00 59.27           C  
ANISOU 3260  CG2 VAL C 227     8217   8759   5542    925    -34  -1195       C  
ATOM   3261  N   GLU C 228      18.994 -33.966  25.279  1.00 67.27           N  
ANISOU 3261  N   GLU C 228     9267   9790   6502    900    -52  -1234       N  
ATOM   3262  CA  GLU C 228      17.930 -34.788  24.749  1.00 68.94           C  
ANISOU 3262  CA  GLU C 228     9475  10024   6694    890    -78  -1243       C  
ATOM   3263  C   GLU C 228      17.450 -35.725  25.846  1.00 68.49           C  
ANISOU 3263  C   GLU C 228     9403   9966   6654    875    -96  -1253       C  
ATOM   3264  O   GLU C 228      18.046 -35.800  26.924  1.00 67.08           O  
ANISOU 3264  O   GLU C 228     9219   9767   6502    872    -88  -1256       O  
ATOM   3265  CB  GLU C 228      18.391 -35.543  23.504  1.00 71.22           C  
ANISOU 3265  CB  GLU C 228     9781  10310   6971    880    -76  -1259       C  
ATOM   3266  CG  GLU C 228      18.587 -34.616  22.312  1.00 72.09           C  
ANISOU 3266  CG  GLU C 228     9904  10428   7059    894    -62  -1247       C  
ATOM   3267  CD  GLU C 228      18.321 -35.293  20.978  1.00 74.80           C  
ANISOU 3267  CD  GLU C 228    10259  10784   7379    886    -72  -1259       C  
ATOM   3268  OE1 GLU C 228      18.111 -34.565  19.981  1.00 75.94           O  
ANISOU 3268  OE1 GLU C 228    10412  10943   7500    898    -67  -1248       O  
ATOM   3269  OE2 GLU C 228      18.323 -36.547  20.922  1.00 75.92           O  
ANISOU 3269  OE2 GLU C 228    10401  10921   7525    868    -85  -1278       O  
ATOM   3270  N   ILE C 229      16.367 -36.437  25.566  1.00 68.11           N  
ANISOU 3270  N   ILE C 229     9348   9940   6591    865   -122  -1259       N  
ATOM   3271  CA  ILE C 229      15.601 -37.040  26.640  1.00 67.64           C  
ANISOU 3271  CA  ILE C 229     9271   9886   6543    855   -142  -1263       C  
ATOM   3272  C   ILE C 229      15.159 -38.450  26.239  1.00 69.13           C  
ANISOU 3272  C   ILE C 229     9460  10081   6727    835   -163  -1283       C  
ATOM   3273  O   ILE C 229      14.460 -38.627  25.245  1.00 70.42           O  
ANISOU 3273  O   ILE C 229     9627  10265   6865    834   -176  -1284       O  
ATOM   3274  CB  ILE C 229      14.415 -36.082  27.018  1.00 66.98           C  
ANISOU 3274  CB  ILE C 229     9173   9828   6447    869   -152  -1242       C  
ATOM   3275  CG1 ILE C 229      13.726 -36.489  28.321  1.00 66.06           C  
ANISOU 3275  CG1 ILE C 229     9038   9716   6347    862   -169  -1242       C  
ATOM   3276  CG2 ILE C 229      13.443 -35.845  25.844  1.00 68.28           C  
ANISOU 3276  CG2 ILE C 229     9341  10023   6579    875   -165  -1235       C  
ATOM   3277  CD1 ILE C 229      13.046 -35.311  29.005  1.00 64.74           C  
ANISOU 3277  CD1 ILE C 229     8859   9563   6178    878   -169  -1220       C  
ATOM   3278  N   GLU C 230      15.609 -39.455  26.993  1.00 68.60           N  
ANISOU 3278  N   GLU C 230     9389   9994   6683    819   -167  -1300       N  
ATOM   3279  CA  GLU C 230      15.423 -40.868  26.608  1.00 70.12           C  
ANISOU 3279  CA  GLU C 230     9583  10187   6874    798   -184  -1320       C  
ATOM   3280  C   GLU C 230      14.094 -41.433  27.109  1.00 70.51           C  
ANISOU 3280  C   GLU C 230     9614  10256   6919    789   -212  -1321       C  
ATOM   3281  O   GLU C 230      13.185 -41.706  26.325  1.00 71.90           O  
ANISOU 3281  O   GLU C 230     9791  10456   7073    786   -229  -1322       O  
ATOM   3282  CB  GLU C 230      16.575 -41.740  27.136  1.00 70.12           C  
ANISOU 3282  CB  GLU C 230     9587  10155   6902    784   -174  -1338       C  
ATOM   3283  CG  GLU C 230      16.436 -43.237  26.793  1.00 71.72           C  
ANISOU 3283  CG  GLU C 230     9791  10355   7105    762   -191  -1360       C  
ATOM   3284  CD  GLU C 230      17.514 -44.125  27.439  1.00 71.70           C  
ANISOU 3284  CD  GLU C 230     9791  10321   7132    748   -182  -1378       C  
ATOM   3285  OE1 GLU C 230      17.130 -45.130  28.083  1.00 71.54           O  
ANISOU 3285  OE1 GLU C 230     9760  10298   7124    731   -200  -1389       O  
ATOM   3286  OE2 GLU C 230      18.729 -43.837  27.295  1.00 71.91           O  
ANISOU 3286  OE2 GLU C 230     9829  10324   7169    752   -159  -1380       O  
ATOM   3287  N   LYS C 231      13.986 -41.619  28.419  1.00 66.68           N  
ANISOU 3287  N   LYS C 231     9115   9763   6457    784   -217  -1322       N  
ATOM   3288  CA  LYS C 231      12.708 -41.999  28.993  1.00 66.94           C  
ANISOU 3288  CA  LYS C 231     9131   9817   6487    778   -243  -1320       C  
ATOM   3289  C   LYS C 231      12.292 -41.083  30.150  1.00 65.32           C  
ANISOU 3289  C   LYS C 231     8910   9616   6292    789   -242  -1302       C  
ATOM   3290  O   LYS C 231      12.973 -40.112  30.499  1.00 64.10           O  
ANISOU 3290  O   LYS C 231     8759   9450   6146    804   -221  -1291       O  
ATOM   3291  CB  LYS C 231      12.716 -43.475  29.438  1.00 67.71           C  
ANISOU 3291  CB  LYS C 231     9223   9903   6602    754   -258  -1341       C  
ATOM   3292  CG  LYS C 231      13.725 -43.916  30.505  1.00 66.53           C  
ANISOU 3292  CG  LYS C 231     9072   9723   6485    746   -247  -1351       C  
ATOM   3293  CD  LYS C 231      13.919 -45.462  30.426  1.00 67.61           C  
ANISOU 3293  CD  LYS C 231     9210   9847   6632    722   -260  -1374       C  
ATOM   3294  CE  LYS C 231      14.814 -46.052  31.543  1.00 67.99           C  
ANISOU 3294  CE  LYS C 231     9254   9865   6713    711   -252  -1385       C  
ATOM   3295  NZ  LYS C 231      15.833 -47.109  31.119  1.00 68.71           N  
ANISOU 3295  NZ  LYS C 231     9358   9933   6816    696   -245  -1406       N  
ATOM   3296  N   VAL C 232      11.136 -41.402  30.710  1.00 64.12           N  
ANISOU 3296  N   VAL C 232     8742   9482   6139    783   -265  -1300       N  
ATOM   3297  CA  VAL C 232      10.487 -40.636  31.753  1.00 62.86           C  
ANISOU 3297  CA  VAL C 232     8567   9332   5986    793   -269  -1283       C  
ATOM   3298  C   VAL C 232       9.834 -41.646  32.685  1.00 63.27           C  
ANISOU 3298  C   VAL C 232     8602   9384   6052    775   -291  -1293       C  
ATOM   3299  O   VAL C 232       9.249 -42.615  32.215  1.00 64.71           O  
ANISOU 3299  O   VAL C 232     8784   9577   6227    761   -310  -1305       O  
ATOM   3300  CB  VAL C 232       9.432 -39.699  31.158  1.00 62.73           C  
ANISOU 3300  CB  VAL C 232     8547   9346   5943    808   -276  -1264       C  
ATOM   3301  CG1 VAL C 232       8.468 -39.215  32.234  1.00 62.73           C  
ANISOU 3301  CG1 VAL C 232     8528   9360   5948    813   -288  -1250       C  
ATOM   3302  CG2 VAL C 232      10.093 -38.545  30.429  1.00 62.84           C  
ANISOU 3302  CG2 VAL C 232     8575   9357   5944    827   -253  -1251       C  
ATOM   3303  N   VAL C 233       9.939 -41.478  33.992  1.00 58.30           N  
ANISOU 3303  N   VAL C 233     7961   8744   5445    775   -289  -1290       N  
ATOM   3304  CA  VAL C 233       9.283 -42.445  34.863  1.00 58.72           C  
ANISOU 3304  CA  VAL C 233     7999   8798   5513    758   -311  -1299       C  
ATOM   3305  C   VAL C 233       8.599 -41.746  36.036  1.00 57.52           C  
ANISOU 3305  C   VAL C 233     7830   8656   5370    766   -316  -1284       C  
ATOM   3306  O   VAL C 233       9.144 -40.807  36.596  1.00 56.19           O  
ANISOU 3306  O   VAL C 233     7662   8477   5211    780   -298  -1272       O  
ATOM   3307  CB  VAL C 233      10.283 -43.542  35.379  1.00 58.76           C  
ANISOU 3307  CB  VAL C 233     8007   8774   5545    741   -306  -1320       C  
ATOM   3308  CG1 VAL C 233      11.685 -43.379  34.780  1.00 58.79           C  
ANISOU 3308  CG1 VAL C 233     8031   8755   5553    745   -281  -1326       C  
ATOM   3309  CG2 VAL C 233      10.339 -43.581  36.912  1.00 57.49           C  
ANISOU 3309  CG2 VAL C 233     7832   8599   5411    737   -308  -1319       C  
ATOM   3310  N   LEU C 234       7.399 -42.200  36.394  1.00 56.77           N  
ANISOU 3310  N   LEU C 234     7720   8579   5271    758   -341  -1283       N  
ATOM   3311  CA  LEU C 234       6.545 -41.502  37.364  1.00 55.83           C  
ANISOU 3311  CA  LEU C 234     7583   8473   5155    766   -348  -1267       C  
ATOM   3312  C   LEU C 234       6.455 -42.244  38.664  1.00 55.51           C  
ANISOU 3312  C   LEU C 234     7529   8421   5141    751   -359  -1275       C  
ATOM   3313  O   LEU C 234       6.417 -43.453  38.655  1.00 56.29           O  
ANISOU 3313  O   LEU C 234     7627   8513   5248    732   -372  -1293       O  
ATOM   3314  CB  LEU C 234       5.127 -41.328  36.830  1.00 56.67           C  
ANISOU 3314  CB  LEU C 234     7682   8613   5238    768   -369  -1256       C  
ATOM   3315  CG  LEU C 234       4.844 -40.431  35.635  1.00 56.76           C  
ANISOU 3315  CG  LEU C 234     7702   8643   5220    784   -363  -1243       C  
ATOM   3316  CD1 LEU C 234       5.304 -41.008  34.309  1.00 57.55           C  
ANISOU 3316  CD1 LEU C 234     7819   8741   5305    779   -360  -1256       C  
ATOM   3317  CD2 LEU C 234       3.370 -40.220  35.613  1.00 57.60           C  
ANISOU 3317  CD2 LEU C 234     7795   8780   5311    786   -385  -1230       C  
ATOM   3318  N   HIS C 235       6.379 -41.537  39.778  1.00 55.08           N  
ANISOU 3318  N   HIS C 235     7464   8364   5101    759   -354  -1263       N  
ATOM   3319  CA  HIS C 235       6.253 -42.184  41.067  1.00 54.85           C  
ANISOU 3319  CA  HIS C 235     7421   8323   5097    746   -364  -1270       C  
ATOM   3320  C   HIS C 235       4.913 -42.921  41.145  1.00 55.43           C  
ANISOU 3320  C   HIS C 235     7480   8418   5164    733   -393  -1273       C  
ATOM   3321  O   HIS C 235       3.878 -42.387  40.746  1.00 55.77           O  
ANISOU 3321  O   HIS C 235     7517   8487   5186    741   -404  -1259       O  
ATOM   3322  CB  HIS C 235       6.373 -41.154  42.149  1.00 54.19           C  
ANISOU 3322  CB  HIS C 235     7329   8236   5026    759   -353  -1255       C  
ATOM   3323  CG  HIS C 235       6.511 -41.704  43.526  1.00 53.86           C  
ANISOU 3323  CG  HIS C 235     7275   8177   5013    747   -358  -1262       C  
ATOM   3324  ND1 HIS C 235       5.445 -42.182  44.249  1.00 54.07           N  
ANISOU 3324  ND1 HIS C 235     7284   8216   5045    737   -380  -1262       N  
ATOM   3325  CD2 HIS C 235       7.581 -41.772  44.350  1.00 53.31           C  
ANISOU 3325  CD2 HIS C 235     7208   8080   4969    745   -342  -1268       C  
ATOM   3326  CE1 HIS C 235       5.856 -42.549  45.450  1.00 53.68           C  
ANISOU 3326  CE1 HIS C 235     7227   8147   5022    728   -379  -1268       C  
ATOM   3327  NE2 HIS C 235       7.151 -42.308  45.537  1.00 53.22           N  
ANISOU 3327  NE2 HIS C 235     7180   8064   4977    733   -356  -1272       N  
ATOM   3328  N   PRO C 236       4.928 -44.176  41.619  1.00 62.23           N  
ANISOU 3328  N   PRO C 236     8335   9267   6042    712   -406  -1290       N  
ATOM   3329  CA  PRO C 236       3.737 -45.024  41.724  1.00 63.56           C  
ANISOU 3329  CA  PRO C 236     8490   9452   6207    697   -434  -1295       C  
ATOM   3330  C   PRO C 236       2.598 -44.356  42.473  1.00 63.19           C  
ANISOU 3330  C   PRO C 236     8426   9425   6158    704   -446  -1277       C  
ATOM   3331  O   PRO C 236       1.438 -44.717  42.262  1.00 64.18           O  
ANISOU 3331  O   PRO C 236     8541   9572   6272    697   -468  -1275       O  
ATOM   3332  CB  PRO C 236       4.248 -46.235  42.501  1.00 63.91           C  
ANISOU 3332  CB  PRO C 236     8530   9472   6279    676   -439  -1314       C  
ATOM   3333  CG  PRO C 236       5.689 -46.316  42.128  1.00 63.37           C  
ANISOU 3333  CG  PRO C 236     8480   9379   6218    677   -416  -1324       C  
ATOM   3334  CD  PRO C 236       6.153 -44.901  42.002  1.00 61.95           C  
ANISOU 3334  CD  PRO C 236     8307   9200   6030    701   -395  -1307       C  
ATOM   3335  N   ASN C 237       2.944 -43.445  43.374  1.00 66.32           N  
ANISOU 3335  N   ASN C 237     8817   9814   6566    716   -432  -1266       N  
ATOM   3336  CA  ASN C 237       1.992 -42.597  44.090  1.00 65.76           C  
ANISOU 3336  CA  ASN C 237     8732   9761   6493    726   -439  -1247       C  
ATOM   3337  C   ASN C 237       1.792 -41.184  43.511  1.00 64.98           C  
ANISOU 3337  C   ASN C 237     8637   9679   6372    750   -427  -1226       C  
ATOM   3338  O   ASN C 237       1.487 -40.268  44.272  1.00 64.11           O  
ANISOU 3338  O   ASN C 237     8518   9575   6265    762   -423  -1210       O  
ATOM   3339  CB  ASN C 237       2.344 -42.505  45.568  1.00 64.85           C  
ANISOU 3339  CB  ASN C 237     8606   9628   6405    724   -434  -1246       C  
ATOM   3340  CG  ASN C 237       1.177 -42.896  46.452  1.00 64.94           C  
ANISOU 3340  CG  ASN C 237     8597   9652   6424    713   -458  -1243       C  
ATOM   3341  OD1 ASN C 237       0.091 -43.191  45.967  1.00 65.89           O  
ANISOU 3341  OD1 ASN C 237     8711   9794   6529    708   -477  -1241       O  
ATOM   3342  ND2 ASN C 237       1.404 -42.905  47.748  1.00 64.05           N  
ANISOU 3342  ND2 ASN C 237     8475   9526   6336    710   -455  -1243       N  
ATOM   3343  N   TYR C 238       2.053 -40.989  42.214  1.00 65.50           N  
ANISOU 3343  N   TYR C 238     8719   9752   6417    757   -420  -1226       N  
ATOM   3344  CA  TYR C 238       2.032 -39.674  41.535  1.00 64.77           C  
ANISOU 3344  CA  TYR C 238     8634   9673   6304    779   -406  -1207       C  
ATOM   3345  C   TYR C 238       0.968 -38.706  42.093  1.00 64.25           C  
ANISOU 3345  C   TYR C 238     8552   9628   6231    791   -413  -1185       C  
ATOM   3346  O   TYR C 238       1.265 -37.543  42.342  1.00 63.15           O  
ANISOU 3346  O   TYR C 238     8415   9489   6091    809   -396  -1170       O  
ATOM   3347  CB  TYR C 238       1.757 -39.878  40.023  1.00 65.74           C  
ANISOU 3347  CB  TYR C 238     8768   9811   6400    779   -411  -1210       C  
ATOM   3348  CG  TYR C 238       0.487 -40.690  39.790  1.00 67.18           C  
ANISOU 3348  CG  TYR C 238     8939  10013   6572    765   -439  -1214       C  
ATOM   3349  CD1 TYR C 238       0.419 -42.046  40.178  1.00 67.68           C  
ANISOU 3349  CD1 TYR C 238     8997  10067   6652    743   -455  -1233       C  
ATOM   3350  CD2 TYR C 238      -0.657 -40.117  39.247  1.00 68.08           C  
ANISOU 3350  CD2 TYR C 238     9047  10156   6663    774   -451  -1199       C  
ATOM   3351  CE1 TYR C 238      -0.738 -42.819  40.036  1.00 69.07           C  
ANISOU 3351  CE1 TYR C 238     9162  10260   6821    729   -480  -1237       C  
ATOM   3352  CE2 TYR C 238      -1.845 -40.892  39.094  1.00 69.45           C  
ANISOU 3352  CE2 TYR C 238     9209  10348   6830    760   -478  -1202       C  
ATOM   3353  CZ  TYR C 238      -1.865 -42.254  39.492  1.00 69.95           C  
ANISOU 3353  CZ  TYR C 238     9267  10400   6909    738   -492  -1222       C  
ATOM   3354  OH  TYR C 238      -2.989 -43.068  39.368  1.00 71.40           O  
ANISOU 3354  OH  TYR C 238     9440  10599   7088    723   -518  -1226       O  
ATOM   3355  N   SER C 239      -0.238 -39.193  42.370  1.00 65.74           N  
ANISOU 3355  N   SER C 239     8727   9835   6418    781   -437  -1185       N  
ATOM   3356  CA  SER C 239      -1.316 -38.344  42.863  1.00 65.44           C  
ANISOU 3356  CA  SER C 239     8674   9818   6373    792   -446  -1164       C  
ATOM   3357  C   SER C 239      -1.153 -37.927  44.329  1.00 64.24           C  
ANISOU 3357  C   SER C 239     8510   9655   6244    794   -440  -1158       C  
ATOM   3358  O   SER C 239      -1.867 -37.045  44.819  1.00 63.75           O  
ANISOU 3358  O   SER C 239     8437   9607   6178    806   -442  -1139       O  
ATOM   3359  CB  SER C 239      -2.650 -39.058  42.689  1.00 66.79           C  
ANISOU 3359  CB  SER C 239     8832  10011   6536    779   -474  -1166       C  
ATOM   3360  OG  SER C 239      -2.976 -39.765  43.877  1.00 66.69           O  
ANISOU 3360  OG  SER C 239     8804   9990   6544    764   -488  -1173       O  
ATOM   3361  N   GLN C 240      -0.219 -38.555  45.022  1.00 63.13           N  
ANISOU 3361  N   GLN C 240     8372   9488   6127    784   -433  -1172       N  
ATOM   3362  CA  GLN C 240       0.053 -38.266  46.431  1.00 62.14           C  
ANISOU 3362  CA  GLN C 240     8237   9349   6026    785   -426  -1169       C  
ATOM   3363  C   GLN C 240       1.460 -37.682  46.577  1.00 61.00           C  
ANISOU 3363  C   GLN C 240     8105   9180   5892    796   -398  -1169       C  
ATOM   3364  O   GLN C 240       1.676 -36.624  47.184  1.00 59.99           O  
ANISOU 3364  O   GLN C 240     7974   9049   5769    811   -383  -1154       O  
ATOM   3365  CB  GLN C 240      -0.102 -39.519  47.273  1.00 62.78           C  
ANISOU 3365  CB  GLN C 240     8306   9418   6128    763   -443  -1185       C  
ATOM   3366  CG  GLN C 240      -1.522 -40.001  47.333  1.00 63.92           C  
ANISOU 3366  CG  GLN C 240     8436   9585   6266    752   -470  -1183       C  
ATOM   3367  CD  GLN C 240      -2.270 -39.378  48.473  1.00 63.40           C  
ANISOU 3367  CD  GLN C 240     8352   9528   6208    757   -476  -1167       C  
ATOM   3368  OE1 GLN C 240      -1.673 -38.920  49.450  1.00 62.67           O  
ANISOU 3368  OE1 GLN C 240     8258   9421   6134    763   -463  -1164       O  
ATOM   3369  NE2 GLN C 240      -3.589 -39.352  48.363  1.00 63.81           N  
ANISOU 3369  NE2 GLN C 240     8392   9605   6248    756   -496  -1158       N  
ATOM   3370  N   VAL C 241       2.433 -38.443  46.097  1.00 59.52           N  
ANISOU 3370  N   VAL C 241     7931   8973   5711    787   -390  -1187       N  
ATOM   3371  CA  VAL C 241       3.774 -37.923  45.960  1.00 58.66           C  
ANISOU 3371  CA  VAL C 241     7837   8842   5609    797   -363  -1188       C  
ATOM   3372  C   VAL C 241       3.937 -37.361  44.542  1.00 58.81           C  
ANISOU 3372  C   VAL C 241     7871   8872   5602    810   -353  -1181       C  
ATOM   3373  O   VAL C 241       4.019 -38.112  43.553  1.00 59.75           O  
ANISOU 3373  O   VAL C 241     7999   8992   5710    801   -359  -1194       O  
ATOM   3374  CB  VAL C 241       4.806 -39.012  46.238  1.00 58.99           C  
ANISOU 3374  CB  VAL C 241     7886   8856   5673    780   -359  -1210       C  
ATOM   3375  CG1 VAL C 241       6.228 -38.462  46.116  1.00 58.20           C  
ANISOU 3375  CG1 VAL C 241     7801   8731   5581    791   -330  -1210       C  
ATOM   3376  CG2 VAL C 241       4.552 -39.621  47.611  1.00 59.03           C  
ANISOU 3376  CG2 VAL C 241     7875   8852   5703    767   -371  -1216       C  
ATOM   3377  N   ASP C 242       4.027 -36.029  44.444  1.00 57.13           N  
ANISOU 3377  N   ASP C 242     7661   8665   5380    831   -337  -1162       N  
ATOM   3378  CA  ASP C 242       4.018 -35.396  43.121  1.00 57.36           C  
ANISOU 3378  CA  ASP C 242     7703   8708   5383    844   -329  -1153       C  
ATOM   3379  C   ASP C 242       5.471 -35.280  42.601  1.00 56.91           C  
ANISOU 3379  C   ASP C 242     7666   8627   5332    849   -304  -1161       C  
ATOM   3380  O   ASP C 242       6.184 -34.294  42.828  1.00 55.93           O  
ANISOU 3380  O   ASP C 242     7546   8491   5212    864   -282  -1149       O  
ATOM   3381  CB  ASP C 242       3.333 -34.018  43.234  1.00 56.77           C  
ANISOU 3381  CB  ASP C 242     7622   8653   5295    864   -325  -1128       C  
ATOM   3382  CG  ASP C 242       3.226 -33.307  41.901  1.00 57.08           C  
ANISOU 3382  CG  ASP C 242     7672   8707   5307    879   -318  -1117       C  
ATOM   3383  OD1 ASP C 242       3.059 -34.007  40.858  1.00 58.10           O  
ANISOU 3383  OD1 ASP C 242     7810   8844   5422    870   -327  -1128       O  
ATOM   3384  OD2 ASP C 242       3.307 -32.043  41.909  1.00 56.32           O  
ANISOU 3384  OD2 ASP C 242     7578   8616   5205    898   -302  -1098       O  
ATOM   3385  N   ILE C 243       5.868 -36.297  41.838  1.00 55.28           N  
ANISOU 3385  N   ILE C 243     7469   8413   5122    835   -308  -1180       N  
ATOM   3386  CA  ILE C 243       7.283 -36.486  41.485  1.00 55.06           C  
ANISOU 3386  CA  ILE C 243     7458   8359   5105    834   -287  -1191       C  
ATOM   3387  C   ILE C 243       7.485 -37.248  40.159  1.00 56.20           C  
ANISOU 3387  C   ILE C 243     7616   8504   5233    826   -291  -1205       C  
ATOM   3388  O   ILE C 243       6.867 -38.271  39.941  1.00 57.22           O  
ANISOU 3388  O   ILE C 243     7740   8642   5358    810   -312  -1217       O  
ATOM   3389  CB  ILE C 243       8.018 -37.243  42.613  1.00 54.72           C  
ANISOU 3389  CB  ILE C 243     7410   8288   5092    820   -284  -1206       C  
ATOM   3390  CG1 ILE C 243       8.348 -36.302  43.779  1.00 53.42           C  
ANISOU 3390  CG1 ILE C 243     7239   8112   4945    832   -270  -1192       C  
ATOM   3391  CG2 ILE C 243       9.258 -37.901  42.078  1.00 54.98           C  
ANISOU 3391  CG2 ILE C 243     7460   8297   5134    812   -271  -1223       C  
ATOM   3392  CD1 ILE C 243       9.134 -35.102  43.376  1.00 52.64           C  
ANISOU 3392  CD1 ILE C 243     7152   8007   4841    852   -243  -1178       C  
ATOM   3393  N   GLY C 244       8.329 -36.753  39.268  1.00 56.45           N  
ANISOU 3393  N   GLY C 244     7961   8017   5471    388   -835    -22       N  
ATOM   3394  CA  GLY C 244       8.788 -37.550  38.143  1.00 56.66           C  
ANISOU 3394  CA  GLY C 244     7994   8036   5500    359   -830    -17       C  
ATOM   3395  C   GLY C 244      10.273 -37.903  38.199  1.00 56.33           C  
ANISOU 3395  C   GLY C 244     7960   7975   5466    376   -826    -21       C  
ATOM   3396  O   GLY C 244      11.017 -37.410  39.055  1.00 55.87           O  
ANISOU 3396  O   GLY C 244     7903   7910   5415    411   -828    -29       O  
ATOM   3397  N   LEU C 245      10.726 -38.719  37.251  1.00 56.88           N  
ANISOU 3397  N   LEU C 245     8037   8038   5536    352   -821    -16       N  
ATOM   3398  CA  LEU C 245      12.157 -38.864  37.000  1.00 56.58           C  
ANISOU 3398  CA  LEU C 245     8006   7981   5512    364   -819    -22       C  
ATOM   3399  C   LEU C 245      12.420 -38.752  35.505  1.00 56.65           C  
ANISOU 3399  C   LEU C 245     8011   7980   5532    337   -822    -26       C  
ATOM   3400  O   LEU C 245      11.723 -39.381  34.683  1.00 57.33           O  
ANISOU 3400  O   LEU C 245     8096   8075   5610    303   -818    -18       O  
ATOM   3401  CB  LEU C 245      12.702 -40.190  37.544  1.00 57.16           C  
ANISOU 3401  CB  LEU C 245     8094   8053   5573    369   -808    -12       C  
ATOM   3402  CG  LEU C 245      13.244 -40.066  38.958  1.00 56.90           C  
ANISOU 3402  CG  LEU C 245     8065   8018   5538    409   -806    -15       C  
ATOM   3403  CD1 LEU C 245      14.145 -41.203  39.311  1.00 57.51           C  
ANISOU 3403  CD1 LEU C 245     8156   8087   5609    416   -796     -8       C  
ATOM   3404  CD2 LEU C 245      13.980 -38.764  39.063  1.00 56.06           C  
ANISOU 3404  CD2 LEU C 245     7952   7899   5451    435   -816    -31       C  
ATOM   3405  N   ILE C 246      13.406 -37.936  35.141  1.00 58.85           N  
ANISOU 3405  N   ILE C 246     8288   8241   5830    351   -829    -38       N  
ATOM   3406  CA  ILE C 246      13.805 -37.885  33.749  1.00 58.98           C  
ANISOU 3406  CA  ILE C 246     8303   8248   5860    328   -830    -42       C  
ATOM   3407  C   ILE C 246      15.155 -38.578  33.545  1.00 58.85           C  
ANISOU 3407  C   ILE C 246     8298   8214   5849    335   -825    -43       C  
ATOM   3408  O   ILE C 246      16.101 -38.325  34.297  1.00 58.24           O  
ANISOU 3408  O   ILE C 246     8226   8125   5779    365   -826    -49       O  
ATOM   3409  CB  ILE C 246      13.903 -36.473  33.249  1.00 58.48           C  
ANISOU 3409  CB  ILE C 246     8229   8177   5815    334   -842    -56       C  
ATOM   3410  CG1 ILE C 246      12.531 -35.828  33.168  1.00 58.00           C  
ANISOU 3410  CG1 ILE C 246     8156   8132   5748    321   -848    -55       C  
ATOM   3411  CG2 ILE C 246      14.496 -36.465  31.874  1.00 58.59           C  
ANISOU 3411  CG2 ILE C 246     8243   8178   5842    313   -843    -60       C  
ATOM   3412  CD1 ILE C 246      12.568 -34.390  32.601  1.00 57.53           C  
ANISOU 3412  CD1 ILE C 246     8086   8065   5708    325   -860    -68       C  
ATOM   3413  N   LYS C 247      15.240 -39.465  32.548  1.00 62.34           N  
ANISOU 3413  N   LYS C 247     8744   8654   6288    307   -818    -37       N  
ATOM   3414  CA  LYS C 247      16.521 -40.029  32.150  1.00 62.41           C  
ANISOU 3414  CA  LYS C 247     8763   8644   6305    311   -814    -39       C  
ATOM   3415  C   LYS C 247      16.982 -39.373  30.859  1.00 62.19           C  
ANISOU 3415  C   LYS C 247     8730   8604   6296    298   -820    -49       C  
ATOM   3416  O   LYS C 247      16.251 -39.369  29.858  1.00 62.61           O  
ANISOU 3416  O   LYS C 247     8775   8665   6348    269   -820    -47       O  
ATOM   3417  CB  LYS C 247      16.438 -41.547  31.971  1.00 63.42           C  
ANISOU 3417  CB  LYS C 247     8901   8779   6418    292   -801    -26       C  
ATOM   3418  CG  LYS C 247      17.778 -42.206  31.601  1.00 63.59           C  
ANISOU 3418  CG  LYS C 247     8934   8780   6447    297   -796    -28       C  
ATOM   3419  CD  LYS C 247      17.638 -43.702  31.438  1.00 64.81           C  
ANISOU 3419  CD  LYS C 247     9098   8941   6586    279   -783    -15       C  
ATOM   3420  CE  LYS C 247      18.952 -44.385  31.108  1.00 65.04           C  
ANISOU 3420  CE  LYS C 247     9140   8951   6622    285   -778    -16       C  
ATOM   3421  NZ  LYS C 247      18.816 -45.876  31.176  1.00 66.36           N  
ANISOU 3421  NZ  LYS C 247     9317   9124   6772    272   -764     -3       N  
ATOM   3422  N   LEU C 248      18.200 -38.822  30.903  1.00 64.77           N  
ANISOU 3422  N   LEU C 248     9060   8910   6639    320   -825    -59       N  
ATOM   3423  CA  LEU C 248      18.860 -38.222  29.739  1.00 64.59           C  
ANISOU 3423  CA  LEU C 248     9034   8872   6635    311   -830    -69       C  
ATOM   3424  C   LEU C 248      19.547 -39.270  28.862  1.00 65.29           C  
ANISOU 3424  C   LEU C 248     9133   8951   6725    294   -822    -65       C  
ATOM   3425  O   LEU C 248      20.249 -40.165  29.369  1.00 65.61           O  
ANISOU 3425  O   LEU C 248     9185   8985   6760    305   -815    -60       O  
ATOM   3426  CB  LEU C 248      19.881 -37.176  30.186  1.00 63.75           C  
ANISOU 3426  CB  LEU C 248     8928   8749   6546    343   -838    -81       C  
ATOM   3427  CG  LEU C 248      19.330 -35.967  30.944  1.00 63.09           C  
ANISOU 3427  CG  LEU C 248     8835   8673   6465    363   -847    -88       C  
ATOM   3428  CD1 LEU C 248      20.460 -35.057  31.373  1.00 62.23           C  
ANISOU 3428  CD1 LEU C 248     8727   8547   6372    395   -854   -100       C  
ATOM   3429  CD2 LEU C 248      18.304 -35.212  30.090  1.00 63.13           C  
ANISOU 3429  CD2 LEU C 248     8826   8686   6473    340   -854    -90       C  
ATOM   3430  N   LYS C 249      19.366 -39.122  27.548  1.00 68.65           N  
ANISOU 3430  N   LYS C 249     9552   9374   7159    269   -824    -68       N  
ATOM   3431  CA  LYS C 249      19.789 -40.113  26.560  1.00 69.49           C  
ANISOU 3431  CA  LYS C 249     9665   9473   7265    249   -816    -64       C  
ATOM   3432  C   LYS C 249      21.233 -40.547  26.786  1.00 69.36           C  
ANISOU 3432  C   LYS C 249     9663   9436   7256    268   -813    -66       C  
ATOM   3433  O   LYS C 249      21.589 -41.709  26.619  1.00 69.97           O  
ANISOU 3433  O   LYS C 249     9750   9510   7326    260   -803    -60       O  
ATOM   3434  CB  LYS C 249      19.614 -39.540  25.150  1.00 69.89           C  
ANISOU 3434  CB  LYS C 249     9707   9520   7329    227   -821    -71       C  
ATOM   3435  CG  LYS C 249      19.584 -40.577  24.034  1.00 70.98           C  
ANISOU 3435  CG  LYS C 249     9848   9657   7465    201   -812    -66       C  
ATOM   3436  CD  LYS C 249      18.922 -40.012  22.780  1.00 71.76           C  
ANISOU 3436  CD  LYS C 249     9934   9761   7572    178   -816    -71       C  
ATOM   3437  CE  LYS C 249      17.424 -39.808  22.986  1.00 73.33           C  
ANISOU 3437  CE  LYS C 249    10120   9985   7757    165   -817    -66       C  
ATOM   3438  NZ  LYS C 249      16.818 -39.100  21.827  1.00 74.34           N  
ANISOU 3438  NZ  LYS C 249    10235  10117   7895    146   -822    -72       N  
ATOM   3439  N   GLN C 250      22.052 -39.599  27.203  1.00 71.68           N  
ANISOU 3439  N   GLN C 250     9956   9716   7564    293   -821    -76       N  
ATOM   3440  CA  GLN C 250      23.420 -39.872  27.591  1.00 71.61           C  
ANISOU 3440  CA  GLN C 250     9959   9687   7561    315   -819    -79       C  
ATOM   3441  C   GLN C 250      23.727 -39.092  28.871  1.00 70.85           C  
ANISOU 3441  C   GLN C 250     9862   9591   7467    349   -825    -85       C  
ATOM   3442  O   GLN C 250      22.856 -38.400  29.410  1.00 70.44           O  
ANISOU 3442  O   GLN C 250     9801   9552   7411    355   -830    -86       O  
ATOM   3443  CB  GLN C 250      24.371 -39.480  26.466  1.00 71.39           C  
ANISOU 3443  CB  GLN C 250     9933   9639   7553    309   -823    -88       C  
ATOM   3444  CG  GLN C 250      24.005 -38.141  25.842  1.00 71.82           C  
ANISOU 3444  CG  GLN C 250     9974   9693   7621    304   -834    -98       C  
ATOM   3445  CD  GLN C 250      25.040 -37.657  24.841  1.00 72.34           C  
ANISOU 3445  CD  GLN C 250    10042   9736   7707    303   -839   -107       C  
ATOM   3446  OE1 GLN C 250      26.226 -37.990  24.952  1.00 72.93           O  
ANISOU 3446  OE1 GLN C 250    10127   9794   7788    316   -837   -109       O  
ATOM   3447  NE2 GLN C 250      24.598 -36.874  23.849  1.00 72.22           N  
ANISOU 3447  NE2 GLN C 250    10017   9722   7703    286   -845   -113       N  
ATOM   3448  N   LYS C 251      24.950 -39.197  29.374  1.00 66.91           N  
ANISOU 3448  N   LYS C 251     9373   9076   6975    374   -824    -89       N  
ATOM   3449  CA  LYS C 251      25.314 -38.392  30.529  1.00 66.22           C  
ANISOU 3449  CA  LYS C 251     9283   8987   6890    408   -830    -96       C  
ATOM   3450  C   LYS C 251      25.611 -36.993  30.011  1.00 65.54           C  
ANISOU 3450  C   LYS C 251     9188   8891   6824    414   -841   -109       C  
ATOM   3451  O   LYS C 251      25.961 -36.847  28.826  1.00 65.68           O  
ANISOU 3451  O   LYS C 251     9205   8897   6854    396   -843   -113       O  
ATOM   3452  CB  LYS C 251      26.507 -38.996  31.270  1.00 66.47           C  
ANISOU 3452  CB  LYS C 251     9328   9007   6922    432   -825    -95       C  
ATOM   3453  CG  LYS C 251      26.232 -40.393  31.812  1.00 67.20           C  
ANISOU 3453  CG  LYS C 251     9430   9109   6995    428   -813    -82       C  
ATOM   3454  CD  LYS C 251      27.088 -40.716  33.024  1.00 66.63           C  
ANISOU 3454  CD  LYS C 251     9366   9031   6918    460   -809    -82       C  
ATOM   3455  CE  LYS C 251      28.540 -40.985  32.634  1.00 66.70           C  
ANISOU 3455  CE  LYS C 251     9386   9018   6940    468   -808    -87       C  
ATOM   3456  NZ  LYS C 251      29.406 -41.011  33.846  1.00 66.22           N  
ANISOU 3456  NZ  LYS C 251     9331   8951   6877    504   -807    -89       N  
ATOM   3457  N   VAL C 252      25.436 -35.974  30.863  1.00 60.66           N  
ANISOU 3457  N   VAL C 252     8562   8277   6209    438   -848   -116       N  
ATOM   3458  CA  VAL C 252      25.794 -34.585  30.509  1.00 60.10           C  
ANISOU 3458  CA  VAL C 252     8483   8195   6156    448   -859   -129       C  
ATOM   3459  C   VAL C 252      27.143 -34.183  31.133  1.00 59.75           C  
ANISOU 3459  C   VAL C 252     8445   8135   6124    481   -862   -138       C  
ATOM   3460  O   VAL C 252      27.438 -34.526  32.274  1.00 59.54           O  
ANISOU 3460  O   VAL C 252     8422   8111   6088    506   -858   -137       O  
ATOM   3461  CB  VAL C 252      24.673 -33.571  30.940  1.00 59.67           C  
ANISOU 3461  CB  VAL C 252     8415   8155   6100    453   -866   -132       C  
ATOM   3462  CG1 VAL C 252      24.502 -33.522  32.458  1.00 59.30           C  
ANISOU 3462  CG1 VAL C 252     8369   8120   6044    483   -865   -132       C  
ATOM   3463  CG2 VAL C 252      24.955 -32.191  30.397  1.00 59.33           C  
ANISOU 3463  CG2 VAL C 252     8363   8102   6076    459   -877   -145       C  
ATOM   3464  N   SER C 253      27.977 -33.471  30.384  1.00 58.67           N  
ANISOU 3464  N   SER C 253     8306   7980   6005    483   -868   -148       N  
ATOM   3465  CA  SER C 253      29.284 -33.082  30.920  1.00 58.50           C  
ANISOU 3465  CA  SER C 253     8290   7943   5994    513   -870   -157       C  
ATOM   3466  C   SER C 253      29.133 -32.040  32.016  1.00 57.93           C  
ANISOU 3466  C   SER C 253     8210   7877   5924    544   -876   -165       C  
ATOM   3467  O   SER C 253      28.562 -30.970  31.779  1.00 57.60           O  
ANISOU 3467  O   SER C 253     8158   7839   5889    543   -884   -172       O  
ATOM   3468  CB  SER C 253      30.182 -32.535  29.814  1.00 58.61           C  
ANISOU 3468  CB  SER C 253     8305   7937   6028    506   -876   -165       C  
ATOM   3469  OG  SER C 253      29.465 -32.498  28.586  1.00 58.35           O  
ANISOU 3469  OG  SER C 253     8266   7906   5997    473   -877   -163       O  
ATOM   3470  N   VAL C 254      29.640 -32.349  33.205  1.00 53.45           N  
ANISOU 3470  N   VAL C 254     7648   7311   5350    573   -873   -165       N  
ATOM   3471  CA  VAL C 254      29.576 -31.441  34.340  1.00 53.71           C  
ANISOU 3471  CA  VAL C 254     7674   7350   5384    605   -877   -174       C  
ATOM   3472  C   VAL C 254      30.595 -30.310  34.217  1.00 53.48           C  
ANISOU 3472  C   VAL C 254     7642   7304   5374    625   -886   -188       C  
ATOM   3473  O   VAL C 254      31.718 -30.530  33.787  1.00 53.17           O  
ANISOU 3473  O   VAL C 254     7611   7248   5344    627   -885   -191       O  
ATOM   3474  CB  VAL C 254      29.812 -32.206  35.635  1.00 53.98           C  
ANISOU 3474  CB  VAL C 254     7715   7390   5404    629   -870   -168       C  
ATOM   3475  CG1 VAL C 254      29.913 -31.277  36.806  1.00 54.25           C  
ANISOU 3475  CG1 VAL C 254     7742   7429   5440    665   -874   -178       C  
ATOM   3476  CG2 VAL C 254      28.722 -33.199  35.828  1.00 54.26           C  
ANISOU 3476  CG2 VAL C 254     7752   7444   5420    610   -862   -155       C  
ATOM   3477  N   ASN C 255      30.186 -29.089  34.545  1.00 57.03           N  
ANISOU 3477  N   ASN C 255     8081   7758   5830    640   -893   -197       N  
ATOM   3478  CA  ASN C 255      31.106 -27.944  34.662  1.00 56.86           C  
ANISOU 3478  CA  ASN C 255     8056   7723   5825    664   -901   -212       C  
ATOM   3479  C   ASN C 255      30.517 -26.844  35.541  1.00 56.52           C  
ANISOU 3479  C   ASN C 255     8002   7691   5783    687   -907   -220       C  
ATOM   3480  O   ASN C 255      29.582 -27.087  36.293  1.00 56.41           O  
ANISOU 3480  O   ASN C 255     7985   7695   5755    691   -904   -214       O  
ATOM   3481  CB  ASN C 255      31.485 -27.381  33.301  1.00 56.98           C  
ANISOU 3481  CB  ASN C 255     8070   7723   5858    644   -907   -217       C  
ATOM   3482  CG  ASN C 255      30.306 -26.951  32.522  1.00 56.92           C  
ANISOU 3482  CG  ASN C 255     8054   7724   5850    618   -911   -215       C  
ATOM   3483  OD1 ASN C 255      29.693 -25.952  32.850  1.00 56.65           O  
ANISOU 3483  OD1 ASN C 255     8009   7697   5818    628   -917   -221       O  
ATOM   3484  ND2 ASN C 255      29.968 -27.698  31.481  1.00 57.25           N  
ANISOU 3484  ND2 ASN C 255     8099   7766   5889    584   -908   -206       N  
ATOM   3485  N   GLU C 256      31.085 -25.651  35.492  1.00 59.88           N  
ANISOU 3485  N   GLU C 256     8423   8106   6224    705   -915   -233       N  
ATOM   3486  CA  GLU C 256      30.674 -24.624  36.440  1.00 59.68           C  
ANISOU 3486  CA  GLU C 256     8388   8090   6199    731   -919   -242       C  
ATOM   3487  C   GLU C 256      29.182 -24.266  36.295  1.00 59.57           C  
ANISOU 3487  C   GLU C 256     8363   8092   6177    715   -922   -238       C  
ATOM   3488  O   GLU C 256      28.515 -23.924  37.284  1.00 59.47           O  
ANISOU 3488  O   GLU C 256     8344   8095   6156    733   -922   -240       O  
ATOM   3489  CB  GLU C 256      31.565 -23.360  36.311  1.00 59.74           C  
ANISOU 3489  CB  GLU C 256     8391   8082   6224    751   -928   -257       C  
ATOM   3490  CG  GLU C 256      31.296 -22.428  35.135  1.00 59.80           C  
ANISOU 3490  CG  GLU C 256     8393   8083   6247    731   -936   -263       C  
ATOM   3491  CD  GLU C 256      32.146 -22.725  33.896  1.00 60.03           C  
ANISOU 3491  CD  GLU C 256     8429   8092   6287    710   -937   -262       C  
ATOM   3492  OE1 GLU C 256      33.196 -23.416  34.003  1.00 60.19           O  
ANISOU 3492  OE1 GLU C 256     8459   8102   6308    717   -932   -260       O  
ATOM   3493  OE2 GLU C 256      31.753 -22.263  32.799  1.00 60.11           O  
ANISOU 3493  OE2 GLU C 256     8435   8099   6306    687   -942   -262       O  
ATOM   3494  N   ARG C 257      28.648 -24.314  35.080  1.00 60.13           N  
ANISOU 3494  N   ARG C 257     8433   8162   6252    682   -924   -234       N  
ATOM   3495  CA  ARG C 257      27.239 -23.946  34.894  1.00 60.14           C  
ANISOU 3495  CA  ARG C 257     8424   8179   6247    666   -927   -231       C  
ATOM   3496  C   ARG C 257      26.248 -25.121  34.878  1.00 60.08           C  
ANISOU 3496  C   ARG C 257     8419   8188   6221    642   -919   -215       C  
ATOM   3497  O   ARG C 257      25.042 -24.915  35.030  1.00 59.89           O  
ANISOU 3497  O   ARG C 257     8387   8180   6189    634   -920   -212       O  
ATOM   3498  CB  ARG C 257      27.085 -23.138  33.598  1.00 60.43           C  
ANISOU 3498  CB  ARG C 257     8455   8206   6298    644   -934   -235       C  
ATOM   3499  CG  ARG C 257      27.370 -23.937  32.328  1.00 60.39           C  
ANISOU 3499  CG  ARG C 257     8457   8192   6296    611   -931   -228       C  
ATOM   3500  CD  ARG C 257      27.774 -23.045  31.134  1.00 60.67           C  
ANISOU 3500  CD  ARG C 257     8490   8212   6350    599   -939   -236       C  
ATOM   3501  NE  ARG C 257      28.976 -22.237  31.376  1.00 60.94           N  
ANISOU 3501  NE  ARG C 257     8525   8229   6399    626   -944   -248       N  
ATOM   3502  CZ  ARG C 257      28.953 -20.936  31.673  1.00 60.86           C  
ANISOU 3502  CZ  ARG C 257     8507   8217   6399    645   -952   -260       C  
ATOM   3503  NH1 ARG C 257      27.790 -20.311  31.755  1.00 60.47           N  
ANISOU 3503  NH1 ARG C 257     8447   8181   6346    641   -956   -260       N  
ATOM   3504  NH2 ARG C 257      30.081 -20.251  31.889  1.00 61.22           N  
ANISOU 3504  NH2 ARG C 257     8555   8248   6459    669   -956   -271       N  
ATOM   3505  N   VAL C 258      26.743 -26.348  34.736  1.00 54.84           N  
ANISOU 3505  N   VAL C 258     7766   7520   5550    632   -911   -206       N  
ATOM   3506  CA  VAL C 258      25.879 -27.535  34.630  1.00 54.88           C  
ANISOU 3506  CA  VAL C 258     7775   7539   5539    607   -904   -192       C  
ATOM   3507  C   VAL C 258      26.381 -28.601  35.558  1.00 55.06           C  
ANISOU 3507  C   VAL C 258     7808   7564   5549    622   -895   -185       C  
ATOM   3508  O   VAL C 258      27.459 -29.130  35.321  1.00 55.30           O  
ANISOU 3508  O   VAL C 258     7848   7580   5585    624   -891   -185       O  
ATOM   3509  CB  VAL C 258      25.890 -28.126  33.212  1.00 55.05           C  
ANISOU 3509  CB  VAL C 258     7800   7552   5563    570   -902   -185       C  
ATOM   3510  CG1 VAL C 258      25.156 -29.424  33.181  1.00 55.83           C  
ANISOU 3510  CG1 VAL C 258     7904   7664   5644    548   -893   -171       C  
ATOM   3511  CG2 VAL C 258      25.309 -27.163  32.234  1.00 55.16           C  
ANISOU 3511  CG2 VAL C 258     7805   7566   5588    552   -910   -190       C  
ATOM   3512  N   MET C 259      25.627 -28.970  36.576  1.00 49.90           N  
ANISOU 3512  N   MET C 259     7152   6927   4879    632   -890   -179       N  
ATOM   3513  CA  MET C 259      26.194 -29.895  37.545  1.00 50.13           C  
ANISOU 3513  CA  MET C 259     7192   6958   4899    651   -882   -174       C  
ATOM   3514  C   MET C 259      25.186 -30.327  38.606  1.00 50.24           C  
ANISOU 3514  C   MET C 259     7203   6993   4894    658   -877   -166       C  
ATOM   3515  O   MET C 259      24.405 -29.531  39.079  1.00 50.05           O  
ANISOU 3515  O   MET C 259     7168   6980   4867    668   -881   -170       O  
ATOM   3516  CB  MET C 259      27.436 -29.266  38.195  1.00 50.13           C  
ANISOU 3516  CB  MET C 259     7193   6946   4910    686   -885   -186       C  
ATOM   3517  CG  MET C 259      27.240 -28.644  39.510  1.00 50.01           C  
ANISOU 3517  CG  MET C 259     7172   6940   4891    720   -886   -192       C  
ATOM   3518  SD  MET C 259      28.748 -28.784  40.457  1.00 50.12           S  
ANISOU 3518  SD  MET C 259     7193   6942   4908    757   -883   -199       S  
ATOM   3519  CE  MET C 259      27.990 -29.306  41.990  1.00 50.23           C  
ANISOU 3519  CE  MET C 259     7206   6978   4901    778   -876   -192       C  
ATOM   3520  N   PRO C 260      25.187 -31.613  38.970  1.00 49.84           N  
ANISOU 3520  N   PRO C 260     7161   6947   4828    653   -867   -154       N  
ATOM   3521  CA  PRO C 260      24.118 -32.147  39.815  1.00 50.03           C  
ANISOU 3521  CA  PRO C 260     7184   6991   4833    653   -862   -144       C  
ATOM   3522  C   PRO C 260      24.151 -31.683  41.259  1.00 49.99           C  
ANISOU 3522  C   PRO C 260     7175   6995   4823    691   -862   -149       C  
ATOM   3523  O   PRO C 260      25.183 -31.237  41.747  1.00 49.90           O  
ANISOU 3523  O   PRO C 260     7165   6973   4821    720   -864   -159       O  
ATOM   3524  CB  PRO C 260      24.351 -33.662  39.742  1.00 50.56           C  
ANISOU 3524  CB  PRO C 260     7264   7058   4888    639   -851   -131       C  
ATOM   3525  CG  PRO C 260      25.783 -33.816  39.450  1.00 50.72           C  
ANISOU 3525  CG  PRO C 260     7294   7059   4920    648   -851   -136       C  
ATOM   3526  CD  PRO C 260      26.110 -32.676  38.531  1.00 50.22           C  
ANISOU 3526  CD  PRO C 260     7223   6983   4876    643   -861   -148       C  
ATOM   3527  N   ILE C 261      23.024 -31.840  41.937  1.00 48.91           N  
ANISOU 3527  N   ILE C 261     7034   6878   4672    692   -859   -143       N  
ATOM   3528  CA  ILE C 261      22.884 -31.417  43.313  1.00 48.93           C  
ANISOU 3528  CA  ILE C 261     7032   6892   4669    726   -859   -147       C  
ATOM   3529  C   ILE C 261      22.958 -32.658  44.192  1.00 49.44           C  
ANISOU 3529  C   ILE C 261     7105   6963   4716    734   -848   -136       C  
ATOM   3530  O   ILE C 261      22.672 -33.739  43.722  1.00 49.78           O  
ANISOU 3530  O   ILE C 261     7157   7008   4749    708   -842   -123       O  
ATOM   3531  CB  ILE C 261      21.555 -30.642  43.534  1.00 48.82           C  
ANISOU 3531  CB  ILE C 261     7005   6895   4651    724   -864   -149       C  
ATOM   3532  CG1 ILE C 261      21.606 -29.848  44.839  1.00 49.25           C  
ANISOU 3532  CG1 ILE C 261     7052   6956   4704    764   -866   -158       C  
ATOM   3533  CG2 ILE C 261      20.378 -31.580  43.558  1.00 49.32           C  
ANISOU 3533  CG2 ILE C 261     7070   6974   4695    700   -858   -133       C  
ATOM   3534  CD1 ILE C 261      20.310 -29.277  45.233  1.00 49.71           C  
ANISOU 3534  CD1 ILE C 261     7099   7032   4755    764   -869   -158       C  
ATOM   3535  N   CYS C 262      23.403 -32.531  45.435  1.00 50.14           N  
ANISOU 3535  N   CYS C 262     7194   7055   4801    769   -846   -140       N  
ATOM   3536  CA  CYS C 262      23.459 -33.686  46.337  1.00 50.79           C  
ANISOU 3536  CA  CYS C 262     7286   7145   4867    778   -835   -129       C  
ATOM   3537  C   CYS C 262      22.134 -34.123  46.965  1.00 51.18           C  
ANISOU 3537  C   CYS C 262     7332   7217   4898    772   -830   -118       C  
ATOM   3538  O   CYS C 262      21.422 -33.280  47.487  1.00 51.07           O  
ANISOU 3538  O   CYS C 262     7307   7214   4882    785   -835   -123       O  
ATOM   3539  CB  CYS C 262      24.438 -33.394  47.460  1.00 51.05           C  
ANISOU 3539  CB  CYS C 262     7320   7174   4902    819   -834   -137       C  
ATOM   3540  SG  CYS C 262      26.072 -33.763  46.976  1.00 51.06           S  
ANISOU 3540  SG  CYS C 262     7333   7152   4916    824   -833   -141       S  
ATOM   3541  N   LEU C 263      21.809 -35.422  46.950  1.00 49.70           N  
ANISOU 3541  N   LEU C 263     7154   7034   4695    754   -821   -103       N  
ATOM   3542  CA  LEU C 263      20.663 -35.896  47.735  1.00 50.26           C  
ANISOU 3542  CA  LEU C 263     7224   7126   4747    753   -816    -92       C  
ATOM   3543  C   LEU C 263      21.092 -36.042  49.172  1.00 50.64           C  
ANISOU 3543  C   LEU C 263     7273   7179   4787    790   -810    -93       C  
ATOM   3544  O   LEU C 263      22.154 -36.563  49.446  1.00 50.50           O  
ANISOU 3544  O   LEU C 263     7265   7151   4771    804   -806    -93       O  
ATOM   3545  CB  LEU C 263      20.121 -37.220  47.240  1.00 50.31           C  
ANISOU 3545  CB  LEU C 263     7239   7137   4739    720   -808    -75       C  
ATOM   3546  CG  LEU C 263      19.695 -37.329  45.786  1.00 49.97           C  
ANISOU 3546  CG  LEU C 263     7196   7089   4700    680   -811    -72       C  
ATOM   3547  CD1 LEU C 263      20.890 -37.694  44.950  1.00 49.41           C  
ANISOU 3547  CD1 LEU C 263     7134   6997   4641    671   -810    -74       C  
ATOM   3548  CD2 LEU C 263      18.648 -38.387  45.702  1.00 50.27           C  
ANISOU 3548  CD2 LEU C 263     7238   7141   4720    653   -803    -56       C  
ATOM   3549  N   PRO C 264      20.280 -35.556  50.100  1.00 52.61           N  
ANISOU 3549  N   PRO C 264     7514   7446   5029    808   -811    -94       N  
ATOM   3550  CA  PRO C 264      20.655 -35.478  51.508  1.00 53.40           C  
ANISOU 3550  CA  PRO C 264     7613   7552   5123    847   -807    -97       C  
ATOM   3551  C   PRO C 264      20.584 -36.799  52.226  1.00 54.61           C  
ANISOU 3551  C   PRO C 264     7777   7713   5259    848   -795    -83       C  
ATOM   3552  O   PRO C 264      19.640 -37.552  52.026  1.00 54.98           O  
ANISOU 3552  O   PRO C 264     7827   7770   5292    823   -791    -70       O  
ATOM   3553  CB  PRO C 264      19.614 -34.528  52.081  1.00 53.33           C  
ANISOU 3553  CB  PRO C 264     7590   7561   5112    858   -812   -103       C  
ATOM   3554  CG  PRO C 264      18.419 -34.824  51.312  1.00 53.10           C  
ANISOU 3554  CG  PRO C 264     7560   7541   5076    822   -813    -93       C  
ATOM   3555  CD  PRO C 264      18.887 -35.149  49.896  1.00 52.36           C  
ANISOU 3555  CD  PRO C 264     7473   7430   4992    791   -815    -92       C  
ATOM   3556  N   SER C 265      21.573 -37.071  53.065  1.00 60.93           N  
ANISOU 3556  N   SER C 265     8584   8509   6059    877   -791    -85       N  
ATOM   3557  CA  SER C 265      21.450 -38.152  54.027  1.00 62.28           C  
ANISOU 3557  CA  SER C 265     8763   8690   6212    886   -780    -73       C  
ATOM   3558  C   SER C 265      20.543 -37.643  55.123  1.00 62.78           C  
ANISOU 3558  C   SER C 265     8815   8773   6265    907   -780    -74       C  
ATOM   3559  O   SER C 265      19.489 -38.226  55.407  1.00 63.37           O  
ANISOU 3559  O   SER C 265     8890   8863   6324    895   -774    -62       O  
ATOM   3560  CB  SER C 265      22.812 -38.559  54.594  1.00 62.85           C  
ANISOU 3560  CB  SER C 265     8845   8750   6287    912   -775    -75       C  
ATOM   3561  OG  SER C 265      23.822 -38.523  53.589  1.00 62.22           O  
ANISOU 3561  OG  SER C 265     8770   8649   6222    901   -779    -81       O  
ATOM   3562  N   LYS C 266      20.936 -36.504  55.689  1.00 61.35           N  
ANISOU 3562  N   LYS C 266     8624   8591   6094    938   -786    -89       N  
ATOM   3563  CA  LYS C 266      20.144 -35.841  56.708  1.00 61.79           C  
ANISOU 3563  CA  LYS C 266     8669   8666   6144    960   -787    -92       C  
ATOM   3564  C   LYS C 266      18.875 -35.297  56.064  1.00 60.94           C  
ANISOU 3564  C   LYS C 266     8552   8568   6036    936   -793    -92       C  
ATOM   3565  O   LYS C 266      18.771 -35.217  54.835  1.00 59.90           O  
ANISOU 3565  O   LYS C 266     8420   8426   5912    906   -798    -92       O  
ATOM   3566  CB  LYS C 266      20.930 -34.715  57.383  1.00 61.93           C  
ANISOU 3566  CB  LYS C 266     8679   8679   6173    998   -792   -110       C  
ATOM   3567  CG  LYS C 266      20.485 -34.458  58.827  1.00 62.72           C  
ANISOU 3567  CG  LYS C 266     8771   8798   6262   1031   -788   -111       C  
ATOM   3568  CD  LYS C 266      20.690 -33.001  59.289  1.00 63.21           C  
ANISOU 3568  CD  LYS C 266     8820   8861   6336   1060   -796   -129       C  
ATOM   3569  CE  LYS C 266      22.171 -32.658  59.488  1.00 63.02           C  
ANISOU 3569  CE  LYS C 266     8799   8821   6325   1086   -798   -141       C  
ATOM   3570  NZ  LYS C 266      22.382 -31.487  60.405  1.00 62.77           N  
ANISOU 3570  NZ  LYS C 266     8757   8795   6299   1123   -802   -157       N  
ATOM   3571  N   ASP C 267      17.882 -34.970  56.876  1.00 58.62           N  
ANISOU 3571  N   ASP C 267     8248   8293   5732    948   -792    -91       N  
ATOM   3572  CA  ASP C 267      16.708 -34.328  56.325  1.00 57.93           C  
ANISOU 3572  CA  ASP C 267     8151   8215   5645    928   -799    -92       C  
ATOM   3573  C   ASP C 267      16.577 -32.903  56.855  1.00 57.73           C  
ANISOU 3573  C   ASP C 267     8110   8195   5628    956   -807   -108       C  
ATOM   3574  O   ASP C 267      16.239 -32.713  58.034  1.00 58.64           O  
ANISOU 3574  O   ASP C 267     8221   8326   5735    983   -803   -109       O  
ATOM   3575  CB  ASP C 267      15.464 -35.148  56.665  1.00 58.71           C  
ANISOU 3575  CB  ASP C 267     8251   8332   5724    912   -792    -76       C  
ATOM   3576  CG  ASP C 267      14.187 -34.375  56.455  1.00 58.47           C  
ANISOU 3576  CG  ASP C 267     8208   8315   5692    901   -798    -79       C  
ATOM   3577  OD1 ASP C 267      13.792 -34.185  55.275  1.00 57.42           O  
ANISOU 3577  OD1 ASP C 267     8074   8177   5566    870   -804    -78       O  
ATOM   3578  OD2 ASP C 267      13.593 -33.952  57.475  1.00 59.41           O  
ANISOU 3578  OD2 ASP C 267     8318   8451   5803    924   -797    -81       O  
ATOM   3579  N   TYR C 268      16.822 -31.889  56.022  1.00 56.50           N  
ANISOU 3579  N   TYR C 268     7949   8029   5491    951   -816   -120       N  
ATOM   3580  CA  TYR C 268      16.509 -30.580  56.546  1.00 56.43           C  
ANISOU 3580  CA  TYR C 268     7926   8028   5488    975   -823   -134       C  
ATOM   3581  C   TYR C 268      15.184 -30.108  55.961  1.00 55.92           C  
ANISOU 3581  C   TYR C 268     7852   7974   5422    952   -829   -133       C  
ATOM   3582  O   TYR C 268      15.148 -29.278  55.057  1.00 54.98           O  
ANISOU 3582  O   TYR C 268     7727   7846   5316    939   -838   -141       O  
ATOM   3583  CB  TYR C 268      17.597 -29.581  56.163  1.00 55.71           C  
ANISOU 3583  CB  TYR C 268     7831   7918   5417    990   -831   -151       C  
ATOM   3584  CG  TYR C 268      19.011 -30.119  55.993  1.00 55.74           C  
ANISOU 3584  CG  TYR C 268     7847   7904   5428    995   -828   -152       C  
ATOM   3585  CD1 TYR C 268      19.964 -29.934  56.987  1.00 56.48           C  
ANISOU 3585  CD1 TYR C 268     7942   7995   5523   1032   -826   -160       C  
ATOM   3586  CD2 TYR C 268      19.411 -30.764  54.820  1.00 55.09           C  
ANISOU 3586  CD2 TYR C 268     7774   7806   5350    964   -828   -145       C  
ATOM   3587  CE1 TYR C 268      21.261 -30.405  56.832  1.00 56.56           C  
ANISOU 3587  CE1 TYR C 268     7963   7988   5541   1037   -823   -161       C  
ATOM   3588  CE2 TYR C 268      20.722 -31.239  54.660  1.00 55.18           C  
ANISOU 3588  CE2 TYR C 268     7797   7801   5369    970   -825   -147       C  
ATOM   3589  CZ  TYR C 268      21.633 -31.052  55.671  1.00 55.91           C  
ANISOU 3589  CZ  TYR C 268     7890   7891   5463   1006   -823   -154       C  
ATOM   3590  OH  TYR C 268      22.933 -31.502  55.543  1.00 56.09           O  
ANISOU 3590  OH  TYR C 268     7923   7897   5492   1013   -820   -156       O  
ATOM   3591  N   ALA C 269      14.095 -30.582  56.559  1.00 55.93           N  
ANISOU 3591  N   ALA C 269     7851   7994   5406    948   -824   -122       N  
ATOM   3592  CA  ALA C 269      12.740 -30.141  56.281  1.00 55.76           C  
ANISOU 3592  CA  ALA C 269     7819   7987   5380    932   -828   -120       C  
ATOM   3593  C   ALA C 269      12.200 -29.408  57.484  1.00 56.63           C  
ANISOU 3593  C   ALA C 269     7918   8115   5485    964   -828   -127       C  
ATOM   3594  O   ALA C 269      11.044 -29.034  57.502  1.00 56.75           O  
ANISOU 3594  O   ALA C 269     7924   8143   5494    957   -831   -126       O  
ATOM   3595  CB  ALA C 269      11.854 -31.305  55.922  1.00 55.99           C  
ANISOU 3595  CB  ALA C 269     7855   8024   5393    899   -822   -102       C  
ATOM   3596  N   GLU C 270      13.000 -29.295  58.531  1.00 55.18           N  
ANISOU 3596  N   GLU C 270     7734   7930   5300   1000   -824   -133       N  
ATOM   3597  CA  GLU C 270      12.506 -28.761  59.786  1.00 56.20           C  
ANISOU 3597  CA  GLU C 270     7854   8078   5422   1032   -823   -138       C  
ATOM   3598  C   GLU C 270      12.468 -27.233  59.790  1.00 55.84           C  
ANISOU 3598  C   GLU C 270     7794   8031   5390   1050   -832   -156       C  
ATOM   3599  O   GLU C 270      13.198 -26.589  59.031  1.00 54.90           O  
ANISOU 3599  O   GLU C 270     7676   7896   5289   1047   -840   -167       O  
ATOM   3600  CB  GLU C 270      13.365 -29.270  60.935  1.00 57.31           C  
ANISOU 3600  CB  GLU C 270     8000   8218   5556   1063   -815   -137       C  
ATOM   3601  CG  GLU C 270      13.572 -30.763  60.893  1.00 57.66           C  
ANISOU 3601  CG  GLU C 270     8059   8261   5588   1046   -805   -120       C  
ATOM   3602  CD  GLU C 270      14.012 -31.317  62.226  1.00 59.04           C  
ANISOU 3602  CD  GLU C 270     8237   8443   5751   1076   -796   -117       C  
ATOM   3603  OE1 GLU C 270      13.432 -30.896  63.259  1.00 59.92           O  
ANISOU 3603  OE1 GLU C 270     8339   8571   5855   1100   -794   -119       O  
ATOM   3604  OE2 GLU C 270      14.940 -32.167  62.234  1.00 59.30           O  
ANISOU 3604  OE2 GLU C 270     8283   8465   5784   1077   -790   -111       O  
ATOM   3605  N   VAL C 271      11.602 -26.648  60.621  1.00 55.27           N  
ANISOU 3605  N   VAL C 271     7711   7978   5311   1068   -833   -160       N  
ATOM   3606  CA  VAL C 271      11.579 -25.197  60.729  1.00 55.08           C  
ANISOU 3606  CA  VAL C 271     7674   7954   5299   1089   -841   -177       C  
ATOM   3607  C   VAL C 271      12.810 -24.794  61.543  1.00 55.59           C  
ANISOU 3607  C   VAL C 271     7739   8011   5370   1126   -840   -189       C  
ATOM   3608  O   VAL C 271      13.218 -25.468  62.477  1.00 56.56           O  
ANISOU 3608  O   VAL C 271     7867   8139   5483   1145   -832   -184       O  
ATOM   3609  CB  VAL C 271      10.245 -24.621  61.341  1.00 55.76           C  
ANISOU 3609  CB  VAL C 271     7747   8064   5377   1097   -842   -178       C  
ATOM   3610  CG1 VAL C 271       9.214 -25.708  61.521  1.00 56.23           C  
ANISOU 3610  CG1 VAL C 271     7810   8139   5417   1077   -835   -160       C  
ATOM   3611  CG2 VAL C 271      10.498 -23.846  62.646  1.00 56.94           C  
ANISOU 3611  CG2 VAL C 271     7887   8222   5525   1141   -842   -190       C  
ATOM   3612  N   GLY C 272      13.366 -23.655  61.156  1.00 57.53           N  
ANISOU 3612  N   GLY C 272     7979   8245   5633   1136   -849   -205       N  
ATOM   3613  CA  GLY C 272      14.667 -23.186  61.563  1.00 57.68           C  
ANISOU 3613  CA  GLY C 272     8000   8251   5663   1164   -850   -218       C  
ATOM   3614  C   GLY C 272      15.647 -23.322  60.419  1.00 56.44           C  
ANISOU 3614  C   GLY C 272     7853   8071   5522   1145   -854   -219       C  
ATOM   3615  O   GLY C 272      16.543 -22.506  60.303  1.00 56.17           O  
ANISOU 3615  O   GLY C 272     7817   8024   5502   1161   -859   -233       O  
ATOM   3616  N   ARG C 273      15.439 -24.264  59.513  1.00 55.62           N  
ANISOU 3616  N   ARG C 273     7757   7961   5414   1110   -852   -206       N  
ATOM   3617  CA  ARG C 273      16.279 -24.315  58.326  1.00 54.49           C  
ANISOU 3617  CA  ARG C 273     7622   7796   5285   1089   -856   -208       C  
ATOM   3618  C   ARG C 273      15.850 -23.260  57.318  1.00 53.53           C  
ANISOU 3618  C   ARG C 273     7492   7669   5178   1073   -867   -217       C  
ATOM   3619  O   ARG C 273      14.717 -22.771  57.355  1.00 53.59           O  
ANISOU 3619  O   ARG C 273     7490   7690   5181   1068   -870   -217       O  
ATOM   3620  CB  ARG C 273      16.246 -25.696  57.670  1.00 54.17           C  
ANISOU 3620  CB  ARG C 273     7594   7751   5237   1057   -850   -191       C  
ATOM   3621  CG  ARG C 273      17.089 -26.782  58.363  1.00 54.93           C  
ANISOU 3621  CG  ARG C 273     7702   7844   5325   1070   -841   -183       C  
ATOM   3622  CD  ARG C 273      18.502 -26.287  58.680  1.00 55.10           C  
ANISOU 3622  CD  ARG C 273     7726   7851   5359   1098   -842   -196       C  
ATOM   3623  NE  ARG C 273      19.411 -27.323  59.182  1.00 55.59           N  
ANISOU 3623  NE  ARG C 273     7800   7908   5415   1108   -834   -189       N  
ATOM   3624  CZ  ARG C 273      19.220 -28.037  60.294  1.00 56.89           C  
ANISOU 3624  CZ  ARG C 273     7966   8085   5563   1124   -825   -181       C  
ATOM   3625  NH1 ARG C 273      18.118 -27.872  61.044  1.00 57.86           N  
ANISOU 3625  NH1 ARG C 273     8081   8230   5674   1133   -823   -178       N  
ATOM   3626  NH2 ARG C 273      20.131 -28.937  60.649  1.00 57.31           N  
ANISOU 3626  NH2 ARG C 273     8031   8131   5612   1132   -818   -175       N  
ATOM   3627  N   VAL C 274      16.757 -22.899  56.419  1.00 48.23           N  
ANISOU 3627  N   VAL C 274     6825   6977   4523   1065   -872   -224       N  
ATOM   3628  CA  VAL C 274      16.466 -21.950  55.343  1.00 47.30           C  
ANISOU 3628  CA  VAL C 274     6701   6852   4420   1047   -882   -232       C  
ATOM   3629  C   VAL C 274      16.879 -22.622  54.052  1.00 46.40           C  
ANISOU 3629  C   VAL C 274     6597   6721   4312   1013   -883   -224       C  
ATOM   3630  O   VAL C 274      17.746 -23.474  54.077  1.00 46.48           O  
ANISOU 3630  O   VAL C 274     6618   6722   4320   1012   -878   -219       O  
ATOM   3631  CB  VAL C 274      17.227 -20.629  55.552  1.00 47.35           C  
ANISOU 3631  CB  VAL C 274     6700   6848   4441   1076   -889   -251       C  
ATOM   3632  CG1 VAL C 274      17.187 -19.758  54.324  1.00 46.37           C  
ANISOU 3632  CG1 VAL C 274     6573   6712   4334   1056   -899   -259       C  
ATOM   3633  CG2 VAL C 274      16.698 -19.892  56.771  1.00 48.37           C  
ANISOU 3633  CG2 VAL C 274     6819   6995   4565   1108   -889   -259       C  
ATOM   3634  N   GLY C 275      16.318 -22.235  52.921  1.00 43.51           N  
ANISOU 3634  N   GLY C 275     6227   6351   3953    984   -890   -224       N  
ATOM   3635  CA  GLY C 275      16.584 -22.956  51.697  1.00 42.76           C  
ANISOU 3635  CA  GLY C 275     6142   6242   3862    949   -890   -216       C  
ATOM   3636  C   GLY C 275      16.695 -21.989  50.557  1.00 41.86           C  
ANISOU 3636  C   GLY C 275     6023   6115   3765    935   -899   -225       C  
ATOM   3637  O   GLY C 275      16.465 -20.819  50.733  1.00 41.81           O  
ANISOU 3637  O   GLY C 275     6007   6112   3767    950   -906   -237       O  
ATOM   3638  N   TYR C 276      17.095 -22.459  49.396  1.00 45.41           N  
ANISOU 3638  N   TYR C 276     6480   6551   4222    906   -900   -220       N  
ATOM   3639  CA  TYR C 276      17.263 -21.590  48.248  1.00 44.60           C  
ANISOU 3639  CA  TYR C 276     6375   6435   4137    890   -909   -228       C  
ATOM   3640  C   TYR C 276      16.447 -22.140  47.102  1.00 44.08           C  
ANISOU 3640  C   TYR C 276     6311   6371   4068    848   -910   -217       C  
ATOM   3641  O   TYR C 276      16.675 -23.289  46.697  1.00 43.94           O  
ANISOU 3641  O   TYR C 276     6304   6349   4044    827   -904   -205       O  
ATOM   3642  CB  TYR C 276      18.730 -21.522  47.833  1.00 44.29           C  
ANISOU 3642  CB  TYR C 276     6343   6373   4112    897   -911   -235       C  
ATOM   3643  CG  TYR C 276      19.606 -20.558  48.635  1.00 44.71           C  
ANISOU 3643  CG  TYR C 276     6392   6420   4174    936   -914   -251       C  
ATOM   3644  CD1 TYR C 276      19.576 -20.547  50.042  1.00 45.49           C  
ANISOU 3644  CD1 TYR C 276     6489   6532   4264    969   -909   -254       C  
ATOM   3645  CD2 TYR C 276      20.499 -19.677  47.982  1.00 44.38           C  
ANISOU 3645  CD2 TYR C 276     6350   6360   4152    940   -921   -264       C  
ATOM   3646  CE1 TYR C 276      20.382 -19.685  50.760  1.00 45.94           C  
ANISOU 3646  CE1 TYR C 276     6542   6583   4329   1004   -912   -268       C  
ATOM   3647  CE2 TYR C 276      21.302 -18.816  48.703  1.00 44.83           C  
ANISOU 3647  CE2 TYR C 276     6404   6411   4217    975   -924   -278       C  
ATOM   3648  CZ  TYR C 276      21.236 -18.824  50.091  1.00 45.62           C  
ANISOU 3648  CZ  TYR C 276     6501   6524   4307   1007   -919   -281       C  
ATOM   3649  OH  TYR C 276      22.027 -17.975  50.837  1.00 46.16           O  
ANISOU 3649  OH  TYR C 276     6567   6589   4384   1042   -922   -295       O  
ATOM   3650  N   VAL C 277      15.514 -21.377  46.548  1.00 38.80           N  
ANISOU 3650  N   VAL C 277     5632   5707   3402    834   -917   -220       N  
ATOM   3651  CA  VAL C 277      14.804 -21.923  45.400  1.00 38.72           C  
ANISOU 3651  CA  VAL C 277     5624   5697   3389    793   -917   -208       C  
ATOM   3652  C   VAL C 277      15.173 -21.176  44.145  1.00 38.56           C  
ANISOU 3652  C   VAL C 277     5602   5661   3387    776   -926   -216       C  
ATOM   3653  O   VAL C 277      15.046 -19.998  44.093  1.00 38.55           O  
ANISOU 3653  O   VAL C 277     5593   5659   3397    788   -933   -228       O  
ATOM   3654  CB  VAL C 277      13.286 -21.895  45.598  1.00 38.83           C  
ANISOU 3654  CB  VAL C 277     5630   5732   3390    781   -918   -202       C  
ATOM   3655  CG1 VAL C 277      12.614 -22.560  44.442  1.00 38.74           C  
ANISOU 3655  CG1 VAL C 277     5623   5722   3376    738   -917   -190       C  
ATOM   3656  CG2 VAL C 277      12.898 -22.605  46.888  1.00 38.99           C  
ANISOU 3656  CG2 VAL C 277     5653   5770   3393    799   -909   -195       C  
ATOM   3657  N   SER C 278      15.677 -21.860  43.139  1.00 42.20           N  
ANISOU 3657  N   SER C 278     6072   6110   3853    749   -924   -210       N  
ATOM   3658  CA  SER C 278      15.900 -21.210  41.863  1.00 41.64           C  
ANISOU 3658  CA  SER C 278     5999   6024   3797    730   -931   -215       C  
ATOM   3659  C   SER C 278      14.586 -21.287  41.160  1.00 41.56           C  
ANISOU 3659  C   SER C 278     5984   6026   3781    698   -933   -207       C  
ATOM   3660  O   SER C 278      13.730 -21.982  41.652  1.00 41.93           O  
ANISOU 3660  O   SER C 278     6031   6090   3812    692   -928   -197       O  
ATOM   3661  CB  SER C 278      17.005 -21.912  41.049  1.00 41.32           C  
ANISOU 3661  CB  SER C 278     5970   5966   3765    714   -929   -212       C  
ATOM   3662  OG  SER C 278      17.306 -23.211  41.542  1.00 41.75           O  
ANISOU 3662  OG  SER C 278     6034   6023   3805    714   -919   -201       O  
ATOM   3663  N   GLY C 279      14.421 -20.634  40.009  1.00 45.41           N  
ANISOU 3663  N   GLY C 279     6467   6505   4281    677   -941   -211       N  
ATOM   3664  CA  GLY C 279      13.255 -20.882  39.170  1.00 45.39           C  
ANISOU 3664  CA  GLY C 279     6461   6513   4272    642   -942   -202       C  
ATOM   3665  C   GLY C 279      13.224 -20.265  37.782  1.00 45.24           C  
ANISOU 3665  C   GLY C 279     6440   6483   4268    617   -949   -206       C  
ATOM   3666  O   GLY C 279      13.795 -19.219  37.538  1.00 45.19           O  
ANISOU 3666  O   GLY C 279     6428   6464   4277    630   -956   -218       O  
ATOM   3667  N   TRP C 280      12.546 -20.935  36.857  1.00 51.19           N  
ANISOU 3667  N   TRP C 280     7194   7240   5014    579   -947   -195       N  
ATOM   3668  CA  TRP C 280      12.276 -20.387  35.526  1.00 50.94           C  
ANISOU 3668  CA  TRP C 280     7158   7202   4994    552   -954   -197       C  
ATOM   3669  C   TRP C 280      10.861 -19.861  35.408  1.00 51.16           C  
ANISOU 3669  C   TRP C 280     7176   7247   5017    540   -958   -195       C  
ATOM   3670  O   TRP C 280      10.437 -19.464  34.312  1.00 51.07           O  
ANISOU 3670  O   TRP C 280     7160   7233   5012    515   -963   -195       O  
ATOM   3671  CB  TRP C 280      12.554 -21.435  34.439  1.00 50.81           C  
ANISOU 3671  CB  TRP C 280     7150   7179   4977    518   -949   -186       C  
ATOM   3672  CG  TRP C 280      14.027 -21.580  34.260  1.00 50.59           C  
ANISOU 3672  CG  TRP C 280     7130   7131   4960    529   -947   -192       C  
ATOM   3673  CD1 TRP C 280      14.845 -22.547  34.808  1.00 50.76           C  
ANISOU 3673  CD1 TRP C 280     7162   7149   4976    539   -940   -187       C  
ATOM   3674  CD2 TRP C 280      14.892 -20.682  33.552  1.00 50.25           C  
ANISOU 3674  CD2 TRP C 280     7086   7069   4936    533   -954   -203       C  
ATOM   3675  NE1 TRP C 280      16.160 -22.309  34.454  1.00 50.53           N  
ANISOU 3675  NE1 TRP C 280     7138   7099   4962    549   -941   -195       N  
ATOM   3676  CE2 TRP C 280      16.209 -21.169  33.692  1.00 50.22           C  
ANISOU 3676  CE2 TRP C 280     7092   7051   4938    546   -950   -205       C  
ATOM   3677  CE3 TRP C 280      14.678 -19.523  32.804  1.00 50.03           C  
ANISOU 3677  CE3 TRP C 280     7050   7036   4923    528   -963   -212       C  
ATOM   3678  CZ2 TRP C 280      17.292 -20.539  33.111  1.00 49.98           C  
ANISOU 3678  CZ2 TRP C 280     7064   7001   4926    552   -954   -214       C  
ATOM   3679  CZ3 TRP C 280      15.764 -18.902  32.221  1.00 49.79           C  
ANISOU 3679  CZ3 TRP C 280     7021   6986   4910    535   -967   -221       C  
ATOM   3680  CH2 TRP C 280      17.057 -19.411  32.386  1.00 49.77           C  
ANISOU 3680  CH2 TRP C 280     7029   6968   4912    547   -963   -223       C  
ATOM   3681  N   GLY C 281      10.123 -19.890  36.518  1.00 49.59           N  
ANISOU 3681  N   GLY C 281     6973   7064   4805    558   -956   -193       N  
ATOM   3682  CA  GLY C 281       8.709 -19.555  36.479  1.00 49.92           C  
ANISOU 3682  CA  GLY C 281     7006   7123   4839    545   -960   -190       C  
ATOM   3683  C   GLY C 281       8.423 -18.073  36.279  1.00 49.92           C  
ANISOU 3683  C   GLY C 281     6994   7120   4852    557   -970   -203       C  
ATOM   3684  O   GLY C 281       9.370 -17.275  36.196  1.00 49.60           O  
ANISOU 3684  O   GLY C 281     6953   7064   4827    575   -974   -215       O  
ATOM   3685  N   ARG C 282       7.130 -17.717  36.266  1.00 48.28           N  
ANISOU 3685  N   ARG C 282     6778   6928   4637    547   -973   -200       N  
ATOM   3686  CA  ARG C 282       6.619 -16.359  36.017  1.00 48.41           C  
ANISOU 3686  CA  ARG C 282     6783   6945   4664    554   -982   -211       C  
ATOM   3687  C   ARG C 282       7.022 -15.322  37.073  1.00 48.52           C  
ANISOU 3687  C   ARG C 282     6792   6958   4685    596   -986   -225       C  
ATOM   3688  O   ARG C 282       7.426 -15.659  38.178  1.00 48.63           O  
ANISOU 3688  O   ARG C 282     6809   6976   4692    622   -981   -226       O  
ATOM   3689  CB  ARG C 282       5.077 -16.409  35.906  1.00 48.89           C  
ANISOU 3689  CB  ARG C 282     6837   7025   4713    534   -984   -203       C  
ATOM   3690  CG  ARG C 282       4.583 -16.886  34.517  1.00 48.83           C  
ANISOU 3690  CG  ARG C 282     6832   7017   4706    489   -985   -194       C  
ATOM   3691  CD  ARG C 282       3.069 -17.165  34.389  1.00 49.39           C  
ANISOU 3691  CD  ARG C 282     6897   7107   4762    466   -985   -184       C  
ATOM   3692  NE  ARG C 282       2.687 -17.298  32.970  1.00 49.10           N  
ANISOU 3692  NE  ARG C 282     6860   7067   4729    426   -988   -178       N  
ATOM   3693  CZ  ARG C 282       2.265 -18.425  32.381  1.00 49.52           C  
ANISOU 3693  CZ  ARG C 282     6919   7126   4771    392   -982   -165       C  
ATOM   3694  NH1 ARG C 282       2.111 -19.547  33.089  1.00 50.29           N  
ANISOU 3694  NH1 ARG C 282     7023   7233   4851    392   -974   -154       N  
ATOM   3695  NH2 ARG C 282       1.985 -18.420  31.076  1.00 49.28           N  
ANISOU 3695  NH2 ARG C 282     6886   7093   4745    359   -985   -161       N  
ATOM   3696  N   ASN C 283       6.912 -14.050  36.730  1.00 48.80           N  
ANISOU 3696  N   ASN C 283     6820   6989   4734    604   -994   -237       N  
ATOM   3697  CA  ASN C 283       7.137 -12.970  37.695  1.00 49.11           C  
ANISOU 3697  CA  ASN C 283     6852   7028   4778    644   -998   -251       C  
ATOM   3698  C   ASN C 283       5.919 -12.029  37.832  1.00 49.55           C  
ANISOU 3698  C   ASN C 283     6896   7098   4833    647  -1004   -255       C  
ATOM   3699  O   ASN C 283       4.798 -12.371  37.442  1.00 49.62           O  
ANISOU 3699  O   ASN C 283     6902   7120   4833    622  -1004   -246       O  
ATOM   3700  CB  ASN C 283       8.358 -12.170  37.302  1.00 48.96           C  
ANISOU 3700  CB  ASN C 283     6835   6988   4779    657  -1003   -263       C  
ATOM   3701  CG  ASN C 283       8.313 -11.740  35.847  1.00 48.74           C  
ANISOU 3701  CG  ASN C 283     6806   6949   4764    628  -1009   -264       C  
ATOM   3702  OD1 ASN C 283       7.226 -11.659  35.238  1.00 48.80           O  
ANISOU 3702  OD1 ASN C 283     6808   6966   4767    604  -1012   -258       O  
ATOM   3703  ND2 ASN C 283       9.501 -11.468  35.267  1.00 48.57           N  
ANISOU 3703  ND2 ASN C 283     6790   6907   4758    630  -1011   -270       N  
ATOM   3704  N   ALA C 284       6.120 -10.880  38.472  1.00 47.73           N  
ANISOU 3704  N   ALA C 284     6659   6866   4611    680  -1009   -270       N  
ATOM   3705  CA  ALA C 284       5.010  -9.971  38.800  1.00 48.41           C  
ANISOU 3705  CA  ALA C 284     6733   6966   4695    689  -1014   -275       C  
ATOM   3706  C   ALA C 284       4.366  -9.290  37.597  1.00 48.48           C  
ANISOU 3706  C   ALA C 284     6737   6972   4712    663  -1022   -276       C  
ATOM   3707  O   ALA C 284       3.367  -8.618  37.769  1.00 49.05           O  
ANISOU 3707  O   ALA C 284     6799   7056   4782    667  -1027   -279       O  
ATOM   3708  CB  ALA C 284       5.468  -8.927  39.779  1.00 48.80           C  
ANISOU 3708  CB  ALA C 284     6777   7014   4750    731  -1017   -291       C  
ATOM   3709  N   ASN C 285       4.934  -9.430  36.400  1.00 49.90           N  
ANISOU 3709  N   ASN C 285     6922   7136   4903    638  -1024   -274       N  
ATOM   3710  CA  ASN C 285       4.170  -9.165  35.168  1.00 50.01           C  
ANISOU 3710  CA  ASN C 285     6932   7150   4921    605  -1030   -270       C  
ATOM   3711  C   ASN C 285       3.540 -10.452  34.632  1.00 49.93           C  
ANISOU 3711  C   ASN C 285     6926   7148   4897    569  -1024   -253       C  
ATOM   3712  O   ASN C 285       3.059 -10.468  33.489  1.00 49.99           O  
ANISOU 3712  O   ASN C 285     6933   7154   4907    537  -1027   -248       O  
ATOM   3713  CB  ASN C 285       5.022  -8.553  34.054  1.00 49.70           C  
ANISOU 3713  CB  ASN C 285     6894   7089   4900    596  -1035   -277       C  
ATOM   3714  CG  ASN C 285       5.670  -7.247  34.456  1.00 49.92           C  
ANISOU 3714  CG  ASN C 285     6918   7106   4942    629  -1041   -294       C  
ATOM   3715  OD1 ASN C 285       5.187  -6.547  35.356  1.00 50.30           O  
ANISOU 3715  OD1 ASN C 285     6959   7164   4987    655  -1043   -301       O  
ATOM   3716  ND2 ASN C 285       6.779  -6.903  33.784  1.00 49.77           N  
ANISOU 3716  ND2 ASN C 285     6904   7066   4939    629  -1044   -300       N  
ATOM   3717  N   PHE C 286       3.631 -11.542  35.410  1.00 47.61           N  
ANISOU 3717  N   PHE C 286     6638   6862   4588    573  -1016   -244       N  
ATOM   3718  CA  PHE C 286       3.105 -12.863  35.020  1.00 47.57           C  
ANISOU 3718  CA  PHE C 286     6639   6865   4569    540  -1009   -228       C  
ATOM   3719  C   PHE C 286       3.697 -13.273  33.676  1.00 47.16           C  
ANISOU 3719  C   PHE C 286     6593   6799   4526    509  -1009   -223       C  
ATOM   3720  O   PHE C 286       3.121 -14.069  32.950  1.00 47.36           O  
ANISOU 3720  O   PHE C 286     6621   6830   4543    475  -1007   -211       O  
ATOM   3721  CB  PHE C 286       1.565 -12.888  34.963  1.00 48.18           C  
ANISOU 3721  CB  PHE C 286     6709   6962   4634    523  -1011   -221       C  
ATOM   3722  CG  PHE C 286       0.890 -13.196  36.291  1.00 48.66           C  
ANISOU 3722  CG  PHE C 286     6767   7042   4679    543  -1007   -218       C  
ATOM   3723  CD1 PHE C 286       1.628 -13.485  37.421  1.00 48.51           C  
ANISOU 3723  CD1 PHE C 286     6753   7023   4657    574  -1001   -221       C  
ATOM   3724  CD2 PHE C 286      -0.479 -13.202  36.401  1.00 49.33           C  
ANISOU 3724  CD2 PHE C 286     6846   7145   4753    532  -1008   -212       C  
ATOM   3725  CE1 PHE C 286       1.009 -13.760  38.637  1.00 49.07           C  
ANISOU 3725  CE1 PHE C 286     6821   7111   4713    593   -997   -218       C  
ATOM   3726  CE2 PHE C 286      -1.085 -13.480  37.610  1.00 49.87           C  
ANISOU 3726  CE2 PHE C 286     6912   7230   4806    551  -1004   -209       C  
ATOM   3727  CZ  PHE C 286      -0.329 -13.761  38.726  1.00 49.74           C  
ANISOU 3727  CZ  PHE C 286     6899   7213   4786    582   -998   -212       C  
ATOM   3728  N   LYS C 287       4.870 -12.717  33.379  1.00 52.49           N  
ANISOU 3728  N   LYS C 287     7271   7454   5217    522  -1012   -233       N  
ATOM   3729  CA  LYS C 287       5.744 -13.157  32.294  1.00 52.08           C  
ANISOU 3729  CA  LYS C 287     7227   7387   5175    500  -1011   -230       C  
ATOM   3730  C   LYS C 287       6.673 -14.280  32.776  1.00 51.65           C  
ANISOU 3730  C   LYS C 287     7184   7327   5114    506  -1002   -225       C  
ATOM   3731  O   LYS C 287       7.274 -14.209  33.880  1.00 51.56           O  
ANISOU 3731  O   LYS C 287     7175   7315   5102    539  -1000   -231       O  
ATOM   3732  CB  LYS C 287       6.603 -11.995  31.773  1.00 51.97           C  
ANISOU 3732  CB  LYS C 287     7211   7354   5181    512  -1018   -244       C  
ATOM   3733  CG  LYS C 287       6.100 -11.307  30.505  1.00 52.30           C  
ANISOU 3733  CG  LYS C 287     7247   7392   5233    487  -1025   -246       C  
ATOM   3734  CD  LYS C 287       7.150 -10.313  29.930  1.00 51.97           C  
ANISOU 3734  CD  LYS C 287     7206   7329   5212    498  -1031   -258       C  
ATOM   3735  CE  LYS C 287       7.186  -8.923  30.663  1.00 52.21           C  
ANISOU 3735  CE  LYS C 287     7229   7357   5251    534  -1038   -273       C  
ATOM   3736  NZ  LYS C 287       8.187  -7.909  30.099  1.00 51.70           N  
ANISOU 3736  NZ  LYS C 287     7164   7271   5207    544  -1044   -286       N  
ATOM   3737  N   PHE C 288       6.811 -15.311  31.948  1.00 49.86           N  
ANISOU 3737  N   PHE C 288     6963   7097   4883    475   -997   -214       N  
ATOM   3738  CA  PHE C 288       7.861 -16.301  32.188  1.00 49.44           C  
ANISOU 3738  CA  PHE C 288     6921   7036   4828    479   -989   -210       C  
ATOM   3739  C   PHE C 288       9.191 -15.551  32.212  1.00 49.06           C  
ANISOU 3739  C   PHE C 288     6876   6968   4798    504   -993   -223       C  
ATOM   3740  O   PHE C 288       9.464 -14.756  31.316  1.00 49.03           O  
ANISOU 3740  O   PHE C 288     6869   6952   4809    496   -999   -230       O  
ATOM   3741  CB  PHE C 288       7.837 -17.411  31.115  1.00 49.35           C  
ANISOU 3741  CB  PHE C 288     6916   7023   4812    440   -984   -198       C  
ATOM   3742  CG  PHE C 288       6.816 -18.509  31.379  1.00 49.67           C  
ANISOU 3742  CG  PHE C 288     6959   7083   4832    420   -978   -183       C  
ATOM   3743  CD1 PHE C 288       6.654 -19.053  32.654  1.00 49.82           C  
ANISOU 3743  CD1 PHE C 288     6980   7112   4836    440   -972   -179       C  
ATOM   3744  CD2 PHE C 288       6.035 -18.999  30.351  1.00 49.94           C  
ANISOU 3744  CD2 PHE C 288     6991   7124   4860    381   -977   -174       C  
ATOM   3745  CE1 PHE C 288       5.738 -20.049  32.890  1.00 50.19           C  
ANISOU 3745  CE1 PHE C 288     7029   7175   4865    422   -967   -166       C  
ATOM   3746  CE2 PHE C 288       5.114 -20.005  30.583  1.00 50.32           C  
ANISOU 3746  CE2 PHE C 288     7041   7189   4890    362   -971   -161       C  
ATOM   3747  CZ  PHE C 288       4.970 -20.527  31.857  1.00 50.45           C  
ANISOU 3747  CZ  PHE C 288     7061   7215   4892    383   -966   -157       C  
ATOM   3748  N   THR C 289       9.998 -15.796  33.243  1.00 46.91           N  
ANISOU 3748  N   THR C 289     6609   6692   4524    533   -989   -226       N  
ATOM   3749  CA  THR C 289      11.170 -14.955  33.506  1.00 46.69           C  
ANISOU 3749  CA  THR C 289     6582   6647   4511    562   -992   -240       C  
ATOM   3750  C   THR C 289      12.269 -15.044  32.456  1.00 46.34           C  
ANISOU 3750  C   THR C 289     6544   6582   4481    549   -993   -242       C  
ATOM   3751  O   THR C 289      12.526 -16.105  31.889  1.00 46.06           O  
ANISOU 3751  O   THR C 289     6516   6544   4441    526   -987   -232       O  
ATOM   3752  CB  THR C 289      11.812 -15.262  34.883  1.00 46.75           C  
ANISOU 3752  CB  THR C 289     6594   6657   4512    597   -987   -243       C  
ATOM   3753  OG1 THR C 289      12.996 -14.469  35.024  1.00 46.37           O  
ANISOU 3753  OG1 THR C 289     6546   6591   4480    622   -991   -256       O  
ATOM   3754  CG2 THR C 289      12.150 -16.718  35.012  1.00 46.45           C  
ANISOU 3754  CG2 THR C 289     6566   6620   4463    585   -978   -230       C  
ATOM   3755  N   ASP C 290      12.911 -13.909  32.215  1.00 45.57           N  
ANISOU 3755  N   ASP C 290     6444   6471   4401    564  -1000   -255       N  
ATOM   3756  CA  ASP C 290      13.984 -13.815  31.236  1.00 45.40           C  
ANISOU 3756  CA  ASP C 290     6428   6428   4394    555  -1002   -258       C  
ATOM   3757  C   ASP C 290      15.348 -14.303  31.731  1.00 45.22           C  
ANISOU 3757  C   ASP C 290     6415   6393   4375    574   -997   -261       C  
ATOM   3758  O   ASP C 290      16.265 -14.553  30.952  1.00 45.07           O  
ANISOU 3758  O   ASP C 290     6403   6357   4365    564   -996   -261       O  
ATOM   3759  CB  ASP C 290      14.113 -12.374  30.781  1.00 45.64           C  
ANISOU 3759  CB  ASP C 290     6451   6448   4441    564  -1011   -271       C  
ATOM   3760  CG  ASP C 290      13.151 -12.048  29.704  1.00 45.99           C  
ANISOU 3760  CG  ASP C 290     6490   6498   4488    534  -1016   -267       C  
ATOM   3761  OD1 ASP C 290      12.649 -13.026  29.101  1.00 45.82           O  
ANISOU 3761  OD1 ASP C 290     6471   6483   4457    503  -1011   -255       O  
ATOM   3762  OD2 ASP C 290      12.916 -10.839  29.479  1.00 46.50           O  
ANISOU 3762  OD2 ASP C 290     6547   6559   4563    541  -1024   -277       O  
ATOM   3763  N   HIS C 291      15.464 -14.396  33.040  1.00 45.32           N  
ANISOU 3763  N   HIS C 291     6428   6412   4379    604   -994   -263       N  
ATOM   3764  CA  HIS C 291      16.702 -14.770  33.682  1.00 45.24           C  
ANISOU 3764  CA  HIS C 291     6427   6392   4372    627   -990   -266       C  
ATOM   3765  C   HIS C 291      16.383 -15.628  34.879  1.00 45.34           C  
ANISOU 3765  C   HIS C 291     6442   6420   4367    641   -982   -259       C  
ATOM   3766  O   HIS C 291      15.499 -15.296  35.655  1.00 45.58           O  
ANISOU 3766  O   HIS C 291     6464   6465   4388    653   -983   -260       O  
ATOM   3767  CB  HIS C 291      17.483 -13.547  34.146  1.00 45.38           C  
ANISOU 3767  CB  HIS C 291     6442   6398   4404    660   -996   -282       C  
ATOM   3768  CG  HIS C 291      17.915 -12.639  33.050  1.00 45.38           C  
ANISOU 3768  CG  HIS C 291     6439   6381   4421    651  -1004   -290       C  
ATOM   3769  ND1 HIS C 291      17.034 -11.837  32.360  1.00 45.59           N  
ANISOU 3769  ND1 HIS C 291     6457   6411   4453    636  -1010   -292       N  
ATOM   3770  CD2 HIS C 291      19.137 -12.391  32.532  1.00 45.24           C  
ANISOU 3770  CD2 HIS C 291     6428   6344   4419    655  -1006   -296       C  
ATOM   3771  CE1 HIS C 291      17.696 -11.142  31.452  1.00 45.60           C  
ANISOU 3771  CE1 HIS C 291     6460   6395   4471    631  -1016   -299       C  
ATOM   3772  NE2 HIS C 291      18.976 -11.459  31.536  1.00 45.39           N  
ANISOU 3772  NE2 HIS C 291     6442   6354   4452    642  -1013   -302       N  
ATOM   3773  N   LEU C 292      17.128 -16.710  35.042  1.00 45.08           N  
ANISOU 3773  N   LEU C 292     6418   6382   4328    639   -975   -253       N  
ATOM   3774  CA  LEU C 292      16.964 -17.558  36.201  1.00 45.27           C  
ANISOU 3774  CA  LEU C 292     6446   6419   4335    654   -967   -246       C  
ATOM   3775  C   LEU C 292      17.007 -16.663  37.437  1.00 45.59           C  
ANISOU 3775  C   LEU C 292     6480   6464   4377    693   -970   -258       C  
ATOM   3776  O   LEU C 292      17.773 -15.711  37.485  1.00 45.62           O  
ANISOU 3776  O   LEU C 292     6482   6456   4395    714   -975   -270       O  
ATOM   3777  CB  LEU C 292      18.056 -18.635  36.220  1.00 45.20           C  
ANISOU 3777  CB  LEU C 292     6449   6399   4325    653   -960   -241       C  
ATOM   3778  CG  LEU C 292      17.998 -19.622  37.377  1.00 45.45           C  
ANISOU 3778  CG  LEU C 292     6486   6443   4340    667   -952   -233       C  
ATOM   3779  CD1 LEU C 292      16.638 -20.241  37.372  1.00 45.80           C  
ANISOU 3779  CD1 LEU C 292     6527   6507   4368    645   -948   -221       C  
ATOM   3780  CD2 LEU C 292      19.048 -20.712  37.273  1.00 45.26           C  
ANISOU 3780  CD2 LEU C 292     6474   6407   4314    664   -944   -227       C  
ATOM   3781  N   LYS C 293      16.149 -16.896  38.410  1.00 41.23           N  
ANISOU 3781  N   LYS C 293     5924   5931   3810    704   -967   -253       N  
ATOM   3782  CA  LYS C 293      16.257 -16.105  39.628  1.00 41.60           C  
ANISOU 3782  CA  LYS C 293     5965   5984   3857    743   -968   -264       C  
ATOM   3783  C   LYS C 293      16.185 -17.060  40.787  1.00 41.94           C  
ANISOU 3783  C   LYS C 293     6012   6039   3883    758   -960   -257       C  
ATOM   3784  O   LYS C 293      16.039 -18.264  40.579  1.00 41.85           O  
ANISOU 3784  O   LYS C 293     6008   6031   3861    737   -953   -244       O  
ATOM   3785  CB  LYS C 293      15.158 -15.046  39.740  1.00 41.79           C  
ANISOU 3785  CB  LYS C 293     5978   6020   3882    747   -975   -270       C  
ATOM   3786  CG  LYS C 293      14.830 -14.291  38.453  1.00 41.51           C  
ANISOU 3786  CG  LYS C 293     5937   5976   3859    723   -983   -273       C  
ATOM   3787  CD  LYS C 293      14.001 -13.037  38.769  1.00 41.77           C  
ANISOU 3787  CD  LYS C 293     5958   6018   3895    737   -990   -283       C  
ATOM   3788  CE  LYS C 293      12.559 -13.035  38.180  1.00 41.77           C  
ANISOU 3788  CE  LYS C 293     5951   6033   3888    709   -992   -275       C  
ATOM   3789  NZ  LYS C 293      11.643 -12.301  39.127  1.00 42.51           N  
ANISOU 3789  NZ  LYS C 293     6034   6143   3975    731   -995   -281       N  
ATOM   3790  N   TYR C 294      16.267 -16.534  42.000  1.00 37.83           N  
ANISOU 3790  N   TYR C 294     5487   5526   3360    793   -959   -265       N  
ATOM   3791  CA  TYR C 294      16.288 -17.393  43.157  1.00 37.95           C  
ANISOU 3791  CA  TYR C 294     5507   5553   3360    810   -951   -259       C  
ATOM   3792  C   TYR C 294      15.829 -16.619  44.360  1.00 38.10           C  
ANISOU 3792  C   TYR C 294     5517   5586   3375    843   -952   -267       C  
ATOM   3793  O   TYR C 294      15.858 -15.425  44.336  1.00 38.10           O  
ANISOU 3793  O   TYR C 294     5509   5582   3386    857   -959   -280       O  
ATOM   3794  CB  TYR C 294      17.694 -17.984  43.361  1.00 37.89           C  
ANISOU 3794  CB  TYR C 294     5510   5531   3357    822   -946   -260       C  
ATOM   3795  CG  TYR C 294      18.726 -17.123  44.072  1.00 37.92           C  
ANISOU 3795  CG  TYR C 294     5512   5524   3370    860   -949   -275       C  
ATOM   3796  CD1 TYR C 294      18.781 -17.061  45.472  1.00 38.06           C  
ANISOU 3796  CD1 TYR C 294     5528   5554   3380    894   -945   -279       C  
ATOM   3797  CD2 TYR C 294      19.670 -16.415  43.350  1.00 37.79           C  
ANISOU 3797  CD2 TYR C 294     5497   5488   3372    861   -955   -285       C  
ATOM   3798  CE1 TYR C 294      19.713 -16.277  46.134  1.00 38.09           C  
ANISOU 3798  CE1 TYR C 294     5530   5549   3393    928   -948   -293       C  
ATOM   3799  CE2 TYR C 294      20.640 -15.632  44.002  1.00 37.81           C  
ANISOU 3799  CE2 TYR C 294     5499   5482   3385    895   -958   -299       C  
ATOM   3800  CZ  TYR C 294      20.652 -15.565  45.400  1.00 37.96           C  
ANISOU 3800  CZ  TYR C 294     5515   5512   3395    928   -954   -303       C  
ATOM   3801  OH  TYR C 294      21.620 -14.810  46.045  1.00 38.25           O  
ANISOU 3801  OH  TYR C 294     5552   5541   3441    962   -956   -317       O  
ATOM   3802  N   VAL C 295      15.408 -17.282  45.419  1.00 38.60           N  
ANISOU 3802  N   VAL C 295     5580   5664   3421    856   -945   -261       N  
ATOM   3803  CA  VAL C 295      14.889 -16.568  46.565  1.00 38.75           C  
ANISOU 3803  CA  VAL C 295     5590   5699   3436    886   -946   -268       C  
ATOM   3804  C   VAL C 295      15.192 -17.471  47.724  1.00 38.86           C  
ANISOU 3804  C   VAL C 295     5609   5721   3436    906   -937   -262       C  
ATOM   3805  O   VAL C 295      15.245 -18.682  47.555  1.00 38.84           O  
ANISOU 3805  O   VAL C 295     5616   5719   3424    888   -930   -249       O  
ATOM   3806  CB  VAL C 295      13.299 -16.210  46.422  1.00 38.83           C  
ANISOU 3806  CB  VAL C 295     5589   5726   3438    871   -949   -264       C  
ATOM   3807  CG1 VAL C 295      12.429 -17.367  45.852  1.00 38.82           C  
ANISOU 3807  CG1 VAL C 295     5592   5734   3423    835   -945   -247       C  
ATOM   3808  CG2 VAL C 295      12.705 -15.681  47.715  1.00 39.00           C  
ANISOU 3808  CG2 VAL C 295     5602   5766   3451    903   -948   -270       C  
ATOM   3809  N   MET C 296      15.462 -16.892  48.883  1.00 41.00           N  
ANISOU 3809  N   MET C 296     5875   5997   3706    943   -936   -272       N  
ATOM   3810  CA  MET C 296      15.588 -17.648  50.125  1.00 41.72           C  
ANISOU 3810  CA  MET C 296     5969   6099   3782    965   -927   -267       C  
ATOM   3811  C   MET C 296      14.218 -17.688  50.787  1.00 42.33           C  
ANISOU 3811  C   MET C 296     6039   6201   3845    967   -925   -261       C  
ATOM   3812  O   MET C 296      13.500 -16.677  50.757  1.00 42.56           O  
ANISOU 3812  O   MET C 296     6057   6236   3877    971   -931   -269       O  
ATOM   3813  CB  MET C 296      16.642 -17.012  51.036  1.00 42.20           C  
ANISOU 3813  CB  MET C 296     6030   6154   3850   1005   -928   -281       C  
ATOM   3814  CG  MET C 296      18.040 -17.124  50.459  1.00 41.68           C  
ANISOU 3814  CG  MET C 296     5973   6065   3797   1004   -929   -285       C  
ATOM   3815  SD  MET C 296      19.171 -15.734  50.613  1.00 42.02           S  
ANISOU 3815  SD  MET C 296     6013   6093   3860   1035   -936   -306       S  
ATOM   3816  CE  MET C 296      18.795 -15.273  52.293  1.00 43.16           C  
ANISOU 3816  CE  MET C 296     6149   6257   3993   1076   -933   -313       C  
ATOM   3817  N   LEU C 297      13.816 -18.844  51.327  1.00 42.58           N  
ANISOU 3817  N   LEU C 297     6075   6244   3858    962   -916   -248       N  
ATOM   3818  CA  LEU C 297      12.526 -18.964  52.031  1.00 43.28           C  
ANISOU 3818  CA  LEU C 297     6156   6356   3931    964   -914   -242       C  
ATOM   3819  C   LEU C 297      12.737 -19.799  53.262  1.00 44.11           C  
ANISOU 3819  C   LEU C 297     6266   6471   4022    986   -904   -235       C  
ATOM   3820  O   LEU C 297      13.477 -20.768  53.202  1.00 43.99           O  
ANISOU 3820  O   LEU C 297     6262   6448   4004    980   -898   -228       O  
ATOM   3821  CB  LEU C 297      11.475 -19.611  51.139  1.00 42.91           C  
ANISOU 3821  CB  LEU C 297     6111   6315   3877    924   -913   -228       C  
ATOM   3822  CG  LEU C 297      11.536 -19.159  49.674  1.00 41.96           C  
ANISOU 3822  CG  LEU C 297     5990   6180   3771    895   -921   -230       C  
ATOM   3823  CD1 LEU C 297      11.098 -20.249  48.730  1.00 41.42           C  
ANISOU 3823  CD1 LEU C 297     5929   6111   3696    854   -918   -215       C  
ATOM   3824  CD2 LEU C 297      10.693 -17.933  49.478  1.00 42.08           C  
ANISOU 3824  CD2 LEU C 297     5993   6202   3793    897   -930   -240       C  
ATOM   3825  N   PRO C 298      12.109 -19.456  54.391  1.00 44.59           N  
ANISOU 3825  N   PRO C 298     6319   6551   4074   1011   -902   -238       N  
ATOM   3826  CA  PRO C 298      12.242 -20.364  55.542  1.00 45.46           C  
ANISOU 3826  CA  PRO C 298     6434   6672   4168   1029   -892   -230       C  
ATOM   3827  C   PRO C 298      11.370 -21.617  55.341  1.00 45.54           C  
ANISOU 3827  C   PRO C 298     6450   6693   4162   1000   -885   -211       C  
ATOM   3828  O   PRO C 298      10.493 -21.605  54.455  1.00 45.10           O  
ANISOU 3828  O   PRO C 298     6391   6640   4106    969   -889   -206       O  
ATOM   3829  CB  PRO C 298      11.754 -19.516  56.711  1.00 46.46           C  
ANISOU 3829  CB  PRO C 298     6548   6814   4289   1063   -892   -240       C  
ATOM   3830  CG  PRO C 298      10.804 -18.615  56.107  1.00 46.14           C  
ANISOU 3830  CG  PRO C 298     6498   6779   4255   1050   -900   -245       C  
ATOM   3831  CD  PRO C 298      11.198 -18.355  54.675  1.00 44.99           C  
ANISOU 3831  CD  PRO C 298     6355   6613   4125   1022   -907   -247       C  
ATOM   3832  N   VAL C 299      11.604 -22.702  56.073  1.00 49.50           N  
ANISOU 3832  N   VAL C 299     6959   7200   4650   1006   -876   -201       N  
ATOM   3833  CA  VAL C 299      10.645 -23.804  55.933  1.00 49.74           C  
ANISOU 3833  CA  VAL C 299     6994   7242   4664    979   -870   -183       C  
ATOM   3834  C   VAL C 299       9.630 -23.579  57.037  1.00 50.84           C  
ANISOU 3834  C   VAL C 299     7123   7404   4789    999   -867   -182       C  
ATOM   3835  O   VAL C 299      10.006 -23.113  58.125  1.00 51.63           O  
ANISOU 3835  O   VAL C 299     7219   7510   4889   1035   -865   -191       O  
ATOM   3836  CB  VAL C 299      11.267 -25.246  56.026  1.00 49.91           C  
ANISOU 3836  CB  VAL C 299     7030   7258   4676    970   -860   -169       C  
ATOM   3837  CG1 VAL C 299      12.789 -25.243  55.886  1.00 49.45           C  
ANISOU 3837  CG1 VAL C 299     6980   7179   4630    983   -861   -177       C  
ATOM   3838  CG2 VAL C 299      10.813 -25.942  57.282  1.00 51.19           C  
ANISOU 3838  CG2 VAL C 299     7192   7438   4818    987   -851   -161       C  
ATOM   3839  N   ALA C 300       8.363 -23.897  56.759  1.00 49.82           N  
ANISOU 3839  N   ALA C 300     6991   7288   4649    975   -867   -172       N  
ATOM   3840  CA  ALA C 300       7.254 -23.470  57.604  1.00 50.77           C  
ANISOU 3840  CA  ALA C 300     7100   7431   4759    990   -866   -173       C  
ATOM   3841  C   ALA C 300       6.638 -24.598  58.410  1.00 51.76           C  
ANISOU 3841  C   ALA C 300     7229   7573   4863    989   -856   -157       C  
ATOM   3842  O   ALA C 300       6.652 -25.762  57.988  1.00 51.57           O  
ANISOU 3842  O   ALA C 300     7217   7546   4832    963   -850   -143       O  
ATOM   3843  CB  ALA C 300       6.201 -22.826  56.770  1.00 50.31           C  
ANISOU 3843  CB  ALA C 300     7034   7378   4705    967   -874   -174       C  
ATOM   3844  N   ASP C 301       6.102 -24.237  59.576  1.00 53.77           N  
ANISOU 3844  N   ASP C 301     7475   7846   5109   1017   -853   -161       N  
ATOM   3845  CA  ASP C 301       5.492 -25.199  60.481  1.00 54.94           C  
ANISOU 3845  CA  ASP C 301     7626   8012   5237   1020   -843   -147       C  
ATOM   3846  C   ASP C 301       4.403 -25.943  59.757  1.00 54.86           C  
ANISOU 3846  C   ASP C 301     7619   8008   5216    981   -842   -132       C  
ATOM   3847  O   ASP C 301       3.524 -25.314  59.181  1.00 54.56           O  
ANISOU 3847  O   ASP C 301     7574   7976   5182    967   -849   -135       O  
ATOM   3848  CB  ASP C 301       4.935 -24.490  61.706  1.00 56.15           C  
ANISOU 3848  CB  ASP C 301     7767   8185   5384   1054   -843   -154       C  
ATOM   3849  CG  ASP C 301       4.090 -25.399  62.572  1.00 57.49           C  
ANISOU 3849  CG  ASP C 301     7938   8374   5532   1055   -833   -140       C  
ATOM   3850  OD1 ASP C 301       2.904 -25.620  62.232  1.00 57.67           O  
ANISOU 3850  OD1 ASP C 301     7958   8409   5546   1032   -833   -131       O  
ATOM   3851  OD2 ASP C 301       4.606 -25.884  63.606  1.00 58.45           O  
ANISOU 3851  OD2 ASP C 301     8063   8500   5645   1079   -825   -137       O  
ATOM   3852  N   GLN C 302       4.456 -27.278  59.785  1.00 54.95           N  
ANISOU 3852  N   GLN C 302     7643   8020   5215    965   -834   -116       N  
ATOM   3853  CA  GLN C 302       3.534 -28.104  58.986  1.00 54.82           C  
ANISOU 3853  CA  GLN C 302     7633   8008   5190    925   -832   -101       C  
ATOM   3854  C   GLN C 302       2.045 -27.944  59.372  1.00 55.82           C  
ANISOU 3854  C   GLN C 302     7749   8156   5303    921   -832    -96       C  
ATOM   3855  O   GLN C 302       1.186 -27.980  58.503  1.00 55.54           O  
ANISOU 3855  O   GLN C 302     7713   8124   5266    890   -836    -91       O  
ATOM   3856  CB  GLN C 302       3.923 -29.581  59.056  1.00 55.05           C  
ANISOU 3856  CB  GLN C 302     7678   8033   5207    911   -822    -85       C  
ATOM   3857  CG  GLN C 302       4.532 -30.134  57.762  1.00 53.79           C  
ANISOU 3857  CG  GLN C 302     7529   7853   5055    878   -824    -81       C  
ATOM   3858  CD  GLN C 302       3.539 -30.290  56.593  1.00 53.60           C  
ANISOU 3858  CD  GLN C 302     7506   7831   5030    836   -828    -74       C  
ATOM   3859  OE1 GLN C 302       2.401 -29.820  56.658  1.00 54.49           O  
ANISOU 3859  OE1 GLN C 302     7608   7957   5137    832   -832    -74       O  
ATOM   3860  NE2 GLN C 302       3.974 -30.952  55.516  1.00 52.52           N  
ANISOU 3860  NE2 GLN C 302     7380   7678   4897    805   -828    -67       N  
ATOM   3861  N   ASP C 303       1.734 -27.743  60.647  1.00 55.26           N  
ANISOU 3861  N   ASP C 303     7671   8102   5222    952   -828    -98       N  
ATOM   3862  CA  ASP C 303       0.337 -27.538  61.045  1.00 56.24           C  
ANISOU 3862  CA  ASP C 303     7786   8249   5335    951   -828    -94       C  
ATOM   3863  C   ASP C 303      -0.237 -26.173  60.604  1.00 55.79           C  
ANISOU 3863  C   ASP C 303     7714   8194   5289    952   -838   -108       C  
ATOM   3864  O   ASP C 303      -1.337 -26.137  60.044  1.00 55.87           O  
ANISOU 3864  O   ASP C 303     7721   8213   5295    928   -842   -103       O  
ATOM   3865  CB  ASP C 303       0.197 -27.718  62.561  1.00 57.80           C  
ANISOU 3865  CB  ASP C 303     7980   8464   5519    985   -819    -93       C  
ATOM   3866  CG  ASP C 303       0.248 -29.200  62.986  1.00 58.68           C  
ANISOU 3866  CG  ASP C 303     8104   8578   5613    976   -808    -75       C  
ATOM   3867  OD1 ASP C 303       0.567 -30.066  62.123  1.00 58.03           O  
ANISOU 3867  OD1 ASP C 303     8035   8482   5530    946   -806    -65       O  
ATOM   3868  OD2 ASP C 303      -0.025 -29.493  64.180  1.00 60.09           O  
ANISOU 3868  OD2 ASP C 303     8281   8773   5778    999   -800    -71       O  
ATOM   3869  N   GLN C 304       0.505 -25.079  60.844  1.00 56.24           N  
ANISOU 3869  N   GLN C 304     7764   8244   5361    981   -844   -125       N  
ATOM   3870  CA  GLN C 304       0.136 -23.732  60.375  1.00 55.79           C  
ANISOU 3870  CA  GLN C 304     7694   8187   5318    984   -854   -139       C  
ATOM   3871  C   GLN C 304      -0.164 -23.742  58.890  1.00 54.58           C  
ANISOU 3871  C   GLN C 304     7544   8021   5172    944   -861   -136       C  
ATOM   3872  O   GLN C 304      -1.090 -23.076  58.417  1.00 54.53           O  
ANISOU 3872  O   GLN C 304     7529   8022   5168    932   -868   -139       O  
ATOM   3873  CB  GLN C 304       1.246 -22.715  60.633  1.00 55.43           C  
ANISOU 3873  CB  GLN C 304     7644   8129   5288   1015   -859   -157       C  
ATOM   3874  CG  GLN C 304       1.490 -22.354  62.100  1.00 56.29           C  
ANISOU 3874  CG  GLN C 304     7746   8249   5391   1058   -854   -165       C  
ATOM   3875  CD  GLN C 304       0.446 -21.358  62.678  1.00 56.78           C  
ANISOU 3875  CD  GLN C 304     7792   8330   5450   1076   -858   -173       C  
ATOM   3876  OE1 GLN C 304      -0.756 -21.381  62.312  1.00 56.54           O  
ANISOU 3876  OE1 GLN C 304     7757   8313   5414   1055   -860   -166       O  
ATOM   3877  NE2 GLN C 304       0.910 -20.479  63.595  1.00 57.52           N  
ANISOU 3877  NE2 GLN C 304     7878   8428   5549   1115   -859   -187       N  
ATOM   3878  N   CYS C 305       0.627 -24.507  58.158  1.00 51.02           N  
ANISOU 3878  N   CYS C 305     7107   7554   4726    923   -860   -130       N  
ATOM   3879  CA  CYS C 305       0.470 -24.614  56.727  1.00 49.93           C  
ANISOU 3879  CA  CYS C 305     6973   7403   4595    884   -865   -126       C  
ATOM   3880  C   CYS C 305      -0.794 -25.374  56.376  1.00 50.43           C  
ANISOU 3880  C   CYS C 305     7039   7480   4644    852   -863   -111       C  
ATOM   3881  O   CYS C 305      -1.476 -25.056  55.392  1.00 49.95           O  
ANISOU 3881  O   CYS C 305     6975   7417   4587    825   -869   -110       O  
ATOM   3882  CB  CYS C 305       1.688 -25.315  56.118  1.00 49.01           C  
ANISOU 3882  CB  CYS C 305     6871   7266   4486    872   -863   -123       C  
ATOM   3883  SG  CYS C 305       1.597 -25.487  54.336  1.00 47.77           S  
ANISOU 3883  SG  CYS C 305     6720   7093   4339    824   -870   -119       S  
ATOM   3884  N   ILE C 306      -1.076 -26.409  57.161  1.00 50.86           N  
ANISOU 3884  N   ILE C 306     7099   7545   4680    855   -853    -98       N  
ATOM   3885  CA  ILE C 306      -2.225 -27.253  56.900  1.00 51.45           C  
ANISOU 3885  CA  ILE C 306     7178   7632   4739    825   -849    -83       C  
ATOM   3886  C   ILE C 306      -3.459 -26.418  57.167  1.00 52.17           C  
ANISOU 3886  C   ILE C 306     7254   7741   4826    831   -854    -87       C  
ATOM   3887  O   ILE C 306      -4.305 -26.216  56.275  1.00 51.91           O  
ANISOU 3887  O   ILE C 306     7218   7709   4795    803   -860    -85       O  
ATOM   3888  CB  ILE C 306      -2.229 -28.545  57.769  1.00 52.56           C  
ANISOU 3888  CB  ILE C 306     7328   7781   4860    828   -837    -68       C  
ATOM   3889  CG1 ILE C 306      -1.163 -29.528  57.287  1.00 51.88           C  
ANISOU 3889  CG1 ILE C 306     7258   7677   4776    814   -832    -61       C  
ATOM   3890  CG2 ILE C 306      -3.593 -29.239  57.735  1.00 53.45           C  
ANISOU 3890  CG2 ILE C 306     7442   7910   4955    804   -833    -53       C  
ATOM   3891  CD1 ILE C 306      -1.089 -29.636  55.815  1.00 50.74           C  
ANISOU 3891  CD1 ILE C 306     7120   7518   4642    776   -838    -59       C  
ATOM   3892  N   ARG C 307      -3.527 -25.882  58.381  1.00 53.52           N  
ANISOU 3892  N   ARG C 307     7415   7925   4994    868   -852    -94       N  
ATOM   3893  CA  ARG C 307      -4.635 -25.039  58.767  1.00 54.27           C  
ANISOU 3893  CA  ARG C 307     7496   8038   5085    879   -856   -100       C  
ATOM   3894  C   ARG C 307      -4.851 -23.906  57.776  1.00 53.30           C  
ANISOU 3894  C   ARG C 307     7365   7908   4979    868   -867   -111       C  
ATOM   3895  O   ARG C 307      -5.953 -23.405  57.629  1.00 53.75           O  
ANISOU 3895  O   ARG C 307     7412   7977   5034    861   -872   -112       O  
ATOM   3896  CB  ARG C 307      -4.408 -24.480  60.157  1.00 55.25           C  
ANISOU 3896  CB  ARG C 307     7611   8175   5208    924   -852   -109       C  
ATOM   3897  CG  ARG C 307      -4.634 -25.484  61.234  1.00 56.31           C  
ANISOU 3897  CG  ARG C 307     7750   8323   5323    934   -841    -97       C  
ATOM   3898  CD  ARG C 307      -4.542 -24.842  62.598  1.00 57.68           C  
ANISOU 3898  CD  ARG C 307     7913   8510   5493    979   -838   -106       C  
ATOM   3899  NE  ARG C 307      -3.702 -25.647  63.472  1.00 58.65           N  
ANISOU 3899  NE  ARG C 307     8045   8632   5609    997   -829   -101       N  
ATOM   3900  CZ  ARG C 307      -2.417 -25.389  63.710  1.00 59.05           C  
ANISOU 3900  CZ  ARG C 307     8099   8668   5671   1019   -829   -110       C  
ATOM   3901  NH1 ARG C 307      -1.844 -24.325  63.151  1.00 58.63           N  
ANISOU 3901  NH1 ARG C 307     8039   8601   5635   1025   -838   -126       N  
ATOM   3902  NH2 ARG C 307      -1.709 -26.186  64.516  1.00 60.00           N  
ANISOU 3902  NH2 ARG C 307     8227   8788   5783   1035   -820   -104       N  
ATOM   3903  N   HIS C 308      -3.805 -23.499  57.092  1.00 50.63           N  
ANISOU 3903  N   HIS C 308     7030   7549   4658    866   -873   -120       N  
ATOM   3904  CA  HIS C 308      -3.961 -22.480  56.086  1.00 49.82           C  
ANISOU 3904  CA  HIS C 308     6921   7438   4572    854   -884   -130       C  
ATOM   3905  C   HIS C 308      -4.711 -23.012  54.884  1.00 49.23           C  
ANISOU 3905  C   HIS C 308     6851   7360   4493    809   -886   -119       C  
ATOM   3906  O   HIS C 308      -5.679 -22.428  54.483  1.00 48.97           O  
ANISOU 3906  O   HIS C 308     6810   7336   4462    798   -892   -121       O  
ATOM   3907  CB  HIS C 308      -2.587 -21.919  55.658  1.00 48.73           C  
ANISOU 3907  CB  HIS C 308     6785   7278   4452    864   -888   -143       C  
ATOM   3908  CG  HIS C 308      -2.663 -20.708  54.769  1.00 47.90           C  
ANISOU 3908  CG  HIS C 308     6671   7163   4364    858   -899   -155       C  
ATOM   3909  ND1 HIS C 308      -2.564 -20.785  53.396  1.00 46.80           N  
ANISOU 3909  ND1 HIS C 308     6537   7009   4234    824   -905   -153       N  
ATOM   3910  CD2 HIS C 308      -2.821 -19.397  55.059  1.00 48.10           C  
ANISOU 3910  CD2 HIS C 308     6684   7193   4399    882   -906   -171       C  
ATOM   3911  CE1 HIS C 308      -2.664 -19.577  52.876  1.00 46.37           C  
ANISOU 3911  CE1 HIS C 308     6473   6950   4194    827   -914   -166       C  
ATOM   3912  NE2 HIS C 308      -2.829 -18.719  53.864  1.00 47.12           N  
ANISOU 3912  NE2 HIS C 308     6558   7057   4290    862   -915   -177       N  
ATOM   3913  N   TYR C 309      -4.271 -24.113  54.310  1.00 50.71           N  
ANISOU 3913  N   TYR C 309     7053   7538   4678    783   -882   -108       N  
ATOM   3914  CA  TYR C 309      -4.807 -24.567  53.019  1.00 50.10           C  
ANISOU 3914  CA  TYR C 309     6982   7454   4600    739   -885    -98       C  
ATOM   3915  C   TYR C 309      -6.148 -25.362  53.027  1.00 51.10           C  
ANISOU 3915  C   TYR C 309     7110   7597   4708    714   -881    -83       C  
ATOM   3916  O   TYR C 309      -6.990 -25.292  52.109  1.00 50.97           O  
ANISOU 3916  O   TYR C 309     7092   7582   4691    684   -886    -79       O  
ATOM   3917  CB  TYR C 309      -3.733 -25.413  52.355  1.00 49.15           C  
ANISOU 3917  CB  TYR C 309     6876   7315   4484    721   -882    -93       C  
ATOM   3918  CG  TYR C 309      -2.783 -24.597  51.558  1.00 47.92           C  
ANISOU 3918  CG  TYR C 309     6719   7140   4350    722   -890   -105       C  
ATOM   3919  CD1 TYR C 309      -3.149 -24.110  50.303  1.00 47.31           C  
ANISOU 3919  CD1 TYR C 309     6638   7055   4282    694   -898   -108       C  
ATOM   3920  CD2 TYR C 309      -1.527 -24.289  52.050  1.00 47.48           C  
ANISOU 3920  CD2 TYR C 309     6664   7073   4304    752   -889   -115       C  
ATOM   3921  CE1 TYR C 309      -2.271 -23.376  49.542  1.00 46.25           C  
ANISOU 3921  CE1 TYR C 309     6503   6902   4167    694   -905   -119       C  
ATOM   3922  CE2 TYR C 309      -0.650 -23.535  51.304  1.00 46.43           C  
ANISOU 3922  CE2 TYR C 309     6530   6921   4190    752   -896   -127       C  
ATOM   3923  CZ  TYR C 309      -1.034 -23.091  50.054  1.00 45.82           C  
ANISOU 3923  CZ  TYR C 309     6451   6837   4123    723   -904   -129       C  
ATOM   3924  OH  TYR C 309      -0.175 -22.357  49.307  1.00 44.88           O  
ANISOU 3924  OH  TYR C 309     6330   6700   4022    724   -911   -140       O  
ATOM   3925  N   GLU C 310      -6.263 -26.188  54.048  1.00 51.54           N  
ANISOU 3925  N   GLU C 310     7170   7664   4747    727   -871    -74       N  
ATOM   3926  CA  GLU C 310      -7.473 -26.893  54.387  1.00 52.84           C  
ANISOU 3926  CA  GLU C 310     7336   7847   4893    714   -866    -61       C  
ATOM   3927  C   GLU C 310      -7.756 -26.233  55.712  1.00 53.94           C  
ANISOU 3927  C   GLU C 310     7464   8004   5028    754   -864    -69       C  
ATOM   3928  O   GLU C 310      -7.062 -25.274  56.044  1.00 53.51           O  
ANISOU 3928  O   GLU C 310     7401   7945   4987    783   -868    -83       O  
ATOM   3929  CB  GLU C 310      -7.207 -28.374  54.447  1.00 53.05           C  
ANISOU 3929  CB  GLU C 310     7379   7871   4906    696   -856    -45       C  
ATOM   3930  CG  GLU C 310      -6.325 -28.771  53.228  1.00 51.65           C  
ANISOU 3930  CG  GLU C 310     7213   7671   4740    668   -859    -43       C  
ATOM   3931  CD  GLU C 310      -5.401 -29.963  53.461  1.00 51.57           C  
ANISOU 3931  CD  GLU C 310     7219   7652   4724    667   -849    -34       C  
ATOM   3932  OE1 GLU C 310      -5.059 -30.244  54.630  1.00 52.39           O  
ANISOU 3932  OE1 GLU C 310     7323   7763   4820    696   -842    -33       O  
ATOM   3933  OE2 GLU C 310      -5.019 -30.603  52.455  1.00 50.74           O  
ANISOU 3933  OE2 GLU C 310     7125   7533   4622    636   -849    -28       O  
ATOM   3934  N   GLY C 311      -8.749 -26.633  56.475  1.00 52.85           N  
ANISOU 3934  N   GLY C 311     7322   7885   4872    758   -859    -60       N  
ATOM   3935  CA  GLY C 311      -9.016 -25.776  57.618  1.00 53.97           C  
ANISOU 3935  CA  GLY C 311     7450   8044   5014    797   -859    -70       C  
ATOM   3936  C   GLY C 311      -8.439 -26.323  58.889  1.00 54.32           C  
ANISOU 3936  C   GLY C 311     7498   8094   5049    827   -849    -67       C  
ATOM   3937  O   GLY C 311      -8.456 -25.676  59.941  1.00 54.85           O  
ANISOU 3937  O   GLY C 311     7554   8173   5115    862   -848    -76       O  
ATOM   3938  N   SER C 312      -7.851 -27.503  58.742  1.00 61.37           N  
ANISOU 3938  N   SER C 312     8405   8977   5934    811   -842    -56       N  
ATOM   3939  CA  SER C 312      -8.038 -28.573  59.718  1.00 62.41           C  
ANISOU 3939  CA  SER C 312     8544   9121   6047    819   -830    -43       C  
ATOM   3940  C   SER C 312      -6.967 -28.906  60.756  1.00 63.27           C  
ANISOU 3940  C   SER C 312     8657   9227   6154    851   -822    -44       C  
ATOM   3941  O   SER C 312      -7.114 -28.488  61.918  1.00 64.79           O  
ANISOU 3941  O   SER C 312     8841   9435   6342    885   -819    -49       O  
ATOM   3942  CB  SER C 312      -8.318 -29.863  58.949  1.00 61.51           C  
ANISOU 3942  CB  SER C 312     8446   9001   5923    778   -825    -25       C  
ATOM   3943  OG  SER C 312      -7.138 -30.336  58.294  1.00 61.21           O  
ANISOU 3943  OG  SER C 312     8421   8942   5895    766   -825    -25       O  
ATOM   3944  N   THR C 313      -5.865 -29.553  60.326  1.00 62.87           N  
ANISOU 3944  N   THR C 313     8620   9158   6109    842   -820    -41       N  
ATOM   3945  CA  THR C 313      -5.355 -30.778  60.991  1.00 63.35           C  
ANISOU 3945  CA  THR C 313     8694   9218   6157    846   -808    -28       C  
ATOM   3946  C   THR C 313      -6.433 -31.837  60.718  1.00 64.25           C  
ANISOU 3946  C   THR C 313     8816   9342   6254    813   -803    -11       C  
ATOM   3947  O   THR C 313      -6.482 -32.356  59.593  1.00 63.44           O  
ANISOU 3947  O   THR C 313     8724   9228   6153    777   -805     -4       O  
ATOM   3948  CB  THR C 313      -5.083 -30.647  62.516  1.00 64.62           C  
ANISOU 3948  CB  THR C 313     8848   9392   6311    889   -802    -32       C  
ATOM   3949  OG1 THR C 313      -4.310 -29.478  62.784  1.00 64.17           O  
ANISOU 3949  OG1 THR C 313     8782   9329   6270    920   -808    -50       O  
ATOM   3950  CG2 THR C 313      -4.309 -31.818  63.000  1.00 64.74           C  
ANISOU 3950  CG2 THR C 313     8878   9402   6317    893   -791    -21       C  
ATOM   3951  N   VAL C 314      -7.260 -32.177  61.721  1.00 66.91           N  
ANISOU 3951  N   VAL C 314     9150   9700   6574    825   -796     -3       N  
ATOM   3952  CA  VAL C 314      -8.277 -33.267  61.631  1.00 68.11           C  
ANISOU 3952  CA  VAL C 314     9310   9862   6706    797   -789     15       C  
ATOM   3953  C   VAL C 314      -9.177 -33.309  60.362  1.00 67.65           C  
ANISOU 3953  C   VAL C 314     9254   9801   6648    755   -795     20       C  
ATOM   3954  O   VAL C 314      -9.825 -32.322  60.000  1.00 67.34           O  
ANISOU 3954  O   VAL C 314     9203   9767   6617    754   -804     10       O  
ATOM   3955  CB  VAL C 314      -9.213 -33.204  62.861  1.00 70.03           C  
ANISOU 3955  CB  VAL C 314     9545  10130   6934    820   -783     18       C  
ATOM   3956  CG1 VAL C 314      -9.394 -31.756  63.320  1.00 70.01           C  
ANISOU 3956  CG1 VAL C 314     9522  10136   6941    851   -791      1       C  
ATOM   3957  CG2 VAL C 314     -10.548 -33.882  62.561  1.00 71.12           C  
ANISOU 3957  CG2 VAL C 314     9687  10280   7056    789   -780     32       C  
ATOM   3958  N   PRO C 315      -9.227 -34.477  59.695  1.00 68.56           N  
ANISOU 3958  N   PRO C 315     9386   9908   6756    720   -790     34       N  
ATOM   3959  CA  PRO C 315      -9.744 -34.591  58.322  1.00 67.87           C  
ANISOU 3959  CA  PRO C 315     9303   9812   6671    678   -797     37       C  
ATOM   3960  C   PRO C 315     -11.257 -34.366  58.174  1.00 68.95           C  
ANISOU 3960  C   PRO C 315     9434   9965   6799    663   -800     41       C  
ATOM   3961  O   PRO C 315     -11.766 -34.217  57.044  1.00 68.37           O  
ANISOU 3961  O   PRO C 315     9361   9885   6730    631   -807     42       O  
ATOM   3962  CB  PRO C 315      -9.367 -36.023  57.921  1.00 67.99           C  
ANISOU 3962  CB  PRO C 315     9339   9817   6677    651   -788     53       C  
ATOM   3963  CG  PRO C 315      -8.261 -36.390  58.846  1.00 68.16           C  
ANISOU 3963  CG  PRO C 315     9364   9834   6698    681   -781     52       C  
ATOM   3964  CD  PRO C 315      -8.611 -35.732  60.144  1.00 69.17           C  
ANISOU 3964  CD  PRO C 315     9478   9981   6821    720   -779     46       C  
ATOM   3965  N   GLU C 316     -11.984 -34.382  59.283  1.00 70.77           N  
ANISOU 3965  N   GLU C 316     9657  10216   7016    684   -794     44       N  
ATOM   3966  CA  GLU C 316     -13.428 -34.227  59.195  1.00 71.95           C  
ANISOU 3966  CA  GLU C 316     9800  10381   7155    670   -796     49       C  
ATOM   3967  C   GLU C 316     -13.802 -32.740  59.129  1.00 71.31           C  
ANISOU 3967  C   GLU C 316     9700  10307   7088    687   -807     32       C  
ATOM   3968  O   GLU C 316     -14.913 -32.374  58.716  1.00 71.67           O  
ANISOU 3968  O   GLU C 316     9739  10362   7131    671   -813     33       O  
ATOM   3969  CB  GLU C 316     -14.101 -34.931  60.378  1.00 73.96           C  
ANISOU 3969  CB  GLU C 316    10056  10656   7389    683   -785     60       C  
ATOM   3970  CG  GLU C 316     -13.242 -36.043  61.013  1.00 74.49           C  
ANISOU 3970  CG  GLU C 316    10137  10717   7447    691   -774     70       C  
ATOM   3971  CD  GLU C 316     -12.848 -37.147  60.017  1.00 74.22           C  
ANISOU 3971  CD  GLU C 316    10123  10666   7411    652   -771     81       C  
ATOM   3972  OE1 GLU C 316     -13.589 -37.324  59.013  1.00 74.31           O  
ANISOU 3972  OE1 GLU C 316    10140  10675   7421    617   -775     86       O  
ATOM   3973  OE2 GLU C 316     -11.801 -37.825  60.234  1.00 73.97           O  
ANISOU 3973  OE2 GLU C 316    10102  10623   7379    658   -764     85       O  
ATOM   3974  N   LYS C 317     -12.868 -31.896  59.564  1.00 67.47           N  
ANISOU 3974  N   LYS C 317     9204   9816   6615    719   -811     18       N  
ATOM   3975  CA  LYS C 317     -13.031 -30.448  59.537  1.00 66.90           C  
ANISOU 3975  CA  LYS C 317     9114   9747   6557    739   -821      2       C  
ATOM   3976  C   LYS C 317     -12.341 -29.813  58.319  1.00 64.94           C  
ANISOU 3976  C   LYS C 317     8867   9478   6330    724   -831     -8       C  
ATOM   3977  O   LYS C 317     -12.262 -28.585  58.184  1.00 64.37           O  
ANISOU 3977  O   LYS C 317     8781   9404   6272    739   -840    -23       O  
ATOM   3978  CB  LYS C 317     -12.514 -29.871  60.845  1.00 67.42           C  
ANISOU 3978  CB  LYS C 317     9170   9822   6625    786   -817     -8       C  
ATOM   3979  CG  LYS C 317     -12.912 -30.735  62.035  1.00 69.35           C  
ANISOU 3979  CG  LYS C 317     9418  10084   6848    799   -805      4       C  
ATOM   3980  CD  LYS C 317     -13.156 -29.894  63.267  1.00 70.11           C  
ANISOU 3980  CD  LYS C 317     9498  10199   6943    841   -804     -6       C  
ATOM   3981  CE  LYS C 317     -14.156 -30.568  64.192  1.00 72.22           C  
ANISOU 3981  CE  LYS C 317     9764  10488   7189    845   -795      7       C  
ATOM   3982  NZ  LYS C 317     -14.486 -29.720  65.380  1.00 73.09           N  
ANISOU 3982  NZ  LYS C 317     9857  10618   7297    885   -794     -3       N  
ATOM   3983  N   LYS C 318     -11.821 -30.670  57.445  1.00 62.90           N  
ANISOU 3983  N   LYS C 318     8625   9203   6073    694   -829      0       N  
ATOM   3984  CA  LYS C 318     -11.165 -30.235  56.211  1.00 61.13           C  
ANISOU 3984  CA  LYS C 318     8402   8957   5866    675   -838     -7       C  
ATOM   3985  C   LYS C 318     -12.148 -29.592  55.241  1.00 60.94           C  
ANISOU 3985  C   LYS C 318     8372   8936   5848    650   -848    -10       C  
ATOM   3986  O   LYS C 318     -13.202 -30.164  54.946  1.00 61.90           O  
ANISOU 3986  O   LYS C 318     8497   9066   5956    624   -846      1       O  
ATOM   3987  CB  LYS C 318     -10.460 -31.416  55.515  1.00 60.43           C  
ANISOU 3987  CB  LYS C 318     8332   8852   5775    646   -833      4       C  
ATOM   3988  CG  LYS C 318      -9.113 -31.818  56.117  1.00 60.12           C  
ANISOU 3988  CG  LYS C 318     8300   8803   5739    669   -827      3       C  
ATOM   3989  CD  LYS C 318      -8.114 -32.142  55.006  1.00 58.70           C  
ANISOU 3989  CD  LYS C 318     8132   8601   5572    646   -829      2       C  
ATOM   3990  CE  LYS C 318      -6.795 -32.692  55.548  1.00 58.47           C  
ANISOU 3990  CE  LYS C 318     8110   8561   5544    666   -822      3       C  
ATOM   3991  NZ  LYS C 318      -5.995 -31.653  56.244  1.00 58.02           N  
ANISOU 3991  NZ  LYS C 318     8043   8503   5500    707   -825    -13       N  
ATOM   3992  N   THR C 319     -11.785 -28.400  54.761  1.00 55.94           N  
ANISOU 3992  N   THR C 319     7728   8295   5233    659   -858    -25       N  
ATOM   3993  CA  THR C 319     -12.517 -27.670  53.711  1.00 55.65           C  
ANISOU 3993  CA  THR C 319     7684   8256   5204    636   -868    -30       C  
ATOM   3994  C   THR C 319     -11.516 -26.941  52.832  1.00 53.95           C  
ANISOU 3994  C   THR C 319     7468   8020   5011    634   -877    -42       C  
ATOM   3995  O   THR C 319     -10.428 -26.638  53.306  1.00 53.29           O  
ANISOU 3995  O   THR C 319     7383   7929   4936    661   -875    -50       O  
ATOM   3996  CB  THR C 319     -13.499 -26.662  54.299  1.00 56.64           C  
ANISOU 3996  CB  THR C 319     7793   8400   5329    657   -873    -38       C  
ATOM   3997  OG1 THR C 319     -12.872 -25.958  55.378  1.00 56.65           O  
ANISOU 3997  OG1 THR C 319     7784   8406   5335    701   -871    -50       O  
ATOM   3998  CG2 THR C 319     -14.709 -27.379  54.836  1.00 58.36           C  
ANISOU 3998  CG2 THR C 319     8012   8638   5526    649   -866    -25       C  
ATOM   3999  N   PRO C 320     -11.855 -26.671  51.562  1.00 49.89           N  
ANISOU 3999  N   PRO C 320     6954   7497   4505    602   -885    -43       N  
ATOM   4000  CA  PRO C 320     -10.897 -25.989  50.688  1.00 48.30           C  
ANISOU 4000  CA  PRO C 320     6752   7276   4323    599   -892    -53       C  
ATOM   4001  C   PRO C 320     -10.713 -24.486  50.970  1.00 47.92           C  
ANISOU 4001  C   PRO C 320     6688   7230   4291    631   -900    -72       C  
ATOM   4002  O   PRO C 320     -11.385 -23.668  50.341  1.00 47.86           O  
ANISOU 4002  O   PRO C 320     6671   7223   4290    621   -909    -77       O  
ATOM   4003  CB  PRO C 320     -11.480 -26.213  49.288  1.00 47.95           C  
ANISOU 4003  CB  PRO C 320     6713   7224   4281    555   -898    -47       C  
ATOM   4004  CG  PRO C 320     -12.225 -27.426  49.408  1.00 49.12           C  
ANISOU 4004  CG  PRO C 320     6872   7381   4410    532   -890    -31       C  
ATOM   4005  CD  PRO C 320     -12.869 -27.364  50.771  1.00 50.47           C  
ANISOU 4005  CD  PRO C 320     7036   7574   4568    562   -885    -30       C  
ATOM   4006  N   LYS C 321      -9.827 -24.138  51.904  1.00 48.40           N  
ANISOU 4006  N   LYS C 321     6745   7288   4356    668   -897    -80       N  
ATOM   4007  CA  LYS C 321      -9.575 -22.747  52.300  1.00 48.16           C  
ANISOU 4007  CA  LYS C 321     6700   7259   4339    701   -903    -98       C  
ATOM   4008  C   LYS C 321      -8.537 -22.010  51.438  1.00 46.66           C  
ANISOU 4008  C   LYS C 321     6510   7048   4170    700   -911   -110       C  
ATOM   4009  O   LYS C 321      -8.163 -20.874  51.743  1.00 46.43           O  
ANISOU 4009  O   LYS C 321     6471   7017   4154    728   -916   -125       O  
ATOM   4010  CB  LYS C 321      -9.115 -22.689  53.762  1.00 48.85           C  
ANISOU 4010  CB  LYS C 321     6783   7355   4421    743   -896   -102       C  
ATOM   4011  CG  LYS C 321      -9.860 -23.620  54.685  1.00 50.29           C  
ANISOU 4011  CG  LYS C 321     6968   7557   4582    746   -887    -89       C  
ATOM   4012  CD  LYS C 321     -11.226 -23.049  55.074  1.00 51.53           C  
ANISOU 4012  CD  LYS C 321     7113   7735   4731    752   -889    -91       C  
ATOM   4013  CE  LYS C 321     -11.090 -21.785  55.966  1.00 52.21           C  
ANISOU 4013  CE  LYS C 321     7183   7830   4825    794   -893   -107       C  
ATOM   4014  NZ  LYS C 321     -12.396 -21.031  56.133  1.00 53.27           N  
ANISOU 4014  NZ  LYS C 321     7303   7983   4955    798   -897   -111       N  
ATOM   4015  N   SER C 322      -8.046 -22.670  50.397  1.00 48.64           N  
ANISOU 4015  N   SER C 322     6773   7282   4425    668   -911   -103       N  
ATOM   4016  CA  SER C 322      -6.914 -22.152  49.621  1.00 47.23           C  
ANISOU 4016  CA  SER C 322     6597   7083   4267    667   -917   -113       C  
ATOM   4017  C   SER C 322      -7.184 -20.824  48.905  1.00 46.91           C  
ANISOU 4017  C   SER C 322     6544   7037   4241    666   -928   -125       C  
ATOM   4018  O   SER C 322      -8.032 -20.770  48.035  1.00 47.10           O  
ANISOU 4018  O   SER C 322     6567   7063   4265    637   -933   -121       O  
ATOM   4019  CB  SER C 322      -6.476 -23.195  48.580  1.00 46.39           C  
ANISOU 4019  CB  SER C 322     6505   6962   4160    630   -914   -101       C  
ATOM   4020  OG  SER C 322      -5.404 -22.727  47.786  1.00 45.67           O  
ANISOU 4020  OG  SER C 322     6416   6851   4087    627   -919   -110       O  
ATOM   4021  N   PRO C 323      -6.426 -19.764  49.254  1.00 47.23           N  
ANISOU 4021  N   PRO C 323     6577   7071   4296    697   -932   -141       N  
ATOM   4022  CA  PRO C 323      -6.450 -18.425  48.655  1.00 46.92           C  
ANISOU 4022  CA  PRO C 323     6529   7026   4274    702   -942   -155       C  
ATOM   4023  C   PRO C 323      -6.451 -18.334  47.132  1.00 46.02           C  
ANISOU 4023  C   PRO C 323     6418   6898   4171    665   -949   -153       C  
ATOM   4024  O   PRO C 323      -7.179 -17.467  46.611  1.00 46.22           O  
ANISOU 4024  O   PRO C 323     6434   6926   4202    657   -957   -159       O  
ATOM   4025  CB  PRO C 323      -5.196 -17.804  49.214  1.00 46.47           C  
ANISOU 4025  CB  PRO C 323     6470   6957   4229    736   -942   -169       C  
ATOM   4026  CG  PRO C 323      -5.184 -18.313  50.614  1.00 47.11           C  
ANISOU 4026  CG  PRO C 323     6552   7053   4296    764   -933   -165       C  
ATOM   4027  CD  PRO C 323      -5.734 -19.721  50.555  1.00 47.44           C  
ANISOU 4027  CD  PRO C 323     6603   7102   4320    737   -926   -147       C  
ATOM   4028  N   VAL C 324      -5.692 -19.155  46.417  1.00 44.19           N  
ANISOU 4028  N   VAL C 324     6199   6651   3942    642   -946   -146       N  
ATOM   4029  CA  VAL C 324      -5.919 -19.222  44.970  1.00 43.58           C  
ANISOU 4029  CA  VAL C 324     6125   6563   3871    602   -952   -142       C  
ATOM   4030  C   VAL C 324      -6.979 -20.288  44.712  1.00 44.32           C  
ANISOU 4030  C   VAL C 324     6224   6668   3947    570   -948   -125       C  
ATOM   4031  O   VAL C 324      -7.499 -20.873  45.657  1.00 45.26           O  
ANISOU 4031  O   VAL C 324     6344   6802   4049    580   -941   -118       O  
ATOM   4032  CB  VAL C 324      -4.645 -19.533  44.197  1.00 42.36           C  
ANISOU 4032  CB  VAL C 324     5980   6387   3728    591   -952   -143       C  
ATOM   4033  CG1 VAL C 324      -3.452 -18.776  44.811  1.00 41.78           C  
ANISOU 4033  CG1 VAL C 324     5903   6303   3667    629   -952   -157       C  
ATOM   4034  CG2 VAL C 324      -4.382 -21.025  44.212  1.00 42.36           C  
ANISOU 4034  CG2 VAL C 324     5993   6386   3715    573   -942   -128       C  
ATOM   4035  N   GLY C 325      -7.312 -20.548  43.454  1.00 43.94           N  
ANISOU 4035  N   GLY C 325     6181   6614   3902    531   -952   -119       N  
ATOM   4036  CA  GLY C 325      -8.376 -21.510  43.163  1.00 44.76           C  
ANISOU 4036  CA  GLY C 325     6290   6728   3989    499   -949   -104       C  
ATOM   4037  C   GLY C 325      -8.143 -22.976  43.554  1.00 45.01           C  
ANISOU 4037  C   GLY C 325     6335   6761   4004    489   -938    -89       C  
ATOM   4038  O   GLY C 325      -9.075 -23.686  43.917  1.00 46.00           O  
ANISOU 4038  O   GLY C 325     6464   6901   4113    479   -934    -78       O  
ATOM   4039  N   VAL C 326      -6.890 -23.420  43.495  1.00 44.41           N  
ANISOU 4039  N   VAL C 326     6267   6671   3934    494   -934    -90       N  
ATOM   4040  CA  VAL C 326      -6.579 -24.838  43.522  1.00 44.49           C  
ANISOU 4040  CA  VAL C 326     6292   6679   3932    477   -924    -76       C  
ATOM   4041  C   VAL C 326      -5.861 -25.268  44.787  1.00 44.61           C  
ANISOU 4041  C   VAL C 326     6311   6697   3941    510   -916    -76       C  
ATOM   4042  O   VAL C 326      -5.209 -24.481  45.452  1.00 44.27           O  
ANISOU 4042  O   VAL C 326     6261   6652   3908    545   -917    -88       O  
ATOM   4043  CB  VAL C 326      -5.754 -25.246  42.302  1.00 43.53           C  
ANISOU 4043  CB  VAL C 326     6179   6539   3820    449   -925    -74       C  
ATOM   4044  CG1 VAL C 326      -6.048 -24.323  41.148  1.00 43.10           C  
ANISOU 4044  CG1 VAL C 326     6118   6479   3780    430   -935    -81       C  
ATOM   4045  CG2 VAL C 326      -4.310 -25.224  42.614  1.00 43.12           C  
ANISOU 4045  CG2 VAL C 326     6132   6474   3779    472   -922    -81       C  
ATOM   4046  N   GLN C 327      -6.051 -26.536  45.141  1.00 46.75           N  
ANISOU 4046  N   GLN C 327     6593   6974   4195    498   -907    -62       N  
ATOM   4047  CA  GLN C 327      -5.525 -27.081  46.390  1.00 47.14           C  
ANISOU 4047  CA  GLN C 327     6647   7029   4236    528   -898    -60       C  
ATOM   4048  C   GLN C 327      -4.166 -27.781  46.236  1.00 46.46           C  
ANISOU 4048  C   GLN C 327     6572   6926   4155    528   -892    -58       C  
ATOM   4049  O   GLN C 327      -3.934 -28.542  45.290  1.00 46.14           O  
ANISOU 4049  O   GLN C 327     6542   6876   4114    496   -890    -50       O  
ATOM   4050  CB  GLN C 327      -6.532 -28.046  46.988  1.00 48.45           C  
ANISOU 4050  CB  GLN C 327     6818   7212   4380    518   -890    -45       C  
ATOM   4051  CG  GLN C 327      -7.740 -27.398  47.522  1.00 49.25           C  
ANISOU 4051  CG  GLN C 327     6907   7330   4474    529   -894    -48       C  
ATOM   4052  CD  GLN C 327      -7.513 -26.722  48.869  1.00 49.76           C  
ANISOU 4052  CD  GLN C 327     6963   7405   4540    575   -892    -58       C  
ATOM   4053  OE1 GLN C 327      -6.702 -27.163  49.695  1.00 49.73           O  
ANISOU 4053  OE1 GLN C 327     6964   7399   4533    598   -885    -57       O  
ATOM   4054  NE2 GLN C 327      -8.254 -25.637  49.099  1.00 50.32           N  
ANISOU 4054  NE2 GLN C 327     7018   7486   4614    590   -899    -67       N  
ATOM   4055  N   PRO C 328      -3.255 -27.514  47.168  1.00 49.07           N  
ANISOU 4055  N   PRO C 328     6901   7254   4490    565   -889    -66       N  
ATOM   4056  CA  PRO C 328      -1.956 -28.184  47.120  1.00 48.50           C  
ANISOU 4056  CA  PRO C 328     6840   7167   4421    568   -884    -64       C  
ATOM   4057  C   PRO C 328      -2.135 -29.599  47.654  1.00 49.41           C  
ANISOU 4057  C   PRO C 328     6968   7290   4517    560   -872    -49       C  
ATOM   4058  O   PRO C 328      -3.143 -29.848  48.343  1.00 50.56           O  
ANISOU 4058  O   PRO C 328     7111   7453   4648    563   -869    -42       O  
ATOM   4059  CB  PRO C 328      -1.087 -27.336  48.055  1.00 48.15           C  
ANISOU 4059  CB  PRO C 328     6788   7119   4387    613   -885    -79       C  
ATOM   4060  CG  PRO C 328      -2.068 -26.947  49.141  1.00 49.08           C  
ANISOU 4060  CG  PRO C 328     6897   7258   4494    636   -884    -80       C  
ATOM   4061  CD  PRO C 328      -3.442 -26.774  48.429  1.00 49.53           C  
ANISOU 4061  CD  PRO C 328     6949   7325   4546    606   -889    -75       C  
ATOM   4062  N   ILE C 329      -1.201 -30.497  47.330  1.00 45.67           N  
ANISOU 4062  N   ILE C 329     6506   6803   4044    549   -867    -43       N  
ATOM   4063  CA  ILE C 329      -1.171 -31.832  47.890  1.00 45.76           C  
ANISOU 4063  CA  ILE C 329     6529   6819   4037    545   -855    -29       C  
ATOM   4064  C   ILE C 329      -0.489 -31.806  49.224  1.00 45.86           C  
ANISOU 4064  C   ILE C 329     6542   6835   4048    587   -850    -33       C  
ATOM   4065  O   ILE C 329       0.638 -31.387  49.310  1.00 45.79           O  
ANISOU 4065  O   ILE C 329     6532   6813   4052    607   -852    -43       O  
ATOM   4066  CB  ILE C 329      -0.444 -32.753  46.972  1.00 45.62           C  
ANISOU 4066  CB  ILE C 329     6525   6787   4022    517   -852    -22       C  
ATOM   4067  CG1 ILE C 329      -0.960 -32.556  45.542  1.00 45.49           C  
ANISOU 4067  CG1 ILE C 329     6507   6766   4012    478   -858    -21       C  
ATOM   4068  CG2 ILE C 329      -0.583 -34.170  47.450  1.00 45.72           C  
ANISOU 4068  CG2 ILE C 329     6550   6805   4015    508   -840     -6       C  
ATOM   4069  CD1 ILE C 329      -0.648 -33.717  44.627  1.00 45.39           C  
ANISOU 4069  CD1 ILE C 329     6507   6745   3995    443   -853     -9       C  
ATOM   4070  N   LEU C 330      -1.161 -32.213  50.283  1.00 47.40           N  
ANISOU 4070  N   LEU C 330     6736   7046   4227    600   -844    -26       N  
ATOM   4071  CA  LEU C 330      -0.544 -32.138  51.606  1.00 48.36           C  
ANISOU 4071  CA  LEU C 330     6856   7172   4346    641   -839    -30       C  
ATOM   4072  C   LEU C 330      -0.650 -33.410  52.435  1.00 49.84           C  
ANISOU 4072  C   LEU C 330     7055   7368   4515    643   -826    -16       C  
ATOM   4073  O   LEU C 330      -1.724 -33.758  52.918  1.00 51.09           O  
ANISOU 4073  O   LEU C 330     7212   7543   4657    638   -823     -7       O  
ATOM   4074  CB  LEU C 330      -1.146 -30.989  52.402  1.00 49.00           C  
ANISOU 4074  CB  LEU C 330     6921   7266   4429    671   -844    -41       C  
ATOM   4075  CG  LEU C 330      -0.590 -29.618  52.052  1.00 47.64           C  
ANISOU 4075  CG  LEU C 330     6739   7085   4278    687   -854    -59       C  
ATOM   4076  CD1 LEU C 330      -1.489 -28.554  52.617  1.00 47.38           C  
ANISOU 4076  CD1 LEU C 330     6691   7067   4245    706   -859    -67       C  
ATOM   4077  CD2 LEU C 330       0.832 -29.466  52.584  1.00 47.86           C  
ANISOU 4077  CD2 LEU C 330     6769   7099   4315    718   -852    -68       C  
ATOM   4078  N   ASN C 331       0.494 -34.049  52.670  1.00 54.56           N  
ANISOU 4078  N   ASN C 331     7663   7955   5114    653   -820    -14       N  
ATOM   4079  CA  ASN C 331       0.582 -35.294  53.425  1.00 56.04           C  
ANISOU 4079  CA  ASN C 331     7862   8147   5284    656   -808      0       C  
ATOM   4080  C   ASN C 331       1.864 -35.291  54.234  1.00 56.37           C  
ANISOU 4080  C   ASN C 331     7906   8181   5332    691   -804     -7       C  
ATOM   4081  O   ASN C 331       2.435 -34.236  54.483  1.00 56.07           O  
ANISOU 4081  O   ASN C 331     7858   8138   5307    718   -811    -21       O  
ATOM   4082  CB  ASN C 331       0.507 -36.499  52.494  1.00 55.80           C  
ANISOU 4082  CB  ASN C 331     7846   8110   5246    615   -803     14       C  
ATOM   4083  CG  ASN C 331       1.452 -36.392  51.332  1.00 54.10           C  
ANISOU 4083  CG  ASN C 331     7634   7874   5047    599   -808      8       C  
ATOM   4084  OD1 ASN C 331       2.623 -36.076  51.503  1.00 53.67           O  
ANISOU 4084  OD1 ASN C 331     7580   7807   5004    621   -809     -1       O  
ATOM   4085  ND2 ASN C 331       0.947 -36.657  50.133  1.00 53.21           N  
ANISOU 4085  ND2 ASN C 331     7525   7759   4935    559   -811     14       N  
ATOM   4086  N   GLU C 332       2.271 -36.457  54.715  1.00 60.75           N  
ANISOU 4086  N   GLU C 332     8473   8735   5874    692   -794      5       N  
ATOM   4087  CA  GLU C 332       3.534 -36.597  55.461  1.00 61.16           C  
ANISOU 4087  CA  GLU C 332     8530   8778   5930    724   -789      0       C  
ATOM   4088  C   GLU C 332       4.766 -36.624  54.556  1.00 59.65           C  
ANISOU 4088  C   GLU C 332     8345   8565   5755    715   -792     -5       C  
ATOM   4089  O   GLU C 332       5.884 -36.537  55.050  1.00 59.68           O  
ANISOU 4089  O   GLU C 332     8351   8559   5766    742   -790    -12       O  
ATOM   4090  CB  GLU C 332       3.507 -37.865  56.334  1.00 62.99           C  
ANISOU 4090  CB  GLU C 332     8773   9018   6144    728   -776     15       C  
ATOM   4091  CG  GLU C 332       3.498 -39.188  55.567  1.00 63.14           C  
ANISOU 4091  CG  GLU C 332     8807   9030   6153    691   -770     30       C  
ATOM   4092  CD  GLU C 332       2.177 -39.464  54.840  1.00 63.23           C  
ANISOU 4092  CD  GLU C 332     8819   9050   6155    653   -771     40       C  
ATOM   4093  OE1 GLU C 332       1.176 -38.722  55.045  1.00 63.45           O  
ANISOU 4093  OE1 GLU C 332     8836   9093   6181    657   -776     36       O  
ATOM   4094  OE2 GLU C 332       2.143 -40.441  54.056  1.00 63.12           O  
ANISOU 4094  OE2 GLU C 332     8816   9030   6135    620   -767     51       O  
ATOM   4095  N   HIS C 333       4.559 -36.739  53.244  1.00 59.60           N  
ANISOU 4095  N   HIS C 333     8342   8550   5754    679   -796     -3       N  
ATOM   4096  CA  HIS C 333       5.658 -36.676  52.279  1.00 58.22           C  
ANISOU 4096  CA  HIS C 333     8171   8354   5595    669   -800     -9       C  
ATOM   4097  C   HIS C 333       5.921 -35.249  51.745  1.00 56.80           C  
ANISOU 4097  C   HIS C 333     7980   8167   5436    677   -812    -26       C  
ATOM   4098  O   HIS C 333       6.734 -35.060  50.830  1.00 55.58           O  
ANISOU 4098  O   HIS C 333     7827   7995   5296    667   -816    -32       O  
ATOM   4099  CB  HIS C 333       5.392 -37.610  51.093  1.00 57.69           C  
ANISOU 4099  CB  HIS C 333     8114   8281   5523    624   -797      3       C  
ATOM   4100  CG  HIS C 333       5.299 -39.060  51.465  1.00 59.05           C  
ANISOU 4100  CG  HIS C 333     8301   8459   5678    613   -785     20       C  
ATOM   4101  ND1 HIS C 333       4.483 -39.949  50.793  1.00 59.10           N  
ANISOU 4101  ND1 HIS C 333     8315   8470   5672    574   -781     33       N  
ATOM   4102  CD2 HIS C 333       5.913 -39.778  52.440  1.00 60.49           C  
ANISOU 4102  CD2 HIS C 333     8491   8641   5851    635   -776     25       C  
ATOM   4103  CE1 HIS C 333       4.590 -41.149  51.343  1.00 60.55           C  
ANISOU 4103  CE1 HIS C 333     8510   8656   5839    574   -770     46       C  
ATOM   4104  NE2 HIS C 333       5.447 -41.071  52.348  1.00 61.42           N  
ANISOU 4104  NE2 HIS C 333     8621   8763   5952    610   -767     41       N  
ATOM   4105  N   THR C 334       5.212 -34.253  52.288  1.00 53.18           N  
ANISOU 4105  N   THR C 334     7507   7720   4978    696   -818    -34       N  
ATOM   4106  CA  THR C 334       5.368 -32.857  51.862  1.00 51.98           C  
ANISOU 4106  CA  THR C 334     7344   7562   4845    705   -829    -50       C  
ATOM   4107  C   THR C 334       5.827 -31.969  53.008  1.00 52.61           C  
ANISOU 4107  C   THR C 334     7414   7645   4930    751   -830    -63       C  
ATOM   4108  O   THR C 334       5.694 -32.340  54.184  1.00 54.05           O  
ANISOU 4108  O   THR C 334     7598   7840   5100    773   -823    -59       O  
ATOM   4109  CB  THR C 334       4.057 -32.256  51.313  1.00 51.65           C  
ANISOU 4109  CB  THR C 334     7292   7532   4802    685   -836    -50       C  
ATOM   4110  OG1 THR C 334       3.014 -32.464  52.266  1.00 53.17           O  
ANISOU 4110  OG1 THR C 334     7480   7744   4977    694   -831    -44       O  
ATOM   4111  CG2 THR C 334       3.676 -32.850  49.957  1.00 50.51           C  
ANISOU 4111  CG2 THR C 334     7154   7381   4657    639   -837    -41       C  
ATOM   4112  N   PHE C 335       6.385 -30.809  52.654  1.00 51.70           N  
ANISOU 4112  N   PHE C 335     7291   7520   4833    763   -839    -79       N  
ATOM   4113  CA  PHE C 335       6.616 -29.745  53.628  1.00 52.21           C  
ANISOU 4113  CA  PHE C 335     7345   7589   4903    804   -843    -93       C  
ATOM   4114  C   PHE C 335       6.364 -28.383  52.996  1.00 51.18           C  
ANISOU 4114  C   PHE C 335     7202   7455   4789    803   -854   -106       C  
ATOM   4115  O   PHE C 335       6.454 -28.248  51.771  1.00 49.86           O  
ANISOU 4115  O   PHE C 335     7037   7277   4632    776   -860   -107       O  
ATOM   4116  CB  PHE C 335       8.029 -29.810  54.188  1.00 52.41           C  
ANISOU 4116  CB  PHE C 335     7376   7602   4936    833   -839    -99       C  
ATOM   4117  CG  PHE C 335       9.111 -29.484  53.189  1.00 50.97           C  
ANISOU 4117  CG  PHE C 335     7197   7397   4772    824   -845   -107       C  
ATOM   4118  CD1 PHE C 335       9.401 -28.172  52.850  1.00 50.20           C  
ANISOU 4118  CD1 PHE C 335     7090   7292   4692    836   -855   -123       C  
ATOM   4119  CD2 PHE C 335       9.892 -30.489  52.646  1.00 50.51           C  
ANISOU 4119  CD2 PHE C 335     7153   7326   4714    807   -840    -99       C  
ATOM   4120  CE1 PHE C 335      10.399 -27.868  51.956  1.00 48.98           C  
ANISOU 4120  CE1 PHE C 335     6939   7117   4554    829   -860   -131       C  
ATOM   4121  CE2 PHE C 335      10.919 -30.187  51.748  1.00 49.30           C  
ANISOU 4121  CE2 PHE C 335     7002   7151   4577    801   -845   -107       C  
ATOM   4122  CZ  PHE C 335      11.164 -28.870  51.407  1.00 48.53           C  
ANISOU 4122  CZ  PHE C 335     6895   7047   4497    811   -855   -123       C  
ATOM   4123  N   CYS C 336       6.078 -27.367  53.809  1.00 49.07           N  
ANISOU 4123  N   CYS C 336     6923   7198   4524    833   -858   -117       N  
ATOM   4124  CA  CYS C 336       5.807 -26.037  53.267  1.00 48.22           C  
ANISOU 4124  CA  CYS C 336     6803   7088   4431    835   -868   -131       C  
ATOM   4125  C   CYS C 336       6.898 -25.017  53.568  1.00 47.91           C  
ANISOU 4125  C   CYS C 336     6759   7036   4407    867   -873   -148       C  
ATOM   4126  O   CYS C 336       7.408 -24.925  54.693  1.00 48.89           O  
ANISOU 4126  O   CYS C 336     6882   7164   4529    901   -869   -153       O  
ATOM   4127  CB  CYS C 336       4.494 -25.512  53.815  1.00 49.14           C  
ANISOU 4127  CB  CYS C 336     6907   7225   4538    841   -870   -131       C  
ATOM   4128  SG  CYS C 336       3.085 -26.477  53.367  1.00 49.52           S  
ANISOU 4128  SG  CYS C 336     6959   7288   4569    802   -867   -113       S  
ATOM   4129  N   ALA C 337       7.238 -24.224  52.563  1.00 45.71           N  
ANISOU 4129  N   ALA C 337     6477   6743   4146    856   -882   -158       N  
ATOM   4130  CA  ALA C 337       8.150 -23.103  52.761  1.00 45.66           C  
ANISOU 4130  CA  ALA C 337     6466   6726   4157    885   -888   -175       C  
ATOM   4131  C   ALA C 337       7.385 -21.756  52.800  1.00 45.70           C  
ANISOU 4131  C   ALA C 337     6457   6740   4168    895   -896   -187       C  
ATOM   4132  O   ALA C 337       6.543 -21.468  51.940  1.00 45.65           O  
ANISOU 4132  O   ALA C 337     6446   6736   4164    870   -901   -185       O  
ATOM   4133  CB  ALA C 337       9.211 -23.093  51.671  1.00 45.47           C  
ANISOU 4133  CB  ALA C 337     6450   6679   4148    870   -891   -179       C  
ATOM   4134  N   GLY C 338       7.737 -20.921  53.772  1.00 43.06           N  
ANISOU 4134  N   GLY C 338     6114   6408   3837    934   -897   -200       N  
ATOM   4135  CA  GLY C 338       7.086 -19.649  53.959  1.00 43.43           C  
ANISOU 4135  CA  GLY C 338     6148   6464   3889    948   -904   -211       C  
ATOM   4136  C   GLY C 338       7.316 -18.671  52.811  1.00 42.35           C  
ANISOU 4136  C   GLY C 338     6008   6312   3772    935   -914   -222       C  
ATOM   4137  O   GLY C 338       7.780 -19.048  51.713  1.00 42.20           O  
ANISOU 4137  O   GLY C 338     5997   6277   3760    908   -916   -218       O  
ATOM   4138  N   MET C 339       6.899 -17.419  53.029  1.00 47.02           N  
ANISOU 4138  N   MET C 339     6587   6909   4370    952   -921   -235       N  
ATOM   4139  CA  MET C 339       7.191 -16.385  52.049  1.00 46.00           C  
ANISOU 4139  CA  MET C 339     6455   6765   4259    945   -931   -246       C  
ATOM   4140  C   MET C 339       8.543 -15.734  52.367  1.00 46.06           C  
ANISOU 4140  C   MET C 339     6464   6756   4281    974   -933   -260       C  
ATOM   4141  O   MET C 339       9.089 -15.909  53.467  1.00 47.08           O  
ANISOU 4141  O   MET C 339     6594   6889   4404   1004   -927   -263       O  
ATOM   4142  CB  MET C 339       6.070 -15.345  52.025  1.00 46.38           C  
ANISOU 4142  CB  MET C 339     6489   6825   4308    947   -937   -253       C  
ATOM   4143  CG  MET C 339       4.880 -15.752  51.195  1.00 45.91           C  
ANISOU 4143  CG  MET C 339     6428   6773   4241    910   -939   -241       C  
ATOM   4144  SD  MET C 339       3.836 -14.343  50.695  1.00 46.04           S  
ANISOU 4144  SD  MET C 339     6430   6796   4266    907   -949   -251       S  
ATOM   4145  CE  MET C 339       3.109 -13.823  52.288  1.00 47.95           C  
ANISOU 4145  CE  MET C 339     6660   7062   4496    946   -946   -257       C  
ATOM   4146  N   SER C 340       9.016 -14.896  51.453  1.00 47.55           N  
ANISOU 4146  N   SER C 340     6651   6928   4486    967   -941   -270       N  
ATOM   4147  CA  SER C 340      10.333 -14.295  51.586  1.00 47.56           C  
ANISOU 4147  CA  SER C 340     6656   6913   4502    990   -943   -283       C  
ATOM   4148  C   SER C 340      10.371 -13.251  52.713  1.00 48.92           C  
ANISOU 4148  C   SER C 340     6819   7094   4676   1031   -945   -298       C  
ATOM   4149  O   SER C 340       9.368 -13.005  53.382  1.00 49.86           O  
ANISOU 4149  O   SER C 340     6928   7231   4785   1041   -944   -298       O  
ATOM   4150  CB  SER C 340      10.744 -13.670  50.246  1.00 46.32           C  
ANISOU 4150  CB  SER C 340     6500   6737   4364    970   -952   -289       C  
ATOM   4151  OG  SER C 340      11.557 -12.515  50.408  1.00 46.59           O  
ANISOU 4151  OG  SER C 340     6531   6759   4412    996   -957   -306       O  
ATOM   4152  N   LYS C 341      11.528 -12.640  52.925  1.00 47.06           N  
ANISOU 4152  N   LYS C 341     6584   6843   4452   1054   -947   -311       N  
ATOM   4153  CA  LYS C 341      11.647 -11.561  53.896  1.00 48.35           C  
ANISOU 4153  CA  LYS C 341     6739   7012   4618   1092   -949   -326       C  
ATOM   4154  C   LYS C 341      10.916 -10.349  53.358  1.00 48.15           C  
ANISOU 4154  C   LYS C 341     6704   6988   4602   1088   -959   -336       C  
ATOM   4155  O   LYS C 341      10.294  -9.594  54.099  1.00 49.26           O  
ANISOU 4155  O   LYS C 341     6835   7143   4740   1110   -960   -344       O  
ATOM   4156  CB  LYS C 341      13.121 -11.244  54.134  1.00 48.68           C  
ANISOU 4156  CB  LYS C 341     6788   7037   4673   1115   -950   -337       C  
ATOM   4157  CG  LYS C 341      13.448 -10.292  55.273  1.00 49.32           C  
ANISOU 4157  CG  LYS C 341     6861   7122   4755   1157   -951   -353       C  
ATOM   4158  CD  LYS C 341      14.934  -9.844  55.176  1.00 49.77           C  
ANISOU 4158  CD  LYS C 341     6925   7158   4827   1173   -954   -365       C  
ATOM   4159  CE  LYS C 341      15.444  -9.133  56.442  1.00 51.26           C  
ANISOU 4159  CE  LYS C 341     7110   7352   5016   1216   -952   -379       C  
ATOM   4160  NZ  LYS C 341      15.712 -10.073  57.587  1.00 52.46           N  
ANISOU 4160  NZ  LYS C 341     7265   7514   5153   1235   -943   -372       N  
ATOM   4161  N   TYR C 342      11.065 -10.172  52.048  1.00 47.87           N  
ANISOU 4161  N   TYR C 342     6672   6937   4579   1060   -965   -335       N  
ATOM   4162  CA  TYR C 342      10.488  -9.091  51.253  1.00 47.50           C  
ANISOU 4162  CA  TYR C 342     6616   6887   4543   1049   -974   -343       C  
ATOM   4163  C   TYR C 342       9.214  -9.460  50.492  1.00 46.81           C  
ANISOU 4163  C   TYR C 342     6526   6810   4449   1015   -975   -331       C  
ATOM   4164  O   TYR C 342       8.891  -8.799  49.498  1.00 46.07           O  
ANISOU 4164  O   TYR C 342     6429   6709   4365    997   -983   -334       O  
ATOM   4165  CB  TYR C 342      11.539  -8.527  50.297  1.00 46.55           C  
ANISOU 4165  CB  TYR C 342     6502   6743   4442   1043   -980   -351       C  
ATOM   4166  CG  TYR C 342      12.754  -7.999  51.043  1.00 47.35           C  
ANISOU 4166  CG  TYR C 342     6606   6834   4552   1078   -980   -365       C  
ATOM   4167  CD1 TYR C 342      12.799  -6.696  51.525  1.00 48.36           C  
ANISOU 4167  CD1 TYR C 342     6726   6962   4687   1106   -986   -381       C  
ATOM   4168  CD2 TYR C 342      13.844  -8.830  51.297  1.00 47.20           C  
ANISOU 4168  CD2 TYR C 342     6596   6805   4531   1084   -974   -361       C  
ATOM   4169  CE1 TYR C 342      13.893  -6.225  52.224  1.00 49.21           C  
ANISOU 4169  CE1 TYR C 342     6835   7061   4800   1138   -985   -393       C  
ATOM   4170  CE2 TYR C 342      14.945  -8.366  51.978  1.00 48.02           C  
ANISOU 4170  CE2 TYR C 342     6702   6900   4642   1115   -974   -373       C  
ATOM   4171  CZ  TYR C 342      14.962  -7.060  52.443  1.00 49.02           C  
ANISOU 4171  CZ  TYR C 342     6821   7028   4776   1142   -980   -389       C  
ATOM   4172  OH  TYR C 342      16.075  -6.611  53.124  1.00 49.90           O  
ANISOU 4172  OH  TYR C 342     6936   7131   4894   1173   -979   -401       O  
ATOM   4173  N   GLN C 343       8.559 -10.562  50.873  1.00 47.95           N  
ANISOU 4173  N   GLN C 343     6673   6970   4577   1004   -968   -316       N  
ATOM   4174  CA  GLN C 343       7.290 -11.017  50.240  1.00 47.47           C  
ANISOU 4174  CA  GLN C 343     6609   6920   4506    971   -968   -304       C  
ATOM   4175  C   GLN C 343       7.502 -11.487  48.814  1.00 45.98           C  
ANISOU 4175  C   GLN C 343     6428   6717   4325    933   -971   -296       C  
ATOM   4176  O   GLN C 343       6.603 -11.397  47.986  1.00 45.49           O  
ANISOU 4176  O   GLN C 343     6363   6659   4263    906   -975   -291       O  
ATOM   4177  CB  GLN C 343       6.183  -9.924  50.187  1.00 47.97           C  
ANISOU 4177  CB  GLN C 343     6660   6995   4571    974   -975   -311       C  
ATOM   4178  CG  GLN C 343       6.081  -8.941  51.348  1.00 49.55           C  
ANISOU 4178  CG  GLN C 343     6851   7206   4771   1014   -976   -325       C  
ATOM   4179  CD  GLN C 343       5.833  -9.621  52.694  1.00 50.95           C  
ANISOU 4179  CD  GLN C 343     7027   7401   4931   1036   -967   -319       C  
ATOM   4180  OE1 GLN C 343       6.764 -10.187  53.315  1.00 51.60           O  
ANISOU 4180  OE1 GLN C 343     7117   7479   5011   1052   -961   -319       O  
ATOM   4181  NE2 GLN C 343       4.569  -9.566  53.161  1.00 51.54           N  
ANISOU 4181  NE2 GLN C 343     7092   7496   4993   1037   -966   -316       N  
ATOM   4182  N   GLU C 344       8.706 -11.951  48.515  1.00 45.27           N  
ANISOU 4182  N   GLU C 344     6349   6610   4243    931   -969   -295       N  
ATOM   4183  CA  GLU C 344       8.944 -12.595  47.237  1.00 43.96           C  
ANISOU 4183  CA  GLU C 344     6191   6431   4082    894   -969   -286       C  
ATOM   4184  C   GLU C 344       8.289 -13.973  47.356  1.00 43.95           C  
ANISOU 4184  C   GLU C 344     6194   6442   4062    873   -962   -268       C  
ATOM   4185  O   GLU C 344       8.169 -14.538  48.455  1.00 44.87           O  
ANISOU 4185  O   GLU C 344     6312   6571   4165    891   -954   -264       O  
ATOM   4186  CB  GLU C 344      10.440 -12.689  46.949  1.00 43.42           C  
ANISOU 4186  CB  GLU C 344     6132   6340   4026    900   -969   -291       C  
ATOM   4187  CG  GLU C 344      11.179 -11.408  47.266  1.00 43.83           C  
ANISOU 4187  CG  GLU C 344     6179   6382   4092    931   -975   -309       C  
ATOM   4188  CD  GLU C 344      12.710 -11.547  47.248  1.00 43.60           C  
ANISOU 4188  CD  GLU C 344     6159   6334   4073    943   -974   -314       C  
ATOM   4189  OE1 GLU C 344      13.364 -11.417  46.170  1.00 42.66           O  
ANISOU 4189  OE1 GLU C 344     6045   6195   3967    925   -978   -316       O  
ATOM   4190  OE2 GLU C 344      13.268 -11.773  48.341  1.00 44.49           O  
ANISOU 4190  OE2 GLU C 344     6274   6449   4180    972   -968   -317       O  
ATOM   4191  N   ASP C 345       7.833 -14.515  46.248  1.00 40.29           N  
ANISOU 4191  N   ASP C 345     5734   5976   3597    835   -962   -258       N  
ATOM   4192  CA  ASP C 345       7.367 -15.874  46.316  1.00 40.33           C  
ANISOU 4192  CA  ASP C 345     5746   5990   3586    814   -955   -241       C  
ATOM   4193  C   ASP C 345       7.480 -16.510  44.954  1.00 39.59           C  
ANISOU 4193  C   ASP C 345     5660   5885   3496    774   -955   -231       C  
ATOM   4194  O   ASP C 345       7.981 -15.898  43.983  1.00 39.34           O  
ANISOU 4194  O   ASP C 345     5629   5838   3481    764   -962   -238       O  
ATOM   4195  CB  ASP C 345       5.925 -15.951  46.838  1.00 41.06           C  
ANISOU 4195  CB  ASP C 345     5831   6106   3664    811   -953   -234       C  
ATOM   4196  CG  ASP C 345       5.453 -17.384  47.093  1.00 41.22           C  
ANISOU 4196  CG  ASP C 345     5859   6138   3665    794   -944   -217       C  
ATOM   4197  OD1 ASP C 345       6.282 -18.203  47.546  1.00 41.22           O  
ANISOU 4197  OD1 ASP C 345     5868   6133   3661    802   -937   -213       O  
ATOM   4198  OD2 ASP C 345       4.285 -17.685  46.797  1.00 41.34           O  
ANISOU 4198  OD2 ASP C 345     5870   6166   3670    771   -944   -208       O  
ATOM   4199  N   THR C 346       6.987 -17.740  44.906  1.00 40.77           N  
ANISOU 4199  N   THR C 346     5816   6044   3631    752   -949   -216       N  
ATOM   4200  CA  THR C 346       7.282 -18.657  43.859  1.00 40.64           C  
ANISOU 4200  CA  THR C 346     5810   6017   3615    717   -946   -205       C  
ATOM   4201  C   THR C 346       5.956 -18.966  43.163  1.00 40.65           C  
ANISOU 4201  C   THR C 346     5808   6030   3608    683   -948   -195       C  
ATOM   4202  O   THR C 346       4.996 -19.342  43.808  1.00 40.78           O  
ANISOU 4202  O   THR C 346     5821   6065   3609    683   -944   -188       O  
ATOM   4203  CB  THR C 346       7.999 -19.896  44.457  1.00 40.66           C  
ANISOU 4203  CB  THR C 346     5824   6018   3608    723   -936   -197       C  
ATOM   4204  OG1 THR C 346       8.213 -20.891  43.459  1.00 40.55           O  
ANISOU 4204  OG1 THR C 346     5819   5995   3592    688   -933   -185       O  
ATOM   4205  CG2 THR C 346       7.242 -20.471  45.667  1.00 40.85           C  
ANISOU 4205  CG2 THR C 346     5846   6062   3612    737   -930   -189       C  
ATOM   4206  N   CYS C 347       5.912 -18.771  41.850  1.00 41.91           N  
ANISOU 4206  N   CYS C 347     5967   6180   3777    653   -953   -194       N  
ATOM   4207  CA  CYS C 347       4.673 -18.767  41.095  1.00 41.80           C  
ANISOU 4207  CA  CYS C 347     5949   6176   3758    622   -956   -187       C  
ATOM   4208  C   CYS C 347       4.781 -19.784  39.966  1.00 41.05           C  
ANISOU 4208  C   CYS C 347     5863   6073   3661    582   -953   -175       C  
ATOM   4209  O   CYS C 347       5.674 -20.605  40.003  1.00 40.85           O  
ANISOU 4209  O   CYS C 347     5848   6040   3635    582   -947   -171       O  
ATOM   4210  CB  CYS C 347       4.353 -17.362  40.556  1.00 41.55           C  
ANISOU 4210  CB  CYS C 347     5906   6140   3740    624   -967   -199       C  
ATOM   4211  SG  CYS C 347       2.550 -16.973  40.461  1.00 42.16           S  
ANISOU 4211  SG  CYS C 347     5972   6239   3808    609   -971   -195       S  
ATOM   4212  N   TYR C 348       3.850 -19.748  39.007  1.00 42.47           N  
ANISOU 4212  N   TYR C 348     6039   6258   3839    549   -957   -170       N  
ATOM   4213  CA  TYR C 348       3.708 -20.716  37.919  1.00 42.35           C  
ANISOU 4213  CA  TYR C 348     6032   6240   3820    508   -954   -158       C  
ATOM   4214  C   TYR C 348       5.006 -21.005  37.138  1.00 42.19           C  
ANISOU 4214  C   TYR C 348     6019   6199   3812    500   -953   -159       C  
ATOM   4215  O   TYR C 348       5.622 -20.118  36.543  1.00 42.09           O  
ANISOU 4215  O   TYR C 348     6003   6172   3816    505   -959   -170       O  
ATOM   4216  CB  TYR C 348       2.672 -20.192  36.911  1.00 42.31           C  
ANISOU 4216  CB  TYR C 348     6019   6240   3818    480   -961   -156       C  
ATOM   4217  CG  TYR C 348       1.349 -19.646  37.471  1.00 42.56           C  
ANISOU 4217  CG  TYR C 348     6040   6289   3840    486   -965   -157       C  
ATOM   4218  CD1 TYR C 348       0.953 -19.845  38.808  1.00 43.47           C  
ANISOU 4218  CD1 TYR C 348     6155   6420   3943    512   -960   -155       C  
ATOM   4219  CD2 TYR C 348       0.468 -18.970  36.642  1.00 42.52           C  
ANISOU 4219  CD2 TYR C 348     6027   6288   3840    466   -972   -158       C  
ATOM   4220  CE1 TYR C 348      -0.242 -19.365  39.281  1.00 44.31           C  
ANISOU 4220  CE1 TYR C 348     6251   6542   4041    517   -963   -155       C  
ATOM   4221  CE2 TYR C 348      -0.743 -18.490  37.116  1.00 43.34           C  
ANISOU 4221  CE2 TYR C 348     6123   6409   3937    471   -975   -158       C  
ATOM   4222  CZ  TYR C 348      -1.081 -18.693  38.425  1.00 44.22           C  
ANISOU 4222  CZ  TYR C 348     6233   6534   4035    497   -971   -157       C  
ATOM   4223  OH  TYR C 348      -2.285 -18.195  38.871  1.00 45.17           O  
ANISOU 4223  OH  TYR C 348     6344   6670   4148    502   -974   -158       O  
ATOM   4224  N   GLY C 349       5.394 -22.269  37.079  1.00 44.32           N  
ANISOU 4224  N   GLY C 349     6300   6468   4073    486   -944   -149       N  
ATOM   4225  CA  GLY C 349       6.634 -22.632  36.405  1.00 44.18           C  
ANISOU 4225  CA  GLY C 349     6290   6431   4065    480   -942   -150       C  
ATOM   4226  C   GLY C 349       7.726 -23.051  37.364  1.00 44.21           C  
ANISOU 4226  C   GLY C 349     6302   6428   4068    510   -936   -152       C  
ATOM   4227  O   GLY C 349       8.721 -23.670  36.976  1.00 44.11           O  
ANISOU 4227  O   GLY C 349     6298   6402   4060    504   -932   -150       O  
ATOM   4228  N   ASP C 350       7.510 -22.748  38.637  1.00 42.97           N  
ANISOU 4228  N   ASP C 350     6141   6281   3905    541   -935   -156       N  
ATOM   4229  CA  ASP C 350       8.523 -22.952  39.643  1.00 43.34           C  
ANISOU 4229  CA  ASP C 350     6194   6323   3952    574   -931   -160       C  
ATOM   4230  C   ASP C 350       8.467 -24.322  40.251  1.00 43.99           C  
ANISOU 4230  C   ASP C 350     6285   6412   4016    570   -920   -147       C  
ATOM   4231  O   ASP C 350       9.258 -24.617  41.109  1.00 44.39           O  
ANISOU 4231  O   ASP C 350     6341   6460   4065    596   -916   -148       O  
ATOM   4232  CB  ASP C 350       8.381 -21.928  40.759  1.00 43.95           C  
ANISOU 4232  CB  ASP C 350     6262   6406   4031    612   -934   -171       C  
ATOM   4233  CG  ASP C 350       8.919 -20.556  40.395  1.00 43.42           C  
ANISOU 4233  CG  ASP C 350     6187   6326   3984    627   -944   -187       C  
ATOM   4234  OD1 ASP C 350       8.900 -19.696  41.302  1.00 43.78           O  
ANISOU 4234  OD1 ASP C 350     6226   6377   4032    660   -946   -197       O  
ATOM   4235  OD2 ASP C 350       9.371 -20.332  39.241  1.00 42.75           O  
ANISOU 4235  OD2 ASP C 350     6104   6227   3912    608   -948   -190       O  
ATOM   4236  N   ALA C 351       7.502 -25.147  39.879  1.00 46.66           N  
ANISOU 4236  N   ALA C 351     6626   6763   4341    539   -917   -133       N  
ATOM   4237  CA  ALA C 351       7.507 -26.549  40.337  1.00 47.28           C  
ANISOU 4237  CA  ALA C 351     6715   6847   4403    532   -906   -120       C  
ATOM   4238  C   ALA C 351       8.659 -27.289  39.679  1.00 46.75           C  
ANISOU 4238  C   ALA C 351     6658   6763   4341    521   -902   -117       C  
ATOM   4239  O   ALA C 351       9.020 -26.988  38.519  1.00 45.94           O  
ANISOU 4239  O   ALA C 351     6555   6649   4252    501   -906   -121       O  
ATOM   4240  CB  ALA C 351       6.188 -27.259  40.022  1.00 47.67           C  
ANISOU 4240  CB  ALA C 351     6764   6913   4436    500   -904   -106       C  
ATOM   4241  N   GLY C 352       9.238 -28.247  40.408  1.00 48.08           N  
ANISOU 4241  N   GLY C 352     6837   6931   4500    533   -893   -111       N  
ATOM   4242  CA  GLY C 352      10.335 -29.043  39.884  1.00 47.76           C  
ANISOU 4242  CA  GLY C 352     6807   6876   4464    523   -888   -108       C  
ATOM   4243  C   GLY C 352      11.663 -28.389  40.171  1.00 47.45           C  
ANISOU 4243  C   GLY C 352     6769   6820   4441    554   -891   -121       C  
ATOM   4244  O   GLY C 352      12.699 -29.028  40.095  1.00 47.38           O  
ANISOU 4244  O   GLY C 352     6770   6799   4435    557   -886   -119       O  
ATOM   4245  N   SER C 353      11.639 -27.103  40.485  1.00 44.94           N  
ANISOU 4245  N   SER C 353     6441   6501   4134    577   -899   -134       N  
ATOM   4246  CA  SER C 353      12.830 -26.426  40.991  1.00 45.00           C  
ANISOU 4246  CA  SER C 353     6449   6495   4154    611   -902   -147       C  
ATOM   4247  C   SER C 353      13.076 -26.898  42.437  1.00 46.11           C  
ANISOU 4247  C   SER C 353     6593   6644   4283    642   -895   -145       C  
ATOM   4248  O   SER C 353      12.132 -27.229  43.162  1.00 46.87           O  
ANISOU 4248  O   SER C 353     6687   6758   4364    645   -891   -137       O  
ATOM   4249  CB  SER C 353      12.682 -24.907  40.913  1.00 44.63           C  
ANISOU 4249  CB  SER C 353     6389   6446   4121    626   -912   -161       C  
ATOM   4250  OG  SER C 353      12.532 -24.465  39.562  1.00 43.66           O  
ANISOU 4250  OG  SER C 353     6263   6314   4010    599   -918   -163       O  
ATOM   4251  N   ALA C 354      14.342 -26.965  42.843  1.00 41.14           N  
ANISOU 4251  N   ALA C 354     5970   6002   3661    666   -893   -150       N  
ATOM   4252  CA  ALA C 354      14.670 -27.651  44.083  1.00 42.23           C  
ANISOU 4252  CA  ALA C 354     6114   6146   3787    691   -885   -146       C  
ATOM   4253  C   ALA C 354      14.725 -26.684  45.223  1.00 42.81           C  
ANISOU 4253  C   ALA C 354     6178   6224   3862    730   -888   -158       C  
ATOM   4254  O   ALA C 354      15.250 -25.605  45.084  1.00 42.40           O  
ANISOU 4254  O   ALA C 354     6120   6163   3826    746   -895   -171       O  
ATOM   4255  CB  ALA C 354      16.005 -28.388  43.956  1.00 42.29           C  
ANISOU 4255  CB  ALA C 354     6134   6137   3799    694   -879   -145       C  
ATOM   4256  N   PHE C 355      14.243 -27.095  46.376  1.00 40.31           N  
ANISOU 4256  N   PHE C 355     5861   5924   3531    747   -882   -152       N  
ATOM   4257  CA  PHE C 355      14.393 -26.251  47.531  1.00 40.42           C  
ANISOU 4257  CA  PHE C 355     5867   5944   3546    786   -884   -163       C  
ATOM   4258  C   PHE C 355      15.697 -26.688  48.078  1.00 40.41           C  
ANISOU 4258  C   PHE C 355     5875   5931   3548    809   -878   -166       C  
ATOM   4259  O   PHE C 355      15.738 -27.691  48.755  1.00 40.64           O  
ANISOU 4259  O   PHE C 355     5912   5967   3563    813   -870   -156       O  
ATOM   4260  CB  PHE C 355      13.249 -26.499  48.512  1.00 40.60           C  
ANISOU 4260  CB  PHE C 355     5885   5989   3551    794   -879   -156       C  
ATOM   4261  CG  PHE C 355      13.388 -25.824  49.858  1.00 41.41           C  
ANISOU 4261  CG  PHE C 355     5981   6100   3653    836   -879   -166       C  
ATOM   4262  CD1 PHE C 355      12.829 -24.595  50.096  1.00 41.41           C  
ANISOU 4262  CD1 PHE C 355     5968   6108   3659    851   -886   -177       C  
ATOM   4263  CD2 PHE C 355      13.987 -26.458  50.908  1.00 42.48           C  
ANISOU 4263  CD2 PHE C 355     6123   6239   3780    860   -871   -163       C  
ATOM   4264  CE1 PHE C 355      12.920 -24.010  51.349  1.00 42.48           C  
ANISOU 4264  CE1 PHE C 355     6097   6252   3791    890   -885   -186       C  
ATOM   4265  CE2 PHE C 355      14.054 -25.858  52.147  1.00 43.54           C  
ANISOU 4265  CE2 PHE C 355     6250   6381   3911    898   -871   -171       C  
ATOM   4266  CZ  PHE C 355      13.522 -24.650  52.361  1.00 43.53           C  
ANISOU 4266  CZ  PHE C 355     6235   6387   3916    913   -877   -183       C  
ATOM   4267  N   ALA C 356      16.750 -25.903  47.851  1.00 42.53           N  
ANISOU 4267  N   ALA C 356     6143   6183   3833    824   -884   -179       N  
ATOM   4268  CA  ALA C 356      18.135 -26.379  48.008  1.00 42.81           C  
ANISOU 4268  CA  ALA C 356     6189   6204   3874    838   -880   -181       C  
ATOM   4269  C   ALA C 356      18.768 -25.808  49.250  1.00 43.85           C  
ANISOU 4269  C   ALA C 356     6317   6337   4007    881   -879   -191       C  
ATOM   4270  O   ALA C 356      18.989 -24.610  49.322  1.00 43.74           O  
ANISOU 4270  O   ALA C 356     6296   6319   4006    899   -887   -206       O  
ATOM   4271  CB  ALA C 356      18.967 -26.016  46.778  1.00 41.74           C  
ANISOU 4271  CB  ALA C 356     6056   6047   3757    822   -886   -187       C  
ATOM   4272  N   VAL C 357      19.055 -26.649  50.234  1.00 45.36           N  
ANISOU 4272  N   VAL C 357     6514   6534   4186    898   -871   -185       N  
ATOM   4273  CA  VAL C 357      19.639 -26.171  51.485  1.00 46.51           C  
ANISOU 4273  CA  VAL C 357     6657   6682   4332    940   -870   -195       C  
ATOM   4274  C   VAL C 357      21.156 -26.379  51.546  1.00 46.72           C  
ANISOU 4274  C   VAL C 357     6693   6692   4368    955   -868   -200       C  
ATOM   4275  O   VAL C 357      21.664 -27.476  51.391  1.00 46.93           O  
ANISOU 4275  O   VAL C 357     6731   6712   4389    945   -861   -190       O  
ATOM   4276  CB  VAL C 357      19.006 -26.844  52.680  1.00 47.81           C  
ANISOU 4276  CB  VAL C 357     6822   6867   4478    953   -861   -185       C  
ATOM   4277  CG1 VAL C 357      18.787 -28.286  52.356  1.00 47.82           C  
ANISOU 4277  CG1 VAL C 357     6835   6870   4466    927   -853   -168       C  
ATOM   4278  CG2 VAL C 357      19.890 -26.709  53.914  1.00 49.15           C  
ANISOU 4278  CG2 VAL C 357     6992   7036   4646    994   -858   -193       C  
ATOM   4279  N   HIS C 358      21.861 -25.280  51.778  1.00 51.98           N  
ANISOU 4279  N   HIS C 358     7354   7349   5048    981   -874   -216       N  
ATOM   4280  CA  HIS C 358      23.310 -25.234  51.805  1.00 52.25           C  
ANISOU 4280  CA  HIS C 358     7395   7366   5093    997   -874   -223       C  
ATOM   4281  C   HIS C 358      23.748 -25.558  53.230  1.00 53.84           C  
ANISOU 4281  C   HIS C 358     7598   7575   5284   1032   -867   -224       C  
ATOM   4282  O   HIS C 358      23.320 -24.936  54.211  1.00 54.67           O  
ANISOU 4282  O   HIS C 358     7695   7694   5385   1058   -867   -230       O  
ATOM   4283  CB  HIS C 358      23.772 -23.859  51.322  1.00 51.69           C  
ANISOU 4283  CB  HIS C 358     7316   7282   5040   1006   -884   -240       C  
ATOM   4284  CG  HIS C 358      25.247 -23.655  51.300  1.00 51.97           C  
ANISOU 4284  CG  HIS C 358     7358   7299   5089   1023   -885   -249       C  
ATOM   4285  ND1 HIS C 358      25.820 -22.536  50.736  1.00 51.29           N  
ANISOU 4285  ND1 HIS C 358     7268   7199   5021   1028   -894   -263       N  
ATOM   4286  CD2 HIS C 358      26.271 -24.394  51.789  1.00 52.96           C  
ANISOU 4286  CD2 HIS C 358     7494   7418   5212   1038   -879   -247       C  
ATOM   4287  CE1 HIS C 358      27.135 -22.601  50.863  1.00 51.82           C  
ANISOU 4287  CE1 HIS C 358     7342   7252   5097   1044   -893   -269       C  
ATOM   4288  NE2 HIS C 358      27.436 -23.723  51.496  1.00 52.84           N  
ANISOU 4288  NE2 HIS C 358     7480   7385   5213   1050   -884   -260       N  
ATOM   4289  N   ASP C 359      24.575 -26.597  53.329  1.00 57.44           N  
ANISOU 4289  N   ASP C 359     8066   8023   5736   1032   -860   -217       N  
ATOM   4290  CA  ASP C 359      25.065 -27.110  54.605  1.00 59.01           C  
ANISOU 4290  CA  ASP C 359     8268   8228   5924   1062   -852   -215       C  
ATOM   4291  C   ASP C 359      26.396 -26.474  54.852  1.00 59.38           C  
ANISOU 4291  C   ASP C 359     8316   8260   5984   1089   -855   -229       C  
ATOM   4292  O   ASP C 359      27.337 -26.794  54.142  1.00 58.90           O  
ANISOU 4292  O   ASP C 359     8265   8182   5933   1079   -856   -229       O  
ATOM   4293  CB  ASP C 359      25.205 -28.630  54.562  1.00 59.49           C  
ANISOU 4293  CB  ASP C 359     8342   8288   5972   1046   -843   -199       C  
ATOM   4294  CG  ASP C 359      25.415 -29.233  55.930  1.00 61.18           C  
ANISOU 4294  CG  ASP C 359     8560   8514   6173   1074   -834   -194       C  
ATOM   4295  OD1 ASP C 359      26.117 -28.592  56.751  1.00 61.79           O  
ANISOU 4295  OD1 ASP C 359     8634   8589   6255   1108   -835   -206       O  
ATOM   4296  OD2 ASP C 359      24.878 -30.342  56.181  1.00 61.98           O  
ANISOU 4296  OD2 ASP C 359     8667   8624   6258   1062   -826   -179       O  
ATOM   4297  N   LEU C 360      26.496 -25.594  55.844  1.00 60.24           N  
ANISOU 4297  N   LEU C 360     8417   8376   6094   1123   -857   -241       N  
ATOM   4298  CA  LEU C 360      27.709 -24.787  55.959  1.00 60.56           C  
ANISOU 4298  CA  LEU C 360     8457   8402   6150   1146   -862   -256       C  
ATOM   4299  C   LEU C 360      28.933 -25.596  56.472  1.00 61.66           C  
ANISOU 4299  C   LEU C 360     8608   8533   6287   1163   -855   -254       C  
ATOM   4300  O   LEU C 360      30.067 -25.321  56.072  1.00 61.63           O  
ANISOU 4300  O   LEU C 360     8608   8511   6296   1168   -859   -262       O  
ATOM   4301  CB  LEU C 360      27.458 -23.551  56.841  1.00 61.22           C  
ANISOU 4301  CB  LEU C 360     8528   8495   6236   1178   -866   -270       C  
ATOM   4302  CG  LEU C 360      26.578 -22.493  56.169  1.00 60.15           C  
ANISOU 4302  CG  LEU C 360     8383   8363   6109   1164   -875   -277       C  
ATOM   4303  CD1 LEU C 360      26.790 -21.090  56.741  1.00 60.93           C  
ANISOU 4303  CD1 LEU C 360     8471   8462   6217   1194   -882   -295       C  
ATOM   4304  CD2 LEU C 360      26.771 -22.510  54.653  1.00 58.63           C  
ANISOU 4304  CD2 LEU C 360     8195   8154   5929   1130   -881   -275       C  
ATOM   4305  N   GLU C 361      28.700 -26.606  57.313  1.00 64.79           N  
ANISOU 4305  N   GLU C 361     9010   8942   6667   1170   -846   -243       N  
ATOM   4306  CA  GLU C 361      29.791 -27.406  57.868  1.00 66.00           C  
ANISOU 4306  CA  GLU C 361     9173   9088   6817   1186   -839   -240       C  
ATOM   4307  C   GLU C 361      30.525 -28.187  56.789  1.00 65.30           C  
ANISOU 4307  C   GLU C 361     9096   8981   6734   1161   -838   -233       C  
ATOM   4308  O   GLU C 361      31.750 -28.148  56.721  1.00 65.77           O  
ANISOU 4308  O   GLU C 361     9161   9025   6802   1173   -839   -240       O  
ATOM   4309  CB  GLU C 361      29.266 -28.364  58.939  1.00 67.22           C  
ANISOU 4309  CB  GLU C 361     9330   9260   6951   1196   -829   -227       C  
ATOM   4310  CG  GLU C 361      28.653 -27.649  60.153  1.00 68.36           C  
ANISOU 4310  CG  GLU C 361     9463   9422   7087   1225   -829   -234       C  
ATOM   4311  CD  GLU C 361      29.699 -26.961  61.035  1.00 69.70           C  
ANISOU 4311  CD  GLU C 361     9631   9588   7264   1264   -830   -248       C  
ATOM   4312  OE1 GLU C 361      30.436 -27.680  61.758  1.00 70.85           O  
ANISOU 4312  OE1 GLU C 361     9784   9733   7403   1282   -822   -245       O  
ATOM   4313  OE2 GLU C 361      29.779 -25.708  61.010  1.00 69.66           O  
ANISOU 4313  OE2 GLU C 361     9617   9581   7271   1277   -838   -264       O  
ATOM   4314  N   GLU C 362      29.786 -28.905  55.952  1.00 60.84           N  
ANISOU 4314  N   GLU C 362     8535   8417   6164   1126   -836   -220       N  
ATOM   4315  CA  GLU C 362      30.406 -29.660  54.864  1.00 60.13           C  
ANISOU 4315  CA  GLU C 362     8456   8311   6079   1100   -835   -214       C  
ATOM   4316  C   GLU C 362      30.419 -28.908  53.538  1.00 58.54           C  
ANISOU 4316  C   GLU C 362     8251   8096   5894   1076   -845   -221       C  
ATOM   4317  O   GLU C 362      30.779 -29.487  52.515  1.00 57.85           O  
ANISOU 4317  O   GLU C 362     8172   7996   5812   1051   -845   -215       O  
ATOM   4318  CB  GLU C 362      29.709 -31.006  54.669  1.00 60.11           C  
ANISOU 4318  CB  GLU C 362     8462   8316   6062   1074   -827   -195       C  
ATOM   4319  CG  GLU C 362      28.307 -31.112  55.268  1.00 60.62           C  
ANISOU 4319  CG  GLU C 362     8519   8402   6110   1071   -824   -187       C  
ATOM   4320  CD  GLU C 362      27.736 -32.512  55.114  1.00 60.85           C  
ANISOU 4320  CD  GLU C 362     8558   8438   6124   1046   -815   -169       C  
ATOM   4321  OE1 GLU C 362      28.426 -33.383  54.527  1.00 60.21           O  
ANISOU 4321  OE1 GLU C 362     8489   8344   6044   1032   -812   -162       O  
ATOM   4322  OE2 GLU C 362      26.591 -32.735  55.569  1.00 61.78           O  
ANISOU 4322  OE2 GLU C 362     8672   8574   6228   1042   -812   -161       O  
ATOM   4323  N   ASP C 363      29.988 -27.647  53.553  1.00 57.90           N  
ANISOU 4323  N   ASP C 363     8159   8019   5822   1085   -853   -232       N  
ATOM   4324  CA  ASP C 363      29.954 -26.805  52.354  1.00 56.44           C  
ANISOU 4324  CA  ASP C 363     7969   7822   5653   1065   -862   -240       C  
ATOM   4325  C   ASP C 363      29.383 -27.510  51.096  1.00 55.19           C  
ANISOU 4325  C   ASP C 363     7815   7660   5493   1022   -862   -228       C  
ATOM   4326  O   ASP C 363      29.947 -27.455  49.998  1.00 54.36           O  
ANISOU 4326  O   ASP C 363     7715   7540   5401   1003   -866   -230       O  
ATOM   4327  CB  ASP C 363      31.342 -26.267  52.058  1.00 56.51           C  
ANISOU 4327  CB  ASP C 363     7981   7811   5678   1078   -867   -252       C  
ATOM   4328  CG  ASP C 363      31.305 -25.099  51.102  1.00 55.32           C  
ANISOU 4328  CG  ASP C 363     7824   7651   5545   1068   -877   -263       C  
ATOM   4329  OD1 ASP C 363      30.972 -23.990  51.571  1.00 55.50           O  
ANISOU 4329  OD1 ASP C 363     7836   7681   5572   1086   -883   -274       O  
ATOM   4330  OD2 ASP C 363      31.579 -25.284  49.887  1.00 54.31           O  
ANISOU 4330  OD2 ASP C 363     7700   7509   5426   1040   -880   -261       O  
ATOM   4331  N   THR C 364      28.247 -28.167  51.265  1.00 54.93           N  
ANISOU 4331  N   THR C 364     7782   7644   5445   1007   -857   -215       N  
ATOM   4332  CA  THR C 364      27.635 -28.859  50.150  1.00 53.94           C  
ANISOU 4332  CA  THR C 364     7660   7517   5317    967   -856   -203       C  
ATOM   4333  C   THR C 364      26.157 -28.468  49.996  1.00 53.32           C  
ANISOU 4333  C   THR C 364     7572   7455   5232    951   -859   -200       C  
ATOM   4334  O   THR C 364      25.480 -28.150  50.982  1.00 54.02           O  
ANISOU 4334  O   THR C 364     7654   7560   5312    970   -858   -201       O  
ATOM   4335  CB  THR C 364      27.768 -30.378  50.322  1.00 54.75           C  
ANISOU 4335  CB  THR C 364     7776   7622   5405    957   -846   -188       C  
ATOM   4336  OG1 THR C 364      29.150 -30.718  50.550  1.00 55.40           O  
ANISOU 4336  OG1 THR C 364     7868   7690   5493    974   -843   -192       O  
ATOM   4337  CG2 THR C 364      27.216 -31.134  49.086  1.00 53.98           C  
ANISOU 4337  CG2 THR C 364     7683   7521   5305    914   -844   -176       C  
ATOM   4338  N   TRP C 365      25.689 -28.480  48.749  1.00 50.75           N  
ANISOU 4338  N   TRP C 365     7246   7124   4912    916   -863   -196       N  
ATOM   4339  CA  TRP C 365      24.318 -28.147  48.428  1.00 50.78           C  
ANISOU 4339  CA  TRP C 365     7241   7142   4910    897   -866   -193       C  
ATOM   4340  C   TRP C 365      23.395 -29.365  48.246  1.00 50.82           C  
ANISOU 4340  C   TRP C 365     7252   7159   4899    869   -859   -175       C  
ATOM   4341  O   TRP C 365      23.461 -30.092  47.265  1.00 50.72           O  
ANISOU 4341  O   TRP C 365     7246   7138   4886    839   -857   -167       O  
ATOM   4342  CB  TRP C 365      24.299 -27.297  47.162  1.00 50.62           C  
ANISOU 4342  CB  TRP C 365     7217   7111   4907    877   -876   -200       C  
ATOM   4343  CG  TRP C 365      24.901 -25.926  47.340  1.00 50.60           C  
ANISOU 4343  CG  TRP C 365     7206   7099   4920    902   -884   -218       C  
ATOM   4344  CD1 TRP C 365      26.237 -25.604  47.358  1.00 50.53           C  
ANISOU 4344  CD1 TRP C 365     7201   7074   4924    921   -886   -227       C  
ATOM   4345  CD2 TRP C 365      24.192 -24.689  47.514  1.00 50.64           C  
ANISOU 4345  CD2 TRP C 365     7198   7113   4930    912   -891   -227       C  
ATOM   4346  NE1 TRP C 365      26.394 -24.245  47.541  1.00 50.53           N  
ANISOU 4346  NE1 TRP C 365     7192   7071   4936    941   -894   -243       N  
ATOM   4347  CE2 TRP C 365      25.157 -23.665  47.635  1.00 50.60           C  
ANISOU 4347  CE2 TRP C 365     7190   7095   4940    936   -897   -243       C  
ATOM   4348  CE3 TRP C 365      22.843 -24.354  47.585  1.00 50.71           C  
ANISOU 4348  CE3 TRP C 365     7198   7139   4932    903   -893   -225       C  
ATOM   4349  CZ2 TRP C 365      24.815 -22.341  47.799  1.00 50.62           C  
ANISOU 4349  CZ2 TRP C 365     7182   7101   4952    951   -905   -256       C  
ATOM   4350  CZ3 TRP C 365      22.507 -23.014  47.767  1.00 50.74           C  
ANISOU 4350  CZ3 TRP C 365     7190   7145   4944    918   -901   -237       C  
ATOM   4351  CH2 TRP C 365      23.491 -22.033  47.868  1.00 50.70           C  
ANISOU 4351  CH2 TRP C 365     7182   7126   4954    942   -907   -253       C  
ATOM   4352  N   TYR C 366      22.492 -29.551  49.184  1.00 50.33           N  
ANISOU 4352  N   TYR C 366     7186   7116   4822    879   -855   -169       N  
ATOM   4353  CA  TYR C 366      21.563 -30.662  49.116  1.00 50.54           C  
ANISOU 4353  CA  TYR C 366     7217   7155   4831    854   -848   -153       C  
ATOM   4354  C   TYR C 366      20.198 -30.260  48.540  1.00 49.72           C  
ANISOU 4354  C   TYR C 366     7104   7063   4724    829   -852   -150       C  
ATOM   4355  O   TYR C 366      19.732 -29.156  48.763  1.00 49.47           O  
ANISOU 4355  O   TYR C 366     7060   7037   4698    842   -859   -160       O  
ATOM   4356  CB  TYR C 366      21.392 -31.273  50.519  1.00 52.01           C  
ANISOU 4356  CB  TYR C 366     7405   7355   5000    879   -839   -146       C  
ATOM   4357  CG  TYR C 366      22.674 -31.828  51.063  1.00 52.95           C  
ANISOU 4357  CG  TYR C 366     7534   7463   5120    900   -834   -147       C  
ATOM   4358  CD1 TYR C 366      23.214 -33.011  50.550  1.00 53.03           C  
ANISOU 4358  CD1 TYR C 366     7558   7465   5127    881   -827   -137       C  
ATOM   4359  CD2 TYR C 366      23.361 -31.171  52.069  1.00 53.86           C  
ANISOU 4359  CD2 TYR C 366     7645   7578   5240    939   -835   -159       C  
ATOM   4360  CE1 TYR C 366      24.415 -33.523  51.027  1.00 53.98           C  
ANISOU 4360  CE1 TYR C 366     7687   7574   5248    901   -822   -138       C  
ATOM   4361  CE2 TYR C 366      24.562 -31.686  52.563  1.00 54.81           C  
ANISOU 4361  CE2 TYR C 366     7776   7689   5362    959   -830   -160       C  
ATOM   4362  CZ  TYR C 366      25.078 -32.859  52.032  1.00 54.86           C  
ANISOU 4362  CZ  TYR C 366     7795   7685   5364    940   -823   -149       C  
ATOM   4363  OH  TYR C 366      26.258 -33.371  52.504  1.00 55.89           O  
ANISOU 4363  OH  TYR C 366     7934   7805   5495    959   -818   -150       O  
ATOM   4364  N   ALA C 367      19.544 -31.159  47.823  1.00 45.82           N  
ANISOU 4364  N   ALA C 367     6616   6573   4222    795   -849   -136       N  
ATOM   4365  CA  ALA C 367      18.169 -30.900  47.496  1.00 45.91           C  
ANISOU 4365  CA  ALA C 367     6619   6599   4227    774   -852   -132       C  
ATOM   4366  C   ALA C 367      17.311 -31.481  48.603  1.00 46.26           C  
ANISOU 4366  C   ALA C 367     6663   6663   4252    783   -845   -122       C  
ATOM   4367  O   ALA C 367      17.079 -32.668  48.659  1.00 46.31           O  
ANISOU 4367  O   ALA C 367     6678   6674   4244    768   -836   -109       O  
ATOM   4368  CB  ALA C 367      17.816 -31.514  46.148  1.00 45.67           C  
ANISOU 4368  CB  ALA C 367     6593   6563   4196    731   -852   -123       C  
ATOM   4369  N   THR C 368      16.788 -30.624  49.457  1.00 45.82           N  
ANISOU 4369  N   THR C 368     6595   6619   4194    808   -848   -130       N  
ATOM   4370  CA  THR C 368      15.930 -31.086  50.522  1.00 46.04           C  
ANISOU 4370  CA  THR C 368     6622   6667   4203    818   -841   -121       C  
ATOM   4371  C   THR C 368      14.530 -31.374  49.979  1.00 46.02           C  
ANISOU 4371  C   THR C 368     6616   6678   4191    785   -842   -111       C  
ATOM   4372  O   THR C 368      13.910 -32.377  50.371  1.00 46.51           O  
ANISOU 4372  O   THR C 368     6684   6752   4236    775   -834    -97       O  
ATOM   4373  CB  THR C 368      15.856 -30.073  51.665  1.00 46.77           C  
ANISOU 4373  CB  THR C 368     6704   6769   4297    856   -844   -133       C  
ATOM   4374  OG1 THR C 368      16.769 -30.461  52.697  1.00 47.91           O  
ANISOU 4374  OG1 THR C 368     6854   6911   4439    887   -838   -134       O  
ATOM   4375  CG2 THR C 368      14.438 -29.998  52.224  1.00 47.44           C  
ANISOU 4375  CG2 THR C 368     6780   6876   4368    854   -843   -127       C  
ATOM   4376  N   GLY C 369      14.053 -30.549  49.045  1.00 46.42           N  
ANISOU 4376  N   GLY C 369     6659   6726   4251    767   -851   -117       N  
ATOM   4377  CA  GLY C 369      12.743 -30.766  48.460  1.00 46.07           C  
ANISOU 4377  CA  GLY C 369     6612   6694   4199    735   -851   -107       C  
ATOM   4378  C   GLY C 369      12.598 -30.414  46.983  1.00 44.63           C  
ANISOU 4378  C   GLY C 369     6428   6501   4028    702   -859   -110       C  
ATOM   4379  O   GLY C 369      13.443 -29.727  46.408  1.00 43.73           O  
ANISOU 4379  O   GLY C 369     6313   6372   3932    707   -865   -121       O  
ATOM   4380  N   ILE C 370      11.526 -30.906  46.362  1.00 48.26           N  
ANISOU 4380  N   ILE C 370     6887   6970   4478    668   -858    -99       N  
ATOM   4381  CA  ILE C 370      11.143 -30.460  45.031  1.00 47.09           C  
ANISOU 4381  CA  ILE C 370     6735   6817   4340    637   -865   -101       C  
ATOM   4382  C   ILE C 370       9.797 -29.710  45.094  1.00 47.18           C  
ANISOU 4382  C   ILE C 370     6734   6844   4347    632   -870   -102       C  
ATOM   4383  O   ILE C 370       8.876 -30.119  45.828  1.00 48.16           O  
ANISOU 4383  O   ILE C 370     6857   6986   4455    634   -866    -94       O  
ATOM   4384  CB  ILE C 370      11.039 -31.624  44.074  1.00 46.83           C  
ANISOU 4384  CB  ILE C 370     6713   6781   4301    599   -859    -87       C  
ATOM   4385  CG1 ILE C 370      12.391 -32.323  43.985  1.00 46.83           C  
ANISOU 4385  CG1 ILE C 370     6724   6764   4305    605   -854    -87       C  
ATOM   4386  CG2 ILE C 370      10.575 -31.160  42.697  1.00 45.74           C  
ANISOU 4386  CG2 ILE C 370     6569   6639   4172    566   -867    -89       C  
ATOM   4387  CD1 ILE C 370      13.348 -31.664  43.047  1.00 45.74           C  
ANISOU 4387  CD1 ILE C 370     6585   6607   4187    602   -861    -98       C  
ATOM   4388  N   LEU C 371       9.669 -28.626  44.330  1.00 45.38           N  
ANISOU 4388  N   LEU C 371     6497   6611   4134    626   -880   -112       N  
ATOM   4389  CA  LEU C 371       8.473 -27.816  44.418  1.00 45.61           C  
ANISOU 4389  CA  LEU C 371     6515   6654   4161    625   -886   -115       C  
ATOM   4390  C   LEU C 371       7.279 -28.482  43.741  1.00 45.32           C  
ANISOU 4390  C   LEU C 371     6479   6628   4112    586   -884   -102       C  
ATOM   4391  O   LEU C 371       7.330 -28.760  42.554  1.00 44.28           O  
ANISOU 4391  O   LEU C 371     6350   6488   3985    554   -886    -98       O  
ATOM   4392  CB  LEU C 371       8.739 -26.421  43.817  1.00 44.88           C  
ANISOU 4392  CB  LEU C 371     6413   6551   4088    631   -897   -130       C  
ATOM   4393  CG  LEU C 371       7.517 -25.546  44.063  1.00 45.20           C  
ANISOU 4393  CG  LEU C 371     6440   6607   4126    635   -903   -134       C  
ATOM   4394  CD1 LEU C 371       7.043 -25.368  45.489  1.00 46.48           C  
ANISOU 4394  CD1 LEU C 371     6598   6786   4278    666   -900   -135       C  
ATOM   4395  CD2 LEU C 371       7.323 -24.376  43.248  1.00 44.68           C  
ANISOU 4395  CD2 LEU C 371     6366   6536   4076    628   -913   -144       C  
ATOM   4396  N   SER C 372       6.206 -28.724  44.496  1.00 46.22           N  
ANISOU 4396  N   SER C 372     6590   6761   4210    589   -881    -95       N  
ATOM   4397  CA  SER C 372       4.973 -29.246  43.901  1.00 46.32           C  
ANISOU 4397  CA  SER C 372     6603   6786   4211    553   -881    -83       C  
ATOM   4398  C   SER C 372       4.048 -28.129  43.528  1.00 46.02           C  
ANISOU 4398  C   SER C 372     6552   6755   4179    548   -890    -90       C  
ATOM   4399  O   SER C 372       3.684 -27.989  42.350  1.00 45.23           O  
ANISOU 4399  O   SER C 372     6450   6650   4084    517   -895    -88       O  
ATOM   4400  CB  SER C 372       4.221 -30.198  44.836  1.00 47.62           C  
ANISOU 4400  CB  SER C 372     6773   6968   4354    554   -872    -70       C  
ATOM   4401  OG  SER C 372       3.253 -30.963  44.121  1.00 47.68           O  
ANISOU 4401  OG  SER C 372     6784   6983   4350    515   -870    -57       O  
ATOM   4402  N   PHE C 373       3.635 -27.364  44.542  1.00 45.29           N  
ANISOU 4402  N   PHE C 373     6450   6673   4085    578   -892    -97       N  
ATOM   4403  CA  PHE C 373       2.623 -26.323  44.348  1.00 45.27           C  
ANISOU 4403  CA  PHE C 373     6435   6680   4086    576   -901   -103       C  
ATOM   4404  C   PHE C 373       3.247 -24.927  44.091  1.00 44.46           C  
ANISOU 4404  C   PHE C 373     6323   6565   4004    596   -910   -120       C  
ATOM   4405  O   PHE C 373       3.656 -24.195  45.016  1.00 44.86           O  
ANISOU 4405  O   PHE C 373     6369   6617   4060    633   -911   -131       O  
ATOM   4406  CB  PHE C 373       1.748 -26.311  45.592  1.00 46.68           C  
ANISOU 4406  CB  PHE C 373     6608   6878   4250    597   -898   -100       C  
ATOM   4407  CG  PHE C 373       0.557 -25.425  45.523  1.00 46.90           C  
ANISOU 4407  CG  PHE C 373     6623   6918   4277    595   -905   -104       C  
ATOM   4408  CD1 PHE C 373      -0.602 -25.855  44.889  1.00 46.92           C  
ANISOU 4408  CD1 PHE C 373     6627   6930   4270    560   -905    -94       C  
ATOM   4409  CD2 PHE C 373       0.565 -24.181  46.160  1.00 47.19           C  
ANISOU 4409  CD2 PHE C 373     6649   6959   4323    628   -910   -119       C  
ATOM   4410  CE1 PHE C 373      -1.708 -25.039  44.852  1.00 47.20           C  
ANISOU 4410  CE1 PHE C 373     6651   6977   4305    559   -912    -97       C  
ATOM   4411  CE2 PHE C 373      -0.541 -23.366  46.131  1.00 47.48           C  
ANISOU 4411  CE2 PHE C 373     6674   7008   4359    627   -917   -122       C  
ATOM   4412  CZ  PHE C 373      -1.674 -23.787  45.474  1.00 47.49           C  
ANISOU 4412  CZ  PHE C 373     6675   7017   4351    593   -918   -112       C  
ATOM   4413  N   ASP C 374       3.260 -24.558  42.817  1.00 44.64           N  
ANISOU 4413  N   ASP C 374     6345   6578   4039    570   -916   -123       N  
ATOM   4414  CA  ASP C 374       3.807 -23.302  42.373  1.00 44.16           C  
ANISOU 4414  CA  ASP C 374     6277   6505   3998    582   -925   -138       C  
ATOM   4415  C   ASP C 374       2.729 -22.281  42.105  1.00 44.57           C  
ANISOU 4415  C   ASP C 374     6317   6566   4053    578   -934   -143       C  
ATOM   4416  O   ASP C 374       2.990 -21.312  41.400  1.00 44.41           O  
ANISOU 4416  O   ASP C 374     6290   6535   4048    577   -941   -154       O  
ATOM   4417  CB  ASP C 374       4.645 -23.497  41.135  1.00 43.54           C  
ANISOU 4417  CB  ASP C 374     6205   6407   3931    559   -927   -138       C  
ATOM   4418  CG  ASP C 374       4.049 -24.469  40.213  1.00 43.68           C  
ANISOU 4418  CG  ASP C 374     6229   6429   3940    517   -924   -124       C  
ATOM   4419  OD1 ASP C 374       2.994 -25.025  40.589  1.00 44.27           O  
ANISOU 4419  OD1 ASP C 374     6303   6520   3998    506   -920   -114       O  
ATOM   4420  OD2 ASP C 374       4.634 -24.676  39.125  1.00 43.31           O  
ANISOU 4420  OD2 ASP C 374     6185   6367   3902    494   -925   -124       O  
ATOM   4421  N   LYS C 375       1.493 -22.560  42.520  1.00 43.02           N  
ANISOU 4421  N   LYS C 375     6116   6388   3840    571   -932   -135       N  
ATOM   4422  CA  LYS C 375       0.370 -21.656  42.286  1.00 43.06           C  
ANISOU 4422  CA  LYS C 375     6110   6404   3848    565   -939   -139       C  
ATOM   4423  C   LYS C 375       0.243 -20.448  43.233  1.00 43.17           C  
ANISOU 4423  C   LYS C 375     6112   6423   3866    604   -944   -153       C  
ATOM   4424  O   LYS C 375      -0.449 -19.508  42.882  1.00 43.17           O  
ANISOU 4424  O   LYS C 375     6103   6428   3873    601   -951   -159       O  
ATOM   4425  CB  LYS C 375      -0.917 -22.443  42.368  1.00 43.16           C  
ANISOU 4425  CB  LYS C 375     6124   6434   3841    542   -936   -125       C  
ATOM   4426  CG  LYS C 375      -0.925 -23.691  41.533  1.00 43.08           C  
ANISOU 4426  CG  LYS C 375     6126   6420   3824    504   -931   -111       C  
ATOM   4427  CD  LYS C 375      -0.736 -23.415  40.039  1.00 42.91           C  
ANISOU 4427  CD  LYS C 375     6104   6385   3815    473   -937   -113       C  
ATOM   4428  CE  LYS C 375      -1.288 -24.598  39.218  1.00 42.87           C  
ANISOU 4428  CE  LYS C 375     6107   6383   3798    430   -932    -97       C  
ATOM   4429  NZ  LYS C 375      -1.081 -24.420  37.760  1.00 42.70           N  
ANISOU 4429  NZ  LYS C 375     6086   6350   3788    399   -937    -98       N  
ATOM   4430  N   SER C 376       0.907 -20.461  44.400  1.00 42.08           N  
ANISOU 4430  N   SER C 376     5975   6287   3726    640   -939   -158       N  
ATOM   4431  CA  SER C 376       0.602 -19.550  45.536  1.00 42.22           C  
ANISOU 4431  CA  SER C 376     5982   6317   3743    677   -941   -168       C  
ATOM   4432  C   SER C 376       0.894 -18.054  45.366  1.00 42.18           C  
ANISOU 4432  C   SER C 376     5967   6304   3756    697   -950   -186       C  
ATOM   4433  O   SER C 376       0.137 -17.215  45.827  1.00 42.28           O  
ANISOU 4433  O   SER C 376     5968   6328   3768    712   -954   -192       O  
ATOM   4434  CB  SER C 376       1.342 -20.026  46.796  1.00 42.31           C  
ANISOU 4434  CB  SER C 376     5998   6330   3748    709   -933   -169       C  
ATOM   4435  OG  SER C 376       2.756 -20.108  46.620  1.00 42.20           O  
ANISOU 4435  OG  SER C 376     5991   6297   3745    718   -932   -174       O  
ATOM   4436  N   CYS C 377       2.034 -17.726  44.791  1.00 41.93           N  
ANISOU 4436  N   CYS C 377     5939   6253   3741    699   -953   -193       N  
ATOM   4437  CA  CYS C 377       2.346 -16.362  44.399  1.00 41.80           C  
ANISOU 4437  CA  CYS C 377     5915   6226   3742    711   -962   -209       C  
ATOM   4438  C   CYS C 377       2.155 -15.203  45.439  1.00 42.41           C  
ANISOU 4438  C   CYS C 377     5980   6311   3821    750   -965   -223       C  
ATOM   4439  O   CYS C 377       2.601 -15.245  46.609  1.00 42.67           O  
ANISOU 4439  O   CYS C 377     6014   6350   3850    783   -961   -227       O  
ATOM   4440  CB  CYS C 377       1.520 -16.079  43.169  1.00 41.75           C  
ANISOU 4440  CB  CYS C 377     5905   6219   3740    676   -969   -205       C  
ATOM   4441  SG  CYS C 377       1.445 -17.520  42.095  1.00 41.30           S  
ANISOU 4441  SG  CYS C 377     5860   6158   3675    629   -964   -188       S  
ATOM   4442  N   ALA C 378       1.539 -14.125  44.997  1.00 47.47           N  
ANISOU 4442  N   ALA C 378     6611   6954   4470    748   -974   -231       N  
ATOM   4443  CA  ALA C 378       1.255 -13.087  45.952  1.00 48.14           C  
ANISOU 4443  CA  ALA C 378     6685   7049   4556    783   -976   -243       C  
ATOM   4444  C   ALA C 378       0.345 -13.661  47.059  1.00 48.85           C  
ANISOU 4444  C   ALA C 378     6772   7161   4626    794   -970   -235       C  
ATOM   4445  O   ALA C 378       0.605 -13.521  48.278  1.00 49.30           O  
ANISOU 4445  O   ALA C 378     6826   7226   4678    828   -966   -241       O  
ATOM   4446  CB  ALA C 378       0.578 -11.865  45.243  1.00 48.48           C  
ANISOU 4446  CB  ALA C 378     6718   7092   4610    776   -986   -252       C  
ATOM   4447  N   VAL C 379      -0.705 -14.340  46.604  1.00 43.63           N  
ANISOU 4447  N   VAL C 379     6112   6511   3954    763   -968   -222       N  
ATOM   4448  CA  VAL C 379      -1.924 -14.365  47.378  1.00 44.52           C  
ANISOU 4448  CA  VAL C 379     6216   6646   4052    770   -966   -218       C  
ATOM   4449  C   VAL C 379      -1.961 -15.426  48.458  1.00 44.81           C  
ANISOU 4449  C   VAL C 379     6258   6695   4071    782   -956   -208       C  
ATOM   4450  O   VAL C 379      -2.738 -15.280  49.404  1.00 45.60           O  
ANISOU 4450  O   VAL C 379     6351   6815   4161    800   -954   -208       O  
ATOM   4451  CB  VAL C 379      -3.133 -14.518  46.440  1.00 44.73           C  
ANISOU 4451  CB  VAL C 379     6240   6680   4074    734   -970   -209       C  
ATOM   4452  CG1 VAL C 379      -2.710 -14.224  45.029  1.00 44.24           C  
ANISOU 4452  CG1 VAL C 379     6182   6599   4027    707   -977   -211       C  
ATOM   4453  CG2 VAL C 379      -3.696 -15.886  46.507  1.00 44.90           C  
ANISOU 4453  CG2 VAL C 379     6270   6712   4078    711   -963   -191       C  
ATOM   4454  N   ALA C 380      -1.101 -16.445  48.357  1.00 44.91           N  
ANISOU 4454  N   ALA C 380     6283   6698   4082    773   -950   -200       N  
ATOM   4455  CA  ALA C 380      -1.257 -17.659  49.166  1.00 45.23           C  
ANISOU 4455  CA  ALA C 380     6331   6751   4105    775   -940   -188       C  
ATOM   4456  C   ALA C 380      -0.015 -17.974  49.943  1.00 45.16           C  
ANISOU 4456  C   ALA C 380     6329   6734   4097    802   -934   -191       C  
ATOM   4457  O   ALA C 380       1.021 -18.288  49.353  1.00 44.60           O  
ANISOU 4457  O   ALA C 380     6267   6644   4035    793   -934   -191       O  
ATOM   4458  CB  ALA C 380      -1.605 -18.819  48.307  1.00 44.96           C  
ANISOU 4458  CB  ALA C 380     6306   6714   4062    734   -937   -171       C  
ATOM   4459  N   GLU C 381      -0.140 -17.961  51.268  1.00 47.55           N  
ANISOU 4459  N   GLU C 381     6627   7050   4390    834   -929   -193       N  
ATOM   4460  CA  GLU C 381       1.016 -17.865  52.154  1.00 47.56           C  
ANISOU 4460  CA  GLU C 381     6630   7045   4395    868   -925   -201       C  
ATOM   4461  C   GLU C 381       2.125 -18.947  52.096  1.00 47.02           C  
ANISOU 4461  C   GLU C 381     6577   6964   4326    863   -918   -193       C  
ATOM   4462  O   GLU C 381       3.226 -18.703  52.607  1.00 47.00           O  
ANISOU 4462  O   GLU C 381     6576   6951   4330    889   -917   -202       O  
ATOM   4463  CB  GLU C 381       0.504 -17.764  53.587  1.00 48.63           C  
ANISOU 4463  CB  GLU C 381     6759   7201   4518    900   -920   -202       C  
ATOM   4464  CG  GLU C 381      -0.401 -16.564  53.777  1.00 49.25           C  
ANISOU 4464  CG  GLU C 381     6823   7291   4599    913   -926   -213       C  
ATOM   4465  CD  GLU C 381      -0.479 -16.094  55.232  1.00 50.32           C  
ANISOU 4465  CD  GLU C 381     6950   7443   4728    954   -923   -221       C  
ATOM   4466  OE1 GLU C 381      -1.119 -16.784  56.060  1.00 50.90           O  
ANISOU 4466  OE1 GLU C 381     7023   7533   4784    959   -916   -211       O  
ATOM   4467  OE2 GLU C 381       0.110 -15.032  55.558  1.00 50.67           O  
ANISOU 4467  OE2 GLU C 381     6989   7481   4784    982   -927   -237       O  
ATOM   4468  N   TYR C 382       1.880 -20.123  51.514  1.00 44.08           N  
ANISOU 4468  N   TYR C 382     6214   6590   3944    830   -914   -178       N  
ATOM   4469  CA  TYR C 382       2.951 -21.137  51.457  1.00 43.66           C  
ANISOU 4469  CA  TYR C 382     6175   6524   3890    826   -907   -171       C  
ATOM   4470  C   TYR C 382       3.061 -21.913  50.150  1.00 42.96           C  
ANISOU 4470  C   TYR C 382     6096   6423   3803    784   -908   -161       C  
ATOM   4471  O   TYR C 382       2.120 -22.550  49.728  1.00 43.09           O  
ANISOU 4471  O   TYR C 382     6115   6449   3810    755   -906   -149       O  
ATOM   4472  CB  TYR C 382       2.794 -22.148  52.581  1.00 44.40           C  
ANISOU 4472  CB  TYR C 382     6273   6631   3965    838   -897   -160       C  
ATOM   4473  CG  TYR C 382       2.604 -21.568  53.943  1.00 45.24           C  
ANISOU 4473  CG  TYR C 382     6371   6753   4067    878   -895   -168       C  
ATOM   4474  CD1 TYR C 382       3.660 -21.402  54.787  1.00 45.35           C  
ANISOU 4474  CD1 TYR C 382     6386   6761   4085    911   -892   -176       C  
ATOM   4475  CD2 TYR C 382       1.360 -21.234  54.400  1.00 46.01           C  
ANISOU 4475  CD2 TYR C 382     6458   6870   4154    881   -896   -167       C  
ATOM   4476  CE1 TYR C 382       3.487 -20.899  56.046  1.00 46.25           C  
ANISOU 4476  CE1 TYR C 382     6491   6888   4192    947   -890   -183       C  
ATOM   4477  CE2 TYR C 382       1.175 -20.725  55.652  1.00 46.90           C  
ANISOU 4477  CE2 TYR C 382     6561   6997   4261    917   -893   -174       C  
ATOM   4478  CZ  TYR C 382       2.246 -20.560  56.477  1.00 47.02           C  
ANISOU 4478  CZ  TYR C 382     6578   7006   4280    950   -890   -182       C  
ATOM   4479  OH  TYR C 382       2.096 -20.053  57.752  1.00 48.00           O  
ANISOU 4479  OH  TYR C 382     6694   7145   4400    987   -888   -189       O  
ATOM   4480  N   GLY C 383       4.233 -21.888  49.535  1.00 45.46           N  
ANISOU 4480  N   GLY C 383     6419   6719   4133    781   -909   -166       N  
ATOM   4481  CA  GLY C 383       4.549 -22.837  48.486  1.00 45.03           C  
ANISOU 4481  CA  GLY C 383     6376   6653   4079    746   -907   -155       C  
ATOM   4482  C   GLY C 383       4.812 -24.127  49.227  1.00 45.46           C  
ANISOU 4482  C   GLY C 383     6441   6712   4118    750   -896   -143       C  
ATOM   4483  O   GLY C 383       5.160 -24.096  50.411  1.00 45.91           O  
ANISOU 4483  O   GLY C 383     6498   6776   4171    783   -892   -146       O  
ATOM   4484  N   VAL C 384       4.641 -25.262  48.562  1.00 47.84           N  
ANISOU 4484  N   VAL C 384     6753   7012   4412    716   -892   -129       N  
ATOM   4485  CA  VAL C 384       4.735 -26.544  49.260  1.00 48.37           C  
ANISOU 4485  CA  VAL C 384     6831   7086   4463    718   -881   -116       C  
ATOM   4486  C   VAL C 384       5.598 -27.555  48.491  1.00 48.02           C  
ANISOU 4486  C   VAL C 384     6800   7026   4420    695   -877   -108       C  
ATOM   4487  O   VAL C 384       5.484 -27.723  47.265  1.00 47.56           O  
ANISOU 4487  O   VAL C 384     6744   6959   4366    661   -880   -104       O  
ATOM   4488  CB  VAL C 384       3.302 -27.133  49.531  1.00 49.11           C  
ANISOU 4488  CB  VAL C 384     6922   7200   4537    701   -877   -103       C  
ATOM   4489  CG1 VAL C 384       2.700 -27.689  48.297  1.00 49.09           C  
ANISOU 4489  CG1 VAL C 384     6925   7195   4532    656   -878    -93       C  
ATOM   4490  CG2 VAL C 384       3.353 -28.231  50.529  1.00 49.78           C  
ANISOU 4490  CG2 VAL C 384     7016   7294   4605    711   -866    -92       C  
ATOM   4491  N   TYR C 385       6.474 -28.230  49.223  1.00 48.32           N  
ANISOU 4491  N   TYR C 385     6846   7059   4454    714   -869   -105       N  
ATOM   4492  CA  TYR C 385       7.480 -29.094  48.616  1.00 47.91           C  
ANISOU 4492  CA  TYR C 385     6807   6991   4405    699   -865   -100       C  
ATOM   4493  C   TYR C 385       7.291 -30.504  49.140  1.00 48.32           C  
ANISOU 4493  C   TYR C 385     6870   7051   4438    691   -854    -84       C  
ATOM   4494  O   TYR C 385       6.804 -30.674  50.271  1.00 48.96           O  
ANISOU 4494  O   TYR C 385     6949   7148   4507    711   -849    -81       O  
ATOM   4495  CB  TYR C 385       8.897 -28.571  48.927  1.00 47.79           C  
ANISOU 4495  CB  TYR C 385     6793   6960   4405    729   -866   -113       C  
ATOM   4496  CG  TYR C 385       9.101 -27.132  48.500  1.00 47.46           C  
ANISOU 4496  CG  TYR C 385     6740   6910   4381    740   -877   -129       C  
ATOM   4497  CD1 TYR C 385       8.651 -26.080  49.287  1.00 47.81           C  
ANISOU 4497  CD1 TYR C 385     6773   6966   4428    767   -881   -140       C  
ATOM   4498  CD2 TYR C 385       9.725 -26.823  47.304  1.00 46.80           C  
ANISOU 4498  CD2 TYR C 385     6659   6809   4313    722   -883   -134       C  
ATOM   4499  CE1 TYR C 385       8.813 -24.757  48.887  1.00 47.54           C  
ANISOU 4499  CE1 TYR C 385     6729   6924   4410    776   -891   -154       C  
ATOM   4500  CE2 TYR C 385       9.905 -25.507  46.899  1.00 46.52           C  
ANISOU 4500  CE2 TYR C 385     6614   6766   4295    731   -892   -149       C  
ATOM   4501  CZ  TYR C 385       9.438 -24.479  47.691  1.00 46.89           C  
ANISOU 4501  CZ  TYR C 385     6650   6824   4343    758   -897   -159       C  
ATOM   4502  OH  TYR C 385       9.596 -23.163  47.297  1.00 46.66           O  
ANISOU 4502  OH  TYR C 385     6611   6787   4330    767   -906   -173       O  
ATOM   4503  N   VAL C 386       7.657 -31.498  48.313  1.00 49.06           N  
ANISOU 4503  N   VAL C 386     6976   7135   4530    662   -849    -75       N  
ATOM   4504  CA  VAL C 386       7.757 -32.908  48.747  1.00 49.42           C  
ANISOU 4504  CA  VAL C 386     7034   7185   4559    656   -838    -60       C  
ATOM   4505  C   VAL C 386       9.186 -33.237  49.192  1.00 49.45           C  
ANISOU 4505  C   VAL C 386     7046   7175   4569    680   -834    -64       C  
ATOM   4506  O   VAL C 386      10.134 -33.084  48.422  1.00 48.92           O  
ANISOU 4506  O   VAL C 386     6983   7090   4516    674   -837    -70       O  
ATOM   4507  CB  VAL C 386       7.318 -33.928  47.642  1.00 49.15           C  
ANISOU 4507  CB  VAL C 386     7008   7148   4517    611   -835    -46       C  
ATOM   4508  CG1 VAL C 386       7.744 -33.488  46.268  1.00 48.40           C  
ANISOU 4508  CG1 VAL C 386     6912   7038   4439    588   -842    -53       C  
ATOM   4509  CG2 VAL C 386       7.900 -35.281  47.921  1.00 49.37           C  
ANISOU 4509  CG2 VAL C 386     7051   7172   4534    607   -824    -35       C  
ATOM   4510  N   LYS C 387       9.315 -33.673  50.445  1.00 49.80           N  
ANISOU 4510  N   LYS C 387     7093   7227   4602    706   -826    -60       N  
ATOM   4511  CA  LYS C 387      10.597 -33.973  51.047  1.00 49.98           C  
ANISOU 4511  CA  LYS C 387     7123   7239   4628    732   -822    -63       C  
ATOM   4512  C   LYS C 387      11.334 -34.956  50.160  1.00 49.60           C  
ANISOU 4512  C   LYS C 387     7088   7175   4581    708   -817    -56       C  
ATOM   4513  O   LYS C 387      10.729 -35.917  49.672  1.00 49.59           O  
ANISOU 4513  O   LYS C 387     7094   7179   4568    676   -812    -42       O  
ATOM   4514  CB  LYS C 387      10.400 -34.536  52.446  1.00 50.81           C  
ANISOU 4514  CB  LYS C 387     7231   7358   4717    757   -813    -56       C  
ATOM   4515  CG  LYS C 387       9.271 -33.866  53.148  1.00 51.20           C  
ANISOU 4515  CG  LYS C 387     7267   7427   4759    769   -815    -59       C  
ATOM   4516  CD  LYS C 387       8.821 -34.610  54.371  1.00 52.00           C  
ANISOU 4516  CD  LYS C 387     7372   7544   4841    785   -806    -48       C  
ATOM   4517  CE  LYS C 387       9.591 -34.192  55.622  1.00 52.54           C  
ANISOU 4517  CE  LYS C 387     7437   7614   4912    830   -804    -57       C  
ATOM   4518  NZ  LYS C 387       8.699 -34.190  56.828  1.00 53.35           N  
ANISOU 4518  NZ  LYS C 387     7533   7738   4999    849   -799    -53       N  
ATOM   4519  N   VAL C 388      12.623 -34.713  49.913  1.00 51.62           N  
ANISOU 4519  N   VAL C 388     7348   7414   4853    720   -819    -65       N  
ATOM   4520  CA  VAL C 388      13.354 -35.602  49.015  1.00 51.70           C  
ANISOU 4520  CA  VAL C 388     7370   7409   4865    697   -816    -59       C  
ATOM   4521  C   VAL C 388      13.724 -36.898  49.757  1.00 52.76           C  
ANISOU 4521  C   VAL C 388     7517   7545   4984    704   -804    -46       C  
ATOM   4522  O   VAL C 388      13.645 -37.990  49.190  1.00 53.26           O  
ANISOU 4522  O   VAL C 388     7590   7606   5039    676   -798    -34       O  
ATOM   4523  CB  VAL C 388      14.584 -34.914  48.421  1.00 51.06           C  
ANISOU 4523  CB  VAL C 388     7289   7308   4805    706   -822    -72       C  
ATOM   4524  CG1 VAL C 388      15.793 -35.848  48.422  1.00 51.57           C  
ANISOU 4524  CG1 VAL C 388     7366   7358   4869    710   -815    -68       C  
ATOM   4525  CG2 VAL C 388      14.252 -34.428  47.013  1.00 50.28           C  
ANISOU 4525  CG2 VAL C 388     7185   7202   4717    674   -830    -75       C  
ATOM   4526  N   THR C 389      14.057 -36.773  51.041  1.00 54.67           N  
ANISOU 4526  N   THR C 389     7757   7792   5222    740   -800    -50       N  
ATOM   4527  CA  THR C 389      14.316 -37.933  51.890  1.00 55.81           C  
ANISOU 4527  CA  THR C 389     7913   7941   5352    750   -789    -38       C  
ATOM   4528  C   THR C 389      13.218 -39.002  51.800  1.00 56.60           C  
ANISOU 4528  C   THR C 389     8019   8054   5432    721   -782    -21       C  
ATOM   4529  O   THR C 389      13.497 -40.192  51.928  1.00 57.56           O  
ANISOU 4529  O   THR C 389     8153   8174   5543    714   -772     -9       O  
ATOM   4530  CB  THR C 389      14.469 -37.509  53.352  1.00 56.26           C  
ANISOU 4530  CB  THR C 389     7965   8008   5405    792   -787    -44       C  
ATOM   4531  OG1 THR C 389      13.185 -37.176  53.894  1.00 56.96           O  
ANISOU 4531  OG1 THR C 389     8044   8116   5483    794   -788    -41       O  
ATOM   4532  CG2 THR C 389      15.356 -36.308  53.431  1.00 55.22           C  
ANISOU 4532  CG2 THR C 389     7825   7865   5291    819   -795    -62       C  
ATOM   4533  N   SER C 390      11.974 -38.583  51.580  1.00 56.87           N  
ANISOU 4533  N   SER C 390     8044   8102   5461    705   -786    -19       N  
ATOM   4534  CA  SER C 390      10.865 -39.531  51.475  1.00 57.65           C  
ANISOU 4534  CA  SER C 390     8149   8215   5542    677   -779     -3       C  
ATOM   4535  C   SER C 390      10.760 -40.246  50.117  1.00 57.55           C  
ANISOU 4535  C   SER C 390     8143   8193   5530    634   -778      5       C  
ATOM   4536  O   SER C 390      10.211 -41.333  50.050  1.00 58.43           O  
ANISOU 4536  O   SER C 390     8263   8312   5625    612   -770     20       O  
ATOM   4537  CB  SER C 390       9.544 -38.831  51.786  1.00 57.49           C  
ANISOU 4537  CB  SER C 390     8116   8212   5516    677   -784     -4       C  
ATOM   4538  OG  SER C 390       9.404 -38.665  53.189  1.00 58.01           O  
ANISOU 4538  OG  SER C 390     8177   8290   5573    712   -781     -5       O  
ATOM   4539  N   ILE C 391      11.267 -39.654  49.041  1.00 57.46           N  
ANISOU 4539  N   ILE C 391     8129   8169   5536    622   -786     -4       N  
ATOM   4540  CA  ILE C 391      11.366 -40.368  47.757  1.00 57.53           C  
ANISOU 4540  CA  ILE C 391     8145   8167   5545    584   -784      3       C  
ATOM   4541  C   ILE C 391      12.721 -41.043  47.528  1.00 57.94           C  
ANISOU 4541  C   ILE C 391     8208   8202   5603    588   -779      3       C  
ATOM   4542  O   ILE C 391      13.041 -41.403  46.390  1.00 57.93           O  
ANISOU 4542  O   ILE C 391     8212   8190   5608    561   -780      4       O  
ATOM   4543  CB  ILE C 391      11.125 -39.469  46.551  1.00 56.41           C  
ANISOU 4543  CB  ILE C 391     7995   8021   5419    563   -795     -6       C  
ATOM   4544  CG1 ILE C 391      11.915 -38.169  46.699  1.00 55.37           C  
ANISOU 4544  CG1 ILE C 391     7854   7878   5306    592   -804    -24       C  
ATOM   4545  CG2 ILE C 391       9.659 -39.209  46.396  1.00 56.38           C  
ANISOU 4545  CG2 ILE C 391     7982   8033   5405    543   -798     -2       C  
ATOM   4546  CD1 ILE C 391      12.459 -37.639  45.391  1.00 54.48           C  
ANISOU 4546  CD1 ILE C 391     7739   7750   5211    575   -812    -32       C  
ATOM   4547  N   GLN C 392      13.553 -41.098  48.568  1.00 61.14           N  
ANISOU 4547  N   GLN C 392     8618   8604   6009    623   -776      0       N  
ATOM   4548  CA  GLN C 392      14.895 -41.693  48.483  1.00 61.52           C  
ANISOU 4548  CA  GLN C 392     8677   8635   6062    632   -771     -1       C  
ATOM   4549  C   GLN C 392      14.957 -43.108  47.880  1.00 62.55           C  
ANISOU 4549  C   GLN C 392     8821   8762   6182    602   -761     13       C  
ATOM   4550  O   GLN C 392      15.525 -43.337  46.814  1.00 62.35           O  
ANISOU 4550  O   GLN C 392     8801   8724   6166    582   -762     12       O  
ATOM   4551  CB  GLN C 392      15.534 -41.738  49.882  1.00 62.13           C  
ANISOU 4551  CB  GLN C 392     8757   8714   6136    673   -766     -3       C  
ATOM   4552  CG  GLN C 392      16.317 -40.488  50.253  1.00 61.24           C  
ANISOU 4552  CG  GLN C 392     8635   8593   6040    706   -775    -21       C  
ATOM   4553  CD  GLN C 392      17.572 -40.341  49.420  1.00 60.79           C  
ANISOU 4553  CD  GLN C 392     8582   8514   6000    704   -778    -29       C  
ATOM   4554  OE1 GLN C 392      17.900 -41.231  48.621  1.00 60.19           O  
ANISOU 4554  OE1 GLN C 392     8517   8429   5923    679   -774    -21       O  
ATOM   4555  NE2 GLN C 392      18.295 -39.227  49.604  1.00 61.17           N  
ANISOU 4555  NE2 GLN C 392     8623   8554   6064    730   -786    -45       N  
ATOM   4556  N   ASP C 393      14.377 -44.068  48.581  1.00 60.84           N  
ANISOU 4556  N   ASP C 393     8611   8558   5946    600   -752     27       N  
ATOM   4557  CA  ASP C 393      14.555 -45.448  48.194  1.00 62.05           C  
ANISOU 4557  CA  ASP C 393     8779   8708   6089    577   -741     41       C  
ATOM   4558  C   ASP C 393      13.922 -45.716  46.855  1.00 61.82           C  
ANISOU 4558  C   ASP C 393     8749   8679   6060    534   -743     45       C  
ATOM   4559  O   ASP C 393      14.218 -46.727  46.237  1.00 62.60           O  
ANISOU 4559  O   ASP C 393     8859   8772   6155    513   -736     54       O  
ATOM   4560  CB  ASP C 393      13.996 -46.381  49.264  1.00 63.43           C  
ANISOU 4560  CB  ASP C 393     8961   8897   6243    584   -731     54       C  
ATOM   4561  CG  ASP C 393      14.827 -46.347  50.536  1.00 64.15           C  
ANISOU 4561  CG  ASP C 393     9055   8986   6334    626   -727     51       C  
ATOM   4562  OD1 ASP C 393      16.016 -46.775  50.492  1.00 64.22           O  
ANISOU 4562  OD1 ASP C 393     9073   8979   6349    636   -724     49       O  
ATOM   4563  OD2 ASP C 393      14.309 -45.876  51.572  1.00 64.72           O  
ANISOU 4563  OD2 ASP C 393     9119   9070   6400    649   -728     49       O  
ATOM   4564  N   TRP C 394      13.051 -44.824  46.403  1.00 58.03           N  
ANISOU 4564  N   TRP C 394     8257   8207   5585    522   -752     40       N  
ATOM   4565  CA  TRP C 394      12.449 -44.995  45.091  1.00 57.85           C  
ANISOU 4565  CA  TRP C 394     8232   8185   5562    481   -753     44       C  
ATOM   4566  C   TRP C 394      13.359 -44.503  43.980  1.00 57.10           C  
ANISOU 4566  C   TRP C 394     8135   8072   5487    474   -760     33       C  
ATOM   4567  O   TRP C 394      13.390 -45.102  42.901  1.00 57.46           O  
ANISOU 4567  O   TRP C 394     8186   8114   5534    443   -757     38       O  
ATOM   4568  CB  TRP C 394      11.107 -44.278  44.987  1.00 57.24           C  
ANISOU 4568  CB  TRP C 394     8143   8123   5481    468   -760     43       C  
ATOM   4569  CG  TRP C 394      10.609 -44.308  43.594  1.00 57.10           C  
ANISOU 4569  CG  TRP C 394     8123   8106   5468    429   -763     45       C  
ATOM   4570  CD1 TRP C 394      10.089 -45.378  42.951  1.00 58.18           C  
ANISOU 4570  CD1 TRP C 394     8265   8248   5591    394   -756     58       C  
ATOM   4571  CD2 TRP C 394      10.606 -43.228  42.648  1.00 55.97           C  
ANISOU 4571  CD2 TRP C 394     7968   7956   5341    419   -774     33       C  
ATOM   4572  NE1 TRP C 394       9.747 -45.046  41.663  1.00 57.80           N  
ANISOU 4572  NE1 TRP C 394     8211   8199   5551    364   -761     55       N  
ATOM   4573  CE2 TRP C 394      10.057 -43.731  41.446  1.00 56.45           C  
ANISOU 4573  CE2 TRP C 394     8030   8021   5399    379   -773     40       C  
ATOM   4574  CE3 TRP C 394      10.994 -41.884  42.702  1.00 54.71           C  
ANISOU 4574  CE3 TRP C 394     7799   7790   5199    442   -785     18       C  
ATOM   4575  CZ2 TRP C 394       9.887 -42.938  40.302  1.00 55.69           C  
ANISOU 4575  CZ2 TRP C 394     7923   7920   5316    360   -782     31       C  
ATOM   4576  CZ3 TRP C 394      10.832 -41.101  41.563  1.00 53.95           C  
ANISOU 4576  CZ3 TRP C 394     7693   7688   5116    423   -794     10       C  
ATOM   4577  CH2 TRP C 394      10.280 -41.631  40.380  1.00 54.44           C  
ANISOU 4577  CH2 TRP C 394     7756   7754   5175    382   -792     17       C  
ATOM   4578  N   VAL C 395      14.083 -43.402  44.226  1.00 60.79           N  
ANISOU 4578  N   VAL C 395     8596   8530   5971    502   -768     18       N  
ATOM   4579  CA  VAL C 395      14.880 -42.785  43.158  1.00 59.98           C  
ANISOU 4579  CA  VAL C 395     8490   8410   5888    495   -776      7       C  
ATOM   4580  C   VAL C 395      16.084 -43.669  42.952  1.00 60.77           C  
ANISOU 4580  C   VAL C 395     8604   8496   5991    497   -769     10       C  
ATOM   4581  O   VAL C 395      16.458 -43.954  41.824  1.00 60.82           O  
ANISOU 4581  O   VAL C 395     8613   8491   6004    474   -768      9       O  
ATOM   4582  CB  VAL C 395      15.312 -41.281  43.437  1.00 58.67           C  
ANISOU 4582  CB  VAL C 395     8313   8238   5740    524   -787    -10       C  
ATOM   4583  CG1 VAL C 395      14.201 -40.314  43.053  1.00 57.94           C  
ANISOU 4583  CG1 VAL C 395     8207   8156   5650    511   -796    -14       C  
ATOM   4584  CG2 VAL C 395      15.748 -41.044  44.866  1.00 58.60           C  
ANISOU 4584  CG2 VAL C 395     8305   8231   5728    566   -786    -14       C  
ATOM   4585  N   GLN C 396      16.662 -44.139  44.049  1.00 63.95           N  
ANISOU 4585  N   GLN C 396     9014   8896   6387    525   -762     12       N  
ATOM   4586  CA  GLN C 396      17.779 -45.058  43.959  1.00 64.94           C  
ANISOU 4586  CA  GLN C 396     9153   9009   6514    528   -755     16       C  
ATOM   4587  C   GLN C 396      17.364 -46.284  43.140  1.00 65.98           C  
ANISOU 4587  C   GLN C 396     9293   9144   6634    491   -746     29       C  
ATOM   4588  O   GLN C 396      18.064 -46.674  42.196  1.00 66.36           O  
ANISOU 4588  O   GLN C 396     9346   9177   6689    476   -745     28       O  
ATOM   4589  CB  GLN C 396      18.253 -45.463  45.349  1.00 65.82           C  
ANISOU 4589  CB  GLN C 396     9271   9121   6616    562   -748     19       C  
ATOM   4590  CG  GLN C 396      19.020 -44.373  46.085  1.00 65.29           C  
ANISOU 4590  CG  GLN C 396     9198   9048   6563    601   -755      4       C  
ATOM   4591  CD  GLN C 396      19.956 -44.958  47.147  1.00 65.40           C  
ANISOU 4591  CD  GLN C 396     9221   9056   6571    632   -748      6       C  
ATOM   4592  OE1 GLN C 396      19.803 -46.122  47.554  1.00 66.60           O  
ANISOU 4592  OE1 GLN C 396     9384   9214   6708    627   -737     20       O  
ATOM   4593  NE2 GLN C 396      20.943 -44.166  47.582  1.00 64.18           N  
ANISOU 4593  NE2 GLN C 396     9063   8891   6430    664   -753     -7       N  
ATOM   4594  N   LYS C 397      16.214 -46.861  43.491  1.00 60.45           N  
ANISOU 4594  N   LYS C 397     8593   8461   5916    477   -740     42       N  
ATOM   4595  CA  LYS C 397      15.664 -48.027  42.823  1.00 61.59           C  
ANISOU 4595  CA  LYS C 397     8744   8611   6046    442   -732     55       C  
ATOM   4596  C   LYS C 397      15.502 -47.799  41.319  1.00 61.03           C  
ANISOU 4596  C   LYS C 397     8668   8536   5986    409   -736     51       C  
ATOM   4597  O   LYS C 397      15.815 -48.671  40.514  1.00 61.92           O  
ANISOU 4597  O   LYS C 397     8788   8643   6097    388   -730     57       O  
ATOM   4598  CB  LYS C 397      14.310 -48.388  43.450  1.00 62.17           C  
ANISOU 4598  CB  LYS C 397     8816   8706   6101    433   -727     67       C  
ATOM   4599  CG  LYS C 397      13.791 -49.785  43.136  1.00 63.44           C  
ANISOU 4599  CG  LYS C 397     8986   8874   6243    404   -715     83       C  
ATOM   4600  CD  LYS C 397      12.301 -49.920  43.437  1.00 63.77           C  
ANISOU 4600  CD  LYS C 397     9023   8937   6268    387   -713     93       C  
ATOM   4601  CE  LYS C 397      11.433 -49.263  42.352  1.00 63.22           C  
ANISOU 4601  CE  LYS C 397     8942   8875   6204    357   -721     89       C  
ATOM   4602  NZ  LYS C 397      11.520 -49.915  40.997  1.00 63.37           N  
ANISOU 4602  NZ  LYS C 397     8962   8890   6224    323   -717     92       N  
ATOM   4603  N   THR C 398      15.015 -46.628  40.931  1.00 61.21           N  
ANISOU 4603  N   THR C 398     8677   8561   6018    406   -747     42       N  
ATOM   4604  CA  THR C 398      14.733 -46.369  39.520  1.00 60.74           C  
ANISOU 4604  CA  THR C 398     8611   8501   5968    374   -752     39       C  
ATOM   4605  C   THR C 398      16.012 -46.233  38.712  1.00 60.38           C  
ANISOU 4605  C   THR C 398     8568   8434   5939    377   -754     29       C  
ATOM   4606  O   THR C 398      16.082 -46.692  37.573  1.00 60.61           O  
ANISOU 4606  O   THR C 398     8599   8459   5972    350   -751     31       O  
ATOM   4607  CB  THR C 398      13.885 -45.086  39.333  1.00 59.52           C  
ANISOU 4607  CB  THR C 398     8442   8354   5820    371   -763     30       C  
ATOM   4608  OG1 THR C 398      12.680 -45.178  40.107  1.00 59.67           O  
ANISOU 4608  OG1 THR C 398     8457   8392   5822    370   -762     39       O  
ATOM   4609  CG2 THR C 398      13.533 -44.877  37.852  1.00 59.42           C  
ANISOU 4609  CG2 THR C 398     8421   8341   5815    337   -767     28       C  
ATOM   4610  N   ILE C 399      17.011 -45.592  39.325  1.00 63.72           N  
ANISOU 4610  N   ILE C 399     8993   8844   6375    410   -759     19       N  
ATOM   4611  CA  ILE C 399      18.302 -45.284  38.700  1.00 63.40           C  
ANISOU 4611  CA  ILE C 399     8954   8782   6352    418   -762      9       C  
ATOM   4612  C   ILE C 399      18.966 -46.532  38.147  1.00 64.70           C  
ANISOU 4612  C   ILE C 399     9132   8938   6514    404   -752     16       C  
ATOM   4613  O   ILE C 399      19.660 -46.489  37.113  1.00 64.69           O  
ANISOU 4613  O   ILE C 399     9132   8921   6525    392   -754     11       O  
ATOM   4614  CB  ILE C 399      19.285 -44.621  39.702  1.00 62.72           C  
ANISOU 4614  CB  ILE C 399     8870   8686   6276    460   -767     -1       C  
ATOM   4615  CG1 ILE C 399      18.845 -43.202  40.070  1.00 62.55           C  
ANISOU 4615  CG1 ILE C 399     8835   8669   6263    476   -778    -12       C  
ATOM   4616  CG2 ILE C 399      20.689 -44.537  39.106  1.00 61.89           C  
ANISOU 4616  CG2 ILE C 399     8770   8558   6187    467   -768    -10       C  
ATOM   4617  CD1 ILE C 399      18.997 -42.215  38.941  1.00 61.38           C  
ANISOU 4617  CD1 ILE C 399     8677   8511   6132    463   -788    -23       C  
ATOM   4618  N   ALA C 400      18.725 -47.638  38.854  1.00 62.74           N  
ANISOU 4618  N   ALA C 400     8893   8697   6247    405   -742     29       N  
ATOM   4619  CA  ALA C 400      19.201 -48.966  38.489  1.00 64.25           C  
ANISOU 4619  CA  ALA C 400     9098   8883   6432    391   -730     38       C  
ATOM   4620  C   ALA C 400      18.690 -49.456  37.117  1.00 64.80           C  
ANISOU 4620  C   ALA C 400     9165   8956   6499    352   -727     43       C  
ATOM   4621  O   ALA C 400      19.223 -50.402  36.569  1.00 65.97           O  
ANISOU 4621  O   ALA C 400     9323   9097   6647    341   -719     47       O  
ATOM   4622  CB  ALA C 400      18.817 -49.947  39.574  1.00 65.46           C  
ANISOU 4622  CB  ALA C 400     9260   9047   6564    399   -720     52       C  
ATOM   4623  N   GLU C 401      17.678 -48.819  36.548  1.00 63.18           N  
ANISOU 4623  N   GLU C 401     8947   8763   6296    332   -734     41       N  
ATOM   4624  CA  GLU C 401      17.259 -49.166  35.198  1.00 63.70           C  
ANISOU 4624  CA  GLU C 401     9009   8832   6362    298   -731     43       C  
ATOM   4625  C   GLU C 401      17.368 -47.980  34.241  1.00 62.60           C  
ANISOU 4625  C   GLU C 401     8858   8686   6243    291   -743     29       C  
ATOM   4626  O   GLU C 401      18.271 -47.927  33.412  1.00 62.24           O  
ANISOU 4626  O   GLU C 401     8814   8623   6210    289   -744     22       O  
ATOM   4627  CB  GLU C 401      15.825 -49.696  35.210  1.00 64.20           C  
ANISOU 4627  CB  GLU C 401     9068   8919   6407    273   -726     54       C  
ATOM   4628  CG  GLU C 401      15.646 -51.004  35.977  1.00 65.79           C  
ANISOU 4628  CG  GLU C 401     9280   9128   6588    274   -713     69       C  
ATOM   4629  CD  GLU C 401      15.157 -50.800  37.410  1.00 65.56           C  
ANISOU 4629  CD  GLU C 401     9253   9110   6548    296   -713     74       C  
ATOM   4630  OE1 GLU C 401      15.987 -50.406  38.256  1.00 64.89           O  
ANISOU 4630  OE1 GLU C 401     9173   9013   6470    328   -717     68       O  
ATOM   4631  OE2 GLU C 401      13.949 -51.043  37.685  1.00 66.14           O  
ANISOU 4631  OE2 GLU C 401     9322   9202   6606    281   -711     83       O  
TER    4632      GLU C 401                                                      
ATOM   4633  N   ALA D  86     -18.268  -2.027  75.025  1.00 81.26           N  
ANISOU 4633  N   ALA D  86    10102  10173  10599    533  -1903   2089       N  
ATOM   4634  CA  ALA D  86     -18.362  -2.868  73.835  1.00 78.78           C  
ANISOU 4634  CA  ALA D  86     9812   9830  10290    510  -1851   2100       C  
ATOM   4635  C   ALA D  86     -18.333  -2.049  72.536  1.00 74.37           C  
ANISOU 4635  C   ALA D  86     9217   9271   9771    470  -1886   2091       C  
ATOM   4636  O   ALA D  86     -17.565  -2.358  71.617  1.00 71.53           O  
ANISOU 4636  O   ALA D  86     8854   8903   9422    471  -1874   2118       O  
ATOM   4637  CB  ALA D  86     -19.628  -3.716  73.895  1.00 80.60           C  
ANISOU 4637  CB  ALA D  86    10088  10035  10503    488  -1793   2079       C  
ATOM   4638  N   ASP D  87     -19.185  -1.020  72.464  1.00 79.54           N  
ANISOU 4638  N   ASP D  87     9843   9932  10446    435  -1929   2053       N  
ATOM   4639  CA  ASP D  87     -19.338  -0.221  71.244  1.00 75.43           C  
ANISOU 4639  CA  ASP D  87     9288   9409   9962    392  -1961   2039       C  
ATOM   4640  C   ASP D  87     -18.502   1.071  71.260  1.00 75.11           C  
ANISOU 4640  C   ASP D  87     9192   9398   9947    400  -2038   2043       C  
ATOM   4641  O   ASP D  87     -18.580   1.906  70.333  1.00 72.12           O  
ANISOU 4641  O   ASP D  87     8778   9022   9601    366  -2075   2030       O  
ATOM   4642  CB  ASP D  87     -20.834   0.084  70.982  1.00 74.80           C  
ANISOU 4642  CB  ASP D  87     9212   9315   9892    343  -1958   1995       C  
ATOM   4643  CG  ASP D  87     -21.497   0.974  72.060  1.00 78.02           C  
ANISOU 4643  CG  ASP D  87     9602   9744  10299    343  -2002   1963       C  
ATOM   4644  OD1 ASP D  87     -20.885   1.968  72.539  1.00 80.85           O  
ANISOU 4644  OD1 ASP D  87     9921  10130  10668    360  -2064   1964       O  
ATOM   4645  OD2 ASP D  87     -22.678   0.688  72.394  1.00 77.71           O  
ANISOU 4645  OD2 ASP D  87     9588   9691  10247    324  -1975   1935       O  
ATOM   4646  N   GLU D  88     -17.725   1.242  72.327  1.00 75.16           N  
ANISOU 4646  N   GLU D  88     9190   9428   9939    445  -2063   2060       N  
ATOM   4647  CA  GLU D  88     -16.767   2.339  72.389  1.00 75.85           C  
ANISOU 4647  CA  GLU D  88     9229   9545  10047    460  -2131   2069       C  
ATOM   4648  C   GLU D  88     -15.572   1.975  71.493  1.00 74.37           C  
ANISOU 4648  C   GLU D  88     9035   9353   9868    473  -2121   2109       C  
ATOM   4649  O   GLU D  88     -15.157   2.783  70.657  1.00 72.69           O  
ANISOU 4649  O   GLU D  88     8783   9148   9686    454  -2163   2109       O  
ATOM   4650  CB  GLU D  88     -16.347   2.656  73.848  1.00 80.76           C  
ANISOU 4650  CB  GLU D  88     9844  10193  10650    503  -2161   2074       C  
ATOM   4651  CG  GLU D  88     -15.731   1.506  74.658  1.00 84.00           C  
ANISOU 4651  CG  GLU D  88    10292  10600  11023    552  -2114   2106       C  
ATOM   4652  CD  GLU D  88     -16.744   0.419  75.064  1.00 85.58           C  
ANISOU 4652  CD  GLU D  88    10545  10777  11194    547  -2048   2094       C  
ATOM   4653  OE1 GLU D  88     -17.920   0.756  75.358  1.00 85.97           O  
ANISOU 4653  OE1 GLU D  88    10597  10822  11244    520  -2053   2057       O  
ATOM   4654  OE2 GLU D  88     -16.362  -0.782  75.090  1.00 86.67           O  
ANISOU 4654  OE2 GLU D  88    10722  10899  11309    571  -1990   2122       O  
ATOM   4655  N   SER D  89     -15.036   0.765  71.651  1.00 71.55           N  
ANISOU 4655  N   SER D  89     8716   8984   9485    504  -2066   2141       N  
ATOM   4656  CA  SER D  89     -14.021   0.267  70.725  1.00 70.52           C  
ANISOU 4656  CA  SER D  89     8586   8846   9362    513  -2047   2177       C  
ATOM   4657  C   SER D  89     -14.258  -1.195  70.339  1.00 68.68           C  
ANISOU 4657  C   SER D  89     8407   8582   9108    513  -1966   2192       C  
ATOM   4658  O   SER D  89     -14.151  -2.105  71.178  1.00 70.90           O  
ANISOU 4658  O   SER D  89     8723   8858   9356    546  -1925   2207       O  
ATOM   4659  CB  SER D  89     -12.627   0.411  71.320  1.00 74.51           C  
ANISOU 4659  CB  SER D  89     9075   9375   9861    562  -2074   2212       C  
ATOM   4660  OG  SER D  89     -11.704  -0.360  70.578  1.00 75.88           O  
ANISOU 4660  OG  SER D  89     9260   9537  10033    577  -2041   2249       O  
ATOM   4661  N   LEU D  90     -14.536  -1.419  69.056  1.00 64.76           N  
ANISOU 4661  N   LEU D  90     7913   8064   8629    476  -1943   2190       N  
ATOM   4662  CA  LEU D  90     -14.901  -2.747  68.565  1.00 64.07           C  
ANISOU 4662  CA  LEU D  90     7875   7944   8524    469  -1867   2200       C  
ATOM   4663  C   LEU D  90     -13.674  -3.615  68.319  1.00 65.01           C  
ANISOU 4663  C   LEU D  90     8010   8059   8631    505  -1835   2246       C  
ATOM   4664  O   LEU D  90     -13.722  -4.824  68.519  1.00 65.98           O  
ANISOU 4664  O   LEU D  90     8179   8164   8727    522  -1773   2262       O  
ATOM   4665  CB  LEU D  90     -15.734  -2.621  67.293  1.00 63.80           C  
ANISOU 4665  CB  LEU D  90     7838   7889   8514    414  -1856   2178       C  
ATOM   4666  CG  LEU D  90     -16.403  -3.860  66.730  1.00 63.83           C  
ANISOU 4666  CG  LEU D  90     7890   7858   8503    396  -1781   2178       C  
ATOM   4667  CD1 LEU D  90     -17.869  -3.625  66.505  1.00 63.64           C  
ANISOU 4667  CD1 LEU D  90     7873   7820   8486    350  -1775   2136       C  
ATOM   4668  CD2 LEU D  90     -15.746  -4.176  65.429  1.00 63.74           C  
ANISOU 4668  CD2 LEU D  90     7877   7834   8509    385  -1765   2203       C  
ATOM   4669  N   LYS D  91     -12.570  -3.003  67.894  1.00 64.31           N  
ANISOU 4669  N   LYS D  91     7884   7988   8562    517  -1877   2268       N  
ATOM   4670  CA  LYS D  91     -11.342  -3.763  67.601  1.00 64.48           C  
ANISOU 4670  CA  LYS D  91     7917   8006   8575    550  -1850   2313       C  
ATOM   4671  C   LYS D  91     -10.614  -4.151  68.878  1.00 64.77           C  
ANISOU 4671  C   LYS D  91     7968   8059   8582    605  -1846   2337       C  
ATOM   4672  O   LYS D  91      -9.819  -5.079  68.868  1.00 64.96           O  
ANISOU 4672  O   LYS D  91     8016   8077   8589    636  -1807   2372       O  
ATOM   4673  CB  LYS D  91     -10.407  -2.983  66.672  1.00 64.33           C  
ANISOU 4673  CB  LYS D  91     7855   8000   8588    543  -1896   2329       C  
ATOM   4674  CG  LYS D  91      -9.778  -1.754  67.289  1.00 64.31           C  
ANISOU 4674  CG  LYS D  91     7804   8032   8599    562  -1971   2327       C  
ATOM   4675  CD  LYS D  91      -9.234  -0.799  66.222  1.00 64.09           C  
ANISOU 4675  CD  LYS D  91     7729   8013   8609    539  -2021   2330       C  
ATOM   4676  CE  LYS D  91      -7.865  -0.254  66.618  1.00 64.20           C  
ANISOU 4676  CE  LYS D  91     7710   8055   8627    579  -2068   2359       C  
ATOM   4677  NZ  LYS D  91      -7.313   0.658  65.584  1.00 63.98           N  
ANISOU 4677  NZ  LYS D  91     7638   8037   8636    558  -2115   2363       N  
ATOM   4678  N   ASP D  92     -10.888  -3.450  69.976  1.00 65.98           N  
ANISOU 4678  N   ASP D  92     8105   8234   8730    617  -1886   2318       N  
ATOM   4679  CA  ASP D  92     -10.441  -3.893  71.300  1.00 70.14           C  
ANISOU 4679  CA  ASP D  92     8650   8774   9225    666  -1876   2335       C  
ATOM   4680  C   ASP D  92     -11.366  -4.998  71.793  1.00 70.63           C  
ANISOU 4680  C   ASP D  92     8767   8814   9257    667  -1811   2325       C  
ATOM   4681  O   ASP D  92     -10.936  -5.913  72.501  1.00 73.67           O  
ANISOU 4681  O   ASP D  92     9184   9197   9612    705  -1773   2349       O  
ATOM   4682  CB  ASP D  92     -10.420  -2.736  72.307  1.00 72.92           C  
ANISOU 4682  CB  ASP D  92     8967   9157   9583    679  -1943   2317       C  
ATOM   4683  CG  ASP D  92      -9.243  -1.808  72.097  1.00 75.19           C  
ANISOU 4683  CG  ASP D  92     9207   9470   9892    694  -2003   2336       C  
ATOM   4684  OD1 ASP D  92      -8.080  -2.293  72.166  1.00 76.83           O  
ANISOU 4684  OD1 ASP D  92     9419   9683  10090    732  -1992   2375       O  
ATOM   4685  OD2 ASP D  92      -9.482  -0.598  71.846  1.00 75.61           O  
ANISOU 4685  OD2 ASP D  92     9218   9538   9973    668  -2062   2312       O  
ATOM   4686  N   ALA D  93     -12.641  -4.910  71.411  1.00 68.09           N  
ANISOU 4686  N   ALA D  93     8453   8475   8943    623  -1798   2289       N  
ATOM   4687  CA  ALA D  93     -13.636  -5.867  71.862  1.00 68.69           C  
ANISOU 4687  CA  ALA D  93     8578   8530   8992    618  -1740   2275       C  
ATOM   4688  C   ALA D  93     -13.318  -7.267  71.367  1.00 68.46           C  
ANISOU 4688  C   ALA D  93     8592   8475   8944    630  -1668   2305       C  
ATOM   4689  O   ALA D  93     -13.400  -8.219  72.135  1.00 70.59           O  
ANISOU 4689  O   ALA D  93     8902   8737   9182    657  -1622   2316       O  
ATOM   4690  CB  ALA D  93     -15.006  -5.446  71.413  1.00 67.68           C  
ANISOU 4690  CB  ALA D  93     8447   8389   8878    566  -1743   2232       C  
ATOM   4691  N   ILE D  94     -12.920  -7.402  70.105  1.00 66.77           N  
ANISOU 4691  N   ILE D  94     8371   8248   8749    611  -1658   2320       N  
ATOM   4692  CA  ILE D  94     -12.694  -8.739  69.545  1.00 67.34           C  
ANISOU 4692  CA  ILE D  94     8487   8294   8806    617  -1588   2346       C  
ATOM   4693  C   ILE D  94     -11.477  -9.442  70.167  1.00 69.13           C  
ANISOU 4693  C   ILE D  94     8728   8529   9008    673  -1569   2389       C  
ATOM   4694  O   ILE D  94     -11.260 -10.627  69.928  1.00 69.78           O  
ANISOU 4694  O   ILE D  94     8850   8592   9073    686  -1508   2412       O  
ATOM   4695  CB  ILE D  94     -12.541  -8.698  68.003  1.00 67.00           C  
ANISOU 4695  CB  ILE D  94     8431   8235   8790    583  -1582   2352       C  
ATOM   4696  CG1 ILE D  94     -11.233  -8.036  67.566  1.00 67.02           C  
ANISOU 4696  CG1 ILE D  94     8393   8258   8815    600  -1629   2378       C  
ATOM   4697  CG2 ILE D  94     -13.690  -7.933  67.400  1.00 66.09           C  
ANISOU 4697  CG2 ILE D  94     8298   8113   8700    529  -1605   2310       C  
ATOM   4698  CD1 ILE D  94     -11.099  -7.884  66.041  1.00 66.59           C  
ANISOU 4698  CD1 ILE D  94     8323   8190   8790    564  -1629   2382       C  
ATOM   4699  N   LYS D  95     -10.710  -8.719  70.984  1.00 69.22           N  
ANISOU 4699  N   LYS D  95     8709   8570   9020    705  -1620   2398       N  
ATOM   4700  CA  LYS D  95      -9.509  -9.259  71.612  1.00 72.50           C  
ANISOU 4700  CA  LYS D  95     9134   8998   9415    758  -1610   2438       C  
ATOM   4701  C   LYS D  95      -9.815 -10.249  72.732  1.00 76.46           C  
ANISOU 4701  C   LYS D  95     9682   9492   9878    789  -1562   2442       C  
ATOM   4702  O   LYS D  95      -8.945 -11.021  73.130  1.00 79.37           O  
ANISOU 4702  O   LYS D  95    10070   9862  10225    830  -1534   2477       O  
ATOM   4703  CB  LYS D  95      -8.641  -8.127  72.161  1.00 74.19           C  
ANISOU 4703  CB  LYS D  95     9300   9246   9642    782  -1682   2445       C  
ATOM   4704  CG  LYS D  95      -7.909  -7.319  71.092  1.00 71.60           C  
ANISOU 4704  CG  LYS D  95     8929   8927   9349    766  -1726   2454       C  
ATOM   4705  CD  LYS D  95      -7.088  -6.191  71.702  1.00 73.97           C  
ANISOU 4705  CD  LYS D  95     9182   9261   9661    790  -1798   2460       C  
ATOM   4706  CE  LYS D  95      -6.510  -5.285  70.627  1.00 72.24           C  
ANISOU 4706  CE  LYS D  95     8918   9052   9479    769  -1846   2464       C  
ATOM   4707  NZ  LYS D  95      -5.837  -4.088  71.213  1.00 74.99           N  
ANISOU 4707  NZ  LYS D  95     9218   9434   9840    787  -1919   2464       N  
ATOM   4708  N   ASP D  96     -11.040 -10.229  73.246  1.00 76.95           N  
ANISOU 4708  N   ASP D  96     9760   9548   9931    769  -1552   2408       N  
ATOM   4709  CA  ASP D  96     -11.455 -11.198  74.262  1.00 79.93           C  
ANISOU 4709  CA  ASP D  96    10182   9916  10271    793  -1503   2409       C  
ATOM   4710  C   ASP D  96     -11.439 -12.594  73.651  1.00 79.43           C  
ANISOU 4710  C   ASP D  96    10166   9823  10191    794  -1427   2431       C  
ATOM   4711  O   ASP D  96     -12.160 -12.868  72.694  1.00 76.23           O  
ANISOU 4711  O   ASP D  96     9774   9394   9797    754  -1398   2416       O  
ATOM   4712  CB  ASP D  96     -12.841 -10.835  74.810  1.00 79.33           C  
ANISOU 4712  CB  ASP D  96    10112   9837  10191    766  -1509   2365       C  
ATOM   4713  CG  ASP D  96     -13.390 -11.859  75.808  1.00 83.09           C  
ANISOU 4713  CG  ASP D  96    10638  10303  10630    787  -1455   2364       C  
ATOM   4714  OD1 ASP D  96     -14.600 -11.748  76.139  1.00 84.00           O  
ANISOU 4714  OD1 ASP D  96    10765  10412  10741    762  -1449   2329       O  
ATOM   4715  OD2 ASP D  96     -12.646 -12.762  76.257  1.00 85.37           O  
ANISOU 4715  OD2 ASP D  96    10953  10590  10894    828  -1420   2397       O  
ATOM   4716  N   PRO D  97     -10.589 -13.479  74.195  1.00 81.50           N  
ANISOU 4716  N   PRO D  97    10453  10085  10427    840  -1394   2466       N  
ATOM   4717  CA  PRO D  97     -10.412 -14.834  73.652  1.00 81.53           C  
ANISOU 4717  CA  PRO D  97    10501  10062  10414    846  -1322   2492       C  
ATOM   4718  C   PRO D  97     -11.643 -15.721  73.820  1.00 81.11           C  
ANISOU 4718  C   PRO D  97    10496   9983  10340    827  -1263   2471       C  
ATOM   4719  O   PRO D  97     -11.783 -16.722  73.118  1.00 79.86           O  
ANISOU 4719  O   PRO D  97    10371   9797  10174    817  -1205   2483       O  
ATOM   4720  CB  PRO D  97      -9.237 -15.389  74.467  1.00 85.97           C  
ANISOU 4720  CB  PRO D  97    11074  10637  10952    903  -1312   2531       C  
ATOM   4721  CG  PRO D  97      -9.251 -14.599  75.735  1.00 88.42           C  
ANISOU 4721  CG  PRO D  97    11364  10976  11256    925  -1361   2517       C  
ATOM   4722  CD  PRO D  97      -9.693 -13.221  75.336  1.00 85.45           C  
ANISOU 4722  CD  PRO D  97    10941  10614  10914    888  -1425   2486       C  
ATOM   4723  N   ALA D  98     -12.532 -15.353  74.733  1.00 80.91           N  
ANISOU 4723  N   ALA D  98    10472   9966  10306    822  -1278   2440       N  
ATOM   4724  CA  ALA D  98     -13.682 -16.190  75.023  1.00 81.87           C  
ANISOU 4724  CA  ALA D  98    10638  10064  10405    808  -1223   2420       C  
ATOM   4725  C   ALA D  98     -14.664 -16.200  73.857  1.00 78.31           C  
ANISOU 4725  C   ALA D  98    10192   9588   9973    753  -1204   2395       C  
ATOM   4726  O   ALA D  98     -15.578 -17.024  73.798  1.00 79.35           O  
ANISOU 4726  O   ALA D  98    10364   9696  10089    736  -1151   2383       O  
ATOM   4727  CB  ALA D  98     -14.368 -15.714  76.298  1.00 85.48           C  
ANISOU 4727  CB  ALA D  98    11094  10537  10849    816  -1247   2393       C  
ATOM   4728  N   LEU D  99     -14.481 -15.269  72.932  1.00 81.79           N  
ANISOU 4728  N   LEU D  99    10593  10036  10449    725  -1249   2388       N  
ATOM   4729  CA  LEU D  99     -15.478 -15.052  71.890  1.00 78.34           C  
ANISOU 4729  CA  LEU D  99    10153   9579  10033    671  -1242   2359       C  
ATOM   4730  C   LEU D  99     -15.160 -15.713  70.547  1.00 76.15           C  
ANISOU 4730  C   LEU D  99     9889   9278   9766    653  -1204   2379       C  
ATOM   4731  O   LEU D  99     -15.949 -15.554  69.599  1.00 73.37           O  
ANISOU 4731  O   LEU D  99     9535   8909   9433    607  -1197   2357       O  
ATOM   4732  CB  LEU D  99     -15.686 -13.549  71.664  1.00 75.96           C  
ANISOU 4732  CB  LEU D  99     9799   9299   9765    643  -1317   2332       C  
ATOM   4733  CG  LEU D  99     -16.523 -12.734  72.656  1.00 77.65           C  
ANISOU 4733  CG  LEU D  99     9998   9529   9977    636  -1355   2296       C  
ATOM   4734  CD1 LEU D  99     -16.621 -13.359  74.041  1.00 82.43           C  
ANISOU 4734  CD1 LEU D  99    10634  10139  10545    675  -1330   2301       C  
ATOM   4735  CD2 LEU D  99     -15.948 -11.329  72.767  1.00 76.59           C  
ANISOU 4735  CD2 LEU D  99     9807   9426   9869    639  -1435   2291       C  
ATOM   4736  N   GLU D 100     -14.032 -16.426  70.438  1.00 74.14           N  
ANISOU 4736  N   GLU D 100     9646   9022   9500    688  -1179   2420       N  
ATOM   4737  CA  GLU D 100     -13.600 -16.859  69.106  1.00 72.94           C  
ANISOU 4737  CA  GLU D 100     9498   8851   9363    672  -1153   2440       C  
ATOM   4738  C   GLU D 100     -14.244 -18.169  68.656  1.00 74.72           C  
ANISOU 4738  C   GLU D 100     9777   9043   9571    658  -1076   2442       C  
ATOM   4739  O   GLU D 100     -14.145 -19.205  69.315  1.00 78.47           O  
ANISOU 4739  O   GLU D 100    10292   9509  10014    688  -1027   2459       O  
ATOM   4740  CB  GLU D 100     -12.073 -16.953  69.015  1.00 73.66           C  
ANISOU 4740  CB  GLU D 100     9576   8957   9456    711  -1165   2483       C  
ATOM   4741  CG  GLU D 100     -11.372 -17.773  70.066  1.00 77.87           C  
ANISOU 4741  CG  GLU D 100    10137   9496   9955    765  -1137   2513       C  
ATOM   4742  CD  GLU D 100      -9.863 -17.733  69.869  1.00 78.48           C  
ANISOU 4742  CD  GLU D 100    10193   9587  10037    800  -1155   2554       C  
ATOM   4743  OE1 GLU D 100      -9.424 -16.977  68.966  1.00 75.67           O  
ANISOU 4743  OE1 GLU D 100     9801   9239   9713    781  -1194   2556       O  
ATOM   4744  OE2 GLU D 100      -9.124 -18.447  70.600  1.00 82.02           O  
ANISOU 4744  OE2 GLU D 100    10663  10040  10459    846  -1131   2584       O  
ATOM   4745  N   ASN D 101     -14.917 -18.077  67.512  1.00 72.77           N  
ANISOU 4745  N   ASN D 101     9528   8776   9344    611  -1066   2424       N  
ATOM   4746  CA  ASN D 101     -15.646 -19.178  66.901  1.00 74.27           C  
ANISOU 4746  CA  ASN D 101     9764   8933   9523    588   -997   2421       C  
ATOM   4747  C   ASN D 101     -16.671 -19.760  67.864  1.00 76.86           C  
ANISOU 4747  C   ASN D 101    10129   9251   9822    591   -961   2401       C  
ATOM   4748  O   ASN D 101     -17.017 -20.946  67.800  1.00 80.13           O  
ANISOU 4748  O   ASN D 101    10591   9641  10214    593   -896   2409       O  
ATOM   4749  CB  ASN D 101     -14.670 -20.233  66.406  1.00 76.76           C  
ANISOU 4749  CB  ASN D 101    10104   9235   9827    613   -950   2464       C  
ATOM   4750  CG  ASN D 101     -13.685 -19.666  65.405  1.00 74.50           C  
ANISOU 4750  CG  ASN D 101     9781   8957   9569    609   -985   2483       C  
ATOM   4751  OD1 ASN D 101     -12.600 -19.198  65.771  1.00 74.19           O  
ANISOU 4751  OD1 ASN D 101     9714   8942   9534    642  -1023   2506       O  
ATOM   4752  ND2 ASN D 101     -14.072 -19.669  64.132  1.00 73.31           N  
ANISOU 4752  ND2 ASN D 101     9628   8787   9440    567   -973   2475       N  
ATOM   4753  N   LYS D 102     -17.158 -18.894  68.750  1.00 73.92           N  
ANISOU 4753  N   LYS D 102     9736   8900   9452    590  -1006   2374       N  
ATOM   4754  CA  LYS D 102     -18.257 -19.215  69.644  1.00 76.47           C  
ANISOU 4754  CA  LYS D 102    10087   9216   9752    586   -982   2348       C  
ATOM   4755  C   LYS D 102     -19.534 -19.307  68.811  1.00 76.05           C  
ANISOU 4755  C   LYS D 102    10047   9138   9710    532   -958   2316       C  
ATOM   4756  O   LYS D 102     -19.617 -18.670  67.758  1.00 73.08           O  
ANISOU 4756  O   LYS D 102     9643   8759   9364    497   -984   2306       O  
ATOM   4757  CB  LYS D 102     -18.364 -18.155  70.733  1.00 75.51           C  
ANISOU 4757  CB  LYS D 102     9934   9125   9632    599  -1042   2328       C  
ATOM   4758  CG  LYS D 102     -19.350 -18.463  71.822  1.00 79.12           C  
ANISOU 4758  CG  LYS D 102    10419   9579  10064    603  -1022   2305       C  
ATOM   4759  CD  LYS D 102     -19.220 -17.454  72.933  1.00 79.25           C  
ANISOU 4759  CD  LYS D 102    10403   9627  10081    623  -1082   2292       C  
ATOM   4760  CE  LYS D 102     -20.424 -17.465  73.857  1.00 81.57           C  
ANISOU 4760  CE  LYS D 102    10715   9919  10357    614  -1073   2259       C  
ATOM   4761  NZ  LYS D 102     -20.562 -16.154  74.564  1.00 78.56           N  
ANISOU 4761  NZ  LYS D 102    10292   9567   9990    614  -1143   2235       N  
ATOM   4762  N   GLU D 103     -20.506 -20.112  69.252  1.00 76.69           N  
ANISOU 4762  N   GLU D 103    10171   9201   9767    526   -909   2301       N  
ATOM   4763  CA  GLU D 103     -21.764 -20.266  68.518  1.00 76.95           C  
ANISOU 4763  CA  GLU D 103    10220   9210   9809    475   -882   2271       C  
ATOM   4764  C   GLU D 103     -22.731 -19.125  68.790  1.00 74.27           C  
ANISOU 4764  C   GLU D 103     9850   8882   9486    444   -932   2228       C  
ATOM   4765  O   GLU D 103     -23.078 -18.854  69.942  1.00 75.62           O  
ANISOU 4765  O   GLU D 103    10021   9068   9642    461   -949   2213       O  
ATOM   4766  CB  GLU D 103     -22.454 -21.571  68.880  1.00 82.44           C  
ANISOU 4766  CB  GLU D 103    10972   9880  10472    480   -809   2271       C  
ATOM   4767  CG  GLU D 103     -21.572 -22.766  68.880  1.00 86.22           C  
ANISOU 4767  CG  GLU D 103    11485  10347  10928    516   -758   2312       C  
ATOM   4768  CD  GLU D 103     -22.303 -23.983  69.390  1.00 92.24           C  
ANISOU 4768  CD  GLU D 103    12303  11087  11657    522   -690   2309       C  
ATOM   4769  OE1 GLU D 103     -23.537 -23.891  69.575  1.00 93.26           O  
ANISOU 4769  OE1 GLU D 103    12443  11207  11784    493   -682   2275       O  
ATOM   4770  OE2 GLU D 103     -21.638 -25.025  69.609  1.00 96.33           O  
ANISOU 4770  OE2 GLU D 103    12853  11596  12151    557   -645   2342       O  
ATOM   4771  N   HIS D 104     -23.095 -18.407  67.738  1.00 75.77           N  
ANISOU 4771  N   HIS D 104    10013   9068   9708    400   -959   2209       N  
ATOM   4772  CA  HIS D 104     -24.191 -17.451  67.785  1.00 73.94           C  
ANISOU 4772  CA  HIS D 104     9758   8842   9494    362   -996   2166       C  
ATOM   4773  C   HIS D 104     -25.480 -17.932  67.077  1.00 75.52           C  
ANISOU 4773  C   HIS D 104     9986   9012   9696    315   -952   2140       C  
ATOM   4774  O   HIS D 104     -26.451 -17.176  66.999  1.00 74.73           O  
ANISOU 4774  O   HIS D 104     9869   8914   9612    279   -980   2103       O  
ATOM   4775  CB  HIS D 104     -23.723 -16.115  67.206  1.00 69.06           C  
ANISOU 4775  CB  HIS D 104     9083   8245   8913    346  -1067   2160       C  
ATOM   4776  CG  HIS D 104     -22.935 -16.254  65.946  1.00 67.24           C  
ANISOU 4776  CG  HIS D 104     8842   8004   8701    337  -1061   2185       C  
ATOM   4777  ND1 HIS D 104     -21.705 -16.873  65.905  1.00 67.38           N  
ANISOU 4777  ND1 HIS D 104     8868   8024   8708    376  -1043   2226       N  
ATOM   4778  CD2 HIS D 104     -23.205 -15.865  64.677  1.00 65.68           C  
ANISOU 4778  CD2 HIS D 104     8627   7796   8533    294  -1071   2173       C  
ATOM   4779  CE1 HIS D 104     -21.251 -16.867  64.663  1.00 66.00           C  
ANISOU 4779  CE1 HIS D 104     8682   7839   8555    357  -1041   2240       C  
ATOM   4780  NE2 HIS D 104     -22.139 -16.252  63.900  1.00 64.98           N  
ANISOU 4780  NE2 HIS D 104     8536   7702   8450    307  -1058   2208       N  
ATOM   4781  N   ASP D 105     -25.491 -19.154  66.534  1.00 77.17           N  
ANISOU 4781  N   ASP D 105    10237   9193   9890    314   -886   2158       N  
ATOM   4782  CA  ASP D 105     -26.579 -19.563  65.621  1.00 78.37           C  
ANISOU 4782  CA  ASP D 105    10411   9316  10049    266   -848   2137       C  
ATOM   4783  C   ASP D 105     -27.724 -20.366  66.235  1.00 83.30           C  
ANISOU 4783  C   ASP D 105    11082   9923  10647    259   -797   2117       C  
ATOM   4784  O   ASP D 105     -28.615 -20.817  65.521  1.00 85.25           O  
ANISOU 4784  O   ASP D 105    11350  10144  10896    222   -760   2101       O  
ATOM   4785  CB  ASP D 105     -26.016 -20.362  64.447  1.00 78.80           C  
ANISOU 4785  CB  ASP D 105    10484   9349  10109    260   -806   2165       C  
ATOM   4786  CG  ASP D 105     -25.559 -21.747  64.848  1.00 83.29           C  
ANISOU 4786  CG  ASP D 105    11100   9903  10643    297   -742   2196       C  
ATOM   4787  OD1 ASP D 105     -25.609 -22.082  66.057  1.00 85.72           O  
ANISOU 4787  OD1 ASP D 105    11427  10220  10924    330   -732   2198       O  
ATOM   4788  OD2 ASP D 105     -25.122 -22.502  63.945  1.00 84.70           O  
ANISOU 4788  OD2 ASP D 105    11298  10063  10823    295   -703   2220       O  
ATOM   4789  N   ILE D 106     -27.682 -20.574  67.543  1.00 78.01           N  
ANISOU 4789  N   ILE D 106    10425   9265   9950    295   -795   2120       N  
ATOM   4790  CA  ILE D 106     -28.722 -21.345  68.225  1.00 83.12           C  
ANISOU 4790  CA  ILE D 106    11115   9897  10569    293   -747   2103       C  
ATOM   4791  C   ILE D 106     -30.042 -20.594  68.309  1.00 82.05           C  
ANISOU 4791  C   ILE D 106    10967   9762  10446    251   -772   2057       C  
ATOM   4792  O   ILE D 106     -30.073 -19.442  68.731  1.00 77.76           O  
ANISOU 4792  O   ILE D 106    10384   9243   9919    249   -833   2039       O  
ATOM   4793  CB  ILE D 106     -28.276 -21.723  69.647  1.00 85.81           C  
ANISOU 4793  CB  ILE D 106    11472  10253  10879    344   -741   2118       C  
ATOM   4794  CG1 ILE D 106     -27.202 -22.808  69.580  1.00 86.09           C  
ANISOU 4794  CG1 ILE D 106    11536  10281  10895    383   -697   2162       C  
ATOM   4795  CG2 ILE D 106     -29.459 -22.175  70.490  1.00 91.77           C  
ANISOU 4795  CG2 ILE D 106    12260  10998  11609    338   -710   2092       C  
ATOM   4796  CD1 ILE D 106     -26.324 -22.860  70.808  1.00 86.79           C  
ANISOU 4796  CD1 ILE D 106    11623  10392  10962    438   -711   2185       C  
ATOM   4797  N   GLY D 107     -31.132 -21.251  67.925  1.00 77.33           N  
ANISOU 4797  N   GLY D 107    10402   9137   9841    219   -724   2039       N  
ATOM   4798  CA  GLY D 107     -32.458 -20.676  68.076  1.00 77.36           C  
ANISOU 4798  CA  GLY D 107    10400   9139   9853    181   -739   1995       C  
ATOM   4799  C   GLY D 107     -33.143 -20.241  66.801  1.00 74.74           C  
ANISOU 4799  C   GLY D 107    10053   8792   9552    126   -747   1973       C  
ATOM   4800  O   GLY D 107     -32.573 -20.352  65.717  1.00 74.59           O  
ANISOU 4800  O   GLY D 107    10026   8764   9549    115   -741   1991       O  
ATOM   4801  N   PRO D 108     -34.391 -19.763  66.933  1.00 80.20           N  
ANISOU 4801  N   PRO D 108    10741   9481  10249     91   -758   1933       N  
ATOM   4802  CA  PRO D 108     -35.256 -19.301  65.840  1.00 79.37           C  
ANISOU 4802  CA  PRO D 108    10622   9362  10172     35   -766   1906       C  
ATOM   4803  C   PRO D 108     -34.848 -17.912  65.346  1.00 73.38           C  
ANISOU 4803  C   PRO D 108     9806   8625   9450     20   -839   1897       C  
ATOM   4804  O   PRO D 108     -34.429 -17.058  66.148  1.00 71.13           O  
ANISOU 4804  O   PRO D 108     9490   8369   9168     42   -892   1894       O  
ATOM   4805  CB  PRO D 108     -36.639 -19.271  66.484  1.00 83.99           C  
ANISOU 4805  CB  PRO D 108    11225   9942  10747     14   -756   1869       C  
ATOM   4806  CG  PRO D 108     -36.362 -18.953  67.914  1.00 84.26           C  
ANISOU 4806  CG  PRO D 108    11251  10001  10762     55   -783   1869       C  
ATOM   4807  CD  PRO D 108     -35.033 -19.592  68.248  1.00 83.46           C  
ANISOU 4807  CD  PRO D 108    11161   9907  10643    105   -767   1913       C  
ATOM   4808  N   ARG D 109     -34.977 -17.675  64.043  1.00 79.75           N  
ANISOU 4808  N   ARG D 109     8201   9291  12810    412     83     86       N  
ATOM   4809  CA  ARG D 109     -34.404 -16.470  63.443  1.00 74.19           C  
ANISOU 4809  CA  ARG D 109     7568   8553  12069    455    104     79       C  
ATOM   4810  C   ARG D 109     -35.148 -16.087  62.183  1.00 74.71           C  
ANISOU 4810  C   ARG D 109     7649   8621  12117    527     91     46       C  
ATOM   4811  O   ARG D 109     -35.720 -16.948  61.524  1.00 79.46           O  
ANISOU 4811  O   ARG D 109     8212   9235  12744    539     63     33       O  
ATOM   4812  CB  ARG D 109     -32.914 -16.686  63.123  1.00 70.02           C  
ANISOU 4812  CB  ARG D 109     7075   7976  11555    427    109    102       C  
ATOM   4813  CG  ARG D 109     -32.636 -17.509  61.859  1.00 71.39           C  
ANISOU 4813  CG  ARG D 109     7244   8126  11756    443     82     95       C  
ATOM   4814  CD  ARG D 109     -31.253 -18.129  61.913  1.00 69.05           C  
ANISOU 4814  CD  ARG D 109     6958   7791  11486    393     83    124       C  
ATOM   4815  NE  ARG D 109     -30.661 -18.331  60.588  1.00 68.48           N  
ANISOU 4815  NE  ARG D 109     6915   7683  11423    421     70    117       N  
ATOM   4816  CZ  ARG D 109     -29.413 -18.758  60.385  1.00 66.88           C  
ANISOU 4816  CZ  ARG D 109     6730   7442  11240    388     71    139       C  
ATOM   4817  NH1 ARG D 109     -28.632 -19.037  61.424  1.00 65.64           N  
ANISOU 4817  NH1 ARG D 109     6566   7278  11097    327     83    168       N  
ATOM   4818  NH2 ARG D 109     -28.952 -18.912  59.147  1.00 66.92           N  
ANISOU 4818  NH2 ARG D 109     6760   7414  11251    417     59    130       N  
ATOM   4819  N   GLU D 110     -35.135 -14.807  61.839  1.00 71.80           N  
ANISOU 4819  N   GLU D 110     7336   8238  11705    576    111     33       N  
ATOM   4820  CA  GLU D 110     -35.722 -14.365  60.587  1.00 72.35           C  
ANISOU 4820  CA  GLU D 110     7428   8306  11757    647    101      2       C  
ATOM   4821  C   GLU D 110     -34.607 -13.808  59.763  1.00 67.81           C  
ANISOU 4821  C   GLU D 110     6918   7680  11168    667    112      7       C  
ATOM   4822  O   GLU D 110     -33.636 -13.326  60.330  1.00 63.89           O  
ANISOU 4822  O   GLU D 110     6456   7158  10660    638    136     28       O  
ATOM   4823  CB  GLU D 110     -36.797 -13.305  60.823  1.00 72.83           C  
ANISOU 4823  CB  GLU D 110     7498   8396  11777    694    114    -21       C  
ATOM   4824  CG  GLU D 110     -37.646 -12.977  59.608  1.00 73.81           C  
ANISOU 4824  CG  GLU D 110     7633   8527  11884    767     99    -55       C  
ATOM   4825  CD  GLU D 110     -38.686 -11.919  59.919  1.00 74.90           C  
ANISOU 4825  CD  GLU D 110     7781   8696  11983    810    113    -76       C  
ATOM   4826  OE1 GLU D 110     -39.886 -12.144  59.632  1.00 76.67           O  
ANISOU 4826  OE1 GLU D 110     7968   8955  12207    842     94   -100       O  
ATOM   4827  OE2 GLU D 110     -38.306 -10.853  60.455  1.00 74.33           O  
ANISOU 4827  OE2 GLU D 110     7752   8612  11877    813    142    -69       O  
ATOM   4828  N   GLN D 111     -34.722 -13.842  58.440  1.00 68.84           N  
ANISOU 4828  N   GLN D 111     7066   7794  11296    717     97    -13       N  
ATOM   4829  CA  GLN D 111     -33.721 -13.166  57.600  1.00 65.09           C  
ANISOU 4829  CA  GLN D 111     6658   7271  10803    744    109    -12       C  
ATOM   4830  C   GLN D 111     -34.262 -11.922  56.902  1.00 64.13           C  
ANISOU 4830  C   GLN D 111     6583   7147  10635    817    121    -39       C  
ATOM   4831  O   GLN D 111     -35.094 -12.019  56.006  1.00 67.41           O  
ANISOU 4831  O   GLN D 111     6988   7575  11048    867    102    -65       O  
ATOM   4832  CB  GLN D 111     -33.179 -14.138  56.574  1.00 66.71           C  
ANISOU 4832  CB  GLN D 111     6855   7450  11041    740     85     -9       C  
ATOM   4833  CG  GLN D 111     -32.662 -15.386  57.228  1.00 67.61           C  
ANISOU 4833  CG  GLN D 111     6923   7566  11201    669     73     17       C  
ATOM   4834  CD  GLN D 111     -31.971 -16.292  56.261  1.00 69.15           C  
ANISOU 4834  CD  GLN D 111     7115   7730  11428    662     52     22       C  
ATOM   4835  OE1 GLN D 111     -30.742 -16.355  56.241  1.00 66.88           O  
ANISOU 4835  OE1 GLN D 111     6857   7404  11149    633     62     43       O  
ATOM   4836  NE2 GLN D 111     -32.752 -17.011  55.448  1.00 73.41           N  
ANISOU 4836  NE2 GLN D 111     7619   8286  11987    689     23      2       N  
ATOM   4837  N   VAL D 112     -33.797 -10.751  57.313  1.00 62.42           N  
ANISOU 4837  N   VAL D 112     6420   6915  10383    825    152    -33       N  
ATOM   4838  CA  VAL D 112     -34.323  -9.509  56.757  1.00 61.61           C  
ANISOU 4838  CA  VAL D 112     6363   6812  10235    893    165    -58       C  
ATOM   4839  C   VAL D 112     -33.280  -8.727  55.960  1.00 58.31           C  
ANISOU 4839  C   VAL D 112     6018   6343   9794    920    182    -56       C  
ATOM   4840  O   VAL D 112     -32.319  -8.201  56.540  1.00 54.98           O  
ANISOU 4840  O   VAL D 112     5632   5897   9361    891    208    -36       O  
ATOM   4841  CB  VAL D 112     -34.859  -8.596  57.864  1.00 60.62           C  
ANISOU 4841  CB  VAL D 112     6241   6713  10077    892    189    -59       C  
ATOM   4842  CG1 VAL D 112     -35.626  -7.452  57.256  1.00 60.49           C  
ANISOU 4842  CG1 VAL D 112     6262   6704  10019    965    198    -88       C  
ATOM   4843  CG2 VAL D 112     -35.715  -9.388  58.824  1.00 63.99           C  
ANISOU 4843  CG2 VAL D 112     6597   7187  10528    854    176    -55       C  
ATOM   4844  N   ASN D 113     -33.478  -8.630  54.648  1.00 60.90           N  
ANISOU 4844  N   ASN D 113     6368   6656  10116    975    169    -77       N  
ATOM   4845  CA  ASN D 113     -32.663  -7.734  53.831  1.00 58.54           C  
ANISOU 4845  CA  ASN D 113     6142   6312   9790   1010    186    -79       C  
ATOM   4846  C   ASN D 113     -32.750  -6.305  54.337  1.00 55.97           C  
ANISOU 4846  C   ASN D 113     5863   5987   9416   1034    219    -84       C  
ATOM   4847  O   ASN D 113     -33.826  -5.874  54.804  1.00 56.77           O  
ANISOU 4847  O   ASN D 113     5944   6127   9500   1053    221    -98       O  
ATOM   4848  CB  ASN D 113     -33.106  -7.760  52.373  1.00 61.35           C  
ANISOU 4848  CB  ASN D 113     6513   6657  10140   1073    167   -105       C  
ATOM   4849  CG  ASN D 113     -32.840  -9.073  51.714  1.00 64.07           C  
ANISOU 4849  CG  ASN D 113     6816   6998  10529   1054    135   -103       C  
ATOM   4850  OD1 ASN D 113     -31.870  -9.214  50.963  1.00 65.92           O  
ANISOU 4850  OD1 ASN D 113     6990   7269  10789   1043    112   -110       O  
ATOM   4851  ND2 ASN D 113     -33.692 -10.058  51.985  1.00 64.73           N  
ANISOU 4851  ND2 ASN D 113     6933   7038  10625   1049    134    -93       N  
ATOM   4852  N   PHE D 114     -31.639  -5.569  54.233  1.00 54.64           N  
ANISOU 4852  N   PHE D 114     5756   5776   9228   1034    244    -73       N  
ATOM   4853  CA  PHE D 114     -31.633  -4.158  54.577  1.00 54.72           C  
ANISOU 4853  CA  PHE D 114     5818   5780   9192   1061    276    -78       C  
ATOM   4854  C   PHE D 114     -30.845  -3.378  53.549  1.00 54.62           C  
ANISOU 4854  C   PHE D 114     5878   5721   9156   1102    289    -83       C  
ATOM   4855  O   PHE D 114     -30.183  -3.952  52.698  1.00 54.47           O  
ANISOU 4855  O   PHE D 114     5867   5672   9157   1100    276    -80       O  
ATOM   4856  CB  PHE D 114     -31.049  -3.936  55.959  1.00 54.59           C  
ANISOU 4856  CB  PHE D 114     5801   5766   9174   1002    300    -52       C  
ATOM   4857  CG  PHE D 114     -29.662  -4.450  56.100  1.00 54.27           C  
ANISOU 4857  CG  PHE D 114     5772   5690   9159    949    305    -24       C  
ATOM   4858  CD1 PHE D 114     -28.591  -3.730  55.615  1.00 54.11           C  
ANISOU 4858  CD1 PHE D 114     5818   5622   9120    960    326    -19       C  
ATOM   4859  CD2 PHE D 114     -29.417  -5.666  56.717  1.00 54.14           C  
ANISOU 4859  CD2 PHE D 114     5701   5684   9186    886    289     -4       C  
ATOM   4860  CE1 PHE D 114     -27.318  -4.199  55.744  1.00 53.83           C  
ANISOU 4860  CE1 PHE D 114     5792   5553   9107    911    331      6       C  
ATOM   4861  CE2 PHE D 114     -28.130  -6.141  56.852  1.00 53.85           C  
ANISOU 4861  CE2 PHE D 114     5675   5614   9173    837    293     21       C  
ATOM   4862  CZ  PHE D 114     -27.086  -5.404  56.366  1.00 53.70           C  
ANISOU 4862  CZ  PHE D 114     5720   5549   9133    850    314     26       C  
ATOM   4863  N   GLN D 115     -30.948  -2.061  53.629  1.00 53.79           N  
ANISOU 4863  N   GLN D 115     5823   5610   9005   1139    316    -93       N  
ATOM   4864  CA  GLN D 115     -30.070  -1.178  52.897  1.00 53.69           C  
ANISOU 4864  CA  GLN D 115     5883   5550   8965   1169    337    -94       C  
ATOM   4865  C   GLN D 115     -29.271  -0.343  53.897  1.00 53.56           C  
ANISOU 4865  C   GLN D 115     5904   5518   8928   1135    373    -75       C  
ATOM   4866  O   GLN D 115     -29.710  -0.088  55.023  1.00 53.64           O  
ANISOU 4866  O   GLN D 115     5893   5558   8930   1112    385    -69       O  
ATOM   4867  CB  GLN D 115     -30.850  -0.287  51.932  1.00 53.92           C  
ANISOU 4867  CB  GLN D 115     5949   5581   8958   1249    337   -125       C  
ATOM   4868  CG  GLN D 115     -31.074  -0.908  50.554  1.00 53.96           C  
ANISOU 4868  CG  GLN D 115     5948   5576   8978   1288    308   -142       C  
ATOM   4869  CD  GLN D 115     -31.597   0.094  49.511  1.00 54.16           C  
ANISOU 4869  CD  GLN D 115     6022   5592   8963   1369    313   -170       C  
ATOM   4870  OE1 GLN D 115     -32.225   1.095  49.852  1.00 54.35           O  
ANISOU 4870  OE1 GLN D 115     6066   5633   8950   1402    330   -182       O  
ATOM   4871  NE2 GLN D 115     -31.338  -0.185  48.237  1.00 54.12           N  
ANISOU 4871  NE2 GLN D 115     6036   5561   8965   1402    297   -180       N  
ATOM   4872  N   LEU D 116     -28.069   0.035  53.482  1.00 54.18           N  
ANISOU 4872  N   LEU D 116     6037   5549   9000   1131    390    -64       N  
ATOM   4873  CA  LEU D 116     -27.201   0.906  54.254  1.00 53.61           C  
ANISOU 4873  CA  LEU D 116     6008   5455   8905   1105    425    -47       C  
ATOM   4874  C   LEU D 116     -26.956   2.178  53.437  1.00 53.66           C  
ANISOU 4874  C   LEU D 116     6091   5430   8868   1164    447    -63       C  
ATOM   4875  O   LEU D 116     -26.333   2.100  52.364  1.00 53.55           O  
ANISOU 4875  O   LEU D 116     6110   5380   8858   1185    442    -66       O  
ATOM   4876  CB  LEU D 116     -25.875   0.206  54.568  1.00 53.29           C  
ANISOU 4876  CB  LEU D 116     5966   5385   8897   1041    427    -18       C  
ATOM   4877  CG  LEU D 116     -25.797  -0.795  55.726  1.00 53.19           C  
ANISOU 4877  CG  LEU D 116     5891   5398   8920    969    418      4       C  
ATOM   4878  CD1 LEU D 116     -24.572  -1.584  55.603  1.00 52.90           C  
ANISOU 4878  CD1 LEU D 116     5854   5328   8917    921    413     27       C  
ATOM   4879  CD2 LEU D 116     -25.788  -0.123  57.080  1.00 53.21           C  
ANISOU 4879  CD2 LEU D 116     5896   5417   8903    938    445     17       C  
ATOM   4880  N   LEU D 117     -27.445   3.326  53.932  1.00 55.15           N  
ANISOU 4880  N   LEU D 117     6306   5632   9017   1191    472    -72       N  
ATOM   4881  CA  LEU D 117     -27.380   4.595  53.203  1.00 56.10           C  
ANISOU 4881  CA  LEU D 117     6496   5726   9092   1252    493    -89       C  
ATOM   4882  C   LEU D 117     -26.764   5.737  54.026  1.00 55.45           C  
ANISOU 4882  C   LEU D 117     6462   5628   8978   1237    533    -78       C  
ATOM   4883  O   LEU D 117     -26.839   5.733  55.260  1.00 55.17           O  
ANISOU 4883  O   LEU D 117     6400   5616   8946   1194    544    -64       O  
ATOM   4884  CB  LEU D 117     -28.774   5.010  52.757  1.00 57.92           C  
ANISOU 4884  CB  LEU D 117     6718   5989   9299   1316    482   -118       C  
ATOM   4885  CG  LEU D 117     -29.801   3.976  52.309  1.00 59.41           C  
ANISOU 4885  CG  LEU D 117     6846   6212   9516   1330    444   -132       C  
ATOM   4886  CD1 LEU D 117     -31.181   4.568  52.534  1.00 60.45           C  
ANISOU 4886  CD1 LEU D 117     6963   6385   9620   1374    443   -155       C  
ATOM   4887  CD2 LEU D 117     -29.618   3.613  50.846  1.00 61.76           C  
ANISOU 4887  CD2 LEU D 117     7161   6483   9822   1369    423   -145       C  
ATOM   4888  N   ASP D 118     -26.175   6.721  53.344  1.00 57.57           N  
ANISOU 4888  N   ASP D 118     6801   5858   9215   1275    555    -84       N  
ATOM   4889  CA  ASP D 118     -25.622   7.911  54.009  1.00 58.03           C  
ANISOU 4889  CA  ASP D 118     6911   5899   9238   1269    594    -77       C  
ATOM   4890  C   ASP D 118     -26.683   9.027  54.145  1.00 60.42           C  
ANISOU 4890  C   ASP D 118     7233   6226   9498   1323    608    -98       C  
ATOM   4891  O   ASP D 118     -27.862   8.778  53.942  1.00 61.32           O  
ANISOU 4891  O   ASP D 118     7311   6376   9612   1354    587   -116       O  
ATOM   4892  CB  ASP D 118     -24.388   8.433  53.263  1.00 58.83           C  
ANISOU 4892  CB  ASP D 118     7080   5944   9327   1278    613    -72       C  
ATOM   4893  CG  ASP D 118     -24.737   9.117  51.944  1.00 61.76           C  
ANISOU 4893  CG  ASP D 118     7499   6297   9669   1355    613    -97       C  
ATOM   4894  OD1 ASP D 118     -25.821   8.856  51.390  1.00 62.87           O  
ANISOU 4894  OD1 ASP D 118     7613   6464   9809   1397    589   -118       O  
ATOM   4895  OD2 ASP D 118     -23.916   9.918  51.449  1.00 63.35           O  
ANISOU 4895  OD2 ASP D 118     7767   6457   9848   1373    636    -97       O  
ATOM   4896  N   LYS D 119     -26.278  10.249  54.493  1.00 58.69           N  
ANISOU 4896  N   LYS D 119     7069   5989   9240   1333    644    -97       N  
ATOM   4897  CA  LYS D 119     -27.264  11.271  54.825  1.00 61.39           C  
ANISOU 4897  CA  LYS D 119     7425   6357   9543   1376    658   -114       C  
ATOM   4898  C   LYS D 119     -27.948  11.869  53.597  1.00 63.56           C  
ANISOU 4898  C   LYS D 119     7734   6626   9790   1456    652   -143       C  
ATOM   4899  O   LYS D 119     -28.901  12.651  53.728  1.00 65.03           O  
ANISOU 4899  O   LYS D 119     7928   6837   9944   1499    660   -161       O  
ATOM   4900  CB  LYS D 119     -26.627  12.382  55.659  1.00 63.14           C  
ANISOU 4900  CB  LYS D 119     7693   6563   9734   1359    699   -103       C  
ATOM   4901  CG  LYS D 119     -25.829  13.393  54.875  1.00 62.98           C  
ANISOU 4901  CG  LYS D 119     7753   6494   9683   1394    725   -108       C  
ATOM   4902  CD  LYS D 119     -25.050  14.301  55.802  1.00 65.35           C  
ANISOU 4902  CD  LYS D 119     8093   6778   9960   1364    764    -93       C  
ATOM   4903  CE  LYS D 119     -24.259  15.314  55.005  1.00 67.48           C  
ANISOU 4903  CE  LYS D 119     8443   6998  10198   1400    790    -99       C  
ATOM   4904  NZ  LYS D 119     -23.591  16.337  55.885  1.00 69.76           N  
ANISOU 4904  NZ  LYS D 119     8774   7271  10459   1378    830    -87       N  
ATOM   4905  N   ASN D 120     -27.458  11.528  52.411  1.00 60.35           N  
ANISOU 4905  N   ASN D 120     7349   6187   9393   1478    639   -148       N  
ATOM   4906  CA  ASN D 120     -28.146  11.908  51.179  1.00 63.31           C  
ANISOU 4906  CA  ASN D 120     7749   6558   9747   1553    628   -175       C  
ATOM   4907  C   ASN D 120     -28.994  10.784  50.586  1.00 63.03           C  
ANISOU 4907  C   ASN D 120     7655   6551   9743   1567    587   -187       C  
ATOM   4908  O   ASN D 120     -29.494  10.900  49.471  1.00 65.65           O  
ANISOU 4908  O   ASN D 120     8003   6879  10063   1625    572   -209       O  
ATOM   4909  CB  ASN D 120     -27.143  12.425  50.154  1.00 65.41           C  
ANISOU 4909  CB  ASN D 120     8085   6770   9998   1579    642   -176       C  
ATOM   4910  CG  ASN D 120     -26.500  13.723  50.590  1.00 66.99           C  
ANISOU 4910  CG  ASN D 120     8350   6945  10160   1582    684   -170       C  
ATOM   4911  OD1 ASN D 120     -26.613  14.128  51.751  1.00 66.64           O  
ANISOU 4911  OD1 ASN D 120     8296   6920  10106   1553    703   -161       O  
ATOM   4912  ND2 ASN D 120     -25.817  14.383  49.666  1.00 69.05           N  
ANISOU 4912  ND2 ASN D 120     8676   7161  10399   1616    700   -176       N  
ATOM   4913  N   ASN D 121     -29.101   9.682  51.319  1.00 62.34           N  
ANISOU 4913  N   ASN D 121     7501   6490   9694   1511    568   -172       N  
ATOM   4914  CA  ASN D 121     -29.842   8.475  50.901  1.00 62.13           C  
ANISOU 4914  CA  ASN D 121     7412   6492   9703   1512    528   -180       C  
ATOM   4915  C   ASN D 121     -29.293   7.802  49.638  1.00 62.81           C  
ANISOU 4915  C   ASN D 121     7508   6546   9811   1525    507   -183       C  
ATOM   4916  O   ASN D 121     -30.044   7.295  48.806  1.00 64.91           O  
ANISOU 4916  O   ASN D 121     7750   6827  10086   1562    479   -201       O  
ATOM   4917  CB  ASN D 121     -31.334   8.781  50.716  1.00 64.67           C  
ANISOU 4917  CB  ASN D 121     7713   6855  10005   1567    515   -208       C  
ATOM   4918  CG  ASN D 121     -32.141   8.535  51.984  1.00 63.98           C  
ANISOU 4918  CG  ASN D 121     7568   6816   9924   1534    512   -203       C  
ATOM   4919  OD1 ASN D 121     -31.592   8.202  53.039  1.00 61.74           O  
ANISOU 4919  OD1 ASN D 121     7262   6536   9659   1470    522   -180       O  
ATOM   4920  ND2 ASN D 121     -33.453   8.712  51.887  1.00 66.33           N  
ANISOU 4920  ND2 ASN D 121     7841   7152  10208   1578    500   -226       N  
ATOM   4921  N   GLU D 122     -27.968   7.799  49.521  1.00 63.87           N  
ANISOU 4921  N   GLU D 122     7679   6637   9953   1494    522   -164       N  
ATOM   4922  CA  GLU D 122     -27.248   6.920  48.602  1.00 63.97           C  
ANISOU 4922  CA  GLU D 122     7690   6620   9997   1484    502   -159       C  
ATOM   4923  C   GLU D 122     -26.438   5.951  49.445  1.00 60.42           C  
ANISOU 4923  C   GLU D 122     7201   6168   9588   1404    498   -130       C  
ATOM   4924  O   GLU D 122     -26.106   6.244  50.597  1.00 58.32           O  
ANISOU 4924  O   GLU D 122     6933   5909   9318   1361    519   -113       O  
ATOM   4925  CB  GLU D 122     -26.345   7.706  47.646  1.00 65.85           C  
ANISOU 4925  CB  GLU D 122     8004   6806  10211   1518    521   -162       C  
ATOM   4926  CG  GLU D 122     -27.112   8.426  46.526  1.00 70.08           C  
ANISOU 4926  CG  GLU D 122     8576   7340  10713   1600    518   -192       C  
ATOM   4927  CD  GLU D 122     -26.311   9.579  45.910  1.00 72.07           C  
ANISOU 4927  CD  GLU D 122     8912   7544  10928   1634    548   -195       C  
ATOM   4928  OE1 GLU D 122     -25.052   9.560  46.062  1.00 69.88           O  
ANISOU 4928  OE1 GLU D 122     8663   7230  10660   1594    565   -175       O  
ATOM   4929  OE2 GLU D 122     -26.936  10.495  45.293  1.00 76.13           O  
ANISOU 4929  OE2 GLU D 122     9464   8058  11404   1701    555   -218       O  
ATOM   4930  N   THR D 123     -26.148   4.788  48.872  1.00 60.19           N  
ANISOU 4930  N   THR D 123     7139   6131   9598   1384    470   -125       N  
ATOM   4931  CA  THR D 123     -25.578   3.680  49.630  1.00 57.25           C  
ANISOU 4931  CA  THR D 123     6719   5765   9270   1310    460   -100       C  
ATOM   4932  C   THR D 123     -24.291   4.103  50.306  1.00 55.34           C  
ANISOU 4932  C   THR D 123     6513   5490   9023   1264    490    -76       C  
ATOM   4933  O   THR D 123     -23.467   4.816  49.728  1.00 56.55           O  
ANISOU 4933  O   THR D 123     6729   5601   9155   1283    510    -76       O  
ATOM   4934  CB  THR D 123     -25.320   2.438  48.738  1.00 57.87           C  
ANISOU 4934  CB  THR D 123     6768   5831   9389   1302    427    -98       C  
ATOM   4935  OG1 THR D 123     -24.753   2.850  47.491  1.00 60.59           O  
ANISOU 4935  OG1 THR D 123     7170   6134   9719   1344    431   -108       O  
ATOM   4936  CG2 THR D 123     -26.625   1.676  48.467  1.00 58.75           C  
ANISOU 4936  CG2 THR D 123     6819   5986   9518   1324    393   -116       C  
ATOM   4937  N   GLN D 124     -24.110   3.654  51.538  1.00 55.32           N  
ANISOU 4937  N   GLN D 124     6472   5507   9041   1201    494    -55       N  
ATOM   4938  CA  GLN D 124     -22.870   3.939  52.212  1.00 53.82           C  
ANISOU 4938  CA  GLN D 124     6311   5288   8851   1153    520    -31       C  
ATOM   4939  C   GLN D 124     -21.959   2.807  51.809  1.00 52.93           C  
ANISOU 4939  C   GLN D 124     6180   5151   8780   1112    502    -15       C  
ATOM   4940  O   GLN D 124     -22.008   1.720  52.376  1.00 51.89           O  
ANISOU 4940  O   GLN D 124     5990   5040   8686   1063    482     -1       O  
ATOM   4941  CB  GLN D 124     -23.079   3.971  53.720  1.00 52.26           C  
ANISOU 4941  CB  GLN D 124     6080   5123   8655   1104    533    -16       C  
ATOM   4942  CG  GLN D 124     -21.828   4.207  54.488  1.00 51.99           C  
ANISOU 4942  CG  GLN D 124     6071   5061   8622   1050    559     10       C  
ATOM   4943  CD  GLN D 124     -21.435   5.660  54.462  1.00 52.17           C  
ANISOU 4943  CD  GLN D 124     6166   5058   8598   1081    596      4       C  
ATOM   4944  OE1 GLN D 124     -21.844   6.426  55.335  1.00 53.97           O  
ANISOU 4944  OE1 GLN D 124     6399   5306   8800   1081    616      3       O  
ATOM   4945  NE2 GLN D 124     -20.652   6.061  53.451  1.00 51.96           N  
ANISOU 4945  NE2 GLN D 124     6196   4987   8561   1108    605     -1       N  
ATOM   4946  N   TYR D 125     -21.067   3.077  50.868  1.00 52.08           N  
ANISOU 4946  N   TYR D 125     6125   4997   8666   1131    509    -16       N  
ATOM   4947  CA  TYR D 125     -20.372   1.975  50.212  1.00 52.11           C  
ANISOU 4947  CA  TYR D 125     6111   4978   8709   1106    486     -7       C  
ATOM   4948  C   TYR D 125     -19.384   1.277  51.122  1.00 51.38           C  
ANISOU 4948  C   TYR D 125     5995   4878   8649   1029    490     23       C  
ATOM   4949  O   TYR D 125     -19.149   0.086  50.958  1.00 51.26           O  
ANISOU 4949  O   TYR D 125     5937   4863   8675    997    465     33       O  
ATOM   4950  CB  TYR D 125     -19.644   2.443  48.962  1.00 54.72           C  
ANISOU 4950  CB  TYR D 125     6504   5261   9025   1145    494    -15       C  
ATOM   4951  CG  TYR D 125     -20.533   2.661  47.760  1.00 57.79           C  
ANISOU 4951  CG  TYR D 125     6906   5655   9398   1218    478    -44       C  
ATOM   4952  CD1 TYR D 125     -20.931   1.593  46.965  1.00 59.11           C  
ANISOU 4952  CD1 TYR D 125     7033   5831   9597   1228    442    -52       C  
ATOM   4953  CD2 TYR D 125     -20.944   3.939  47.401  1.00 59.86           C  
ANISOU 4953  CD2 TYR D 125     7220   5911   9613   1277    499    -63       C  
ATOM   4954  CE1 TYR D 125     -21.725   1.780  45.853  1.00 62.44           C  
ANISOU 4954  CE1 TYR D 125     7465   6256  10004   1294    427    -78       C  
ATOM   4955  CE2 TYR D 125     -21.733   4.141  46.289  1.00 63.05           C  
ANISOU 4955  CE2 TYR D 125     7636   6318  10001   1344    484    -89       C  
ATOM   4956  CZ  TYR D 125     -22.126   3.054  45.515  1.00 64.38           C  
ANISOU 4956  CZ  TYR D 125     7763   6497  10202   1353    448    -96       C  
ATOM   4957  OH  TYR D 125     -22.931   3.244  44.402  1.00 68.07           O  
ANISOU 4957  OH  TYR D 125     8241   6968  10653   1420    432   -123       O  
ATOM   4958  N   TYR D 126     -18.807   1.978  52.089  1.00 51.30           N  
ANISOU 4958  N   TYR D 126     6010   4861   8622    998    521     38       N  
ATOM   4959  CA  TYR D 126     -17.916   1.258  52.980  1.00 51.07           C  
ANISOU 4959  CA  TYR D 126     5953   4827   8624    924    522     66       C  
ATOM   4960  C   TYR D 126     -18.681   0.320  53.885  1.00 51.13           C  
ANISOU 4960  C   TYR D 126     5885   4881   8660    886    501     74       C  
ATOM   4961  O   TYR D 126     -18.282  -0.824  54.064  1.00 50.98           O  
ANISOU 4961  O   TYR D 126     5824   4863   8682    839    482     90       O  
ATOM   4962  CB  TYR D 126     -17.061   2.181  53.833  1.00 50.96           C  
ANISOU 4962  CB  TYR D 126     5981   4794   8586    897    560     81       C  
ATOM   4963  CG  TYR D 126     -16.080   1.374  54.654  1.00 50.70           C  
ANISOU 4963  CG  TYR D 126     5922   4754   8589    821    560    109       C  
ATOM   4964  CD1 TYR D 126     -14.936   0.824  54.075  1.00 50.46           C  
ANISOU 4964  CD1 TYR D 126     5907   4685   8582    798    555    121       C  
ATOM   4965  CD2 TYR D 126     -16.324   1.127  55.998  1.00 50.71           C  
ANISOU 4965  CD2 TYR D 126     5881   4788   8599    773    563    125       C  
ATOM   4966  CE1 TYR D 126     -14.069   0.076  54.826  1.00 50.24           C  
ANISOU 4966  CE1 TYR D 126     5853   4651   8586    730    554    147       C  
ATOM   4967  CE2 TYR D 126     -15.450   0.394  56.749  1.00 50.49           C  
ANISOU 4967  CE2 TYR D 126     5828   4754   8602    706    563    151       C  
ATOM   4968  CZ  TYR D 126     -14.331  -0.130  56.165  1.00 50.26           C  
ANISOU 4968  CZ  TYR D 126     5814   4686   8595    684    558    162       C  
ATOM   4969  OH  TYR D 126     -13.492  -0.861  56.961  1.00 50.05           O  
ANISOU 4969  OH  TYR D 126     5761   4655   8599    616    557    188       O  
ATOM   4970  N   HIS D 127     -19.777   0.798  54.462  1.00 51.36           N  
ANISOU 4970  N   HIS D 127     5897   4949   8668    906    505     63       N  
ATOM   4971  CA  HIS D 127     -20.598  -0.071  55.304  1.00 51.44           C  
ANISOU 4971  CA  HIS D 127     5835   5006   8705    874    485     68       C  
ATOM   4972  C   HIS D 127     -21.272  -1.138  54.454  1.00 51.52           C  
ANISOU 4972  C   HIS D 127     5800   5030   8744    892    447     56       C  
ATOM   4973  O   HIS D 127     -21.433  -2.273  54.884  1.00 51.46           O  
ANISOU 4973  O   HIS D 127     5734   5045   8775    850    424     68       O  
ATOM   4974  CB  HIS D 127     -21.630   0.738  56.087  1.00 51.68           C  
ANISOU 4974  CB  HIS D 127     5859   5074   8703    893    499     58       C  
ATOM   4975  CG  HIS D 127     -21.039   1.561  57.190  1.00 51.60           C  
ANISOU 4975  CG  HIS D 127     5877   5058   8672    861    533     73       C  
ATOM   4976  ND1 HIS D 127     -20.269   2.680  56.954  1.00 51.54           N  
ANISOU 4976  ND1 HIS D 127     5939   5013   8631    880    564     72       N  
ATOM   4977  CD2 HIS D 127     -21.099   1.422  58.536  1.00 51.59           C  
ANISOU 4977  CD2 HIS D 127     5842   5082   8677    811    542     90       C  
ATOM   4978  CE1 HIS D 127     -19.883   3.196  58.109  1.00 51.48           C  
ANISOU 4978  CE1 HIS D 127     5940   5010   8611    843    590     88       C  
ATOM   4979  NE2 HIS D 127     -20.375   2.452  59.084  1.00 51.51           N  
ANISOU 4979  NE2 HIS D 127     5882   5052   8638    801    577     99       N  
ATOM   4980  N   PHE D 128     -21.635  -0.764  53.235  1.00 51.63           N  
ANISOU 4980  N   PHE D 128     5845   5032   8741    955    440     33       N  
ATOM   4981  CA  PHE D 128     -22.333  -1.669  52.340  1.00 51.72           C  
ANISOU 4981  CA  PHE D 128     5818   5057   8776    980    404     19       C  
ATOM   4982  C   PHE D 128     -21.558  -2.920  52.202  1.00 51.49           C  
ANISOU 4982  C   PHE D 128     5758   5013   8794    931    384     37       C  
ATOM   4983  O   PHE D 128     -22.109  -4.012  52.257  1.00 51.52           O  
ANISOU 4983  O   PHE D 128     5702   5044   8831    913    355     38       O  
ATOM   4984  CB  PHE D 128     -22.524  -1.046  50.966  1.00 51.83           C  
ANISOU 4984  CB  PHE D 128     5880   5048   8764   1051    403     -6       C  
ATOM   4985  CG  PHE D 128     -22.924  -2.031  49.894  1.00 51.86           C  
ANISOU 4985  CG  PHE D 128     5853   5055   8797   1073    367    -18       C  
ATOM   4986  CD1 PHE D 128     -21.979  -2.539  49.024  1.00 51.66           C  
ANISOU 4986  CD1 PHE D 128     5846   4990   8792   1066    358    -12       C  
ATOM   4987  CD2 PHE D 128     -24.244  -2.421  49.738  1.00 52.09           C  
ANISOU 4987  CD2 PHE D 128     5836   5126   8831   1101    343    -37       C  
ATOM   4988  CE1 PHE D 128     -22.334  -3.415  48.023  1.00 51.69           C  
ANISOU 4988  CE1 PHE D 128     5823   4996   8820   1087    326    -23       C  
ATOM   4989  CE2 PHE D 128     -24.606  -3.292  48.735  1.00 52.13           C  
ANISOU 4989  CE2 PHE D 128     5814   5132   8860   1123    311    -49       C  
ATOM   4990  CZ  PHE D 128     -23.646  -3.786  47.871  1.00 51.93           C  
ANISOU 4990  CZ  PHE D 128     5808   5067   8855   1116    303    -42       C  
ATOM   4991  N   PHE D 129     -20.254  -2.704  52.030  1.00 51.26           N  
ANISOU 4991  N   PHE D 129     5773   4939   8764    910    401     52       N  
ATOM   4992  CA  PHE D 129     -19.232  -3.724  51.772  1.00 51.00           C  
ANISOU 4992  CA  PHE D 129     5727   4880   8771    866    387     70       C  
ATOM   4993  C   PHE D 129     -18.827  -4.460  53.015  1.00 50.85           C  
ANISOU 4993  C   PHE D 129     5664   4876   8782    792    387     97       C  
ATOM   4994  O   PHE D 129     -18.342  -5.557  52.938  1.00 50.70           O  
ANISOU 4994  O   PHE D 129     5612   4849   8801    753    368    111       O  
ATOM   4995  CB  PHE D 129     -17.995  -3.077  51.167  1.00 50.82           C  
ANISOU 4995  CB  PHE D 129     5772   4804   8733    874    409     75       C  
ATOM   4996  CG  PHE D 129     -18.138  -2.720  49.722  1.00 50.90           C  
ANISOU 4996  CG  PHE D 129     5822   4790   8726    939    403     52       C  
ATOM   4997  CD1 PHE D 129     -18.816  -3.539  48.855  1.00 50.99           C  
ANISOU 4997  CD1 PHE D 129     5799   4814   8759    965    369     38       C  
ATOM   4998  CD2 PHE D 129     -17.556  -1.578  49.218  1.00 50.87           C  
ANISOU 4998  CD2 PHE D 129     5891   4751   8687    973    430     45       C  
ATOM   4999  CE1 PHE D 129     -18.928  -3.203  47.513  1.00 51.06           C  
ANISOU 4999  CE1 PHE D 129     5845   4801   8753   1025    363     17       C  
ATOM   5000  CE2 PHE D 129     -17.668  -1.242  47.878  1.00 50.95           C  
ANISOU 5000  CE2 PHE D 129     5938   4738   8681   1033    424     25       C  
ATOM   5001  CZ  PHE D 129     -18.357  -2.049  47.029  1.00 51.04           C  
ANISOU 5001  CZ  PHE D 129     5915   4763   8713   1059    391     11       C  
ATOM   5002  N   SER D 130     -18.986  -3.829  54.164  1.00 50.91           N  
ANISOU 5002  N   SER D 130     5672   4902   8769    772    409    104       N  
ATOM   5003  CA  SER D 130     -18.527  -4.425  55.396  1.00 50.77           C  
ANISOU 5003  CA  SER D 130     5617   4896   8776    702    412    131       C  
ATOM   5004  C   SER D 130     -19.538  -5.253  56.139  1.00 50.90           C  
ANISOU 5004  C   SER D 130     5561   4962   8815    678    391    133       C  
ATOM   5005  O   SER D 130     -19.133  -5.995  57.027  1.00 50.76           O  
ANISOU 5005  O   SER D 130     5508   4953   8827    617    387    155       O  
ATOM   5006  CB  SER D 130     -18.037  -3.341  56.344  1.00 50.73           C  
ANISOU 5006  CB  SER D 130     5651   4884   8740    685    449    141       C  
ATOM   5007  OG  SER D 130     -17.013  -2.563  55.743  1.00 50.60           O  
ANISOU 5007  OG  SER D 130     5702   4821   8702    702    472    141       O  
ATOM   5008  N   ILE D 131     -20.832  -5.147  55.799  1.00 51.15           N  
ANISOU 5008  N   ILE D 131     5573   5026   8837    724    377    109       N  
ATOM   5009  CA  ILE D 131     -21.876  -5.850  56.559  1.00 51.30           C  
ANISOU 5009  CA  ILE D 131     5524   5094   8874    704    359    109       C  
ATOM   5010  C   ILE D 131     -22.755  -6.758  55.722  1.00 51.43           C  
ANISOU 5010  C   ILE D 131     5497   5130   8914    730    323     93       C  
ATOM   5011  O   ILE D 131     -23.393  -6.296  54.771  1.00 52.03           O  
ANISOU 5011  O   ILE D 131     5594   5206   8970    792    317     68       O  
ATOM   5012  CB  ILE D 131     -22.818  -4.905  57.263  1.00 51.53           C  
ANISOU 5012  CB  ILE D 131     5556   5156   8867    727    376     98       C  
ATOM   5013  CG1 ILE D 131     -22.058  -3.818  57.982  1.00 51.44           C  
ANISOU 5013  CG1 ILE D 131     5594   5126   8826    713    413    110       C  
ATOM   5014  CG2 ILE D 131     -23.599  -5.651  58.280  1.00 51.62           C  
ANISOU 5014  CG2 ILE D 131     5499   5214   8901    690    362    105       C  
ATOM   5015  CD1 ILE D 131     -22.867  -3.125  59.052  1.00 51.63           C  
ANISOU 5015  CD1 ILE D 131     5607   5186   8823    713    430    106       C  
ATOM   5016  N   LYS D 132     -22.847  -8.024  56.136  1.00 52.34           N  
ANISOU 5016  N   LYS D 132     5550   5264   9071    683    300    106       N  
ATOM   5017  CA  LYS D 132     -23.578  -9.061  55.408  1.00 52.43           C  
ANISOU 5017  CA  LYS D 132     5515   5293   9112    698    264     93       C  
ATOM   5018  C   LYS D 132     -25.069  -8.802  55.271  1.00 52.74           C  
ANISOU 5018  C   LYS D 132     5530   5373   9134    746    254     67       C  
ATOM   5019  O   LYS D 132     -25.773  -8.534  56.253  1.00 52.88           O  
ANISOU 5019  O   LYS D 132     5524   5426   9141    735    262     67       O  
ATOM   5020  CB  LYS D 132     -23.369 -10.411  56.086  1.00 52.30           C  
ANISOU 5020  CB  LYS D 132     5437   5292   9143    632    245    115       C  
ATOM   5021  CG  LYS D 132     -24.265 -11.541  55.570  1.00 53.35           C  
ANISOU 5021  CG  LYS D 132     5512   5451   9308    640    209    103       C  
ATOM   5022  CD  LYS D 132     -24.179 -12.769  56.479  1.00 54.57           C  
ANISOU 5022  CD  LYS D 132     5603   5626   9505    573    194    126       C  
ATOM   5023  CE  LYS D 132     -25.341 -13.698  56.258  1.00 57.47           C  
ANISOU 5023  CE  LYS D 132     5908   6031   9896    582    162    112       C  
ATOM   5024  NZ  LYS D 132     -25.336 -14.815  57.249  1.00 59.20           N  
ANISOU 5024  NZ  LYS D 132     6066   6273  10154    516    150    133       N  
ATOM   5025  N   ASP D 133     -25.531  -8.895  54.027  1.00 51.87           N  
ANISOU 5025  N   ASP D 133     5427   5258   9022    799    235     45       N  
ATOM   5026  CA  ASP D 133     -26.944  -8.744  53.662  1.00 53.98           C  
ANISOU 5026  CA  ASP D 133     5672   5562   9277    850    221     17       C  
ATOM   5027  C   ASP D 133     -27.517 -10.012  53.038  1.00 57.15           C  
ANISOU 5027  C   ASP D 133     6018   5981   9716    851    183      9       C  
ATOM   5028  O   ASP D 133     -27.036 -10.430  51.985  1.00 58.19           O  
ANISOU 5028  O   ASP D 133     6164   6084   9863    865    169      5       O  
ATOM   5029  CB  ASP D 133     -27.089  -7.593  52.683  1.00 54.40           C  
ANISOU 5029  CB  ASP D 133     5786   5595   9288    921    233     -6       C  
ATOM   5030  CG  ASP D 133     -28.503  -7.373  52.253  1.00 56.60           C  
ANISOU 5030  CG  ASP D 133     6046   5910   9551    978    219    -36       C  
ATOM   5031  OD1 ASP D 133     -29.350  -7.177  53.149  1.00 56.46           O  
ANISOU 5031  OD1 ASP D 133     5998   5930   9523    971    223    -39       O  
ATOM   5032  OD2 ASP D 133     -28.747  -7.395  51.024  1.00 58.76           O  
ANISOU 5032  OD2 ASP D 133     6335   6171   9821   1028    204    -55       O  
ATOM   5033  N   PRO D 134     -28.564 -10.614  53.633  1.00 55.50           N  
ANISOU 5033  N   PRO D 134     5748   5818   9523    838    167      4       N  
ATOM   5034  CA  PRO D 134     -29.490 -10.240  54.704  1.00 55.70           C  
ANISOU 5034  CA  PRO D 134     5745   5885   9532    832    176      0       C  
ATOM   5035  C   PRO D 134     -28.980 -10.372  56.118  1.00 55.57           C  
ANISOU 5035  C   PRO D 134     5712   5876   9525    765    193     28       C  
ATOM   5036  O   PRO D 134     -27.899 -10.863  56.315  1.00 55.33           O  
ANISOU 5036  O   PRO D 134     5685   5819   9517    719    195     52       O  
ATOM   5037  CB  PRO D 134     -30.632 -11.219  54.504  1.00 55.88           C  
ANISOU 5037  CB  PRO D 134     5702   5947   9581    838    144    -14       C  
ATOM   5038  CG  PRO D 134     -29.987 -12.390  53.964  1.00 55.69           C  
ANISOU 5038  CG  PRO D 134     5657   5903   9599    809    122     -3       C  
ATOM   5039  CD  PRO D 134     -28.989 -11.867  53.002  1.00 55.53           C  
ANISOU 5039  CD  PRO D 134     5700   5834   9565    835    132     -3       C  
ATOM   5040  N   ALA D 135     -29.792  -9.975  57.090  1.00 55.81           N  
ANISOU 5040  N   ALA D 135     5721   5945   9540    760    203     25       N  
ATOM   5041  CA  ALA D 135     -29.389  -9.934  58.486  1.00 55.71           C  
ANISOU 5041  CA  ALA D 135     5696   5942   9531    702    221     50       C  
ATOM   5042  C   ALA D 135     -30.188 -10.913  59.329  1.00 55.81           C  
ANISOU 5042  C   ALA D 135     5635   5999   9573    663    203     55       C  
ATOM   5043  O   ALA D 135     -31.415 -10.924  59.320  1.00 56.06           O  
ANISOU 5043  O   ALA D 135     5634   6068   9598    692    192     35       O  
ATOM   5044  CB  ALA D 135     -29.546  -8.544  59.032  1.00 55.82           C  
ANISOU 5044  CB  ALA D 135     5752   5958   9498    725    253     45       C  
ATOM   5045  N   ASP D 136     -29.484 -11.751  60.068  1.00 60.34           N  
ANISOU 5045  N   ASP D 136     6181   6568  10179    597    201     82       N  
ATOM   5046  CA  ASP D 136     -30.163 -12.691  60.937  1.00 63.83           C  
ANISOU 5046  CA  ASP D 136     6553   7050  10650    555    185     90       C  
ATOM   5047  C   ASP D 136     -30.768 -11.901  62.089  1.00 64.71           C  
ANISOU 5047  C   ASP D 136     6661   7193  10733    550    207     89       C  
ATOM   5048  O   ASP D 136     -30.090 -11.120  62.738  1.00 62.20           O  
ANISOU 5048  O   ASP D 136     6381   6860  10394    533    235    103       O  
ATOM   5049  CB  ASP D 136     -29.203 -13.790  61.441  1.00 63.32           C  
ANISOU 5049  CB  ASP D 136     6461   6971  10627    485    178    120       C  
ATOM   5050  CG  ASP D 136     -28.580 -14.616  60.301  1.00 64.43           C  
ANISOU 5050  CG  ASP D 136     6604   7080  10797    488    156    121       C  
ATOM   5051  OD1 ASP D 136     -28.746 -14.258  59.109  1.00 64.95           O  
ANISOU 5051  OD1 ASP D 136     6699   7130  10848    544    149    100       O  
ATOM   5052  OD2 ASP D 136     -27.889 -15.619  60.601  1.00 65.08           O  
ANISOU 5052  OD2 ASP D 136     6659   7152  10916    434    145    144       O  
ATOM   5053  N   VAL D 137     -32.059 -12.083  62.308  1.00 62.34           N  
ANISOU 5053  N   VAL D 137     6318   6937  10433    566    194     72       N  
ATOM   5054  CA  VAL D 137     -32.738 -11.489  63.450  1.00 62.50           C  
ANISOU 5054  CA  VAL D 137     6325   6992  10432    558    211     72       C  
ATOM   5055  C   VAL D 137     -33.263 -12.569  64.394  1.00 66.64           C  
ANISOU 5055  C   VAL D 137     6778   7554  10990    505    196     84       C  
ATOM   5056  O   VAL D 137     -34.167 -13.336  64.041  1.00 70.49           O  
ANISOU 5056  O   VAL D 137     7217   8068  11498    517    170     69       O  
ATOM   5057  CB  VAL D 137     -33.925 -10.620  63.026  1.00 63.66           C  
ANISOU 5057  CB  VAL D 137     6482   7163  10544    625    213     40       C  
ATOM   5058  CG1 VAL D 137     -34.387  -9.771  64.195  1.00 64.96           C  
ANISOU 5058  CG1 VAL D 137     6648   7354  10678    617    237     42       C  
ATOM   5059  CG2 VAL D 137     -33.567  -9.783  61.832  1.00 62.77           C  
ANISOU 5059  CG2 VAL D 137     6432   7016  10403    683    220     24       C  
ATOM   5060  N   TYR D 138     -32.720 -12.606  65.602  1.00 69.55           N  
ANISOU 5060  N   TYR D 138     7139   7925  11363    449    213    109       N  
ATOM   5061  CA  TYR D 138     -33.008 -13.700  66.509  1.00 73.64           C  
ANISOU 5061  CA  TYR D 138     7592   8471  11916    392    199    125       C  
ATOM   5062  C   TYR D 138     -34.134 -13.355  67.451  1.00 77.53           C  
ANISOU 5062  C   TYR D 138     8054   9011  12393    393    206    116       C  
ATOM   5063  O   TYR D 138     -34.204 -12.241  67.956  1.00 76.43           O  
ANISOU 5063  O   TYR D 138     7948   8875  12217    408    232    113       O  
ATOM   5064  CB  TYR D 138     -31.740 -14.091  67.274  1.00 71.87           C  
ANISOU 5064  CB  TYR D 138     7373   8223  11711    326    210    159       C  
ATOM   5065  CG  TYR D 138     -30.845 -14.934  66.407  1.00 70.15           C  
ANISOU 5065  CG  TYR D 138     7159   7969  11524    314    193    169       C  
ATOM   5066  CD1 TYR D 138     -30.162 -14.372  65.341  1.00 66.10           C  
ANISOU 5066  CD1 TYR D 138     6702   7416  10996    352    198    161       C  
ATOM   5067  CD2 TYR D 138     -30.731 -16.301  66.614  1.00 73.10           C  
ANISOU 5067  CD2 TYR D 138     7480   8351  11944    266    170    184       C  
ATOM   5068  CE1 TYR D 138     -29.367 -15.132  64.527  1.00 64.97           C  
ANISOU 5068  CE1 TYR D 138     6563   7241  10881    342    182    169       C  
ATOM   5069  CE2 TYR D 138     -29.938 -17.081  65.801  1.00 71.88           C  
ANISOU 5069  CE2 TYR D 138     7329   8164  11819    256    154    192       C  
ATOM   5070  CZ  TYR D 138     -29.258 -16.492  64.756  1.00 67.81           C  
ANISOU 5070  CZ  TYR D 138     6869   7608  11286    294    159    184       C  
ATOM   5071  OH  TYR D 138     -28.462 -17.264  63.936  1.00 66.92           O  
ANISOU 5071  OH  TYR D 138     6761   7464  11203    284    143    192       O  
ATOM   5072  N   TYR D 139     -35.020 -14.325  67.670  1.00 70.38           N  
ANISOU 5072  N   TYR D 139     7085   8142  11516    378    183    111       N  
ATOM   5073  CA  TYR D 139     -36.218 -14.128  68.488  1.00 74.97           C  
ANISOU 5073  CA  TYR D 139     7630   8770  12085    380    186    100       C  
ATOM   5074  C   TYR D 139     -35.919 -14.365  69.964  1.00 77.31           C  
ANISOU 5074  C   TYR D 139     7902   9082  12391    314    200    127       C  
ATOM   5075  O   TYR D 139     -35.142 -15.247  70.301  1.00 77.48           O  
ANISOU 5075  O   TYR D 139     7905   9089  12445    261    193    151       O  
ATOM   5076  CB  TYR D 139     -37.346 -15.057  68.006  1.00 80.16           C  
ANISOU 5076  CB  TYR D 139     8230   9460  12768    396    154     80       C  
ATOM   5077  CG  TYR D 139     -37.903 -14.676  66.648  1.00 79.21           C  
ANISOU 5077  CG  TYR D 139     8131   9335  12631    468    142     48       C  
ATOM   5078  CD1 TYR D 139     -38.176 -13.343  66.342  1.00 76.88           C  
ANISOU 5078  CD1 TYR D 139     7885   9036  12291    523    161     30       C  
ATOM   5079  CD2 TYR D 139     -38.140 -15.639  65.669  1.00 81.11           C  
ANISOU 5079  CD2 TYR D 139     8343   9573  12901    481    112     38       C  
ATOM   5080  CE1 TYR D 139     -38.681 -12.974  65.103  1.00 76.44           C  
ANISOU 5080  CE1 TYR D 139     7849   8974  12219    590    150      1       C  
ATOM   5081  CE2 TYR D 139     -38.645 -15.282  64.423  1.00 80.81           C  
ANISOU 5081  CE2 TYR D 139     8325   9531  12849    548    101      9       C  
ATOM   5082  CZ  TYR D 139     -38.919 -13.941  64.146  1.00 78.47           C  
ANISOU 5082  CZ  TYR D 139     8078   9231  12507    603    120     -9       C  
ATOM   5083  OH  TYR D 139     -39.423 -13.543  62.919  1.00 78.56           O  
ANISOU 5083  OH  TYR D 139     8111   9237  12500    670    109    -38       O  
ATOM   5084  N   THR D 140     -36.523 -13.567  70.838  1.00 80.18           N  
ANISOU 5084  N   THR D 140     8266   9472  12726    319    219    122       N  
ATOM   5085  CA  THR D 140     -36.334 -13.707  72.282  1.00 83.54           C  
ANISOU 5085  CA  THR D 140     8670   9915  13158    259    233    146       C  
ATOM   5086  C   THR D 140     -37.642 -13.579  73.043  1.00 89.49           C  
ANISOU 5086  C   THR D 140     9382  10719  13902    264    234    132       C  
ATOM   5087  O   THR D 140     -38.720 -13.509  72.452  1.00 90.72           O  
ANISOU 5087  O   THR D 140     9521  10897  14050    310    220    105       O  
ATOM   5088  CB  THR D 140     -35.373 -12.653  72.846  1.00 79.78           C  
ANISOU 5088  CB  THR D 140     8249   9413  12652    248    266    162       C  
ATOM   5089  OG1 THR D 140     -35.964 -11.347  72.722  1.00 78.66           O  
ANISOU 5089  OG1 THR D 140     8143   9279  12465    301    284    140       O  
ATOM   5090  CG2 THR D 140     -34.051 -12.690  72.118  1.00 73.89           C  
ANISOU 5090  CG2 THR D 140     7546   8615  11912    244    268    175       C  
ATOM   5091  N   LYS D 141     -37.534 -13.539  74.366  1.00 88.21           N  
ANISOU 5091  N   LYS D 141     9203  10573  13738    215    249    152       N  
ATOM   5092  CA  LYS D 141     -38.692 -13.315  75.224  1.00 93.76           C  
ANISOU 5092  CA  LYS D 141     9872  11323  14429    216    254    141       C  
ATOM   5093  C   LYS D 141     -39.207 -11.886  75.083  1.00 91.40           C  
ANISOU 5093  C   LYS D 141     9615  11030  14082    272    274    120       C  
ATOM   5094  O   LYS D 141     -40.415 -11.651  75.003  1.00 94.85           O  
ANISOU 5094  O   LYS D 141    10031  11502  14507    308    268     95       O  
ATOM   5095  CB  LYS D 141     -38.345 -13.590  76.693  1.00 98.44           C  
ANISOU 5095  CB  LYS D 141    10441  11929  15033    148    268    170       C  
ATOM   5096  CG  LYS D 141     -37.791 -14.980  76.974  1.00102.81           C  
ANISOU 5096  CG  LYS D 141    10953  12477  15633     87    250    194       C  
ATOM   5097  CD  LYS D 141     -38.861 -16.044  76.789  1.00107.40           C  
ANISOU 5097  CD  LYS D 141    11470  13094  16245     86    221    181       C  
ATOM   5098  CE  LYS D 141     -40.085 -15.750  77.649  1.00112.19           C  
ANISOU 5098  CE  LYS D 141    12042  13748  16836     89    227    168       C  
ATOM   5099  NZ  LYS D 141     -41.108 -16.834  77.550  1.00116.26           N  
ANISOU 5099  NZ  LYS D 141    12492  14298  17382     84    200    156       N  
ATOM   5100  N   LYS D 142     -38.287 -10.928  75.042  1.00 92.98           N  
ANISOU 5100  N   LYS D 142     9876  11196  14255    281    299    128       N  
ATOM   5101  CA  LYS D 142     -38.683  -9.531  75.144  1.00 91.11           C  
ANISOU 5101  CA  LYS D 142     9680  10965  13971    325    322    112       C  
ATOM   5102  C   LYS D 142     -38.670  -8.782  73.796  1.00 85.54           C  
ANISOU 5102  C   LYS D 142     9026  10234  13241    394    322     89       C  
ATOM   5103  O   LYS D 142     -39.739  -8.508  73.237  1.00 85.91           O  
ANISOU 5103  O   LYS D 142     9064  10304  13274    446    312     60       O  
ATOM   5104  CB  LYS D 142     -37.800  -8.839  76.182  1.00 90.97           C  
ANISOU 5104  CB  LYS D 142     9696  10933  13935    288    353    136       C  
ATOM   5105  CG  LYS D 142     -37.802  -9.581  77.523  1.00 97.00           C  
ANISOU 5105  CG  LYS D 142    10411  11722  14723    219    354    160       C  
ATOM   5106  CD  LYS D 142     -37.304  -8.714  78.669  1.00 97.52           C  
ANISOU 5106  CD  LYS D 142    10504  11786  14763    191    386    177       C  
ATOM   5107  CE  LYS D 142     -37.426  -9.442  79.999  1.00104.08           C  
ANISOU 5107  CE  LYS D 142    11284  12646  15617    126    386    198       C  
ATOM   5108  NZ  LYS D 142     -38.823  -9.897  80.265  1.00107.60           N  
ANISOU 5108  NZ  LYS D 142    11672  13139  16071    134    370    181       N  
ATOM   5109  N   LYS D 143     -37.493  -8.447  73.265  1.00 86.45           N  
ANISOU 5109  N   LYS D 143     9193  10304  13350    397    332     99       N  
ATOM   5110  CA  LYS D 143     -37.439  -7.862  71.920  1.00 81.45           C  
ANISOU 5110  CA  LYS D 143     8605   9644  12697    461    329     78       C  
ATOM   5111  C   LYS D 143     -36.528  -8.686  71.009  1.00 77.99           C  
ANISOU 5111  C   LYS D 143     8173   9169  12289    450    311     88       C  
ATOM   5112  O   LYS D 143     -35.608  -9.355  71.483  1.00 77.48           O  
ANISOU 5112  O   LYS D 143     8099   9088  12251    394    312    115       O  
ATOM   5113  CB  LYS D 143     -36.956  -6.416  71.955  1.00 78.83           C  
ANISOU 5113  CB  LYS D 143     8341   9289  12320    490    361     76       C  
ATOM   5114  CG  LYS D 143     -37.500  -5.578  73.096  1.00 81.66           C  
ANISOU 5114  CG  LYS D 143     8700   9678  12650    484    385     76       C  
ATOM   5115  CD  LYS D 143     -37.154  -4.100  72.908  1.00 78.81           C  
ANISOU 5115  CD  LYS D 143     8409   9294  12243    525    414     68       C  
ATOM   5116  CE  LYS D 143     -37.295  -3.319  74.204  1.00 81.85           C  
ANISOU 5116  CE  LYS D 143     8799   9698  12602    503    442     76       C  
ATOM   5117  NZ  LYS D 143     -37.301  -1.848  73.963  1.00 79.35           N  
ANISOU 5117  NZ  LYS D 143     8544   9368  12237    553    468     62       N  
ATOM   5118  N   ALA D 144     -36.795  -8.640  69.704  1.00 80.75           N  
ANISOU 5118  N   ALA D 144     8797   9888  11995    573    264    148       N  
ATOM   5119  CA  ALA D 144     -35.990  -9.371  68.727  1.00 77.35           C  
ANISOU 5119  CA  ALA D 144     8360   9432  11598    561    217    152       C  
ATOM   5120  C   ALA D 144     -34.605  -8.783  68.677  1.00 72.67           C  
ANISOU 5120  C   ALA D 144     7790   8823  10997    553    204     98       C  
ATOM   5121  O   ALA D 144     -34.455  -7.578  68.694  1.00 69.96           O  
ANISOU 5121  O   ALA D 144     7463   8470  10648    563    235     56       O  
ATOM   5122  CB  ALA D 144     -36.621  -9.316  67.360  1.00 75.42           C  
ANISOU 5122  CB  ALA D 144     8098   9154  11406    572    221    169       C  
ATOM   5123  N   GLU D 145     -33.584  -9.621  68.608  1.00 74.53           N  
ANISOU 5123  N   GLU D 145     8026   9057  11234    535    157     98       N  
ATOM   5124  CA  GLU D 145     -32.213  -9.124  68.584  1.00 70.46           C  
ANISOU 5124  CA  GLU D 145     7533   8528  10710    526    141     47       C  
ATOM   5125  C   GLU D 145     -31.587  -9.299  67.214  1.00 65.36           C  
ANISOU 5125  C   GLU D 145     6881   7842  10110    522    111     39       C  
ATOM   5126  O   GLU D 145     -31.404 -10.419  66.747  1.00 65.22           O  
ANISOU 5126  O   GLU D 145     6849   7820  10113    512     71     70       O  
ATOM   5127  CB  GLU D 145     -31.366  -9.837  69.630  1.00 72.40           C  
ANISOU 5127  CB  GLU D 145     7789   8803  10918    509    111     46       C  
ATOM   5128  CG  GLU D 145     -31.576  -9.341  71.049  1.00 76.83           C  
ANISOU 5128  CG  GLU D 145     8364   9399  11427    512    142     33       C  
ATOM   5129  CD  GLU D 145     -30.602  -9.992  72.020  1.00 78.85           C  
ANISOU 5129  CD  GLU D 145     8632   9681  11646    494    110     26       C  
ATOM   5130  OE1 GLU D 145     -30.558 -11.249  72.088  1.00 76.98           O  
ANISOU 5130  OE1 GLU D 145     8381   9455  11412    481     73     64       O  
ATOM   5131  OE2 GLU D 145     -29.854  -9.246  72.694  1.00 82.48           O  
ANISOU 5131  OE2 GLU D 145     9115  10148  12075    491    120    -18       O  
ATOM   5132  N   VAL D 146     -31.262  -8.186  66.569  1.00 62.65           N  
ANISOU 5132  N   VAL D 146     6550   7471   9784    530    130     -3       N  
ATOM   5133  CA  VAL D 146     -30.634  -8.231  65.260  1.00 62.23           C  
ANISOU 5133  CA  VAL D 146     6492   7379   9773    527    104    -15       C  
ATOM   5134  C   VAL D 146     -29.165  -8.640  65.396  1.00 62.11           C  
ANISOU 5134  C   VAL D 146     6490   7361   9747    508     62    -41       C  
ATOM   5135  O   VAL D 146     -28.492  -8.230  66.339  1.00 62.33           O  
ANISOU 5135  O   VAL D 146     6539   7408   9737    503     67    -73       O  
ATOM   5136  CB  VAL D 146     -30.766  -6.869  64.546  1.00 62.13           C  
ANISOU 5136  CB  VAL D 146     6489   7337   9781    542    140    -53       C  
ATOM   5137  CG1 VAL D 146     -29.906  -6.815  63.310  1.00 61.71           C  
ANISOU 5137  CG1 VAL D 146     6436   7245   9766    537    112    -74       C  
ATOM   5138  CG2 VAL D 146     -32.194  -6.634  64.168  1.00 62.17           C  
ANISOU 5138  CG2 VAL D 146     6477   7338   9805    560    174    -23       C  
ATOM   5139  N   GLU D 147     -28.678  -9.481  64.485  1.00 66.66           N  
ANISOU 5139  N   GLU D 147     7054   7918  10356    499     19    -26       N  
ATOM   5140  CA  GLU D 147     -27.260  -9.834  64.492  1.00 64.55           C  
ANISOU 5140  CA  GLU D 147     6798   7645  10083    481    -21    -52       C  
ATOM   5141  C   GLU D 147     -26.566  -9.371  63.205  1.00 60.97           C  
ANISOU 5141  C   GLU D 147     6348   7150   9669    482    -34    -82       C  
ATOM   5142  O   GLU D 147     -26.993  -9.717  62.089  1.00 60.53           O  
ANISOU 5142  O   GLU D 147     6274   7070   9656    486    -44    -58       O  
ATOM   5143  CB  GLU D 147     -27.050 -11.340  64.688  1.00 66.34           C  
ANISOU 5143  CB  GLU D 147     7011   7887  10308    466    -68    -12       C  
ATOM   5144  CG  GLU D 147     -25.606 -11.751  64.426  1.00 64.02           C  
ANISOU 5144  CG  GLU D 147     6726   7582  10017    449   -113    -36       C  
ATOM   5145  CD  GLU D 147     -25.398 -13.254  64.400  1.00 65.67           C  
ANISOU 5145  CD  GLU D 147     6919   7800  10232    435   -162      4       C  
ATOM   5146  OE1 GLU D 147     -25.303 -13.847  63.290  1.00 64.27           O  
ANISOU 5146  OE1 GLU D 147     6726   7597  10095    432   -190     22       O  
ATOM   5147  OE2 GLU D 147     -25.320 -13.841  65.501  1.00 68.75           O  
ANISOU 5147  OE2 GLU D 147     7313   8224  10586    426   -171     19       O  
ATOM   5148  N   LEU D 148     -25.490  -8.598  63.381  1.00 62.20           N  
ANISOU 5148  N   LEU D 148     6526   7298   9809    477    -34   -134       N  
ATOM   5149  CA  LEU D 148     -24.764  -8.014  62.267  1.00 59.47           C  
ANISOU 5149  CA  LEU D 148     6186   6914   9496    477    -42   -169       C  
ATOM   5150  C   LEU D 148     -23.409  -8.714  61.994  1.00 58.04           C  
ANISOU 5150  C   LEU D 148     6009   6724   9320    458    -94   -183       C  
ATOM   5151  O   LEU D 148     -22.614  -9.006  62.913  1.00 58.93           O  
ANISOU 5151  O   LEU D 148     6134   6859   9396    446   -112   -197       O  
ATOM   5152  CB  LEU D 148     -24.551  -6.532  62.532  1.00 58.33           C  
ANISOU 5152  CB  LEU D 148     6065   6764   9335    486     -2   -221       C  
ATOM   5153  CG  LEU D 148     -25.746  -5.626  62.263  1.00 59.07           C  
ANISOU 5153  CG  LEU D 148     6154   6849   9441    507     47   -217       C  
ATOM   5154  CD1 LEU D 148     -25.456  -4.190  62.665  1.00 59.95           C  
ANISOU 5154  CD1 LEU D 148     6290   6958   9530    515     85   -269       C  
ATOM   5155  CD2 LEU D 148     -26.135  -5.699  60.799  1.00 56.98           C  
ANISOU 5155  CD2 LEU D 148     5871   6548   9229    514     41   -201       C  
ATOM   5156  N   ASP D 149     -23.140  -8.968  60.716  1.00 58.63           N  
ANISOU 5156  N   ASP D 149     6072   6766   9438    457   -117   -180       N  
ATOM   5157  CA  ASP D 149     -21.950  -9.694  60.299  1.00 57.60           C  
ANISOU 5157  CA  ASP D 149     5942   6624   9318    440   -168   -188       C  
ATOM   5158  C   ASP D 149     -20.936  -8.701  59.700  1.00 55.37           C  
ANISOU 5158  C   ASP D 149     5678   6313   9046    439   -166   -244       C  
ATOM   5159  O   ASP D 149     -21.088  -8.248  58.570  1.00 54.18           O  
ANISOU 5159  O   ASP D 149     5522   6131   8934    447   -159   -251       O  
ATOM   5160  CB  ASP D 149     -22.390 -10.748  59.287  1.00 57.95           C  
ANISOU 5160  CB  ASP D 149     5960   6653   9405    439   -197   -143       C  
ATOM   5161  CG  ASP D 149     -21.347 -11.795  59.003  1.00 57.45           C  
ANISOU 5161  CG  ASP D 149     5893   6585   9350    421   -252   -138       C  
ATOM   5162  OD1 ASP D 149     -20.129 -11.498  58.921  1.00 55.90           O  
ANISOU 5162  OD1 ASP D 149     5712   6379   9148    411   -271   -179       O  
ATOM   5163  OD2 ASP D 149     -21.768 -12.956  58.834  1.00 58.97           O  
ANISOU 5163  OD2 ASP D 149     6066   6785   9556    416   -278    -91       O  
ATOM   5164  N   ILE D 150     -19.883  -8.370  60.420  1.00 53.80           N  
ANISOU 5164  N   ILE D 150     5500   6125   8815    429   -173   -283       N  
ATOM   5165  CA  ILE D 150     -19.016  -7.319  59.916  1.00 53.29           C  
ANISOU 5165  CA  ILE D 150     5453   6035   8758    429   -166   -337       C  
ATOM   5166  C   ILE D 150     -17.585  -7.786  59.664  1.00 52.82           C  
ANISOU 5166  C   ILE D 150     5401   5966   8701    412   -212   -360       C  
ATOM   5167  O   ILE D 150     -16.940  -8.292  60.584  1.00 52.99           O  
ANISOU 5167  O   ILE D 150     5431   6012   8689    399   -233   -364       O  
ATOM   5168  CB  ILE D 150     -18.966  -6.119  60.893  1.00 54.23           C  
ANISOU 5168  CB  ILE D 150     5597   6170   8839    436   -125   -376       C  
ATOM   5169  CG1 ILE D 150     -20.281  -5.969  61.662  1.00 55.29           C  
ANISOU 5169  CG1 ILE D 150     5725   6329   8953    449    -86   -348       C  
ATOM   5170  CG2 ILE D 150     -18.603  -4.833  60.150  1.00 53.74           C  
ANISOU 5170  CG2 ILE D 150     5548   6076   8795    444   -102   -423       C  
ATOM   5171  CD1 ILE D 150     -20.145  -5.065  62.862  1.00 56.34           C  
ANISOU 5171  CD1 ILE D 150     5881   6485   9039    452    -53   -381       C  
ATOM   5172  N   ASN D 151     -17.069  -7.613  58.445  1.00 52.61           N  
ANISOU 5172  N   ASN D 151     5371   5904   8713    410   -229   -377       N  
ATOM   5173  CA  ASN D 151     -15.681  -8.017  58.207  1.00 52.41           C  
ANISOU 5173  CA  ASN D 151     5354   5871   8690    394   -272   -401       C  
ATOM   5174  C   ASN D 151     -14.731  -6.892  58.636  1.00 52.69           C  
ANISOU 5174  C   ASN D 151     5416   5903   8699    391   -257   -461       C  
ATOM   5175  O   ASN D 151     -15.185  -5.821  59.065  1.00 53.01           O  
ANISOU 5175  O   ASN D 151     5469   5948   8724    403   -213   -482       O  
ATOM   5176  CB  ASN D 151     -15.440  -8.442  56.737  1.00 51.51           C  
ANISOU 5176  CB  ASN D 151     5223   5721   8626    392   -301   -392       C  
ATOM   5177  CG  ASN D 151     -15.480  -7.274  55.738  1.00 50.68           C  
ANISOU 5177  CG  ASN D 151     5124   5581   8551    403   -275   -424       C  
ATOM   5178  OD1 ASN D 151     -15.463  -6.107  56.123  1.00 50.73           O  
ANISOU 5178  OD1 ASN D 151     5149   5588   8539    410   -239   -460       O  
ATOM   5179  ND2 ASN D 151     -15.521  -7.599  54.436  1.00 50.33           N  
ANISOU 5179  ND2 ASN D 151     5063   5507   8553    404   -294   -410       N  
ATOM   5180  N   THR D 152     -13.428  -7.165  58.528  1.00 51.27           N  
ANISOU 5180  N   THR D 152     5246   5718   8517    376   -294   -487       N  
ATOM   5181  CA  THR D 152     -12.349  -6.286  58.993  1.00 51.37           C  
ANISOU 5181  CA  THR D 152     5284   5731   8503    370   -288   -543       C  
ATOM   5182  C   THR D 152     -12.614  -5.699  60.360  1.00 51.80           C  
ANISOU 5182  C   THR D 152     5355   5816   8510    374   -254   -556       C  
ATOM   5183  O   THR D 152     -12.300  -4.550  60.593  1.00 51.91           O  
ANISOU 5183  O   THR D 152     5389   5826   8510    379   -226   -599       O  
ATOM   5184  CB  THR D 152     -12.054  -5.106  58.014  1.00 51.16           C  
ANISOU 5184  CB  THR D 152     5267   5668   8504    378   -268   -584       C  
ATOM   5185  OG1 THR D 152     -13.161  -4.216  57.957  1.00 51.29           O  
ANISOU 5185  OG1 THR D 152     5283   5680   8525    396   -220   -581       O  
ATOM   5186  CG2 THR D 152     -11.762  -5.606  56.617  1.00 50.73           C  
ANISOU 5186  CG2 THR D 152     5196   5581   8497    374   -300   -574       C  
ATOM   5187  N   ALA D 153     -13.171  -6.493  61.259  1.00 53.20           N  
ANISOU 5187  N   ALA D 153     5525   6025   8663    373   -258   -519       N  
ATOM   5188  CA  ALA D 153     -13.494  -6.031  62.598  1.00 53.62           C  
ANISOU 5188  CA  ALA D 153     5592   6110   8670    376   -227   -527       C  
ATOM   5189  C   ALA D 153     -12.305  -5.422  63.304  1.00 53.75           C  
ANISOU 5189  C   ALA D 153     5635   6135   8653    367   -229   -579       C  
ATOM   5190  O   ALA D 153     -12.457  -4.525  64.133  1.00 54.05           O  
ANISOU 5190  O   ALA D 153     5689   6187   8659    374   -194   -603       O  
ATOM   5191  CB  ALA D 153     -14.027  -7.149  63.424  1.00 53.81           C  
ANISOU 5191  CB  ALA D 153     5605   6168   8674    372   -240   -481       C  
ATOM   5192  N   SER D 154     -11.114  -5.914  62.991  1.00 57.61           N  
ANISOU 5192  N   SER D 154     6128   6615   9148    352   -272   -595       N  
ATOM   5193  CA  SER D 154      -9.905  -5.373  63.604  1.00 59.67           C  
ANISOU 5193  CA  SER D 154     6412   6881   9377    342   -277   -645       C  
ATOM   5194  C   SER D 154      -9.633  -3.906  63.219  1.00 60.09           C  
ANISOU 5194  C   SER D 154     6483   6911   9436    351   -244   -695       C  
ATOM   5195  O   SER D 154      -8.965  -3.202  63.956  1.00 62.64           O  
ANISOU 5195  O   SER D 154     6829   7245   9728    347   -233   -735       O  
ATOM   5196  CB  SER D 154      -8.707  -6.229  63.240  1.00 59.32           C  
ANISOU 5196  CB  SER D 154     6366   6829   9342    325   -331   -650       C  
ATOM   5197  OG  SER D 154      -8.393  -6.045  61.880  1.00 56.94           O  
ANISOU 5197  OG  SER D 154     6058   6491   9085    325   -343   -661       O  
ATOM   5198  N   THR D 155     -10.135  -3.448  62.075  1.00 56.63           N  
ANISOU 5198  N   THR D 155     6036   6443   9039    361   -230   -693       N  
ATOM   5199  CA  THR D 155     -10.023  -2.029  61.706  1.00 57.19           C  
ANISOU 5199  CA  THR D 155     6122   6491   9116    371   -195   -737       C  
ATOM   5200  C   THR D 155     -11.293  -1.207  62.025  1.00 57.41           C  
ANISOU 5200  C   THR D 155     6150   6526   9137    390   -142   -729       C  
ATOM   5201  O   THR D 155     -11.342  -0.005  61.774  1.00 58.18           O  
ANISOU 5201  O   THR D 155     6261   6607   9239    399   -109   -763       O  
ATOM   5202  CB  THR D 155      -9.694  -1.864  60.204  1.00 55.54           C  
ANISOU 5202  CB  THR D 155     5905   6241   8955    371   -209   -748       C  
ATOM   5203  OG1 THR D 155     -10.895  -2.019  59.429  1.00 53.37           O  
ANISOU 5203  OG1 THR D 155     5610   5953   8715    384   -194   -710       O  
ATOM   5204  CG2 THR D 155      -8.661  -2.895  59.773  1.00 55.35           C  
ANISOU 5204  CG2 THR D 155     5875   6212   8944    354   -264   -744       C  
ATOM   5205  N   TRP D 156     -12.329  -1.843  62.553  1.00 53.32           N  
ANISOU 5205  N   TRP D 156     5618   6031   8610    395   -133   -684       N  
ATOM   5206  CA  TRP D 156     -13.485  -1.096  63.044  1.00 53.60           C  
ANISOU 5206  CA  TRP D 156     5655   6078   8632    412    -83   -677       C  
ATOM   5207  C   TRP D 156     -13.219  -0.549  64.458  1.00 54.28           C  
ANISOU 5207  C   TRP D 156     5764   6195   8666    411    -62   -704       C  
ATOM   5208  O   TRP D 156     -12.658  -1.251  65.295  1.00 55.72           O  
ANISOU 5208  O   TRP D 156     5950   6402   8818    398    -87   -699       O  
ATOM   5209  CB  TRP D 156     -14.744  -1.979  63.044  1.00 53.64           C  
ANISOU 5209  CB  TRP D 156     5637   6096   8648    419    -81   -617       C  
ATOM   5210  CG  TRP D 156     -15.338  -2.117  61.716  1.00 53.32           C  
ANISOU 5210  CG  TRP D 156     5577   6025   8657    427    -83   -594       C  
ATOM   5211  CD1 TRP D 156     -15.110  -3.104  60.830  1.00 52.99           C  
ANISOU 5211  CD1 TRP D 156     5518   5968   8649    419   -123   -569       C  
ATOM   5212  CD2 TRP D 156     -16.257  -1.217  61.091  1.00 53.29           C  
ANISOU 5212  CD2 TRP D 156     5569   6001   8676    444    -43   -596       C  
ATOM   5213  NE1 TRP D 156     -15.826  -2.890  59.678  1.00 52.75           N  
ANISOU 5213  NE1 TRP D 156     5472   5910   8662    430   -111   -554       N  
ATOM   5214  CE2 TRP D 156     -16.539  -1.734  59.817  1.00 52.93           C  
ANISOU 5214  CE2 TRP D 156     5503   5929   8679    446    -62   -570       C  
ATOM   5215  CE3 TRP D 156     -16.865  -0.021  61.486  1.00 53.52           C  
ANISOU 5215  CE3 TRP D 156     5611   6034   8692    459      7   -617       C  
ATOM   5216  CZ2 TRP D 156     -17.400  -1.110  58.942  1.00 52.80           C  
ANISOU 5216  CZ2 TRP D 156     5479   5889   8695    461    -33   -565       C  
ATOM   5217  CZ3 TRP D 156     -17.703   0.599  60.619  1.00 53.40           C  
ANISOU 5217  CZ3 TRP D 156     5588   5995   8708    474     35   -612       C  
ATOM   5218  CH2 TRP D 156     -17.966   0.060  59.354  1.00 53.04           C  
ANISOU 5218  CH2 TRP D 156     5522   5922   8710    475     16   -586       C  
ATOM   5219  N   LYS D 157     -13.627   0.686  64.741  1.00 55.63           N  
ANISOU 5219  N   LYS D 157     5948   6363   8824    424    -16   -731       N  
ATOM   5220  CA  LYS D 157     -13.436   1.222  66.090  1.00 60.10           C  
ANISOU 5220  CA  LYS D 157     6535   6960   9341    423      5   -755       C  
ATOM   5221  C   LYS D 157     -14.747   1.547  66.819  1.00 62.29           C  
ANISOU 5221  C   LYS D 157     6809   7259   9598    439     49   -733       C  
ATOM   5222  O   LYS D 157     -15.135   0.847  67.749  1.00 64.55           O  
ANISOU 5222  O   LYS D 157     7090   7578   9858    436     45   -703       O  
ATOM   5223  CB  LYS D 157     -12.554   2.476  66.041  1.00 62.07           C  
ANISOU 5223  CB  LYS D 157     6810   7193   9582    423     21   -816       C  
ATOM   5224  CG  LYS D 157     -12.175   3.036  67.414  1.00 67.10           C  
ANISOU 5224  CG  LYS D 157     7469   7859  10167    421     39   -846       C  
ATOM   5225  CD  LYS D 157     -11.257   4.232  67.262  1.00 69.42           C  
ANISOU 5225  CD  LYS D 157     7787   8134  10457    421     52   -906       C  
ATOM   5226  CE  LYS D 157     -10.360   4.418  68.471  1.00 73.25           C  
ANISOU 5226  CE  LYS D 157     8293   8644  10893    410     47   -938       C  
ATOM   5227  NZ  LYS D 157      -9.065   5.097  68.099  1.00 74.97           N  
ANISOU 5227  NZ  LYS D 157     8530   8840  11114    402     35   -992       N  
ATOM   5228  N   LYS D 158     -15.410   2.624  66.423  1.00 61.26           N  
ANISOU 5228  N   LYS D 158     6682   7112   9482    455     90   -747       N  
ATOM   5229  CA  LYS D 158     -16.642   3.015  67.086  1.00 63.59           C  
ANISOU 5229  CA  LYS D 158     6975   7428   9760    470    132   -728       C  
ATOM   5230  C   LYS D 158     -17.801   2.429  66.315  1.00 60.35           C  
ANISOU 5230  C   LYS D 158     6538   7007   9384    479    135   -679       C  
ATOM   5231  O   LYS D 158     -17.896   2.669  65.126  1.00 57.50           O  
ANISOU 5231  O   LYS D 158     6169   6614   9065    484    134   -681       O  
ATOM   5232  CB  LYS D 158     -16.768   4.534  67.146  1.00 66.30           C  
ANISOU 5232  CB  LYS D 158     7337   7759  10095    483    177   -772       C  
ATOM   5233  CG  LYS D 158     -18.009   5.025  67.866  1.00 68.36           C  
ANISOU 5233  CG  LYS D 158     7597   8041  10336    500    223   -756       C  
ATOM   5234  CD  LYS D 158     -18.475   6.357  67.317  1.00 71.23           C  
ANISOU 5234  CD  LYS D 158     7967   8380  10716    516    265   -784       C  
ATOM   5235  CE  LYS D 158     -17.461   7.473  67.545  1.00 70.10           C  
ANISOU 5235  CE  LYS D 158     7852   8228  10555    514    276   -844       C  
ATOM   5236  NZ  LYS D 158     -17.839   8.734  66.818  1.00 72.84           N  
ANISOU 5236  NZ  LYS D 158     8206   8546  10925    529    312   -871       N  
ATOM   5237  N   PHE D 159     -18.630   1.597  66.933  1.00 60.34           N  
ANISOU 5237  N   PHE D 159     6522   7034   9369    481    135   -633       N  
ATOM   5238  CA  PHE D 159     -19.831   1.156  66.236  1.00 60.11           C  
ANISOU 5238  CA  PHE D 159     6468   6997   9373    491    143   -587       C  
ATOM   5239  C   PHE D 159     -21.016   1.295  67.171  1.00 61.67           C  
ANISOU 5239  C   PHE D 159     6663   7224   9544    503    180   -563       C  
ATOM   5240  O   PHE D 159     -21.244   0.431  68.023  1.00 62.46           O  
ANISOU 5240  O   PHE D 159     6757   7356   9620    497    168   -532       O  
ATOM   5241  CB  PHE D 159     -19.681  -0.293  65.771  1.00 59.43           C  
ANISOU 5241  CB  PHE D 159     6362   6911   9309    479     95   -545       C  
ATOM   5242  CG  PHE D 159     -20.591  -0.687  64.639  1.00 58.79           C  
ANISOU 5242  CG  PHE D 159     6257   6807   9273    488     94   -507       C  
ATOM   5243  CD1 PHE D 159     -21.843  -1.176  64.882  1.00 59.32           C  
ANISOU 5243  CD1 PHE D 159     6306   6892   9341    497    110   -460       C  
ATOM   5244  CD2 PHE D 159     -20.165  -0.614  63.328  1.00 57.64           C  
ANISOU 5244  CD2 PHE D 159     6105   6624   9170    486     77   -517       C  
ATOM   5245  CE1 PHE D 159     -22.657  -1.556  63.829  1.00 58.71           C  
ANISOU 5245  CE1 PHE D 159     6206   6794   9306    504    108   -425       C  
ATOM   5246  CE2 PHE D 159     -20.983  -1.002  62.274  1.00 57.01           C  
ANISOU 5246  CE2 PHE D 159     6004   6525   9134    494     75   -482       C  
ATOM   5247  CZ  PHE D 159     -22.213  -1.464  62.522  1.00 57.55           C  
ANISOU 5247  CZ  PHE D 159     6055   6610   9202    503     90   -437       C  
ATOM   5248  N   GLU D 160     -21.828   2.319  66.936  1.00 64.08           N  
ANISOU 5248  N   GLU D 160     6971   7519   9858    521    223   -573       N  
ATOM   5249  CA  GLU D 160     -22.915   2.648  67.833  1.00 67.87           C  
ANISOU 5249  CA  GLU D 160     7450   8025  10311    534    263   -557       C  
ATOM   5250  C   GLU D 160     -24.181   2.514  67.024  1.00 65.61           C  
ANISOU 5250  C   GLU D 160     7141   7726  10061    548    280   -518       C  
ATOM   5251  O   GLU D 160     -24.220   2.996  65.879  1.00 62.32           O  
ANISOU 5251  O   GLU D 160     6721   7275   9683    554    285   -529       O  
ATOM   5252  CB  GLU D 160     -22.772   4.072  68.393  1.00 71.04           C  
ANISOU 5252  CB  GLU D 160     7876   8429  10688    543    304   -606       C  
ATOM   5253  CG  GLU D 160     -21.692   4.258  69.461  1.00 74.71           C  
ANISOU 5253  CG  GLU D 160     8364   8915  11108    531    295   -642       C  
ATOM   5254  CD  GLU D 160     -21.574   5.715  69.929  1.00 78.23           C  
ANISOU 5254  CD  GLU D 160     8833   9358  11531    541    336   -691       C  
ATOM   5255  OE1 GLU D 160     -22.325   6.564  69.410  1.00 77.05           O  
ANISOU 5255  OE1 GLU D 160     8683   9193  11401    557    371   -697       O  
ATOM   5256  OE2 GLU D 160     -20.732   6.016  70.809  1.00 82.42           O  
ANISOU 5256  OE2 GLU D 160     9385   9906  12026    533    333   -724       O  
ATOM   5257  N   VAL D 161     -25.209   1.865  67.581  1.00 65.67           N  
ANISOU 5257  N   VAL D 161     7134   7760  10058    552    289   -473       N  
ATOM   5258  CA  VAL D 161     -26.474   1.763  66.858  1.00 64.16           C  
ANISOU 5258  CA  VAL D 161     6921   7558   9898    566    308   -436       C  
ATOM   5259  C   VAL D 161     -27.657   2.369  67.624  1.00 68.14           C  
ANISOU 5259  C   VAL D 161     7426   8084  10380    583    356   -426       C  
ATOM   5260  O   VAL D 161     -27.917   2.048  68.789  1.00 72.39           O  
ANISOU 5260  O   VAL D 161     7966   8658  10880    581    362   -412       O  
ATOM   5261  CB  VAL D 161     -26.784   0.318  66.498  1.00 62.27           C  
ANISOU 5261  CB  VAL D 161     6657   7323   9679    558    271   -382       C  
ATOM   5262  CG1 VAL D 161     -28.004   0.273  65.591  1.00 59.78           C  
ANISOU 5262  CG1 VAL D 161     6320   6990   9402    573    289   -348       C  
ATOM   5263  CG2 VAL D 161     -25.597  -0.315  65.800  1.00 59.78           C  
ANISOU 5263  CG2 VAL D 161     6342   6988   9385    542    222   -392       C  
ATOM   5264  N   TYR D 162     -28.371   3.255  66.941  1.00 66.23           N  
ANISOU 5264  N   TYR D 162     7181   7820  10162    600    390   -434       N  
ATOM   5265  CA  TYR D 162     -29.410   4.072  67.565  1.00 69.78           C  
ANISOU 5265  CA  TYR D 162     7635   8286  10592    617    440   -434       C  
ATOM   5266  C   TYR D 162     -30.821   3.765  67.019  1.00 68.90           C  
ANISOU 5266  C   TYR D 162     7499   8170  10508    631    457   -388       C  
ATOM   5267  O   TYR D 162     -31.014   3.619  65.805  1.00 65.12           O  
ANISOU 5267  O   TYR D 162     7007   7661  10074    634    447   -375       O  
ATOM   5268  CB  TYR D 162     -29.088   5.563  67.374  1.00 70.21           C  
ANISOU 5268  CB  TYR D 162     7711   8320  10646    627    472   -489       C  
ATOM   5269  CG  TYR D 162     -27.906   6.070  68.177  1.00 72.54           C  
ANISOU 5269  CG  TYR D 162     8033   8625  10905    617    467   -536       C  
ATOM   5270  CD1 TYR D 162     -28.003   6.267  69.547  1.00 77.91           C  
ANISOU 5270  CD1 TYR D 162     8725   9341  11537    617    486   -544       C  
ATOM   5271  CD2 TYR D 162     -26.701   6.375  67.562  1.00 69.86           C  
ANISOU 5271  CD2 TYR D 162     7706   8259  10579    607    444   -575       C  
ATOM   5272  CE1 TYR D 162     -26.933   6.741  70.282  1.00 80.25           C  
ANISOU 5272  CE1 TYR D 162     9045   9646  11800    608    482   -587       C  
ATOM   5273  CE2 TYR D 162     -25.621   6.845  68.293  1.00 72.28           C  
ANISOU 5273  CE2 TYR D 162     8036   8574  10852    598    440   -619       C  
ATOM   5274  CZ  TYR D 162     -25.748   7.026  69.646  1.00 77.36           C  
ANISOU 5274  CZ  TYR D 162     8692   9254  11449    599    459   -625       C  
ATOM   5275  OH  TYR D 162     -24.685   7.494  70.368  1.00 80.03           O  
ANISOU 5275  OH  TYR D 162     9053   9601  11754    590    454   -668       O  
ATOM   5276  N   GLU D 163     -31.792   3.665  67.924  1.00 66.64           N  
ANISOU 5276  N   GLU D 163     7207   7916  10196    638    483   -362       N  
ATOM   5277  CA  GLU D 163     -33.182   3.479  67.551  1.00 66.94           C  
ANISOU 5277  CA  GLU D 163     7224   7955  10255    653    505   -321       C  
ATOM   5278  C   GLU D 163     -34.004   4.631  68.116  1.00 70.78           C  
ANISOU 5278  C   GLU D 163     7721   8452  10722    671    558   -337       C  
ATOM   5279  O   GLU D 163     -34.077   4.797  69.336  1.00 74.93           O  
ANISOU 5279  O   GLU D 163     8257   9010  11204    671    575   -344       O  
ATOM   5280  CB  GLU D 163     -33.690   2.139  68.063  1.00 68.41           C  
ANISOU 5280  CB  GLU D 163     7391   8170  10431    645    483   -267       C  
ATOM   5281  CG  GLU D 163     -35.206   2.045  68.292  1.00 71.45           C  
ANISOU 5281  CG  GLU D 163     7759   8573  10816    660    515   -226       C  
ATOM   5282  CD  GLU D 163     -35.625   0.651  68.737  1.00 74.13           C  
ANISOU 5282  CD  GLU D 163     8080   8939  11148    650    490   -173       C  
ATOM   5283  OE1 GLU D 163     -35.677   0.390  69.960  1.00 77.96           O  
ANISOU 5283  OE1 GLU D 163     8570   9460  11590    646    494   -166       O  
ATOM   5284  OE2 GLU D 163     -35.878  -0.191  67.854  1.00 73.18           O  
ANISOU 5284  OE2 GLU D 163     7939   8803  11063    647    465   -138       O  
ATOM   5285  N   ASN D 164     -34.613   5.422  67.227  1.00 74.23           N  
ANISOU 5285  N   ASN D 164     8153   8861  11189    687    585   -345       N  
ATOM   5286  CA  ASN D 164     -35.287   6.681  67.589  1.00 77.71           C  
ANISOU 5286  CA  ASN D 164     8606   9305  11617    705    637   -368       C  
ATOM   5287  C   ASN D 164     -34.374   7.650  68.335  1.00 79.55           C  
ANISOU 5287  C   ASN D 164     8868   9544  11814    702    650   -423       C  
ATOM   5288  O   ASN D 164     -34.781   8.257  69.326  1.00 84.04           O  
ANISOU 5288  O   ASN D 164     9447  10137  12348    711    683   -435       O  
ATOM   5289  CB  ASN D 164     -36.529   6.406  68.428  1.00 82.10           C  
ANISOU 5289  CB  ASN D 164     9150   9895  12150    714    663   -331       C  
ATOM   5290  CG  ASN D 164     -37.740   6.110  67.575  1.00 81.98           C  
ANISOU 5290  CG  ASN D 164     9110   9867  12172    727    674   -289       C  
ATOM   5291  OD1 ASN D 164     -38.316   5.008  67.630  1.00 80.66           O  
ANISOU 5291  OD1 ASN D 164     8921   9715  12010    723    657   -240       O  
ATOM   5292  ND2 ASN D 164     -38.141   7.098  66.769  1.00 83.84           N  
ANISOU 5292  ND2 ASN D 164     9348  10074  12435    742    702   -308       N  
ATOM   5293  N   ASN D 165     -33.143   7.779  67.850  1.00 77.50           N  
ANISOU 5293  N   ASN D 165     8620   9261  11564    691    623   -457       N  
ATOM   5294  CA  ASN D 165     -32.121   8.607  68.472  1.00 79.51           C  
ANISOU 5294  CA  ASN D 165     8902   9518  11789    686    628   -510       C  
ATOM   5295  C   ASN D 165     -31.846   8.314  69.943  1.00 84.29           C  
ANISOU 5295  C   ASN D 165     9518  10165  12342    677    627   -512       C  
ATOM   5296  O   ASN D 165     -31.569   9.235  70.705  1.00 87.34           O  
ANISOU 5296  O   ASN D 165     9926  10562  12697    681    652   -550       O  
ATOM   5297  CB  ASN D 165     -32.472  10.089  68.330  1.00 81.39           C  
ANISOU 5297  CB  ASN D 165     9155   9741  12028    703    674   -547       C  
ATOM   5298  CG  ASN D 165     -32.158  10.634  66.948  1.00 77.45           C  
ANISOU 5298  CG  ASN D 165     8656   9197  11574    707    670   -568       C  
ATOM   5299  OD1 ASN D 165     -31.001  10.991  66.636  1.00 74.95           O  
ANISOU 5299  OD1 ASN D 165     8355   8861  11261    697    652   -607       O  
ATOM   5300  ND2 ASN D 165     -33.192  10.710  66.103  1.00 77.77           N  
ANISOU 5300  ND2 ASN D 165     8679   9220  11649    721    687   -543       N  
ATOM   5301  N   GLN D 166     -31.903   7.052  70.351  1.00 79.31           N  
ANISOU 5301  N   GLN D 166     8874   9558  11703    666    597   -472       N  
ATOM   5302  CA  GLN D 166     -31.364   6.694  71.662  1.00 82.94           C  
ANISOU 5302  CA  GLN D 166     9345  10053  12114    654    587   -478       C  
ATOM   5303  C   GLN D 166     -30.543   5.407  71.586  1.00 80.53           C  
ANISOU 5303  C   GLN D 166     9032   9753  11813    634    534   -458       C  
ATOM   5304  O   GLN D 166     -30.789   4.548  70.740  1.00 76.58           O  
ANISOU 5304  O   GLN D 166     8511   9238  11347    630    509   -422       O  
ATOM   5305  CB  GLN D 166     -32.471   6.569  72.690  1.00 86.84           C  
ANISOU 5305  CB  GLN D 166     9833  10585  12579    663    616   -449       C  
ATOM   5306  CG  GLN D 166     -33.606   5.724  72.230  1.00 85.07           C  
ANISOU 5306  CG  GLN D 166     9580  10362  12379    669    614   -392       C  
ATOM   5307  CD  GLN D 166     -34.767   5.743  73.200  1.00 89.32           C  
ANISOU 5307  CD  GLN D 166    10113  10936  12889    680    648   -366       C  
ATOM   5308  OE1 GLN D 166     -35.374   6.801  73.451  1.00 93.12           O  
ANISOU 5308  OE1 GLN D 166    10603  11419  13361    696    691   -385       O  
ATOM   5309  NE2 GLN D 166     -35.092   4.565  73.757  1.00 88.97           N  
ANISOU 5309  NE2 GLN D 166    10053  10919  12831    671    628   -322       N  
ATOM   5310  N   LYS D 167     -29.553   5.293  72.468  1.00 81.25           N  
ANISOU 5310  N   LYS D 167     9140   9862  11868    620    517   -481       N  
ATOM   5311  CA  LYS D 167     -28.493   4.303  72.328  1.00 79.05           C  
ANISOU 5311  CA  LYS D 167     8860   9581  11593    600    466   -477       C  
ATOM   5312  C   LYS D 167     -28.982   2.888  72.600  1.00 79.25           C  
ANISOU 5312  C   LYS D 167     8864   9630  11616    592    440   -421       C  
ATOM   5313  O   LYS D 167     -29.598   2.633  73.634  1.00 83.55           O  
ANISOU 5313  O   LYS D 167     9406  10209  12129    594    455   -400       O  
ATOM   5314  CB  LYS D 167     -27.340   4.652  73.275  1.00 81.68           C  
ANISOU 5314  CB  LYS D 167     9218   9930  11885    589    459   -519       C  
ATOM   5315  CG  LYS D 167     -26.007   3.990  72.943  1.00 79.09           C  
ANISOU 5315  CG  LYS D 167     8895   9591  11565    569    409   -532       C  
ATOM   5316  CD  LYS D 167     -24.977   4.256  74.038  1.00 82.56           C  
ANISOU 5316  CD  LYS D 167     9358  10052  11960    559    403   -569       C  
ATOM   5317  CE  LYS D 167     -23.633   3.585  73.753  1.00 80.10           C  
ANISOU 5317  CE  LYS D 167     9052   9730  11654    539    353   -582       C  
ATOM   5318  NZ  LYS D 167     -22.761   4.460  72.918  1.00 76.16           N  
ANISOU 5318  NZ  LYS D 167     8566   9195  11175    538    352   -629       N  
ATOM   5319  N   LEU D 168     -28.723   1.972  71.671  1.00 77.16           N  
ANISOU 5319  N   LEU D 168     8583   9346  11387    583    402   -396       N  
ATOM   5320  CA  LEU D 168     -28.988   0.563  71.929  1.00 77.35           C  
ANISOU 5320  CA  LEU D 168     8589   9392  11409    573    371   -346       C  
ATOM   5321  C   LEU D 168     -27.768  -0.058  72.578  1.00 78.51           C  
ANISOU 5321  C   LEU D 168     8748   9554  11529    553    333   -360       C  
ATOM   5322  O   LEU D 168     -26.644   0.282  72.215  1.00 76.59           O  
ANISOU 5322  O   LEU D 168     8518   9290  11291    545    315   -398       O  
ATOM   5323  CB  LEU D 168     -29.331  -0.186  70.644  1.00 72.49           C  
ANISOU 5323  CB  LEU D 168     7949   8749  10843    572    347   -311       C  
ATOM   5324  CG  LEU D 168     -30.499   0.332  69.807  1.00 70.66           C  
ANISOU 5324  CG  LEU D 168     7704   8497  10645    591    379   -295       C  
ATOM   5325  CD1 LEU D 168     -30.811  -0.675  68.695  1.00 66.44           C  
ANISOU 5325  CD1 LEU D 168     7145   7944  10155    588    349   -253       C  
ATOM   5326  CD2 LEU D 168     -31.728   0.632  70.676  1.00 74.86           C  
ANISOU 5326  CD2 LEU D 168     8233   9059  11152    605    422   -276       C  
ATOM   5327  N   PRO D 169     -27.977  -0.988  73.526  1.00 73.58           N  
ANISOU 5327  N   PRO D 169     8117   8965  10876    545    319   -327       N  
ATOM   5328  CA  PRO D 169     -26.889  -1.691  74.216  1.00 75.19           C  
ANISOU 5328  CA  PRO D 169     8330   9187  11053    526    282   -335       C  
ATOM   5329  C   PRO D 169     -26.233  -2.752  73.337  1.00 71.00           C  
ANISOU 5329  C   PRO D 169     7786   8636  10553    511    231   -317       C  
ATOM   5330  O   PRO D 169     -26.598  -3.927  73.417  1.00 71.49           O  
ANISOU 5330  O   PRO D 169     7831   8713  10620    505    206   -271       O  
ATOM   5331  CB  PRO D 169     -27.601  -2.342  75.404  1.00 80.31           C  
ANISOU 5331  CB  PRO D 169     8971   9877  11665    525    289   -299       C  
ATOM   5332  CG  PRO D 169     -28.953  -2.627  74.889  1.00 79.58           C  
ANISOU 5332  CG  PRO D 169     8856   9782  11599    537    306   -254       C  
ATOM   5333  CD  PRO D 169     -29.294  -1.451  73.992  1.00 76.63           C  
ANISOU 5333  CD  PRO D 169     8486   9376  11255    553    339   -280       C  
ATOM   5334  N   VAL D 170     -25.294  -2.347  72.493  1.00 71.20           N  
ANISOU 5334  N   VAL D 170     7821   8630  10603    507    215   -352       N  
ATOM   5335  CA  VAL D 170     -24.663  -3.286  71.571  1.00 67.52           C  
ANISOU 5335  CA  VAL D 170     7342   8142  10169    494    167   -337       C  
ATOM   5336  C   VAL D 170     -23.636  -4.175  72.282  1.00 68.87           C  
ANISOU 5336  C   VAL D 170     7520   8334  10313    475    125   -337       C  
ATOM   5337  O   VAL D 170     -22.877  -3.708  73.133  1.00 70.96           O  
ANISOU 5337  O   VAL D 170     7806   8613  10542    469    129   -373       O  
ATOM   5338  CB  VAL D 170     -23.990  -2.544  70.407  1.00 65.11           C  
ANISOU 5338  CB  VAL D 170     7044   7796   9898    496    163   -375       C  
ATOM   5339  CG1 VAL D 170     -23.424  -3.517  69.412  1.00 63.69           C  
ANISOU 5339  CG1 VAL D 170     6851   7594   9755    484    116   -357       C  
ATOM   5340  CG2 VAL D 170     -25.000  -1.655  69.721  1.00 65.23           C  
ANISOU 5340  CG2 VAL D 170     7054   7791   9939    516    205   -375       C  
ATOM   5341  N   ARG D 171     -23.629  -5.463  71.945  1.00 66.76           N  
ANISOU 5341  N   ARG D 171     8902   7848   8614   1465  -1148   2354       N  
ATOM   5342  CA  ARG D 171     -22.642  -6.379  72.503  1.00 68.69           C  
ANISOU 5342  CA  ARG D 171     9150   8086   8864   1468  -1170   2348       C  
ATOM   5343  C   ARG D 171     -22.111  -7.357  71.448  1.00 65.54           C  
ANISOU 5343  C   ARG D 171     8722   7705   8475   1480  -1180   2340       C  
ATOM   5344  O   ARG D 171     -22.794  -7.663  70.463  1.00 62.63           O  
ANISOU 5344  O   ARG D 171     8338   7352   8108   1486  -1171   2337       O  
ATOM   5345  CB  ARG D 171     -23.234  -7.143  73.688  1.00 72.65           C  
ANISOU 5345  CB  ARG D 171     9678   8569   9356   1463  -1178   2343       C  
ATOM   5346  CG  ARG D 171     -24.031  -8.351  73.292  1.00 71.98           C  
ANISOU 5346  CG  ARG D 171     9589   8490   9271   1470  -1180   2333       C  
ATOM   5347  CD  ARG D 171     -24.956  -8.784  74.396  1.00 76.55           C  
ANISOU 5347  CD  ARG D 171    10197   9051   9839   1465  -1181   2331       C  
ATOM   5348  NE  ARG D 171     -26.255  -9.111  73.824  1.00 76.14           N  
ANISOU 5348  NE  ARG D 171    10142   9006   9783   1467  -1168   2328       N  
ATOM   5349  CZ  ARG D 171     -26.601 -10.317  73.395  1.00 77.24           C  
ANISOU 5349  CZ  ARG D 171    10271   9152   9924   1474  -1175   2319       C  
ATOM   5350  NH1 ARG D 171     -25.759 -11.343  73.496  1.00 78.65           N  
ANISOU 5350  NH1 ARG D 171    10446   9330  10108   1481  -1194   2312       N  
ATOM   5351  NH2 ARG D 171     -27.801 -10.496  72.874  1.00 77.31           N  
ANISOU 5351  NH2 ARG D 171    10277   9168   9929   1476  -1162   2318       N  
ATOM   5352  N   LEU D 172     -20.883  -7.826  71.665  1.00 66.36           N  
ANISOU 5352  N   LEU D 172     8821   7808   8586   1483  -1199   2337       N  
ATOM   5353  CA  LEU D 172     -20.233  -8.743  70.747  1.00 64.70           C  
ANISOU 5353  CA  LEU D 172     8584   7614   8386   1494  -1209   2330       C  
ATOM   5354  C   LEU D 172     -20.473 -10.183  71.184  1.00 67.15           C  
ANISOU 5354  C   LEU D 172     8903   7917   8695   1498  -1223   2319       C  
ATOM   5355  O   LEU D 172     -20.238 -10.535  72.343  1.00 70.32           O  
ANISOU 5355  O   LEU D 172     9325   8301   9091   1494  -1235   2318       O  
ATOM   5356  CB  LEU D 172     -18.738  -8.441  70.689  1.00 64.44           C  
ANISOU 5356  CB  LEU D 172     8539   7585   8362   1495  -1221   2333       C  
ATOM   5357  CG  LEU D 172     -17.782  -9.174  69.744  1.00 63.50           C  
ANISOU 5357  CG  LEU D 172     8390   7482   8255   1506  -1233   2326       C  
ATOM   5358  CD1 LEU D 172     -18.062  -8.853  68.271  1.00 60.17           C  
ANISOU 5358  CD1 LEU D 172     7941   7082   7838   1512  -1219   2327       C  
ATOM   5359  CD2 LEU D 172     -16.346  -8.816  70.114  1.00 64.78           C  
ANISOU 5359  CD2 LEU D 172     8548   7642   8423   1504  -1247   2331       C  
ATOM   5360  N   VAL D 173     -20.946 -11.018  70.263  1.00 66.35           N  
ANISOU 5360  N   VAL D 173     8785   7829   8597   1507  -1222   2312       N  
ATOM   5361  CA  VAL D 173     -21.209 -12.408  70.604  1.00 68.66           C  
ANISOU 5361  CA  VAL D 173     9085   8116   8888   1512  -1234   2302       C  
ATOM   5362  C   VAL D 173     -20.095 -13.345  70.078  1.00 68.56           C  
ANISOU 5362  C   VAL D 173     9051   8112   8886   1522  -1251   2295       C  
ATOM   5363  O   VAL D 173     -19.453 -14.023  70.885  1.00 71.63           O  
ANISOU 5363  O   VAL D 173     9451   8490   9275   1523  -1268   2291       O  
ATOM   5364  CB  VAL D 173     -22.607 -12.849  70.137  1.00 68.19           C  
ANISOU 5364  CB  VAL D 173     9026   8061   8823   1513  -1222   2299       C  
ATOM   5365  CG1 VAL D 173     -23.629 -12.290  71.082  1.00 71.11           C  
ANISOU 5365  CG1 VAL D 173     9423   8414   9180   1503  -1211   2303       C  
ATOM   5366  CG2 VAL D 173     -22.908 -12.386  68.731  1.00 64.20           C  
ANISOU 5366  CG2 VAL D 173     8493   7577   8322   1518  -1207   2301       C  
ATOM   5367  N   SER D 174     -19.852 -13.414  68.769  1.00 67.47           N  
ANISOU 5367  N   SER D 174     8885   7995   8757   1530  -1247   2293       N  
ATOM   5368  CA  SER D 174     -18.711 -14.213  68.308  1.00 68.06           C  
ANISOU 5368  CA  SER D 174     8940   8078   8842   1539  -1263   2287       C  
ATOM   5369  C   SER D 174     -17.746 -13.396  67.481  1.00 65.36           C  
ANISOU 5369  C   SER D 174     8573   7751   8509   1541  -1261   2292       C  
ATOM   5370  O   SER D 174     -18.139 -12.374  66.915  1.00 62.73           O  
ANISOU 5370  O   SER D 174     8234   7427   8175   1538  -1244   2299       O  
ATOM   5371  CB  SER D 174     -19.168 -15.425  67.491  1.00 69.21           C  
ANISOU 5371  CB  SER D 174     9071   8234   8990   1549  -1265   2277       C  
ATOM   5372  OG  SER D 174     -18.052 -16.142  66.967  1.00 70.30           O  
ANISOU 5372  OG  SER D 174     9189   8381   9139   1559  -1280   2272       O  
ATOM   5373  N   TYR D 175     -16.489 -13.844  67.423  1.00 65.96           N  
ANISOU 5373  N   TYR D 175     8637   7830   8594   1547  -1277   2289       N  
ATOM   5374  CA  TYR D 175     -15.506 -13.273  66.508  1.00 64.12           C  
ANISOU 5374  CA  TYR D 175     8377   7613   8371   1551  -1277   2292       C  
ATOM   5375  C   TYR D 175     -14.799 -14.362  65.709  1.00 64.87           C  
ANISOU 5375  C   TYR D 175     8450   7722   8477   1563  -1289   2283       C  
ATOM   5376  O   TYR D 175     -14.524 -15.432  66.238  1.00 67.45           O  
ANISOU 5376  O   TYR D 175     8784   8040   8804   1567  -1304   2276       O  
ATOM   5377  CB  TYR D 175     -14.472 -12.434  67.263  1.00 64.92           C  
ANISOU 5377  CB  TYR D 175     8487   7707   8474   1544  -1284   2300       C  
ATOM   5378  CG  TYR D 175     -13.339 -11.945  66.366  1.00 63.73           C  
ANISOU 5378  CG  TYR D 175     8308   7573   8334   1548  -1286   2303       C  
ATOM   5379  CD1 TYR D 175     -13.608 -11.131  65.264  1.00 61.06           C  
ANISOU 5379  CD1 TYR D 175     7951   7251   7999   1549  -1269   2308       C  
ATOM   5380  CD2 TYR D 175     -12.010 -12.300  66.611  1.00 65.67           C  
ANISOU 5380  CD2 TYR D 175     8546   7819   8588   1552  -1304   2301       C  
ATOM   5381  CE1 TYR D 175     -12.590 -10.686  64.425  1.00 60.47           C  
ANISOU 5381  CE1 TYR D 175     7851   7192   7934   1553  -1271   2310       C  
ATOM   5382  CE2 TYR D 175     -10.987 -11.854  65.778  1.00 65.05           C  
ANISOU 5382  CE2 TYR D 175     8441   7756   8519   1555  -1306   2304       C  
ATOM   5383  CZ  TYR D 175     -11.291 -11.043  64.690  1.00 62.50           C  
ANISOU 5383  CZ  TYR D 175     8100   7448   8198   1556  -1289   2309       C  
ATOM   5384  OH  TYR D 175     -10.318 -10.586  63.841  1.00 62.29           O  
ANISOU 5384  OH  TYR D 175     8048   7438   8181   1560  -1290   2312       O  
ATOM   5385  N   SER D 176     -14.499 -14.095  64.441  1.00 62.42           N  
ANISOU 5385  N   SER D 176     8111   7431   8174   1569  -1282   2283       N  
ATOM   5386  CA  SER D 176     -13.788 -15.069  63.617  1.00 63.37           C  
ANISOU 5386  CA  SER D 176     8208   7565   8305   1580  -1293   2275       C  
ATOM   5387  C   SER D 176     -12.397 -14.572  63.211  1.00 63.34           C  
ANISOU 5387  C   SER D 176     8184   7570   8311   1583  -1300   2278       C  
ATOM   5388  O   SER D 176     -12.313 -13.617  62.450  1.00 61.44           O  
ANISOU 5388  O   SER D 176     7929   7343   8074   1581  -1288   2285       O  
ATOM   5389  CB  SER D 176     -14.606 -15.398  62.373  1.00 62.25           C  
ANISOU 5389  CB  SER D 176     8049   7440   8165   1587  -1280   2271       C  
ATOM   5390  OG  SER D 176     -15.796 -16.075  62.733  1.00 63.62           O  
ANISOU 5390  OG  SER D 176     8239   7604   8330   1585  -1277   2267       O  
ATOM   5391  N   PRO D 177     -11.316 -15.249  63.683  1.00 60.65           N  
ANISOU 5391  N   PRO D 177     7842   7225   7976   1587  -1320   2274       N  
ATOM   5392  CA  PRO D 177      -9.932 -14.759  63.648  1.00 61.58           C  
ANISOU 5392  CA  PRO D 177     7946   7348   8103   1587  -1330   2278       C  
ATOM   5393  C   PRO D 177      -9.369 -14.542  62.248  1.00 61.00           C  
ANISOU 5393  C   PRO D 177     7840   7297   8039   1594  -1325   2278       C  
ATOM   5394  O   PRO D 177     -10.019 -14.826  61.255  1.00 60.36           O  
ANISOU 5394  O   PRO D 177     7746   7229   7960   1600  -1315   2274       O  
ATOM   5395  CB  PRO D 177      -9.157 -15.854  64.379  1.00 64.84           C  
ANISOU 5395  CB  PRO D 177     8365   7752   8519   1592  -1351   2271       C  
ATOM   5396  CG  PRO D 177     -10.179 -16.591  65.185  1.00 65.63           C  
ANISOU 5396  CG  PRO D 177     8491   7836   8609   1590  -1352   2266       C  
ATOM   5397  CD  PRO D 177     -11.386 -16.586  64.307  1.00 63.24           C  
ANISOU 5397  CD  PRO D 177     8182   7542   8303   1592  -1335   2265       C  
ATOM   5398  N   VAL D 178      -8.123 -14.091  62.201  1.00 66.08           N  
ANISOU 5398  N   VAL D 178     8471   7947   8691   1594  -1334   2282       N  
ATOM   5399  CA  VAL D 178      -7.690 -13.074  61.227  1.00 65.13           C  
ANISOU 5399  CA  VAL D 178     8327   7842   8576   1594  -1323   2288       C  
ATOM   5400  C   VAL D 178      -7.751 -13.297  59.695  1.00 64.67           C  
ANISOU 5400  C   VAL D 178     8240   7807   8525   1604  -1314   2284       C  
ATOM   5401  O   VAL D 178      -7.886 -12.284  58.953  1.00 63.15           O  
ANISOU 5401  O   VAL D 178     8035   7625   8333   1601  -1299   2291       O  
ATOM   5402  CB  VAL D 178      -6.271 -12.608  61.542  1.00 67.07           C  
ANISOU 5402  CB  VAL D 178     8565   8089   8828   1592  -1336   2293       C  
ATOM   5403  CG1 VAL D 178      -6.072 -11.169  61.019  1.00 67.29           C  
ANISOU 5403  CG1 VAL D 178     8583   8127   8857   1586  -1322   2305       C  
ATOM   5404  CG2 VAL D 178      -6.048 -12.665  63.062  1.00 66.84           C  
ANISOU 5404  CG2 VAL D 178     8564   8039   8793   1585  -1348   2296       C  
ATOM   5405  N   PRO D 179      -7.594 -14.541  59.189  1.00 54.31           N  
ANISOU 5405  N   PRO D 179     6915   6501   7219   1614  -1323   2273       N  
ATOM   5406  CA  PRO D 179      -7.961 -14.639  57.762  1.00 54.25           C  
ANISOU 5406  CA  PRO D 179     6883   6513   7215   1621  -1311   2270       C  
ATOM   5407  C   PRO D 179      -9.458 -14.289  57.518  1.00 54.12           C  
ANISOU 5407  C   PRO D 179     6877   6497   7190   1617  -1291   2273       C  
ATOM   5408  O   PRO D 179      -9.870 -13.893  56.411  1.00 54.06           O  
ANISOU 5408  O   PRO D 179     6851   6506   7183   1620  -1276   2275       O  
ATOM   5409  CB  PRO D 179      -7.674 -16.089  57.426  1.00 54.29           C  
ANISOU 5409  CB  PRO D 179     6878   6521   7227   1633  -1324   2258       C  
ATOM   5410  CG  PRO D 179      -7.885 -16.783  58.721  1.00 54.31           C  
ANISOU 5410  CG  PRO D 179     6908   6503   7224   1630  -1336   2255       C  
ATOM   5411  CD  PRO D 179      -7.319 -15.850  59.770  1.00 54.36           C  
ANISOU 5411  CD  PRO D 179     6930   6498   7227   1620  -1341   2264       C  
ATOM   5412  N   GLU D 180     -10.243 -14.423  58.583  1.00 57.98           N  
ANISOU 5412  N   GLU D 180     7394   6967   7669   1611  -1291   2273       N  
ATOM   5413  CA  GLU D 180     -11.667 -14.157  58.556  1.00 56.02           C  
ANISOU 5413  CA  GLU D 180     7158   6716   7410   1606  -1274   2276       C  
ATOM   5414  C   GLU D 180     -11.979 -12.712  59.022  1.00 53.81           C  
ANISOU 5414  C   GLU D 180     6891   6430   7123   1595  -1261   2288       C  
ATOM   5415  O   GLU D 180     -12.534 -11.914  58.263  1.00 52.30           O  
ANISOU 5415  O   GLU D 180     6690   6250   6930   1594  -1243   2293       O  
ATOM   5416  CB  GLU D 180     -12.400 -15.202  59.417  1.00 56.97           C  
ANISOU 5416  CB  GLU D 180     7301   6820   7524   1606  -1282   2269       C  
ATOM   5417  CG  GLU D 180     -13.734 -15.658  58.841  1.00 56.58           C  
ANISOU 5417  CG  GLU D 180     7252   6777   7470   1608  -1269   2266       C  
ATOM   5418  CD  GLU D 180     -13.637 -16.030  57.359  1.00 57.47           C  
ANISOU 5418  CD  GLU D 180     7333   6912   7590   1618  -1263   2261       C  
ATOM   5419  OE1 GLU D 180     -12.625 -16.677  56.973  1.00 59.78           O  
ANISOU 5419  OE1 GLU D 180     7609   7211   7892   1626  -1276   2256       O  
ATOM   5420  OE2 GLU D 180     -14.565 -15.661  56.589  1.00 56.16           O  
ANISOU 5420  OE2 GLU D 180     7160   6757   7420   1617  -1245   2264       O  
ATOM   5421  N   ASP D 181     -11.644 -12.409  60.277  1.00 57.60           N  
ANISOU 5421  N   ASP D 181     7393   6892   7599   1587  -1270   2292       N  
ATOM   5422  CA  ASP D 181     -11.708 -11.060  60.801  1.00 56.32           C  
ANISOU 5422  CA  ASP D 181     7244   6723   7431   1577  -1260   2303       C  
ATOM   5423  C   ASP D 181     -13.135 -10.540  60.725  1.00 54.23           C  
ANISOU 5423  C   ASP D 181     6991   6457   7157   1572  -1240   2307       C  
ATOM   5424  O   ASP D 181     -13.345  -9.389  60.328  1.00 52.89           O  
ANISOU 5424  O   ASP D 181     6817   6293   6986   1568  -1224   2316       O  
ATOM   5425  CB  ASP D 181     -10.745 -10.168  60.009  1.00 56.43           C  
ANISOU 5425  CB  ASP D 181     7235   6753   7454   1578  -1257   2310       C  
ATOM   5426  CG  ASP D 181     -10.334  -8.892  60.748  1.00 56.65           C  
ANISOU 5426  CG  ASP D 181     7275   6770   7478   1567  -1254   2321       C  
ATOM   5427  OD1 ASP D 181     -10.623  -8.753  61.970  1.00 56.90           O  
ANISOU 5427  OD1 ASP D 181     7334   6783   7502   1559  -1257   2324       O  
ATOM   5428  OD2 ASP D 181      -9.690  -8.041  60.077  1.00 57.03           O  
ANISOU 5428  OD2 ASP D 181     7305   6831   7532   1567  -1248   2328       O  
ATOM   5429  N   HIS D 182     -14.121 -11.385  61.060  1.00 55.83           N  
ANISOU 5429  N   HIS D 182     6300   6602   8310    282    243    283       N  
ATOM   5430  CA  HIS D 182     -15.543 -10.976  61.126  1.00 55.69           C  
ANISOU 5430  CA  HIS D 182     6256   6604   8300    324    249    345       C  
ATOM   5431  C   HIS D 182     -16.001 -10.851  62.570  1.00 56.59           C  
ANISOU 5431  C   HIS D 182     6340   6749   8412    361    273    355       C  
ATOM   5432  O   HIS D 182     -15.796 -11.760  63.363  1.00 57.99           O  
ANISOU 5432  O   HIS D 182     6489   6954   8590    350    260    349       O  
ATOM   5433  CB  HIS D 182     -16.465 -11.985  60.444  1.00 56.73           C  
ANISOU 5433  CB  HIS D 182     6348   6760   8445    310    202    404       C  
ATOM   5434  CG  HIS D 182     -16.489 -11.911  58.954  1.00 56.46           C  
ANISOU 5434  CG  HIS D 182     6338   6700   8416    287    180    416       C  
ATOM   5435  ND1 HIS D 182     -17.626 -12.180  58.222  1.00 57.73           N  
ANISOU 5435  ND1 HIS D 182     6472   6874   8587    294    153    477       N  
ATOM   5436  CD2 HIS D 182     -15.518 -11.642  58.054  1.00 55.59           C  
ANISOU 5436  CD2 HIS D 182     6271   6550   8299    257    179    374       C  
ATOM   5437  CE1 HIS D 182     -17.357 -12.061  56.934  1.00 57.64           C  
ANISOU 5437  CE1 HIS D 182     6490   6834   8577    269    137    473       C  
ATOM   5438  NE2 HIS D 182     -16.086 -11.729  56.804  1.00 56.33           N  
ANISOU 5438  NE2 HIS D 182     6366   6634   8401    246    152    411       N  
ATOM   5439  N   ALA D 183     -16.644  -9.757  62.930  1.00 57.27           N  
ANISOU 5439  N   ALA D 183     6432   6832   8497    405    309    371       N  
ATOM   5440  CA  ALA D 183     -17.197  -9.690  64.267  1.00 57.49           C  
ANISOU 5440  CA  ALA D 183     6428   6892   8525    441    330    387       C  
ATOM   5441  C   ALA D 183     -18.707  -9.831  64.211  1.00 57.77           C  
ANISOU 5441  C   ALA D 183     6422   6957   8572    471    316    460       C  
ATOM   5442  O   ALA D 183     -19.362  -9.344  63.272  1.00 57.85           O  
ANISOU 5442  O   ALA D 183     6440   6953   8587    480    312    492       O  
ATOM   5443  CB  ALA D 183     -16.814  -8.409  64.939  1.00 57.56           C  
ANISOU 5443  CB  ALA D 183     6468   6879   8522    472    382    350       C  
ATOM   5444  N   TYR D 184     -19.265 -10.479  65.230  1.00 58.55           N  
ANISOU 5444  N   TYR D 184     6476   7096   8674    486    310    485       N  
ATOM   5445  CA  TYR D 184     -20.705 -10.716  65.303  1.00 60.19           C  
ANISOU 5445  CA  TYR D 184     6640   7337   8893    514    296    554       C  
ATOM   5446  C   TYR D 184     -21.317 -10.000  66.501  1.00 61.68           C  
ANISOU 5446  C   TYR D 184     6813   7543   9079    563    334    567       C  
ATOM   5447  O   TYR D 184     -20.988 -10.290  67.645  1.00 63.67           O  
ANISOU 5447  O   TYR D 184     7051   7815   9327    568    346    545       O  
ATOM   5448  CB  TYR D 184     -20.973 -12.226  65.340  1.00 62.42           C  
ANISOU 5448  CB  TYR D 184     6878   7655   9185    487    250    582       C  
ATOM   5449  CG  TYR D 184     -20.561 -12.876  64.033  1.00 61.48           C  
ANISOU 5449  CG  TYR D 184     6772   7518   9069    441    211    579       C  
ATOM   5450  CD1 TYR D 184     -21.342 -12.734  62.892  1.00 61.60           C  
ANISOU 5450  CD1 TYR D 184     6787   7525   9093    442    192    623       C  
ATOM   5451  CD2 TYR D 184     -19.371 -13.585  63.922  1.00 60.76           C  
ANISOU 5451  CD2 TYR D 184     6696   7417   8974    398    194    531       C  
ATOM   5452  CE1 TYR D 184     -20.974 -13.299  61.692  1.00 61.23           C  
ANISOU 5452  CE1 TYR D 184     6753   7462   9050    402    157    620       C  
ATOM   5453  CE2 TYR D 184     -18.986 -14.155  62.703  1.00 60.27           C  
ANISOU 5453  CE2 TYR D 184     6647   7338   8915    356    159    528       C  
ATOM   5454  CZ  TYR D 184     -19.798 -14.000  61.588  1.00 60.57           C  
ANISOU 5454  CZ  TYR D 184     6684   7368   8961    358    141    573       C  
ATOM   5455  OH  TYR D 184     -19.440 -14.542  60.367  1.00 60.60           O  
ANISOU 5455  OH  TYR D 184     6701   7355   8969    318    107    570       O  
ATOM   5456  N   ILE D 185     -22.187  -9.037  66.224  1.00 60.19           N  
ANISOU 5456  N   ILE D 185     6629   7346   8893    599    354    600       N  
ATOM   5457  CA  ILE D 185     -22.826  -8.250  67.283  1.00 61.67           C  
ANISOU 5457  CA  ILE D 185     6805   7548   9078    648    393    614       C  
ATOM   5458  C   ILE D 185     -24.359  -8.340  67.301  1.00 63.81           C  
ANISOU 5458  C   ILE D 185     7034   7849   9362    680    382    687       C  
ATOM   5459  O   ILE D 185     -25.015  -8.495  66.264  1.00 63.44           O  
ANISOU 5459  O   ILE D 185     6981   7801   9324    674    356    727       O  
ATOM   5460  CB  ILE D 185     -22.450  -6.760  67.176  1.00 59.86           C  
ANISOU 5460  CB  ILE D 185     6623   7280   8840    671    438    582       C  
ATOM   5461  CG1 ILE D 185     -22.890  -6.204  65.819  1.00 58.20           C  
ANISOU 5461  CG1 ILE D 185     6435   7044   8635    670    430    607       C  
ATOM   5462  CG2 ILE D 185     -20.968  -6.588  67.342  1.00 58.35           C  
ANISOU 5462  CG2 ILE D 185     6472   7061   8636    644    454    509       C  
ATOM   5463  CD1 ILE D 185     -23.001  -4.721  65.774  1.00 57.44           C  
ANISOU 5463  CD1 ILE D 185     6372   6919   8533    705    475    598       C  
ATOM   5464  N   ARG D 186     -24.912  -8.217  68.502  1.00 60.94           N  
ANISOU 5464  N   ARG D 186     6643   7515   8998    715    403    702       N  
ATOM   5465  CA  ARG D 186     -26.349  -8.243  68.704  1.00 63.79           C  
ANISOU 5465  CA  ARG D 186     6963   7906   9370    749    398    768       C  
ATOM   5466  C   ARG D 186     -26.859  -7.061  69.546  1.00 65.64           C  
ANISOU 5466  C   ARG D 186     7201   8140   9600    801    446    774       C  
ATOM   5467  O   ARG D 186     -26.195  -6.594  70.477  1.00 66.67           O  
ANISOU 5467  O   ARG D 186     7347   8264   9719    811    479    730       O  
ATOM   5468  CB  ARG D 186     -26.759  -9.560  69.365  1.00 67.34           C  
ANISOU 5468  CB  ARG D 186     7361   8401   9826    740    367    796       C  
ATOM   5469  CG  ARG D 186     -26.813 -10.741  68.412  1.00 66.54           C  
ANISOU 5469  CG  ARG D 186     7242   8306   9733    699    314    817       C  
ATOM   5470  CD  ARG D 186     -26.658 -12.041  69.180  1.00 69.84           C  
ANISOU 5470  CD  ARG D 186     7622   8761  10153    680    289    817       C  
ATOM   5471  NE  ARG D 186     -26.730 -13.205  68.312  1.00 69.63           N  
ANISOU 5471  NE  ARG D 186     7578   8744  10136    641    239    839       N  
ATOM   5472  CZ  ARG D 186     -27.804 -13.975  68.210  1.00 72.92           C  
ANISOU 5472  CZ  ARG D 186     7949   9194  10564    646    208    898       C  
ATOM   5473  NH1 ARG D 186     -28.882 -13.705  68.935  1.00 76.65           N  
ANISOU 5473  NH1 ARG D 186     8389   9693  11041    687    223    940       N  
ATOM   5474  NH2 ARG D 186     -27.798 -15.016  67.393  1.00 72.95           N  
ANISOU 5474  NH2 ARG D 186     7939   9205  10575    609    163    914       N  
ATOM   5475  N   PHE D 187     -28.042  -6.577  69.193  1.00 65.77           N  
ANISOU 5475  N   PHE D 187     7203   8162   9624    832    448    827       N  
ATOM   5476  CA  PHE D 187     -28.714  -5.544  69.958  1.00 67.99           C  
ANISOU 5476  CA  PHE D 187     7481   8448   9904    882    490    842       C  
ATOM   5477  C   PHE D 187     -30.228  -5.708  69.845  1.00 70.43           C  
ANISOU 5477  C   PHE D 187     7748   8786  10226    911    475    916       C  
ATOM   5478  O   PHE D 187     -30.725  -6.143  68.805  1.00 69.27           O  
ANISOU 5478  O   PHE D 187     7592   8640  10088    895    441    952       O  
ATOM   5479  CB  PHE D 187     -28.284  -4.180  69.451  1.00 65.24           C  
ANISOU 5479  CB  PHE D 187     7185   8056   9548    895    525    812       C  
ATOM   5480  CG  PHE D 187     -28.216  -4.097  67.955  1.00 61.46           C  
ANISOU 5480  CG  PHE D 187     6730   7549   9073    871    503    820       C  
ATOM   5481  CD1 PHE D 187     -27.000  -4.189  67.298  1.00 58.44           C  
ANISOU 5481  CD1 PHE D 187     6386   7134   8683    831    495    769       C  
ATOM   5482  CD2 PHE D 187     -29.363  -3.945  67.205  1.00 61.33           C  
ANISOU 5482  CD2 PHE D 187     6698   7538   9068    888    488    879       C  
ATOM   5483  CE1 PHE D 187     -26.929  -4.111  65.920  1.00 56.88           C  
ANISOU 5483  CE1 PHE D 187     6212   6911   8490    809    475    776       C  
ATOM   5484  CE2 PHE D 187     -29.299  -3.881  65.836  1.00 58.41           C  
ANISOU 5484  CE2 PHE D 187     6351   7143   8701    866    467    886       C  
ATOM   5485  CZ  PHE D 187     -28.076  -3.963  65.191  1.00 57.13           C  
ANISOU 5485  CZ  PHE D 187     6227   6948   8531    826    460    835       C  
ATOM   5486  N   PRO D 188     -30.972  -5.352  70.906  1.00 67.86           N  
ANISOU 5486  N   PRO D 188     7397   8485   9902    952    500    939       N  
ATOM   5487  CA  PRO D 188     -32.441  -5.427  70.861  1.00 70.48           C  
ANISOU 5487  CA  PRO D 188     7689   8844  10245    983    489   1009       C  
ATOM   5488  C   PRO D 188     -33.069  -4.329  70.022  1.00 68.47           C  
ANISOU 5488  C   PRO D 188     7456   8565   9994   1008    505   1035       C  
ATOM   5489  O   PRO D 188     -32.618  -3.203  70.085  1.00 66.89           O  
ANISOU 5489  O   PRO D 188     7294   8335   9785   1024    544   1002       O  
ATOM   5490  CB  PRO D 188     -32.842  -5.260  72.327  1.00 75.07           C  
ANISOU 5490  CB  PRO D 188     8245   9454  10825   1019    518   1015       C  
ATOM   5491  CG  PRO D 188     -31.747  -4.454  72.917  1.00 74.23           C  
ANISOU 5491  CG  PRO D 188     8178   9321  10704   1022    558    950       C  
ATOM   5492  CD  PRO D 188     -30.483  -4.912  72.225  1.00 70.55           C  
ANISOU 5492  CD  PRO D 188     7744   8830  10233    972    539    901       C  
ATOM   5493  N   VAL D 189     -34.104  -4.638  69.254  1.00 69.28           N  
ANISOU 5493  N   VAL D 189     7534   8681  10109   1011    477   1093       N  
ATOM   5494  CA  VAL D 189     -34.859  -3.585  68.587  1.00 68.57           C  
ANISOU 5494  CA  VAL D 189     7459   8572  10023   1041    494   1123       C  
ATOM   5495  C   VAL D 189     -36.348  -3.695  68.959  1.00 72.96           C  
ANISOU 5495  C   VAL D 189     7967   9164  10590   1078    489   1191       C  
ATOM   5496  O   VAL D 189     -36.898  -4.797  69.099  1.00 75.99           O  
ANISOU 5496  O   VAL D 189     8307   9582  10982   1068    455   1227       O  
ATOM   5497  CB  VAL D 189     -34.662  -3.612  67.047  1.00 65.13           C  
ANISOU 5497  CB  VAL D 189     7048   8107   9590   1011    468   1127       C  
ATOM   5498  CG1 VAL D 189     -33.280  -4.089  66.712  1.00 61.39           C  
ANISOU 5498  CG1 VAL D 189     6604   7612   9108    964    454   1069       C  
ATOM   5499  CG2 VAL D 189     -35.675  -4.487  66.372  1.00 67.42           C  
ANISOU 5499  CG2 VAL D 189     7299   8423   9893   1003    423   1189       C  
ATOM   5500  N   SER D 190     -36.971  -2.537  69.176  1.00 66.59           N  
ANISOU 5500  N   SER D 190     7170   8349   9784   1122    526   1208       N  
ATOM   5501  CA  SER D 190     -38.365  -2.470  69.576  1.00 71.14           C  
ANISOU 5501  CA  SER D 190     7704   8955  10370   1161    528   1270       C  
ATOM   5502  C   SER D 190     -39.223  -2.882  68.398  1.00 71.64           C  
ANISOU 5502  C   SER D 190     7750   9025  10446   1152    489   1324       C  
ATOM   5503  O   SER D 190     -38.944  -2.475  67.263  1.00 68.37           O  
ANISOU 5503  O   SER D 190     7369   8579  10031   1137    484   1316       O  
ATOM   5504  CB  SER D 190     -38.731  -1.058  70.051  1.00 72.09           C  
ANISOU 5504  CB  SER D 190     7843   9062  10487   1209    578   1269       C  
ATOM   5505  OG  SER D 190     -38.339  -0.853  71.401  1.00 73.40           O  
ANISOU 5505  OG  SER D 190     8006   9239  10645   1226    610   1238       O  
ATOM   5506  N   ASP D 191     -40.254  -3.689  68.679  1.00 66.21           N  
ANISOU 5506  N   ASP D 191     7011   8376   9768   1161    464   1378       N  
ATOM   5507  CA  ASP D 191     -41.210  -4.144  67.667  1.00 67.83           C  
ANISOU 5507  CA  ASP D 191     7193   8593   9986   1156    427   1435       C  
ATOM   5508  C   ASP D 191     -41.732  -2.944  66.873  1.00 66.69           C  
ANISOU 5508  C   ASP D 191     7074   8421   9844   1182    447   1455       C  
ATOM   5509  O   ASP D 191     -42.200  -1.972  67.459  1.00 68.17           O  
ANISOU 5509  O   ASP D 191     7265   8607  10031   1224    485   1463       O  
ATOM   5510  CB  ASP D 191     -42.387  -4.889  68.327  1.00 73.87           C  
ANISOU 5510  CB  ASP D 191     7899   9405  10762   1176    409   1492       C  
ATOM   5511  CG  ASP D 191     -42.305  -6.414  68.174  1.00 75.52           C  
ANISOU 5511  CG  ASP D 191     8076   9642  10977   1136    360   1504       C  
ATOM   5512  OD1 ASP D 191     -41.209  -6.946  67.908  1.00 71.83           O  
ANISOU 5512  OD1 ASP D 191     7628   9160  10503   1095    345   1460       O  
ATOM   5513  OD2 ASP D 191     -43.344  -7.086  68.333  1.00 80.90           O  
ANISOU 5513  OD2 ASP D 191     8710  10358  11669   1147    337   1558       O  
ATOM   5514  N   GLY D 192     -41.638  -3.017  65.548  1.00 64.99           N  
ANISOU 5514  N   GLY D 192     6878   8184   9632   1157    422   1463       N  
ATOM   5515  CA  GLY D 192     -42.076  -1.937  64.693  1.00 65.25           C  
ANISOU 5515  CA  GLY D 192     6936   8189   9666   1178    438   1481       C  
ATOM   5516  C   GLY D 192     -40.985  -1.107  64.048  1.00 65.13           C  
ANISOU 5516  C   GLY D 192     6980   8126   9641   1162    458   1427       C  
ATOM   5517  O   GLY D 192     -41.246  -0.394  63.076  1.00 65.28           O  
ANISOU 5517  O   GLY D 192     7023   8120   9662   1168    461   1441       O  
ATOM   5518  N   THR D 193     -39.770  -1.199  64.585  1.00 70.63           N  
ANISOU 5518  N   THR D 193     7701   8811  10326   1141    471   1366       N  
ATOM   5519  CA  THR D 193     -38.596  -0.497  64.050  1.00 66.34           C  
ANISOU 5519  CA  THR D 193     7213   8222   9772   1122    490   1308       C  
ATOM   5520  C   THR D 193     -38.297  -0.878  62.605  1.00 64.38           C  
ANISOU 5520  C   THR D 193     6983   7952   9525   1083    454   1309       C  
ATOM   5521  O   THR D 193     -38.385  -2.045  62.246  1.00 65.38           O  
ANISOU 5521  O   THR D 193     7084   8099   9659   1052    411   1327       O  
ATOM   5522  CB  THR D 193     -37.334  -0.805  64.893  1.00 64.13           C  
ANISOU 5522  CB  THR D 193     6948   7938   9480   1100    502   1244       C  
ATOM   5523  OG1 THR D 193     -37.547  -0.424  66.256  1.00 66.76           O  
ANISOU 5523  OG1 THR D 193     7266   8290   9810   1136    537   1239       O  
ATOM   5524  CG2 THR D 193     -36.107  -0.076  64.349  1.00 60.46           C  
ANISOU 5524  CG2 THR D 193     6542   7427   9004   1080    522   1184       C  
ATOM   5525  N   GLN D 194     -37.943   0.095  61.777  1.00 62.40           N  
ANISOU 5525  N   GLN D 194     6778   7662   9271   1084    472   1291       N  
ATOM   5526  CA  GLN D 194     -37.454  -0.203  60.437  1.00 60.54           C  
ANISOU 5526  CA  GLN D 194     6566   7401   9035   1044    442   1281       C  
ATOM   5527  C   GLN D 194     -36.110   0.489  60.188  1.00 60.09           C  
ANISOU 5527  C   GLN D 194     6565   7300   8965   1026    467   1213       C  
ATOM   5528  O   GLN D 194     -35.146  -0.148  59.801  1.00 59.77           O  
ANISOU 5528  O   GLN D 194     6541   7248   8920    983    446   1177       O  
ATOM   5529  CB  GLN D 194     -38.476   0.165  59.362  1.00 62.72           C  
ANISOU 5529  CB  GLN D 194     6839   7672   9321   1058    428   1335       C  
ATOM   5530  CG  GLN D 194     -38.695  -0.981  58.388  1.00 62.30           C  
ANISOU 5530  CG  GLN D 194     6764   7630   9276   1020    374   1365       C  
ATOM   5531  CD  GLN D 194     -39.556  -0.635  57.190  1.00 65.19           C  
ANISOU 5531  CD  GLN D 194     7132   7987   9650   1028    359   1412       C  
ATOM   5532  OE1 GLN D 194     -40.167   0.429  57.127  1.00 68.01           O  
ANISOU 5532  OE1 GLN D 194     7499   8332  10008   1065    387   1432       O  
ATOM   5533  NE2 GLN D 194     -39.607  -1.543  56.224  1.00 64.89           N  
ANISOU 5533  NE2 GLN D 194     7084   7954   9618    992    313   1431       N  
ATOM   5534  N   GLU D 195     -36.078   1.810  60.322  1.00 68.93           N  
ANISOU 5534  N   GLU D 195     7717   8394  10079   1057    510   1198       N  
ATOM   5535  CA  GLU D 195     -34.845   2.588  60.200  1.00 66.33           C  
ANISOU 5535  CA  GLU D 195     7441   8023   9737   1045    540   1133       C  
ATOM   5536  C   GLU D 195     -33.931   2.441  61.412  1.00 65.18           C  
ANISOU 5536  C   GLU D 195     7300   7883   9581   1041    561   1081       C  
ATOM   5537  O   GLU D 195     -34.403   2.332  62.543  1.00 67.07           O  
ANISOU 5537  O   GLU D 195     7508   8152   9822   1068    575   1095       O  
ATOM   5538  CB  GLU D 195     -35.172   4.069  60.012  1.00 67.67           C  
ANISOU 5538  CB  GLU D 195     7642   8166   9905   1084    581   1137       C  
ATOM   5539  CG  GLU D 195     -35.843   4.413  58.703  1.00 68.02           C  
ANISOU 5539  CG  GLU D 195     7695   8195   9956   1086    565   1177       C  
ATOM   5540  CD  GLU D 195     -35.533   5.838  58.263  1.00 68.82           C  
ANISOU 5540  CD  GLU D 195     7846   8253  10051   1104    603   1152       C  
ATOM   5541  OE1 GLU D 195     -35.009   6.649  59.085  1.00 68.85           O  
ANISOU 5541  OE1 GLU D 195     7872   8243  10045   1124    647   1113       O  
ATOM   5542  OE2 GLU D 195     -35.805   6.147  57.079  1.00 69.81           O  
ANISOU 5542  OE2 GLU D 195     7987   8357  10179   1098    591   1173       O  
ATOM   5543  N   LEU D 196     -32.621   2.457  61.174  1.00 64.74           N  
ANISOU 5543  N   LEU D 196     7284   7799   9516   1008    565   1021       N  
ATOM   5544  CA  LEU D 196     -31.651   2.479  62.264  1.00 63.82           C  
ANISOU 5544  CA  LEU D 196     7178   7681   9388   1004    590    965       C  
ATOM   5545  C   LEU D 196     -30.465   3.416  61.996  1.00 62.19           C  
ANISOU 5545  C   LEU D 196     7031   7430   9170    994    622    902       C  
ATOM   5546  O   LEU D 196     -29.971   3.519  60.863  1.00 60.72           O  
ANISOU 5546  O   LEU D 196     6876   7213   8982    967    608    887       O  
ATOM   5547  CB  LEU D 196     -31.154   1.068  62.531  1.00 62.51           C  
ANISOU 5547  CB  LEU D 196     6987   7540   9224    965    554    953       C  
ATOM   5548  CG  LEU D 196     -31.999   0.242  63.495  1.00 64.69           C  
ANISOU 5548  CG  LEU D 196     7207   7865   9508    981    540    993       C  
ATOM   5549  CD1 LEU D 196     -31.440  -1.189  63.633  1.00 63.43           C  
ANISOU 5549  CD1 LEU D 196     7025   7727   9349    938    501    979       C  
ATOM   5550  CD2 LEU D 196     -32.078   0.933  64.852  1.00 66.73           C  
ANISOU 5550  CD2 LEU D 196     7462   8134   9760   1021    585    979       C  
ATOM   5551  N   LYS D 197     -30.010   4.085  63.051  1.00 66.57           N  
ANISOU 5551  N   LYS D 197     7599   7980   9716   1016    664    865       N  
ATOM   5552  CA  LYS D 197     -28.903   5.034  62.963  1.00 65.72           C  
ANISOU 5552  CA  LYS D 197     7545   7829   9595   1011    698    804       C  
ATOM   5553  C   LYS D 197     -27.564   4.394  63.371  1.00 63.94           C  
ANISOU 5553  C   LYS D 197     7334   7600   9361    973    693    743       C  
ATOM   5554  O   LYS D 197     -27.460   3.833  64.472  1.00 64.74           O  
ANISOU 5554  O   LYS D 197     7408   7729   9460    975    695    734       O  
ATOM   5555  CB  LYS D 197     -29.194   6.236  63.859  1.00 68.26           C  
ANISOU 5555  CB  LYS D 197     7877   8147   9912   1059    750    798       C  
ATOM   5556  CG  LYS D 197     -28.246   7.420  63.696  1.00 68.16           C  
ANISOU 5556  CG  LYS D 197     7920   8089   9887   1061    790    743       C  
ATOM   5557  CD  LYS D 197     -28.558   8.506  64.723  1.00 71.15           C  
ANISOU 5557  CD  LYS D 197     8304   8468  10262   1109    841    739       C  
ATOM   5558  CE  LYS D 197     -27.663   9.724  64.571  1.00 72.67           C  
ANISOU 5558  CE  LYS D 197     8553   8617  10443   1114    882    685       C  
ATOM   5559  NZ  LYS D 197     -27.851  10.638  65.733  1.00 76.11           N  
ANISOU 5559  NZ  LYS D 197     8990   9056  10873   1157    930    675       N  
ATOM   5560  N   ILE D 198     -26.538   4.476  62.515  1.00 63.76           N  
ANISOU 5560  N   ILE D 198     7353   7542   9332    937    686    700       N  
ATOM   5561  CA  ILE D 198     -25.215   3.964  62.893  1.00 62.40           C  
ANISOU 5561  CA  ILE D 198     7197   7362   9150    902    684    639       C  
ATOM   5562  C   ILE D 198     -24.131   5.033  62.882  1.00 62.63           C  
ANISOU 5562  C   ILE D 198     7281   7349   9166    901    724    577       C  
ATOM   5563  O   ILE D 198     -23.749   5.554  61.824  1.00 62.17           O  
ANISOU 5563  O   ILE D 198     7261   7255   9106    887    724    563       O  
ATOM   5564  CB  ILE D 198     -24.728   2.810  61.976  1.00 60.13           C  
ANISOU 5564  CB  ILE D 198     6907   7074   8866    850    635    635       C  
ATOM   5565  CG1 ILE D 198     -25.685   1.621  62.008  1.00 60.28           C  
ANISOU 5565  CG1 ILE D 198     6870   7135   8897    846    593    692       C  
ATOM   5566  CG2 ILE D 198     -23.378   2.303  62.439  1.00 59.01           C  
ANISOU 5566  CG2 ILE D 198     6781   6926   8715    816    635    572       C  
ATOM   5567  CD1 ILE D 198     -25.243   0.493  61.102  1.00 58.45           C  
ANISOU 5567  CD1 ILE D 198     6636   6904   8670    795    545    690       C  
ATOM   5568  N   VAL D 199     -23.627   5.332  64.076  1.00 62.22           N  
ANISOU 5568  N   VAL D 199     7233   7301   9105    915    756    540       N  
ATOM   5569  CA  VAL D 199     -22.451   6.177  64.247  1.00 62.80           C  
ANISOU 5569  CA  VAL D 199     7356   7339   9166    910    792    474       C  
ATOM   5570  C   VAL D 199     -21.220   5.290  64.360  1.00 61.36           C  
ANISOU 5570  C   VAL D 199     7182   7154   8977    864    773    424       C  
ATOM   5571  O   VAL D 199     -21.031   4.621  65.374  1.00 62.13           O  
ANISOU 5571  O   VAL D 199     7254   7280   9073    861    770    413       O  
ATOM   5572  CB  VAL D 199     -22.583   7.066  65.506  1.00 65.92           C  
ANISOU 5572  CB  VAL D 199     7752   7739   9554    953    841    461       C  
ATOM   5573  CG1 VAL D 199     -21.445   8.055  65.609  1.00 65.07           C  
ANISOU 5573  CG1 VAL D 199     7698   7593   9434    950    881    396       C  
ATOM   5574  CG2 VAL D 199     -23.893   7.809  65.469  1.00 69.72           C  
ANISOU 5574  CG2 VAL D 199     8219   8229  10044    999    857    517       C  
ATOM   5575  N   SER D 200     -20.372   5.304  63.334  1.00 61.40           N  
ANISOU 5575  N   SER D 200     7225   7127   8979    829    761    392       N  
ATOM   5576  CA  SER D 200     -19.210   4.406  63.298  1.00 59.82           C  
ANISOU 5576  CA  SER D 200     7033   6923   8774    782    739    346       C  
ATOM   5577  C   SER D 200     -17.873   5.094  62.977  1.00 60.74           C  
ANISOU 5577  C   SER D 200     7206   6995   8878    761    762    278       C  
ATOM   5578  O   SER D 200     -17.865   6.245  62.548  1.00 62.75           O  
ANISOU 5578  O   SER D 200     7495   7218   9129    780    792    269       O  
ATOM   5579  CB  SER D 200     -19.464   3.272  62.289  1.00 57.69           C  
ANISOU 5579  CB  SER D 200     6742   6663   8513    746    684    377       C  
ATOM   5580  OG  SER D 200     -20.163   3.741  61.148  1.00 57.80           O  
ANISOU 5580  OG  SER D 200     6766   6661   8534    754    676    415       O  
ATOM   5581  N   SER D 201     -16.754   4.399  63.209  1.00 59.18           N  
ANISOU 5581  N   SER D 201     7015   6795   8674    724    751    229       N  
ATOM   5582  CA  SER D 201     -15.438   4.864  62.735  1.00 58.97           C  
ANISOU 5582  CA  SER D 201     7042   6727   8637    697    765    166       C  
ATOM   5583  C   SER D 201     -14.457   3.727  62.435  1.00 58.58           C  
ANISOU 5583  C   SER D 201     6994   6678   8586    645    729    133       C  
ATOM   5584  O   SER D 201     -14.466   2.696  63.109  1.00 58.43           O  
ANISOU 5584  O   SER D 201     6939   6692   8570    633    708    139       O  
ATOM   5585  CB  SER D 201     -14.796   5.821  63.748  1.00 59.02           C  
ANISOU 5585  CB  SER D 201     7074   6720   8632    720    815    117       C  
ATOM   5586  OG  SER D 201     -14.421   5.151  64.932  1.00 58.87           O  
ANISOU 5586  OG  SER D 201     7031   6728   8608    715    816     97       O  
ATOM   5587  N   THR D 202     -13.598   3.926  61.435  1.00 58.09           N  
ANISOU 5587  N   THR D 202     6973   6579   8520    613    724     98       N  
ATOM   5588  CA  THR D 202     -12.570   2.935  61.082  1.00 56.76           C  
ANISOU 5588  CA  THR D 202     6811   6406   8350    563    693     62       C  
ATOM   5589  C   THR D 202     -11.143   3.501  61.158  1.00 58.60           C  
ANISOU 5589  C   THR D 202     7094   6602   8570    544    720    -12       C  
ATOM   5590  O   THR D 202     -10.847   4.521  60.540  1.00 60.46           O  
ANISOU 5590  O   THR D 202     7371   6800   8800    549    744    -32       O  
ATOM   5591  CB  THR D 202     -12.811   2.360  59.657  1.00 55.54           C  
ANISOU 5591  CB  THR D 202     6657   6242   8204    532    650     91       C  
ATOM   5592  OG1 THR D 202     -12.296   3.242  58.654  1.00 57.42           O  
ANISOU 5592  OG1 THR D 202     6945   6435   8438    523    664     65       O  
ATOM   5593  CG2 THR D 202     -14.284   2.170  59.418  1.00 55.72           C  
ANISOU 5593  CG2 THR D 202     6640   6291   8239    557    632    165       C  
ATOM   5594  N   GLN D 203     -10.270   2.829  61.913  1.00 57.95           N  
ANISOU 5594  N   GLN D 203     7006   6531   8482    522    716    -53       N  
ATOM   5595  CA  GLN D 203      -8.868   3.231  62.085  1.00 60.08           C  
ANISOU 5595  CA  GLN D 203     7319   6770   8739    501    740   -125       C  
ATOM   5596  C   GLN D 203      -7.912   2.062  61.935  1.00 59.10           C  
ANISOU 5596  C   GLN D 203     7192   6650   8614    452    706   -157       C  
ATOM   5597  O   GLN D 203      -8.065   1.061  62.635  1.00 58.26           O  
ANISOU 5597  O   GLN D 203     7046   6578   8511    445    685   -145       O  
ATOM   5598  CB  GLN D 203      -8.668   3.860  63.465  1.00 62.67           C  
ANISOU 5598  CB  GLN D 203     7647   7106   9058    533    783   -152       C  
ATOM   5599  CG  GLN D 203      -7.287   3.607  64.087  1.00 64.95           C  
ANISOU 5599  CG  GLN D 203     7956   7386   9336    506    793   -220       C  
ATOM   5600  CD  GLN D 203      -7.213   4.018  65.555  1.00 67.92           C  
ANISOU 5600  CD  GLN D 203     8322   7779   9704    537    830   -240       C  
ATOM   5601  OE1 GLN D 203      -7.497   3.218  66.450  1.00 67.37           O  
ANISOU 5601  OE1 GLN D 203     8213   7747   9637    541    818   -225       O  
ATOM   5602  NE2 GLN D 203      -6.822   5.268  65.805  1.00 71.91           N  
ANISOU 5602  NE2 GLN D 203     8866   8257  10201    559    876   -274       N  
ATOM   5603  N   ILE D 204      -6.913   2.177  61.056  1.00 56.36           N  
ANISOU 5603  N   ILE D 204     8315   6323   6776    193  -1057  -1876       N  
ATOM   5604  CA  ILE D 204      -5.927   1.083  60.895  1.00 56.29           C  
ANISOU 5604  CA  ILE D 204     8292   6347   6748    199  -1060  -1859       C  
ATOM   5605  C   ILE D 204      -4.745   1.248  61.848  1.00 56.42           C  
ANISOU 5605  C   ILE D 204     8314   6387   6736    183  -1068  -1853       C  
ATOM   5606  O   ILE D 204      -3.987   2.196  61.737  1.00 56.52           O  
ANISOU 5606  O   ILE D 204     8329   6406   6739    164  -1083  -1848       O  
ATOM   5607  CB  ILE D 204      -5.361   0.993  59.468  1.00 56.19           C  
ANISOU 5607  CB  ILE D 204     8261   6349   6740    201  -1075  -1842       C  
ATOM   5608  CG1 ILE D 204      -6.439   1.238  58.422  1.00 56.09           C  
ANISOU 5608  CG1 ILE D 204     8244   6312   6757    212  -1072  -1849       C  
ATOM   5609  CG2 ILE D 204      -4.751  -0.343  59.261  1.00 56.09           C  
ANISOU 5609  CG2 ILE D 204     8233   6363   6714    214  -1072  -1828       C  
ATOM   5610  CD1 ILE D 204      -5.914   1.301  57.011  1.00 56.01           C  
ANISOU 5610  CD1 ILE D 204     8217   6313   6751    213  -1087  -1833       C  
ATOM   5611  N   ASP D 205      -4.590   0.319  62.778  1.00 59.41           N  
ANISOU 5611  N   ASP D 205     8695   6779   7100    190  -1057  -1853       N  
ATOM   5612  CA  ASP D 205      -3.552   0.412  63.808  1.00 62.51           C  
ANISOU 5612  CA  ASP D 205     9094   7193   7464    175  -1061  -1849       C  
ATOM   5613  C   ASP D 205      -3.643   1.741  64.569  1.00 65.73           C  
ANISOU 5613  C   ASP D 205     9520   7584   7870    155  -1065  -1861       C  
ATOM   5614  O   ASP D 205      -4.667   2.019  65.191  1.00 64.74           O  
ANISOU 5614  O   ASP D 205     9408   7433   7757    158  -1053  -1878       O  
ATOM   5615  CB  ASP D 205      -2.162   0.221  63.186  1.00 64.71           C  
ANISOU 5615  CB  ASP D 205     9359   7504   7725    168  -1078  -1828       C  
ATOM   5616  CG  ASP D 205      -2.053  -1.084  62.427  1.00 61.95           C  
ANISOU 5616  CG  ASP D 205     8991   7171   7377    187  -1074  -1815       C  
ATOM   5617  OD1 ASP D 205      -2.529  -2.104  62.961  1.00 59.38           O  
ANISOU 5617  OD1 ASP D 205     8665   6845   7050    202  -1059  -1819       O  
ATOM   5618  OD2 ASP D 205      -1.527  -1.094  61.291  1.00 62.68           O  
ANISOU 5618  OD2 ASP D 205     9069   7276   7472    187  -1087  -1801       O  
ATOM   5619  N   ASP D 206      -2.580   2.549  64.524  1.00 67.98           N  
ANISOU 5619  N   ASP D 206     9806   7883   8140    135  -1082  -1853       N  
ATOM   5620  CA  ASP D 206      -2.541   3.836  65.229  1.00 71.90           C  
ANISOU 5620  CA  ASP D 206    10319   8367   8633    115  -1087  -1863       C  
ATOM   5621  C   ASP D 206      -2.896   5.032  64.353  1.00 73.69           C  
ANISOU 5621  C   ASP D 206    10547   8573   8878    106  -1098  -1867       C  
ATOM   5622  O   ASP D 206      -2.970   6.169  64.833  1.00 76.99           O  
ANISOU 5622  O   ASP D 206    10978   8977   9296     89  -1102  -1877       O  
ATOM   5623  CB  ASP D 206      -1.163   4.055  65.833  1.00 76.29           C  
ANISOU 5623  CB  ASP D 206    10876   8950   9160     97  -1099  -1853       C  
ATOM   5624  CG  ASP D 206      -0.847   3.037  66.891  1.00 75.32           C  
ANISOU 5624  CG  ASP D 206    10756   8845   9018    104  -1089  -1852       C  
ATOM   5625  OD1 ASP D 206      -1.822   2.640  67.587  1.00 72.66           O  
ANISOU 5625  OD1 ASP D 206    10427   8490   8689    115  -1072  -1866       O  
ATOM   5626  OD2 ASP D 206       0.350   2.629  67.011  1.00 77.47           O  
ANISOU 5626  OD2 ASP D 206    11020   9148   9267     98  -1097  -1838       O  
ATOM   5627  N   GLY D 207      -3.163   4.767  63.079  1.00 69.34           N  
ANISOU 5627  N   GLY D 207     9982   8021   8344    117  -1101  -1860       N  
ATOM   5628  CA  GLY D 207      -3.245   5.822  62.093  1.00 69.35           C  
ANISOU 5628  CA  GLY D 207     9981   8009   8360    108  -1114  -1859       C  
ATOM   5629  C   GLY D 207      -4.485   6.689  62.172  1.00 69.38           C  
ANISOU 5629  C   GLY D 207     9998   7977   8388    107  -1107  -1877       C  
ATOM   5630  O   GLY D 207      -5.148   6.782  63.213  1.00 69.45           O  
ANISOU 5630  O   GLY D 207    10021   7969   8397    108  -1094  -1893       O  
ATOM   5631  N   GLU D 208      -4.761   7.358  61.057  1.00 71.92           N  
ANISOU 5631  N   GLU D 208    10314   8285   8726    106  -1116  -1876       N  
ATOM   5632  CA  GLU D 208      -5.919   8.225  60.909  1.00 71.48           C  
ANISOU 5632  CA  GLU D 208    10268   8195   8695    105  -1111  -1892       C  
ATOM   5633  C   GLU D 208      -7.229   7.483  61.191  1.00 66.39           C  
ANISOU 5633  C   GLU D 208     9627   7530   8067    126  -1091  -1905       C  
ATOM   5634  O   GLU D 208      -7.519   6.444  60.595  1.00 63.04           O  
ANISOU 5634  O   GLU D 208     9190   7111   7650    144  -1084  -1899       O  
ATOM   5635  CB  GLU D 208      -5.938   8.810  59.490  1.00 73.56           C  
ANISOU 5635  CB  GLU D 208    10521   8453   8974    104  -1124  -1884       C  
ATOM   5636  CG  GLU D 208      -6.960   9.918  59.246  1.00 79.76           C  
ANISOU 5636  CG  GLU D 208    11317   9205   9783    100  -1123  -1899       C  
ATOM   5637  CD  GLU D 208      -6.395  11.323  59.523  1.00 83.81           C  
ANISOU 5637  CD  GLU D 208    11841   9715  10289     75  -1136  -1901       C  
ATOM   5638  OE1 GLU D 208      -5.165  11.438  59.772  1.00 81.49           O  
ANISOU 5638  OE1 GLU D 208    11545   9446   9972     61  -1148  -1890       O  
ATOM   5639  OE2 GLU D 208      -7.188  12.307  59.494  1.00 89.76           O  
ANISOU 5639  OE2 GLU D 208    12605  10441  11060     69  -1135  -1914       O  
ATOM   5640  N   GLU D 209      -8.017   8.030  62.107  1.00 68.96           N  
ANISOU 5640  N   GLU D 209     9970   7832   8400    122  -1081  -1923       N  
ATOM   5641  CA  GLU D 209      -9.358   7.527  62.405  1.00 64.88           C  
ANISOU 5641  CA  GLU D 209     9459   7291   7901    139  -1062  -1938       C  
ATOM   5642  C   GLU D 209     -10.336   8.129  61.427  1.00 64.32           C  
ANISOU 5642  C   GLU D 209     9387   7194   7859    144  -1062  -1945       C  
ATOM   5643  O   GLU D 209     -10.415   9.345  61.319  1.00 67.81           O  
ANISOU 5643  O   GLU D 209     9837   7621   8307    129  -1071  -1950       O  
ATOM   5644  CB  GLU D 209      -9.745   7.885  63.844  1.00 65.93           C  
ANISOU 5644  CB  GLU D 209     9612   7412   8028    132  -1051  -1954       C  
ATOM   5645  CG  GLU D 209     -11.180   7.627  64.237  1.00 64.70           C  
ANISOU 5645  CG  GLU D 209     9464   7227   7892    146  -1032  -1971       C  
ATOM   5646  CD  GLU D 209     -11.364   7.562  65.763  1.00 67.18           C  
ANISOU 5646  CD  GLU D 209     9794   7536   8194    142  -1020  -1984       C  
ATOM   5647  OE1 GLU D 209     -10.350   7.441  66.478  1.00 70.40           O  
ANISOU 5647  OE1 GLU D 209    10205   7968   8577    132  -1025  -1977       O  
ATOM   5648  OE2 GLU D 209     -12.517   7.618  66.255  1.00 66.23           O  
ANISOU 5648  OE2 GLU D 209     9685   7390   8089    150  -1006  -2001       O  
ATOM   5649  N   THR D 210     -11.071   7.297  60.700  1.00 60.26           N  
ANISOU 5649  N   THR D 210     8862   6672   7361    165  -1054  -1944       N  
ATOM   5650  CA  THR D 210     -12.067   7.834  59.777  1.00 60.20           C  
ANISOU 5650  CA  THR D 210     8853   6638   7381    171  -1053  -1951       C  
ATOM   5651  C   THR D 210     -13.468   7.766  60.386  1.00 60.19           C  
ANISOU 5651  C   THR D 210     8864   6607   7398    182  -1035  -1971       C  
ATOM   5652  O   THR D 210     -14.030   6.684  60.549  1.00 60.09           O  
ANISOU 5652  O   THR D 210     8848   6594   7391    200  -1021  -1974       O  
ATOM   5653  CB  THR D 210     -12.065   7.093  58.443  1.00 60.03           C  
ANISOU 5653  CB  THR D 210     8813   6626   7371    186  -1057  -1939       C  
ATOM   5654  OG1 THR D 210     -10.814   7.292  57.792  1.00 60.04           O  
ANISOU 5654  OG1 THR D 210     8803   6653   7358    175  -1075  -1921       O  
ATOM   5655  CG2 THR D 210     -13.140   7.629  57.549  1.00 59.97           C  
ANISOU 5655  CG2 THR D 210     8804   6591   7392    193  -1056  -1947       C  
ATOM   5656  N   ASN D 211     -14.029   8.919  60.727  1.00 61.36           N  
ANISOU 5656  N   ASN D 211     9026   6730   7557    170  -1035  -1985       N  
ATOM   5657  CA  ASN D 211     -15.337   8.927  61.342  1.00 60.16           C  
ANISOU 5657  CA  ASN D 211     8887   6549   7422    179  -1018  -2004       C  
ATOM   5658  C   ASN D 211     -16.413   8.877  60.288  1.00 58.22           C  
ANISOU 5658  C   ASN D 211     8635   6282   7205    194  -1014  -2009       C  
ATOM   5659  O   ASN D 211     -16.331   9.586  59.284  1.00 59.61           O  
ANISOU 5659  O   ASN D 211     8805   6453   7391    189  -1026  -2004       O  
ATOM   5660  CB  ASN D 211     -15.515  10.155  62.220  1.00 63.88           C  
ANISOU 5660  CB  ASN D 211     9377   7003   7891    161  -1019  -2018       C  
ATOM   5661  CG  ASN D 211     -14.690  10.080  63.485  1.00 65.33           C  
ANISOU 5661  CG  ASN D 211     9570   7204   8048    149  -1019  -2017       C  
ATOM   5662  OD1 ASN D 211     -15.124   9.506  64.491  1.00 63.79           O  
ANISOU 5662  OD1 ASN D 211     9383   7005   7849    156  -1004  -2026       O  
ATOM   5663  ND2 ASN D 211     -13.484  10.650  63.442  1.00 68.94           N  
ANISOU 5663  ND2 ASN D 211    10025   7681   8487    131  -1035  -2006       N  
ATOM   5664  N   TYR D 212     -17.402   8.010  60.514  1.00 59.87           N  
ANISOU 5664  N   TYR D 212     8844   6478   7426    214   -996  -2018       N  
ATOM   5665  CA  TYR D 212     -18.582   7.900  59.665  1.00 59.63           C  
ANISOU 5665  CA  TYR D 212     8809   6424   7424    229   -989  -2025       C  
ATOM   5666  C   TYR D 212     -19.762   8.370  60.477  1.00 60.32           C  
ANISOU 5666  C   TYR D 212     8913   6480   7526    230   -975  -2047       C  
ATOM   5667  O   TYR D 212     -20.225   7.673  61.361  1.00 60.06           O  
ANISOU 5667  O   TYR D 212     8887   6443   7490    240   -960  -2055       O  
ATOM   5668  CB  TYR D 212     -18.764   6.471  59.188  1.00 58.76           C  
ANISOU 5668  CB  TYR D 212     8684   6326   7317    252   -980  -2018       C  
ATOM   5669  CG  TYR D 212     -17.781   6.085  58.114  1.00 58.18           C  
ANISOU 5669  CG  TYR D 212     8591   6278   7235    253   -994  -1998       C  
ATOM   5670  CD1 TYR D 212     -18.085   6.268  56.780  1.00 58.30           C  
ANISOU 5670  CD1 TYR D 212     8595   6287   7269    259  -1002  -1993       C  
ATOM   5671  CD2 TYR D 212     -16.543   5.565  58.432  1.00 57.49           C  
ANISOU 5671  CD2 TYR D 212     8499   6224   7122    247  -1001  -1984       C  
ATOM   5672  CE1 TYR D 212     -17.199   5.935  55.783  1.00 57.78           C  
ANISOU 5672  CE1 TYR D 212     8512   6244   7196    260  -1015  -1975       C  
ATOM   5673  CE2 TYR D 212     -15.628   5.225  57.431  1.00 56.94           C  
ANISOU 5673  CE2 TYR D 212     8412   6179   7045    247  -1014  -1965       C  
ATOM   5674  CZ  TYR D 212     -15.972   5.416  56.102  1.00 57.09           C  
ANISOU 5674  CZ  TYR D 212     8420   6189   7083    254  -1021  -1960       C  
ATOM   5675  OH  TYR D 212     -15.105   5.092  55.080  1.00 56.56           O  
ANISOU 5675  OH  TYR D 212     8336   6146   7010    255  -1034  -1942       O  
ATOM   5676  N   ASP D 213     -20.244   9.562  60.144  1.00 60.19           N  
ANISOU 5676  N   ASP D 213     8904   6440   7524    221   -981  -2055       N  
ATOM   5677  CA  ASP D 213     -21.062  10.374  61.041  1.00 62.23           C  
ANISOU 5677  CA  ASP D 213     9182   6672   7792    213   -972  -2074       C  
ATOM   5678  C   ASP D 213     -22.395   9.793  61.303  1.00 60.38           C  
ANISOU 5678  C   ASP D 213     8951   6414   7576    232   -953  -2089       C  
ATOM   5679  O   ASP D 213     -22.806   9.620  62.448  1.00 60.69           O  
ANISOU 5679  O   ASP D 213     9004   6446   7611    233   -940  -2101       O  
ATOM   5680  CB  ASP D 213     -21.259  11.761  60.458  1.00 65.50           C  
ANISOU 5680  CB  ASP D 213     9601   7067   8219    200   -984  -2078       C  
ATOM   5681  CG  ASP D 213     -20.213  12.704  60.924  1.00 69.09           C  
ANISOU 5681  CG  ASP D 213    10063   7534   8654    176   -998  -2073       C  
ATOM   5682  OD1 ASP D 213     -19.087  12.196  61.163  1.00 68.83           O  
ANISOU 5682  OD1 ASP D 213    10024   7531   8598    171  -1004  -2060       O  
ATOM   5683  OD2 ASP D 213     -20.515  13.922  61.082  1.00 72.50           O  
ANISOU 5683  OD2 ASP D 213    10507   7946   9093    162  -1002  -2083       O  
ATOM   5684  N   TYR D 214     -23.063   9.529  60.193  1.00 60.23           N  
ANISOU 5684  N   TYR D 214     8922   6385   7579    246   -952  -2088       N  
ATOM   5685  CA  TYR D 214     -24.418   9.060  60.170  1.00 58.94           C  
ANISOU 5685  CA  TYR D 214     8760   6196   7437    265   -935  -2101       C  
ATOM   5686  C   TYR D 214     -24.490   7.961  59.119  1.00 58.50           C  
ANISOU 5686  C   TYR D 214     8686   6153   7390    284   -934  -2090       C  
ATOM   5687  O   TYR D 214     -24.024   8.128  57.988  1.00 58.45           O  
ANISOU 5687  O   TYR D 214     8666   6155   7386    283   -947  -2078       O  
ATOM   5688  CB  TYR D 214     -25.351  10.217  59.854  1.00 61.22           C  
ANISOU 5688  CB  TYR D 214     9059   6453   7749    260   -936  -2115       C  
ATOM   5689  CG  TYR D 214     -26.753   9.861  59.481  1.00 60.38           C  
ANISOU 5689  CG  TYR D 214     8951   6320   7670    279   -922  -2127       C  
ATOM   5690  CD1 TYR D 214     -27.723   9.626  60.461  1.00 60.52           C  
ANISOU 5690  CD1 TYR D 214     8982   6318   7695    286   -904  -2144       C  
ATOM   5691  CD2 TYR D 214     -27.133   9.801  58.148  1.00 60.02           C  
ANISOU 5691  CD2 TYR D 214     8893   6269   7644    289   -927  -2122       C  
ATOM   5692  CE1 TYR D 214     -29.037   9.304  60.117  1.00 60.22           C  
ANISOU 5692  CE1 TYR D 214     8942   6255   7682    304   -891  -2155       C  
ATOM   5693  CE2 TYR D 214     -28.440   9.475  57.789  1.00 59.71           C  
ANISOU 5693  CE2 TYR D 214     8852   6205   7629    307   -914  -2133       C  
ATOM   5694  CZ  TYR D 214     -29.386   9.234  58.777  1.00 59.80           C  
ANISOU 5694  CZ  TYR D 214     8876   6197   7647    314   -896  -2150       C  
ATOM   5695  OH  TYR D 214     -30.672   8.931  58.414  1.00 59.93           O  
ANISOU 5695  OH  TYR D 214     8892   6189   7690    331   -883  -2162       O  
ATOM   5696  N   THR D 215     -25.034   6.819  59.502  1.00 60.99           N  
ANISOU 5696  N   THR D 215     8026   6978   8170    288   1094   1523       N  
ATOM   5697  CA  THR D 215     -25.318   5.780  58.541  1.00 59.38           C  
ANISOU 5697  CA  THR D 215     7804   6779   7977    273   1141   1514       C  
ATOM   5698  C   THR D 215     -26.721   5.277  58.846  1.00 59.74           C  
ANISOU 5698  C   THR D 215     7829   6843   8027    283   1171   1456       C  
ATOM   5699  O   THR D 215     -27.018   4.898  59.981  1.00 60.17           O  
ANISOU 5699  O   THR D 215     7876   6906   8079    290   1198   1445       O  
ATOM   5700  CB  THR D 215     -24.280   4.635  58.614  1.00 57.33           C  
ANISOU 5700  CB  THR D 215     7542   6518   7724    251   1195   1562       C  
ATOM   5701  OG1 THR D 215     -22.952   5.170  58.448  1.00 56.33           O  
ANISOU 5701  OG1 THR D 215     7436   6374   7592    243   1164   1617       O  
ATOM   5702  CG2 THR D 215     -24.564   3.586  57.536  1.00 57.76           C  
ANISOU 5702  CG2 THR D 215     7579   6578   7790    236   1242   1553       C  
ATOM   5703  N   LYS D 216     -27.602   5.312  57.852  1.00 58.91           N  
ANISOU 5703  N   LYS D 216     7713   6744   7926    284   1166   1418       N  
ATOM   5704  CA  LYS D 216     -28.991   4.912  58.063  1.00 59.80           C  
ANISOU 5704  CA  LYS D 216     7806   6874   8043    295   1191   1361       C  
ATOM   5705  C   LYS D 216     -29.141   3.473  57.634  1.00 58.56           C  
ANISOU 5705  C   LYS D 216     7628   6725   7897    278   1260   1360       C  
ATOM   5706  O   LYS D 216     -28.863   3.156  56.473  1.00 57.83           O  
ANISOU 5706  O   LYS D 216     7533   6628   7811    264   1268   1372       O  
ATOM   5707  CB  LYS D 216     -29.956   5.803  57.269  1.00 61.53           C  
ANISOU 5707  CB  LYS D 216     8024   7094   8260    307   1144   1316       C  
ATOM   5708  CG  LYS D 216     -31.427   5.627  57.626  1.00 63.35           C  
ANISOU 5708  CG  LYS D 216     8237   7341   8492    322   1159   1255       C  
ATOM   5709  CD  LYS D 216     -32.337   6.086  56.490  1.00 65.05           C  
ANISOU 5709  CD  LYS D 216     8446   7559   8710    327   1132   1214       C  
ATOM   5710  CE  LYS D 216     -32.927   7.469  56.733  1.00 67.33           C  
ANISOU 5710  CE  LYS D 216     8747   7847   8990    349   1066   1184       C  
ATOM   5711  NZ  LYS D 216     -33.560   8.016  55.498  1.00 69.08           N  
ANISOU 5711  NZ  LYS D 216     8967   8067   9214    351   1033   1155       N  
ATOM   5712  N   LEU D 217     -29.552   2.599  58.552  1.00 56.95           N  
ANISOU 5712  N   LEU D 217     7409   6533   7695    279   1310   1346       N  
ATOM   5713  CA  LEU D 217     -29.840   1.224  58.168  1.00 56.89           C  
ANISOU 5713  CA  LEU D 217     7381   6535   7699    265   1376   1338       C  
ATOM   5714  C   LEU D 217     -31.334   1.047  58.001  1.00 57.05           C  
ANISOU 5714  C   LEU D 217     7382   6571   7723    275   1388   1276       C  
ATOM   5715  O   LEU D 217     -32.093   1.260  58.951  1.00 57.28           O  
ANISOU 5715  O   LEU D 217     7407   6610   7748    292   1385   1243       O  
ATOM   5716  CB  LEU D 217     -29.305   0.228  59.196  1.00 56.83           C  
ANISOU 5716  CB  LEU D 217     7367   6531   7693    256   1431   1365       C  
ATOM   5717  CG  LEU D 217     -29.624  -1.248  58.942  1.00 56.78           C  
ANISOU 5717  CG  LEU D 217     7339   6536   7699    242   1503   1357       C  
ATOM   5718  CD1 LEU D 217     -28.373  -2.044  58.846  1.00 56.63           C  
ANISOU 5718  CD1 LEU D 217     7323   6509   7684    222   1538   1412       C  
ATOM   5719  CD2 LEU D 217     -30.487  -1.790  60.054  1.00 56.87           C  
ANISOU 5719  CD2 LEU D 217     7334   6563   7710    252   1539   1323       C  
ATOM   5720  N   VAL D 218     -31.742   0.650  56.792  1.00 56.13           N  
ANISOU 5720  N   VAL D 218     7255   6457   7615    266   1401   1259       N  
ATOM   5721  CA  VAL D 218     -33.153   0.436  56.472  1.00 57.46           C  
ANISOU 5721  CA  VAL D 218     7404   6639   7788    275   1413   1200       C  
ATOM   5722  C   VAL D 218     -33.528  -1.023  56.161  1.00 58.13           C  
ANISOU 5722  C   VAL D 218     7466   6735   7885    261   1485   1189       C  
ATOM   5723  O   VAL D 218     -33.239  -1.526  55.074  1.00 57.79           O  
ANISOU 5723  O   VAL D 218     7418   6689   7849    245   1502   1203       O  
ATOM   5724  CB  VAL D 218     -33.551   1.280  55.264  1.00 58.48           C  
ANISOU 5724  CB  VAL D 218     7539   6764   7917    279   1365   1180       C  
ATOM   5725  CG1 VAL D 218     -34.978   1.000  54.883  1.00 61.05           C  
ANISOU 5725  CG1 VAL D 218     7844   7104   8248    287   1380   1120       C  
ATOM   5726  CG2 VAL D 218     -33.381   2.723  55.581  1.00 58.68           C  
ANISOU 5726  CG2 VAL D 218     7584   6780   7931    295   1295   1182       C  
ATOM   5727  N   PHE D 219     -34.226  -1.682  57.086  1.00 57.72           N  
ANISOU 5727  N   PHE D 219     7399   6697   7834    267   1525   1163       N  
ATOM   5728  CA  PHE D 219     -34.690  -3.047  56.845  1.00 59.04           C  
ANISOU 5728  CA  PHE D 219     7543   6876   8012    255   1592   1148       C  
ATOM   5729  C   PHE D 219     -35.741  -3.035  55.759  1.00 61.34           C  
ANISOU 5729  C   PHE D 219     7822   7174   8310    258   1587   1103       C  
ATOM   5730  O   PHE D 219     -36.625  -2.175  55.758  1.00 62.62           O  
ANISOU 5730  O   PHE D 219     7985   7340   8467    275   1547   1063       O  
ATOM   5731  CB  PHE D 219     -35.261  -3.667  58.105  1.00 60.79           C  
ANISOU 5731  CB  PHE D 219     7751   7111   8234    263   1631   1127       C  
ATOM   5732  CG  PHE D 219     -34.238  -3.982  59.131  1.00 59.05           C  
ANISOU 5732  CG  PHE D 219     7540   6886   8011    257   1651   1172       C  
ATOM   5733  CD1 PHE D 219     -33.313  -4.987  58.911  1.00 57.49           C  
ANISOU 5733  CD1 PHE D 219     7340   6684   7820    237   1696   1215       C  
ATOM   5734  CD2 PHE D 219     -34.199  -3.288  60.327  1.00 59.41           C  
ANISOU 5734  CD2 PHE D 219     7596   6930   8046    273   1624   1172       C  
ATOM   5735  CE1 PHE D 219     -32.359  -5.291  59.868  1.00 56.20           C  
ANISOU 5735  CE1 PHE D 219     7185   6517   7653    231   1715   1257       C  
ATOM   5736  CE2 PHE D 219     -33.253  -3.585  61.291  1.00 58.29           C  
ANISOU 5736  CE2 PHE D 219     7462   6784   7901    268   1642   1213       C  
ATOM   5737  CZ  PHE D 219     -32.330  -4.591  61.059  1.00 56.66           C  
ANISOU 5737  CZ  PHE D 219     7253   6574   7702    247   1688   1256       C  
ATOM   5738  N   ALA D 220     -35.665  -3.983  54.832  1.00 58.79           N  
ANISOU 5738  N   ALA D 220     7487   6853   7997    240   1627   1109       N  
ATOM   5739  CA  ALA D 220     -36.634  -4.011  53.729  1.00 61.45           C  
ANISOU 5739  CA  ALA D 220     7812   7196   8341    241   1624   1068       C  
ATOM   5740  C   ALA D 220     -38.054  -4.275  54.218  1.00 64.89           C  
ANISOU 5740  C   ALA D 220     8228   7648   8778    255   1644   1009       C  
ATOM   5741  O   ALA D 220     -38.993  -4.091  53.469  1.00 67.76           O  
ANISOU 5741  O   ALA D 220     8583   8018   9145    260   1632    969       O  
ATOM   5742  CB  ALA D 220     -36.232  -5.047  52.685  1.00 61.95           C  
ANISOU 5742  CB  ALA D 220     7865   7258   8414    220   1667   1088       C  
ATOM   5743  N   LYS D 221     -38.193  -4.730  55.461  1.00 59.48           N  
ANISOU 5743  N   LYS D 221     7537   6971   8091    260   1674   1006       N  
ATOM   5744  CA  LYS D 221     -39.487  -4.834  56.121  1.00 61.12           C  
ANISOU 5744  CA  LYS D 221     7730   7195   8299    276   1687    952       C  
ATOM   5745  C   LYS D 221     -39.321  -4.598  57.617  1.00 60.59           C  
ANISOU 5745  C   LYS D 221     7668   7130   8223    287   1685    959       C  
ATOM   5746  O   LYS D 221     -38.249  -4.801  58.140  1.00 59.57           O  
ANISOU 5746  O   LYS D 221     7549   6993   8092    279   1695   1006       O  
ATOM   5747  CB  LYS D 221     -40.127  -6.196  55.843  1.00 64.15           C  
ANISOU 5747  CB  LYS D 221     8088   7591   8694    265   1754    930       C  
ATOM   5748  CG  LYS D 221     -39.547  -7.405  56.572  1.00 63.59           C  
ANISOU 5748  CG  LYS D 221     8009   7524   8628    252   1816    960       C  
ATOM   5749  CD  LYS D 221     -40.302  -8.664  56.111  1.00 66.80           C  
ANISOU 5749  CD  LYS D 221     8391   7943   9047    243   1877    933       C  
ATOM   5750  CE  LYS D 221     -39.837  -9.937  56.812  1.00 66.92           C  
ANISOU 5750  CE  LYS D 221     8396   7964   9068    230   1942    958       C  
ATOM   5751  NZ  LYS D 221     -40.415 -11.149  56.152  1.00 69.87           N  
ANISOU 5751  NZ  LYS D 221     8746   8347   9453    218   1998    937       N  
ATOM   5752  N   PRO D 222     -40.376  -4.154  58.311  1.00 60.54           N  
ANISOU 5752  N   PRO D 222     7656   7133   8212    306   1670    914       N  
ATOM   5753  CA  PRO D 222     -40.268  -3.883  59.755  1.00 60.66           C  
ANISOU 5753  CA  PRO D 222     7677   7151   8219    319   1665    918       C  
ATOM   5754  C   PRO D 222     -39.845  -5.088  60.574  1.00 60.99           C  
ANISOU 5754  C   PRO D 222     7709   7198   8266    308   1729    941       C  
ATOM   5755  O   PRO D 222     -40.006  -6.192  60.089  1.00 62.27           O  
ANISOU 5755  O   PRO D 222     7855   7366   8438    294   1780    939       O  
ATOM   5756  CB  PRO D 222     -41.684  -3.465  60.130  1.00 64.81           C  
ANISOU 5756  CB  PRO D 222     8193   7690   8743    339   1651    857       C  
ATOM   5757  CG  PRO D 222     -42.227  -2.862  58.863  1.00 65.44           C  
ANISOU 5757  CG  PRO D 222     8273   7767   8824    341   1615    831       C  
ATOM   5758  CD  PRO D 222     -41.660  -3.696  57.754  1.00 63.94           C  
ANISOU 5758  CD  PRO D 222     8078   7572   8644    319   1647    858       C  
ATOM   5759  N   ILE D 223     -39.307  -4.889  61.773  1.00 62.34           N  
ANISOU 5759  N   ILE D 223     7890   7367   8429    313   1725    964       N  
ATOM   5760  CA  ILE D 223     -38.914  -6.016  62.624  1.00 62.99           C  
ANISOU 5760  CA  ILE D 223     7963   7455   8515    304   1785    986       C  
ATOM   5761  C   ILE D 223     -39.950  -6.261  63.716  1.00 67.53           C  
ANISOU 5761  C   ILE D 223     8524   8046   9089    318   1807    944       C  
ATOM   5762  O   ILE D 223     -40.275  -5.348  64.471  1.00 68.76           O  
ANISOU 5762  O   ILE D 223     8688   8202   9234    337   1768    927       O  
ATOM   5763  CB  ILE D 223     -37.525  -5.806  63.302  1.00 59.65           C  
ANISOU 5763  CB  ILE D 223     7559   7019   8085    298   1775   1044       C  
ATOM   5764  CG1 ILE D 223     -36.396  -5.673  62.265  1.00 56.15           C  
ANISOU 5764  CG1 ILE D 223     7130   6561   7645    282   1759   1090       C  
ATOM   5765  CG2 ILE D 223     -37.217  -6.943  64.275  1.00 61.03           C  
ANISOU 5765  CG2 ILE D 223     7724   7201   8264    290   1837   1062       C  
ATOM   5766  CD1 ILE D 223     -36.064  -6.937  61.508  1.00 56.04           C  
ANISOU 5766  CD1 ILE D 223     7103   6548   7643    260   1816   1108       C  
ATOM   5767  N   TYR D 224     -40.463  -7.493  63.794  1.00 65.47           N  
ANISOU 5767  N   TYR D 224     8241   7797   8837    311   1869    928       N  
ATOM   5768  CA  TYR D 224     -41.370  -7.885  64.874  1.00 70.26           C  
ANISOU 5768  CA  TYR D 224     8833   8419   9442    322   1898    892       C  
ATOM   5769  C   TYR D 224     -40.938  -9.169  65.569  1.00 71.96           C  
ANISOU 5769  C   TYR D 224     9038   8640   9664    309   1964    916       C  
ATOM   5770  O   TYR D 224     -40.767 -10.205  64.927  1.00 72.25           O  
ANISOU 5770  O   TYR D 224     9063   8679   9711    292   2010    927       O  
ATOM   5771  CB  TYR D 224     -42.791  -8.075  64.357  1.00 74.45           C  
ANISOU 5771  CB  TYR D 224     9345   8963   9979    330   1907    833       C  
ATOM   5772  CG  TYR D 224     -43.539  -6.804  64.082  1.00 74.59           C  
ANISOU 5772  CG  TYR D 224     9371   8981   9990    348   1845    796       C  
ATOM   5773  CD1 TYR D 224     -43.844  -5.921  65.108  1.00 75.61           C  
ANISOU 5773  CD1 TYR D 224     9508   9112  10109    368   1809    780       C  
ATOM   5774  CD2 TYR D 224     -43.960  -6.495  62.790  1.00 74.20           C  
ANISOU 5774  CD2 TYR D 224     9319   8928   9944    346   1823    776       C  
ATOM   5775  CE1 TYR D 224     -44.539  -4.735  64.852  1.00 76.05           C  
ANISOU 5775  CE1 TYR D 224     9571   9167  10158    386   1751    746       C  
ATOM   5776  CE2 TYR D 224     -44.653  -5.315  62.517  1.00 74.61           C  
ANISOU 5776  CE2 TYR D 224     9378   8980   9990    364   1765    742       C  
ATOM   5777  CZ  TYR D 224     -44.945  -4.435  63.550  1.00 75.48           C  
ANISOU 5777  CZ  TYR D 224     9497   9092  10090    383   1729    727       C  
ATOM   5778  OH  TYR D 224     -45.627  -3.265  63.281  1.00 76.15           O  
ANISOU 5778  OH  TYR D 224     9589   9176  10169    400   1672    693       O  
ATOM   5779  N   ASN D 225     -40.796  -9.097  66.887  1.00 74.61           N  
ANISOU 5779  N   ASN D 225     9377   8979   9993    318   1968    923       N  
ATOM   5780  CA  ASN D 225     -40.487 -10.269  67.702  1.00 77.09           C  
ANISOU 5780  CA  ASN D 225     9680   9299  10311    308   2030    941       C  
ATOM   5781  C   ASN D 225     -41.600 -11.313  67.640  1.00 82.44           C  
ANISOU 5781  C   ASN D 225    10331   9994  10998    307   2084    899       C  
ATOM   5782  O   ASN D 225     -42.778 -10.975  67.492  1.00 85.58           O  
ANISOU 5782  O   ASN D 225    10720  10402  11396    320   2069    848       O  
ATOM   5783  CB  ASN D 225     -40.247  -9.854  69.157  1.00 78.82           C  
ANISOU 5783  CB  ASN D 225     9909   9520  10520    321   2019    951       C  
ATOM   5784  CG  ASN D 225     -39.580 -10.944  69.982  1.00 80.39           C  
ANISOU 5784  CG  ASN D 225    10102   9721  10723    309   2075    984       C  
ATOM   5785  OD1 ASN D 225     -38.814 -11.762  69.459  1.00 78.45           O  
ANISOU 5785  OD1 ASN D 225     9854   9470  10484    289   2110   1019       O  
ATOM   5786  ND2 ASN D 225     -39.861 -10.952  71.285  1.00 84.83           N  
ANISOU 5786  ND2 ASN D 225    10661  10291  11279    321   2085    974       N  
ATOM   5787  N   ASP D 226     -41.220 -12.581  67.761  1.00 79.65           N  
ANISOU 5787  N   ASP D 226     9966   9644  10653    291   2145    920       N  
ATOM   5788  CA  ASP D 226     -42.168 -13.691  67.720  1.00 84.89           C  
ANISOU 5788  CA  ASP D 226    10604  10323  11326    287   2202    886       C  
ATOM   5789  C   ASP D 226     -41.856 -14.695  68.817  1.00 88.52           C  
ANISOU 5789  C   ASP D 226    11056  10790  11788    281   2257    904       C  
ATOM   5790  O   ASP D 226     -41.353 -15.782  68.531  1.00 88.86           O  
ANISOU 5790  O   ASP D 226    11090  10832  11840    262   2307    929       O  
ATOM   5791  CB  ASP D 226     -42.127 -14.372  66.347  1.00 82.88           C  
ANISOU 5791  CB  ASP D 226    10341  10067  11084    269   2226    889       C  
ATOM   5792  CG  ASP D 226     -43.080 -15.550  66.238  1.00 88.47           C  
ANISOU 5792  CG  ASP D 226    11022  10790  11802    265   2285    854       C  
ATOM   5793  OD1 ASP D 226     -43.955 -15.699  67.117  1.00 94.31           O  
ANISOU 5793  OD1 ASP D 226    11750  11543  12540    277   2300    819       O  
ATOM   5794  OD2 ASP D 226     -42.954 -16.322  65.262  1.00 87.38           O  
ANISOU 5794  OD2 ASP D 226    10875  10651  11674    248   2316    861       O  
ATOM   5795  N   PRO D 227     -42.158 -14.346  70.078  1.00 85.37           N  
ANISOU 5795  N   PRO D 227    10658  10397  11382    296   2249    891       N  
ATOM   5796  CA  PRO D 227     -41.826 -15.216  71.218  1.00 89.31           C  
ANISOU 5796  CA  PRO D 227    11151  10902  11882    292   2298    910       C  
ATOM   5797  C   PRO D 227     -42.473 -16.612  71.122  1.00 95.09           C  
ANISOU 5797  C   PRO D 227    11856  11647  12625    282   2367    889       C  
ATOM   5798  O   PRO D 227     -42.081 -17.534  71.848  1.00 98.39           O  
ANISOU 5798  O   PRO D 227    12268  12069  13046    273   2415    910       O  
ATOM   5799  CB  PRO D 227     -42.364 -14.436  72.423  1.00 92.62           C  
ANISOU 5799  CB  PRO D 227    11575  11327  12290    314   2269    885       C  
ATOM   5800  CG  PRO D 227     -42.391 -13.008  71.966  1.00 88.19           C  
ANISOU 5800  CG  PRO D 227    11031  10756  11720    327   2197    878       C  
ATOM   5801  CD  PRO D 227     -42.748 -13.068  70.512  1.00 85.73           C  
ANISOU 5801  CD  PRO D 227    10713  10443  11416    319   2191    862       C  
ATOM   5802  N   SER D 228     -43.443 -16.755  70.218  1.00 92.11           N  
ANISOU 5802  N   SER D 228    11466  11277  12255    283   2370    848       N  
ATOM   5803  CA  SER D 228     -44.196 -17.994  70.052  1.00 98.45           C  
ANISOU 5803  CA  SER D 228    12244  12093  13068    275   2431    822       C  
ATOM   5804  C   SER D 228     -43.346 -19.188  69.568  1.00 99.39           C  
ANISOU 5804  C   SER D 228    12357  12208  13198    251   2484    862       C  
ATOM   5805  O   SER D 228     -43.836 -20.325  69.538  1.00105.73           O  
ANISOU 5805  O   SER D 228    13140  13023  14011    242   2540    847       O  
ATOM   5806  CB  SER D 228     -45.366 -17.754  69.083  1.00 99.16           C  
ANISOU 5806  CB  SER D 228    12323  12191  13163    281   2416    772       C  
ATOM   5807  OG  SER D 228     -46.350 -18.773  69.171  1.00 99.03           O  
ANISOU 5807  OG  SER D 228    12281  12189  13155    280   2469    735       O  
ATOM   5808  N   LEU D 229     -42.088 -18.942  69.199  1.00100.85           N  
ANISOU 5808  N   LEU D 229    12560  12378  13382    239   2466    913       N  
ATOM   5809  CA  LEU D 229     -41.209 -20.010  68.698  1.00100.98           C  
ANISOU 5809  CA  LEU D 229    12572  12389  13407    216   2513    953       C  
ATOM   5810  C   LEU D 229     -40.180 -20.495  69.728  1.00101.96           C  
ANISOU 5810  C   LEU D 229    12702  12509  13528    209   2540    999       C  
ATOM   5811  O   LEU D 229     -39.465 -21.475  69.495  1.00102.21           O  
ANISOU 5811  O   LEU D 229    12730  12538  13567    190   2584   1033       O  
ATOM   5812  CB  LEU D 229     -40.485 -19.547  67.425  1.00 94.33           C  
ANISOU 5812  CB  LEU D 229    11743  11532  12565    206   2480    980       C  
ATOM   5813  CG  LEU D 229     -41.185 -19.865  66.098  1.00 89.34           C  
ANISOU 5813  CG  LEU D 229    11099  10904  11943    200   2488    951       C  
ATOM   5814  CD1 LEU D 229     -40.394 -19.339  64.898  1.00 87.26           C  
ANISOU 5814  CD1 LEU D 229    10850  10624  11679    190   2453    980       C  
ATOM   5815  CD2 LEU D 229     -41.446 -21.375  65.978  1.00 84.83           C  
ANISOU 5815  CD2 LEU D 229    10505  10343  11385    185   2561    946       C  
TER    5816      LEU D 229                                                      
ATOM   7781  N   VAL F   1     112.166 -75.612  50.235  1.00 61.53           N  
ANISOU 7781  N   VAL F   1     5906   7092  10381   1607    910    570       N  
ATOM   7782  CA  VAL F   1     112.740 -74.784  51.305  1.00 61.75           C  
ANISOU 7782  CA  VAL F   1     5960   7105  10398   1623    953    564       C  
ATOM   7783  C   VAL F   1     113.874 -75.435  52.076  1.00 61.75           C  
ANISOU 7783  C   VAL F   1     6009   7064  10391   1622    919    522       C  
ATOM   7784  O   VAL F   1     114.518 -74.769  52.897  1.00 61.59           O  
ANISOU 7784  O   VAL F   1     6012   7029  10360   1638    950    510       O  
ATOM   7785  CB  VAL F   1     111.782 -74.387  52.460  1.00 62.49           C  
ANISOU 7785  CB  VAL F   1     6055   7199  10491   1610    999    614       C  
ATOM   7786  CG1 VAL F   1     111.324 -72.977  52.455  1.00 61.05           C  
ANISOU 7786  CG1 VAL F   1     5846   7045  10306   1629   1069    642       C  
ATOM   7787  CG2 VAL F   1     110.886 -75.487  52.984  1.00 64.96           C  
ANISOU 7787  CG2 VAL F   1     6374   7498  10809   1574    969    647       C  
ATOM   7788  N   LEU F   2     114.059 -76.739  51.884  1.00 57.98           N  
ANISOU 7788  N   LEU F   2     5546   6566   9917   1603    855    505       N  
ATOM   7789  CA  LEU F   2     115.269 -77.452  52.341  1.00 57.89           C  
ANISOU 7789  CA  LEU F   2     5579   6517   9899   1604    812    457       C  
ATOM   7790  C   LEU F   2     115.545 -77.368  53.834  1.00 57.89           C  
ANISOU 7790  C   LEU F   2     5618   6487   9890   1601    831    461       C  
ATOM   7791  O   LEU F   2     116.356 -76.573  54.293  1.00 57.68           O  
ANISOU 7791  O   LEU F   2     5608   6452   9854   1624    862    439       O  
ATOM   7792  CB  LEU F   2     116.462 -76.976  51.564  1.00 57.61           C  
ANISOU 7792  CB  LEU F   2     5544   6485   9859   1634    807    406       C  
ATOM   7793  CG  LEU F   2     116.461 -77.751  50.257  1.00 57.66           C  
ANISOU 7793  CG  LEU F   2     5530   6503   9874   1628    755    388       C  
ATOM   7794  CD1 LEU F   2     115.749 -77.006  49.146  1.00 57.64           C  
ANISOU 7794  CD1 LEU F   2     5479   6544   9878   1638    784    410       C  
ATOM   7795  CD2 LEU F   2     117.882 -78.111  49.850  1.00 57.46           C  
ANISOU 7795  CD2 LEU F   2     5529   6459   9844   1644    714    326       C  
ATOM   7796  N   SER F   3     114.778 -78.157  54.579  1.00 58.14           N  
ANISOU 7796  N   SER F   3     5661   6505   9925   1571    816    493       N  
ATOM   7797  CA  SER F   3     114.952 -78.345  56.013  1.00 58.19           C  
ANISOU 7797  CA  SER F   3     5706   6479   9924   1562    824    499       C  
ATOM   7798  C   SER F   3     116.258 -79.039  56.285  1.00 58.08           C  
ANISOU 7798  C   SER F   3     5734   6429   9904   1566    778    445       C  
ATOM   7799  O   SER F   3     116.910 -79.521  55.358  1.00 57.99           O  
ANISOU 7799  O   SER F   3     5721   6418   9896   1573    735    408       O  
ATOM   7800  CB  SER F   3     113.818 -79.188  56.589  1.00 58.51           C  
ANISOU 7800  CB  SER F   3     5747   6513   9971   1527    810    543       C  
ATOM   7801  OG  SER F   3     114.089 -80.573  56.447  1.00 58.63           O  
ANISOU 7801  OG  SER F   3     5782   6505   9990   1507    741    522       O  
ATOM   7802  N   PRO F   4     116.662 -79.093  57.560  1.00 58.49           N  
ANISOU 7802  N   PRO F   4     5824   6451   9947   1564    786    442       N  
ATOM   7803  CA  PRO F   4     117.765 -80.017  57.846  1.00 58.95           C  
ANISOU 7803  CA  PRO F   4     5924   6473  10002   1561    732    395       C  
ATOM   7804  C   PRO F   4     117.527 -81.428  57.255  1.00 58.99           C  
ANISOU 7804  C   PRO F   4     5928   6469  10016   1536    664    389       C  
ATOM   7805  O   PRO F   4     118.433 -81.996  56.642  1.00 58.36           O  
ANISOU 7805  O   PRO F   4     5860   6379   9937   1543    618    344       O  
ATOM   7806  CB  PRO F   4     117.784 -80.064  59.375  1.00 60.68           C  
ANISOU 7806  CB  PRO F   4     6180   6664  10213   1552    750    409       C  
ATOM   7807  CG  PRO F   4     117.228 -78.744  59.802  1.00 60.82           C  
ANISOU 7807  CG  PRO F   4     6180   6703  10227   1565    823    443       C  
ATOM   7808  CD  PRO F   4     116.209 -78.366  58.763  1.00 59.65           C  
ANISOU 7808  CD  PRO F   4     5981   6595  10088   1563    841    476       C  
ATOM   7809  N   ALA F   5     116.315 -81.963  57.399  1.00 58.48           N  
ANISOU 7809  N   ALA F   5     5849   6413   9959   1508    659    435       N  
ATOM   7810  CA  ALA F   5     116.011 -83.289  56.865  1.00 58.68           C  
ANISOU 7810  CA  ALA F   5     5872   6430   9994   1484    597    433       C  
ATOM   7811  C   ALA F   5     116.325 -83.377  55.371  1.00 58.58           C  
ANISOU 7811  C   ALA F   5     5831   6439   9987   1495    569    405       C  
ATOM   7812  O   ALA F   5     117.119 -84.223  54.954  1.00 58.54           O  
ANISOU 7812  O   ALA F   5     5844   6416   9983   1494    513    364       O  
ATOM   7813  CB  ALA F   5     114.571 -83.637  57.117  1.00 59.43           C  
ANISOU 7813  CB  ALA F   5     5947   6537  10097   1455    605    490       C  
ATOM   7814  N   ASP F   6     115.727 -82.491  54.579  1.00 58.53           N  
ANISOU 7814  N   ASP F   6     5784   6471   9985   1507    607    427       N  
ATOM   7815  CA  ASP F   6     116.030 -82.444  53.158  1.00 58.42           C  
ANISOU 7815  CA  ASP F   6     5742   6479   9976   1521    586    401       C  
ATOM   7816  C   ASP F   6     117.531 -82.424  52.921  1.00 58.17           C  
ANISOU 7816  C   ASP F   6     5735   6429   9937   1544    563    340       C  
ATOM   7817  O   ASP F   6     118.049 -83.241  52.178  1.00 58.16           O  
ANISOU 7817  O   ASP F   6     5737   6421   9939   1542    509    307       O  
ATOM   7818  CB  ASP F   6     115.441 -81.206  52.506  1.00 58.34           C  
ANISOU 7818  CB  ASP F   6     5689   6509   9967   1539    642    426       C  
ATOM   7819  CG  ASP F   6     114.032 -81.003  52.851  1.00 58.55           C  
ANISOU 7819  CG  ASP F   6     5693   6554  10000   1520    675    486       C  
ATOM   7820  OD1 ASP F   6     113.213 -81.846  52.408  1.00 58.78           O  
ANISOU 7820  OD1 ASP F   6     5704   6589  10039   1497    643    508       O  
ATOM   7821  OD2 ASP F   6     113.747 -80.003  53.551  1.00 58.50           O  
ANISOU 7821  OD2 ASP F   6     5684   6555   9988   1530    734    511       O  
ATOM   7822  N   LYS F   7     118.204 -81.466  53.560  1.00 57.96           N  
ANISOU 7822  N   LYS F   7     5726   6396   9900   1567    605    326       N  
ATOM   7823  CA  LYS F   7     119.608 -81.206  53.305  1.00 57.69           C  
ANISOU 7823  CA  LYS F   7     5711   6350   9859   1593    594    270       C  
ATOM   7824  C   LYS F   7     120.399 -82.516  53.463  1.00 57.74           C  
ANISOU 7824  C   LYS F   7     5753   6320   9865   1580    525    231       C  
ATOM   7825  O   LYS F   7     121.179 -82.895  52.576  1.00 57.63           O  
ANISOU 7825  O   LYS F   7     5739   6305   9852   1590    486    189       O  
ATOM   7826  CB  LYS F   7     120.148 -80.108  54.243  1.00 57.50           C  
ANISOU 7826  CB  LYS F   7     5706   6318   9824   1615    648    265       C  
ATOM   7827  CG  LYS F   7     119.700 -78.650  53.982  1.00 57.39           C  
ANISOU 7827  CG  LYS F   7     5658   6338   9808   1636    718    290       C  
ATOM   7828  CD  LYS F   7     120.370 -77.700  55.012  1.00 57.20           C  
ANISOU 7828  CD  LYS F   7     5660   6300   9772   1656    764    280       C  
ATOM   7829  CE  LYS F   7     119.699 -76.334  55.137  1.00 57.14           C  
ANISOU 7829  CE  LYS F   7     5625   6322   9764   1670    837    317       C  
ATOM   7830  NZ  LYS F   7     119.841 -75.583  53.895  1.00 56.98           N  
ANISOU 7830  NZ  LYS F   7     5569   6334   9746   1692    853    305       N  
ATOM   7831  N   THR F   8     120.148 -83.222  54.569  1.00 57.91           N  
ANISOU 7831  N   THR F   8     5804   6314   9885   1558    511    247       N  
ATOM   7832  CA  THR F   8     120.766 -84.533  54.830  1.00 57.99           C  
ANISOU 7832  CA  THR F   8     5849   6288   9895   1542    446    216       C  
ATOM   7833  C   THR F   8     120.526 -85.498  53.685  1.00 58.10           C  
ANISOU 7833  C   THR F   8     5844   6312   9920   1528    390    208       C  
ATOM   7834  O   THR F   8     121.460 -86.041  53.140  1.00 58.00           O  
ANISOU 7834  O   THR F   8     5844   6287   9907   1535    345    162       O  
ATOM   7835  CB  THR F   8     120.236 -85.169  56.118  1.00 58.20           C  
ANISOU 7835  CB  THR F   8     5904   6290   9921   1515    441    246       C  
ATOM   7836  OG1 THR F   8     120.696 -84.422  57.245  1.00 58.08           O  
ANISOU 7836  OG1 THR F   8     5915   6258   9895   1529    483    244       O  
ATOM   7837  CG2 THR F   8     120.739 -86.531  56.236  1.00 58.30           C  
ANISOU 7837  CG2 THR F   8     5947   6270   9936   1498    373    218       C  
ATOM   7838  N   ASN F   9     119.265 -85.680  53.308  1.00 58.31           N  
ANISOU 7838  N   ASN F   9     5839   6362   9956   1509    395    253       N  
ATOM   7839  CA  ASN F   9     118.903 -86.574  52.209  1.00 58.45           C  
ANISOU 7839  CA  ASN F   9     5833   6390   9984   1495    345    250       C  
ATOM   7840  C   ASN F   9     119.621 -86.286  50.906  1.00 58.24           C  
ANISOU 7840  C   ASN F   9     5788   6383   9959   1518    331    211       C  
ATOM   7841  O   ASN F   9     120.097 -87.195  50.259  1.00 58.26           O  
ANISOU 7841  O   ASN F   9     5796   6375   9965   1513    275    179       O  
ATOM   7842  CB  ASN F   9     117.407 -86.511  51.960  1.00 58.67           C  
ANISOU 7842  CB  ASN F   9     5824   6446  10021   1476    366    307       C  
ATOM   7843  CG  ASN F   9     116.631 -87.302  52.958  1.00 58.94           C  
ANISOU 7843  CG  ASN F   9     5875   6460  10058   1445    354    343       C  
ATOM   7844  OD1 ASN F   9     116.555 -86.954  54.139  1.00 58.95           O  
ANISOU 7844  OD1 ASN F   9     5899   6447  10053   1442    386    360       O  
ATOM   7845  ND2 ASN F   9     116.049 -88.389  52.496  1.00 59.15           N  
ANISOU 7845  ND2 ASN F   9     5893   6487  10095   1420    306    354       N  
ATOM   7846  N   VAL F  10     119.699 -85.018  50.522  1.00 58.06           N  
ANISOU 7846  N   VAL F  10     5742   6385   9932   1544    383    213       N  
ATOM   7847  CA  VAL F  10     120.357 -84.647  49.273  1.00 57.86           C  
ANISOU 7847  CA  VAL F  10     5697   6380   9908   1567    375    177       C  
ATOM   7848  C   VAL F  10     121.826 -84.986  49.307  1.00 57.67           C  
ANISOU 7848  C   VAL F  10     5707   6328   9877   1582    340    116       C  
ATOM   7849  O   VAL F  10     122.368 -85.486  48.327  1.00 57.61           O  
ANISOU 7849  O   VAL F  10     5694   6323   9873   1587    297     81       O  
ATOM   7850  CB  VAL F  10     120.213 -83.172  48.968  1.00 57.69           C  
ANISOU 7850  CB  VAL F  10     5647   6389   9882   1593    441    190       C  
ATOM   7851  CG1 VAL F  10     120.601 -82.908  47.533  1.00 57.54           C  
ANISOU 7851  CG1 VAL F  10     5600   6396   9867   1612    429    162       C  
ATOM   7852  CG2 VAL F  10     118.776 -82.758  49.200  1.00 57.87           C  
ANISOU 7852  CG2 VAL F  10     5641   6436   9911   1579    482    252       C  
ATOM   7853  N   LYS F  11     122.474 -84.726  50.435  1.00 57.58           N  
ANISOU 7853  N   LYS F  11     5731   6289   9856   1589    357    104       N  
ATOM   7854  CA  LYS F  11     123.900 -85.065  50.547  1.00 57.40           C  
ANISOU 7854  CA  LYS F  11     5744   6238   9826   1602    323     45       C  
ATOM   7855  C   LYS F  11     124.079 -86.585  50.491  1.00 57.56           C  
ANISOU 7855  C   LYS F  11     5785   6232   9852   1579    250     27       C  
ATOM   7856  O   LYS F  11     124.879 -87.096  49.701  1.00 57.47           O  
ANISOU 7856  O   LYS F  11     5778   6215   9842   1586    205    -17       O  
ATOM   7857  CB  LYS F  11     124.528 -84.507  51.835  1.00 57.27           C  
ANISOU 7857  CB  LYS F  11     5764   6197   9800   1613    356     37       C  
ATOM   7858  CG  LYS F  11     124.893 -83.048  51.762  1.00 57.03           C  
ANISOU 7858  CG  LYS F  11     5720   6186   9762   1644    417     32       C  
ATOM   7859  CD  LYS F  11     125.491 -82.570  53.057  1.00 56.92           C  
ANISOU 7859  CD  LYS F  11     5743   6147   9738   1654    446     24       C  
ATOM   7860  CE  LYS F  11     124.713 -83.054  54.260  1.00 57.15           C  
ANISOU 7860  CE  LYS F  11     5791   6157   9767   1627    450     63       C  
ATOM   7861  NZ  LYS F  11     125.236 -82.453  55.513  1.00 57.04           N  
ANISOU 7861  NZ  LYS F  11     5809   6122   9742   1638    486     59       N  
ATOM   7862  N   ALA F  12     123.314 -87.293  51.321  1.00 57.80           N  
ANISOU 7862  N   ALA F  12     5829   6247   9885   1550    239     61       N  
ATOM   7863  CA  ALA F  12     123.426 -88.725  51.421  1.00 57.97           C  
ANISOU 7863  CA  ALA F  12     5872   6242   9911   1526    172     47       C  
ATOM   7864  C   ALA F  12     123.119 -89.356  50.072  1.00 58.05           C  
ANISOU 7864  C   ALA F  12     5852   6272   9932   1519    131     41       C  
ATOM   7865  O   ALA F  12     123.745 -90.334  49.679  1.00 58.06           O  
ANISOU 7865  O   ALA F  12     5869   6255   9936   1513     72      5       O  
ATOM   7866  CB  ALA F  12     122.520 -89.251  52.496  1.00 58.22           C  
ANISOU 7866  CB  ALA F  12     5918   6259   9945   1498    175     91       C  
ATOM   7867  N   ALA F  13     122.202 -88.785  49.321  1.00 58.09           N  
ANISOU 7867  N   ALA F  13     5815   6314   9944   1521    160     74       N  
ATOM   7868  CA  ALA F  13     121.867 -89.403  48.044  1.00 58.18           C  
ANISOU 7868  CA  ALA F  13     5797   6344   9965   1513    120     70       C  
ATOM   7869  C   ALA F  13     122.884 -89.069  46.960  1.00 57.94           C  
ANISOU 7869  C   ALA F  13     5758   6325   9932   1540    108     21       C  
ATOM   7870  O   ALA F  13     123.168 -89.881  46.093  1.00 57.97           O  
ANISOU 7870  O   ALA F  13     5757   6327   9941   1535     55     -5       O  
ATOM   7871  CB  ALA F  13     120.464 -88.989  47.596  1.00 58.34           C  
ANISOU 7871  CB  ALA F  13     5773   6400   9992   1503    153    125       C  
ATOM   7872  N   TRP F  14     123.426 -87.859  47.005  1.00 57.70           N  
ANISOU 7872  N   TRP F  14     5725   6305   9894   1568    157      9       N  
ATOM   7873  CA  TRP F  14     124.308 -87.379  45.937  1.00 57.46           C  
ANISOU 7873  CA  TRP F  14     5682   6290   9862   1596    153    -33       C  
ATOM   7874  C   TRP F  14     125.687 -87.939  46.155  1.00 57.33           C  
ANISOU 7874  C   TRP F  14     5704   6239   9839   1604    111    -90       C  
ATOM   7875  O   TRP F  14     126.487 -88.016  45.226  1.00 57.18           O  
ANISOU 7875  O   TRP F  14     5681   6225   9820   1620     85   -132       O  
ATOM   7876  CB  TRP F  14     124.335 -85.844  45.898  1.00 57.27           C  
ANISOU 7876  CB  TRP F  14     5638   6290   9831   1623    223    -24       C  
ATOM   7877  CG  TRP F  14     125.027 -85.255  44.720  1.00 57.05           C  
ANISOU 7877  CG  TRP F  14     5590   6283   9802   1650    226    -58       C  
ATOM   7878  CD1 TRP F  14     126.222 -84.634  44.719  1.00 56.78           C  
ANISOU 7878  CD1 TRP F  14     5572   6242   9760   1678    239   -101       C  
ATOM   7879  CD2 TRP F  14     124.558 -85.229  43.373  1.00 57.08           C  
ANISOU 7879  CD2 TRP F  14     5553   6320   9813   1653    217    -53       C  
ATOM   7880  NE1 TRP F  14     126.535 -84.208  43.453  1.00 56.64           N  
ANISOU 7880  NE1 TRP F  14     5527   6250   9744   1697    239   -123       N  
ATOM   7881  CE2 TRP F  14     125.533 -84.573  42.606  1.00 56.81           C  
ANISOU 7881  CE2 TRP F  14     5514   6297   9776   1682    225    -94       C  
ATOM   7882  CE3 TRP F  14     123.413 -85.702  42.741  1.00 57.29           C  
ANISOU 7882  CE3 TRP F  14     5549   6369   9851   1633    202    -17       C  
ATOM   7883  CZ2 TRP F  14     125.409 -84.379  41.251  1.00 56.77           C  
ANISOU 7883  CZ2 TRP F  14     5473   6322   9775   1692    218   -101       C  
ATOM   7884  CZ3 TRP F  14     123.283 -85.506  41.389  1.00 57.25           C  
ANISOU 7884  CZ3 TRP F  14     5508   6394   9851   1643    196    -24       C  
ATOM   7885  CH2 TRP F  14     124.277 -84.843  40.657  1.00 56.99           C  
ANISOU 7885  CH2 TRP F  14     5470   6371   9813   1673    204    -65       C  
ATOM   7886  N   GLY F  15     125.945 -88.334  47.401  1.00 58.82           N  
ANISOU 7886  N   GLY F  15     5932   6395  10023   1593    105    -91       N  
ATOM   7887  CA  GLY F  15     127.138 -89.088  47.762  1.00 58.79           C  
ANISOU 7887  CA  GLY F  15     5969   6353  10014   1595     58   -141       C  
ATOM   7888  C   GLY F  15     127.076 -90.439  47.098  1.00 59.47           C  
ANISOU 7888  C   GLY F  15     6054   6431  10109   1575    -12   -155       C  
ATOM   7889  O   GLY F  15     127.926 -90.751  46.276  1.00 59.27           O  
ANISOU 7889  O   GLY F  15     6030   6404  10084   1587    -48   -200       O  
ATOM   7890  N   LYS F  16     126.004 -91.187  47.356  1.00 60.87           N  
ANISOU 7890  N   LYS F  16     6227   6608  10294   1545    -28   -115       N  
ATOM   7891  CA  LYS F  16     125.797 -92.494  46.727  1.00 62.25           C  
ANISOU 7891  CA  LYS F  16     6398   6776  10478   1523    -94   -123       C  
ATOM   7892  C   LYS F  16     125.842 -92.415  45.190  1.00 62.12           C  
ANISOU 7892  C   LYS F  16     6346   6790  10468   1535   -110   -140       C  
ATOM   7893  O   LYS F  16     125.840 -93.435  44.508  1.00 63.43           O  
ANISOU 7893  O   LYS F  16     6507   6952  10640   1522   -166   -154       O  
ATOM   7894  CB  LYS F  16     124.457 -93.100  47.156  1.00 63.00           C  
ANISOU 7894  CB  LYS F  16     6484   6873  10581   1491    -98    -69       C  
ATOM   7895  CG  LYS F  16     124.411 -93.656  48.581  1.00 63.64           C  
ANISOU 7895  CG  LYS F  16     6604   6918  10658   1472   -105    -56       C  
ATOM   7896  CD  LYS F  16     125.162 -94.996  48.703  1.00 65.29           C  
ANISOU 7896  CD  LYS F  16     6848   7092  10868   1458   -177    -95       C  
ATOM   7897  CE  LYS F  16     124.512 -95.949  49.721  1.00 67.02           C  
ANISOU 7897  CE  LYS F  16     7090   7286  11090   1426   -199    -65       C  
ATOM   7898  NZ  LYS F  16     124.680 -95.557  51.165  1.00 66.96           N  
ANISOU 7898  NZ  LYS F  16     7115   7255  11073   1426   -164    -54       N  
ATOM   7899  N   VAL F  17     125.833 -91.205  44.647  1.00 60.83           N  
ANISOU 7899  N   VAL F  17     6155   6656  10301   1559    -61   -136       N  
ATOM   7900  CA  VAL F  17     126.031 -91.004  43.222  1.00 60.73           C  
ANISOU 7900  CA  VAL F  17     6110   6671  10292   1574    -72   -157       C  
ATOM   7901  C   VAL F  17     127.528 -91.066  42.903  1.00 60.49           C  
ANISOU 7901  C   VAL F  17     6103   6624  10256   1596    -99   -220       C  
ATOM   7902  O   VAL F  17     127.943 -91.739  41.953  1.00 60.48           O  
ANISOU 7902  O   VAL F  17     6096   6624  10259   1597   -148   -252       O  
ATOM   7903  CB  VAL F  17     125.391 -89.664  42.765  1.00 60.64           C  
ANISOU 7903  CB  VAL F  17     6060   6700  10281   1592     -7   -126       C  
ATOM   7904  CG1 VAL F  17     125.772 -89.324  41.355  1.00 60.49           C  
ANISOU 7904  CG1 VAL F  17     6013   6708  10264   1612    -14   -152       C  
ATOM   7905  CG2 VAL F  17     123.890 -89.744  42.880  1.00 60.89           C  
ANISOU 7905  CG2 VAL F  17     6065   6750  10320   1568     11    -65       C  
ATOM   7906  N   GLY F  18     128.333 -90.376  43.707  1.00 63.98           N  
ANISOU 7906  N   GLY F  18     6572   7050  10688   1615    -68   -239       N  
ATOM   7907  CA  GLY F  18     129.794 -90.459  43.612  1.00 64.61           C  
ANISOU 7907  CA  GLY F  18     6679   7109  10762   1634    -93   -300       C  
ATOM   7908  C   GLY F  18     130.383 -90.068  42.264  1.00 64.79           C  
ANISOU 7908  C   GLY F  18     6677   7155  10784   1658    -99   -334       C  
ATOM   7909  O   GLY F  18     129.819 -89.204  41.578  1.00 63.96           O  
ANISOU 7909  O   GLY F  18     6535   7085  10681   1669    -60   -312       O  
ATOM   7910  N   ALA F  19     131.468 -90.736  41.861  1.00 62.81           N  
ANISOU 7910  N   ALA F  19     6446   6885  10533   1664   -150   -387       N  
ATOM   7911  CA  ALA F  19     132.158 -90.409  40.607  1.00 62.63           C  
ANISOU 7911  CA  ALA F  19     6403   6882  10510   1687   -159   -425       C  
ATOM   7912  C   ALA F  19     131.247 -90.505  39.375  1.00 62.74           C  
ANISOU 7912  C   ALA F  19     6373   6932  10534   1680   -166   -401       C  
ATOM   7913  O   ALA F  19     131.585 -90.012  38.293  1.00 62.60           O  
ANISOU 7913  O   ALA F  19     6331   6938  10516   1700   -160   -422       O  
ATOM   7914  CB  ALA F  19     133.366 -91.306  40.422  1.00 63.32           C  
ANISOU 7914  CB  ALA F  19     6520   6941  10596   1690   -219   -483       C  
ATOM   7915  N   HIS F  20     130.086 -91.131  39.535  1.00 65.20           N  
ANISOU 7915  N   HIS F  20     6673   7247  10852   1653   -178   -358       N  
ATOM   7916  CA  HIS F  20     129.158 -91.253  38.420  1.00 65.54           C  
ANISOU 7916  CA  HIS F  20     6674   7324  10905   1645   -185   -333       C  
ATOM   7917  C   HIS F  20     128.432 -89.914  38.202  1.00 64.22           C  
ANISOU 7917  C   HIS F  20     6472   7192  10736   1659   -115   -295       C  
ATOM   7918  O   HIS F  20     127.790 -89.701  37.162  1.00 64.64           O  
ANISOU 7918  O   HIS F  20     6487   7278  10796   1660   -110   -278       O  
ATOM   7919  CB  HIS F  20     128.187 -92.397  38.670  1.00 66.12           C  
ANISOU 7919  CB  HIS F  20     6748   7388  10987   1610   -222   -300       C  
ATOM   7920  CG  HIS F  20     128.866 -93.668  39.042  1.00 67.67           C  
ANISOU 7920  CG  HIS F  20     6981   7546  11184   1595   -286   -334       C  
ATOM   7921  ND1 HIS F  20     129.294 -94.585  38.106  1.00 69.52           N  
ANISOU 7921  ND1 HIS F  20     7213   7778  11424   1592   -346   -368       N  
ATOM   7922  CD2 HIS F  20     129.232 -94.165  40.250  1.00 67.81           C  
ANISOU 7922  CD2 HIS F  20     7039   7527  11197   1584   -299   -340       C  
ATOM   7923  CE1 HIS F  20     129.876 -95.602  38.721  1.00 70.69           C  
ANISOU 7923  CE1 HIS F  20     7399   7889  11571   1579   -394   -393       C  
ATOM   7924  NE2 HIS F  20     129.853 -95.371  40.023  1.00 69.68           N  
ANISOU 7924  NE2 HIS F  20     7297   7740  11437   1574   -367   -377       N  
ATOM   7925  N   ALA F  21     128.585 -88.998  39.155  1.00 64.39           N  
ANISOU 7925  N   ALA F  21     6508   7208  10750   1670    -63   -285       N  
ATOM   7926  CA  ALA F  21     127.963 -87.694  39.046  1.00 63.66           C  
ANISOU 7926  CA  ALA F  21     6385   7147  10656   1685      4   -251       C  
ATOM   7927  C   ALA F  21     128.180 -87.110  37.653  1.00 63.11           C  
ANISOU 7927  C   ALA F  21     6281   7110  10587   1707     12   -268       C  
ATOM   7928  O   ALA F  21     127.264 -86.556  37.052  1.00 63.00           O  
ANISOU 7928  O   ALA F  21     6229   7130  10577   1707     42   -233       O  
ATOM   7929  CB  ALA F  21     128.508 -86.757  40.115  1.00 62.84           C  
ANISOU 7929  CB  ALA F  21     6305   7029  10541   1702     54   -254       C  
ATOM   7930  N   GLY F  22     129.371 -87.279  37.107  1.00 62.27           N  
ANISOU 7930  N   GLY F  22     6188   6995  10478   1724    -18   -323       N  
ATOM   7931  CA  GLY F  22     129.608 -86.784  35.768  1.00 63.13           C  
ANISOU 7931  CA  GLY F  22     6265   7133  10587   1744    -15   -342       C  
ATOM   7932  C   GLY F  22     128.761 -87.502  34.744  1.00 64.10           C  
ANISOU 7932  C   GLY F  22     6357   7278  10721   1727    -50   -324       C  
ATOM   7933  O   GLY F  22     128.100 -86.888  33.921  1.00 64.10           O  
ANISOU 7933  O   GLY F  22     6319   7313  10724   1734    -23   -300       O  
ATOM   7934  N   GLU F  23     128.775 -88.821  34.823  1.00 64.76           N  
ANISOU 7934  N   GLU F  23     6458   7338  10809   1704   -110   -334       N  
ATOM   7935  CA  GLU F  23     128.201 -89.656  33.792  1.00 66.13           C  
ANISOU 7935  CA  GLU F  23     6607   7528  10993   1689   -155   -328       C  
ATOM   7936  C   GLU F  23     126.666 -89.571  33.811  1.00 65.32           C  
ANISOU 7936  C   GLU F  23     6474   7448  10898   1669   -131   -266       C  
ATOM   7937  O   GLU F  23     126.011 -89.700  32.765  1.00 66.14           O  
ANISOU 7937  O   GLU F  23     6542   7579  11008   1665   -142   -252       O  
ATOM   7938  CB  GLU F  23     128.714 -91.093  33.975  1.00 67.62           C  
ANISOU 7938  CB  GLU F  23     6826   7682  11184   1670   -226   -359       C  
ATOM   7939  CG  GLU F  23     127.659 -92.196  33.983  1.00 68.15           C  
ANISOU 7939  CG  GLU F  23     6886   7747  11262   1637   -264   -325       C  
ATOM   7940  CD  GLU F  23     128.173 -93.492  34.630  1.00 69.29           C  
ANISOU 7940  CD  GLU F  23     7070   7850  11407   1618   -323   -350       C  
ATOM   7941  OE1 GLU F  23     129.281 -93.433  35.244  1.00 68.85           O  
ANISOU 7941  OE1 GLU F  23     7048   7767  11343   1630   -327   -388       O  
ATOM   7942  OE2 GLU F  23     127.463 -94.550  34.526  1.00 70.79           O  
ANISOU 7942  OE2 GLU F  23     7255   8035  11606   1591   -365   -331       O  
ATOM   7943  N   TYR F  24     126.093 -89.320  34.989  1.00 62.29           N  
ANISOU 7943  N   TYR F  24     6102   7053  10512   1658    -97   -229       N  
ATOM   7944  CA  TYR F  24     124.647 -89.120  35.092  1.00 62.49           C  
ANISOU 7944  CA  TYR F  24     6099   7100  10544   1641    -68   -169       C  
ATOM   7945  C   TYR F  24     124.285 -87.824  34.424  1.00 62.37           C  
ANISOU 7945  C   TYR F  24     6046   7123  10527   1662    -12   -151       C  
ATOM   7946  O   TYR F  24     123.329 -87.780  33.668  1.00 62.49           O  
ANISOU 7946  O   TYR F  24     6026   7168  10550   1655     -7   -120       O  
ATOM   7947  CB  TYR F  24     124.166 -89.099  36.540  1.00 62.60           C  
ANISOU 7947  CB  TYR F  24     6135   7094  10555   1625    -43   -135       C  
ATOM   7948  CG  TYR F  24     124.345 -90.407  37.282  1.00 62.75           C  
ANISOU 7948  CG  TYR F  24     6191   7076  10577   1600    -96   -145       C  
ATOM   7949  CD1 TYR F  24     124.221 -90.446  38.659  1.00 62.82           C  
ANISOU 7949  CD1 TYR F  24     6228   7059  10581   1588    -79   -127       C  
ATOM   7950  CD2 TYR F  24     124.649 -91.596  36.612  1.00 62.84           C  
ANISOU 7950  CD2 TYR F  24     6206   7076  10594   1588   -164   -173       C  
ATOM   7951  CE1 TYR F  24     124.379 -91.605  39.345  1.00 62.96           C  
ANISOU 7951  CE1 TYR F  24     6278   7042  10601   1566   -126   -135       C  
ATOM   7952  CE2 TYR F  24     124.802 -92.755  37.299  1.00 62.98           C  
ANISOU 7952  CE2 TYR F  24     6256   7060  10614   1566   -211   -182       C  
ATOM   7953  CZ  TYR F  24     124.665 -92.750  38.668  1.00 63.04           C  
ANISOU 7953  CZ  TYR F  24     6292   7043  10617   1555   -192   -162       C  
ATOM   7954  OH  TYR F  24     124.805 -93.888  39.407  1.00 63.19           O  
ANISOU 7954  OH  TYR F  24     6344   7027  10637   1532   -238   -169       O  
ATOM   7955  N   GLY F  25     125.064 -86.776  34.696  1.00 64.62           N  
ANISOU 7955  N   GLY F  25     6341   7409  10803   1689     30   -171       N  
ATOM   7956  CA  GLY F  25     124.824 -85.464  34.129  1.00 64.06           C  
ANISOU 7956  CA  GLY F  25     6237   7372  10729   1712     87   -156       C  
ATOM   7957  C   GLY F  25     124.597 -85.520  32.634  1.00 64.15           C  
ANISOU 7957  C   GLY F  25     6212   7416  10747   1718     69   -163       C  
ATOM   7958  O   GLY F  25     123.733 -84.820  32.099  1.00 64.12           O  
ANISOU 7958  O   GLY F  25     6172   7445  10746   1722    105   -128       O  
ATOM   7959  N   ALA F  26     125.360 -86.378  31.965  1.00 65.03           N  
ANISOU 7959  N   ALA F  26     6334   7516  10860   1718     11   -206       N  
ATOM   7960  CA  ALA F  26     125.245 -86.537  30.528  1.00 65.46           C  
ANISOU 7960  CA  ALA F  26     6356   7597  10919   1724    -13   -217       C  
ATOM   7961  C   ALA F  26     124.058 -87.389  30.170  1.00 66.35           C  
ANISOU 7961  C   ALA F  26     6447   7720  11043   1696    -42   -181       C  
ATOM   7962  O   ALA F  26     123.353 -87.088  29.215  1.00 67.32           O  
ANISOU 7962  O   ALA F  26     6532   7876  11171   1698    -31   -160       O  
ATOM   7963  CB  ALA F  26     126.482 -87.139  29.971  1.00 67.02           C  
ANISOU 7963  CB  ALA F  26     6572   7777  11114   1734    -63   -277       C  
ATOM   7964  N   GLU F  27     123.855 -88.473  30.910  1.00 66.79           N  
ANISOU 7964  N   GLU F  27     6528   7748  11103   1670    -81   -175       N  
ATOM   7965  CA  GLU F  27     122.696 -89.329  30.666  1.00 67.62           C  
ANISOU 7965  CA  GLU F  27     6613   7860  11218   1641   -109   -138       C  
ATOM   7966  C   GLU F  27     121.416 -88.491  30.820  1.00 66.41           C  
ANISOU 7966  C   GLU F  27     6429   7736  11069   1637    -52    -79       C  
ATOM   7967  O   GLU F  27     120.500 -88.591  30.009  1.00 67.29           O  
ANISOU 7967  O   GLU F  27     6505   7874  11188   1629    -56    -52       O  
ATOM   7968  CB  GLU F  27     122.675 -90.527  31.617  1.00 67.71           C  
ANISOU 7968  CB  GLU F  27     6659   7834  11232   1614   -152   -138       C  
ATOM   7969  CG  GLU F  27     121.823 -91.698  31.128  1.00 69.54           C  
ANISOU 7969  CG  GLU F  27     6876   8069  11476   1586   -202   -118       C  
ATOM   7970  CD  GLU F  27     121.236 -92.535  32.269  1.00 69.57           C  
ANISOU 7970  CD  GLU F  27     6903   8046  11483   1555   -219    -90       C  
ATOM   7971  OE1 GLU F  27     120.824 -93.688  32.026  1.00 71.50           O  
ANISOU 7971  OE1 GLU F  27     7148   8283  11737   1531   -271    -86       O  
ATOM   7972  OE2 GLU F  27     121.173 -92.039  33.414  1.00 67.81           O  
ANISOU 7972  OE2 GLU F  27     6700   7810  11256   1555   -181    -72       O  
ATOM   7973  N   ALA F  28     121.386 -87.653  31.854  1.00 67.06           N  
ANISOU 7973  N   ALA F  28     6524   7811  11144   1644      0    -61       N  
ATOM   7974  CA  ALA F  28     120.276 -86.754  32.109  1.00 65.86           C  
ANISOU 7974  CA  ALA F  28     6345   7684  10993   1642     59     -7       C  
ATOM   7975  C   ALA F  28     120.018 -85.828  30.922  1.00 66.33           C  
ANISOU 7975  C   ALA F  28     6364   7785  11054   1663     90     -2       C  
ATOM   7976  O   ALA F  28     118.893 -85.753  30.429  1.00 66.70           O  
ANISOU 7976  O   ALA F  28     6376   7858  11108   1653    101     38       O  
ATOM   7977  CB  ALA F  28     120.533 -85.954  33.363  1.00 64.10           C  
ANISOU 7977  CB  ALA F  28     6146   7447  10762   1651    109      1       C  
ATOM   7978  N   LEU F  29     121.046 -85.128  30.458  1.00 67.14           N  
ANISOU 7978  N   LEU F  29     6469   7893  11150   1692    104    -41       N  
ATOM   7979  CA  LEU F  29     120.897 -84.250  29.299  1.00 66.53           C  
ANISOU 7979  CA  LEU F  29     6353   7854  11072   1713    131    -39       C  
ATOM   7980  C   LEU F  29     120.386 -85.006  28.106  1.00 68.22           C  
ANISOU 7980  C   LEU F  29     6539   8085  11295   1702     87    -37       C  
ATOM   7981  O   LEU F  29     119.550 -84.519  27.372  1.00 68.69           O  
ANISOU 7981  O   LEU F  29     6561   8178  11359   1704    110     -8       O  
ATOM   7982  CB  LEU F  29     122.217 -83.599  28.908  1.00 66.63           C  
ANISOU 7982  CB  LEU F  29     6377   7865  11076   1744    140    -90       C  
ATOM   7983  CG  LEU F  29     122.889 -82.589  29.816  1.00 64.94           C  
ANISOU 7983  CG  LEU F  29     6184   7640  10852   1764    190    -99       C  
ATOM   7984  CD1 LEU F  29     124.375 -82.749  29.618  1.00 65.92           C  
ANISOU 7984  CD1 LEU F  29     6334   7743  10968   1783    162   -160       C  
ATOM   7985  CD2 LEU F  29     122.429 -81.166  29.473  1.00 64.26           C  
ANISOU 7985  CD2 LEU F  29     6065   7588  10763   1785    257    -72       C  
ATOM   7986  N   GLU F  30     120.911 -86.198  27.898  1.00 69.92           N  
ANISOU 7986  N   GLU F  30     6774   8279  11514   1690     23    -70       N  
ATOM   7987  CA  GLU F  30     120.534 -86.953  26.718  1.00 72.06           C  
ANISOU 7987  CA  GLU F  30     7021   8567  11793   1681    -23    -73       C  
ATOM   7988  C   GLU F  30     119.041 -87.174  26.673  1.00 72.26           C  
ANISOU 7988  C   GLU F  30     7017   8610  11827   1657    -15    -17       C  
ATOM   7989  O   GLU F  30     118.416 -86.928  25.649  1.00 73.38           O  
ANISOU 7989  O   GLU F  30     7122   8784  11975   1661    -10     -1       O  
ATOM   7990  CB  GLU F  30     121.236 -88.298  26.668  1.00 73.27           C  
ANISOU 7990  CB  GLU F  30     7201   8689  11948   1667    -94   -113       C  
ATOM   7991  CG  GLU F  30     120.676 -89.166  25.575  1.00 76.30           C  
ANISOU 7991  CG  GLU F  30     7560   9089  12342   1653   -142   -109       C  
ATOM   7992  CD  GLU F  30     121.621 -90.270  25.194  1.00 77.93           C  
ANISOU 7992  CD  GLU F  30     7788   9272  12548   1650   -210   -159       C  
ATOM   7993  OE1 GLU F  30     121.581 -90.669  24.002  1.00 81.00           O  
ANISOU 7993  OE1 GLU F  30     8156   9679  12943   1651   -243   -174       O  
ATOM   7994  OE2 GLU F  30     122.395 -90.729  26.082  1.00 76.31           O  
ANISOU 7994  OE2 GLU F  30     7623   9031  12339   1646   -229   -185       O  
ATOM   7995  N   ARG F  31     118.491 -87.646  27.793  1.00 70.29           N  
ANISOU 7995  N   ARG F  31     6786   8340  11581   1634    -16     12       N  
ATOM   7996  CA  ARG F  31     117.060 -87.850  27.964  1.00 70.31           C  
ANISOU 7996  CA  ARG F  31     6766   8356  11593   1610     -6     68       C  
ATOM   7997  C   ARG F  31     116.284 -86.600  27.573  1.00 69.56           C  
ANISOU 7997  C   ARG F  31     6634   8299  11498   1624     56    104       C  
ATOM   7998  O   ARG F  31     115.275 -86.687  26.863  1.00 70.71           O  
ANISOU 7998  O   ARG F  31     6744   8471  11652   1614     55    135       O  
ATOM   7999  CB  ARG F  31     116.737 -88.208  29.412  1.00 68.90           C  
ANISOU 7999  CB  ARG F  31     6616   8148  11413   1589      1     92       C  
ATOM   8000  CG  ARG F  31     117.372 -89.462  29.928  1.00 69.64           C  
ANISOU 8000  CG  ARG F  31     6748   8204  11508   1572    -59     62       C  
ATOM   8001  CD  ARG F  31     116.724 -89.867  31.251  1.00 68.85           C  
ANISOU 8001  CD  ARG F  31     6669   8081  11410   1547    -52     98       C  
ATOM   8002  NE  ARG F  31     117.313 -91.074  31.828  1.00 69.42           N  
ANISOU 8002  NE  ARG F  31     6780   8115  11483   1530   -107     71       N  
ATOM   8003  CZ  ARG F  31     117.156 -92.305  31.349  1.00 71.55           C  
ANISOU 8003  CZ  ARG F  31     7049   8376  11761   1510   -169     62       C  
ATOM   8004  NH1 ARG F  31     117.748 -93.311  31.959  1.00 72.04           N  
ANISOU 8004  NH1 ARG F  31     7148   8401  11822   1496   -215     37       N  
ATOM   8005  NH2 ARG F  31     116.419 -92.533  30.268  1.00 73.36           N  
ANISOU 8005  NH2 ARG F  31     7242   8633  11999   1504   -185     78       N  
ATOM   8006  N   MET F  32     116.770 -85.449  28.043  1.00 72.86           N  
ANISOU 8006  N   MET F  32     7058   8718  11906   1647    110     99       N  
ATOM   8007  CA  MET F  32     116.108 -84.170  27.815  1.00 72.27           C  
ANISOU 8007  CA  MET F  32     6951   8678  11831   1661    174    133       C  
ATOM   8008  C   MET F  32     116.003 -83.848  26.330  1.00 74.10           C  
ANISOU 8008  C   MET F  32     7145   8944  12064   1676    170    125       C  
ATOM   8009  O   MET F  32     114.943 -83.426  25.861  1.00 74.57           O  
ANISOU 8009  O   MET F  32     7169   9034  12130   1673    196    165       O  
ATOM   8010  CB  MET F  32     116.837 -83.033  28.544  1.00 70.35           C  
ANISOU 8010  CB  MET F  32     6726   8428  11576   1685    227    122       C  
ATOM   8011  CG  MET F  32     116.346 -81.648  28.132  1.00 69.70           C  
ANISOU 8011  CG  MET F  32     6610   8382  11492   1706    291    148       C  
ATOM   8012  SD  MET F  32     116.746 -80.297  29.275  1.00 68.06           S  
ANISOU 8012  SD  MET F  32     6419   8167  11272   1726    363    155       S  
ATOM   8013  CE  MET F  32     118.325 -79.723  28.681  1.00 68.93           C  
ANISOU 8013  CE  MET F  32     6542   8275  11373   1761    363     92       C  
ATOM   8014  N   PHE F  33     117.092 -84.046  25.590  1.00 71.31           N  
ANISOU 8014  N   PHE F  33     6800   8586  11707   1693    138     74       N  
ATOM   8015  CA  PHE F  33     117.082 -83.753  24.162  1.00 73.41           C  
ANISOU 8015  CA  PHE F  33     7033   8885  11976   1708    133     63       C  
ATOM   8016  C   PHE F  33     116.220 -84.772  23.418  1.00 76.27           C  
ANISOU 8016  C   PHE F  33     7372   9257  12349   1685     87     80       C  
ATOM   8017  O   PHE F  33     115.665 -84.475  22.362  1.00 78.28           O  
ANISOU 8017  O   PHE F  33     7590   9545  12608   1691     93     93       O  
ATOM   8018  CB  PHE F  33     118.500 -83.737  23.591  1.00 74.36           C  
ANISOU 8018  CB  PHE F  33     7168   8996  12088   1731    110      2       C  
ATOM   8019  CG  PHE F  33     119.413 -82.728  24.240  1.00 72.67           C  
ANISOU 8019  CG  PHE F  33     6976   8772  11863   1756    154    -18       C  
ATOM   8020  CD1 PHE F  33     119.120 -81.378  24.200  1.00 72.25           C  
ANISOU 8020  CD1 PHE F  33     6901   8745  11806   1775    220      4       C  
ATOM   8021  CD2 PHE F  33     120.582 -83.131  24.871  1.00 71.93           C  
ANISOU 8021  CD2 PHE F  33     6923   8643  11763   1759    130    -61       C  
ATOM   8022  CE1 PHE F  33     119.978 -80.444  24.794  1.00 71.11           C  
ANISOU 8022  CE1 PHE F  33     6777   8591  11652   1798    260    -16       C  
ATOM   8023  CE2 PHE F  33     121.436 -82.206  25.468  1.00 70.77           C  
ANISOU 8023  CE2 PHE F  33     6796   8487  11606   1782    170    -81       C  
ATOM   8024  CZ  PHE F  33     121.136 -80.864  25.426  1.00 70.40           C  
ANISOU 8024  CZ  PHE F  33     6727   8466  11556   1801    235    -58       C  
ATOM   8025  N   LEU F  34     116.120 -85.976  23.967  1.00 72.93           N  
ANISOU 8025  N   LEU F  34     6972   8807  11932   1659     39     79       N  
ATOM   8026  CA  LEU F  34     115.312 -87.032  23.359  1.00 75.75           C  
ANISOU 8026  CA  LEU F  34     7311   9170  12299   1635     -8     95       C  
ATOM   8027  C   LEU F  34     113.850 -86.900  23.714  1.00 75.12           C  
ANISOU 8027  C   LEU F  34     7208   9106  12228   1615     20    157       C  
ATOM   8028  O   LEU F  34     112.968 -87.105  22.876  1.00 77.33           O  
ANISOU 8028  O   LEU F  34     7455   9411  12517   1606     10    180       O  
ATOM   8029  CB  LEU F  34     115.808 -88.404  23.790  1.00 76.59           C  
ANISOU 8029  CB  LEU F  34     7452   9240  12409   1615    -72     69       C  
ATOM   8030  CG  LEU F  34     116.858 -89.066  22.901  1.00 78.74           C  
ANISOU 8030  CG  LEU F  34     7733   9504  12679   1624   -126     13       C  
ATOM   8031  CD1 LEU F  34     118.197 -88.300  22.862  1.00 77.06           C  
ANISOU 8031  CD1 LEU F  34     7538   9285  12455   1655   -107    -32       C  
ATOM   8032  CD2 LEU F  34     117.065 -90.486  23.390  1.00 79.99           C  
ANISOU 8032  CD2 LEU F  34     7922   9629  12843   1599   -188     -2       C  
ATOM   8033  N   SER F  35     113.597 -86.579  24.976  1.00 76.54           N  
ANISOU 8033  N   SER F  35     7407   9271  12405   1608     55    182       N  
ATOM   8034  CA  SER F  35     112.227 -86.440  25.443  1.00 75.78           C  
ANISOU 8034  CA  SER F  35     7290   9187  12316   1589     84    241       C  
ATOM   8035  C   SER F  35     111.633 -85.112  24.981  1.00 75.21           C  
ANISOU 8035  C   SER F  35     7182   9152  12242   1607    146    270       C  
ATOM   8036  O   SER F  35     110.539 -85.087  24.428  1.00 76.31           O  
ANISOU 8036  O   SER F  35     7287   9318  12391   1597    152    306       O  
ATOM   8037  CB  SER F  35     112.165 -86.580  26.970  1.00 73.31           C  
ANISOU 8037  CB  SER F  35     7011   8844  12000   1574     99    257       C  
ATOM   8038  OG  SER F  35     112.724 -87.833  27.394  1.00 73.78           O  
ANISOU 8038  OG  SER F  35     7105   8867  12061   1556     40    230       O  
ATOM   8039  N   PHE F  36     112.362 -84.018  25.167  1.00 68.93           N  
ANISOU 8039  N   PHE F  36     8237  10620   7332   2002   1415   2203       N  
ATOM   8040  CA  PHE F  36     111.833 -82.685  24.857  1.00 68.91           C  
ANISOU 8040  CA  PHE F  36     8259  10606   7316   1985   1408   2205       C  
ATOM   8041  C   PHE F  36     112.691 -81.937  23.843  1.00 69.03           C  
ANISOU 8041  C   PHE F  36     8284  10641   7305   1968   1411   2204       C  
ATOM   8042  O   PHE F  36     113.475 -81.072  24.217  1.00 69.07           O  
ANISOU 8042  O   PHE F  36     8290  10662   7292   1949   1415   2211       O  
ATOM   8043  CB  PHE F  36     111.714 -81.872  26.140  1.00 68.82           C  
ANISOU 8043  CB  PHE F  36     8252  10592   7306   1974   1406   2217       C  
ATOM   8044  CG  PHE F  36     111.205 -82.673  27.310  1.00 68.71           C  
ANISOU 8044  CG  PHE F  36     8224  10567   7317   1990   1406   2220       C  
ATOM   8045  CD1 PHE F  36     112.074 -83.142  28.280  1.00 68.72           C  
ANISOU 8045  CD1 PHE F  36     8203  10585   7322   1991   1414   2226       C  
ATOM   8046  CD2 PHE F  36     109.869 -82.980  27.426  1.00 68.61           C  
ANISOU 8046  CD2 PHE F  36     8218  10525   7324   2004   1397   2217       C  
ATOM   8047  CE1 PHE F  36     111.614 -83.872  29.358  1.00 68.62           C  
ANISOU 8047  CE1 PHE F  36     8178  10562   7332   2006   1413   2229       C  
ATOM   8048  CE2 PHE F  36     109.415 -83.700  28.488  1.00 68.51           C  
ANISOU 8048  CE2 PHE F  36     8193  10502   7334   2018   1396   2220       C  
ATOM   8049  CZ  PHE F  36     110.294 -84.151  29.456  1.00 68.51           C  
ANISOU 8049  CZ  PHE F  36     8173  10521   7338   2019   1405   2226       C  
ATOM   8050  N   PRO F  37     112.513 -82.247  22.547  1.00 70.53           N  
ANISOU 8050  N   PRO F  37     8481  10828   7491   1974   1409   2194       N  
ATOM   8051  CA  PRO F  37     113.370 -81.802  21.442  1.00 70.71           C  
ANISOU 8051  CA  PRO F  37     8508  10869   7489   1961   1414   2190       C  
ATOM   8052  C   PRO F  37     113.543 -80.300  21.358  1.00 70.68           C  
ANISOU 8052  C   PRO F  37     8523  10869   7463   1937   1411   2196       C  
ATOM   8053  O   PRO F  37     114.452 -79.826  20.667  1.00 70.81           O  
ANISOU 8053  O   PRO F  37     8542  10904   7457   1923   1416   2195       O  
ATOM   8054  CB  PRO F  37     112.637 -82.314  20.197  1.00 70.94           C  
ANISOU 8054  CB  PRO F  37     8546  10884   7524   1973   1408   2178       C  
ATOM   8055  CG  PRO F  37     111.271 -82.593  20.643  1.00 70.63           C  
ANISOU 8055  CG  PRO F  37     8513  10816   7508   1987   1399   2177       C  
ATOM   8056  CD  PRO F  37     111.401 -83.065  22.052  1.00 70.52           C  
ANISOU 8056  CD  PRO F  37     8481  10803   7509   1994   1403   2184       C  
ATOM   8057  N   THR F  38     112.668 -79.556  22.025  1.00 72.20           N  
ANISOU 8057  N   THR F  38     8729  11042   7660   1931   1404   2202       N  
ATOM   8058  CA  THR F  38     112.738 -78.100  21.990  1.00 72.28           C  
ANISOU 8058  CA  THR F  38     8759  11054   7651   1909   1401   2208       C  
ATOM   8059  C   THR F  38     113.967 -77.580  22.759  1.00 71.34           C  
ANISOU 8059  C   THR F  38     8630  10960   7517   1892   1410   2217       C  
ATOM   8060  O   THR F  38     114.493 -76.517  22.453  1.00 72.67           O  
ANISOU 8060  O   THR F  38     8809  11139   7663   1873   1411   2221       O  
ATOM   8061  CB  THR F  38     111.466 -77.470  22.568  1.00 70.98           C  
ANISOU 8061  CB  THR F  38     8610  10862   7496   1908   1391   2211       C  
ATOM   8062  OG1 THR F  38     111.748 -76.989  23.888  1.00 68.52           O  
ANISOU 8062  OG1 THR F  38     8294  10555   7186   1899   1393   2222       O  
ATOM   8063  CG2 THR F  38     110.321 -78.490  22.616  1.00 71.91           C  
ANISOU 8063  CG2 THR F  38     8726  10956   7642   1931   1385   2205       C  
ATOM   8064  N   THR F  39     114.441 -78.336  23.740  1.00 72.47           N  
ANISOU 8064  N   THR F  39     8752  11113   7672   1901   1416   2222       N  
ATOM   8065  CA  THR F  39     115.600 -77.896  24.509  1.00 71.84           C  
ANISOU 8065  CA  THR F  39     8661  11056   7579   1887   1424   2231       C  
ATOM   8066  C   THR F  39     116.875 -77.894  23.680  1.00 73.78           C  
ANISOU 8066  C   THR F  39     8900  11330   7803   1878   1432   2228       C  
ATOM   8067  O   THR F  39     117.880 -77.337  24.105  1.00 73.77           O  
ANISOU 8067  O   THR F  39     8894  11349   7786   1862   1439   2235       O  
ATOM   8068  CB  THR F  39     115.849 -78.772  25.749  1.00 69.56           C  
ANISOU 8068  CB  THR F  39     8349  10772   7308   1898   1429   2236       C  
ATOM   8069  OG1 THR F  39     116.213 -80.095  25.345  1.00 69.99           O  
ANISOU 8069  OG1 THR F  39     8385  10835   7372   1916   1434   2228       O  
ATOM   8070  CG2 THR F  39     114.601 -78.852  26.590  1.00 68.19           C  
ANISOU 8070  CG2 THR F  39     8181  10572   7156   1908   1421   2238       C  
ATOM   8071  N   LYS F  40     116.833 -78.515  22.503  1.00 70.47           N  
ANISOU 8071  N   LYS F  40     8481  10910   7384   1887   1432   2218       N  
ATOM   8072  CA  LYS F  40     117.999 -78.561  21.632  1.00 72.86           C  
ANISOU 8072  CA  LYS F  40     8778  11238   7667   1880   1440   2214       C  
ATOM   8073  C   LYS F  40     118.326 -77.178  21.033  1.00 74.89           C  
ANISOU 8073  C   LYS F  40     9055  11502   7898   1856   1439   2217       C  
ATOM   8074  O   LYS F  40     119.467 -76.910  20.637  1.00 76.34           O  
ANISOU 8074  O   LYS F  40     9234  11710   8062   1845   1446   2218       O  
ATOM   8075  CB  LYS F  40     117.782 -79.591  20.519  1.00 75.09           C  
ANISOU 8075  CB  LYS F  40     9056  11516   7957   1897   1440   2202       C  
ATOM   8076  CG  LYS F  40     117.335 -80.958  21.024  1.00 73.54           C  
ANISOU 8076  CG  LYS F  40     8843  11311   7788   1921   1440   2199       C  
ATOM   8077  CD  LYS F  40     117.637 -82.065  20.020  1.00 76.13           C  
ANISOU 8077  CD  LYS F  40     9160  11646   8119   1936   1444   2189       C  
ATOM   8078  CE  LYS F  40     117.254 -81.679  18.590  1.00 79.32           C  
ANISOU 8078  CE  LYS F  40     9583  12043   8511   1932   1439   2180       C  
ATOM   8079  NZ  LYS F  40     117.749 -82.684  17.590  1.00 82.07           N  
ANISOU 8079  NZ  LYS F  40     9920  12403   8860   1944   1444   2170       N  
ATOM   8080  N   THR F  41     117.335 -76.289  20.994  1.00 74.01           N  
ANISOU 8080  N   THR F  41     8966  11370   7786   1850   1430   2218       N  
ATOM   8081  CA  THR F  41     117.514 -74.979  20.363  1.00 76.21           C  
ANISOU 8081  CA  THR F  41     9263  11652   8040   1828   1428   2220       C  
ATOM   8082  C   THR F  41     118.415 -74.054  21.177  1.00 75.37           C  
ANISOU 8082  C   THR F  41     9156  11564   7918   1808   1433   2231       C  
ATOM   8083  O   THR F  41     118.708 -72.930  20.762  1.00 77.39           O  
ANISOU 8083  O   THR F  41     9427  11826   8153   1789   1432   2234       O  
ATOM   8084  CB  THR F  41     116.172 -74.266  20.135  1.00 76.18           C  
ANISOU 8084  CB  THR F  41     9284  11620   8040   1827   1416   2219       C  
ATOM   8085  OG1 THR F  41     115.758 -73.630  21.349  1.00 73.25           O  
ANISOU 8085  OG1 THR F  41     8917  11239   7675   1820   1413   2228       O  
ATOM   8086  CG2 THR F  41     115.113 -75.256  19.684  1.00 76.55           C  
ANISOU 8086  CG2 THR F  41     9331  11645   8109   1849   1410   2210       C  
ATOM   8087  N   TYR F  42     118.808 -74.507  22.357  1.00 73.52           N  
ANISOU 8087  N   TYR F  42     8903  11337   7694   1813   1438   2237       N  
ATOM   8088  CA  TYR F  42     119.763 -73.763  23.148  1.00 73.55           C  
ANISOU 8088  CA  TYR F  42     8902  11360   7683   1795   1444   2248       C  
ATOM   8089  C   TYR F  42     121.211 -74.208  22.871  1.00 73.67           C  
ANISOU 8089  C   TYR F  42     8900  11407   7686   1792   1455   2247       C  
ATOM   8090  O   TYR F  42     122.166 -73.499  23.217  1.00 73.73           O  
ANISOU 8090  O   TYR F  42     8905  11433   7675   1774   1461   2254       O  
ATOM   8091  CB  TYR F  42     119.405 -73.903  24.624  1.00 73.43           C  
ANISOU 8091  CB  TYR F  42     8879  11337   7685   1800   1443   2256       C  
ATOM   8092  CG  TYR F  42     118.235 -73.040  25.012  1.00 73.32           C  
ANISOU 8092  CG  TYR F  42     8885  11298   7676   1794   1433   2259       C  
ATOM   8093  CD1 TYR F  42     118.404 -71.939  25.831  1.00 73.29           C  
ANISOU 8093  CD1 TYR F  42     8888  11296   7662   1777   1433   2270       C  
ATOM   8094  CD2 TYR F  42     116.966 -73.302  24.531  1.00 73.25           C  
ANISOU 8094  CD2 TYR F  42     8888  11263   7682   1807   1424   2253       C  
ATOM   8095  CE1 TYR F  42     117.342 -71.120  26.168  1.00 73.19           C  
ANISOU 8095  CE1 TYR F  42     8894  11261   7653   1771   1423   2273       C  
ATOM   8096  CE2 TYR F  42     115.881 -72.493  24.875  1.00 73.15           C  
ANISOU 8096  CE2 TYR F  42     8894  11227   7673   1802   1414   2256       C  
ATOM   8097  CZ  TYR F  42     116.079 -71.402  25.699  1.00 73.12           C  
ANISOU 8097  CZ  TYR F  42     8897  11226   7659   1784   1414   2266       C  
ATOM   8098  OH  TYR F  42     115.013 -70.596  26.056  1.00 73.02           O  
ANISOU 8098  OH  TYR F  42     8902  11191   7650   1779   1405   2270       O  
ATOM   8099  N   PHE F  43     121.351 -75.346  22.189  1.00 75.52           N  
ANISOU 8099  N   PHE F  43     9123  11645   7928   1808   1458   2238       N  
ATOM   8100  CA  PHE F  43     122.654 -75.960  21.935  1.00 75.80           C  
ANISOU 8100  CA  PHE F  43     9138  11707   7954   1809   1469   2236       C  
ATOM   8101  C   PHE F  43     122.896 -76.205  20.456  1.00 76.03           C  
ANISOU 8101  C   PHE F  43     9173  11743   7973   1810   1470   2226       C  
ATOM   8102  O   PHE F  43     123.047 -77.351  20.029  1.00 76.11           O  
ANISOU 8102  O   PHE F  43     9169  11756   7993   1827   1473   2219       O  
ATOM   8103  CB  PHE F  43     122.773 -77.288  22.675  1.00 75.71           C  
ANISOU 8103  CB  PHE F  43     9104  11699   7965   1828   1473   2236       C  
ATOM   8104  CG  PHE F  43     122.710 -77.158  24.153  1.00 75.51           C  
ANISOU 8104  CG  PHE F  43     9071  11671   7950   1827   1474   2246       C  
ATOM   8105  CD1 PHE F  43     121.501 -77.174  24.805  1.00 75.20           C  
ANISOU 8105  CD1 PHE F  43     9038  11606   7930   1836   1466   2248       C  
ATOM   8106  CD2 PHE F  43     123.862 -77.025  24.897  1.00 75.63           C  
ANISOU 8106  CD2 PHE F  43     9071  11710   7956   1817   1483   2253       C  
ATOM   8107  CE1 PHE F  43     121.437 -77.056  26.173  1.00 75.02           C  
ANISOU 8107  CE1 PHE F  43     9007  11580   7916   1834   1466   2257       C  
ATOM   8108  CE2 PHE F  43     123.805 -76.909  26.268  1.00 75.45           C  
ANISOU 8108  CE2 PHE F  43     9040  11685   7942   1816   1483   2263       C  
ATOM   8109  CZ  PHE F  43     122.586 -76.923  26.905  1.00 75.14           C  
ANISOU 8109  CZ  PHE F  43     9008  11619   7922   1825   1475   2264       C  
ATOM   8110  N   PRO F  44     122.952 -75.130  19.670  1.00 80.55           N  
ANISOU 8110  N   PRO F  44     9764  12316   8524   1793   1467   2226       N  
ATOM   8111  CA  PRO F  44     122.957 -75.302  18.218  1.00 82.57           C  
ANISOU 8111  CA  PRO F  44    10027  12573   8771   1796   1466   2216       C  
ATOM   8112  C   PRO F  44     124.149 -76.094  17.729  1.00 84.63           C  
ANISOU 8112  C   PRO F  44    10271  12860   9026   1800   1476   2212       C  
ATOM   8113  O   PRO F  44     123.966 -77.065  16.995  1.00 86.10           O  
ANISOU 8113  O   PRO F  44    10451  13043   9221   1816   1476   2203       O  
ATOM   8114  CB  PRO F  44     123.024 -73.869  17.690  1.00 84.97           C  
ANISOU 8114  CB  PRO F  44    10354  12878   9051   1773   1463   2218       C  
ATOM   8115  CG  PRO F  44     122.657 -73.001  18.853  1.00 82.35           C  
ANISOU 8115  CG  PRO F  44    10029  12538   8721   1763   1460   2229       C  
ATOM   8116  CD  PRO F  44     123.113 -73.725  20.064  1.00 80.54           C  
ANISOU 8116  CD  PRO F  44     9777  12318   8506   1771   1466   2235       C  
ATOM   8117  N   HIS F  45     125.345 -75.724  18.183  1.00 86.99           N  
ANISOU 8117  N   HIS F  45    10559  13183   9309   1786   1485   2219       N  
ATOM   8118  CA  HIS F  45     126.585 -76.188  17.549  1.00 89.39           C  
ANISOU 8118  CA  HIS F  45    10850  13514   9601   1785   1494   2215       C  
ATOM   8119  C   HIS F  45     127.076 -77.489  18.149  1.00 87.63           C  
ANISOU 8119  C   HIS F  45    10601  13301   9394   1801   1501   2214       C  
ATOM   8120  O   HIS F  45     128.037 -78.089  17.659  1.00 89.71           O  
ANISOU 8120  O   HIS F  45    10850  13586   9650   1804   1509   2211       O  
ATOM   8121  CB  HIS F  45     127.688 -75.131  17.660  1.00 90.47           C  
ANISOU 8121  CB  HIS F  45    10990  13674   9712   1761   1500   2222       C  
ATOM   8122  CG  HIS F  45     127.311 -73.796  17.091  1.00 92.62           C  
ANISOU 8122  CG  HIS F  45    11287  13938   9967   1743   1494   2223       C  
ATOM   8123  ND1 HIS F  45     126.017 -73.466  16.744  1.00 96.06           N  
ANISOU 8123  ND1 HIS F  45    11742  14347  10410   1747   1483   2220       N  
ATOM   8124  CD2 HIS F  45     128.063 -72.704  16.808  1.00 92.05           C  
ANISOU 8124  CD2 HIS F  45    11224  13881   9869   1721   1497   2228       C  
ATOM   8125  CE1 HIS F  45     125.985 -72.230  16.277  1.00 97.52           C  
ANISOU 8125  CE1 HIS F  45    11947  14531  10575   1728   1480   2222       C  
ATOM   8126  NE2 HIS F  45     127.214 -71.745  16.305  1.00 95.14           N  
ANISOU 8126  NE2 HIS F  45    11640  14255  10254   1712   1488   2227       N  
ATOM   8127  N   PHE F  46     126.422 -77.919  19.219  1.00 86.69           N  
ANISOU 8127  N   PHE F  46    10475  13169   9296   1812   1498   2218       N  
ATOM   8128  CA  PHE F  46     126.789 -79.170  19.852  1.00 84.95           C  
ANISOU 8128  CA  PHE F  46    10230  12956   9093   1829   1504   2218       C  
ATOM   8129  C   PHE F  46     126.381 -80.316  18.954  1.00 86.23           C  
ANISOU 8129  C   PHE F  46    10386  13109   9267   1849   1503   2207       C  
ATOM   8130  O   PHE F  46     125.336 -80.275  18.292  1.00 86.51           O  
ANISOU 8130  O   PHE F  46    10437  13123   9309   1856   1494   2200       O  
ATOM   8131  CB  PHE F  46     126.131 -79.332  21.227  1.00 81.35           C  
ANISOU 8131  CB  PHE F  46     9768  12484   8656   1836   1501   2225       C  
ATOM   8132  CG  PHE F  46     126.708 -78.444  22.298  1.00 80.69           C  
ANISOU 8132  CG  PHE F  46     9683  12412   8562   1819   1504   2236       C  
ATOM   8133  CD1 PHE F  46     126.672 -78.837  23.624  1.00 80.51           C  
ANISOU 8133  CD1 PHE F  46     9646  12388   8555   1826   1506   2243       C  
ATOM   8134  CD2 PHE F  46     127.265 -77.214  21.987  1.00 81.70           C  
ANISOU 8134  CD2 PHE F  46     9825  12552   8666   1797   1505   2241       C  
ATOM   8135  CE1 PHE F  46     127.186 -78.031  24.618  1.00 80.48           C  
ANISOU 8135  CE1 PHE F  46     9641  12394   8543   1810   1509   2254       C  
ATOM   8136  CE2 PHE F  46     127.778 -76.402  22.978  1.00 80.80           C  
ANISOU 8136  CE2 PHE F  46     9710  12448   8544   1781   1508   2251       C  
ATOM   8137  CZ  PHE F  46     127.740 -76.812  24.297  1.00 80.63           C  
ANISOU 8137  CZ  PHE F  46     9674  12425   8537   1788   1510   2258       C  
ATOM   8138  N   ASP F  47     127.207 -81.350  18.953  1.00 85.73           N  
ANISOU 8138  N   ASP F  47    10301  13063   9208   1860   1511   2204       N  
ATOM   8139  CA  ASP F  47     126.802 -82.620  18.400  1.00 86.49           C  
ANISOU 8139  CA  ASP F  47    10388  13152   9321   1882   1510   2194       C  
ATOM   8140  C   ASP F  47     125.918 -83.231  19.468  1.00 84.61           C  
ANISOU 8140  C   ASP F  47    10143  12895   9109   1897   1506   2197       C  
ATOM   8141  O   ASP F  47     126.373 -83.460  20.587  1.00 84.56           O  
ANISOU 8141  O   ASP F  47    10122  12898   9110   1898   1511   2204       O  
ATOM   8142  CB  ASP F  47     128.012 -83.500  18.106  1.00 88.91           C  
ANISOU 8142  CB  ASP F  47    10674  13484   9623   1887   1521   2191       C  
ATOM   8143  CG  ASP F  47     127.626 -84.854  17.600  1.00 87.21           C  
ANISOU 8143  CG  ASP F  47    10447  13262   9427   1910   1520   2182       C  
ATOM   8144  OD1 ASP F  47     126.840 -84.928  16.631  1.00 86.23           O  
ANISOU 8144  OD1 ASP F  47    10337  13122   9305   1916   1514   2174       O  
ATOM   8145  OD2 ASP F  47     128.095 -85.846  18.184  1.00 87.27           O  
ANISOU 8145  OD2 ASP F  47    10433  13279   9446   1922   1526   2182       O  
ATOM   8146  N   LEU F  48     124.649 -83.449  19.148  1.00 82.98           N  
ANISOU 8146  N   LEU F  48     9948  12662   8918   1909   1497   2192       N  
ATOM   8147  CA  LEU F  48     123.690 -83.880  20.157  1.00 82.67           C  
ANISOU 8147  CA  LEU F  48     9905  12602   8903   1922   1492   2194       C  
ATOM   8148  C   LEU F  48     123.441 -85.387  20.164  1.00 82.62           C  
ANISOU 8148  C   LEU F  48     9881  12590   8919   1947   1494   2188       C  
ATOM   8149  O   LEU F  48     122.630 -85.893  20.942  1.00 82.36           O  
ANISOU 8149  O   LEU F  48     9844  12540   8908   1961   1490   2189       O  
ATOM   8150  CB  LEU F  48     122.382 -83.114  19.972  1.00 82.45           C  
ANISOU 8150  CB  LEU F  48     9902  12547   8879   1920   1481   2194       C  
ATOM   8151  CG  LEU F  48     122.503 -81.717  20.585  1.00 82.40           C  
ANISOU 8151  CG  LEU F  48     9908  12542   8857   1897   1479   2204       C  
ATOM   8152  CD1 LEU F  48     121.188 -80.965  20.553  1.00 82.17           C  
ANISOU 8152  CD1 LEU F  48     9902  12485   8832   1895   1468   2204       C  
ATOM   8153  CD2 LEU F  48     123.015 -81.816  22.014  1.00 82.31           C  
ANISOU 8153  CD2 LEU F  48     9881  12541   8852   1896   1484   2214       C  
ATOM   8154  N   SER F  49     124.176 -86.102  19.324  1.00 83.98           N  
ANISOU 8154  N   SER F  49    10043  12779   9086   1953   1500   2181       N  
ATOM   8155  CA  SER F  49     123.938 -87.523  19.106  1.00 84.77           C  
ANISOU 8155  CA  SER F  49    10128  12875   9207   1976   1501   2173       C  
ATOM   8156  C   SER F  49     124.296 -88.357  20.329  1.00 82.71           C  
ANISOU 8156  C   SER F  49     9844  12621   8962   1987   1507   2178       C  
ATOM   8157  O   SER F  49     124.625 -87.818  21.390  1.00 80.97           O  
ANISOU 8157  O   SER F  49     9620  12407   8738   1977   1509   2188       O  
ATOM   8158  CB  SER F  49     124.734 -87.994  17.896  1.00 88.50           C  
ANISOU 8158  CB  SER F  49    10595  13365   9667   1978   1507   2165       C  
ATOM   8159  OG  SER F  49     126.030 -87.419  17.919  1.00 89.69           O  
ANISOU 8159  OG  SER F  49    10740  13543   9795   1960   1515   2170       O  
ATOM   8160  N   HIS F  50     124.191 -89.673  20.193  1.00 85.63           N  
ANISOU 8160  N   HIS F  50    10199  12989   9349   2008   1509   2172       N  
ATOM   8161  CA  HIS F  50     124.402 -90.549  21.335  1.00 83.68           C  
ANISOU 8161  CA  HIS F  50     9929  12745   9119   2020   1513   2176       C  
ATOM   8162  C   HIS F  50     125.864 -90.541  21.795  1.00 83.34           C  
ANISOU 8162  C   HIS F  50     9870  12733   9064   2010   1524   2182       C  
ATOM   8163  O   HIS F  50     126.785 -90.719  20.994  1.00 85.66           O  
ANISOU 8163  O   HIS F  50    10158  13047   9343   2006   1530   2178       O  
ATOM   8164  CB  HIS F  50     123.948 -91.975  21.010  1.00 84.78           C  
ANISOU 8164  CB  HIS F  50    10056  12875   9280   2045   1513   2167       C  
ATOM   8165  CG  HIS F  50     123.930 -92.883  22.201  1.00 82.72           C  
ANISOU 8165  CG  HIS F  50     9775  12613   9040   2059   1516   2171       C  
ATOM   8166  ND1 HIS F  50     124.272 -92.459  23.471  1.00 81.77           N  
ANISOU 8166  ND1 HIS F  50     9649  12500   8921   2051   1519   2182       N  
ATOM   8167  CD2 HIS F  50     123.616 -94.196  22.319  1.00 83.24           C  
ANISOU 8167  CD2 HIS F  50     9825  12673   9128   2081   1517   2166       C  
ATOM   8168  CE1 HIS F  50     124.171 -93.469  24.316  1.00 81.64           C  
ANISOU 8168  CE1 HIS F  50     9614  12481   8925   2067   1521   2183       C  
ATOM   8169  NE2 HIS F  50     123.776 -94.537  23.642  1.00 81.65           N  
ANISOU 8169  NE2 HIS F  50     9609  12474   8940   2086   1520   2173       N  
ATOM   8170  N   GLY F  51     126.051 -90.302  23.094  1.00 83.31           N  
ANISOU 8170  N   GLY F  51     9858  12733   9064   2005   1526   2192       N  
ATOM   8171  CA  GLY F  51     127.352 -90.359  23.733  1.00 83.49           C  
ANISOU 8171  CA  GLY F  51     9863  12782   9077   1998   1536   2198       C  
ATOM   8172  C   GLY F  51     128.368 -89.431  23.106  1.00 83.74           C  
ANISOU 8172  C   GLY F  51     9902  12835   9080   1976   1541   2200       C  
ATOM   8173  O   GLY F  51     129.582 -89.697  23.141  1.00 83.96           O  
ANISOU 8173  O   GLY F  51     9914  12888   9098   1972   1550   2201       O  
ATOM   8174  N   SER F  52     127.867 -88.350  22.516  1.00 82.33           N  
ANISOU 8174  N   SER F  52     9747  12646   8889   1963   1534   2200       N  
ATOM   8175  CA  SER F  52     128.722 -87.336  21.925  1.00 82.57           C  
ANISOU 8175  CA  SER F  52     9786  12695   8892   1942   1538   2202       C  
ATOM   8176  C   SER F  52     129.661 -86.793  22.980  1.00 82.61           C  
ANISOU 8176  C   SER F  52     9783  12719   8887   1927   1544   2212       C  
ATOM   8177  O   SER F  52     129.219 -86.479  24.084  1.00 82.39           O  
ANISOU 8177  O   SER F  52     9755  12681   8868   1926   1541   2220       O  
ATOM   8178  CB  SER F  52     127.890 -86.205  21.331  1.00 82.49           C  
ANISOU 8178  CB  SER F  52     9803  12668   8872   1930   1529   2201       C  
ATOM   8179  OG  SER F  52     128.713 -85.123  20.916  1.00 83.07           O  
ANISOU 8179  OG  SER F  52     9886  12758   8919   1908   1532   2204       O  
ATOM   8180  N   ALA F  53     130.947 -86.707  22.650  1.00 81.52           N  
ANISOU 8180  N   ALA F  53     5844   9470  15661   1232    311    914       N  
ATOM   8181  CA  ALA F  53     131.938 -86.149  23.565  1.00 82.11           C  
ANISOU 8181  CA  ALA F  53     5916   9501  15780   1251    266    904       C  
ATOM   8182  C   ALA F  53     131.516 -84.774  24.078  1.00 80.91           C  
ANISOU 8182  C   ALA F  53     5775   9302  15665   1269    258    932       C  
ATOM   8183  O   ALA F  53     131.724 -84.441  25.250  1.00 79.81           O  
ANISOU 8183  O   ALA F  53     5659   9109  15558   1309    234    928       O  
ATOM   8184  CB  ALA F  53     133.287 -86.053  22.886  1.00 86.04           C  
ANISOU 8184  CB  ALA F  53     6374  10032  16286   1209    232    888       C  
ATOM   8185  N   GLN F  54     130.912 -83.987  23.189  1.00 83.45           N  
ANISOU 8185  N   GLN F  54     6083   9645  15981   1241    277    960       N  
ATOM   8186  CA  GLN F  54     130.462 -82.637  23.522  1.00 82.99           C  
ANISOU 8186  CA  GLN F  54     6032   9547  15955   1253    271    989       C  
ATOM   8187  C   GLN F  54     129.357 -82.655  24.579  1.00 79.34           C  
ANISOU 8187  C   GLN F  54     5616   9035  15494   1306    294   1000       C  
ATOM   8188  O   GLN F  54     129.434 -81.908  25.563  1.00 78.30           O  
ANISOU 8188  O   GLN F  54     5506   8849  15396   1339    272   1006       O  
ATOM   8189  CB  GLN F  54     129.985 -81.920  22.268  1.00 85.10           C  
ANISOU 8189  CB  GLN F  54     6274   9851  16208   1210    291   1017       C  
ATOM   8190  CG  GLN F  54     130.303 -80.448  22.259  1.00 86.31           C  
ANISOU 8190  CG  GLN F  54     6411   9980  16401   1199    265   1038       C  
ATOM   8191  CD  GLN F  54     130.165 -79.848  20.874  1.00 89.35           C  
ANISOU 8191  CD  GLN F  54     6766  10412  16772   1147    278   1059       C  
ATOM   8192  OE1 GLN F  54     130.151 -80.568  19.870  1.00 90.83           O  
ANISOU 8192  OE1 GLN F  54     6937  10653  16920   1114    297   1051       O  
ATOM   8193  NE2 GLN F  54     130.057 -78.522  20.809  1.00 90.53           N  
ANISOU 8193  NE2 GLN F  54     6906  10540  16951   1140    266   1085       N  
ATOM   8194  N   VAL F  55     128.345 -83.507  24.370  1.00 81.64           N  
ANISOU 8194  N   VAL F  55     5927   9346  15747   1314    336   1002       N  
ATOM   8195  CA  VAL F  55     127.317 -83.781  25.374  1.00 78.28           C  
ANISOU 8195  CA  VAL F  55     5548   8878  15315   1365    360   1007       C  
ATOM   8196  C   VAL F  55     127.911 -84.328  26.674  1.00 76.74           C  
ANISOU 8196  C   VAL F  55     5380   8641  15136   1408    334    981       C  
ATOM   8197  O   VAL F  55     127.556 -83.887  27.770  1.00 74.81           O  
ANISOU 8197  O   VAL F  55     5182   8342  14902   1448    327    985       O  
ATOM   8198  CB  VAL F  55     126.281 -84.799  24.856  1.00 77.20           C  
ANISOU 8198  CB  VAL F  55     5426   8777  15130   1361    407   1009       C  
ATOM   8199  CG1 VAL F  55     125.363 -85.269  25.988  1.00 73.95           C  
ANISOU 8199  CG1 VAL F  55     5065   8323  14711   1415    428   1008       C  
ATOM   8200  CG2 VAL F  55     125.466 -84.209  23.713  1.00 78.38           C  
ANISOU 8200  CG2 VAL F  55     5558   8959  15262   1326    436   1038       C  
ATOM   8201  N   LYS F  56     128.826 -85.287  26.533  1.00 77.97           N  
ANISOU 8201  N   LYS F  56     5520   8824  15281   1395    318    950       N  
ATOM   8202  CA  LYS F  56     129.389 -86.029  27.667  1.00 76.72           C  
ANISOU 8202  CA  LYS F  56     5386   8634  15131   1433    297    922       C  
ATOM   8203  C   LYS F  56     130.192 -85.137  28.591  1.00 77.32           C  
ANISOU 8203  C   LYS F  56     5487   8659  15231   1447    250    915       C  
ATOM   8204  O   LYS F  56     130.174 -85.308  29.814  1.00 75.55           O  
ANISOU 8204  O   LYS F  56     5323   8389  14992   1484    238    901       O  
ATOM   8205  CB  LYS F  56     130.265 -87.180  27.168  1.00 78.23           C  
ANISOU 8205  CB  LYS F  56     5552   8870  15301   1407    288    891       C  
ATOM   8206  CG  LYS F  56     130.791 -88.077  28.275  1.00 77.29           C  
ANISOU 8206  CG  LYS F  56     5458   8723  15184   1445    270    861       C  
ATOM   8207  CD  LYS F  56     131.816 -89.137  27.755  1.00 79.10           C  
ANISOU 8207  CD  LYS F  56     5659   8998  15397   1416    256    830       C  
ATOM   8208  CE  LYS F  56     131.191 -90.115  26.734  1.00 77.52           C  
ANISOU 8208  CE  LYS F  56     5451   8855  15149   1390    297    829       C  
ATOM   8209  NZ  LYS F  56     129.740 -90.459  27.034  1.00 77.93           N  
ANISOU 8209  NZ  LYS F  56     5541   8895  15175   1419    341    843       N  
ATOM   8210  N   GLY F  57     130.910 -84.196  27.992  1.00 74.35           N  
ANISOU 8210  N   GLY F  57     5081   8295  14872   1411    224    923       N  
ATOM   8211  CA  GLY F  57     131.726 -83.270  28.752  1.00 75.56           C  
ANISOU 8211  CA  GLY F  57     5272   8407  15029   1412    178    915       C  
ATOM   8212  C   GLY F  57     130.866 -82.201  29.392  1.00 74.30           C  
ANISOU 8212  C   GLY F  57     5171   8200  14859   1432    183    938       C  
ATOM   8213  O   GLY F  57     131.005 -81.888  30.570  1.00 73.66           O  
ANISOU 8213  O   GLY F  57     5152   8068  14768   1460    161    928       O  
ATOM   8214  N   HIS F  58     129.963 -81.640  28.606  1.00 75.11           N  
ANISOU 8214  N   HIS F  58     5253   8321  14964   1416    215    969       N  
ATOM   8215  CA  HIS F  58     129.031 -80.663  29.131  1.00 73.86           C  
ANISOU 8215  CA  HIS F  58     5147   8120  14795   1435    225    993       C  
ATOM   8216  C   HIS F  58     128.307 -81.167  30.378  1.00 70.62           C  
ANISOU 8216  C   HIS F  58     4805   7665  14361   1486    239    984       C  
ATOM   8217  O   HIS F  58     128.063 -80.401  31.319  1.00 69.92           O  
ANISOU 8217  O   HIS F  58     4778   7525  14263   1509    226    989       O  
ATOM   8218  CB  HIS F  58     128.009 -80.288  28.072  1.00 73.95           C  
ANISOU 8218  CB  HIS F  58     5124   8164  14811   1415    266   1026       C  
ATOM   8219  CG  HIS F  58     127.028 -79.275  28.541  1.00 72.75           C  
ANISOU 8219  CG  HIS F  58     5022   7971  14649   1433    278   1052       C  
ATOM   8220  ND1 HIS F  58     127.299 -77.927  28.541  1.00 74.54           N  
ANISOU 8220  ND1 HIS F  58     5260   8176  14885   1416    253   1067       N  
ATOM   8221  CD2 HIS F  58     125.789 -79.411  29.064  1.00 70.06           C  
ANISOU 8221  CD2 HIS F  58     4725   7606  14290   1467    312   1065       C  
ATOM   8222  CE1 HIS F  58     126.255 -77.271  29.017  1.00 73.00           C  
ANISOU 8222  CE1 HIS F  58     5113   7946  14678   1438    272   1089       C  
ATOM   8223  NE2 HIS F  58     125.325 -78.150  29.341  1.00 70.27           N  
ANISOU 8223  NE2 HIS F  58     4787   7597  14315   1469    308   1088       N  
ATOM   8224  N   GLY F  59     127.967 -82.454  30.375  1.00 71.47           N  
ANISOU 8224  N   GLY F  59     4903   7794  14460   1504    265    972       N  
ATOM   8225  CA  GLY F  59     127.364 -83.090  31.530  1.00 68.65           C  
ANISOU 8225  CA  GLY F  59     4606   7398  14081   1552    278    961       C  
ATOM   8226  C   GLY F  59     128.266 -83.027  32.747  1.00 68.62           C  
ANISOU 8226  C   GLY F  59     4652   7348  14071   1573    234    934       C  
ATOM   8227  O   GLY F  59     127.783 -82.945  33.878  1.00 66.85           O  
ANISOU 8227  O   GLY F  59     4494   7076  13829   1612    234    931       O  
ATOM   8228  N   LYS F  60     129.578 -83.074  32.521  1.00 67.51           N  
ANISOU 8228  N   LYS F  60     4480   7224  13946   1548    196    914       N  
ATOM   8229  CA  LYS F  60     130.520 -83.011  33.623  1.00 67.88           C  
ANISOU 8229  CA  LYS F  60     4571   7231  13990   1566    152    888       C  
ATOM   8230  C   LYS F  60     130.450 -81.614  34.233  1.00 68.45           C  
ANISOU 8230  C   LYS F  60     4692   7255  14060   1570    129    902       C  
ATOM   8231  O   LYS F  60     130.717 -81.439  35.426  1.00 67.84           O  
ANISOU 8231  O   LYS F  60     4675   7130  13973   1599    104    888       O  
ATOM   8232  CB  LYS F  60     131.951 -83.342  33.168  1.00 70.38           C  
ANISOU 8232  CB  LYS F  60     4839   7578  14325   1535    116    865       C  
ATOM   8233  CG  LYS F  60     133.038 -83.218  34.262  1.00 71.06           C  
ANISOU 8233  CG  LYS F  60     4967   7624  14410   1550     67    837       C  
ATOM   8234  CD  LYS F  60     132.586 -83.840  35.596  1.00 72.64           C  
ANISOU 8234  CD  LYS F  60     5234   7779  14587   1600     72    822       C  
ATOM   8235  CE  LYS F  60     133.750 -84.420  36.423  1.00 74.51           C  
ANISOU 8235  CE  LYS F  60     5489   7999  14824   1613     32    787       C  
ATOM   8236  NZ  LYS F  60     134.760 -83.393  36.859  1.00 78.06           N  
ANISOU 8236  NZ  LYS F  60     5959   8419  15283   1601    -19    780       N  
ATOM   8237  N   LYS F  61     130.110 -80.610  33.425  1.00 67.26           N  
ANISOU 8237  N   LYS F  61     4516   7118  13920   1542    138    930       N  
ATOM   8238  CA  LYS F  61     130.039 -79.254  33.960  1.00 67.48           C  
ANISOU 8238  CA  LYS F  61     4589   7102  13947   1546    117    944       C  
ATOM   8239  C   LYS F  61     128.819 -79.154  34.845  1.00 67.43           C  
ANISOU 8239  C   LYS F  61     4648   7054  13920   1587    144    956       C  
ATOM   8240  O   LYS F  61     128.928 -78.790  36.016  1.00 67.61           O  
ANISOU 8240  O   LYS F  61     4734   7024  13930   1616    121    947       O  
ATOM   8241  CB  LYS F  61     130.005 -78.213  32.840  1.00 67.51           C  
ANISOU 8241  CB  LYS F  61     4548   7132  13969   1504    119    972       C  
ATOM   8242  CG  LYS F  61     131.335 -77.506  32.624  1.00 67.73           C  
ANISOU 8242  CG  LYS F  61     4555   7164  14017   1472     71    962       C  
ATOM   8243  CD  LYS F  61     131.518 -77.093  31.171  1.00 67.68           C  
ANISOU 8243  CD  LYS F  61     4475   7209  14031   1423     78    981       C  
ATOM   8244  CE  LYS F  61     132.601 -75.998  31.017  1.00 67.93           C  
ANISOU 8244  CE  LYS F  61     4496   7234  14082   1393     32    980       C  
ATOM   8245  NZ  LYS F  61     133.971 -76.366  31.513  1.00 68.09           N  
ANISOU 8245  NZ  LYS F  61     4517   7247  14108   1391    -13    948       N  
ATOM   8246  N   VAL F  62     127.672 -79.522  34.277  1.00 67.20           N  
ANISOU 8246  N   VAL F  62     4602   7047  13884   1591    191    976       N  
ATOM   8247  CA  VAL F  62     126.386 -79.535  34.962  1.00 67.11           C  
ANISOU 8247  CA  VAL F  62     4645   7003  13852   1630    224    990       C  
ATOM   8248  C   VAL F  62     126.402 -80.375  36.219  1.00 67.13           C  
ANISOU 8248  C   VAL F  62     4701   6969  13835   1674    219    965       C  
ATOM   8249  O   VAL F  62     125.838 -79.995  37.237  1.00 67.21           O  
ANISOU 8249  O   VAL F  62     4777   6930  13829   1707    220    968       O  
ATOM   8250  CB  VAL F  62     125.290 -80.080  34.050  1.00 66.83           C  
ANISOU 8250  CB  VAL F  62     4571   7007  13814   1624    277   1010       C  
ATOM   8251  CG1 VAL F  62     123.921 -79.902  34.689  1.00 66.76           C  
ANISOU 8251  CG1 VAL F  62     4617   6963  13786   1661    310   1029       C  
ATOM   8252  CG2 VAL F  62     125.336 -79.382  32.702  1.00 66.80           C  
ANISOU 8252  CG2 VAL F  62     4506   7045  13830   1578    283   1034       C  
ATOM   8253  N   ALA F  63     127.045 -81.531  36.136  1.00 67.04           N  
ANISOU 8253  N   ALA F  63     4662   6984  13826   1673    213    939       N  
ATOM   8254  CA  ALA F  63     127.257 -82.372  37.304  1.00 67.06           C  
ANISOU 8254  CA  ALA F  63     4712   6956  13813   1712    203    912       C  
ATOM   8255  C   ALA F  63     127.938 -81.590  38.419  1.00 67.35           C  
ANISOU 8255  C   ALA F  63     4806   6939  13846   1726    158    899       C  
ATOM   8256  O   ALA F  63     127.538 -81.646  39.592  1.00 67.42           O  
ANISOU 8256  O   ALA F  63     4880   6900  13835   1766    157    893       O  
ATOM   8257  CB  ALA F  63     128.084 -83.567  36.933  1.00 66.97           C  
ANISOU 8257  CB  ALA F  63     4654   6982  13808   1701    195    886       C  
ATOM   8258  N   ASP F  64     128.958 -80.835  38.028  1.00 67.53           N  
ANISOU 8258  N   ASP F  64     4803   6970  13887   1693    121    897       N  
ATOM   8259  CA  ASP F  64     129.837 -80.198  38.991  1.00 67.81           C  
ANISOU 8259  CA  ASP F  64     4883   6961  13922   1701     73    881       C  
ATOM   8260  C   ASP F  64     129.148 -79.015  39.626  1.00 67.96           C  
ANISOU 8260  C   ASP F  64     4959   6931  13931   1718     73    901       C  
ATOM   8261  O   ASP F  64     129.252 -78.805  40.833  1.00 68.12           O  
ANISOU 8261  O   ASP F  64     5043   6901  13938   1749     52    889       O  
ATOM   8262  CB  ASP F  64     131.155 -79.800  38.322  1.00 67.96           C  
ANISOU 8262  CB  ASP F  64     4852   7005  13963   1659     34    872       C  
ATOM   8263  CG  ASP F  64     132.130 -80.970  38.208  1.00 67.91           C  
ANISOU 8263  CG  ASP F  64     4811   7027  13963   1653     19    842       C  
ATOM   8264  OD1 ASP F  64     131.707 -82.157  38.265  1.00 67.70           O  
ANISOU 8264  OD1 ASP F  64     4780   7017  13927   1673     46    832       O  
ATOM   8265  OD2 ASP F  64     133.334 -80.693  38.060  1.00 68.07           O  
ANISOU 8265  OD2 ASP F  64     4809   7054  13999   1629    -22    827       O  
ATOM   8266  N   ALA F  65     128.421 -78.267  38.806  1.00 67.89           N  
ANISOU 8266  N   ALA F  65     4928   6938  13929   1698     97    932       N  
ATOM   8267  CA  ALA F  65     127.549 -77.213  39.303  1.00 67.98           C  
ANISOU 8267  CA  ALA F  65     4990   6908  13931   1715    106    955       C  
ATOM   8268  C   ALA F  65     126.694 -77.759  40.447  1.00 67.92           C  
ANISOU 8268  C   ALA F  65     5048   6861  13898   1765    127    949       C  
ATOM   8269  O   ALA F  65     126.655 -77.182  41.543  1.00 68.11           O  
ANISOU 8269  O   ALA F  65     5136   6832  13910   1791    108    945       O  
ATOM   8270  CB  ALA F  65     126.677 -76.676  38.184  1.00 67.84           C  
ANISOU 8270  CB  ALA F  65     4934   6921  13922   1690    142    989       C  
ATOM   8271  N   LEU F  66     126.065 -78.907  40.205  1.00 67.67           N  
ANISOU 8271  N   LEU F  66     4999   6856  13858   1778    164    947       N  
ATOM   8272  CA  LEU F  66     125.205 -79.519  41.198  1.00 67.59           C  
ANISOU 8272  CA  LEU F  66     5045   6813  13824   1825    187    942       C  
ATOM   8273  C   LEU F  66     125.951 -79.937  42.450  1.00 67.75           C  
ANISOU 8273  C   LEU F  66     5114   6794  13833   1854    153    911       C  
ATOM   8274  O   LEU F  66     125.489 -79.696  43.567  1.00 67.84           O  
ANISOU 8274  O   LEU F  66     5194   6757  13827   1890    152    910       O  
ATOM   8275  CB  LEU F  66     124.499 -80.717  40.591  1.00 67.29           C  
ANISOU 8275  CB  LEU F  66     4971   6815  13782   1830    232    945       C  
ATOM   8276  CG  LEU F  66     123.313 -80.388  39.690  1.00 67.11           C  
ANISOU 8276  CG  LEU F  66     4923   6816  13761   1818    277    979       C  
ATOM   8277  CD1 LEU F  66     122.924 -81.625  38.886  1.00 66.82           C  
ANISOU 8277  CD1 LEU F  66     4835   6830  13725   1813    313    977       C  
ATOM   8278  CD2 LEU F  66     122.165 -79.900  40.547  1.00 67.13           C  
ANISOU 8278  CD2 LEU F  66     4992   6771  13744   1855    298    995       C  
ATOM   8279  N   THR F  67     127.096 -80.582  42.263  1.00 67.77           N  
ANISOU 8279  N   THR F  67     5083   6821  13847   1838    126    886       N  
ATOM   8280  CA  THR F  67     127.899 -81.005  43.403  1.00 67.93           C  
ANISOU 8280  CA  THR F  67     5145   6807  13857   1863     91    855       C  
ATOM   8281  C   THR F  67     128.308 -79.814  44.249  1.00 68.22           C  
ANISOU 8281  C   THR F  67     5235   6793  13893   1869     53    855       C  
ATOM   8282  O   THR F  67     128.375 -79.900  45.482  1.00 68.35           O  
ANISOU 8282  O   THR F  67     5312   6763  13893   1904     37    839       O  
ATOM   8283  CB  THR F  67     129.149 -81.717  42.973  1.00 67.93           C  
ANISOU 8283  CB  THR F  67     5096   6843  13873   1839     65    830       C  
ATOM   8284  OG1 THR F  67     128.915 -82.322  41.697  1.00 67.69           O  
ANISOU 8284  OG1 THR F  67     4996   6871  13854   1812     95    839       O  
ATOM   8285  CG2 THR F  67     129.536 -82.768  44.003  1.00 67.94           C  
ANISOU 8285  CG2 THR F  67     5132   6823  13860   1873     52    799       C  
ATOM   8286  N   ASN F  68     128.597 -78.712  43.563  1.00 68.33           N  
ANISOU 8286  N   ASN F  68     5222   6817  13924   1835     39    871       N  
ATOM   8287  CA  ASN F  68     128.957 -77.470  44.213  1.00 68.61           C  
ANISOU 8287  CA  ASN F  68     5301   6807  13960   1836      4    875       C  
ATOM   8288  C   ASN F  68     127.817 -77.086  45.107  1.00 68.62           C  
ANISOU 8288  C   ASN F  68     5371   6762  13940   1875     26    888       C  
ATOM   8289  O   ASN F  68     128.000 -76.759  46.281  1.00 68.81           O  
ANISOU 8289  O   ASN F  68     5458   6736  13952   1902      2    876       O  
ATOM   8290  CB  ASN F  68     129.228 -76.374  43.179  1.00 68.68           C  
ANISOU 8290  CB  ASN F  68     5266   6839  13990   1792     -5    896       C  
ATOM   8291  CG  ASN F  68     129.804 -75.114  43.798  1.00 68.98           C  
ANISOU 8291  CG  ASN F  68     5344   6834  14032   1789    -47    896       C  
ATOM   8292  OD1 ASN F  68     130.319 -75.138  44.918  1.00 69.15           O  
ANISOU 8292  OD1 ASN F  68     5416   6815  14044   1814    -77    875       O  
ATOM   8293  ND2 ASN F  68     129.734 -74.006  43.062  1.00 69.05           N  
ANISOU 8293  ND2 ASN F  68     5329   6852  14055   1759    -49    919       N  
ATOM   8294  N   ALA F  69     126.624 -77.162  44.530  1.00 68.42           N  
ANISOU 8294  N   ALA F  69     5331   6754  13910   1877     73    913       N  
ATOM   8295  CA  ALA F  69     125.424 -76.755  45.226  1.00 68.41           C  
ANISOU 8295  CA  ALA F  69     5389   6713  13890   1910     99    930       C  
ATOM   8296  C   ALA F  69     125.270 -77.562  46.505  1.00 68.42           C  
ANISOU 8296  C   ALA F  69     5449   6678  13869   1957     98    909       C  
ATOM   8297  O   ALA F  69     125.007 -77.014  47.544  1.00 68.57           O  
ANISOU 8297  O   ALA F  69     5533   6646  13874   1985     88    908       O  
ATOM   8298  CB  ALA F  69     124.224 -76.906  44.337  1.00 68.16           C  
ANISOU 8298  CB  ALA F  69     5326   6713  13858   1904    150    958       C  
ATOM   8299  N   VAL F  70     125.469 -78.865  46.457  1.00 68.26           N  
ANISOU 8299  N   VAL F  70     5407   6683  13845   1965    108    889       N  
ATOM   8300  CA  VAL F  70     125.286 -79.617  47.689  1.00 68.26           C  
ANISOU 8300  CA  VAL F  70     5465   6648  13824   2010    108    870       C  
ATOM   8301  C   VAL F  70     126.492 -79.397  48.623  1.00 68.53           C  
ANISOU 8301  C   VAL F  70     5533   6648  13858   2016     55    842       C  
ATOM   8302  O   VAL F  70     126.372 -79.498  49.867  1.00 68.64           O  
ANISOU 8302  O   VAL F  70     5612   6615  13853   2054     45    830       O  
ATOM   8303  CB  VAL F  70     125.025 -81.123  47.386  1.00 68.00           C  
ANISOU 8303  CB  VAL F  70     5401   6651  13786   2020    138    858       C  
ATOM   8304  CG1 VAL F  70     125.547 -81.480  46.045  1.00 67.87           C  
ANISOU 8304  CG1 VAL F  70     5302   6694  13791   1977    142    860       C  
ATOM   8305  CG2 VAL F  70     125.546 -82.046  48.483  1.00 68.05           C  
ANISOU 8305  CG2 VAL F  70     5445   6633  13779   2052    119    827       C  
ATOM   8306  N   ALA F  71     127.633 -79.039  48.022  1.00 68.65           N  
ANISOU 8306  N   ALA F  71     5504   6685  13893   1979     20    835       N  
ATOM   8307  CA  ALA F  71     128.852 -78.726  48.781  1.00 68.91           C  
ANISOU 8307  CA  ALA F  71     5564   6689  13930   1979    -33    811       C  
ATOM   8308  C   ALA F  71     128.609 -77.523  49.705  1.00 69.15           C  
ANISOU 8308  C   ALA F  71     5660   6662  13950   1998    -51    819       C  
ATOM   8309  O   ALA F  71     128.930 -77.571  50.903  1.00 69.31           O  
ANISOU 8309  O   ALA F  71     5738   6638  13957   2027    -75    800       O  
ATOM   8310  CB  ALA F  71     130.019 -78.463  47.845  1.00 69.28           C  
ANISOU 8310  CB  ALA F  71     5548   6773  14002   1933    -63    805       C  
ATOM   8311  N   HIS F  72     128.077 -76.431  49.166  1.00 69.17           N  
ANISOU 8311  N   HIS F  72     5657   6665  13961   1980    -40    847       N  
ATOM   8312  CA  HIS F  72     127.506 -75.460  50.066  1.00 69.97           C  
ANISOU 8312  CA  HIS F  72     5826   6712  14049   2005    -43    859       C  
ATOM   8313  C   HIS F  72     126.049 -75.360  49.739  1.00 69.15           C  
ANISOU 8313  C   HIS F  72     5727   6612  13936   2016      8    887       C  
ATOM   8314  O   HIS F  72     125.640 -74.517  48.929  1.00 69.13           O  
ANISOU 8314  O   HIS F  72     5699   6624  13945   1991     21    914       O  
ATOM   8315  CB  HIS F  72     128.191 -74.108  49.902  1.00 73.32           C  
ANISOU 8315  CB  HIS F  72     6248   7121  14488   1977    -80    866       C  
ATOM   8316  CG  HIS F  72     129.553 -74.209  49.306  1.00 75.42           C  
ANISOU 8316  CG  HIS F  72     6462   7418  14775   1940   -117    850       C  
ATOM   8317  ND1 HIS F  72     129.761 -74.314  47.947  1.00 74.55           N  
ANISOU 8317  ND1 HIS F  72     6276   7364  14685   1900   -106    860       N  
ATOM   8318  CD2 HIS F  72     130.777 -74.275  49.880  1.00 78.47           C  
ANISOU 8318  CD2 HIS F  72     6860   7790  15166   1939   -164    823       C  
ATOM   8319  CE1 HIS F  72     131.059 -74.410  47.709  1.00 77.05           C  
ANISOU 8319  CE1 HIS F  72     6560   7697  15017   1875   -145    841       C  
ATOM   8320  NE2 HIS F  72     131.697 -74.393  48.865  1.00 79.41           N  
ANISOU 8320  NE2 HIS F  72     6910   7954  15307   1898   -180    818       N  
ATOM   8321  N   VAL F  73     125.233 -76.128  50.445  1.00 69.42           N  
ANISOU 8321  N   VAL F  73     5800   6628  13949   2056     36    883       N  
ATOM   8322  CA  VAL F  73     123.824 -76.128  50.105  1.00 68.84           C  
ANISOU 8322  CA  VAL F  73     5729   6560  13866   2067     86    911       C  
ATOM   8323  C   VAL F  73     123.163 -75.100  50.987  1.00 69.00           C  
ANISOU 8323  C   VAL F  73     5818   6526  13874   2092     86    924       C  
ATOM   8324  O   VAL F  73     122.063 -74.623  50.700  1.00 68.91           O  
ANISOU 8324  O   VAL F  73     5813   6512  13859   2096    120    951       O  
ATOM   8325  CB  VAL F  73     123.203 -77.540  50.243  1.00 68.59           C  
ANISOU 8325  CB  VAL F  73     5695   6545  13820   2094    122    902       C  
ATOM   8326  CG1 VAL F  73     123.173 -77.992  51.689  1.00 68.68           C  
ANISOU 8326  CG1 VAL F  73     5778   6509  13810   2140    111    881       C  
ATOM   8327  CG2 VAL F  73     121.824 -77.556  49.618  1.00 68.37           C  
ANISOU 8327  CG2 VAL F  73     5654   6534  13788   2097    175    932       C  
ATOM   8328  N   ASP F  74     123.879 -74.687  52.026  1.00 69.26           N  
ANISOU 8328  N   ASP F  74     5900   6515  13900   2107     45    906       N  
ATOM   8329  CA  ASP F  74     123.285 -73.771  52.984  1.00 69.42           C  
ANISOU 8329  CA  ASP F  74     5991   6480  13907   2135     42    916       C  
ATOM   8330  C   ASP F  74     123.352 -72.338  52.494  1.00 69.58           C  
ANISOU 8330  C   ASP F  74     6002   6493  13941   2106     29    937       C  
ATOM   8331  O   ASP F  74     122.679 -71.479  53.022  1.00 69.68           O  
ANISOU 8331  O   ASP F  74     6063   6468  13945   2123     35    953       O  
ATOM   8332  CB  ASP F  74     123.960 -73.921  54.336  1.00 69.63           C  
ANISOU 8332  CB  ASP F  74     6077   6461  13919   2164      6    887       C  
ATOM   8333  CG  ASP F  74     123.625 -75.224  54.987  1.00 69.49           C  
ANISOU 8333  CG  ASP F  74     6081   6439  13882   2200     25    870       C  
ATOM   8334  OD1 ASP F  74     123.017 -76.067  54.304  1.00 69.23           O  
ANISOU 8334  OD1 ASP F  74     6010   6444  13849   2198     63    878       O  
ATOM   8335  OD2 ASP F  74     123.955 -75.417  56.169  1.00 69.63           O  
ANISOU 8335  OD2 ASP F  74     6155   6418  13885   2230      2    849       O  
ATOM   8336  N   ASP F  75     124.196 -72.085  51.506  1.00 72.39           N  
ANISOU 8336  N   ASP F  75     6297   6887  14320   2063      9    938       N  
ATOM   8337  CA  ASP F  75     124.037 -70.910  50.686  1.00 73.67           C  
ANISOU 8337  CA  ASP F  75     6433   7060  14499   2031     10    964       C  
ATOM   8338  C   ASP F  75     124.134 -71.319  49.227  1.00 71.51           C  
ANISOU 8338  C   ASP F  75     6076   6849  14244   1992     29    975       C  
ATOM   8339  O   ASP F  75     125.221 -71.389  48.684  1.00 72.90           O  
ANISOU 8339  O   ASP F  75     6208   7053  14438   1961      0    962       O  
ATOM   8340  CB  ASP F  75     125.140 -69.901  51.040  1.00 78.10           C  
ANISOU 8340  CB  ASP F  75     7010   7594  15071   2015    -43    954       C  
ATOM   8341  CG  ASP F  75     125.055 -68.601  50.241  1.00 80.24           C  
ANISOU 8341  CG  ASP F  75     7256   7872  15360   1981    -47    981       C  
ATOM   8342  OD1 ASP F  75     124.625 -68.618  49.058  1.00 78.45           O  
ANISOU 8342  OD1 ASP F  75     6973   7690  15146   1954    -18   1002       O  
ATOM   8343  OD2 ASP F  75     125.428 -67.550  50.820  1.00 84.02           O  
ANISOU 8343  OD2 ASP F  75     7772   8311  15839   1982    -79    981       O  
ATOM   8344  N   MET F  76     123.022 -71.502  48.548  1.00 70.98           N  
ANISOU 8344  N   MET F  76     5988   6807  14176   1991     76    999       N  
ATOM   8345  CA  MET F  76     123.100 -71.730  47.118  1.00 69.45           C  
ANISOU 8345  CA  MET F  76     5714   6672  14000   1951     93   1011       C  
ATOM   8346  C   MET F  76     123.339 -70.502  46.243  1.00 71.66           C  
ANISOU 8346  C   MET F  76     5960   6966  14302   1911     80   1033       C  
ATOM   8347  O   MET F  76     124.090 -70.598  45.285  1.00 72.06           O  
ANISOU 8347  O   MET F  76     5949   7060  14372   1873     68   1030       O  
ATOM   8348  CB  MET F  76     121.880 -72.487  46.641  1.00 68.75           C  
ANISOU 8348  CB  MET F  76     5608   6609  13903   1963    148   1027       C  
ATOM   8349  CG  MET F  76     122.266 -73.904  46.298  1.00 68.56           C  
ANISOU 8349  CG  MET F  76     5544   6625  13880   1961    156   1007       C  
ATOM   8350  SD  MET F  76     121.154 -75.153  46.915  1.00 68.33           S  
ANISOU 8350  SD  MET F  76     5547   6589  13826   2007    200   1003       S  
ATOM   8351  CE  MET F  76     120.231 -74.170  48.123  1.00 68.49           C  
ANISOU 8351  CE  MET F  76     5656   6541  13827   2046    205   1017       C  
ATOM   8352  N   PRO F  77     122.665 -69.360  46.522  1.00 69.26           N  
ANISOU 8352  N   PRO F  77     5694   6627  13994   1918     86   1055       N  
ATOM   8353  CA  PRO F  77     122.753 -68.292  45.517  1.00 69.31           C  
ANISOU 8353  CA  PRO F  77     5659   6654  14022   1877     81   1079       C  
ATOM   8354  C   PRO F  77     124.146 -67.673  45.412  1.00 73.20           C  
ANISOU 8354  C   PRO F  77     6134   7147  14532   1848     29   1065       C  
ATOM   8355  O   PRO F  77     124.533 -67.266  44.327  1.00 74.37           O  
ANISOU 8355  O   PRO F  77     6225   7332  14701   1807     24   1077       O  
ATOM   8356  CB  PRO F  77     121.728 -67.259  46.003  1.00 69.98           C  
ANISOU 8356  CB  PRO F  77     5796   6696  14097   1897     97   1103       C  
ATOM   8357  CG  PRO F  77     120.893 -67.972  47.019  1.00 69.31           C  
ANISOU 8357  CG  PRO F  77     5768   6581  13986   1945    122   1096       C  
ATOM   8358  CD  PRO F  77     121.813 -68.945  47.651  1.00 69.35           C  
ANISOU 8358  CD  PRO F  77     5781   6583  13984   1959     96   1061       C  
ATOM   8359  N   ASN F  78     124.891 -67.581  46.503  1.00 70.67           N  
ANISOU 8359  N   ASN F  78     5862   6786  14204   1867     -9   1041       N  
ATOM   8360  CA  ASN F  78     126.290 -67.187  46.372  1.00 74.27           C  
ANISOU 8360  CA  ASN F  78     6296   7247  14677   1838    -59   1024       C  
ATOM   8361  C   ASN F  78     127.076 -68.182  45.506  1.00 72.79           C  
ANISOU 8361  C   ASN F  78     6039   7114  14503   1812    -63   1009       C  
ATOM   8362  O   ASN F  78     127.768 -67.787  44.557  1.00 74.55           O  
ANISOU 8362  O   ASN F  78     6207   7371  14748   1770    -79   1014       O  
ATOM   8363  CB  ASN F  78     126.954 -67.061  47.747  1.00 77.03           C  
ANISOU 8363  CB  ASN F  78     6709   7544  15015   1866    -99    999       C  
ATOM   8364  CG  ASN F  78     126.519 -65.813  48.487  1.00 79.54           C  
ANISOU 8364  CG  ASN F  78     7087   7808  15325   1882   -109   1012       C  
ATOM   8365  OD1 ASN F  78     125.361 -65.670  48.853  1.00 78.06           O  
ANISOU 8365  OD1 ASN F  78     6937   7598  15123   1909    -76   1029       O  
ATOM   8366  ND2 ASN F  78     127.459 -64.901  48.713  1.00 83.55           N  
ANISOU 8366  ND2 ASN F  78     7605   8296  15845   1866   -154   1006       N  
ATOM   8367  N   ALA F  79     126.959 -69.467  45.844  1.00 73.56           N  
ANISOU 8367  N   ALA F  79     6141   7222  14588   1835    -47    991       N  
ATOM   8368  CA  ALA F  79     127.623 -70.524  45.095  1.00 71.96           C  
ANISOU 8368  CA  ALA F  79     5877   7070  14396   1814    -47    975       C  
ATOM   8369  C   ALA F  79     127.243 -70.484  43.615  1.00 70.56           C  
ANISOU 8369  C   ALA F  79     5627   6948  14234   1777    -17    999       C  
ATOM   8370  O   ALA F  79     128.104 -70.545  42.735  1.00 71.79           O  
ANISOU 8370  O   ALA F  79     5724   7143  14409   1740    -34    995       O  
ATOM   8371  CB  ALA F  79     127.294 -71.882  45.690  1.00 69.34           C  
ANISOU 8371  CB  ALA F  79     5564   6737  14045   1849    -27    957       C  
ATOM   8372  N   LEU F  80     125.955 -70.350  43.338  1.00 69.15           N  
ANISOU 8372  N   LEU F  80     5455   6772  14048   1787     27   1025       N  
ATOM   8373  CA  LEU F  80     125.492 -70.441  41.964  1.00 68.94           C  
ANISOU 8373  CA  LEU F  80     5362   6798  14035   1756     59   1048       C  
ATOM   8374  C   LEU F  80     125.420 -69.098  41.275  1.00 69.05           C  
ANISOU 8374  C   LEU F  80     5357   6815  14065   1724     53   1075       C  
ATOM   8375  O   LEU F  80     124.986 -69.016  40.136  1.00 68.90           O  
ANISOU 8375  O   LEU F  80     5285   6837  14057   1697     80   1096       O  
ATOM   8376  CB  LEU F  80     124.131 -71.106  41.924  1.00 68.70           C  
ANISOU 8376  CB  LEU F  80     5340   6773  13988   1781    112   1062       C  
ATOM   8377  CG  LEU F  80     124.094 -72.618  42.057  1.00 68.50           C  
ANISOU 8377  CG  LEU F  80     5304   6769  13952   1800    130   1041       C  
ATOM   8378  CD1 LEU F  80     123.165 -72.996  43.181  1.00 68.45           C  
ANISOU 8378  CD1 LEU F  80     5366   6722  13921   1849    152   1039       C  
ATOM   8379  CD2 LEU F  80     123.597 -73.173  40.755  1.00 68.23           C  
ANISOU 8379  CD2 LEU F  80     5203   6794  13927   1775    168   1057       C  
ATOM   8380  N   SER F  81     125.862 -68.057  41.974  1.00 70.24           N  
ANISOU 8380  N   SER F  81     5550   6922  14217   1727     18   1073       N  
ATOM   8381  CA  SER F  81     125.761 -66.665  41.510  1.00 73.17           C  
ANISOU 8381  CA  SER F  81     5915   7286  14602   1702      9   1098       C  
ATOM   8382  C   SER F  81     126.251 -66.436  40.081  1.00 74.25           C  
ANISOU 8382  C   SER F  81     5972   7477  14762   1652      8   1110       C  
ATOM   8383  O   SER F  81     125.535 -65.870  39.259  1.00 73.44           O  
ANISOU 8383  O   SER F  81     5843   7393  14667   1633     34   1139       O  
ATOM   8384  CB  SER F  81     126.535 -65.750  42.473  1.00 77.49           C  
ANISOU 8384  CB  SER F  81     6512   7782  15149   1709    -39   1086       C  
ATOM   8385  OG  SER F  81     126.776 -64.455  41.933  1.00 80.98           O  
ANISOU 8385  OG  SER F  81     6937   8223  15608   1678    -56   1105       O  
ATOM   8386  N   ALA F  82     127.461 -66.885  39.778  1.00 73.86           N  
ANISOU 8386  N   ALA F  82     5884   7454  14726   1629    -23   1088       N  
ATOM   8387  CA  ALA F  82     127.979 -66.705  38.436  1.00 75.35           C  
ANISOU 8387  CA  ALA F  82     5997   7694  14937   1582    -26   1098       C  
ATOM   8388  C   ALA F  82     127.125 -67.462  37.425  1.00 71.48           C  
ANISOU 8388  C   ALA F  82     5458   7254  14448   1572     23   1114       C  
ATOM   8389  O   ALA F  82     127.089 -67.112  36.256  1.00 72.28           O  
ANISOU 8389  O   ALA F  82     5503   7396  14566   1536     34   1133       O  
ATOM   8390  CB  ALA F  82     129.410 -67.156  38.359  1.00 78.14           C  
ANISOU 8390  CB  ALA F  82     6320   8066  15303   1563    -66   1070       C  
ATOM   8391  N   LEU F  83     126.472 -68.529  37.873  1.00 76.21           N  
ANISOU 8391  N   LEU F  83     6077   7850  15028   1605     52   1105       N  
ATOM   8392  CA  LEU F  83     125.512 -69.238  37.038  1.00 72.55           C  
ANISOU 8392  CA  LEU F  83     5575   7427  14562   1602    102   1121       C  
ATOM   8393  C   LEU F  83     124.101 -68.572  36.998  1.00 70.98           C  
ANISOU 8393  C   LEU F  83     5402   7212  14355   1615    140   1154       C  
ATOM   8394  O   LEU F  83     123.326 -68.784  36.044  1.00 68.82           O  
ANISOU 8394  O   LEU F  83     5088   6975  14084   1601    179   1175       O  
ATOM   8395  CB  LEU F  83     125.401 -70.682  37.499  1.00 69.32           C  
ANISOU 8395  CB  LEU F  83     5175   7025  14138   1631    118   1098       C  
ATOM   8396  CG  LEU F  83     126.528 -71.571  36.999  1.00 69.82           C  
ANISOU 8396  CG  LEU F  83     5186   7130  14213   1609     98   1073       C  
ATOM   8397  CD1 LEU F  83     126.337 -72.990  37.516  1.00 68.24           C  
ANISOU 8397  CD1 LEU F  83     4998   6933  13996   1640    116   1051       C  
ATOM   8398  CD2 LEU F  83     126.596 -71.554  35.491  1.00 70.70           C  
ANISOU 8398  CD2 LEU F  83     5219   7301  14344   1564    114   1090       C  
ATOM   8399  N   SER F  84     123.747 -67.823  38.044  1.00 72.01           N  
ANISOU 8399  N   SER F  84     5601   7286  14473   1643    130   1158       N  
ATOM   8400  CA  SER F  84     122.509 -67.053  38.022  1.00 71.38           C  
ANISOU 8400  CA  SER F  84     5547   7187  14387   1653    161   1189       C  
ATOM   8401  C   SER F  84     122.491 -66.257  36.740  1.00 73.52           C  
ANISOU 8401  C   SER F  84     5761   7495  14680   1609    167   1215       C  
ATOM   8402  O   SER F  84     121.570 -66.378  35.927  1.00 71.84           O  
ANISOU 8402  O   SER F  84     5517   7312  14468   1600    207   1239       O  
ATOM   8403  CB  SER F  84     122.396 -66.083  39.214  1.00 73.35           C  
ANISOU 8403  CB  SER F  84     5871   7371  14626   1680    139   1189       C  
ATOM   8404  OG  SER F  84     122.092 -66.716  40.443  1.00 71.67           O  
ANISOU 8404  OG  SER F  84     5720   7120  14391   1726    143   1171       O  
ATOM   8405  N   ASP F  85     123.563 -65.487  36.564  1.00 72.12           N  
ANISOU 8405  N   ASP F  85     5568   7316  14520   1581    125   1210       N  
ATOM   8406  CA  ASP F  85     123.662 -64.473  35.540  1.00 75.19           C  
ANISOU 8406  CA  ASP F  85     5913   7727  14928   1540    121   1234       C  
ATOM   8407  C   ASP F  85     123.866 -65.089  34.184  1.00 74.59           C  
ANISOU 8407  C   ASP F  85     5757   7718  14867   1504    138   1239       C  
ATOM   8408  O   ASP F  85     123.479 -64.537  33.175  1.00 75.84           O  
ANISOU 8408  O   ASP F  85     5874   7905  15038   1475    155   1266       O  
ATOM   8409  CB  ASP F  85     124.813 -63.525  35.861  1.00 79.85           C  
ANISOU 8409  CB  ASP F  85     6514   8294  15531   1523     68   1224       C  
ATOM   8410  CG  ASP F  85     124.721 -62.950  37.265  1.00 81.03           C  
ANISOU 8410  CG  ASP F  85     6745   8377  15666   1560     48   1216       C  
ATOM   8411  OD1 ASP F  85     123.779 -63.355  37.990  1.00 77.98           O  
ANISOU 8411  OD1 ASP F  85     6406   7964  15259   1598     75   1218       O  
ATOM   8412  OD2 ASP F  85     125.585 -62.109  37.636  1.00 85.27           O  
ANISOU 8412  OD2 ASP F  85     7299   8888  16211   1549      5   1209       O  
ATOM   8413  N   LEU F  86     124.480 -66.247  34.153  1.00 75.85           N  
ANISOU 8413  N   LEU F  86     5893   7903  15025   1505    132   1213       N  
ATOM   8414  CA  LEU F  86     124.809 -66.838  32.871  1.00 75.68           C  
ANISOU 8414  CA  LEU F  86     5793   7944  15018   1469    144   1215       C  
ATOM   8415  C   LEU F  86     123.538 -67.272  32.138  1.00 72.35           C  
ANISOU 8415  C   LEU F  86     5346   7553  14591   1470    199   1239       C  
ATOM   8416  O   LEU F  86     123.361 -66.980  30.955  1.00 73.37           O  
ANISOU 8416  O   LEU F  86     5419   7723  14734   1436    215   1260       O  
ATOM   8417  CB  LEU F  86     125.772 -68.023  33.051  1.00 74.96           C  
ANISOU 8417  CB  LEU F  86     5684   7871  14926   1472    126   1181       C  
ATOM   8418  CG  LEU F  86     126.182 -68.756  31.778  1.00 75.91           C  
ANISOU 8418  CG  LEU F  86     5723   8057  15061   1436    137   1179       C  
ATOM   8419  CD1 LEU F  86     126.725 -67.784  30.746  1.00 80.03           C  
ANISOU 8419  CD1 LEU F  86     6195   8606  15606   1389    120   1196       C  
ATOM   8420  CD2 LEU F  86     127.195 -69.831  32.110  1.00 74.93           C  
ANISOU 8420  CD2 LEU F  86     5589   7944  14936   1441    114   1143       C  
ATOM   8421  N   HIS F  87     122.649 -67.964  32.842  1.00 76.45           N  
ANISOU 8421  N   HIS F  87     5907   8052  15090   1510    228   1236       N  
ATOM   8422  CA  HIS F  87     121.435 -68.462  32.222  1.00 73.21           C  
ANISOU 8422  CA  HIS F  87     5475   7668  14672   1515    280   1257       C  
ATOM   8423  C   HIS F  87     120.415 -67.353  32.130  1.00 73.76           C  
ANISOU 8423  C   HIS F  87     5568   7717  14742   1516    300   1291       C  
ATOM   8424  O   HIS F  87     119.768 -67.168  31.091  1.00 73.47           O  
ANISOU 8424  O   HIS F  87     5488   7715  14713   1493    330   1317       O  
ATOM   8425  CB  HIS F  87     120.897 -69.649  33.005  1.00 69.42           C  
ANISOU 8425  CB  HIS F  87     5031   7175  14172   1557    302   1240       C  
ATOM   8426  CG  HIS F  87     121.905 -70.739  33.171  1.00 68.90           C  
ANISOU 8426  CG  HIS F  87     4947   7127  14106   1557    281   1206       C  
ATOM   8427  ND1 HIS F  87     123.009 -70.604  33.985  1.00 70.52           N  
ANISOU 8427  ND1 HIS F  87     5179   7303  14312   1564    235   1180       N  
ATOM   8428  CD2 HIS F  87     122.013 -71.958  32.591  1.00 67.42           C  
ANISOU 8428  CD2 HIS F  87     4713   6984  13918   1551    300   1194       C  
ATOM   8429  CE1 HIS F  87     123.738 -71.703  33.920  1.00 69.85           C  
ANISOU 8429  CE1 HIS F  87     5069   7244  14228   1562    226   1153       C  
ATOM   8430  NE2 HIS F  87     123.159 -72.539  33.079  1.00 67.98           N  
ANISOU 8430  NE2 HIS F  87     4787   7052  13992   1554    264   1161       N  
ATOM   8431  N   ALA F  88     120.284 -66.585  33.202  1.00 72.94           N  
ANISOU 8431  N   ALA F  88     5530   7556  14628   1542    282   1291       N  
ATOM   8432  CA  ALA F  88     119.281 -65.547  33.212  1.00 73.04           C  
ANISOU 8432  CA  ALA F  88     5569   7544  14639   1547    302   1322       C  
ATOM   8433  C   ALA F  88     119.527 -64.573  32.066  1.00 76.31           C  
ANISOU 8433  C   ALA F  88     5931   7988  15076   1500    295   1345       C  
ATOM   8434  O   ALA F  88     118.702 -64.449  31.167  1.00 75.74           O  
ANISOU 8434  O   ALA F  88     5825   7945  15008   1485    330   1372       O  
ATOM   8435  CB  ALA F  88     119.280 -64.828  34.546  1.00 74.44           C  
ANISOU 8435  CB  ALA F  88     5824   7656  14805   1579    278   1315       C  
ATOM   8436  N   HIS F  89     120.703 -63.950  32.060  1.00 74.58           N  
ANISOU 8436  N   HIS F  89     8338   9463  10537   1563    532   3310       N  
ATOM   8437  CA  HIS F  89     120.973 -62.792  31.202  1.00 78.46           C  
ANISOU 8437  CA  HIS F  89     8788   9990  11034   1545    567   3325       C  
ATOM   8438  C   HIS F  89     121.595 -63.135  29.857  1.00 79.94           C  
ANISOU 8438  C   HIS F  89     8918  10241  11216   1580    555   3317       C  
ATOM   8439  O   HIS F  89     121.002 -62.897  28.807  1.00 79.86           O  
ANISOU 8439  O   HIS F  89     8885  10244  11214   1589    580   3330       O  
ATOM   8440  CB  HIS F  89     121.879 -61.803  31.945  1.00 82.47           C  
ANISOU 8440  CB  HIS F  89     9293  10505  11537   1507    574   3327       C  
ATOM   8441  CG  HIS F  89     121.247 -61.217  33.170  1.00 81.81           C  
ANISOU 8441  CG  HIS F  89     9261  10362  11460   1468    593   3338       C  
ATOM   8442  ND1 HIS F  89     121.979 -60.840  34.276  1.00 84.07           N  
ANISOU 8442  ND1 HIS F  89     9564  10640  11739   1441    583   3331       N  
ATOM   8443  CD2 HIS F  89     119.949 -60.947  33.464  1.00 79.36           C  
ANISOU 8443  CD2 HIS F  89     8989  10000  11163   1452    622   3356       C  
ATOM   8444  CE1 HIS F  89     121.159 -60.360  35.198  1.00 83.06           C  
ANISOU 8444  CE1 HIS F  89     9482  10457  11619   1410    605   3344       C  
ATOM   8445  NE2 HIS F  89     119.922 -60.415  34.731  1.00 80.20           N  
ANISOU 8445  NE2 HIS F  89     9135  10069  11270   1416    628   3359       N  
ATOM   8446  N   LYS F  90     122.805 -63.666  29.896  1.00 77.79           N  
ANISOU 8446  N   LYS F  90     8621  10008  10929   1598    518   3294       N  
ATOM   8447  CA  LYS F  90     123.562 -63.922  28.679  1.00 80.10           C  
ANISOU 8447  CA  LYS F  90     8855  10364  11214   1628    506   3284       C  
ATOM   8448  C   LYS F  90     122.807 -64.911  27.783  1.00 77.07           C  
ANISOU 8448  C   LYS F  90     8465   9984  10834   1670    497   3280       C  
ATOM   8449  O   LYS F  90     122.466 -64.589  26.641  1.00 78.56           O  
ANISOU 8449  O   LYS F  90     8621  10199  11029   1679    520   3292       O  
ATOM   8450  CB  LYS F  90     124.964 -64.446  29.038  1.00 81.92           C  
ANISOU 8450  CB  LYS F  90     9068  10631  11428   1641    463   3258       C  
ATOM   8451  CG  LYS F  90     125.945 -64.558  27.891  1.00 84.52           C  
ANISOU 8451  CG  LYS F  90     9334  11031  11747   1667    451   3247       C  
ATOM   8452  CD  LYS F  90     127.369 -64.647  28.434  1.00 85.68           C  
ANISOU 8452  CD  LYS F  90     9466  11209  11878   1664    419   3227       C  
ATOM   8453  CE  LYS F  90     128.268 -65.538  27.569  1.00 87.46           C  
ANISOU 8453  CE  LYS F  90     9645  11494  12092   1708    383   3204       C  
ATOM   8454  NZ  LYS F  90     129.530 -65.949  28.268  1.00 87.70           N  
ANISOU 8454  NZ  LYS F  90     9671  11545  12106   1712    344   3180       N  
ATOM   8455  N   LEU F  91     122.518 -66.093  28.331  1.00 80.91           N  
ANISOU 8455  N   LEU F  91     8983  10442  11318   1694    463   3264       N  
ATOM   8456  CA  LEU F  91     121.934 -67.204  27.583  1.00 78.09           C  
ANISOU 8456  CA  LEU F  91     8620  10088  10962   1737    446   3254       C  
ATOM   8457  C   LEU F  91     120.412 -67.116  27.430  1.00 75.82           C  
ANISOU 8457  C   LEU F  91     8363   9754  10691   1732    476   3274       C  
ATOM   8458  O   LEU F  91     119.849 -67.750  26.528  1.00 75.29           O  
ANISOU 8458  O   LEU F  91     8282   9697  10628   1764    474   3272       O  
ATOM   8459  CB  LEU F  91     122.305 -68.525  28.259  1.00 75.20           C  
ANISOU 8459  CB  LEU F  91     8275   9710  10587   1764    396   3229       C  
ATOM   8460  CG  LEU F  91     123.756 -68.972  28.055  1.00 77.34           C  
ANISOU 8460  CG  LEU F  91     8506  10036  10842   1786    358   3204       C  
ATOM   8461  CD1 LEU F  91     124.123 -70.146  28.969  1.00 75.03           C  
ANISOU 8461  CD1 LEU F  91     8243   9724  10542   1805    310   3181       C  
ATOM   8462  CD2 LEU F  91     124.002 -69.340  26.595  1.00 77.92           C  
ANISOU 8462  CD2 LEU F  91     8526  10166  10914   1823    353   3196       C  
ATOM   8463  N   ARG F  92     119.762 -66.349  28.311  1.00 76.29           N  
ANISOU 8463  N   ARG F  92     8463   9764  10758   1693    504   3293       N  
ATOM   8464  CA  ARG F  92     118.292 -66.256  28.381  1.00 73.90           C  
ANISOU 8464  CA  ARG F  92     8197   9410  10470   1684    533   3312       C  
ATOM   8465  C   ARG F  92     117.571 -67.611  28.203  1.00 70.07           C  
ANISOU 8465  C   ARG F  92     7730   8905   9987   1723    507   3300       C  
ATOM   8466  O   ARG F  92     116.980 -67.880  27.156  1.00 69.66           O  
ANISOU 8466  O   ARG F  92     7658   8868   9942   1747    516   3304       O  
ATOM   8467  CB  ARG F  92     117.747 -65.233  27.366  1.00 76.32           C  
ANISOU 8467  CB  ARG F  92     8477   9733  10788   1671    579   3336       C  
ATOM   8468  CG  ARG F  92     116.746 -64.238  28.012  1.00 75.32           C  
ANISOU 8468  CG  ARG F  92     8391   9553  10675   1629    621   3362       C  
ATOM   8469  CD  ARG F  92     116.209 -63.153  27.059  1.00 78.08           C  
ANISOU 8469  CD  ARG F  92     8715   9916  11037   1613    669   3387       C  
ATOM   8470  NE  ARG F  92     114.802 -63.379  26.706  1.00 75.71           N  
ANISOU 8470  NE  ARG F  92     8436   9581  10749   1622    689   3401       N  
ATOM   8471  CZ  ARG F  92     113.758 -62.972  27.428  1.00 74.35           C  
ANISOU 8471  CZ  ARG F  92     8311   9351  10587   1595    715   3417       C  
ATOM   8472  NH1 ARG F  92     113.942 -62.288  28.554  1.00 75.22           N  
ANISOU 8472  NH1 ARG F  92     8451   9432  10698   1557    723   3422       N  
ATOM   8473  NH2 ARG F  92     112.527 -63.253  27.022  1.00 72.32           N  
ANISOU 8473  NH2 ARG F  92     8069   9067  10341   1607    731   3428       N  
ATOM   8474  N   VAL F  93     117.647 -68.470  29.214  1.00 72.46           N  
ANISOU 8474  N   VAL F  93     8070   9177  10285   1730    473   3285       N  
ATOM   8475  CA  VAL F  93     116.991 -69.769  29.142  1.00 69.00           C  
ANISOU 8475  CA  VAL F  93     7651   8717   9849   1765    447   3274       C  
ATOM   8476  C   VAL F  93     115.580 -69.708  29.733  1.00 66.56           C  
ANISOU 8476  C   VAL F  93     7394   8342   9552   1748    470   3292       C  
ATOM   8477  O   VAL F  93     115.405 -69.328  30.885  1.00 66.25           O  
ANISOU 8477  O   VAL F  93     7395   8263   9513   1717    476   3299       O  
ATOM   8478  CB  VAL F  93     117.813 -70.878  29.875  1.00 67.62           C  
ANISOU 8478  CB  VAL F  93     7487   8543   9662   1787    394   3247       C  
ATOM   8479  CG1 VAL F  93     117.179 -72.230  29.648  1.00 64.30           C  
ANISOU 8479  CG1 VAL F  93     7080   8105   9245   1826    367   3235       C  
ATOM   8480  CG2 VAL F  93     119.274 -70.918  29.397  1.00 70.33           C  
ANISOU 8480  CG2 VAL F  93     7781   8950   9992   1802    370   3229       C  
ATOM   8481  N   ASP F  94     114.572 -70.085  28.951  1.00 69.99           N  
ANISOU 8481  N   ASP F  94     7827   8768   9997   1769    482   3298       N  
ATOM   8482  CA  ASP F  94     113.192 -70.010  29.426  1.00 67.86           C  
ANISOU 8482  CA  ASP F  94     7605   8439   9740   1753    505   3316       C  
ATOM   8483  C   ASP F  94     112.947 -70.928  30.619  1.00 65.08           C  
ANISOU 8483  C   ASP F  94     7303   8040   9385   1756    474   3306       C  
ATOM   8484  O   ASP F  94     113.008 -72.152  30.476  1.00 63.36           O  
ANISOU 8484  O   ASP F  94     7085   7825   9165   1793    438   3288       O  
ATOM   8485  CB  ASP F  94     112.220 -70.365  28.302  1.00 67.12           C  
ANISOU 8485  CB  ASP F  94     7497   8348   9656   1779    519   3322       C  
ATOM   8486  CG  ASP F  94     110.764 -70.041  28.651  1.00 65.41           C  
ANISOU 8486  CG  ASP F  94     7324   8075   9453   1759    553   3344       C  
ATOM   8487  OD1 ASP F  94     110.331 -70.274  29.805  1.00 63.86           O  
ANISOU 8487  OD1 ASP F  94     7177   7828   9258   1743    546   3346       O  
ATOM   8488  OD2 ASP F  94     110.047 -69.545  27.755  1.00 65.82           O  
ANISOU 8488  OD2 ASP F  94     7360   8134   9515   1758    586   3359       O  
ATOM   8489  N   PRO F  95     112.580 -70.351  31.777  1.00 65.66           N  
ANISOU 8489  N   PRO F  95     7419   8067   9460   1719    490   3318       N  
ATOM   8490  CA  PRO F  95     112.460 -71.065  33.057  1.00 63.63           C  
ANISOU 8490  CA  PRO F  95     7211   7767   9200   1715    462   3311       C  
ATOM   8491  C   PRO F  95     111.698 -72.396  33.017  1.00 60.81           C  
ANISOU 8491  C   PRO F  95     6876   7382   8846   1749    437   3302       C  
ATOM   8492  O   PRO F  95     111.857 -73.206  33.932  1.00 59.44           O  
ANISOU 8492  O   PRO F  95     6733   7185   8668   1755    403   3291       O  
ATOM   8493  CB  PRO F  95     111.716 -70.055  33.930  1.00 63.97           C  
ANISOU 8493  CB  PRO F  95     7294   7763   9248   1670    500   3333       C  
ATOM   8494  CG  PRO F  95     112.288 -68.760  33.487  1.00 67.02           C  
ANISOU 8494  CG  PRO F  95     7646   8183   9634   1644    531   3343       C  
ATOM   8495  CD  PRO F  95     112.505 -68.896  31.983  1.00 67.86           C  
ANISOU 8495  CD  PRO F  95     7699   8341   9743   1675    533   3339       C  
ATOM   8496  N   VAL F  96     110.889 -72.614  31.989  1.00 62.91           N  
ANISOU 8496  N   VAL F  96     7128   7654   9121   1767    451   3303       N  
ATOM   8497  CA  VAL F  96     110.235 -73.904  31.815  1.00 61.03           C  
ANISOU 8497  CA  VAL F  96     6909   7401   8880   1786    426   3267       C  
ATOM   8498  C   VAL F  96     111.249 -75.022  31.549  1.00 61.31           C  
ANISOU 8498  C   VAL F  96     6917   7470   8907   1830    376   3247       C  
ATOM   8499  O   VAL F  96     110.994 -76.206  31.866  1.00 59.89           O  
ANISOU 8499  O   VAL F  96     6762   7271   8724   1845    343   3218       O  
ATOM   8500  CB  VAL F  96     109.226 -73.876  30.657  1.00 60.86           C  
ANISOU 8500  CB  VAL F  96     6874   7387   8863   1788    452   3256       C  
ATOM   8501  CG1 VAL F  96     109.951 -73.973  29.303  1.00 62.82           C  
ANISOU 8501  CG1 VAL F  96     7061   7697   9111   1824    446   3255       C  
ATOM   8502  CG2 VAL F  96     108.218 -74.986  30.815  1.00 58.93           C  
ANISOU 8502  CG2 VAL F  96     6666   7109   8617   1792    436   3223       C  
ATOM   8503  N   ASN F  97     112.401 -74.653  30.991  1.00 59.02           N  
ANISOU 8503  N   ASN F  97     6577   7231   8617   1850    370   3260       N  
ATOM   8504  CA  ASN F  97     113.321 -75.649  30.505  1.00 59.44           C  
ANISOU 8504  CA  ASN F  97     6599   7325   8662   1890    326   3234       C  
ATOM   8505  C   ASN F  97     114.022 -76.346  31.655  1.00 60.25           C  
ANISOU 8505  C   ASN F  97     6727   7412   8755   1891    285   3218       C  
ATOM   8506  O   ASN F  97     114.293 -77.550  31.590  1.00 60.10           O  
ANISOU 8506  O   ASN F  97     6705   7398   8734   1927    244   3198       O  
ATOM   8507  CB  ASN F  97     114.314 -75.013  29.541  1.00 60.41           C  
ANISOU 8507  CB  ASN F  97     6664   7512   8778   1894    334   3229       C  
ATOM   8508  CG  ASN F  97     113.751 -74.874  28.137  1.00 59.53           C  
ANISOU 8508  CG  ASN F  97     6517   7428   8675   1913    358   3236       C  
ATOM   8509  OD1 ASN F  97     113.272 -75.853  27.546  1.00 58.58           O  
ANISOU 8509  OD1 ASN F  97     6394   7308   8557   1943    341   3217       O  
ATOM   8510  ND2 ASN F  97     113.807 -73.649  27.589  1.00 59.90           N  
ANISOU 8510  ND2 ASN F  97     6539   7499   8723   1889    398   3253       N  
ATOM   8511  N   PHE F  98     114.282 -75.593  32.721  1.00 58.18           N  
ANISOU 8511  N   PHE F  98     6490   7129   8488   1853    296   3227       N  
ATOM   8512  CA  PHE F  98     114.938 -76.137  33.913  1.00 58.63           C  
ANISOU 8512  CA  PHE F  98     6573   7169   8533   1849    260   3214       C  
ATOM   8513  C   PHE F  98     114.093 -77.253  34.541  1.00 57.84           C  
ANISOU 8513  C   PHE F  98     6518   7018   8440   1865    237   3212       C  
ATOM   8514  O   PHE F  98     114.616 -78.218  35.085  1.00 58.07           O  
ANISOU 8514  O   PHE F  98     6557   7044   8463   1884    195   3195       O  
ATOM   8515  CB  PHE F  98     115.203 -75.019  34.928  1.00 59.15           C  
ANISOU 8515  CB  PHE F  98     6661   7219   8594   1802    282   3227       C  
ATOM   8516  CG  PHE F  98     116.211 -74.037  34.465  1.00 60.18           C  
ANISOU 8516  CG  PHE F  98     6749   7399   8718   1787    297   3227       C  
ATOM   8517  CD1 PHE F  98     117.449 -73.974  35.052  1.00 61.38           C  
ANISOU 8517  CD1 PHE F  98     6891   7574   8856   1780    273   3213       C  
ATOM   8518  CD2 PHE F  98     115.937 -73.185  33.396  1.00 60.14           C  
ANISOU 8518  CD2 PHE F  98     6711   7419   8719   1781    335   3240       C  
ATOM   8519  CE1 PHE F  98     118.417 -73.070  34.579  1.00 62.55           C  
ANISOU 8519  CE1 PHE F  98     6997   7771   8997   1768    286   3212       C  
ATOM   8520  CE2 PHE F  98     116.891 -72.277  32.935  1.00 61.31           C  
ANISOU 8520  CE2 PHE F  98     6818   7616   8862   1768    348   3240       C  
ATOM   8521  CZ  PHE F  98     118.129 -72.221  33.526  1.00 62.52           C  
ANISOU 8521  CZ  PHE F  98     6961   7792   9001   1761    324   3226       C  
ATOM   8522  N   LYS F  99     112.777 -77.129  34.438  1.00 56.95           N  
ANISOU 8522  N   LYS F  99     6433   6870   8337   1851    265   3220       N  
ATOM   8523  CA  LYS F  99     111.884 -78.092  35.049  1.00 56.31           C  
ANISOU 8523  CA  LYS F  99     6399   6742   8254   1846    248   3195       C  
ATOM   8524  C   LYS F  99     111.852 -79.426  34.265  1.00 56.00           C  
ANISOU 8524  C   LYS F  99     6345   6721   8213   1884    214   3160       C  
ATOM   8525  O   LYS F  99     111.578 -80.505  34.820  1.00 55.99           O  
ANISOU 8525  O   LYS F  99     6375   6691   8208   1892    182   3136       O  
ATOM   8526  CB  LYS F  99     110.493 -77.465  35.183  1.00 55.68           C  
ANISOU 8526  CB  LYS F  99     6354   6623   8179   1808    291   3200       C  
ATOM   8527  CG  LYS F  99     110.318 -76.811  36.548  1.00 55.78           C  
ANISOU 8527  CG  LYS F  99     6410   6594   8190   1769    305   3219       C  
ATOM   8528  CD  LYS F  99     111.044 -77.679  37.602  1.00 56.08           C  
ANISOU 8528  CD  LYS F  99     6469   6620   8220   1782    259   3211       C  
ATOM   8529  CE  LYS F  99     111.257 -76.988  38.923  1.00 56.42           C  
ANISOU 8529  CE  LYS F  99     6543   6635   8259   1749    267   3233       C  
ATOM   8530  NZ  LYS F  99     109.997 -76.533  39.524  1.00 55.86           N  
ANISOU 8530  NZ  LYS F  99     6518   6517   8190   1709    299   3233       N  
ATOM   8531  N   LEU F 100     112.136 -79.345  32.971  1.00 59.75           N  
ANISOU 8531  N   LEU F 100     6771   7241   8690   1908    220   3155       N  
ATOM   8532  CA  LEU F 100     112.385 -80.533  32.179  1.00 60.04           C  
ANISOU 8532  CA  LEU F 100     6784   7305   8725   1948    184   3123       C  
ATOM   8533  C   LEU F 100     113.630 -81.259  32.696  1.00 60.85           C  
ANISOU 8533  C   LEU F 100     6877   7425   8820   1974    136   3113       C  
ATOM   8534  O   LEU F 100     113.573 -82.409  33.147  1.00 60.33           O  
ANISOU 8534  O   LEU F 100     6835   7338   8751   1988     99   3088       O  
ATOM   8535  CB  LEU F 100     112.587 -80.155  30.717  1.00 61.42           C  
ANISOU 8535  CB  LEU F 100     6904   7531   8901   1967    202   3123       C  
ATOM   8536  CG  LEU F 100     111.440 -79.422  30.053  1.00 61.20           C  
ANISOU 8536  CG  LEU F 100     6879   7493   8880   1945    250   3132       C  
ATOM   8537  CD1 LEU F 100     111.857 -78.841  28.723  1.00 63.25           C  
ANISOU 8537  CD1 LEU F 100     7081   7809   9142   1961    269   3141       C  
ATOM   8538  CD2 LEU F 100     110.333 -80.412  29.877  1.00 59.60           C  
ANISOU 8538  CD2 LEU F 100     6705   7261   8679   1949    241   3102       C  
ATOM   8539  N   LEU F 101     114.761 -80.570  32.646  1.00 56.93           N  
ANISOU 8539  N   LEU F 101     6344   6965   8320   1980    136   3134       N  
ATOM   8540  CA  LEU F 101     116.008 -81.178  33.039  1.00 57.54           C  
ANISOU 8540  CA  LEU F 101     6406   7066   8390   2006     92   3126       C  
ATOM   8541  C   LEU F 101     115.932 -81.585  34.500  1.00 57.50           C  
ANISOU 8541  C   LEU F 101     6452   7013   8382   1990     71   3127       C  
ATOM   8542  O   LEU F 101     116.531 -82.580  34.882  1.00 57.69           O  
ANISOU 8542  O   LEU F 101     6480   7039   8401   2013     27   3107       O  
ATOM   8543  CB  LEU F 101     117.171 -80.216  32.791  1.00 58.35           C  
ANISOU 8543  CB  LEU F 101     6469   7220   8483   1993    102   3128       C  
ATOM   8544  CG  LEU F 101     118.535 -80.580  33.346  1.00 59.08           C  
ANISOU 8544  CG  LEU F 101     6550   7338   8561   2000     63   3108       C  
ATOM   8545  CD1 LEU F 101     119.124 -81.742  32.562  1.00 59.18           C  
ANISOU 8545  CD1 LEU F 101     6528   7387   8572   2050     21   3081       C  
ATOM   8546  CD2 LEU F 101     119.423 -79.357  33.323  1.00 60.24           C  
ANISOU 8546  CD2 LEU F 101     6670   7522   8698   1970     85   3113       C  
ATOM   8547  N   SER F 102     115.188 -80.826  35.307  1.00 59.37           N  
ANISOU 8547  N   SER F 102     6729   7207   8622   1950    103   3149       N  
ATOM   8548  CA  SER F 102     114.974 -81.193  36.704  1.00 58.60           C  
ANISOU 8548  CA  SER F 102     6684   7061   8521   1932     86   3149       C  
ATOM   8549  C   SER F 102     114.433 -82.600  36.758  1.00 57.54           C  
ANISOU 8549  C   SER F 102     6574   6903   8385   1949     53   3114       C  
ATOM   8550  O   SER F 102     114.873 -83.435  37.541  1.00 57.56           O  
ANISOU 8550  O   SER F 102     6596   6893   8383   1960     14   3102       O  
ATOM   8551  CB  SER F 102     113.983 -80.262  37.401  1.00 57.71           C  
ANISOU 8551  CB  SER F 102     6612   6904   8412   1886    128   3171       C  
ATOM   8552  OG  SER F 102     114.587 -79.064  37.864  1.00 59.01           O  
ANISOU 8552  OG  SER F 102     6770   7079   8572   1857    151   3193       O  
ATOM   8553  N   HIS F 103     113.467 -82.855  35.894  1.00 57.39           N  
ANISOU 8553  N   HIS F 103     6554   6880   8371   1952     69   3097       N  
ATOM   8554  CA  HIS F 103     112.765 -84.129  35.860  1.00 56.78           C  
ANISOU 8554  CA  HIS F 103     6502   6777   8294   1965     42   3064       C  
ATOM   8555  C   HIS F 103     113.635 -85.217  35.231  1.00 57.05           C  
ANISOU 8555  C   HIS F 103     6502   6848   8326   2010     -3   3036       C  
ATOM   8556  O   HIS F 103     113.756 -86.304  35.778  1.00 56.98           O  
ANISOU 8556  O   HIS F 103     6515   6820   8315   2023    -42   3014       O  
ATOM   8557  CB  HIS F 103     111.433 -83.947  35.114  1.00 56.03           C  
ANISOU 8557  CB  HIS F 103     6415   6666   8206   1951     77   3057       C  
ATOM   8558  CG  HIS F 103     110.829 -85.214  34.604  1.00 55.45           C  
ANISOU 8558  CG  HIS F 103     6350   6585   8135   1973     52   3020       C  
ATOM   8559  ND1 HIS F 103     110.376 -86.214  35.437  1.00 55.10           N  
ANISOU 8559  ND1 HIS F 103     6349   6498   8089   1971     24   3002       N  
ATOM   8560  CD2 HIS F 103     110.581 -85.630  33.341  1.00 55.18           C  
ANISOU 8560  CD2 HIS F 103     6285   6577   8104   1996     52   3000       C  
ATOM   8561  CE1 HIS F 103     109.884 -87.199  34.706  1.00 54.98           C  
ANISOU 8561  CE1 HIS F 103     6330   6484   8077   1992      7   2971       C  
ATOM   8562  NE2 HIS F 103     110.000 -86.872  33.432  1.00 54.95           N  
ANISOU 8562  NE2 HIS F 103     6281   6521   8075   2008     23   2969       N  
ATOM   8563  N   CYS F 104     114.249 -84.919  34.096  1.00 57.74           N  
ANISOU 8563  N   CYS F 104     6536   6987   8414   2032      3   3035       N  
ATOM   8564  CA  CYS F 104     115.221 -85.838  33.544  1.00 58.27           C  
ANISOU 8564  CA  CYS F 104     6568   7094   8477   2073    -40   3009       C  
ATOM   8565  C   CYS F 104     116.297 -86.222  34.592  1.00 59.61           C  
ANISOU 8565  C   CYS F 104     6746   7263   8640   2082    -79   3012       C  
ATOM   8566  O   CYS F 104     116.671 -87.394  34.693  1.00 59.79           O  
ANISOU 8566  O   CYS F 104     6771   7286   8660   2108   -123   2983       O  
ATOM   8567  CB  CYS F 104     115.881 -85.240  32.304  1.00 58.61           C  
ANISOU 8567  CB  CYS F 104     6551   7198   8520   2091    -26   3014       C  
ATOM   8568  SG  CYS F 104     114.906 -85.341  30.825  1.00 57.20           S  
ANISOU 8568  SG  CYS F 104     6352   7034   8347   2099     -1   2996       S  
ATOM   8569  N   LEU F 105     116.778 -85.254  35.376  1.00 56.88           N  
ANISOU 8569  N   LEU F 105     6405   6914   8291   2060    -63   3044       N  
ATOM   8570  CA  LEU F 105     117.714 -85.556  36.453  1.00 57.93           C  
ANISOU 8570  CA  LEU F 105     6549   7043   8417   2064    -98   3049       C  
ATOM   8571  C   LEU F 105     117.077 -86.437  37.520  1.00 57.57           C  
ANISOU 8571  C   LEU F 105     6560   6942   8371   2054   -120   3036       C  
ATOM   8572  O   LEU F 105     117.781 -87.144  38.257  1.00 58.39           O  
ANISOU 8572  O   LEU F 105     6674   7042   8470   2067   -160   3027       O  
ATOM   8573  CB  LEU F 105     118.237 -84.285  37.088  1.00 59.02           C  
ANISOU 8573  CB  LEU F 105     6686   7187   8551   2034    -72   3080       C  
ATOM   8574  CG  LEU F 105     119.404 -83.756  36.281  1.00 60.08           C  
ANISOU 8574  CG  LEU F 105     6766   7386   8675   2040    -71   3067       C  
ATOM   8575  CD1 LEU F 105     119.516 -82.258  36.442  1.00 60.56           C  
ANISOU 8575  CD1 LEU F 105     6823   7457   8731   1996    -28   3085       C  
ATOM   8576  CD2 LEU F 105     120.693 -84.443  36.711  1.00 61.52           C  
ANISOU 8576  CD2 LEU F 105     6935   7594   8845   2059   -119   3044       C  
ATOM   8577  N   LEU F 106     115.749 -86.388  37.615  1.00 56.86           N  
ANISOU 8577  N   LEU F 106     6508   6811   8287   2029    -94   3035       N  
ATOM   8578  CA  LEU F 106     115.038 -87.245  38.557  1.00 56.40           C  
ANISOU 8578  CA  LEU F 106     6502   6700   8228   2019   -114   3021       C  
ATOM   8579  C   LEU F 106     114.820 -88.646  37.978  1.00 56.04           C  
ANISOU 8579  C   LEU F 106     6453   6654   8184   2050   -150   2982       C  
ATOM   8580  O   LEU F 106     115.001 -89.651  38.680  1.00 56.05           O  
ANISOU 8580  O   LEU F 106     6479   6634   8183   2061   -189   2965       O  
ATOM   8581  CB  LEU F 106     113.720 -86.596  38.973  1.00 55.80           C  
ANISOU 8581  CB  LEU F 106     6467   6579   8155   1978    -72   3035       C  
ATOM   8582  CG  LEU F 106     113.957 -85.565  40.079  1.00 56.17           C  
ANISOU 8582  CG  LEU F 106     6534   6609   8198   1945    -52   3069       C  
ATOM   8583  CD1 LEU F 106     112.698 -84.928  40.521  1.00 55.60           C  
ANISOU 8583  CD1 LEU F 106     6503   6495   8129   1905    -12   3080       C  
ATOM   8584  CD2 LEU F 106     114.626 -86.186  41.281  1.00 57.11           C  
ANISOU 8584  CD2 LEU F 106     6678   6712   8309   1949    -91   3068       C  
ATOM   8585  N   VAL F 107     114.454 -88.710  36.700  1.00 58.45           N  
ANISOU 8585  N   VAL F 107     6729   6984   8494   2065   -136   2967       N  
ATOM   8586  CA  VAL F 107     114.351 -89.990  36.009  1.00 58.50           C  
ANISOU 8586  CA  VAL F 107     6726   6997   8503   2097   -170   2929       C  
ATOM   8587  C   VAL F 107     115.689 -90.718  36.063  1.00 58.78           C  
ANISOU 8587  C   VAL F 107     6736   7065   8534   2132   -218   2913       C  
ATOM   8588  O   VAL F 107     115.740 -91.901  36.406  1.00 58.89           O  
ANISOU 8588  O   VAL F 107     6768   7061   8548   2148   -259   2888       O  
ATOM   8589  CB  VAL F 107     113.930 -89.824  34.541  1.00 58.36           C  
ANISOU 8589  CB  VAL F 107     6674   7011   8491   2109   -148   2917       C  
ATOM   8590  CG1 VAL F 107     114.091 -91.124  33.804  1.00 58.47           C  
ANISOU 8590  CG1 VAL F 107     6670   7039   8506   2147   -187   2877       C  
ATOM   8591  CG2 VAL F 107     112.514 -89.327  34.447  1.00 58.08           C  
ANISOU 8591  CG2 VAL F 107     6666   6941   8461   2079   -106   2926       C  
ATOM   8592  N   THR F 108     116.761 -89.988  35.741  1.00 59.66           N  
ANISOU 8592  N   THR F 108     6805   7223   8641   2141   -213   2929       N  
ATOM   8593  CA  THR F 108     118.126 -90.526  35.702  1.00 61.26           C  
ANISOU 8593  CA  THR F 108     6975   7463   8837   2173   -255   2916       C  
ATOM   8594  C   THR F 108     118.583 -91.102  37.030  1.00 61.56           C  
ANISOU 8594  C   THR F 108     7047   7473   8871   2171   -291   2917       C  
ATOM   8595  O   THR F 108     119.077 -92.233  37.083  1.00 62.52           O  
ANISOU 8595  O   THR F 108     7165   7598   8990   2199   -336   2889       O  
ATOM   8596  CB  THR F 108     119.152 -89.458  35.295  1.00 62.40           C  
ANISOU 8596  CB  THR F 108     7071   7660   8977   2176   -238   2939       C  
ATOM   8597  OG1 THR F 108     119.069 -89.219  33.887  1.00 63.01           O  
ANISOU 8597  OG1 THR F 108     7106   7779   9057   2191   -220   2929       O  
ATOM   8598  CG2 THR F 108     120.566 -89.932  35.616  1.00 63.99           C  
ANISOU 8598  CG2 THR F 108     7250   7894   9171   2203   -282   2930       C  
ATOM   8599  N   LEU F 109     118.449 -90.317  38.097  1.00 58.24           N  
ANISOU 8599  N   LEU F 109     6656   7025   8448   2139   -270   2948       N  
ATOM   8600  CA  LEU F 109     118.813 -90.799  39.424  1.00 59.12           C  
ANISOU 8600  CA  LEU F 109     6802   7107   8554   2134   -301   2952       C  
ATOM   8601  C   LEU F 109     117.984 -92.006  39.821  1.00 58.41           C  
ANISOU 8601  C   LEU F 109     6754   6971   8467   2136   -326   2926       C  
ATOM   8602  O   LEU F 109     118.467 -92.893  40.512  1.00 59.12           O  
ANISOU 8602  O   LEU F 109     6860   7050   8554   2150   -368   2913       O  
ATOM   8603  CB  LEU F 109     118.631 -89.712  40.463  1.00 59.61           C  
ANISOU 8603  CB  LEU F 109     6893   7144   8613   2095   -271   2989       C  
ATOM   8604  CG  LEU F 109     119.703 -88.649  40.478  1.00 60.93           C  
ANISOU 8604  CG  LEU F 109     7025   7351   8776   2093   -258   3017       C  
ATOM   8605  CD1 LEU F 109     119.487 -87.764  41.682  1.00 61.30           C  
ANISOU 8605  CD1 LEU F 109     7108   7365   8819   2054   -234   3049       C  
ATOM   8606  CD2 LEU F 109     121.019 -89.335  40.546  1.00 62.32           C  
ANISOU 8606  CD2 LEU F 109     7173   7561   8945   2127   -305   3003       C  
ATOM   8607  N   ALA F 110     116.724 -92.030  39.395  1.00 60.44           N  
ANISOU 8607  N   ALA F 110     7031   7203   8731   2122   -300   2919       N  
ATOM   8608  CA  ALA F 110     115.860 -93.153  39.726  1.00 60.28           C  
ANISOU 8608  CA  ALA F 110     7050   7138   8714   2122   -322   2895       C  
ATOM   8609  C   ALA F 110     116.472 -94.410  39.146  1.00 61.57           C  
ANISOU 8609  C   ALA F 110     7191   7324   8880   2164   -370   2859       C  
ATOM   8610  O   ALA F 110     116.793 -95.334  39.889  1.00 62.59           O  
ANISOU 8610  O   ALA F 110     7341   7434   9007   2174   -410   2846       O  
ATOM   8611  CB  ALA F 110     114.462 -92.939  39.205  1.00 58.90           C  
ANISOU 8611  CB  ALA F 110     6894   6940   8547   2103   -286   2892       C  
ATOM   8612  N   ALA F 111     116.693 -94.410  37.834  1.00 59.81           N  
ANISOU 8612  N   ALA F 111     6922   7143   8659   2187   -365   2844       N  
ATOM   8613  CA  ALA F 111     117.221 -95.581  37.138  1.00 61.12           C  
ANISOU 8613  CA  ALA F 111     7063   7332   8827   2227   -408   2806       C  
ATOM   8614  C   ALA F 111     118.479 -96.160  37.802  1.00 62.51           C  
ANISOU 8614  C   ALA F 111     7233   7522   8997   2248   -454   2800       C  
ATOM   8615  O   ALA F 111     118.554 -97.363  38.062  1.00 63.51           O  
ANISOU 8615  O   ALA F 111     7374   7631   9126   2267   -496   2773       O  
ATOM   8616  CB  ALA F 111     117.505 -95.241  35.690  1.00 61.59           C  
ANISOU 8616  CB  ALA F 111     7069   7444   8888   2247   -393   2796       C  
ATOM   8617  N   HIS F 112     119.450 -95.304  38.101  1.00 60.68           N  
ANISOU 8617  N   HIS F 112     6978   7320   8757   2245   -447   2824       N  
ATOM   8618  CA  HIS F 112     120.734 -95.792  38.589  1.00 61.94           C  
ANISOU 8618  CA  HIS F 112     7123   7501   8910   2267   -490   2817       C  
ATOM   8619  C   HIS F 112     120.724 -96.082  40.079  1.00 62.53           C  
ANISOU 8619  C   HIS F 112     7246   7532   8982   2250   -509   2830       C  
ATOM   8620  O   HIS F 112     121.612 -96.785  40.556  1.00 63.43           O  
ANISOU 8620  O   HIS F 112     7356   7653   9091   2271   -551   2818       O  
ATOM   8621  CB  HIS F 112     121.864 -94.806  38.269  1.00 63.02           C  
ANISOU 8621  CB  HIS F 112     7213   7692   9040   2273   -478   2836       C  
ATOM   8622  CG  HIS F 112     122.136 -94.663  36.805  1.00 62.74           C  
ANISOU 8622  CG  HIS F 112     7125   7708   9006   2296   -469   2820       C  
ATOM   8623  ND1 HIS F 112     123.192 -95.284  36.183  1.00 63.35           N  
ANISOU 8623  ND1 HIS F 112     7160   7831   9079   2332   -505   2793       N  
ATOM   8624  CD2 HIS F 112     121.478 -93.984  35.836  1.00 61.95           C  
ANISOU 8624  CD2 HIS F 112     7007   7621   8910   2287   -428   2825       C  
ATOM   8625  CE1 HIS F 112     123.179 -94.988  34.896  1.00 62.97           C  
ANISOU 8625  CE1 HIS F 112     7071   7823   9033   2344   -486   2782       C  
ATOM   8626  NE2 HIS F 112     122.147 -94.204  34.656  1.00 62.12           N  
ANISOU 8626  NE2 HIS F 112     6977   7697   8930   2318   -440   2802       N  
ATOM   8627  N   LEU F 113     119.746 -95.585  40.825  1.00 63.24           N  
ANISOU 8627  N   LEU F 113     7378   7577   9073   2214   -479   2852       N  
ATOM   8628  CA  LEU F 113     119.838 -95.724  42.274  1.00 63.42           C  
ANISOU 8628  CA  LEU F 113     7443   7563   9090   2197   -495   2868       C  
ATOM   8629  C   LEU F 113     118.598 -96.194  42.989  1.00 63.16           C  
ANISOU 8629  C   LEU F 113     7467   7470   9061   2173   -491   2865       C  
ATOM   8630  O   LEU F 113     118.180 -95.559  43.958  1.00 62.56           O  
ANISOU 8630  O   LEU F 113     7425   7364   8981   2140   -469   2892       O  
ATOM   8631  CB  LEU F 113     120.210 -94.387  42.889  1.00 62.61           C  
ANISOU 8631  CB  LEU F 113     7340   7469   8981   2170   -464   2907       C  
ATOM   8632  CG  LEU F 113     121.656 -94.099  43.266  1.00 63.37           C  
ANISOU 8632  CG  LEU F 113     7407   7602   9068   2183   -485   2920       C  
ATOM   8633  CD1 LEU F 113     122.525 -93.743  42.047  1.00 63.59           C  
ANISOU 8633  CD1 LEU F 113     7373   7692   9096   2209   -482   2913       C  
ATOM   8634  CD2 LEU F 113     121.657 -92.987  44.311  1.00 64.33           C  
ANISOU 8634  CD2 LEU F 113     7552   7707   9185   2147   -457   2959       C  
ATOM   8635  N   PRO F 114     118.058 -97.348  42.587  1.00 66.02           N  
ANISOU 8635  N   PRO F 114     7839   7815   9429   2191   -515   2833       N  
ATOM   8636  CA  PRO F 114     116.786 -97.805  43.147  1.00 65.89           C  
ANISOU 8636  CA  PRO F 114     7875   7744   9418   2168   -510   2829       C  
ATOM   8637  C   PRO F 114     116.692 -97.754  44.663  1.00 66.16           C  
ANISOU 8637  C   PRO F 114     7955   7739   9445   2142   -516   2849       C  
ATOM   8638  O   PRO F 114     115.663 -97.364  45.159  1.00 65.64           O  
ANISOU 8638  O   PRO F 114     7926   7636   9379   2110   -487   2862       O  
ATOM   8639  CB  PRO F 114     116.705 -99.246  42.662  1.00 67.43           C  
ANISOU 8639  CB  PRO F 114     8067   7933   9619   2200   -551   2790       C  
ATOM   8640  CG  PRO F 114     117.386 -99.211  41.334  1.00 67.62           C  
ANISOU 8640  CG  PRO F 114     8036   8011   9646   2231   -555   2773       C  
ATOM   8641  CD  PRO F 114     118.538 -98.254  41.525  1.00 67.26           C  
ANISOU 8641  CD  PRO F 114     7960   8005   9592   2231   -546   2798       C  
ATOM   8642  N   ALA F 115     117.726 -98.103  45.395  1.00 60.54           N  
ANISOU 8642  N   ALA F 115     7241   7035   8726   2155   -551   2852       N  
ATOM   8643  CA  ALA F 115     117.571 -98.227  46.838  1.00 60.60           C  
ANISOU 8643  CA  ALA F 115     7295   7002   8727   2132   -561   2867       C  
ATOM   8644  C   ALA F 115     117.415 -96.929  47.619  1.00 60.49           C  
ANISOU 8644  C   ALA F 115     7299   6979   8707   2094   -522   2905       C  
ATOM   8645  O   ALA F 115     116.843 -96.964  48.700  1.00 60.46           O  
ANISOU 8645  O   ALA F 115     7339   6934   8698   2068   -519   2916       O  
ATOM   8646  CB  ALA F 115     118.732 -98.987  47.405  1.00 60.90           C  
ANISOU 8646  CB  ALA F 115     7327   7053   8760   2157   -611   2859       C  
ATOM   8647  N   GLU F 116     117.953 -95.808  47.120  1.00 62.35           N  
ANISOU 8647  N   GLU F 116     7499   7252   8941   2091   -493   2924       N  
ATOM   8648  CA  GLU F 116     117.917 -94.522  47.860  1.00 61.59           C  
ANISOU 8648  CA  GLU F 116     7415   7149   8838   2056   -456   2961       C  
ATOM   8649  C   GLU F 116     116.731 -93.640  47.482  1.00 60.00           C  
ANISOU 8649  C   GLU F 116     7225   6930   8641   2025   -404   2972       C  
ATOM   8650  O   GLU F 116     116.466 -92.641  48.122  1.00 59.48           O  
ANISOU 8650  O   GLU F 116     7178   6850   8571   1992   -371   2999       O  
ATOM   8651  CB  GLU F 116     119.212 -93.703  47.653  1.00 61.75           C  
ANISOU 8651  CB  GLU F 116     7391   7218   8853   2067   -454   2979       C  
ATOM   8652  CG  GLU F 116     120.425 -94.243  48.372  1.00 62.19           C  
ANISOU 8652  CG  GLU F 116     7441   7288   8901   2086   -499   2978       C  
ATOM   8653  CD  GLU F 116     120.985 -95.478  47.665  1.00 62.98           C  
ANISOU 8653  CD  GLU F 116     7514   7410   9004   2129   -544   2943       C  
ATOM   8654  OE1 GLU F 116     120.729 -95.588  46.438  1.00 63.22           O  
ANISOU 8654  OE1 GLU F 116     7516   7461   9042   2146   -535   2924       O  
ATOM   8655  OE2 GLU F 116     121.661 -96.337  48.312  1.00 63.50           O  
ANISOU 8655  OE2 GLU F 116     7588   7473   9066   2146   -588   2932       O  
ATOM   8656  N   PHE F 117     116.001 -94.044  46.460  1.00 57.06           N  
ANISOU 8656  N   PHE F 117     6845   6559   8278   2036   -396   2950       N  
ATOM   8657  CA  PHE F 117     114.973 -93.238  45.823  1.00 56.28           C  
ANISOU 8657  CA  PHE F 117     6746   6453   8183   2014   -348   2957       C  
ATOM   8658  C   PHE F 117     113.624 -93.363  46.548  1.00 55.81           C  
ANISOU 8658  C   PHE F 117     6742   6340   8125   1981   -331   2957       C  
ATOM   8659  O   PHE F 117     112.559 -93.176  45.953  1.00 55.12           O  
ANISOU 8659  O   PHE F 117     6661   6240   8043   1968   -302   2951       O  
ATOM   8660  CB  PHE F 117     114.839 -93.610  44.355  1.00 55.78           C  
ANISOU 8660  CB  PHE F 117     6646   6418   8129   2041   -348   2933       C  
ATOM   8661  CG  PHE F 117     114.419 -92.470  43.492  1.00 55.27           C  
ANISOU 8661  CG  PHE F 117     6559   6373   8069   2027   -298   2948       C  
ATOM   8662  CD1 PHE F 117     115.361 -91.623  42.946  1.00 55.50           C  
ANISOU 8662  CD1 PHE F 117     6543   6448   8096   2036   -285   2964       C  
ATOM   8663  CD2 PHE F 117     113.079 -92.225  43.239  1.00 55.00           C  
ANISOU 8663  CD2 PHE F 117     6548   6311   8040   2003   -264   2946       C  
ATOM   8664  CE1 PHE F 117     114.973 -90.553  42.153  1.00 55.16           C  
ANISOU 8664  CE1 PHE F 117     6478   6423   8058   2023   -239   2979       C  
ATOM   8665  CE2 PHE F 117     112.698 -91.152  42.458  1.00 54.82           C  
ANISOU 8665  CE2 PHE F 117     6504   6306   8021   1990   -219   2961       C  
ATOM   8666  CZ  PHE F 117     113.644 -90.319  41.915  1.00 54.90           C  
ANISOU 8666  CZ  PHE F 117     6469   6361   8030   1999   -206   2977       C  
ATOM   8667  N   THR F 118     113.683 -93.776  47.807  1.00 53.93           N  
ANISOU 8667  N   THR F 118     6541   6071   7879   1969   -354   2962       N  
ATOM   8668  CA  THR F 118     112.524 -93.801  48.687  1.00 53.78           C  
ANISOU 8668  CA  THR F 118     6575   6002   7858   1935   -339   2966       C  
ATOM   8669  C   THR F 118     111.787 -92.496  48.580  1.00 53.54           C  
ANISOU 8669  C   THR F 118     6550   5966   7828   1900   -284   2987       C  
ATOM   8670  O   THR F 118     112.422 -91.478  48.303  1.00 53.56           O  
ANISOU 8670  O   THR F 118     6523   5998   7830   1897   -262   3007       O  
ATOM   8671  CB  THR F 118     112.936 -93.956  50.155  1.00 54.73           C  
ANISOU 8671  CB  THR F 118     6728   6100   7968   1922   -361   2979       C  
ATOM   8672  OG1 THR F 118     113.534 -92.730  50.619  1.00 54.22           O  
ANISOU 8672  OG1 THR F 118     6654   6050   7897   1903   -336   3010       O  
ATOM   8673  CG2 THR F 118     113.932 -95.101  50.307  1.00 56.70           C  
ANISOU 8673  CG2 THR F 118     6966   6362   8216   1958   -416   2963       C  
ATOM   8674  N   PRO F 119     110.451 -92.501  48.797  1.00 51.47           N  
ANISOU 8674  N   PRO F 119     6815   6818   5925    873   1317   1079       N  
ATOM   8675  CA  PRO F 119     109.657 -91.286  48.621  1.00 51.54           C  
ANISOU 8675  CA  PRO F 119     6803   6790   5988    839   1311   1120       C  
ATOM   8676  C   PRO F 119     110.242 -90.069  49.343  1.00 51.62           C  
ANISOU 8676  C   PRO F 119     6798   6792   6024    836   1309   1112       C  
ATOM   8677  O   PRO F 119     110.406 -89.038  48.695  1.00 51.76           O  
ANISOU 8677  O   PRO F 119     6784   6820   6061    796   1296   1138       O  
ATOM   8678  CB  PRO F 119     108.317 -91.683  49.209  1.00 51.38           C  
ANISOU 8678  CB  PRO F 119     6811   6713   5999    858   1324   1132       C  
ATOM   8679  CG  PRO F 119     108.244 -93.096  48.960  1.00 51.28           C  
ANISOU 8679  CG  PRO F 119     6821   6718   5945    881   1330   1116       C  
ATOM   8680  CD  PRO F 119     109.601 -93.602  49.255  1.00 51.31           C  
ANISOU 8680  CD  PRO F 119     6828   6767   5899    906   1331   1071       C  
ATOM   8681  N   ALA F 120     110.633 -90.226  50.609  1.00 50.02           N  
ANISOU 8681  N   ALA F 120     6615   6574   5817    877   1321   1076       N  
ATOM   8682  CA  ALA F 120     111.279 -89.152  51.365  1.00 50.34           C  
ANISOU 8682  CA  ALA F 120     6642   6608   5876    878   1320   1064       C  
ATOM   8683  C   ALA F 120     112.405 -88.475  50.585  1.00 50.19           C  
ANISOU 8683  C   ALA F 120     6590   6641   5840    846   1304   1064       C  
ATOM   8684  O   ALA F 120     112.545 -87.257  50.617  1.00 50.28           O  
ANISOU 8684  O   ALA F 120     6577   6644   5883    821   1297   1080       O  
ATOM   8685  CB  ALA F 120     111.809 -89.675  52.688  1.00 51.44           C  
ANISOU 8685  CB  ALA F 120     6808   6740   5997    929   1334   1018       C  
ATOM   8686  N   VAL F 121     113.208 -89.243  49.868  1.00 50.30           N  
ANISOU 8686  N   VAL F 121     6600   6708   5803    846   1298   1048       N  
ATOM   8687  CA  VAL F 121     114.333 -88.652  49.149  1.00 51.03           C  
ANISOU 8687  CA  VAL F 121     6661   6851   5876    817   1284   1046       C  
ATOM   8688  C   VAL F 121     113.817 -87.999  47.892  1.00 50.84           C  
ANISOU 8688  C   VAL F 121     6610   6833   5875    765   1270   1093       C  
ATOM   8689  O   VAL F 121     114.293 -86.933  47.491  1.00 51.34           O  
ANISOU 8689  O   VAL F 121     6643   6912   5953    733   1258   1107       O  
ATOM   8690  CB  VAL F 121     115.396 -89.693  48.805  1.00 51.37           C  
ANISOU 8690  CB  VAL F 121     6710   6951   5856    834   1282   1012       C  
ATOM   8691  CG1 VAL F 121     116.540 -89.046  48.095  1.00 52.14           C  
ANISOU 8691  CG1 VAL F 121     6776   7100   5936    805   1268   1010       C  
ATOM   8692  CG2 VAL F 121     115.841 -90.379  50.068  1.00 51.51           C  
ANISOU 8692  CG2 VAL F 121     6758   6961   5853    887   1297    966       C  
ATOM   8693  N   HIS F 122     112.818 -88.636  47.290  1.00 53.72           N  
ANISOU 8693  N   HIS F 122     6985   7184   6244    757   1271   1117       N  
ATOM   8694  CA  HIS F 122     112.231 -88.115  46.068  1.00 53.21           C  
ANISOU 8694  CA  HIS F 122     6896   7123   6200    709   1258   1163       C  
ATOM   8695  C   HIS F 122     111.723 -86.691  46.294  1.00 52.96           C  
ANISOU 8695  C   HIS F 122     6845   7053   6225    683   1254   1193       C  
ATOM   8696  O   HIS F 122     111.822 -85.813  45.422  1.00 52.91           O  
ANISOU 8696  O   HIS F 122     6807   7062   6234    640   1240   1222       O  
ATOM   8697  CB  HIS F 122     111.089 -88.997  45.584  1.00 52.92           C  
ANISOU 8697  CB  HIS F 122     6876   7066   6164    709   1262   1184       C  
ATOM   8698  CG  HIS F 122     110.632 -88.657  44.202  1.00 52.68           C  
ANISOU 8698  CG  HIS F 122     6822   7049   6145    661   1249   1227       C  
ATOM   8699  ND1 HIS F 122     109.340 -88.859  43.777  1.00 52.60           N  
ANISOU 8699  ND1 HIS F 122     6819   7006   6161    648   1250   1261       N  
ATOM   8700  CD2 HIS F 122     111.301 -88.135  43.146  1.00 52.69           C  
ANISOU 8700  CD2 HIS F 122     6791   7094   6134    623   1233   1241       C  
ATOM   8701  CE1 HIS F 122     109.231 -88.465  42.520  1.00 52.57           C  
ANISOU 8701  CE1 HIS F 122     6788   7025   6161    603   1236   1295       C  
ATOM   8702  NE2 HIS F 122     110.405 -88.020  42.114  1.00 52.61           N  
ANISOU 8702  NE2 HIS F 122     6770   7077   6144    587   1225   1283       N  
ATOM   8703  N   ALA F 123     111.176 -86.483  47.487  1.00 50.30           N  
ANISOU 8703  N   ALA F 123     6527   6666   5919    710   1267   1186       N  
ATOM   8704  CA  ALA F 123     110.774 -85.171  47.954  1.00 50.35           C  
ANISOU 8704  CA  ALA F 123     6519   6633   5978    693   1266   1207       C  
ATOM   8705  C   ALA F 123     111.954 -84.192  47.922  1.00 50.92           C  
ANISOU 8705  C   ALA F 123     6563   6737   6046    676   1256   1196       C  
ATOM   8706  O   ALA F 123     112.007 -83.307  47.069  1.00 51.01           O  
ANISOU 8706  O   ALA F 123     6544   6762   6075    633   1242   1226       O  
ATOM   8707  CB  ALA F 123     110.203 -85.283  49.351  1.00 50.72           C  
ANISOU 8707  CB  ALA F 123     6594   6627   6050    733   1282   1191       C  
ATOM   8708  N   SER F 124     112.917 -84.396  48.821  1.00 48.47           N  
ANISOU 8708  N   SER F 124     6264   6442   5712    710   1262   1153       N  
ATOM   8709  CA  SER F 124     114.021 -83.469  48.993  1.00 48.61           C  
ANISOU 8709  CA  SER F 124     6257   6484   5727    700   1255   1140       C  
ATOM   8710  C   SER F 124     114.923 -83.419  47.776  1.00 48.75           C  
ANISOU 8710  C   SER F 124     6248   6562   5711    668   1239   1144       C  
ATOM   8711  O   SER F 124     115.611 -82.448  47.571  1.00 48.88           O  
ANISOU 8711  O   SER F 124     6238   6598   5736    644   1229   1148       O  
ATOM   8712  CB  SER F 124     114.820 -83.821  50.240  1.00 48.54           C  
ANISOU 8712  CB  SER F 124     6269   6478   5697    746   1266   1091       C  
ATOM   8713  OG  SER F 124     114.732 -85.197  50.536  1.00 48.41           O  
ANISOU 8713  OG  SER F 124     6283   6465   5645    784   1277   1065       O  
ATOM   8714  N   LEU F 125     114.914 -84.433  46.934  1.00 49.24           N  
ANISOU 8714  N   LEU F 125     6317   6655   5738    666   1236   1144       N  
ATOM   8715  CA  LEU F 125     115.747 -84.316  45.740  1.00 49.67           C  
ANISOU 8715  CA  LEU F 125     6344   6767   5763    633   1221   1151       C  
ATOM   8716  C   LEU F 125     115.093 -83.324  44.797  1.00 49.51           C  
ANISOU 8716  C   LEU F 125     6295   6736   5782    582   1209   1200       C  
ATOM   8717  O   LEU F 125     115.769 -82.559  44.110  1.00 50.06           O  
ANISOU 8717  O   LEU F 125     6334   6837   5848    550   1195   1211       O  
ATOM   8718  CB  LEU F 125     115.978 -85.678  45.046  1.00 49.43           C  
ANISOU 8718  CB  LEU F 125     6326   6775   5680    644   1221   1137       C  
ATOM   8719  CG  LEU F 125     117.274 -86.425  45.462  1.00 50.03           C  
ANISOU 8719  CG  LEU F 125     6413   6894   5703    677   1224   1087       C  
ATOM   8720  CD1 LEU F 125     117.466 -87.782  44.774  1.00 49.79           C  
ANISOU 8720  CD1 LEU F 125     6395   6901   5621    688   1224   1075       C  
ATOM   8721  CD2 LEU F 125     118.479 -85.532  45.238  1.00 50.91           C  
ANISOU 8721  CD2 LEU F 125     6494   7044   5805    657   1213   1079       C  
ATOM   8722  N   ASP F 126     113.763 -83.333  44.789  1.00 52.97           N  
ANISOU 8722  N   ASP F 126     6744   7127   6256    577   1214   1231       N  
ATOM   8723  CA  ASP F 126     112.982 -82.457  43.914  1.00 52.80           C  
ANISOU 8723  CA  ASP F 126     6697   7090   6273    530   1203   1280       C  
ATOM   8724  C   ASP F 126     112.998 -81.010  44.389  1.00 53.28           C  
ANISOU 8724  C   ASP F 126     6739   7125   6380    512   1200   1294       C  
ATOM   8725  O   ASP F 126     113.050 -80.076  43.580  1.00 53.75           O  
ANISOU 8725  O   ASP F 126     6768   7197   6459    470   1187   1324       O  
ATOM   8726  CB  ASP F 126     111.539 -82.937  43.829  1.00 51.96           C  
ANISOU 8726  CB  ASP F 126     6611   6941   6192    532   1210   1307       C  
ATOM   8727  CG  ASP F 126     110.672 -82.002  43.011  1.00 51.88           C  
ANISOU 8727  CG  ASP F 126     6576   6910   6225    485   1200   1358       C  
ATOM   8728  OD1 ASP F 126     110.184 -80.970  43.567  1.00 52.13           O  
ANISOU 8728  OD1 ASP F 126     6601   6900   6305    477   1202   1375       O  
ATOM   8729  OD2 ASP F 126     110.494 -82.298  41.801  1.00 51.73           O  
ANISOU 8729  OD2 ASP F 126     6546   6917   6193    457   1190   1381       O  
ATOM   8730  N   LYS F 127     112.900 -80.850  45.708  1.00 51.25           N  
ANISOU 8730  N   LYS F 127     6500   6831   6142    546   1212   1273       N  
ATOM   8731  CA  LYS F 127     113.018 -79.558  46.340  1.00 51.98           C  
ANISOU 8731  CA  LYS F 127     6577   6899   6273    536   1211   1279       C  
ATOM   8732  C   LYS F 127     114.380 -79.004  45.965  1.00 53.08           C  
ANISOU 8732  C   LYS F 127     6690   7090   6389    520   1200   1264       C  
ATOM   8733  O   LYS F 127     114.476 -77.865  45.461  1.00 53.77           O  
ANISOU 8733  O   LYS F 127     6747   7180   6503    481   1188   1290       O  
ATOM   8734  CB  LYS F 127     112.843 -79.660  47.858  1.00 52.12           C  
ANISOU 8734  CB  LYS F 127     6622   6875   6305    581   1227   1251       C  
ATOM   8735  CG  LYS F 127     111.381 -79.886  48.265  1.00 51.36           C  
ANISOU 8735  CG  LYS F 127     6548   6721   6247    591   1238   1273       C  
ATOM   8736  CD  LYS F 127     111.210 -80.177  49.758  1.00 51.72           C  
ANISOU 8736  CD  LYS F 127     6624   6727   6301    639   1254   1242       C  
ATOM   8737  CE  LYS F 127     111.369 -78.922  50.604  1.00 52.82           C  
ANISOU 8737  CE  LYS F 127     6751   6838   6479    636   1255   1242       C  
ATOM   8738  NZ  LYS F 127     111.269 -79.217  52.068  1.00 53.28           N  
ANISOU 8738  NZ  LYS F 127     6839   6861   6544    684   1272   1211       N  
ATOM   8739  N   PHE F 128     115.422 -79.817  46.165  1.00 49.47           N  
ANISOU 8739  N   PHE F 128     6243   6673   5881    547   1202   1223       N  
ATOM   8740  CA  PHE F 128     116.783 -79.408  45.822  1.00 50.13           C  
ANISOU 8740  CA  PHE F 128     6302   6808   5936    534   1192   1205       C  
ATOM   8741  C   PHE F 128     116.894 -78.932  44.366  1.00 50.18           C  
ANISOU 8741  C   PHE F 128     6276   6848   5941    484   1175   1239       C  
ATOM   8742  O   PHE F 128     117.340 -77.824  44.135  1.00 50.57           O  
ANISOU 8742  O   PHE F 128     6298   6908   6010    455   1165   1251       O  
ATOM   8743  CB  PHE F 128     117.792 -80.536  46.096  1.00 50.37           C  
ANISOU 8743  CB  PHE F 128     6351   6880   5909    571   1197   1158       C  
ATOM   8744  CG  PHE F 128     119.154 -80.302  45.483  1.00 50.99           C  
ANISOU 8744  CG  PHE F 128     6404   7018   5952    554   1184   1143       C  
ATOM   8745  CD1 PHE F 128     120.084 -79.518  46.128  1.00 51.59           C  
ANISOU 8745  CD1 PHE F 128     6469   7103   6031    559   1183   1121       C  
ATOM   8746  CD2 PHE F 128     119.482 -80.855  44.265  1.00 50.96           C  
ANISOU 8746  CD2 PHE F 128     6389   7060   5912    533   1174   1151       C  
ATOM   8747  CE1 PHE F 128     121.303 -79.278  45.565  1.00 52.15           C  
ANISOU 8747  CE1 PHE F 128     6516   7228   6071    543   1172   1109       C  
ATOM   8748  CE2 PHE F 128     120.685 -80.633  43.703  1.00 51.51           C  
ANISOU 8748  CE2 PHE F 128     6436   7183   5951    517   1163   1138       C  
ATOM   8749  CZ  PHE F 128     121.607 -79.845  44.348  1.00 52.11           C  
ANISOU 8749  CZ  PHE F 128     6500   7268   6030    522   1162   1117       C  
ATOM   8750  N   LEU F 129     116.482 -79.712  43.380  1.00 51.20           N  
ANISOU 8750  N   LEU F 129     6408   6995   6051    471   1171   1255       N  
ATOM   8751  CA  LEU F 129     116.499 -79.174  42.022  1.00 51.17           C  
ANISOU 8751  CA  LEU F 129     6372   7019   6051    421   1154   1291       C  
ATOM   8752  C   LEU F 129     115.507 -78.015  41.819  1.00 50.93           C  
ANISOU 8752  C   LEU F 129     6325   6946   6080    387   1150   1336       C  
ATOM   8753  O   LEU F 129     115.711 -77.161  40.940  1.00 51.00           O  
ANISOU 8753  O   LEU F 129     6303   6975   6101    344   1136   1363       O  
ATOM   8754  CB  LEU F 129     116.191 -80.249  41.006  1.00 50.95           C  
ANISOU 8754  CB  LEU F 129     6352   7016   5992    414   1151   1300       C  
ATOM   8755  CG  LEU F 129     117.039 -81.485  41.130  1.00 51.14           C  
ANISOU 8755  CG  LEU F 129     6394   7079   5957    448   1156   1259       C  
ATOM   8756  CD1 LEU F 129     116.481 -82.493  40.176  1.00 50.86           C  
ANISOU 8756  CD1 LEU F 129     6367   7058   5899    440   1154   1274       C  
ATOM   8757  CD2 LEU F 129     118.476 -81.144  40.795  1.00 51.59           C  
ANISOU 8757  CD2 LEU F 129     6428   7191   5982    437   1146   1238       C  
ATOM   8758  N   ALA F 130     114.415 -78.000  42.585  1.00 50.72           N  
ANISOU 8758  N   ALA F 130     6318   6863   6090    403   1161   1346       N  
ATOM   8759  CA  ALA F 130     113.572 -76.829  42.584  1.00 50.54           C  
ANISOU 8759  CA  ALA F 130     6280   6798   6124    375   1158   1385       C  
ATOM   8760  C   ALA F 130     114.443 -75.649  43.012  1.00 50.90           C  
ANISOU 8760  C   ALA F 130     6304   6852   6185    365   1153   1376       C  
ATOM   8761  O   ALA F 130     114.738 -74.740  42.219  1.00 51.01           O  
ANISOU 8761  O   ALA F 130     6286   6886   6211    324   1140   1399       O  
ATOM   8762  CB  ALA F 130     112.407 -77.006  43.496  1.00 50.21           C  
ANISOU 8762  CB  ALA F 130     6266   6696   6117    399   1172   1391       C  
ATOM   8763  N   SER F 131     114.897 -75.711  44.259  1.00 50.51           N  
ANISOU 8763  N   SER F 131     6271   6788   6131    403   1164   1339       N  
ATOM   8764  CA  SER F 131     115.683 -74.642  44.847  1.00 50.97           C  
ANISOU 8764  CA  SER F 131     6312   6849   6204    400   1161   1327       C  
ATOM   8765  C   SER F 131     116.787 -74.192  43.914  1.00 51.39           C  
ANISOU 8765  C   SER F 131     6334   6959   6233    369   1146   1327       C  
ATOM   8766  O   SER F 131     117.032 -73.013  43.773  1.00 51.64           O  
ANISOU 8766  O   SER F 131     6339   6989   6291    340   1138   1344       O  
ATOM   8767  CB  SER F 131     116.272 -75.086  46.181  1.00 51.20           C  
ANISOU 8767  CB  SER F 131     6366   6871   6215    449   1174   1279       C  
ATOM   8768  OG  SER F 131     116.636 -73.975  46.982  1.00 51.52           O  
ANISOU 8768  OG  SER F 131     6395   6894   6286    450   1175   1273       O  
ATOM   8769  N   VAL F 132     117.446 -75.121  43.247  1.00 52.14           N  
ANISOU 8769  N   VAL F 132     6430   7102   6277    373   1142   1310       N  
ATOM   8770  CA  VAL F 132     118.487 -74.715  42.316  1.00 52.76           C  
ANISOU 8770  CA  VAL F 132     6479   7236   6331    342   1127   1312       C  
ATOM   8771  C   VAL F 132     117.857 -74.130  41.059  1.00 52.57           C  
ANISOU 8771  C   VAL F 132     6429   7213   6331    292   1114   1361       C  
ATOM   8772  O   VAL F 132     118.232 -73.044  40.617  1.00 53.04           O  
ANISOU 8772  O   VAL F 132     6458   7286   6409    258   1103   1379       O  
ATOM   8773  CB  VAL F 132     119.428 -75.888  41.953  1.00 52.96           C  
ANISOU 8773  CB  VAL F 132     6513   7315   6294    361   1126   1278       C  
ATOM   8774  CG1 VAL F 132     120.141 -75.641  40.619  1.00 53.40           C  
ANISOU 8774  CG1 VAL F 132     6538   7425   6326    321   1110   1293       C  
ATOM   8775  CG2 VAL F 132     120.424 -76.104  43.078  1.00 53.43           C  
ANISOU 8775  CG2 VAL F 132     6587   7385   6329    401   1135   1230       C  
ATOM   8776  N   SER F 133     116.880 -74.832  40.491  1.00 56.08           N  
ANISOU 8776  N   SER F 133     6885   7645   6776    287   1116   1383       N  
ATOM   8777  CA  SER F 133     116.360 -74.411  39.193  1.00 56.48           C  
ANISOU 8777  CA  SER F 133     6912   7704   6842    239   1103   1428       C  
ATOM   8778  C   SER F 133     115.724 -73.040  39.312  1.00 57.05           C  
ANISOU 8778  C   SER F 133     6966   7738   6974    211   1100   1463       C  
ATOM   8779  O   SER F 133     115.697 -72.291  38.339  1.00 58.19           O  
ANISOU 8779  O   SER F 133     7080   7896   7132    168   1087   1495       O  
ATOM   8780  CB  SER F 133     115.360 -75.415  38.631  1.00 55.00           C  
ANISOU 8780  CB  SER F 133     6743   7507   6649    241   1106   1446       C  
ATOM   8781  OG  SER F 133     115.945 -76.160  37.584  1.00 55.34           O  
ANISOU 8781  OG  SER F 133     6779   7603   6645    230   1098   1441       O  
ATOM   8782  N   THR F 134     115.230 -72.713  40.507  1.00 55.71           N  
ANISOU 8782  N   THR F 134     6812   7517   6837    235   1111   1455       N  
ATOM   8783  CA  THR F 134     114.777 -71.358  40.793  1.00 56.56           C  
ANISOU 8783  CA  THR F 134     6903   7589   7000    212   1109   1482       C  
ATOM   8784  C   THR F 134     115.894 -70.321  40.680  1.00 58.78           C  
ANISOU 8784  C   THR F 134     7153   7900   7279    192   1099   1476       C  
ATOM   8785  O   THR F 134     115.755 -69.367  39.918  1.00 60.05           O  
ANISOU 8785  O   THR F 134     7286   8065   7467    149   1088   1510       O  
ATOM   8786  CB  THR F 134     114.170 -71.264  42.189  1.00 55.81           C  
ANISOU 8786  CB  THR F 134     6833   7438   6936    247   1124   1470       C  
ATOM   8787  OG1 THR F 134     112.983 -72.061  42.229  1.00 53.96           O  
ANISOU 8787  OG1 THR F 134     6623   7170   6711    260   1133   1483       O  
ATOM   8788  CG2 THR F 134     113.824 -69.814  42.530  1.00 56.89           C  
ANISOU 8788  CG2 THR F 134     6950   7539   7128    224   1122   1495       C  
ATOM   8789  N   VAL F 135     116.988 -70.531  41.426  1.00 55.60           N  
ANISOU 8789  N   VAL F 135     6758   7520   6848    221   1103   1432       N  
ATOM   8790  CA  VAL F 135     118.076 -69.547  41.592  1.00 55.74           C  
ANISOU 8790  CA  VAL F 135     6751   7561   6867    209   1096   1420       C  
ATOM   8791  C   VAL F 135     118.665 -69.091  40.262  1.00 55.91           C  
ANISOU 8791  C   VAL F 135     6738   7630   6874    165   1079   1440       C  
ATOM   8792  O   VAL F 135     119.011 -67.926  40.099  1.00 56.04           O  
ANISOU 8792  O   VAL F 135     6727   7650   6914    137   1071   1455       O  
ATOM   8793  CB  VAL F 135     119.210 -70.101  42.501  1.00 55.80           C  
ANISOU 8793  CB  VAL F 135     6774   7593   6835    251   1104   1366       C  
ATOM   8794  CG1 VAL F 135     120.446 -69.230  42.420  1.00 56.39           C  
ANISOU 8794  CG1 VAL F 135     6822   7704   6901    235   1094   1353       C  
ATOM   8795  CG2 VAL F 135     118.731 -70.212  43.943  1.00 55.73           C  
ANISOU 8795  CG2 VAL F 135     6793   7533   6847    292   1120   1346       C  
ATOM   8796  N   LEU F 136     118.734 -70.002  39.303  1.00 57.58           N  
ANISOU 8796  N   LEU F 136     6951   7877   7048    158   1074   1443       N  
ATOM   8797  CA  LEU F 136     119.186 -69.658  37.966  1.00 59.10           C  
ANISOU 8797  CA  LEU F 136     7113   8114   7228    115   1058   1465       C  
ATOM   8798  C   LEU F 136     118.177 -68.779  37.263  1.00 59.47           C  
ANISOU 8798  C   LEU F 136     7140   8133   7322     73   1051   1517       C  
ATOM   8799  O   LEU F 136     118.531 -67.810  36.588  1.00 61.59           O  
ANISOU 8799  O   LEU F 136     7378   8420   7604     35   1038   1538       O  
ATOM   8800  CB  LEU F 136     119.438 -70.910  37.144  1.00 58.38           C  
ANISOU 8800  CB  LEU F 136     7031   8065   7086    120   1055   1456       C  
ATOM   8801  CG  LEU F 136     120.378 -71.861  37.859  1.00 57.66           C  
ANISOU 8801  CG  LEU F 136     6962   8000   6948    164   1063   1404       C  
ATOM   8802  CD1 LEU F 136     120.487 -73.178  37.115  1.00 57.56           C  
ANISOU 8802  CD1 LEU F 136     6962   8023   6887    172   1062   1395       C  
ATOM   8803  CD2 LEU F 136     121.736 -71.204  37.995  1.00 59.90           C  
ANISOU 8803  CD2 LEU F 136     7224   8320   7215    160   1057   1381       C  
ATOM   8804  N   THR F 137     116.910 -69.104  37.444  1.00 60.05           N  
ANISOU 8804  N   THR F 137     7233   8162   7422     80   1058   1537       N  
ATOM   8805  CA  THR F 137     115.837 -68.369  36.777  1.00 60.23           C  
ANISOU 8805  CA  THR F 137     7239   8155   7489     41   1052   1587       C  
ATOM   8806  C   THR F 137     115.407 -67.000  37.392  1.00 61.28           C  
ANISOU 8806  C   THR F 137     7360   8244   7680     27   1053   1607       C  
ATOM   8807  O   THR F 137     114.957 -66.109  36.671  1.00 62.49           O  
ANISOU 8807  O   THR F 137     7489   8390   7866    -14   1044   1647       O  
ATOM   8808  CB  THR F 137     114.625 -69.253  36.694  1.00 57.97           C  
ANISOU 8808  CB  THR F 137     6978   7839   7209     53   1060   1602       C  
ATOM   8809  OG1 THR F 137     114.402 -69.836  37.982  1.00 56.42           O  
ANISOU 8809  OG1 THR F 137     6815   7609   7013    100   1076   1572       O  
ATOM   8810  CG2 THR F 137     114.909 -70.335  35.689  1.00 57.41           C  
ANISOU 8810  CG2 THR F 137     6910   7814   7090     49   1054   1598       C  
ATOM   8811  N   SER F 138     115.576 -66.814  38.697  1.00 59.90           N  
ANISOU 8811  N   SER F 138     7201   8042   7518     60   1064   1580       N  
ATOM   8812  CA  SER F 138     114.983 -65.666  39.346  1.00 59.93           C  
ANISOU 8812  CA  SER F 138     7197   7996   7576     51   1067   1600       C  
ATOM   8813  C   SER F 138     115.537 -64.347  38.857  1.00 62.76           C  
ANISOU 8813  C   SER F 138     7519   8372   7955     12   1054   1618       C  
ATOM   8814  O   SER F 138     114.984 -63.307  39.171  1.00 63.81           O  
ANISOU 8814  O   SER F 138     7642   8467   8137     -4   1055   1642       O  
ATOM   8815  CB  SER F 138     115.139 -65.761  40.859  1.00 60.02           C  
ANISOU 8815  CB  SER F 138     7233   7978   7594     96   1082   1564       C  
ATOM   8816  OG  SER F 138     116.469 -65.560  41.248  1.00 60.85           O  
ANISOU 8816  OG  SER F 138     7330   8118   7672    108   1080   1529       O  
ATOM   8817  N   LYS F 139     116.625 -64.364  38.100  1.00 64.27           N  
ANISOU 8817  N   LYS F 139     7690   8619   8109     -4   1043   1608       N  
ATOM   8818  CA  LYS F 139     117.140 -63.126  37.495  1.00 67.24           C  
ANISOU 8818  CA  LYS F 139     8029   9015   8504    -46   1030   1629       C  
ATOM   8819  C   LYS F 139     116.664 -62.978  36.054  1.00 67.81           C  
ANISOU 8819  C   LYS F 139     8080   9104   8581    -90   1017   1671       C  
ATOM   8820  O   LYS F 139     117.166 -62.138  35.309  1.00 70.38           O  
ANISOU 8820  O   LYS F 139     8375   9456   8912   -127   1005   1689       O  
ATOM   8821  CB  LYS F 139     118.672 -63.052  37.580  1.00 69.16           C  
ANISOU 8821  CB  LYS F 139     8260   9308   8708    -39   1025   1593       C  
ATOM   8822  CG  LYS F 139     119.160 -62.900  39.010  1.00 69.53           C  
ANISOU 8822  CG  LYS F 139     8323   9336   8759      0   1036   1555       C  
ATOM   8823  CD  LYS F 139     120.660 -62.943  39.116  1.00 71.69           C  
ANISOU 8823  CD  LYS F 139     8587   9660   8991     10   1032   1517       C  
ATOM   8824  CE  LYS F 139     121.087 -62.808  40.560  1.00 71.79           C  
ANISOU 8824  CE  LYS F 139     8616   9651   9009     48   1044   1480       C  
ATOM   8825  NZ  LYS F 139     122.506 -62.335  40.640  1.00 72.91           N  
ANISOU 8825  NZ  LYS F 139     8740   9836   9128     46   1037   1453       N  
ATOM   8826  N   TYR F 140     115.751 -63.844  35.640  1.00 69.24           N  
ANISOU 8826  N   TYR F 140     8278   9273   8757    -87   1021   1687       N  
ATOM   8827  CA  TYR F 140     115.144 -63.707  34.329  1.00 69.71           C  
ANISOU 8827  CA  TYR F 140     8320   9342   8826   -129   1010   1729       C  
ATOM   8828  C   TYR F 140     114.410 -62.346  34.292  1.00 71.16           C  
ANISOU 8828  C   TYR F 140     8482   9486   9069   -162   1006   1770       C  
ATOM   8829  O   TYR F 140     114.064 -61.803  35.347  1.00 70.97           O  
ANISOU 8829  O   TYR F 140     8468   9419   9080   -145   1015   1765       O  
ATOM   8830  CB  TYR F 140     114.195 -64.886  34.070  1.00 67.00           C  
ANISOU 8830  CB  TYR F 140     8002   8984   8471   -115   1016   1737       C  
ATOM   8831  CG  TYR F 140     113.871 -65.194  32.625  1.00 67.38           C  
ANISOU 8831  CG  TYR F 140     8036   9060   8507   -149   1005   1769       C  
ATOM   8832  CD1 TYR F 140     114.845 -65.629  31.749  1.00 68.68           C  
ANISOU 8832  CD1 TYR F 140     8187   9284   8624   -160    995   1757       C  
ATOM   8833  CD2 TYR F 140     112.572 -65.093  32.155  1.00 66.54           C  
ANISOU 8833  CD2 TYR F 140     7930   8919   8433   -170   1004   1810       C  
ATOM   8834  CE1 TYR F 140     114.545 -65.924  30.425  1.00 69.25           C  
ANISOU 8834  CE1 TYR F 140     8247   9382   8684   -192    984   1785       C  
ATOM   8835  CE2 TYR F 140     112.260 -65.384  30.835  1.00 67.08           C  
ANISOU 8835  CE2 TYR F 140     7985   9011   8490   -201    994   1839       C  
ATOM   8836  CZ  TYR F 140     113.246 -65.796  29.974  1.00 68.45           C  
ANISOU 8836  CZ  TYR F 140     8145   9244   8617   -212    984   1827       C  
ATOM   8837  OH  TYR F 140     112.911 -66.077  28.663  1.00 69.19           O  
ANISOU 8837  OH  TYR F 140     8227   9362   8700   -244    974   1856       O  
ATOM   8838  N   ARG F 141     114.234 -61.769  33.102  1.00 69.52           N  
ANISOU 8838  N   ARG F 141     8247   9295   8873   -207    992   1807       N  
ATOM   8839  CA  ARG F 141     113.481 -60.529  32.936  1.00 71.24           C  
ANISOU 8839  CA  ARG F 141     8444   9477   9146   -241    988   1849       C  
ATOM   8840  C   ARG F 141     113.214 -60.328  31.459  1.00 72.83           C  
ANISOU 8840  C   ARG F 141     8621   9703   9348   -287    974   1888       C  
ATOM   8841  O   ARG F 141     113.522 -61.220  30.666  1.00 72.55           O  
ANISOU 8841  O   ARG F 141     8587   9707   9270   -289    969   1882       O  
ATOM   8842  CB  ARG F 141     114.230 -59.322  33.506  1.00 73.76           C  
ANISOU 8842  CB  ARG F 141     8744   9795   9486   -248    986   1840       C  
ATOM   8843  CG  ARG F 141     115.582 -59.040  32.823  1.00 76.54           C  
ANISOU 8843  CG  ARG F 141     9069  10207   9804   -268    973   1827       C  
ATOM   8844  CD  ARG F 141     116.345 -57.852  33.443  1.00 79.09           C  
ANISOU 8844  CD  ARG F 141     9374  10529  10148   -273    971   1816       C  
ATOM   8845  NE  ARG F 141     117.789 -57.987  33.237  1.00 82.78           N  
ANISOU 8845  NE  ARG F 141     9829  11053  10571   -270    965   1785       N  
ATOM   8846  CZ  ARG F 141     118.511 -57.259  32.384  1.00 85.70           C  
ANISOU 8846  CZ  ARG F 141    10166  11460  10936   -306    951   1797       C  
ATOM   8847  NH1 ARG F 141     117.928 -56.311  31.656  1.00 85.34           N  
ANISOU 8847  NH1 ARG F 141    10096  11402  10928   -348    942   1841       N  
ATOM   8848  NH2 ARG F 141     119.822 -57.476  32.268  1.00 89.16           N  
ANISOU 8848  NH2 ARG F 141    10596  11949  11331   -299    946   1766       N  
ATOM   8849  OXT ARG F 141     112.695 -59.285  31.034  1.00 74.65           O  
ANISOU 8849  OXT ARG F 141     8829   9914   9619   -323    967   1926       O  
TER    8850      ARG F 141                                                      
ATOM   8851  N   VAL G   1      99.185 -88.714  19.942  1.00104.33           N  
ANISOU 8851  N   VAL G   1    11829  15510  12301     46   -718  -2070       N  
ATOM   8852  CA  VAL G   1     100.172 -88.304  18.942  1.00107.26           C  
ANISOU 8852  CA  VAL G   1    12201  15911  12642     55   -697  -2059       C  
ATOM   8853  C   VAL G   1     100.686 -89.560  18.219  1.00109.51           C  
ANISOU 8853  C   VAL G   1    12472  16213  12923     55   -693  -2107       C  
ATOM   8854  O   VAL G   1     100.393 -90.687  18.635  1.00107.73           O  
ANISOU 8854  O   VAL G   1    12238  15971  12723     46   -705  -2144       O  
ATOM   8855  CB  VAL G   1     101.360 -87.465  19.594  1.00104.77           C  
ANISOU 8855  CB  VAL G   1    11896  15563  12348     49   -677  -2018       C  
ATOM   8856  CG1 VAL G   1     102.202 -88.304  20.553  1.00105.15           C  
ANISOU 8856  CG1 VAL G   1    11941  15566  12447     33   -673  -2036       C  
ATOM   8857  CG2 VAL G   1     102.245 -86.787  18.535  1.00106.02           C  
ANISOU 8857  CG2 VAL G   1    12057  15756  12471     61   -656  -1999       C  
ATOM   8858  N   HIS G   2     101.411 -89.361  17.118  1.00110.13           N  
ANISOU 8858  N   HIS G   2    12549  16327  12969     65   -676  -2105       N  
ATOM   8859  CA  HIS G   2     102.019 -90.458  16.365  1.00112.91           C  
ANISOU 8859  CA  HIS G   2    12889  16698  13315     66   -670  -2147       C  
ATOM   8860  C   HIS G   2     103.125 -91.134  17.164  1.00110.19           C  
ANISOU 8860  C   HIS G   2    12542  16311  13015     51   -660  -2160       C  
ATOM   8861  O   HIS G   2     103.838 -90.485  17.935  1.00107.55           O  
ANISOU 8861  O   HIS G   2    12216  15944  12704     45   -649  -2127       O  
ATOM   8862  CB  HIS G   2     102.595 -89.957  15.032  1.00117.65           C  
ANISOU 8862  CB  HIS G   2    13489  17344  13869     80   -653  -2138       C  
ATOM   8863  CG  HIS G   2     101.565 -89.434  14.077  1.00121.05           C  
ANISOU 8863  CG  HIS G   2    13920  17821  14251     94   -662  -2132       C  
ATOM   8864  ND1 HIS G   2     100.996 -90.217  13.094  1.00124.50           N  
ANISOU 8864  ND1 HIS G   2    14347  18298  14661    102   -671  -2170       N  
ATOM   8865  CD2 HIS G   2     101.014 -88.203  13.943  1.00121.73           C  
ANISOU 8865  CD2 HIS G   2    14017  17922  14313    103   -663  -2092       C  
ATOM   8866  CE1 HIS G   2     100.135 -89.494  12.401  1.00127.14           C  
ANISOU 8866  CE1 HIS G   2    14685  18668  14956    115   -677  -2154       C  
ATOM   8867  NE2 HIS G   2     100.126 -88.269  12.897  1.00125.50           N  
ANISOU 8867  NE2 HIS G   2    14490  18447  14749    116   -672  -2107       N  
ATOM   8868  N   LEU G   3     103.270 -92.438  16.966  1.00104.64           N  
ANISOU 8868  N   LEU G   3    11826  15610  12323     47   -664  -2207       N  
ATOM   8869  CA  LEU G   3     104.326 -93.197  17.623  1.00102.22           C  
ANISOU 8869  CA  LEU G   3    11516  15266  12057     34   -655  -2223       C  
ATOM   8870  C   LEU G   3     104.933 -94.190  16.646  1.00105.87           C  
ANISOU 8870  C   LEU G   3    11965  15755  12504     38   -648  -2264       C  
ATOM   8871  O   LEU G   3     104.214 -94.976  16.025  1.00109.64           O  
ANISOU 8871  O   LEU G   3    12433  16260  12964     42   -660  -2300       O  
ATOM   8872  CB  LEU G   3     103.784 -93.928  18.860  1.00 98.65           C  
ANISOU 8872  CB  LEU G   3    11061  14770  11651     20   -673  -2242       C  
ATOM   8873  CG  LEU G   3     104.493 -93.683  20.197  1.00 93.68           C  
ANISOU 8873  CG  LEU G   3    10440  14086  11070      5   -666  -2219       C  
ATOM   8874  CD1 LEU G   3     104.214 -92.279  20.708  1.00 92.26           C  
ANISOU 8874  CD1 LEU G   3    10274  13895  10887      8   -665  -2166       C  
ATOM   8875  CD2 LEU G   3     104.109 -94.725  21.238  1.00 90.98           C  
ANISOU 8875  CD2 LEU G   3    10092  13705  10772     -9   -682  -2249       C  
ATOM   8876  N   THR G   4     106.256 -94.153  16.512  1.00101.18           N  
ANISOU 8876  N   THR G   4    11372  15155  11916     36   -627  -2257       N  
ATOM   8877  CA  THR G   4     106.967 -95.127  15.682  1.00104.48           C  
ANISOU 8877  CA  THR G   4    11779  15594  12325     37   -618  -2296       C  
ATOM   8878  C   THR G   4     106.683 -96.531  16.211  1.00103.93           C  
ANISOU 8878  C   THR G   4    11698  15501  12288     26   -633  -2342       C  
ATOM   8879  O   THR G   4     106.571 -96.733  17.419  1.00100.04           O  
ANISOU 8879  O   THR G   4    11208  14965  11838     14   -640  -2340       O  
ATOM   8880  CB  THR G   4     108.510 -94.864  15.648  1.00103.88           C  
ANISOU 8880  CB  THR G   4    11705  15506  12257     35   -594  -2279       C  
ATOM   8881  OG1 THR G   4     109.195 -95.777  16.520  1.00101.28           O  
ANISOU 8881  OG1 THR G   4    11371  15135  11975     20   -592  -2302       O  
ATOM   8882  CG2 THR G   4     108.835 -93.422  16.044  1.00101.54           C  
ANISOU 8882  CG2 THR G   4    11423  15197  11959     37   -583  -2224       C  
ATOM   8883  N   PRO G   5     106.530 -97.501  15.305  1.00103.58           N  
ANISOU 8883  N   PRO G   5    11642  15489  12225     31   -636  -2385       N  
ATOM   8884  CA  PRO G   5     106.232 -98.887  15.699  1.00103.84           C  
ANISOU 8884  CA  PRO G   5    11664  15505  12286     22   -650  -2432       C  
ATOM   8885  C   PRO G   5     107.174 -99.462  16.776  1.00100.14           C  
ANISOU 8885  C   PRO G   5    11195  14986  11869      6   -644  -2439       C  
ATOM   8886  O   PRO G   5     106.711-100.157  17.689  1.00 98.01           O  
ANISOU 8886  O   PRO G   5    10921  14683  11634     -6   -658  -2459       O  
ATOM   8887  CB  PRO G   5     106.377 -99.652  14.380  1.00109.18           C  
ANISOU 8887  CB  PRO G   5    12329  16227  12929     31   -647  -2469       C  
ATOM   8888  CG  PRO G   5     105.973 -98.644  13.339  1.00112.17           C  
ANISOU 8888  CG  PRO G   5    12712  16651  13256     47   -643  -2444       C  
ATOM   8889  CD  PRO G   5     106.475 -97.311  13.844  1.00108.63           C  
ANISOU 8889  CD  PRO G   5    12278  16185  12813     47   -630  -2390       C  
ATOM   8890  N   GLU G   6     108.469 -99.167  16.679  1.00106.35           N  
ANISOU 8890  N   GLU G   6    11984  15766  12660      5   -622  -2424       N  
ATOM   8891  CA  GLU G   6     109.431 -99.644  17.673  1.00102.84           C  
ANISOU 8891  CA  GLU G   6    11539  15274  12263    -10   -615  -2428       C  
ATOM   8892  C   GLU G   6     109.353 -98.823  18.961  1.00 98.06           C  
ANISOU 8892  C   GLU G   6    10945  14623  11689    -19   -617  -2389       C  
ATOM   8893  O   GLU G   6     109.872 -99.238  20.000  1.00 95.35           O  
ANISOU 8893  O   GLU G   6    10603  14235  11391    -33   -615  -2393       O  
ATOM   8894  CB  GLU G   6     110.861 -99.612  17.125  1.00103.17           C  
ANISOU 8894  CB  GLU G   6    11579  15322  12297     -8   -591  -2425       C  
ATOM   8895  CG  GLU G   6     110.958 -99.740  15.618  1.00107.85           C  
ANISOU 8895  CG  GLU G   6    12165  15970  12842      6   -584  -2442       C  
ATOM   8896  CD  GLU G   6     110.834 -98.395  14.918  1.00108.31           C  
ANISOU 8896  CD  GLU G   6    12233  16061  12859     20   -575  -2400       C  
ATOM   8897  OE1 GLU G   6     109.802 -97.707  15.099  1.00106.59           O  
ANISOU 8897  OE1 GLU G   6    12022  15848  12630     24   -588  -2379       O  
ATOM   8898  OE2 GLU G   6     111.780 -98.020  14.196  1.00110.48           O  
ANISOU 8898  OE2 GLU G   6    12509  16355  13112     26   -556  -2388       O  
ATOM   8899  N   GLU G   7     108.725 -97.652  18.892  1.00 99.16           N  
ANISOU 8899  N   GLU G   7    11095  14776  11807    -11   -619  -2351       N  
ATOM   8900  CA  GLU G   7     108.402 -96.936  20.116  1.00 94.91           C  
ANISOU 8900  CA  GLU G   7    10567  14197  11296    -19   -625  -2317       C  
ATOM   8901  C   GLU G   7     107.288 -97.671  20.826  1.00 94.24           C  
ANISOU 8901  C   GLU G   7    10478  14094  11236    -27   -649  -2342       C  
ATOM   8902  O   GLU G   7     107.441 -98.062  21.981  1.00 91.17           O  
ANISOU 8902  O   GLU G   7    10090  13659  10892    -41   -653  -2346       O  
ATOM   8903  CB  GLU G   7     107.998 -95.493  19.840  1.00 94.71           C  
ANISOU 8903  CB  GLU G   7    10553  14191  11241     -9   -622  -2270       C  
ATOM   8904  CG  GLU G   7     109.156 -94.610  19.487  1.00 95.01           C  
ANISOU 8904  CG  GLU G   7    10599  14235  11266     -4   -598  -2236       C  
ATOM   8905  CD  GLU G   7     109.042 -93.256  20.128  1.00 91.61           C  
ANISOU 8905  CD  GLU G   7    10183  13787  10839     -4   -595  -2183       C  
ATOM   8906  OE1 GLU G   7     110.072 -92.727  20.620  1.00 90.00           O  
ANISOU 8906  OE1 GLU G   7     9985  13556  10653     -9   -579  -2156       O  
ATOM   8907  OE2 GLU G   7     107.914 -92.723  20.139  1.00 90.71           O  
ANISOU 8907  OE2 GLU G   7    10073  13684  10709      1   -609  -2170       O  
ATOM   8908  N   LYS G   8     106.185 -97.892  20.114  1.00 93.13           N  
ANISOU 8908  N   LYS G   8    10332  13988  11064    -18   -664  -2361       N  
ATOM   8909  CA  LYS G   8     105.016 -98.560  20.687  1.00 93.03           C  
ANISOU 8909  CA  LYS G   8    10316  13963  11070    -24   -687  -2385       C  
ATOM   8910  C   LYS G   8     105.387 -99.967  21.140  1.00 92.44           C  
ANISOU 8910  C   LYS G   8    10230  13862  11031    -36   -691  -2430       C  
ATOM   8911  O   LYS G   8     104.866-100.472  22.140  1.00 89.84           O  
ANISOU 8911  O   LYS G   8     9900  13499  10737    -47   -706  -2442       O  
ATOM   8912  CB  LYS G   8     103.853 -98.615  19.677  1.00 97.52           C  
ANISOU 8912  CB  LYS G   8    10880  14579  11596    -11   -701  -2401       C  
ATOM   8913  CG  LYS G   8     102.566 -99.248  20.230  1.00 97.62           C  
ANISOU 8913  CG  LYS G   8    10887  14580  11623    -16   -726  -2424       C  
ATOM   8914  CD  LYS G   8     101.573 -99.659  19.135  1.00102.13           C  
ANISOU 8914  CD  LYS G   8    11451  15199  12154     -4   -738  -2452       C  
ATOM   8915  CE  LYS G   8     100.838 -98.467  18.514  1.00106.10           C  
ANISOU 8915  CE  LYS G   8    11962  15737  12615      9   -740  -2419       C  
ATOM   8916  NZ  LYS G   8      99.868 -98.902  17.463  1.00107.91           N  
ANISOU 8916  NZ  LYS G   8    12183  16012  12806     20   -753  -2447       N  
ATOM   8917  N   SER G   9     106.300-100.595  20.406  1.00 92.66           N  
ANISOU 8917  N   SER G   9    10250  13907  11050    -34   -678  -2454       N  
ATOM   8918  CA  SER G   9     106.700-101.950  20.737  1.00 92.60           C  
ANISOU 8918  CA  SER G   9    10231  13878  11074    -45   -681  -2497       C  
ATOM   8919  C   SER G   9     107.516-101.965  22.024  1.00 88.15           C  
ANISOU 8919  C   SER G   9     9673  13259  10561    -60   -674  -2483       C  
ATOM   8920  O   SER G   9     107.288-102.796  22.900  1.00 86.31           O  
ANISOU 8920  O   SER G   9     9435  12992  10366    -72   -686  -2507       O  
ATOM   8921  CB  SER G   9     107.491-102.569  19.595  1.00 96.58           C  
ANISOU 8921  CB  SER G   9    10726  14415  11554    -38   -668  -2525       C  
ATOM   8922  OG  SER G   9     107.400-103.981  19.649  1.00 96.87           O  
ANISOU 8922  OG  SER G   9    10750  14445  11610    -45   -677  -2575       O  
ATOM   8923  N   ALA G  10     108.456-101.032  22.138  1.00 91.85           N  
ANISOU 8923  N   ALA G  10    10151  13719  11030    -59   -655  -2445       N  
ATOM   8924  CA  ALA G  10     109.273-100.909  23.341  1.00 87.79           C  
ANISOU 8924  CA  ALA G  10     9642  13152  10561    -73   -647  -2427       C  
ATOM   8925  C   ALA G  10     108.407-100.499  24.522  1.00 84.28           C  
ANISOU 8925  C   ALA G  10     9205  12673  10144    -81   -663  -2407       C  
ATOM   8926  O   ALA G  10     108.642-100.922  25.661  1.00 81.58           O  
ANISOU 8926  O   ALA G  10     8864  12286   9848    -95   -666  -2412       O  
ATOM   8927  CB  ALA G  10     110.400 -99.904  23.128  1.00 87.14           C  
ANISOU 8927  CB  ALA G  10     9568  13072  10469    -69   -624  -2388       C  
ATOM   8928  N   VAL G  11     107.405 -99.670  24.232  1.00 86.02           N  
ANISOU 8928  N   VAL G  11     9431  12916  10335    -71   -672  -2385       N  
ATOM   8929  CA  VAL G  11     106.457 -99.207  25.240  1.00 83.18           C  
ANISOU 8929  CA  VAL G  11     9079  12530   9996    -77   -688  -2364       C  
ATOM   8930  C   VAL G  11     105.593-100.354  25.753  1.00 83.52           C  
ANISOU 8930  C   VAL G  11     9114  12557  10063    -85   -709  -2405       C  
ATOM   8931  O   VAL G  11     105.574-100.630  26.954  1.00 80.70           O  
ANISOU 8931  O   VAL G  11     8759  12155   9750    -99   -716  -2405       O  
ATOM   8932  CB  VAL G  11     105.532 -98.085  24.699  1.00 83.84           C  
ANISOU 8932  CB  VAL G  11     9171  12647  10039    -64   -693  -2333       C  
ATOM   8933  CG1 VAL G  11     104.347 -97.882  25.628  1.00 81.43           C  
ANISOU 8933  CG1 VAL G  11     8870  12318   9752    -69   -714  -2324       C  
ATOM   8934  CG2 VAL G  11     106.294 -96.785  24.540  1.00 82.90           C  
ANISOU 8934  CG2 VAL G  11     9063  12531   9905    -58   -674  -2285       C  
ATOM   8935  N   THR G  12     104.896-101.036  24.849  1.00 81.49           N  
ANISOU 8935  N   THR G  12     8847  12337   9778    -78   -720  -2439       N  
ATOM   8936  CA  THR G  12     103.939-102.050  25.272  1.00 82.17           C  
ANISOU 8936  CA  THR G  12     8925  12413   9883    -84   -742  -2476       C  
ATOM   8937  C   THR G  12     104.663-103.196  25.966  1.00 81.27           C  
ANISOU 8937  C   THR G  12     8803  12262   9812    -99   -740  -2508       C  
ATOM   8938  O   THR G  12     104.220-103.676  27.017  1.00 79.19           O  
ANISOU 8938  O   THR G  12     8539  11962   9586   -110   -754  -2518       O  
ATOM   8939  CB  THR G  12     103.108-102.592  24.088  1.00 86.74           C  
ANISOU 8939  CB  THR G  12     9494  13041  10421    -73   -752  -2509       C  
ATOM   8940  OG1 THR G  12     103.837-102.406  22.868  1.00 88.89           O  
ANISOU 8940  OG1 THR G  12     9764  13353  10657    -61   -735  -2509       O  
ATOM   8941  CG2 THR G  12     101.751-101.870  23.999  1.00 89.18           C  
ANISOU 8941  CG2 THR G  12     9809  13369  10706    -65   -768  -2490       C  
ATOM   8942  N   ALA G  13     105.790-103.606  25.388  1.00 82.42           N  
ANISOU 8942  N   ALA G  13     8944  12418   9954    -98   -723  -2522       N  
ATOM   8943  CA  ALA G  13     106.581-104.709  25.934  1.00 81.93           C  
ANISOU 8943  CA  ALA G  13     8874  12324   9931   -110   -720  -2553       C  
ATOM   8944  C   ALA G  13     107.030-104.401  27.354  1.00 77.53           C  
ANISOU 8944  C   ALA G  13     8325  11711   9421   -125   -717  -2528       C  
ATOM   8945  O   ALA G  13     107.087-105.283  28.212  1.00 76.61           O  
ANISOU 8945  O   ALA G  13     8204  11559   9346   -138   -725  -2552       O  
ATOM   8946  CB  ALA G  13     107.786-105.000  25.050  1.00 84.06           C  
ANISOU 8946  CB  ALA G  13     9139  12614  10185   -106   -700  -2565       C  
ATOM   8947  N   LEU G  14     107.339-103.138  27.608  1.00 80.21           N  
ANISOU 8947  N   LEU G  14     8677  12042   9756   -122   -706  -2480       N  
ATOM   8948  CA  LEU G  14     107.747-102.752  28.945  1.00 76.21           C  
ANISOU 8948  CA  LEU G  14     8179  11484   9293   -135   -704  -2454       C  
ATOM   8949  C   LEU G  14     106.535-102.736  29.859  1.00 74.62           C  
ANISOU 8949  C   LEU G  14     7981  11261   9112   -141   -726  -2451       C  
ATOM   8950  O   LEU G  14     106.604-103.204  30.995  1.00 72.81           O  
ANISOU 8950  O   LEU G  14     7752  10987   8927   -155   -732  -2458       O  
ATOM   8951  CB  LEU G  14     108.442-101.392  28.939  1.00 74.26           C  
ANISOU 8951  CB  LEU G  14     7944  11236   9035   -130   -686  -2402       C  
ATOM   8952  CG  LEU G  14     109.430-101.229  30.096  1.00 70.55           C  
ANISOU 8952  CG  LEU G  14     7481  10715   8611   -144   -675  -2383       C  
ATOM   8953  CD1 LEU G  14     110.651-100.490  29.608  1.00 70.94           C  
ANISOU 8953  CD1 LEU G  14     7535  10774   8645   -138   -650  -2355       C  
ATOM   8954  CD2 LEU G  14     108.834-100.516  31.293  1.00 68.47           C  
ANISOU 8954  CD2 LEU G  14     7227  10415   8373   -151   -684  -2350       C  
ATOM   8955  N   TRP G  15     105.426-102.208  29.347  1.00 72.11           N  
ANISOU 8955  N   TRP G  15     7665  10974   8761   -130   -737  -2442       N  
ATOM   8956  CA  TRP G  15     104.195-102.101  30.116  1.00 71.91           C  
ANISOU 8956  CA  TRP G  15     7643  10931   8749   -134   -758  -2437       C  
ATOM   8957  C   TRP G  15     103.734-103.490  30.569  1.00 71.83           C  
ANISOU 8957  C   TRP G  15     7622  10904   8768   -145   -775  -2485       C  
ATOM   8958  O   TRP G  15     103.126-103.641  31.636  1.00 71.56           O  
ANISOU 8958  O   TRP G  15     7589  10834   8765   -155   -789  -2484       O  
ATOM   8959  CB  TRP G  15     103.105-101.400  29.292  1.00 72.11           C  
ANISOU 8959  CB  TRP G  15     7671  11000   8728   -120   -767  -2424       C  
ATOM   8960  CG  TRP G  15     101.925-100.864  30.132  1.00 71.88           C  
ANISOU 8960  CG  TRP G  15     7649  10952   8710   -123   -785  -2404       C  
ATOM   8961  CD1 TRP G  15     100.631-101.313  30.117  1.00 71.90           C  
ANISOU 8961  CD1 TRP G  15     7647  10965   8706   -122   -807  -2426       C  
ATOM   8962  CD2 TRP G  15     101.962 -99.798  31.096  1.00 71.59           C  
ANISOU 8962  CD2 TRP G  15     7625  10883   8693   -128   -783  -2358       C  
ATOM   8963  NE1 TRP G  15      99.881-100.597  31.001  1.00 71.65           N  
ANISOU 8963  NE1 TRP G  15     7624  10910   8689   -125   -818  -2396       N  
ATOM   8964  CE2 TRP G  15     100.673 -99.662  31.613  1.00 71.45           C  
ANISOU 8964  CE2 TRP G  15     7610  10859   8680   -129   -803  -2355       C  
ATOM   8965  CE3 TRP G  15     102.960 -98.953  31.563  1.00 71.44           C  
ANISOU 8965  CE3 TRP G  15     7616  10841   8687   -131   -765  -2320       C  
ATOM   8966  CZ2 TRP G  15     100.362 -98.722  32.577  1.00 71.17           C  
ANISOU 8966  CZ2 TRP G  15     7586  10794   8662   -133   -807  -2315       C  
ATOM   8967  CZ3 TRP G  15     102.644 -98.025  32.515  1.00 71.16           C  
ANISOU 8967  CZ3 TRP G  15     7592  10777   8669   -135   -768  -2281       C  
ATOM   8968  CH2 TRP G  15     101.366 -97.918  33.015  1.00 71.03           C  
ANISOU 8968  CH2 TRP G  15     7577  10754   8657   -137   -789  -2279       C  
ATOM   8969  N   GLY G  16     104.048-104.502  29.763  1.00 74.35           N  
ANISOU 8969  N   GLY G  16     7929  11246   9075   -142   -772  -2526       N  
ATOM   8970  CA  GLY G  16     103.826-105.880  30.154  1.00 75.78           C  
ANISOU 8970  CA  GLY G  16     8099  11409   9284   -152   -785  -2572       C  
ATOM   8971  C   GLY G  16     104.448-106.229  31.499  1.00 73.07           C  
ANISOU 8971  C   GLY G  16     7758  11009   8997   -169   -783  -2570       C  
ATOM   8972  O   GLY G  16     103.802-106.829  32.352  1.00 73.31           O  
ANISOU 8972  O   GLY G  16     7785  11011   9057   -179   -800  -2588       O  
ATOM   8973  N   LYS G  17     105.700-105.840  31.705  1.00 75.41           N  
ANISOU 8973  N   LYS G  17     8059  11288   9306   -173   -763  -2549       N  
ATOM   8974  CA  LYS G  17     106.401-106.189  32.938  1.00 74.04           C  
ANISOU 8974  CA  LYS G  17     7887  11060   9184   -189   -760  -2548       C  
ATOM   8975  C   LYS G  17     105.941-105.363  34.154  1.00 72.62           C  
ANISOU 8975  C   LYS G  17     7719  10842   9030   -196   -767  -2511       C  
ATOM   8976  O   LYS G  17     106.365-105.601  35.284  1.00 71.37           O  
ANISOU 8976  O   LYS G  17     7564  10638   8917   -210   -767  -2509       O  
ATOM   8977  CB  LYS G  17     107.916-106.036  32.745  1.00 73.93           C  
ANISOU 8977  CB  LYS G  17     7875  11041   9175   -190   -736  -2538       C  
ATOM   8978  CG  LYS G  17     108.490-106.808  31.555  1.00 75.29           C  
ANISOU 8978  CG  LYS G  17     8036  11248   9322   -183   -727  -2572       C  
ATOM   8979  CD  LYS G  17     110.019-106.825  31.589  1.00 74.97           C  
ANISOU 8979  CD  LYS G  17     7996  11192   9296   -187   -704  -2566       C  
ATOM   8980  CE  LYS G  17     110.618-107.628  30.440  1.00 76.18           C  
ANISOU 8980  CE  LYS G  17     8138  11380   9426   -181   -695  -2601       C  
ATOM   8981  NZ  LYS G  17     112.093-107.711  30.610  1.00 75.65           N  
ANISOU 8981  NZ  LYS G  17     8071  11293   9378   -186   -674  -2596       N  
ATOM   8982  N   VAL G  18     105.076-104.390  33.927  1.00 72.59           N  
ANISOU 8982  N   VAL G  18     7894   6798  12889   1049   -568   -385       N  
ATOM   8983  CA  VAL G  18     104.671-103.491  34.996  1.00 70.86           C  
ANISOU 8983  CA  VAL G  18     7648   6609  12666   1049   -511   -396       C  
ATOM   8984  C   VAL G  18     103.684-104.141  35.963  1.00 72.89           C  
ANISOU 8984  C   VAL G  18     7884   6897  12915   1027   -518   -353       C  
ATOM   8985  O   VAL G  18     102.601-104.558  35.548  1.00 76.04           O  
ANISOU 8985  O   VAL G  18     8269   7290  13331   1019   -539   -306       O  
ATOM   8986  CB  VAL G  18     104.021-102.214  34.420  1.00 70.35           C  
ANISOU 8986  CB  VAL G  18     7564   6534  12633   1066   -465   -399       C  
ATOM   8987  CG1 VAL G  18     103.373-101.390  35.535  1.00 69.42           C  
ANISOU 8987  CG1 VAL G  18     7414   6448  12514   1063   -409   -400       C  
ATOM   8988  CG2 VAL G  18     105.044-101.395  33.636  1.00 67.91           C  
ANISOU 8988  CG2 VAL G  18     7274   6199  12331   1089   -447   -447       C  
ATOM   8989  N   ASN G  19     104.029-104.185  37.252  1.00 66.61           N  
ANISOU 8989  N   ASN G  19     7083   6133  12092   1017   -500   -370       N  
ATOM   8990  CA  ASN G  19     103.117-104.774  38.236  1.00 68.71           C  
ANISOU 8990  CA  ASN G  19     7328   6430  12348    996   -505   -331       C  
ATOM   8991  C   ASN G  19     101.850-103.932  38.401  1.00 69.20           C  
ANISOU 8991  C   ASN G  19     7355   6503  12433    998   -461   -309       C  
ATOM   8992  O   ASN G  19     101.913-102.801  38.847  1.00 66.96           O  
ANISOU 8992  O   ASN G  19     7058   6232  12153   1008   -406   -337       O  
ATOM   8993  CB  ASN G  19     103.827-104.920  39.586  1.00 67.15           C  
ANISOU 8993  CB  ASN G  19     7133   6264  12116    985   -491   -358       C  
ATOM   8994  CG  ASN G  19     102.912-105.461  40.680  1.00 69.25           C  
ANISOU 8994  CG  ASN G  19     7376   6564  12371    964   -492   -321       C  
ATOM   8995  OD1 ASN G  19     101.808-105.911  40.408  1.00 72.12           O  
ANISOU 8995  OD1 ASN G  19     7726   6926  12751    955   -511   -273       O  
ATOM   8996  ND2 ASN G  19     103.386-105.437  41.921  1.00 68.07           N  
ANISOU 8996  ND2 ASN G  19     7225   6446  12194    955   -472   -343       N  
ATOM   8997  N   VAL G  20     100.692-104.516  38.114  1.00 66.73           N  
ANISOU 8997  N   VAL G  20     7029   6190  12137    987   -486   -256       N  
ATOM   8998  CA  VAL G  20      99.458-103.741  38.065  1.00 67.53           C  
ANISOU 8998  CA  VAL G  20     7097   6296  12264    991   -450   -232       C  
ATOM   8999  C   VAL G  20      98.777-103.681  39.407  1.00 68.29           C  
ANISOU 8999  C   VAL G  20     7168   6432  12348    976   -422   -217       C  
ATOM   9000  O   VAL G  20      97.766-102.996  39.554  1.00 68.97           O  
ANISOU 9000  O   VAL G  20     7226   6528  12453    978   -386   -199       O  
ATOM   9001  CB  VAL G  20      98.457-104.307  37.063  1.00 69.12           C  
ANISOU 9001  CB  VAL G  20     7295   6477  12491    987   -487   -182       C  
ATOM   9002  CG1 VAL G  20      99.084-104.433  35.685  1.00 68.96           C  
ANISOU 9002  CG1 VAL G  20     7301   6417  12484   1001   -518   -193       C  
ATOM   9003  CG2 VAL G  20      97.946-105.641  37.555  1.00 72.54           C  
ANISOU 9003  CG2 VAL G  20     7726   6925  12909    963   -533   -138       C  
ATOM   9004  N   ASP G  21      99.301-104.403  40.387  1.00 70.21           N  
ANISOU 9004  N   ASP G  21     7419   6698  12559    961   -438   -223       N  
ATOM   9005  CA  ASP G  21      98.739-104.309  41.728  1.00 70.62           C  
ANISOU 9005  CA  ASP G  21     7447   6789  12597    946   -409   -213       C  
ATOM   9006  C   ASP G  21      99.542-103.335  42.592  1.00 67.12           C  
ANISOU 9006  C   ASP G  21     7001   6364  12137    955   -356   -265       C  
ATOM   9007  O   ASP G  21      99.133-103.035  43.723  1.00 67.07           O  
ANISOU 9007  O   ASP G  21     6974   6390  12120    946   -322   -264       O  
ATOM   9008  CB  ASP G  21      98.681-105.685  42.415  1.00 73.34           C  
ANISOU 9008  CB  ASP G  21     7798   7151  12918    922   -455   -185       C  
ATOM   9009  CG  ASP G  21      97.640-106.629  41.797  1.00 77.43           C  
ANISOU 9009  CG  ASP G  21     8310   7657  13451    911   -501   -127       C  
ATOM   9010  OD1 ASP G  21      96.568-106.154  41.376  1.00 78.57           O  
ANISOU 9010  OD1 ASP G  21     8433   7797  13623    915   -484   -100       O  
ATOM   9011  OD2 ASP G  21      97.895-107.856  41.749  1.00 79.72           O  
ANISOU 9011  OD2 ASP G  21     8619   7945  13727    897   -555   -108       O  
ATOM   9012  N   GLU G  22     100.654-102.818  42.058  1.00 70.15           N  
ANISOU 9012  N   GLU G  22     7406   6727  12519    972   -348   -311       N  
ATOM   9013  CA  GLU G  22     101.515-101.915  42.836  1.00 66.94           C  
ANISOU 9013  CA  GLU G  22     7001   6338  12097    981   -300   -363       C  
ATOM   9014  C   GLU G  22     101.880-100.547  42.220  1.00 64.22           C  
ANISOU 9014  C   GLU G  22     6655   5975  11771   1005   -254   -402       C  
ATOM   9015  O   GLU G  22     101.687 -99.504  42.855  1.00 62.77           O  
ANISOU 9015  O   GLU G  22     6451   5810  11590   1011   -198   -422       O  
ATOM   9016  CB  GLU G  22     102.791-102.637  43.232  1.00 66.07           C  
ANISOU 9016  CB  GLU G  22     6919   6231  11954    974   -329   -391       C  
ATOM   9017  CG  GLU G  22     102.796-103.007  44.714  1.00 67.26           C  
ANISOU 9017  CG  GLU G  22     7060   6421  12074    956   -319   -390       C  
ATOM   9018  CD  GLU G  22     101.960-102.028  45.582  1.00 66.72           C  
ANISOU 9018  CD  GLU G  22     6956   6381  12012    955   -259   -389       C  
ATOM   9019  OE1 GLU G  22     102.173-100.784  45.531  1.00 64.38           O  
ANISOU 9019  OE1 GLU G  22     6653   6083  11727    972   -208   -423       O  
ATOM   9020  OE2 GLU G  22     101.078-102.529  46.322  1.00 68.86           O  
ANISOU 9020  OE2 GLU G  22     7208   6676  12278    938   -265   -352       O  
ATOM   9021  N   VAL G  23     102.473-100.566  41.033  1.00 62.30           N  
ANISOU 9021  N   VAL G  23     6435   5698  11540   1019   -277   -415       N  
ATOM   9022  CA  VAL G  23     103.011 -99.367  40.398  1.00 61.26           C  
ANISOU 9022  CA  VAL G  23     6307   5546  11423   1043   -239   -456       C  
ATOM   9023  C   VAL G  23     102.088 -98.172  40.430  1.00 61.72           C  
ANISOU 9023  C   VAL G  23     6335   5610  11506   1053   -184   -452       C  
ATOM   9024  O   VAL G  23     102.478 -97.111  40.896  1.00 61.03           O  
ANISOU 9024  O   VAL G  23     6240   5532  11415   1064   -133   -491       O  
ATOM   9025  CB  VAL G  23     103.365 -99.636  38.932  1.00 60.81           C  
ANISOU 9025  CB  VAL G  23     6274   5448  11383   1055   -277   -455       C  
ATOM   9026  CG1 VAL G  23     103.525 -98.347  38.161  1.00 60.08           C  
ANISOU 9026  CG1 VAL G  23     6179   5335  11315   1079   -236   -484       C  
ATOM   9027  CG2 VAL G  23     104.633-100.442  38.859  1.00 59.88           C  
ANISOU 9027  CG2 VAL G  23     6190   5322  11241   1052   -317   -479       C  
ATOM   9028  N   GLY G  24     100.862 -98.339  39.969  1.00 62.84           N  
ANISOU 9028  N   GLY G  24     6458   5745  11672   1049   -194   -405       N  
ATOM   9029  CA  GLY G  24      99.933 -97.226  39.932  1.00 62.99           C  
ANISOU 9029  CA  GLY G  24     6448   5769  11717   1058   -144   -399       C  
ATOM   9030  C   GLY G  24      99.752 -96.545  41.274  1.00 61.73           C  
ANISOU 9030  C   GLY G  24     6266   5646  11544   1053    -92   -415       C  
ATOM   9031  O   GLY G  24      99.694 -95.323  41.359  1.00 60.29           O  
ANISOU 9031  O   GLY G  24     6068   5465  11373   1068    -38   -440       O  
ATOM   9032  N   GLY G  25      99.701 -97.344  42.330  1.00 63.67           N  
ANISOU 9032  N   GLY G  25     6508   5919  11763   1033   -107   -401       N  
ATOM   9033  CA  GLY G  25      99.484 -96.826  43.664  1.00 62.95           C  
ANISOU 9033  CA  GLY G  25     6395   5865  11658   1026    -61   -412       C  
ATOM   9034  C   GLY G  25     100.735 -96.161  44.161  1.00 60.41           C  
ANISOU 9034  C   GLY G  25     6087   5550  11316   1036    -29   -471       C  
ATOM   9035  O   GLY G  25     100.683 -95.207  44.933  1.00 59.70           O  
ANISOU 9035  O   GLY G  25     5979   5481  11224   1040     25   -495       O  
ATOM   9036  N   GLU G  26     101.876 -96.648  43.710  1.00 65.18           N  
ANISOU 9036  N   GLU G  26     6722   6136  11906   1040    -62   -496       N  
ATOM   9037  CA  GLU G  26     103.110 -96.005  44.132  1.00 62.78           C  
ANISOU 9037  CA  GLU G  26     6433   5837  11584   1050    -33   -553       C  
ATOM   9038  C   GLU G  26     103.274 -94.648  43.462  1.00 61.24           C  
ANISOU 9038  C   GLU G  26     6233   5623  11412   1074     13   -585       C  
ATOM   9039  O   GLU G  26     103.767 -93.719  44.099  1.00 59.75           O  
ANISOU 9039  O   GLU G  26     6039   5449  11215   1082     62   -625       O  
ATOM   9040  CB  GLU G  26     104.320 -96.870  43.840  1.00 62.23           C  
ANISOU 9040  CB  GLU G  26     6398   5753  11492   1048    -80   -572       C  
ATOM   9041  CG  GLU G  26     105.549 -96.382  44.556  1.00 60.31           C  
ANISOU 9041  CG  GLU G  26     6168   5524  11224   1053    -51   -627       C  
ATOM   9042  CD  GLU G  26     106.757 -97.326  44.396  1.00 59.93           C  
ANISOU 9042  CD  GLU G  26     6154   5464  11151   1050    -99   -645       C  
ATOM   9043  OE1 GLU G  26     106.512 -98.563  44.144  1.00 61.59           O  
ANISOU 9043  OE1 GLU G  26     6374   5670  11357   1035   -155   -608       O  
ATOM   9044  OE2 GLU G  26     107.925 -96.800  44.520  1.00 58.13           O  
ANISOU 9044  OE2 GLU G  26     5942   5234  10909   1061    -80   -696       O  
ATOM   9045  N   ALA G  27     102.851 -94.540  42.194  1.00 57.40           N  
ANISOU 9045  N   ALA G  27     5749   5105  10955   1085     -3   -566       N  
ATOM   9046  CA  ALA G  27     102.934 -93.286  41.458  1.00 56.94           C  
ANISOU 9046  CA  ALA G  27     5687   5027  10922   1108     38   -593       C  
ATOM   9047  C   ALA G  27     102.048 -92.300  42.166  1.00 57.28           C  
ANISOU 9047  C   ALA G  27     5695   5092  10975   1109     96   -589       C  
ATOM   9048  O   ALA G  27     102.421 -91.145  42.343  1.00 56.83           O  
ANISOU 9048  O   ALA G  27     5632   5038  10923   1124    146   -628       O  
ATOM   9049  CB  ALA G  27     102.528 -93.443  40.000  1.00 56.98           C  
ANISOU 9049  CB  ALA G  27     5699   4995  10956   1118      7   -568       C  
ATOM   9050  N   LEU G  28     100.885 -92.746  42.618  1.00 57.19           N  
ANISOU 9050  N   LEU G  28     5661   5099  10969   1094     89   -543       N  
ATOM   9051  CA  LEU G  28      99.927 -91.806  43.206  1.00 57.56           C  
ANISOU 9051  CA  LEU G  28     5674   5166  11030   1095    143   -535       C  
ATOM   9052  C   LEU G  28     100.441 -91.276  44.527  1.00 57.36           C  
ANISOU 9052  C   LEU G  28     5641   5173  10979   1092    187   -572       C  
ATOM   9053  O   LEU G  28     100.428 -90.076  44.754  1.00 57.11           O  
ANISOU 9053  O   LEU G  28     5595   5148  10958   1104    242   -599       O  
ATOM   9054  CB  LEU G  28      98.553 -92.463  43.410  1.00 58.48           C  
ANISOU 9054  CB  LEU G  28     5768   5296  11156   1078    124   -476       C  
ATOM   9055  CG  LEU G  28      97.623 -91.735  44.376  1.00 58.95           C  
ANISOU 9055  CG  LEU G  28     5792   5385  11221   1073    176   -467       C  
ATOM   9056  CD1 LEU G  28      97.189 -90.457  43.754  1.00 58.80           C  
ANISOU 9056  CD1 LEU G  28     5757   5351  11233   1093    222   -477       C  
ATOM   9057  CD2 LEU G  28      96.442 -92.563  44.713  1.00 59.84           C  
ANISOU 9057  CD2 LEU G  28     5886   5513  11336   1054    151   -412       C  
ATOM   9058  N   GLY G  29     100.902 -92.183  45.388  1.00 62.25           N  
ANISOU 9058  N   GLY G  29     6271   5814  11567   1074    161   -571       N  
ATOM   9059  CA  GLY G  29     101.372 -91.818  46.711  1.00 61.45           C  
ANISOU 9059  CA  GLY G  29     6162   5746  11439   1068    198   -603       C  
ATOM   9060  C   GLY G  29     102.612 -90.940  46.696  1.00 59.10           C  
ANISOU 9060  C   GLY G  29     5880   5441  11133   1085    230   -663       C  
ATOM   9061  O   GLY G  29     102.895 -90.238  47.675  1.00 58.41           O  
ANISOU 9061  O   GLY G  29     5783   5379  11032   1086    276   -694       O  
ATOM   9062  N   ARG G  30     103.375 -90.972  45.609  1.00 57.57           N  
ANISOU 9062  N   ARG G  30     5713   5215  10947   1099    207   -681       N  
ATOM   9063  CA  ARG G  30     104.533 -90.109  45.556  1.00 56.16           C  
ANISOU 9063  CA  ARG G  30     5548   5028  10761   1116    238   -739       C  
ATOM   9064  C   ARG G  30     104.070 -88.694  45.238  1.00 56.03           C  
ANISOU 9064  C   ARG G  30     5512   5005  10773   1134    295   -753       C  
ATOM   9065  O   ARG G  30     104.449 -87.731  45.905  1.00 55.71           O  
ANISOU 9065  O   ARG G  30     5462   4980  10725   1142    346   -791       O  
ATOM   9066  CB  ARG G  30     105.565 -90.643  44.561  1.00 55.60           C  
ANISOU 9066  CB  ARG G  30     5513   4926  10687   1124    194   -755       C  
ATOM   9067  CG  ARG G  30     106.570 -91.633  45.223  1.00 55.42           C  
ANISOU 9067  CG  ARG G  30     5514   4916  10627   1111    159   -770       C  
ATOM   9068  CD  ARG G  30     107.481 -92.335  44.237  1.00 54.98           C  
ANISOU 9068  CD  ARG G  30     5492   4829  10567   1116    108   -779       C  
ATOM   9069  NE  ARG G  30     108.186 -93.429  44.889  1.00 54.99           N  
ANISOU 9069  NE  ARG G  30     5512   4845  10535   1100     70   -782       N  
ATOM   9070  CZ  ARG G  30     109.355 -93.317  45.523  1.00 54.47           C  
ANISOU 9070  CZ  ARG G  30     5462   4791  10443   1101     80   -826       C  
ATOM   9071  NH1 ARG G  30     109.995 -92.164  45.586  1.00 53.88           N  
ANISOU 9071  NH1 ARG G  30     5388   4715  10370   1117    128   -874       N  
ATOM   9072  NH2 ARG G  30     109.906 -94.386  46.080  1.00 54.55           N  
ANISOU 9072  NH2 ARG G  30     5489   4814  10425   1085     42   -823       N  
ATOM   9073  N   LEU G  31     103.191 -88.583  44.261  1.00 56.10           N  
ANISOU 9073  N   LEU G  31     5511   4991  10813   1141    286   -721       N  
ATOM   9074  CA  LEU G  31     102.509 -87.316  43.996  1.00 56.32           C  
ANISOU 9074  CA  LEU G  31     5515   5015  10870   1156    339   -725       C  
ATOM   9075  C   LEU G  31     101.945 -86.637  45.241  1.00 56.61           C  
ANISOU 9075  C   LEU G  31     5522   5088  10901   1150    392   -728       C  
ATOM   9076  O   LEU G  31     102.112 -85.431  45.426  1.00 56.02           O  
ANISOU 9076  O   LEU G  31     5436   5016  10833   1164    447   -762       O  
ATOM   9077  CB  LEU G  31     101.369 -87.531  43.011  1.00 57.95           C  
ANISOU 9077  CB  LEU G  31     5710   5200  11108   1157    317   -676       C  
ATOM   9078  CG  LEU G  31     100.571 -86.279  42.737  1.00 58.52           C  
ANISOU 9078  CG  LEU G  31     5756   5269  11211   1172    369   -676       C  
ATOM   9079  CD1 LEU G  31     100.574 -86.081  41.264  1.00 58.91           C  
ANISOU 9079  CD1 LEU G  31     5817   5279  11288   1189    352   -671       C  
ATOM   9080  CD2 LEU G  31      99.170 -86.456  43.234  1.00 60.12           C  
ANISOU 9080  CD2 LEU G  31     5927   5492  11424   1158    376   -628       C  
ATOM   9081  N   LEU G  32     101.265 -87.405  46.085  1.00 56.19           N  
ANISOU 9081  N   LEU G  32     5455   5061  10835   1129    377   -694       N  
ATOM   9082  CA  LEU G  32     100.767 -86.871  47.343  1.00 56.75           C  
ANISOU 9082  CA  LEU G  32     5499   5168  10897   1120    424   -697       C  
ATOM   9083  C   LEU G  32     101.907 -86.295  48.175  1.00 55.31           C  
ANISOU 9083  C   LEU G  32     5326   5002  10689   1125    459   -752       C  
ATOM   9084  O   LEU G  32     101.740 -85.271  48.837  1.00 55.30           O  
ANISOU 9084  O   LEU G  32     5303   5018  10689   1130    515   -774       O  
ATOM   9085  CB  LEU G  32     100.046 -87.954  48.137  1.00 58.02           C  
ANISOU 9085  CB  LEU G  32     5648   5354  11042   1096    394   -653       C  
ATOM   9086  CG  LEU G  32      98.772 -88.416  47.461  1.00 59.64           C  
ANISOU 9086  CG  LEU G  32     5840   5548  11274   1090    368   -597       C  
ATOM   9087  CD1 LEU G  32      98.097 -89.464  48.317  1.00 60.87           C  
ANISOU 9087  CD1 LEU G  32     5984   5730  11412   1065    341   -556       C  
ATOM   9088  CD2 LEU G  32      97.881 -87.211  47.242  1.00 60.33           C  
ANISOU 9088  CD2 LEU G  32     5899   5633  11392   1103    419   -593       C  
ATOM   9089  N   VAL G  33     103.059 -86.966  48.137  1.00 55.13           N  
ANISOU 9089  N   VAL G  33     5333   4973  10642   1122    424   -775       N  
ATOM   9090  CA  VAL G  33     104.187 -86.603  48.982  1.00 55.07           C  
ANISOU 9090  CA  VAL G  33     5336   4983  10606   1124    450   -825       C  
ATOM   9091  C   VAL G  33     105.036 -85.477  48.424  1.00 54.87           C  
ANISOU 9091  C   VAL G  33     5321   4937  10590   1147    485   -876       C  
ATOM   9092  O   VAL G  33     105.427 -84.572  49.163  1.00 54.92           O  
ANISOU 9092  O   VAL G  33     5318   4961  10587   1153    535   -913       O  
ATOM   9093  CB  VAL G  33     105.069 -87.799  49.224  1.00 54.97           C  
ANISOU 9093  CB  VAL G  33     5350   4973  10562   1111    399   -829       C  
ATOM   9094  CG1 VAL G  33     106.396 -87.344  49.731  1.00 54.83           C  
ANISOU 9094  CG1 VAL G  33     5350   4963  10521   1118    422   -886       C  
ATOM   9095  CG2 VAL G  33     104.413 -88.729  50.215  1.00 55.20           C  
ANISOU 9095  CG2 VAL G  33     5367   5033  10574   1086    379   -792       C  
ATOM   9096  N   VAL G  34     105.313 -85.540  47.122  1.00 56.80           N  
ANISOU 9096  N   VAL G  34     5583   5145  10852   1161    458   -876       N  
ATOM   9097  CA  VAL G  34     106.176 -84.570  46.435  1.00 55.70           C  
ANISOU 9097  CA  VAL G  34     5458   4982  10723   1184    485   -922       C  
ATOM   9098  C   VAL G  34     105.508 -83.191  46.177  1.00 56.16           C  
ANISOU 9098  C   VAL G  34     5491   5036  10811   1200    542   -929       C  
ATOM   9099  O   VAL G  34     106.156 -82.131  46.305  1.00 55.63           O  
ANISOU 9099  O   VAL G  34     5425   4968  10744   1215    588   -975       O  
ATOM   9100  CB  VAL G  34     106.645 -85.146  45.099  1.00 55.19           C  
ANISOU 9100  CB  VAL G  34     5422   4880  10669   1192    435   -917       C  
ATOM   9101  CG1 VAL G  34     107.237 -84.050  44.211  1.00 54.61           C  
ANISOU 9101  CG1 VAL G  34     5357   4779  10614   1217    464   -956       C  
ATOM   9102  CG2 VAL G  34     107.647 -86.262  45.346  1.00 54.73           C  
ANISOU 9102  CG2 VAL G  34     5392   4825  10579   1181    387   -926       C  
ATOM   9103  N   TYR G  35     104.214 -83.221  45.828  1.00 54.87           N  
ANISOU 9103  N   TYR G  35     5305   4869  10673   1197    540   -883       N  
ATOM   9104  CA  TYR G  35     103.430 -82.026  45.576  1.00 55.40           C  
ANISOU 9104  CA  TYR G  35     5347   4932  10770   1211    591   -882       C  
ATOM   9105  C   TYR G  35     102.263 -81.978  46.525  1.00 56.95           C  
ANISOU 9105  C   TYR G  35     5511   5160  10969   1196    614   -850       C  
ATOM   9106  O   TYR G  35     101.132 -82.198  46.105  1.00 58.51           O  
ANISOU 9106  O   TYR G  35     5692   5351  11189   1192    602   -805       O  
ATOM   9107  CB  TYR G  35     102.922 -82.012  44.135  1.00 56.06           C  
ANISOU 9107  CB  TYR G  35     5434   4979  10887   1223    568   -857       C  
ATOM   9108  CG  TYR G  35     103.997 -82.299  43.143  1.00 54.68           C  
ANISOU 9108  CG  TYR G  35     5293   4773  10711   1234    534   -880       C  
ATOM   9109  CD1 TYR G  35     105.042 -81.401  42.950  1.00 53.65           C  
ANISOU 9109  CD1 TYR G  35     5175   4631  10577   1252    565   -934       C  
ATOM   9110  CD2 TYR G  35     104.003 -83.488  42.419  1.00 55.00           C  
ANISOU 9110  CD2 TYR G  35     5352   4795  10750   1226    470   -850       C  
ATOM   9111  CE1 TYR G  35     106.062 -81.663  42.050  1.00 53.05           C  
ANISOU 9111  CE1 TYR G  35     5131   4526  10498   1262    533   -956       C  
ATOM   9112  CE2 TYR G  35     105.036 -83.777  41.508  1.00 53.93           C  
ANISOU 9112  CE2 TYR G  35     5249   4631  10611   1236    437   -872       C  
ATOM   9113  CZ  TYR G  35     106.062 -82.854  41.331  1.00 53.19           C  
ANISOU 9113  CZ  TYR G  35     5168   4526  10515   1254    470   -926       C  
ATOM   9114  OH  TYR G  35     107.079 -83.118  40.436  1.00 52.59           O  
ANISOU 9114  OH  TYR G  35     5123   4422  10436   1264    438   -948       O  
ATOM   9115  N   PRO G  36     102.508 -81.665  47.804  1.00 55.83           N  
ANISOU 9115  N   PRO G  36     5358   5050  10803   1188    649   -874       N  
ATOM   9116  CA  PRO G  36     101.511 -81.929  48.849  1.00 56.13           C  
ANISOU 9116  CA  PRO G  36     5369   5121  10835   1170    661   -841       C  
ATOM   9117  C   PRO G  36     100.129 -81.334  48.636  1.00 56.32           C  
ANISOU 9117  C   PRO G  36     5362   5146  10892   1173    688   -807       C  
ATOM   9118  O   PRO G  36      99.202 -81.791  49.300  1.00 56.94           O  
ANISOU 9118  O   PRO G  36     5420   5247  10968   1156    684   -771       O  
ATOM   9119  CB  PRO G  36     102.145 -81.338  50.114  1.00 56.21           C  
ANISOU 9119  CB  PRO G  36     5374   5163  10820   1167    706   -883       C  
ATOM   9120  CG  PRO G  36     103.376 -80.702  49.695  1.00 55.96           C  
ANISOU 9120  CG  PRO G  36     5365   5113  10785   1185    721   -936       C  
ATOM   9121  CD  PRO G  36     103.789 -81.275  48.387  1.00 55.71           C  
ANISOU 9121  CD  PRO G  36     5359   5044  10763   1193    671   -928       C  
ATOM   9122  N   TRP G  37      99.961 -80.367  47.742  1.00 56.83           N  
ANISOU 9122  N   TRP G  37     5421   5186  10986   1193    715   -818       N  
ATOM   9123  CA  TRP G  37      98.644 -79.738  47.603  1.00 57.03           C  
ANISOU 9123  CA  TRP G  37     5414   5212  11041   1196    745   -787       C  
ATOM   9124  C   TRP G  37      97.595 -80.654  46.973  1.00 57.10           C  
ANISOU 9124  C   TRP G  37     5417   5210  11067   1187    699   -728       C  
ATOM   9125  O   TRP G  37      96.400 -80.387  47.067  1.00 57.30           O  
ANISOU 9125  O   TRP G  37     5415   5244  11113   1183    717   -695       O  
ATOM   9126  CB  TRP G  37      98.744 -78.441  46.799  1.00 56.91           C  
ANISOU 9126  CB  TRP G  37     5395   5174  11054   1221    787   -814       C  
ATOM   9127  CG  TRP G  37      99.353 -78.625  45.474  1.00 56.63           C  
ANISOU 9127  CG  TRP G  37     5386   5100  11030   1235    752   -822       C  
ATOM   9128  CD1 TRP G  37      98.739 -79.066  44.338  1.00 56.56           C  
ANISOU 9128  CD1 TRP G  37     5381   5065  11046   1238    715   -784       C  
ATOM   9129  CD2 TRP G  37     100.714 -78.385  45.131  1.00 56.37           C  
ANISOU 9129  CD2 TRP G  37     5381   5051  10985   1248    751   -870       C  
ATOM   9130  NE1 TRP G  37      99.639 -79.114  43.306  1.00 56.28           N  
ANISOU 9130  NE1 TRP G  37     5373   4997  11013   1252    691   -806       N  
ATOM   9131  CE2 TRP G  37     100.861 -78.700  43.770  1.00 56.15           C  
ANISOU 9131  CE2 TRP G  37     5373   4987  10975   1258    713   -859       C  
ATOM   9132  CE3 TRP G  37     101.829 -77.950  45.849  1.00 56.29           C  
ANISOU 9132  CE3 TRP G  37     5383   5055  10950   1251    778   -922       C  
ATOM   9133  CZ2 TRP G  37     102.069 -78.575  43.114  1.00 55.87           C  
ANISOU 9133  CZ2 TRP G  37     5366   4928  10934   1271    701   -898       C  
ATOM   9134  CZ3 TRP G  37     103.022 -77.829  45.195  1.00 56.01           C  
ANISOU 9134  CZ3 TRP G  37     5376   4996  10909   1264    767   -960       C  
ATOM   9135  CH2 TRP G  37     103.134 -78.128  43.841  1.00 55.80           C  
ANISOU 9135  CH2 TRP G  37     5368   4933  10902   1275    729   -948       C  
ATOM   9136  N   THR G  38      98.022 -81.733  46.334  1.00 56.86           N  
ANISOU 9136  N   THR G  38     5413   5162  11028   1181    639   -714       N  
ATOM   9137  CA  THR G  38      97.042 -82.642  45.763  1.00 56.93           C  
ANISOU 9137  CA  THR G  38     5416   5161  11052   1171    593   -658       C  
ATOM   9138  C   THR G  38      96.346 -83.432  46.862  1.00 57.18           C  
ANISOU 9138  C   THR G  38     5433   5228  11066   1147    582   -624       C  
ATOM   9139  O   THR G  38      95.265 -83.983  46.661  1.00 57.72           O  
ANISOU 9139  O   THR G  38     5487   5296  11148   1137    559   -575       O  
ATOM   9140  CB  THR G  38      97.684 -83.603  44.785  1.00 56.68           C  
ANISOU 9140  CB  THR G  38     5417   5102  11017   1172    532   -651       C  
ATOM   9141  OG1 THR G  38      98.938 -84.043  45.326  1.00 56.55           O  
ANISOU 9141  OG1 THR G  38     5426   5095  10967   1167    518   -687       O  
ATOM   9142  CG2 THR G  38      97.929 -82.904  43.463  1.00 56.46           C  
ANISOU 9142  CG2 THR G  38     5400   5037  11017   1195    538   -667       C  
ATOM   9143  N   GLN G  39      96.968 -83.470  48.036  1.00 59.07           N  
ANISOU 9143  N   GLN G  39     5674   5496  11275   1138    599   -651       N  
ATOM   9144  CA  GLN G  39      96.398 -84.193  49.168  1.00 60.06           C  
ANISOU 9144  CA  GLN G  39     5785   5655  11381   1115    590   -623       C  
ATOM   9145  C   GLN G  39      94.980 -83.739  49.446  1.00 61.90           C  
ANISOU 9145  C   GLN G  39     5982   5902  11636   1111    620   -588       C  
ATOM   9146  O   GLN G  39      94.157 -84.475  49.962  1.00 63.28           O  
ANISOU 9146  O   GLN G  39     6143   6095  11805   1092    601   -548       O  
ATOM   9147  CB  GLN G  39      97.256 -84.002  50.405  1.00 58.92           C  
ANISOU 9147  CB  GLN G  39     5644   5539  11203   1108    617   -664       C  
ATOM   9148  CG  GLN G  39      98.631 -84.529  50.214  1.00 57.21           C  
ANISOU 9148  CG  GLN G  39     5463   5312  10963   1110    585   -696       C  
ATOM   9149  CD  GLN G  39      99.429 -84.441  51.464  1.00 56.20           C  
ANISOU 9149  CD  GLN G  39     5338   5214  10801   1102    607   -732       C  
ATOM   9150  OE1 GLN G  39      99.073 -83.729  52.386  1.00 56.66           O  
ANISOU 9150  OE1 GLN G  39     5374   5299  10857   1100    656   -742       O  
ATOM   9151  NE2 GLN G  39     100.513 -85.187  51.519  1.00 55.73           N  
ANISOU 9151  NE2 GLN G  39     5308   5152  10716   1098    571   -751       N  
ATOM   9152  N   ARG G  40      94.713 -82.508  49.068  1.00 60.91           N  
ANISOU 9152  N   ARG G  40     5842   5766  11536   1129    668   -605       N  
ATOM   9153  CA  ARG G  40      93.437 -81.841  49.284  1.00 62.85           C  
ANISOU 9153  CA  ARG G  40     6052   6023  11805   1129    706   -579       C  
ATOM   9154  C   ARG G  40      92.227 -82.608  48.741  1.00 65.05           C  
ANISOU 9154  C   ARG G  40     6319   6293  12103   1119    668   -518       C  
ATOM   9155  O   ARG G  40      91.116 -82.563  49.304  1.00 67.04           O  
ANISOU 9155  O   ARG G  40     6544   6566  12364   1109    685   -486       O  
ATOM   9156  CB  ARG G  40      93.518 -80.466  48.629  1.00 62.32           C  
ANISOU 9156  CB  ARG G  40     5978   5936  11765   1153    754   -608       C  
ATOM   9157  CG  ARG G  40      92.436 -79.577  48.960  1.00 63.98           C  
ANISOU 9157  CG  ARG G  40     6154   6159  11997   1156    803   -594       C  
ATOM   9158  CD  ARG G  40      92.954 -78.175  48.882  1.00 63.00           C  
ANISOU 9158  CD  ARG G  40     6027   6028  11883   1177    860   -642       C  
ATOM   9159  NE  ARG G  40      93.449 -77.795  47.562  1.00 62.09           N  
ANISOU 9159  NE  ARG G  40     5929   5874  11787   1197    850   -658       N  
ATOM   9160  CZ  ARG G  40      94.399 -76.886  47.390  1.00 60.76           C  
ANISOU 9160  CZ  ARG G  40     5772   5695  11618   1215    883   -708       C  
ATOM   9161  NH1 ARG G  40      94.948 -76.316  48.461  1.00 60.19           N  
ANISOU 9161  NH1 ARG G  40     5696   5649  11526   1214    925   -747       N  
ATOM   9162  NH2 ARG G  40      94.804 -76.573  46.165  1.00 60.22           N  
ANISOU 9162  NH2 ARG G  40     5720   5592  11569   1233    872   -720       N  
ATOM   9163  N   PHE G  41      92.455 -83.280  47.617  1.00 59.72           N  
ANISOU 9163  N   PHE G  41     5666   5588  11436   1123    618   -503       N  
ATOM   9164  CA  PHE G  41      91.424 -84.034  46.925  1.00 60.36           C  
ANISOU 9164  CA  PHE G  41     5741   5656  11536   1116    577   -448       C  
ATOM   9165  C   PHE G  41      91.216 -85.430  47.526  1.00 60.86           C  
ANISOU 9165  C   PHE G  41     5809   5738  11576   1091    529   -414       C  
ATOM   9166  O   PHE G  41      90.139 -86.021  47.409  1.00 61.58           O  
ANISOU 9166  O   PHE G  41     5885   5832  11679   1080    506   -364       O  
ATOM   9167  CB  PHE G  41      91.788 -84.146  45.447  1.00 59.97           C  
ANISOU 9167  CB  PHE G  41     5714   5566  11507   1131    545   -448       C  
ATOM   9168  CG  PHE G  41      91.474 -82.906  44.650  1.00 59.78           C  
ANISOU 9168  CG  PHE G  41     5678   5521  11516   1153    585   -459       C  
ATOM   9169  CD1 PHE G  41      91.766 -81.656  45.134  1.00 59.43           C  
ANISOU 9169  CD1 PHE G  41     5621   5485  11473   1165    646   -500       C  
ATOM   9170  CD2 PHE G  41      90.876 -82.990  43.403  1.00 59.97           C  
ANISOU 9170  CD2 PHE G  41     5702   5515  11570   1161    561   -429       C  
ATOM   9171  CE1 PHE G  41      91.479 -80.547  44.387  1.00 59.27           C  
ANISOU 9171  CE1 PHE G  41     5590   5445  11483   1185    682   -510       C  
ATOM   9172  CE2 PHE G  41      90.588 -81.857  42.670  1.00 59.80           C  
ANISOU 9172  CE2 PHE G  41     5670   5474  11579   1181    598   -440       C  
ATOM   9173  CZ  PHE G  41      90.885 -80.660  43.155  1.00 59.47           C  
ANISOU 9173  CZ  PHE G  41     5616   5441  11538   1193    657   -479       C  
ATOM   9174  N   PHE G  42      92.295 -85.970  48.091  1.00 58.79           N  
ANISOU 9174  N   PHE G  42     5570   5487  11281   1084    511   -441       N  
ATOM   9175  CA  PHE G  42      92.319 -87.311  48.636  1.00 58.85           C  
ANISOU 9175  CA  PHE G  42     5587   5510  11264   1061    463   -415       C  
ATOM   9176  C   PHE G  42      92.247 -87.490  50.164  1.00 59.08           C  
ANISOU 9176  C   PHE G  42     5602   5580  11264   1043    483   -418       C  
ATOM   9177  O   PHE G  42      92.260 -88.632  50.618  1.00 59.13           O  
ANISOU 9177  O   PHE G  42     5617   5600  11249   1024    442   -396       O  
ATOM   9178  CB  PHE G  42      93.573 -88.023  48.127  1.00 58.58           C  
ANISOU 9178  CB  PHE G  42     5590   5456  11210   1064    418   -438       C  
ATOM   9179  CG  PHE G  42      93.658 -88.136  46.625  1.00 58.35           C  
ANISOU 9179  CG  PHE G  42     5578   5387  11206   1077    386   -429       C  
ATOM   9180  CD1 PHE G  42      92.918 -89.067  45.932  1.00 58.37           C  
ANISOU 9180  CD1 PHE G  42     5582   5375  11221   1069    337   -380       C  
ATOM   9181  CD2 PHE G  42      94.522 -87.344  45.914  1.00 58.12           C  
ANISOU 9181  CD2 PHE G  42     5565   5334  11185   1099    404   -471       C  
ATOM   9182  CE1 PHE G  42      93.022 -89.181  44.554  1.00 58.16           C  
ANISOU 9182  CE1 PHE G  42     5571   5312  11216   1081    307   -372       C  
ATOM   9183  CE2 PHE G  42      94.626 -87.462  44.543  1.00 57.92           C  
ANISOU 9183  CE2 PHE G  42     5555   5271  11180   1111    374   -463       C  
ATOM   9184  CZ  PHE G  42      93.868 -88.380  43.867  1.00 57.94           C  
ANISOU 9184  CZ  PHE G  42     5558   5260  11195   1102    326   -414       C  
ATOM   9185  N   GLU G  43      92.184 -86.432  50.969  1.00 64.01           N  
ANISOU 9185  N   GLU G  43     6207   6227  11888   1048    543   -445       N  
ATOM   9186  CA  GLU G  43      92.308 -86.623  52.426  1.00 64.16           C  
ANISOU 9186  CA  GLU G  43     6217   6285  11877   1031    560   -454       C  
ATOM   9187  C   GLU G  43      91.262 -87.558  53.050  1.00 65.92           C  
ANISOU 9187  C   GLU G  43     6422   6530  12093   1008    536   -402       C  
ATOM   9188  O   GLU G  43      91.398 -87.943  54.219  1.00 66.09           O  
ANISOU 9188  O   GLU G  43     6441   6584  12088    992    539   -406       O  
ATOM   9189  CB  GLU G  43      92.239 -85.302  53.153  1.00 63.99           C  
ANISOU 9189  CB  GLU G  43     6173   6282  11859   1040    631   -486       C  
ATOM   9190  CG  GLU G  43      93.530 -84.589  53.214  1.00 62.67           C  
ANISOU 9190  CG  GLU G  43     6023   6109  11678   1055    657   -545       C  
ATOM   9191  CD  GLU G  43      93.351 -83.093  53.386  1.00 62.23           C  
ANISOU 9191  CD  GLU G  43     5947   6057  11640   1071    726   -574       C  
ATOM   9192  OE1 GLU G  43      92.329 -82.655  53.989  1.00 63.49           O  
ANISOU 9192  OE1 GLU G  43     6076   6238  11810   1065    760   -554       O  
ATOM   9193  OE2 GLU G  43      94.249 -82.368  52.900  1.00 60.60           O  
ANISOU 9193  OE2 GLU G  43     5756   5833  11437   1089    745   -617       O  
ATOM   9194  N   SER G  44      90.223 -87.897  52.279  1.00 64.61           N  
ANISOU 9194  N   SER G  44     6246   6349  11954   1007    512   -356       N  
ATOM   9195  CA  SER G  44      89.258 -88.932  52.630  1.00 65.44           C  
ANISOU 9195  CA  SER G  44     6340   6470  12056    986    477   -303       C  
ATOM   9196  C   SER G  44      89.917 -90.301  52.847  1.00 65.43           C  
ANISOU 9196  C   SER G  44     6364   6471  12024    969    419   -295       C  
ATOM   9197  O   SER G  44      89.303 -91.215  53.404  1.00 66.08           O  
ANISOU 9197  O   SER G  44     6438   6573  12095    949    392   -258       O  
ATOM   9198  CB  SER G  44      88.199 -89.038  51.525  1.00 66.12           C  
ANISOU 9198  CB  SER G  44     6415   6530  12176    990    458   -259       C  
ATOM   9199  OG  SER G  44      88.707 -89.545  50.304  1.00 65.56           O  
ANISOU 9199  OG  SER G  44     6371   6424  12113    999    412   -257       O  
ATOM   9200  N   PHE G  45      91.161 -90.439  52.392  1.00 65.04           N  
ANISOU 9200  N   PHE G  45     6345   6404  11963    978    400   -330       N  
ATOM   9201  CA  PHE G  45      91.857 -91.711  52.472  1.00 64.44           C  
ANISOU 9201  CA  PHE G  45     6296   6328  11861    965    344   -325       C  
ATOM   9202  C   PHE G  45      92.167 -92.125  53.889  1.00 64.48           C  
ANISOU 9202  C   PHE G  45     6298   6370  11830    947    349   -334       C  
ATOM   9203  O   PHE G  45      91.990 -93.296  54.259  1.00 65.83           O  
ANISOU 9203  O   PHE G  45     6475   6552  11984    927    306   -304       O  
ATOM   9204  CB  PHE G  45      93.165 -91.679  51.693  1.00 62.55           C  
ANISOU 9204  CB  PHE G  45     6090   6061  11616    980    326   -364       C  
ATOM   9205  CG  PHE G  45      92.989 -91.799  50.221  1.00 62.49           C  
ANISOU 9205  CG  PHE G  45     6094   6014  11635    992    295   -347       C  
ATOM   9206  CD1 PHE G  45      94.087 -91.884  49.393  1.00 60.91           C  
ANISOU 9206  CD1 PHE G  45     5925   5786  11433   1005    272   -376       C  
ATOM   9207  CD2 PHE G  45      91.720 -91.814  49.659  1.00 64.02           C  
ANISOU 9207  CD2 PHE G  45     6268   6199  11859    991    290   -301       C  
ATOM   9208  CE1 PHE G  45      93.922 -91.994  48.031  1.00 60.87           C  
ANISOU 9208  CE1 PHE G  45     5929   5745  11452   1016    244   -360       C  
ATOM   9209  CE2 PHE G  45      91.552 -91.924  48.300  1.00 63.98           C  
ANISOU 9209  CE2 PHE G  45     6273   6159  11879   1003    262   -285       C  
ATOM   9210  CZ  PHE G  45      92.644 -92.014  47.486  1.00 62.41           C  
ANISOU 9210  CZ  PHE G  45     6105   5932  11677   1015    239   -314       C  
ATOM   9211  N   GLY G  46      92.668 -91.183  54.673  1.00 66.02           N  
ANISOU 9211  N   GLY G  46     7432   6670  10984   2035    581    584       N  
ATOM   9212  CA  GLY G  46      93.138 -91.514  55.998  1.00 66.02           C  
ANISOU 9212  CA  GLY G  46     7408   6685  10990   2027    573    585       C  
ATOM   9213  C   GLY G  46      94.247 -90.538  56.249  1.00 66.03           C  
ANISOU 9213  C   GLY G  46     7394   6694  11000   2028    596    574       C  
ATOM   9214  O   GLY G  46      94.229 -89.455  55.675  1.00 66.01           O  
ANISOU 9214  O   GLY G  46     7394   6689  10997   2030    615    569       O  
ATOM   9215  N   ASP G  47      95.222 -90.904  57.082  1.00 72.79           N  
ANISOU 9215  N   ASP G  47     8232   7559  11864   2027    596    572       N  
ATOM   9216  CA  ASP G  47      96.378 -90.035  57.294  1.00 70.62           C  
ANISOU 9216  CA  ASP G  47     7943   7291  11599   2028    618    561       C  
ATOM   9217  C   ASP G  47      97.229 -89.982  56.037  1.00 68.55           C  
ANISOU 9217  C   ASP G  47     7695   7013  11337   2043    635    555       C  
ATOM   9218  O   ASP G  47      97.695 -91.005  55.545  1.00 68.73           O  
ANISOU 9218  O   ASP G  47     7730   7026  11360   2053    628    556       O  
ATOM   9219  CB  ASP G  47      97.225 -90.529  58.466  1.00 71.26           C  
ANISOU 9219  CB  ASP G  47     8002   7385  11688   2024    613    561       C  
ATOM   9220  CG  ASP G  47      98.474 -89.688  58.680  1.00 69.50           C  
ANISOU 9220  CG  ASP G  47     7764   7169  11475   2026    636    550       C  
ATOM   9221  OD1 ASP G  47      98.533 -88.548  58.169  1.00 67.59           O  
ANISOU 9221  OD1 ASP G  47     7523   6925  11233   2027    656    544       O  
ATOM   9222  OD2 ASP G  47      99.403 -90.178  59.364  1.00 70.25           O  
ANISOU 9222  OD2 ASP G  47     7845   7271  11577   2026    634    548       O  
ATOM   9223  N   LEU G  48      97.371 -88.783  55.494  1.00 66.49           N  
ANISOU 9223  N   LEU G  48     7436   6751  11078   2045    657    548       N  
ATOM   9224  CA  LEU G  48      98.280 -88.500  54.387  1.00 65.89           C  
ANISOU 9224  CA  LEU G  48     7370   6662  11003   2058    676    540       C  
ATOM   9225  C   LEU G  48      99.551 -87.709  54.756  1.00 65.79           C  
ANISOU 9225  C   LEU G  48     7340   6657  11000   2059    698    530       C  
ATOM   9226  O   LEU G  48     100.221 -87.194  53.869  1.00 65.83           O  
ANISOU 9226  O   LEU G  48     7352   6653  11007   2069    717    523       O  
ATOM   9227  CB  LEU G  48      97.500 -87.799  53.276  1.00 65.96           C  
ANISOU 9227  CB  LEU G  48     7398   6659  11004   2062    685    540       C  
ATOM   9228  CG  LEU G  48      96.583 -88.820  52.587  1.00 66.91           C  
ANISOU 9228  CG  LEU G  48     7541   6766  11115   2066    665    548       C  
ATOM   9229  CD1 LEU G  48      95.752 -88.209  51.483  1.00 67.05           C  
ANISOU 9229  CD1 LEU G  48     7579   6773  11125   2069    672    549       C  
ATOM   9230  CD2 LEU G  48      97.443 -89.937  52.037  1.00 66.99           C  
ANISOU 9230  CD2 LEU G  48     7562   6765  11127   2079    661    548       C  
ATOM   9231  N   SER G  49      99.840 -87.534  56.045  1.00 68.92           N  
ANISOU 9231  N   SER G  49     7712   7071  11403   2049    695    529       N  
ATOM   9232  CA  SER G  49     100.875 -86.577  56.490  1.00 67.91           C  
ANISOU 9232  CA  SER G  49     7565   6952  11284   2048    716    520       C  
ATOM   9233  C   SER G  49     102.326 -87.003  56.205  1.00 66.74           C  
ANISOU 9233  C   SER G  49     7415   6799  11143   2059    727    514       C  
ATOM   9234  O   SER G  49     103.071 -86.294  55.529  1.00 66.21           O  
ANISOU 9234  O   SER G  49     7351   6727  11079   2066    748    506       O  
ATOM   9235  CB  SER G  49     100.726 -86.309  57.993  1.00 69.33           C  
ANISOU 9235  CB  SER G  49     7720   7153  11469   2033    710    521       C  
ATOM   9236  OG  SER G  49     101.027 -87.477  58.744  1.00 70.70           O  
ANISOU 9236  OG  SER G  49     7887   7331  11646   2032    692    526       O  
ATOM   9237  N   THR G  50     102.733 -88.118  56.796  1.00 65.52           N  
ANISOU 9237  N   THR G  50     7255   6647  10991   2059    712    517       N  
ATOM   9238  CA  THR G  50     104.042 -88.714  56.564  1.00 65.61           C  
ANISOU 9238  CA  THR G  50     7266   6653  11009   2070    718    513       C  
ATOM   9239  C   THR G  50     104.095 -89.426  55.210  1.00 65.67           C  
ANISOU 9239  C   THR G  50     7300   6641  11011   2084    716    514       C  
ATOM   9240  O   THR G  50     103.057 -89.769  54.655  1.00 65.65           O  
ANISOU 9240  O   THR G  50     7314   6629  11000   2084    705    520       O  
ATOM   9241  CB  THR G  50     104.359 -89.720  57.678  1.00 65.62           C  
ANISOU 9241  CB  THR G  50     7254   6665  11015   2065    700    517       C  
ATOM   9242  OG1 THR G  50     104.365 -91.064  57.153  1.00 65.68           O  
ANISOU 9242  OG1 THR G  50     7278   6660  11019   2073    684    523       O  
ATOM   9243  CG2 THR G  50     103.304 -89.603  58.783  1.00 65.54           C  
ANISOU 9243  CG2 THR G  50     7230   6669  11002   2049    685    524       C  
ATOM   9244  N   PRO G  51     105.302 -89.671  54.667  1.00 65.75           N  
ANISOU 9244  N   PRO G  51     7313   6643  11026   2095    728    508       N  
ATOM   9245  CA  PRO G  51     105.368 -90.478  53.437  1.00 65.82           C  
ANISOU 9245  CA  PRO G  51     7346   6633  11029   2109    725    509       C  
ATOM   9246  C   PRO G  51     105.027 -91.968  53.656  1.00 65.85           C  
ANISOU 9246  C   PRO G  51     7357   6633  11029   2110    700    518       C  
ATOM   9247  O   PRO G  51     104.522 -92.646  52.752  1.00 65.87           O  
ANISOU 9247  O   PRO G  51     7382   6621  11025   2117    691    523       O  
ATOM   9248  CB  PRO G  51     106.821 -90.309  53.004  1.00 65.90           C  
ANISOU 9248  CB  PRO G  51     7353   6638  11047   2119    745    500       C  
ATOM   9249  CG  PRO G  51     107.530 -90.146  54.280  1.00 65.89           C  
ANISOU 9249  CG  PRO G  51     7326   6654  11055   2111    746    498       C  
ATOM   9250  CD  PRO G  51     106.644 -89.276  55.120  1.00 65.79           C  
ANISOU 9250  CD  PRO G  51     7300   6656  11042   2097    745    500       C  
ATOM   9251  N   ASP G  52     105.304 -92.476  54.851  1.00 65.84           N  
ANISOU 9251  N   ASP G  52     7338   6645  11034   2102    688    521       N  
ATOM   9252  CA  ASP G  52     105.029 -93.877  55.127  1.00 65.87           C  
ANISOU 9252  CA  ASP G  52     7347   6646  11035   2103    664    529       C  
ATOM   9253  C   ASP G  52     103.551 -94.123  55.220  1.00 65.81           C  
ANISOU 9253  C   ASP G  52     7348   6638  11018   2095    645    538       C  
ATOM   9254  O   ASP G  52     103.068 -95.133  54.718  1.00 65.83           O  
ANISOU 9254  O   ASP G  52     7368   6630  11015   2100    629    545       O  
ATOM   9255  CB  ASP G  52     105.711 -94.323  56.407  1.00 65.88           C  
ANISOU 9255  CB  ASP G  52     7326   6662  11044   2097    657    529       C  
ATOM   9256  CG  ASP G  52     107.177 -94.477  56.229  1.00 65.96           C  
ANISOU 9256  CG  ASP G  52     7331   6669  11063   2106    670    522       C  
ATOM   9257  OD1 ASP G  52     107.598 -94.596  55.050  1.00 66.02           O  
ANISOU 9257  OD1 ASP G  52     7356   6661  11068   2119    680    519       O  
ATOM   9258  OD2 ASP G  52     107.884 -94.483  57.258  1.00 65.97           O  
ANISOU 9258  OD2 ASP G  52     7310   6683  11071   2101    671    520       O  
ATOM   9259  N   ALA G  53     102.836 -93.203  55.867  1.00 65.72           N  
ANISOU 9259  N   ALA G  53     7325   6639  11006   2083    647    539       N  
ATOM   9260  CA  ALA G  53     101.391 -93.307  55.949  1.00 65.65           C  
ANISOU 9260  CA  ALA G  53     7325   6631  10989   2075    631    547       C  
ATOM   9261  C   ALA G  53     100.832 -93.340  54.550  1.00 65.67           C  
ANISOU 9261  C   ALA G  53     7353   6615  10983   2085    633    548       C  
ATOM   9262  O   ALA G  53     100.094 -94.249  54.199  1.00 65.67           O  
ANISOU 9262  O   ALA G  53     7369   6607  10976   2087    615    556       O  
ATOM   9263  CB  ALA G  53     100.805 -92.166  56.732  1.00 65.56           C  
ANISOU 9263  CB  ALA G  53     7297   6635  10979   2062    636    546       C  
ATOM   9264  N   VAL G  54     101.218 -92.372  53.739  1.00 65.68           N  
ANISOU 9264  N   VAL G  54     7359   6610  10985   2091    655    541       N  
ATOM   9265  CA  VAL G  54     100.708 -92.296  52.377  1.00 65.69           C  
ANISOU 9265  CA  VAL G  54     7386   6595  10978   2100    659    541       C  
ATOM   9266  C   VAL G  54     100.977 -93.564  51.620  1.00 65.77           C  
ANISOU 9266  C   VAL G  54     7414   6589  10985   2111    649    544       C  
ATOM   9267  O   VAL G  54     100.073 -94.130  51.016  1.00 65.76           O  
ANISOU 9267  O   VAL G  54     7433   6578  10976   2114    635    551       O  
ATOM   9268  CB  VAL G  54     101.327 -91.138  51.581  1.00 65.70           C  
ANISOU 9268  CB  VAL G  54     7390   6591  10983   2106    686    532       C  
ATOM   9269  CG1 VAL G  54     100.891 -91.211  50.121  1.00 65.72           C  
ANISOU 9269  CG1 VAL G  54     7420   6575  10977   2117    690    532       C  
ATOM   9270  CG2 VAL G  54     100.916 -89.821  52.180  1.00 65.62           C  
ANISOU 9270  CG2 VAL G  54     7365   6594  10974   2095    697    529       C  
ATOM   9271  N   MET G  55     102.232 -94.001  51.655  1.00 65.84           N  
ANISOU 9271  N   MET G  55     7418   6597  11001   2119    655    540       N  
ATOM   9272  CA  MET G  55     102.638 -95.171  50.891  1.00 65.93           C  
ANISOU 9272  CA  MET G  55     7446   6593  11010   2131    647    542       C  
ATOM   9273  C   MET G  55     101.952 -96.424  51.431  1.00 65.92           C  
ANISOU 9273  C   MET G  55     7448   6594  11005   2127    619    552       C  
ATOM   9274  O   MET G  55     101.573 -97.310  50.668  1.00 65.96           O  
ANISOU 9274  O   MET G  55     7473   6584  11003   2134    608    557       O  
ATOM   9275  CB  MET G  55     104.156 -95.326  50.902  1.00 66.00           C  
ANISOU 9275  CB  MET G  55     7447   6602  11028   2139    660    534       C  
ATOM   9276  CG  MET G  55     104.936 -94.214  50.200  1.00 66.02           C  
ANISOU 9276  CG  MET G  55     7450   6601  11035   2146    688    524       C  
ATOM   9277  SD  MET G  55     104.439 -93.781  48.513  1.00 66.03           S  
ANISOU 9277  SD  MET G  55     7480   6583  11027   2157    699    522       S  
ATOM   9278  CE  MET G  55     103.944 -95.344  47.759  1.00 66.09           C  
ANISOU 9278  CE  MET G  55     7512   6573  11026   2166    677    531       C  
ATOM   9279  N   GLY G  56     101.752 -96.459  52.746  1.00 65.87           N  
ANISOU 9279  N   GLY G  56     7422   6604  11003   2114    609    555       N  
ATOM   9280  CA  GLY G  56     101.092 -97.571  53.394  1.00 65.86           C  
ANISOU 9280  CA  GLY G  56     7420   6606  10998   2109    583    564       C  
ATOM   9281  C   GLY G  56      99.579 -97.589  53.284  1.00 65.79           C  
ANISOU 9281  C   GLY G  56     7422   6596  10980   2102    568    573       C  
ATOM   9282  O   GLY G  56      98.997 -98.680  53.147  1.00 65.81           O  
ANISOU 9282  O   GLY G  56     7437   6591  10976   2103    547    581       O  
ATOM   9283  N   ASN G  57      98.946 -96.408  53.322  1.00 65.72           N  
ANISOU 9283  N   ASN G  57     7409   6592  10969   2095    578    571       N  
ATOM   9284  CA  ASN G  57      97.494 -96.326  53.435  1.00 65.64           C  
ANISOU 9284  CA  ASN G  57     7406   6585  10951   2086    564    579       C  
ATOM   9285  C   ASN G  57      96.806 -97.137  52.336  1.00 65.68           C  
ANISOU 9285  C   ASN G  57     7437   6571  10946   2094    552    585       C  
ATOM   9286  O   ASN G  57      96.973 -96.835  51.147  1.00 65.71           O  
ANISOU 9286  O   ASN G  57     7458   6561  10947   2105    565    581       O  
ATOM   9287  CB  ASN G  57      97.006 -94.886  53.374  1.00 65.58           C  
ANISOU 9287  CB  ASN G  57     7393   6581  10942   2080    579    575       C  
ATOM   9288  CG  ASN G  57      95.468 -94.795  53.378  1.00 65.50           C  
ANISOU 9288  CG  ASN G  57     7392   6572  10923   2071    565    583       C  
ATOM   9289  OD1 ASN G  57      94.806 -95.135  52.390  1.00 65.51           O  
ANISOU 9289  OD1 ASN G  57     7415   6559  10916   2078    559    587       O  
ATOM   9290  ND2 ASN G  57      94.895 -94.356  54.501  1.00 65.42           N  
ANISOU 9290  ND2 ASN G  57     7364   6579  10915   2058    559    586       N  
ATOM   9291  N   PRO G  58      96.007 -98.160  52.737  1.00 62.59           N  
ANISOU 9291  N   PRO G  58     7312   5666  10803    606   -233    432       N  
ATOM   9292  CA  PRO G  58      95.460 -99.152  51.805  1.00 63.89           C  
ANISOU 9292  CA  PRO G  58     7440   5838  10997    614   -279    419       C  
ATOM   9293  C   PRO G  58      94.534 -98.561  50.778  1.00 64.03           C  
ANISOU 9293  C   PRO G  58     7429   5869  11032    637   -287    422       C  
ATOM   9294  O   PRO G  58      94.322 -99.190  49.754  1.00 64.97           O  
ANISOU 9294  O   PRO G  58     7522   6000  11165    648   -329    408       O  
ATOM   9295  CB  PRO G  58      94.697-100.109  52.716  1.00 67.36           C  
ANISOU 9295  CB  PRO G  58     7864   6254  11476    594   -272    426       C  
ATOM   9296  CG  PRO G  58      95.339 -99.963  54.041  1.00 66.67           C  
ANISOU 9296  CG  PRO G  58     7812   6151  11370    573   -236    434       C  
ATOM   9297  CD  PRO G  58      95.678 -98.504  54.132  1.00 63.46           C  
ANISOU 9297  CD  PRO G  58     7430   5751  10931    583   -201    445       C  
ATOM   9298  N   LYS G  59      93.989 -97.382  51.029  1.00 64.18           N  
ANISOU 9298  N   LYS G  59     7450   5885  11050    646   -249    440       N  
ATOM   9299  CA  LYS G  59      93.067 -96.817  50.051  1.00 64.59           C  
ANISOU 9299  CA  LYS G  59     7472   5949  11120    668   -257    444       C  
ATOM   9300  C   LYS G  59      93.850 -96.181  48.931  1.00 63.66           C  
ANISOU 9300  C   LYS G  59     7364   5856  10966    688   -277    432       C  
ATOM   9301  O   LYS G  59      93.295 -95.932  47.847  1.00 63.96           O  
ANISOU 9301  O   LYS G  59     7377   5909  11015    708   -298    429       O  
ATOM   9302  CB  LYS G  59      92.114 -95.793  50.680  1.00 64.83           C  
ANISOU 9302  CB  LYS G  59     7499   5968  11167    671   -210    467       C  
ATOM   9303  CG  LYS G  59      91.029 -96.399  51.517  1.00 65.95           C  
ANISOU 9303  CG  LYS G  59     7620   6086  11353    656   -195    479       C  
ATOM   9304  CD  LYS G  59      90.423 -95.346  52.390  1.00 65.98           C  
ANISOU 9304  CD  LYS G  59     7631   6076  11361    654   -143    502       C  
ATOM   9305  CE  LYS G  59      89.639 -95.940  53.546  1.00 66.87           C  
ANISOU 9305  CE  LYS G  59     7734   6163  11509    634   -120    514       C  
ATOM   9306  NZ  LYS G  59      88.988 -94.868  54.371  1.00 67.11           N  
ANISOU 9306  NZ  LYS G  59     7771   6180  11546    633    -68    536       N  
ATOM   9307  N   VAL G  60      95.137 -95.924  49.194  1.00 61.75           N  
ANISOU 9307  N   VAL G  60     7160   5620  10682    682   -271    426       N  
ATOM   9308  CA  VAL G  60      95.969 -95.228  48.218  1.00 60.77           C  
ANISOU 9308  CA  VAL G  60     7050   5519  10519    700   -286    415       C  
ATOM   9309  C   VAL G  60      96.334 -96.156  47.075  1.00 60.93           C  
ANISOU 9309  C   VAL G  60     7054   5557  10540    708   -342    393       C  
ATOM   9310  O   VAL G  60      96.179 -95.776  45.913  1.00 60.84           O  
ANISOU 9310  O   VAL G  60     7028   5565  10525    729   -364    386       O  
ATOM   9311  CB  VAL G  60      97.254 -94.664  48.812  1.00 59.56           C  
ANISOU 9311  CB  VAL G  60     6942   5368  10320    692   -264    415       C  
ATOM   9312  CG1 VAL G  60      97.950 -93.851  47.775  1.00 59.42           C  
ANISOU 9312  CG1 VAL G  60     6935   5375  10266    713   -277    406       C  
ATOM   9313  CG2 VAL G  60      96.962 -93.827  50.011  1.00 59.57           C  
ANISOU 9313  CG2 VAL G  60     6961   5351  10320    683   -210    437       C  
ATOM   9314  N   LYS G  61      96.811 -97.364  47.379  1.00 59.87           N  
ANISOU 9314  N   LYS G  61     6923   5416  10410    691   -364    380       N  
ATOM   9315  CA  LYS G  61      97.225 -98.241  46.292  1.00 59.98           C  
ANISOU 9315  CA  LYS G  61     6923   5446  10422    698   -417    358       C  
ATOM   9316  C   LYS G  61      95.985 -98.759  45.651  1.00 61.18           C  
ANISOU 9316  C   LYS G  61     7031   5598  10618    707   -440    358       C  
ATOM   9317  O   LYS G  61      95.961 -99.017  44.451  1.00 61.32           O  
ANISOU 9317  O   LYS G  61     7028   5633  10636    722   -478    344       O  
ATOM   9318  CB  LYS G  61      98.115 -99.390  46.761  1.00 59.89           C  
ANISOU 9318  CB  LYS G  61     6926   5427  10401    679   -436    344       C  
ATOM   9319  CG  LYS G  61      97.732-100.012  48.092  1.00 60.55           C  
ANISOU 9319  CG  LYS G  61     7013   5485  10510    655   -412    355       C  
ATOM   9320  CD  LYS G  61      98.691-101.156  48.441  1.00 60.43           C  
ANISOU 9320  CD  LYS G  61     7012   5464  10483    637   -435    339       C  
ATOM   9321  CE  LYS G  61     100.127-100.645  48.711  1.00 59.09           C  
ANISOU 9321  CE  LYS G  61     6886   5303  10264    633   -424    334       C  
ATOM   9322  NZ  LYS G  61     100.307-100.074  50.083  1.00 58.73           N  
ANISOU 9322  NZ  LYS G  61     6869   5238  10207    617   -375    352       N  
ATOM   9323  N   ALA G  62      94.946 -98.883  46.469  1.00 59.31           N  
ANISOU 9323  N   ALA G  62     6778   5340  10416    697   -415    374       N  
ATOM   9324  CA  ALA G  62      93.634 -99.301  45.998  1.00 60.52           C  
ANISOU 9324  CA  ALA G  62     6889   5491  10614    704   -430    377       C  
ATOM   9325  C   ALA G  62      93.211 -98.341  44.923  1.00 60.36           C  
ANISOU 9325  C   ALA G  62     6855   5490  10590    730   -435    380       C  
ATOM   9326  O   ALA G  62      92.745 -98.737  43.862  1.00 60.92           O  
ANISOU 9326  O   ALA G  62     6896   5573  10678    743   -471    370       O  
ATOM   9327  CB  ALA G  62      92.624 -99.322  47.131  1.00 61.32           C  
ANISOU 9327  CB  ALA G  62     6982   5568  10750    691   -394    397       C  
ATOM   9328  N   HIS G  63      93.411 -97.062  45.209  1.00 60.36           N  
ANISOU 9328  N   HIS G  63     6877   5492  10566    736   -398    393       N  
ATOM   9329  CA  HIS G  63      93.098 -96.015  44.259  1.00 60.10           C  
ANISOU 9329  CA  HIS G  63     6834   5476  10524    760   -398    396       C  
ATOM   9330  C   HIS G  63      94.046 -96.023  43.069  1.00 59.38           C  
ANISOU 9330  C   HIS G  63     6750   5410  10401    774   -436    376       C  
ATOM   9331  O   HIS G  63      93.612 -96.029  41.930  1.00 59.73           O  
ANISOU 9331  O   HIS G  63     6769   5470  10456    791   -465    369       O  
ATOM   9332  CB  HIS G  63      93.139 -94.653  44.935  1.00 59.39           C  
ANISOU 9332  CB  HIS G  63     6769   5382  10416    762   -348    415       C  
ATOM   9333  CG  HIS G  63      92.512 -93.572  44.114  1.00 59.35           C  
ANISOU 9333  CG  HIS G  63     6749   5390  10412    785   -342    423       C  
ATOM   9334  ND1 HIS G  63      91.603 -92.675  44.629  1.00 59.60           N  
ANISOU 9334  ND1 HIS G  63     6775   5411  10461    789   -301    444       N  
ATOM   9335  CD2 HIS G  63      92.649 -93.263  42.804  1.00 59.13           C  
ANISOU 9335  CD2 HIS G  63     6709   5385  10371    806   -371    412       C  
ATOM   9336  CE1 HIS G  63      91.212 -91.856  43.670  1.00 59.53           C  
ANISOU 9336  CE1 HIS G  63     6751   5418  10449    811   -307    447       C  
ATOM   9337  NE2 HIS G  63      91.830 -92.195  42.553  1.00 59.24           N  
ANISOU 9337  NE2 HIS G  63     6712   5402  10395    822   -349    428       N  
ATOM   9338  N   GLY G  64      95.343 -96.033  43.339  1.00 59.89           N  
ANISOU 9338  N   GLY G  64     6849   5479  10427    766   -436    367       N  
ATOM   9339  CA  GLY G  64      96.343 -96.047  42.282  1.00 59.72           C  
ANISOU 9339  CA  GLY G  64     6838   5481  10372    778   -470    348       C  
ATOM   9340  C   GLY G  64      96.058 -97.068  41.194  1.00 59.83           C  
ANISOU 9340  C   GLY G  64     6820   5507  10407    785   -522    330       C  
ATOM   9341  O   GLY G  64      96.257 -96.790  40.007  1.00 59.82           O  
ANISOU 9341  O   GLY G  64     6810   5526  10391    803   -549    319       O  
ATOM   9342  N   LYS G  65      95.561 -98.241  41.604  1.00 59.15           N  
ANISOU 9342  N   LYS G  65     6714   5405  10354    771   -536    327       N  
ATOM   9343  CA  LYS G  65      95.283 -99.332  40.684  1.00 59.26           C  
ANISOU 9343  CA  LYS G  65     6698   5427  10390    775   -584    311       C  
ATOM   9344  C   LYS G  65      94.335 -98.843  39.602  1.00 59.44           C  
ANISOU 9344  C   LYS G  65     6690   5464  10432    797   -598    314       C  
ATOM   9345  O   LYS G  65      94.634 -98.956  38.404  1.00 59.42           O  
ANISOU 9345  O   LYS G  65     6677   5482  10418    812   -635    298       O  
ATOM   9346  CB  LYS G  65      94.700-100.530  41.429  1.00 59.39           C  
ANISOU 9346  CB  LYS G  65     6698   5423  10445    756   -589    312       C  
ATOM   9347  CG  LYS G  65      94.857-101.851  40.676  1.00 59.43           C  
ANISOU 9347  CG  LYS G  65     6682   5435  10462    754   -641    290       C  
ATOM   9348  CD  LYS G  65      94.697-103.046  41.611  1.00 59.48           C  
ANISOU 9348  CD  LYS G  65     6685   5420  10495    731   -643    290       C  
ATOM   9349  CE  LYS G  65      94.220-104.304  40.866  1.00 59.63           C  
ANISOU 9349  CE  LYS G  65     6670   5442  10545    732   -689    275       C  
ATOM   9350  NZ  LYS G  65      93.881-105.420  41.798  1.00 59.72           N  
ANISOU 9350  NZ  LYS G  65     6673   5430  10586    710   -689    277       N  
ATOM   9351  N   LYS G  66      93.214 -98.266  40.044  1.00 60.22           N  
ANISOU 9351  N   LYS G  66     6772   5550  10557    799   -567    334       N  
ATOM   9352  CA  LYS G  66      92.187 -97.739  39.160  1.00 60.76           C  
ANISOU 9352  CA  LYS G  66     6810   5629  10647    819   -573    340       C  
ATOM   9353  C   LYS G  66      92.768 -96.697  38.219  1.00 59.82           C  
ANISOU 9353  C   LYS G  66     6703   5533  10491    840   -578    336       C  
ATOM   9354  O   LYS G  66      92.380 -96.642  37.041  1.00 60.11           O  
ANISOU 9354  O   LYS G  66     6716   5587  10536    857   -607    329       O  
ATOM   9355  CB  LYS G  66      91.055 -97.159  39.986  1.00 61.35           C  
ANISOU 9355  CB  LYS G  66     6875   5686  10751    816   -531    364       C  
ATOM   9356  CG  LYS G  66      90.110 -98.221  40.507  1.00 62.60           C  
ANISOU 9356  CG  LYS G  66     7006   5825  10955    803   -537    367       C  
ATOM   9357  CD  LYS G  66      88.942 -97.647  41.314  1.00 63.27           C  
ANISOU 9357  CD  LYS G  66     7078   5890  11070    800   -495    391       C  
ATOM   9358  CE  LYS G  66      89.455 -96.884  42.552  1.00 62.50           C  
ANISOU 9358  CE  LYS G  66     7018   5780  10949    788   -446    405       C  
ATOM   9359  NZ  LYS G  66      88.366 -96.071  43.222  1.00 63.01           N  
ANISOU 9359  NZ  LYS G  66     7074   5830  11038    789   -403    429       N  
ATOM   9360  N   VAL G  67      93.721 -95.907  38.743  1.00 58.88           N  
ANISOU 9360  N   VAL G  67     6623   5416  10334    836   -550    339       N  
ATOM   9361  CA  VAL G  67      94.419 -94.875  37.985  1.00 58.73           C  
ANISOU 9361  CA  VAL G  67     6621   5418  10276    854   -551    336       C  
ATOM   9362  C   VAL G  67      95.367 -95.490  37.004  1.00 58.60           C  
ANISOU 9362  C   VAL G  67     6608   5421  10236    859   -597    312       C  
ATOM   9363  O   VAL G  67      95.467 -95.067  35.855  1.00 58.59           O  
ANISOU 9363  O   VAL G  67     6599   5441  10222    878   -619    304       O  
ATOM   9364  CB  VAL G  67      95.241 -93.964  38.864  1.00 58.53           C  
ANISOU 9364  CB  VAL G  67     6636   5387  10214    847   -510    345       C  
ATOM   9365  CG1 VAL G  67      95.619 -92.729  38.090  1.00 58.43           C  
ANISOU 9365  CG1 VAL G  67     6636   5395  10170    867   -505    346       C  
ATOM   9366  CG2 VAL G  67      94.491 -93.609  40.105  1.00 58.63           C  
ANISOU 9366  CG2 VAL G  67     6651   5376  10248    835   -464    367       C  
ATOM   9367  N   LEU G  68      96.099 -96.481  37.494  1.00 60.02           N  
ANISOU 9367  N   LEU G  68     6802   5594  10410    841   -610    300       N  
ATOM   9368  CA  LEU G  68      97.044 -97.217  36.679  1.00 59.89           C  
ANISOU 9368  CA  LEU G  68     6789   5593  10372    843   -654    276       C  
ATOM   9369  C   LEU G  68      96.310 -97.897  35.555  1.00 60.08           C  
ANISOU 9369  C   LEU G  68     6774   5628  10426    854   -696    265       C  
ATOM   9370  O   LEU G  68      96.761 -97.891  34.404  1.00 60.03           O  
ANISOU 9370  O   LEU G  68     6763   5643  10401    868   -730    250       O  
ATOM   9371  CB  LEU G  68      97.781 -98.235  37.525  1.00 59.77           C  
ANISOU 9371  CB  LEU G  68     6792   5564  10352    820   -658    267       C  
ATOM   9372  CG  LEU G  68      98.672 -99.283  36.874  1.00 59.65           C  
ANISOU 9372  CG  LEU G  68     6779   5561  10325    817   -704    242       C  
ATOM   9373  CD1 LEU G  68      99.838 -98.658  36.146  1.00 59.43           C  
ANISOU 9373  CD1 LEU G  68     6775   5555  10249    829   -715    230       C  
ATOM   9374  CD2 LEU G  68      99.119-100.159  37.998  1.00 59.57           C  
ANISOU 9374  CD2 LEU G  68     6785   5531  10318    793   -696    241       C  
ATOM   9375  N   GLY G  69      95.170 -98.485  35.904  1.00 62.40           N  
ANISOU 9375  N   GLY G  69     7039   5905  10764    848   -695    274       N  
ATOM   9376  CA  GLY G  69      94.295 -99.055  34.913  1.00 63.37           C  
ANISOU 9376  CA  GLY G  69     7122   6037  10919    859   -730    267       C  
ATOM   9377  C   GLY G  69      93.969 -97.972  33.907  1.00 63.11           C  
ANISOU 9377  C   GLY G  69     7080   6023  10877    883   -732    271       C  
ATOM   9378  O   GLY G  69      94.231 -98.152  32.716  1.00 63.03           O  
ANISOU 9378  O   GLY G  69     7058   6033  10857    896   -769    255       O  
ATOM   9379  N   ALA G  70      93.449 -96.840  34.387  1.00 65.07           N  
ANISOU 9379  N   ALA G  70     7334   6265  11126    888   -690    292       N  
ATOM   9380  CA  ALA G  70      93.100 -95.730  33.513  1.00 64.82           C  
ANISOU 9380  CA  ALA G  70     7294   6250  11086    910   -687    298       C  
ATOM   9381  C   ALA G  70      94.227 -95.415  32.519  1.00 63.81           C  
ANISOU 9381  C   ALA G  70     7183   6147  10915    922   -713    281       C  
ATOM   9382  O   ALA G  70      93.965 -95.121  31.353  1.00 63.89           O  
ANISOU 9382  O   ALA G  70     7175   6177  10925    941   -737    275       O  
ATOM   9383  CB  ALA G  70      92.758 -94.518  34.330  1.00 64.49           C  
ANISOU 9383  CB  ALA G  70     7266   6197  11040    911   -635    321       C  
ATOM   9384  N   PHE G  71      95.477 -95.493  32.970  1.00 66.13           N  
ANISOU 9384  N   PHE G  71     7512   6442  11173    912   -708    272       N  
ATOM   9385  CA  PHE G  71      96.605 -95.353  32.059  1.00 65.22           C  
ANISOU 9385  CA  PHE G  71     7413   6349  11017    922   -735    254       C  
ATOM   9386  C   PHE G  71      96.741 -96.565  31.110  1.00 65.72           C  
ANISOU 9386  C   PHE G  71     7455   6424  11091    923   -789    231       C  
ATOM   9387  O   PHE G  71      97.154 -96.403  29.959  1.00 65.36           O  
ANISOU 9387  O   PHE G  71     7406   6401  11026    938   -819    218       O  
ATOM   9388  CB  PHE G  71      97.912 -95.151  32.837  1.00 64.10           C  
ANISOU 9388  CB  PHE G  71     7315   6204  10835    909   -716    251       C  
ATOM   9389  CG  PHE G  71      98.254 -93.698  33.110  1.00 63.14           C  
ANISOU 9389  CG  PHE G  71     7220   6087  10683    917   -677    265       C  
ATOM   9390  CD1 PHE G  71      98.190 -93.183  34.402  1.00 62.91           C  
ANISOU 9390  CD1 PHE G  71     7212   6039  10653    905   -629    283       C  
ATOM   9391  CD2 PHE G  71      98.657 -92.851  32.082  1.00 62.87           C  
ANISOU 9391  CD2 PHE G  71     7191   6075  10620    937   -688    259       C  
ATOM   9392  CE1 PHE G  71      98.503 -91.860  34.653  1.00 62.79           C  
ANISOU 9392  CE1 PHE G  71     7222   6027  10609    912   -594    295       C  
ATOM   9393  CE2 PHE G  71      98.959 -91.522  32.338  1.00 62.76           C  
ANISOU 9393  CE2 PHE G  71     7202   6065  10578    944   -652    272       C  
ATOM   9394  CZ  PHE G  71      98.880 -91.034  33.618  1.00 62.72           C  
ANISOU 9394  CZ  PHE G  71     7217   6041  10573    932   -605    290       C  
ATOM   9395  N   SER G  72      96.416 -97.774  31.571  1.00 68.62           N  
ANISOU 9395  N   SER G  72     7807   6776  11488    908   -802    227       N  
ATOM   9396  CA  SER G  72      96.539 -98.949  30.694  1.00 69.12           C  
ANISOU 9396  CA  SER G  72     7851   6850  11563    908   -854    205       C  
ATOM   9397  C   SER G  72      95.637 -98.770  29.468  1.00 71.55           C  
ANISOU 9397  C   SER G  72     8122   7172  11890    928   -879    204       C  
ATOM   9398  O   SER G  72      95.998 -99.165  28.355  1.00 72.95           O  
ANISOU 9398  O   SER G  72     8290   7369  12059    938   -919    186       O  
ATOM   9399  CB  SER G  72      96.179-100.256  31.419  1.00 70.07           C  
ANISOU 9399  CB  SER G  72     7958   6949  11716    889   -862    203       C  
ATOM   9400  OG  SER G  72      96.927-100.463  32.599  1.00 69.53           O  
ANISOU 9400  OG  SER G  72     7920   6865  11632    869   -838    205       O  
ATOM   9401  N   ASP G  73      94.471 -98.165  29.689  1.00 75.52           N  
ANISOU 9401  N   ASP G  73     8607   7667  12421    934   -854    224       N  
ATOM   9402  CA  ASP G  73      93.482 -97.958  28.642  1.00 78.94           C  
ANISOU 9402  CA  ASP G  73     9005   8112  12878    952   -873    226       C  
ATOM   9403  C   ASP G  73      94.065 -97.039  27.573  1.00 78.00           C  
ANISOU 9403  C   ASP G  73     8896   8019  12723    972   -884    219       C  
ATOM   9404  O   ASP G  73      93.727 -97.139  26.394  1.00 80.98           O  
ANISOU 9404  O   ASP G  73     9249   8413  13108    987   -917    210       O  
ATOM   9405  CB  ASP G  73      92.192 -97.369  29.237  1.00 79.78           C  
ANISOU 9405  CB  ASP G  73     9093   8202  13017    954   -838    250       C  
ATOM   9406  CG  ASP G  73      90.946 -97.816  28.497  1.00 84.48           C  
ANISOU 9406  CG  ASP G  73     9644   8799  13654    963   -862    251       C  
ATOM   9407  OD1 ASP G  73      91.036 -98.792  27.721  1.00 86.48           O  
ANISOU 9407  OD1 ASP G  73     9880   9062  13916    964   -906    233       O  
ATOM   9408  OD2 ASP G  73      89.870 -97.215  28.701  1.00 86.38           O  
ANISOU 9408  OD2 ASP G  73     9868   9032  13921    969   -838    270       O  
ATOM   9409  N   GLY G  74      94.954 -96.145  27.997  1.00 81.93           N  
ANISOU 9409  N   GLY G  74     9430   8519  13182    972   -857    223       N  
ATOM   9410  CA  GLY G  74      95.586 -95.217  27.081  1.00 80.90           C  
ANISOU 9410  CA  GLY G  74     9312   8411  13014    989   -864    218       C  
ATOM   9411  C   GLY G  74      96.460 -95.965  26.095  1.00 81.75           C  
ANISOU 9411  C   GLY G  74     9420   8538  13102    992   -911    192       C  
ATOM   9412  O   GLY G  74      96.287 -95.852  24.881  1.00 84.21           O  
ANISOU 9412  O   GLY G  74     9713   8870  13413   1009   -941    183       O  
ATOM   9413  N   LEU G  75      97.394 -96.749  26.624  1.00 83.28           N  
ANISOU 9413  N   LEU G  75     9635   8726  13282    976   -919    180       N  
ATOM   9414  CA  LEU G  75      98.276 -97.558  25.796  1.00 84.02           C  
ANISOU 9414  CA  LEU G  75     9730   8835  13357    977   -963    154       C  
ATOM   9415  C   LEU G  75      97.487 -98.484  24.884  1.00 88.62           C  
ANISOU 9415  C   LEU G  75    10273   9424  13973    982  -1005    144       C  
ATOM   9416  O   LEU G  75      97.950 -98.841  23.798  1.00 90.09           O  
ANISOU 9416  O   LEU G  75    10453   9630  14147    991  -1044    125       O  
ATOM   9417  CB  LEU G  75      99.213 -98.368  26.674  1.00 81.77           C  
ANISOU 9417  CB  LEU G  75     9470   8538  13059    956   -962    145       C  
ATOM   9418  CG  LEU G  75     100.063 -97.431  27.516  1.00 77.37           C  
ANISOU 9418  CG  LEU G  75     8955   7977  12466    951   -922    155       C  
ATOM   9419  CD1 LEU G  75     101.037 -98.224  28.378  1.00 75.12           C  
ANISOU 9419  CD1 LEU G  75     8695   7680  12166    931   -920    146       C  
ATOM   9420  CD2 LEU G  75     100.809 -96.484  26.587  1.00 76.07           C  
ANISOU 9420  CD2 LEU G  75     8806   7838  12261    969   -929    148       C  
ATOM   9421  N   ALA G  76      96.299 -98.879  25.340  1.00 86.26           N  
ANISOU 9421  N   ALA G  76     9948   9108  13719    977   -996    156       N  
ATOM   9422  CA  ALA G  76      95.414 -99.718  24.541  1.00 91.03           C  
ANISOU 9422  CA  ALA G  76    10512   9716  14359    982  -1033    149       C  
ATOM   9423  C   ALA G  76      94.985 -98.979  23.278  1.00 93.52           C  
ANISOU 9423  C   ALA G  76    10809  10053  14672   1005  -1049    148       C  
ATOM   9424  O   ALA G  76      95.240 -99.431  22.164  1.00 96.30           O  
ANISOU 9424  O   ALA G  76    11148  10423  15018   1014  -1091    130       O  
ATOM   9425  CB  ALA G  76      94.197-100.146  25.350  1.00 92.93           C  
ANISOU 9425  CB  ALA G  76    10729   9933  14647    972  -1015    164       C  
ATOM   9426  N   HIS G  77      94.328 -97.843  23.439  1.00 93.76           N  
ANISOU 9426  N   HIS G  77     9132  10713  15778   1858  -1369  -2415       N  
ATOM   9427  CA  HIS G  77      93.969 -97.074  22.261  1.00 95.97           C  
ANISOU 9427  CA  HIS G  77     9445  11016  16005   1834  -1367  -2378       C  
ATOM   9428  C   HIS G  77      94.607 -95.682  22.286  1.00 92.88           C  
ANISOU 9428  C   HIS G  77     9031  10623  15638   1830  -1341  -2342       C  
ATOM   9429  O   HIS G  77      94.058 -94.750  22.888  1.00 90.53           O  
ANISOU 9429  O   HIS G  77     8712  10314  15370   1832  -1370  -2305       O  
ATOM   9430  CB  HIS G  77      92.439 -97.004  22.177  1.00 98.28           C  
ANISOU 9430  CB  HIS G  77     9756  11312  16273   1825  -1427  -2351       C  
ATOM   9431  CG  HIS G  77      91.764 -98.227  22.731  1.00 99.59           C  
ANISOU 9431  CG  HIS G  77     9925  11469  16447   1836  -1460  -2384       C  
ATOM   9432  ND1 HIS G  77      91.487 -98.379  24.073  1.00 96.72           N  
ANISOU 9432  ND1 HIS G  77     9527  11080  16143   1857  -1485  -2391       N  
ATOM   9433  CD2 HIS G  77      91.357 -99.373  22.135  1.00103.74           C  
ANISOU 9433  CD2 HIS G  77    10483  12005  16927   1830  -1469  -2413       C  
ATOM   9434  CE1 HIS G  77      90.921 -99.556  24.278  1.00 99.01           C  
ANISOU 9434  CE1 HIS G  77     9828  11365  16425   1863  -1508  -2423       C  
ATOM   9435  NE2 HIS G  77      90.829-100.178  23.117  1.00103.28           N  
ANISOU 9435  NE2 HIS G  77    10410  11929  16904   1847  -1500  -2437       N  
ATOM   9436  N   LEU G  78      95.710 -95.527  21.548  1.00 97.28           N  
ANISOU 9436  N   LEU G  78     9595  11190  16176   1823  -1287  -2351       N  
ATOM   9437  CA  LEU G  78      96.504 -94.292  21.567  1.00 94.55           C  
ANISOU 9437  CA  LEU G  78     9227  10842  15857   1820  -1254  -2323       C  
ATOM   9438  C   LEU G  78      96.082 -93.331  20.474  1.00 96.72           C  
ANISOU 9438  C   LEU G  78     9533  11136  16080   1796  -1254  -2278       C  
ATOM   9439  O   LEU G  78      96.501 -92.183  20.449  1.00 94.98           O  
ANISOU 9439  O   LEU G  78     9298  10914  15877   1792  -1235  -2247       O  
ATOM   9440  CB  LEU G  78      97.994 -94.603  21.410  1.00 92.86           C  
ANISOU 9440  CB  LEU G  78     9000  10626  15658   1826  -1192  -2358       C  
ATOM   9441  CG  LEU G  78      98.737 -95.397  22.494  1.00 89.84           C  
ANISOU 9441  CG  LEU G  78     8581  10222  15334   1851  -1181  -2402       C  
ATOM   9442  CD1 LEU G  78     100.115 -95.837  22.002  1.00 89.70           C  
ANISOU 9442  CD1 LEU G  78     8561  10207  15315   1852  -1118  -2437       C  
ATOM   9443  CD2 LEU G  78      98.881 -94.555  23.743  1.00 85.83           C  
ANISOU 9443  CD2 LEU G  78     8025   9691  14897   1867  -1196  -2383       C  
ATOM   9444  N   ASP G  79      95.267 -93.812  19.550  1.00 97.82           N  
ANISOU 9444  N   ASP G  79     9719  11294  16156   1781  -1276  -2276       N  
ATOM   9445  CA  ASP G  79      94.739 -92.956  18.497  1.00 99.91           C  
ANISOU 9445  CA  ASP G  79    10018  11576  16367   1758  -1283  -2233       C  
ATOM   9446  C   ASP G  79      93.503 -92.171  18.955  1.00 99.31           C  
ANISOU 9446  C   ASP G  79     9934  11495  16306   1757  -1341  -2188       C  
ATOM   9447  O   ASP G  79      93.338 -91.000  18.628  1.00 99.56           O  
ANISOU 9447  O   ASP G  79     9968  11531  16330   1745  -1342  -2145       O  
ATOM   9448  CB  ASP G  79      94.431 -93.793  17.257  1.00105.05           C  
ANISOU 9448  CB  ASP G  79    10725  12248  16941   1742  -1281  -2249       C  
ATOM   9449  CG  ASP G  79      95.688 -94.213  16.526  1.00105.62           C  
ANISOU 9449  CG  ASP G  79    10812  12328  16990   1738  -1215  -2281       C  
ATOM   9450  OD1 ASP G  79      96.739 -93.565  16.749  1.00102.33           O  
ANISOU 9450  OD1 ASP G  79    10368  11904  16610   1742  -1171  -2277       O  
ATOM   9451  OD2 ASP G  79      95.616 -95.182  15.735  1.00109.43           O  
ANISOU 9451  OD2 ASP G  79    11334  12823  17421   1730  -1208  -2308       O  
ATOM   9452  N   ASN G  80      92.624 -92.836  19.688  1.00 94.66           N  
ANISOU 9452  N   ASN G  80     9335  10895  15735   1767  -1388  -2200       N  
ATOM   9453  CA  ASN G  80      91.487 -92.198  20.353  1.00 93.90           C  
ANISOU 9453  CA  ASN G  80     9223  10788  15665   1770  -1442  -2164       C  
ATOM   9454  C   ASN G  80      91.719 -91.860  21.836  1.00 89.29           C  
ANISOU 9454  C   ASN G  80     8587  10178  15161   1792  -1448  -2164       C  
ATOM   9455  O   ASN G  80      91.057 -92.450  22.690  1.00 88.95           O  
ANISOU 9455  O   ASN G  80     8529  10120  15147   1805  -1484  -2178       O  
ATOM   9456  CB  ASN G  80      90.182 -92.958  20.184  1.00 97.24           C  
ANISOU 9456  CB  ASN G  80     9672  11216  16059   1765  -1495  -2168       C  
ATOM   9457  CG  ASN G  80      88.974 -92.110  20.597  1.00 99.53           C  
ANISOU 9457  CG  ASN G  80     9951  11498  16367   1763  -1548  -2122       C  
ATOM   9458  OD1 ASN G  80      89.091 -90.896  20.817  1.00 99.77           O  
ANISOU 9458  OD1 ASN G  80     9962  11523  16422   1761  -1544  -2083       O  
ATOM   9459  ND2 ASN G  80      87.817 -92.748  20.715  1.00101.37           N  
ANISOU 9459  ND2 ASN G  80    10195  11729  16591   1762  -1597  -2126       N  
ATOM   9460  N   LEU G  81      92.839 -91.239  22.167  1.00 92.18           N  
ANISOU 9460  N   LEU G  81     8924  10536  15563   1798  -1406  -2164       N  
ATOM   9461  CA  LEU G  81      93.050 -90.756  23.531  1.00 87.98           C  
ANISOU 9461  CA  LEU G  81     8345   9978  15105   1818  -1413  -2158       C  
ATOM   9462  C   LEU G  81      91.958 -89.843  24.083  1.00 87.39           C  
ANISOU 9462  C   LEU G  81     8258   9894  15053   1817  -1460  -2113       C  
ATOM   9463  O   LEU G  81      91.572 -89.986  25.249  1.00 85.50           O  
ANISOU 9463  O   LEU G  81     7990   9632  14863   1833  -1488  -2118       O  
ATOM   9464  CB  LEU G  81      94.373 -90.025  23.610  1.00 85.26           C  
ANISOU 9464  CB  LEU G  81     7975   9630  14789   1820  -1362  -2156       C  
ATOM   9465  CG  LEU G  81      95.569 -90.955  23.497  1.00 84.10           C  
ANISOU 9465  CG  LEU G  81     7826   9483  14645   1829  -1315  -2207       C  
ATOM   9466  CD1 LEU G  81      96.858 -90.135  23.568  1.00 85.39           C  
ANISOU 9466  CD1 LEU G  81     7962   9641  14841   1831  -1265  -2202       C  
ATOM   9467  CD2 LEU G  81      95.516 -92.024  24.585  1.00 82.20           C  
ANISOU 9467  CD2 LEU G  81     7564   9223  14445   1851  -1334  -2247       C  
ATOM   9468  N   LYS G  82      91.495 -88.897  23.259  1.00 82.54           N  
ANISOU 9468  N   LYS G  82     7664   9294  14403   1798  -1468  -2069       N  
ATOM   9469  CA  LYS G  82      90.460 -87.947  23.658  1.00 82.47           C  
ANISOU 9469  CA  LYS G  82     7645   9277  14413   1795  -1511  -2022       C  
ATOM   9470  C   LYS G  82      89.261 -88.714  24.143  1.00 83.93           C  
ANISOU 9470  C   LYS G  82     7834   9454  14603   1801  -1563  -2031       C  
ATOM   9471  O   LYS G  82      88.827 -88.557  25.275  1.00 81.92           O  
ANISOU 9471  O   LYS G  82     7550   9177  14400   1816  -1588  -2025       O  
ATOM   9472  CB  LYS G  82      90.072 -87.032  22.494  1.00 85.33           C  
ANISOU 9472  CB  LYS G  82     8038   9661  14724   1772  -1513  -1978       C  
ATOM   9473  CG  LYS G  82      89.085 -85.923  22.871  1.00 86.09           C  
ANISOU 9473  CG  LYS G  82     8122   9747  14841   1769  -1554  -1926       C  
ATOM   9474  CD  LYS G  82      88.465 -85.246  21.646  1.00 90.18           C  
ANISOU 9474  CD  LYS G  82     8677  10287  15301   1746  -1567  -1886       C  
ATOM   9475  CE  LYS G  82      89.438 -84.289  20.959  1.00 90.34           C  
ANISOU 9475  CE  LYS G  82     8703  10318  15304   1735  -1520  -1866       C  
ATOM   9476  NZ  LYS G  82      88.751 -83.538  19.852  1.00 90.40           N  
ANISOU 9476  NZ  LYS G  82     8747  10343  15257   1714  -1537  -1822       N  
ATOM   9477  N   GLY G  83      88.765 -89.588  23.282  1.00 83.79           N  
ANISOU 9477  N   GLY G  83     7854   9453  14530   1791  -1576  -2047       N  
ATOM   9478  CA  GLY G  83      87.563 -90.351  23.558  1.00 84.80           C  
ANISOU 9478  CA  GLY G  83     7990   9576  14656   1793  -1626  -2055       C  
ATOM   9479  C   GLY G  83      87.643 -91.295  24.739  1.00 84.66           C  
ANISOU 9479  C   GLY G  83     7947   9535  14685   1815  -1632  -2095       C  
ATOM   9480  O   GLY G  83      86.695 -91.405  25.518  1.00 84.89           O  
ANISOU 9480  O   GLY G  83     7963   9547  14745   1823  -1673  -2088       O  
ATOM   9481  N   THR G  84      88.772 -91.981  24.874  1.00 84.13           N  
ANISOU 9481  N   THR G  84     7874   9467  14626   1826  -1591  -2137       N  
ATOM   9482  CA  THR G  84      88.927 -92.959  25.936  1.00 84.00           C  
ANISOU 9482  CA  THR G  84     7836   9430  14651   1847  -1595  -2178       C  
ATOM   9483  C   THR G  84      88.781 -92.275  27.289  1.00 83.06           C  
ANISOU 9483  C   THR G  84     7677   9282  14600   1863  -1611  -2160       C  
ATOM   9484  O   THR G  84      88.121 -92.786  28.196  1.00 83.31           O  
ANISOU 9484  O   THR G  84     7697   9294  14663   1876  -1642  -2172       O  
ATOM   9485  CB  THR G  84      90.278 -93.673  25.833  1.00 83.57           C  
ANISOU 9485  CB  THR G  84     7778   9378  14595   1855  -1545  -2223       C  
ATOM   9486  OG1 THR G  84      90.371 -94.327  24.559  1.00 84.51           O  
ANISOU 9486  OG1 THR G  84     7938   9523  14649   1839  -1530  -2240       O  
ATOM   9487  CG2 THR G  84      90.425 -94.718  26.928  1.00 83.44           C  
ANISOU 9487  CG2 THR G  84     7743   9340  14621   1878  -1551  -2266       C  
ATOM   9488  N   PHE G  85      89.369 -91.091  27.394  1.00 81.41           N  
ANISOU 9488  N   PHE G  85     7449   9071  14413   1862  -1590  -2130       N  
ATOM   9489  CA  PHE G  85      89.322 -90.292  28.615  1.00 78.01           C  
ANISOU 9489  CA  PHE G  85     6982   8614  14046   1876  -1601  -2110       C  
ATOM   9490  C   PHE G  85      88.227 -89.243  28.608  1.00 78.33           C  
ANISOU 9490  C   PHE G  85     7021   8651  14088   1866  -1637  -2057       C  
ATOM   9491  O   PHE G  85      88.151 -88.431  29.529  1.00 76.56           O  
ANISOU 9491  O   PHE G  85     6769   8406  13913   1875  -1646  -2033       O  
ATOM   9492  CB  PHE G  85      90.673 -89.608  28.842  1.00 75.97           C  
ANISOU 9492  CB  PHE G  85     6699   8351  13817   1882  -1556  -2110       C  
ATOM   9493  CG  PHE G  85      91.786 -90.561  29.117  1.00 75.71           C  
ANISOU 9493  CG  PHE G  85     6656   8312  13797   1896  -1522  -2161       C  
ATOM   9494  CD1 PHE G  85      92.562 -91.055  28.085  1.00 76.01           C  
ANISOU 9494  CD1 PHE G  85     6716   8373  13793   1886  -1485  -2185       C  
ATOM   9495  CD2 PHE G  85      92.048 -90.975  30.413  1.00 75.17           C  
ANISOU 9495  CD2 PHE G  85     6561   8216  13785   1919  -1528  -2187       C  
ATOM   9496  CE1 PHE G  85      93.594 -91.943  28.343  1.00 75.78           C  
ANISOU 9496  CE1 PHE G  85     6677   8338  13779   1900  -1453  -2233       C  
ATOM   9497  CE2 PHE G  85      93.073 -91.864  30.681  1.00 74.94           C  
ANISOU 9497  CE2 PHE G  85     6523   8181  13771   1933  -1499  -2234       C  
ATOM   9498  CZ  PHE G  85      93.849 -92.349  29.645  1.00 75.24           C  
ANISOU 9498  CZ  PHE G  85     6579   8242  13768   1923  -1461  -2258       C  
ATOM   9499  N   ALA G  86      87.407 -89.236  27.560  1.00 74.56           N  
ANISOU 9499  N   ALA G  86     6576   8195  13557   1847  -1658  -2037       N  
ATOM   9500  CA  ALA G  86      86.370 -88.205  27.407  1.00 75.63           C  
ANISOU 9500  CA  ALA G  86     6714   8332  13691   1835  -1693  -1985       C  
ATOM   9501  C   ALA G  86      85.512 -88.112  28.657  1.00 73.99           C  
ANISOU 9501  C   ALA G  86     6481   8095  13538   1850  -1730  -1975       C  
ATOM   9502  O   ALA G  86      85.296 -87.029  29.174  1.00 73.20           O  
ANISOU 9502  O   ALA G  86     6360   7981  13471   1851  -1738  -1938       O  
ATOM   9503  CB  ALA G  86      85.511 -88.476  26.187  1.00 80.28           C  
ANISOU 9503  CB  ALA G  86     7342   8945  14217   1815  -1717  -1974       C  
ATOM   9504  N   THR G  87      85.056 -89.251  29.165  1.00 76.03           N  
ANISOU 9504  N   THR G  87     6741   8341  13805   1860  -1749  -2009       N  
ATOM   9505  CA  THR G  87      84.295 -89.239  30.403  1.00 74.75           C  
ANISOU 9505  CA  THR G  87     6556   8148  13696   1875  -1780  -2004       C  
ATOM   9506  C   THR G  87      85.195 -88.878  31.581  1.00 70.36           C  
ANISOU 9506  C   THR G  87     5967   7568  13198   1894  -1756  -2012       C  
ATOM   9507  O   THR G  87      84.865 -87.982  32.355  1.00 68.63           O  
ANISOU 9507  O   THR G  87     5727   7329  13022   1900  -1769  -1981       O  
ATOM   9508  CB  THR G  87      83.603 -90.579  30.682  1.00 76.93           C  
ANISOU 9508  CB  THR G  87     6844   8417  13970   1882  -1805  -2040       C  
ATOM   9509  OG1 THR G  87      83.738 -90.898  32.072  1.00 74.19           O  
ANISOU 9509  OG1 THR G  87     6471   8038  13680   1905  -1806  -2060       O  
ATOM   9510  CG2 THR G  87      84.206 -91.689  29.841  1.00 79.63           C  
ANISOU 9510  CG2 THR G  87     7210   8780  14264   1878  -1783  -2082       C  
ATOM   9511  N   LEU G  88      86.340 -89.546  31.716  1.00 76.02           N  
ANISOU 9511  N   LEU G  88     6679   8285  13919   1905  -1721  -2054       N  
ATOM   9512  CA  LEU G  88      87.256 -89.202  32.808  1.00 72.13           C  
ANISOU 9512  CA  LEU G  88     6156   7769  13483   1923  -1699  -2063       C  
ATOM   9513  C   LEU G  88      87.547 -87.695  32.828  1.00 70.16           C  
ANISOU 9513  C   LEU G  88     5888   7518  13250   1917  -1688  -2018       C  
ATOM   9514  O   LEU G  88      87.664 -87.089  33.894  1.00 67.43           O  
ANISOU 9514  O   LEU G  88     5517   7147  12958   1930  -1692  -2005       O  
ATOM   9515  CB  LEU G  88      88.556 -89.989  32.706  1.00 71.20           C  
ANISOU 9515  CB  LEU G  88     6036   7656  13360   1932  -1660  -2110       C  
ATOM   9516  CG  LEU G  88      88.669 -91.254  33.560  1.00 69.82           C  
ANISOU 9516  CG  LEU G  88     5858   7462  13209   1952  -1665  -2158       C  
ATOM   9517  CD1 LEU G  88      88.049 -92.465  32.890  1.00 72.52           C  
ANISOU 9517  CD1 LEU G  88     6229   7819  13505   1945  -1679  -2185       C  
ATOM   9518  CD2 LEU G  88      90.135 -91.531  33.845  1.00 66.67           C  
ANISOU 9518  CD2 LEU G  88     5442   7058  12830   1965  -1624  -2192       C  
ATOM   9519  N   SER G  89      87.611 -87.093  31.644  1.00 69.47           N  
ANISOU 9519  N   SER G  89     5818   7459  13119   1897  -1677  -1992       N  
ATOM   9520  CA  SER G  89      87.869 -85.670  31.531  1.00 69.18           C  
ANISOU 9520  CA  SER G  89     5768   7423  13093   1889  -1665  -1948       C  
ATOM   9521  C   SER G  89      86.761 -84.879  32.219  1.00 69.29           C  
ANISOU 9521  C   SER G  89     5770   7418  13139   1891  -1704  -1907       C  
ATOM   9522  O   SER G  89      86.996 -83.807  32.796  1.00 68.68           O  
ANISOU 9522  O   SER G  89     5670   7326  13099   1894  -1698  -1879       O  
ATOM   9523  CB  SER G  89      88.002 -85.264  30.058  1.00 70.10           C  
ANISOU 9523  CB  SER G  89     5911   7572  13150   1866  -1649  -1928       C  
ATOM   9524  OG  SER G  89      88.252 -83.866  29.925  1.00 69.83           O  
ANISOU 9524  OG  SER G  89     5865   7540  13126   1858  -1637  -1885       O  
ATOM   9525  N   GLU G  90      85.550 -85.440  32.166  1.00 70.53           N  
ANISOU 9525  N   GLU G  90     5942   7573  13282   1888  -1743  -1906       N  
ATOM   9526  CA  GLU G  90      84.380 -84.792  32.751  1.00 70.72           C  
ANISOU 9526  CA  GLU G  90     5957   7579  13336   1888  -1781  -1869       C  
ATOM   9527  C   GLU G  90      84.475 -84.847  34.274  1.00 67.60           C  
ANISOU 9527  C   GLU G  90     5540   7149  12997   1905  -1782  -1879       C  
ATOM   9528  O   GLU G  90      84.147 -83.853  34.957  1.00 66.26           O  
ANISOU 9528  O   GLU G  90     5378   6966  12831   1888  -1781  -1834       O  
ATOM   9529  CB  GLU G  90      83.089 -85.444  32.250  1.00 74.28           C  
ANISOU 9529  CB  GLU G  90     6430   8037  13755   1879  -1820  -1867       C  
ATOM   9530  CG  GLU G  90      81.912 -85.309  33.202  1.00 74.99           C  
ANISOU 9530  CG  GLU G  90     6507   8099  13887   1887  -1859  -1850       C  
ATOM   9531  CD  GLU G  90      80.560 -85.571  32.537  1.00 78.86           C  
ANISOU 9531  CD  GLU G  90     7017   8599  14347   1873  -1900  -1833       C  
ATOM   9532  OE1 GLU G  90      80.400 -86.653  31.906  1.00 80.63           O  
ANISOU 9532  OE1 GLU G  90     7264   8839  14532   1868  -1906  -1864       O  
ATOM   9533  OE2 GLU G  90      79.666 -84.685  32.655  1.00 80.28           O  
ANISOU 9533  OE2 GLU G  90     7189   8770  14543   1867  -1927  -1790       O  
ATOM   9534  N   LEU G  91      84.953 -85.983  34.801  1.00 63.22           N  
ANISOU 9534  N   LEU G  91     5004   6589  12429   1905  -1764  -1920       N  
ATOM   9535  CA  LEU G  91      85.015 -86.146  36.245  1.00 62.75           C  
ANISOU 9535  CA  LEU G  91     4977   6508  12359   1883  -1746  -1913       C  
ATOM   9536  C   LEU G  91      85.930 -85.087  36.838  1.00 62.63           C  
ANISOU 9536  C   LEU G  91     4957   6485  12353   1873  -1714  -1887       C  
ATOM   9537  O   LEU G  91      85.547 -84.414  37.795  1.00 62.30           O  
ANISOU 9537  O   LEU G  91     4934   6428  12311   1853  -1713  -1851       O  
ATOM   9538  CB  LEU G  91      85.475 -87.546  36.644  1.00 62.64           C  
ANISOU 9538  CB  LEU G  91     4981   6491  12330   1886  -1733  -1962       C  
ATOM   9539  CG  LEU G  91      85.682 -87.689  38.158  1.00 62.18           C  
ANISOU 9539  CG  LEU G  91     4955   6409  12260   1864  -1713  -1956       C  
ATOM   9540  CD1 LEU G  91      84.526 -87.152  38.910  1.00 61.88           C  
ANISOU 9540  CD1 LEU G  91     4937   6356  12220   1845  -1733  -1915       C  
ATOM   9541  CD2 LEU G  91      85.890 -89.106  38.595  1.00 62.05           C  
ANISOU 9541  CD2 LEU G  91     4960   6388  12227   1865  -1707  -2000       C  
ATOM   9542  N   HIS G  92      87.116 -84.924  36.258  1.00 64.73           N  
ANISOU 9542  N   HIS G  92     5200   6764  12630   1886  -1687  -1906       N  
ATOM   9543  CA  HIS G  92      88.116 -84.018  36.815  1.00 63.21           C  
ANISOU 9543  CA  HIS G  92     5003   6565  12449   1877  -1654  -1887       C  
ATOM   9544  C   HIS G  92      87.854 -82.539  36.496  1.00 63.12           C  
ANISOU 9544  C   HIS G  92     4972   6555  12454   1873  -1659  -1838       C  
ATOM   9545  O   HIS G  92      87.962 -81.676  37.379  1.00 62.61           O  
ANISOU 9545  O   HIS G  92     4919   6477  12392   1856  -1648  -1805       O  
ATOM   9546  CB  HIS G  92      89.512 -84.379  36.318  1.00 62.97           C  
ANISOU 9546  CB  HIS G  92     4953   6545  12428   1891  -1620  -1926       C  
ATOM   9547  CG  HIS G  92      89.877 -85.830  36.461  1.00 63.10           C  
ANISOU 9547  CG  HIS G  92     4983   6562  12430   1898  -1612  -1977       C  
ATOM   9548  ND1 HIS G  92      89.184 -86.843  35.830  1.00 63.97           N  
ANISOU 9548  ND1 HIS G  92     5095   6680  12529   1910  -1637  -2005       N  
ATOM   9549  CD2 HIS G  92      90.904 -86.432  37.113  1.00 62.68           C  
ANISOU 9549  CD2 HIS G  92     4941   6502  12372   1894  -1583  -2005       C  
ATOM   9550  CE1 HIS G  92      89.754 -88.004  36.106  1.00 63.73           C  
ANISOU 9550  CE1 HIS G  92     5078   6649  12488   1914  -1622  -2049       C  
ATOM   9551  NE2 HIS G  92      90.804 -87.782  36.877  1.00 63.08           N  
ANISOU 9551  NE2 HIS G  92     5001   6557  12409   1904  -1589  -2049       N  
ATOM   9552  N   CYS G  93      87.537 -82.239  35.235  1.00 65.40           N  
ANISOU 9552  N   CYS G  93     5234   6861  12754   1890  -1678  -1834       N  
ATOM   9553  CA  CYS G  93      87.355 -80.843  34.816  1.00 65.95           C  
ANISOU 9553  CA  CYS G  93     5283   6934  12840   1889  -1683  -1789       C  
ATOM   9554  C   CYS G  93      85.989 -80.242  35.180  1.00 66.71           C  
ANISOU 9554  C   CYS G  93     5394   7022  12932   1874  -1717  -1743       C  
ATOM   9555  O   CYS G  93      85.899 -79.164  35.752  1.00 65.26           O  
ANISOU 9555  O   CYS G  93     5214   6827  12755   1860  -1710  -1702       O  
ATOM   9556  CB  CYS G  93      87.587 -80.735  33.309  1.00 68.56           C  
ANISOU 9556  CB  CYS G  93     5613   7296  13142   1888  -1676  -1789       C  
ATOM   9557  SG  CYS G  93      89.070 -81.683  32.735  1.00 68.26           S  
ANISOU 9557  SG  CYS G  93     5581   7275  13079   1890  -1628  -1842       S  
ATOM   9558  N   ASP G  94      84.913 -80.945  34.855  1.00 66.78           N  
ANISOU 9558  N   ASP G  94     5411   7033  12931   1878  -1753  -1751       N  
ATOM   9559  CA  ASP G  94      83.581 -80.387  35.048  1.00 68.17           C  
ANISOU 9559  CA  ASP G  94     5597   7201  13105   1866  -1787  -1708       C  
ATOM   9560  C   ASP G  94      83.046 -80.549  36.469  1.00 66.61           C  
ANISOU 9560  C   ASP G  94     5435   6979  12894   1842  -1783  -1695       C  
ATOM   9561  O   ASP G  94      82.415 -79.618  37.003  1.00 66.78           O  
ANISOU 9561  O   ASP G  94     5465   6989  12920   1826  -1789  -1650       O  
ATOM   9562  CB  ASP G  94      82.610 -81.009  34.045  1.00 71.77           C  
ANISOU 9562  CB  ASP G  94     6044   7669  13558   1879  -1830  -1720       C  
ATOM   9563  CG  ASP G  94      82.705 -80.367  32.659  1.00 74.09           C  
ANISOU 9563  CG  ASP G  94     6354   7995  13801   1860  -1823  -1692       C  
ATOM   9564  OD1 ASP G  94      82.129 -80.945  31.704  1.00 77.29           O  
ANISOU 9564  OD1 ASP G  94     6787   8422  14159   1847  -1840  -1697       O  
ATOM   9565  OD2 ASP G  94      83.356 -79.298  32.524  1.00 72.92           O  
ANISOU 9565  OD2 ASP G  94     6196   7851  13659   1855  -1800  -1666       O  
ATOM   9566  N   LYS G  95      83.233 -81.737  37.058  1.00 62.46           N  
ANISOU 9566  N   LYS G  95     4931   6447  12354   1840  -1773  -1733       N  
ATOM   9567  CA  LYS G  95      82.766 -81.967  38.433  1.00 62.00           C  
ANISOU 9567  CA  LYS G  95     4909   6366  12284   1818  -1768  -1724       C  
ATOM   9568  C   LYS G  95      83.744 -81.532  39.531  1.00 61.71           C  
ANISOU 9568  C   LYS G  95     4886   6315  12246   1805  -1731  -1718       C  
ATOM   9569  O   LYS G  95      83.350 -80.949  40.532  1.00 61.39           O  
ANISOU 9569  O   LYS G  95     4866   6257  12204   1786  -1727  -1687       O  
ATOM   9570  CB  LYS G  95      82.413 -83.447  38.622  1.00 61.92           C  
ANISOU 9570  CB  LYS G  95     4917   6352  12257   1821  -1778  -1765       C  
ATOM   9571  CG  LYS G  95      81.627 -84.057  37.454  1.00 62.25           C  
ANISOU 9571  CG  LYS G  95     4943   6409  12299   1837  -1815  -1781       C  
ATOM   9572  CD  LYS G  95      80.233 -84.508  37.844  1.00 62.08           C  
ANISOU 9572  CD  LYS G  95     4942   6374  12270   1826  -1845  -1771       C  
ATOM   9573  CE  LYS G  95      79.191 -83.842  36.964  1.00 62.34           C  
ANISOU 9573  CE  LYS G  95     4956   6415  12314   1829  -1883  -1739       C  
ATOM   9574  NZ  LYS G  95      78.841 -82.435  37.393  1.00 62.20           N  
ANISOU 9574  NZ  LYS G  95     4939   6388  12307   1814  -1881  -1683       N  
ATOM   9575  N   LEU G  96      85.010 -81.903  39.345  1.00 61.54           N  
ANISOU 9575  N   LEU G  96     4853   6302  12226   1815  -1704  -1750       N  
ATOM   9576  CA  LEU G  96      86.105 -81.713  40.325  1.00 60.75           C  
ANISOU 9576  CA  LEU G  96     4767   6191  12126   1805  -1670  -1755       C  
ATOM   9577  C   LEU G  96      86.874 -80.404  40.261  1.00 60.24           C  
ANISOU 9577  C   LEU G  96     4682   6128  12078   1803  -1649  -1726       C  
ATOM   9578  O   LEU G  96      87.237 -79.847  41.296  1.00 59.68           O  
ANISOU 9578  O   LEU G  96     4628   6041  12007   1787  -1632  -1708       O  
ATOM   9579  CB  LEU G  96      87.103 -82.872  40.213  1.00 60.67           C  
ANISOU 9579  CB  LEU G  96     4755   6187  12109   1816  -1651  -1807       C  
ATOM   9580  CG  LEU G  96      86.715 -84.226  40.819  1.00 60.89           C  
ANISOU 9580  CG  LEU G  96     4813   6206  12118   1813  -1659  -1839       C  
ATOM   9581  CD1 LEU G  96      87.765 -85.242  40.440  1.00 60.85           C  
ANISOU 9581  CD1 LEU G  96     4800   6212  12110   1827  -1641  -1890       C  
ATOM   9582  CD2 LEU G  96      86.594 -84.141  42.331  1.00 60.46           C  
ANISOU 9582  CD2 LEU G  96     4793   6127  12053   1791  -1651  -1824       C  
ATOM   9583  N   HIS G  97      87.150 -79.951  39.040  1.00 58.79           N  
ANISOU 9583  N   HIS G  97     4465   5964  11910   1819  -1650  -1724       N  
ATOM   9584  CA  HIS G  97      87.965 -78.753  38.775  1.00 58.95           C  
ANISOU 9584  CA  HIS G  97     4461   5988  11949   1820  -1629  -1701       C  
ATOM   9585  C   HIS G  97      89.405 -78.940  39.225  1.00 58.91           C  
ANISOU 9585  C   HIS G  97     4455   5980  11948   1820  -1592  -1727       C  
ATOM   9586  O   HIS G  97      89.996 -78.072  39.846  1.00 58.78           O  
ANISOU 9586  O   HIS G  97     4439   5954  11940   1809  -1572  -1705       O  
ATOM   9587  CB  HIS G  97      87.364 -77.489  39.434  1.00 58.72           C  
ANISOU 9587  CB  HIS G  97     4441   5945  11924   1802  -1634  -1647       C  
ATOM   9588  CG  HIS G  97      85.897 -77.302  39.165  1.00 58.71           C  
ANISOU 9588  CG  HIS G  97     4445   5944  11919   1799  -1671  -1619       C  
ATOM   9589  ND1 HIS G  97      85.371 -77.228  37.892  1.00 59.08           N  
ANISOU 9589  ND1 HIS G  97     4467   6008  11974   1815  -1696  -1616       N  
ATOM   9590  CD2 HIS G  97      84.849 -77.194  40.014  1.00 58.39           C  
ANISOU 9590  CD2 HIS G  97     4432   5886  11869   1783  -1687  -1594       C  
ATOM   9591  CE1 HIS G  97      84.064 -77.099  37.969  1.00 58.99           C  
ANISOU 9591  CE1 HIS G  97     4467   5990  11957   1808  -1727  -1589       C  
ATOM   9592  NE2 HIS G  97      83.724 -77.068  39.243  1.00 58.58           N  
ANISOU 9592  NE2 HIS G  97     4445   5917  11895   1788  -1720  -1576       N  
ATOM   9593  N   VAL G  98      89.963 -80.100  38.919  1.00 59.90           N  
ANISOU 9593  N   VAL G  98     4579   6114  12068   1832  -1583  -1775       N  
ATOM   9594  CA  VAL G  98      91.397 -80.328  39.052  1.00 59.44           C  
ANISOU 9594  CA  VAL G  98     4512   6056  12017   1836  -1548  -1804       C  
ATOM   9595  C   VAL G  98      92.109 -79.428  38.053  1.00 59.50           C  
ANISOU 9595  C   VAL G  98     4480   6077  12049   1848  -1530  -1795       C  
ATOM   9596  O   VAL G  98      91.652 -79.316  36.912  1.00 60.27           O  
ANISOU 9596  O   VAL G  98     4555   6190  12154   1864  -1546  -1793       O  
ATOM   9597  CB  VAL G  98      91.770 -81.792  38.766  1.00 59.70           C  
ANISOU 9597  CB  VAL G  98     4548   6096  12039   1848  -1544  -1857       C  
ATOM   9598  CG1 VAL G  98      93.234 -82.042  39.026  1.00 59.27           C  
ANISOU 9598  CG1 VAL G  98     4487   6040  11993   1849  -1508  -1886       C  
ATOM   9599  CG2 VAL G  98      90.904 -82.710  39.579  1.00 59.90           C  
ANISOU 9599  CG2 VAL G  98     4609   6109  12041   1838  -1565  -1866       C  
ATOM   9600  N   ASP G  99      93.201 -78.782  38.471  1.00 59.48           N  
ANISOU 9600  N   ASP G  99     4470   6068  12060   1842  -1500  -1789       N  
ATOM   9601  CA  ASP G  99      93.988 -77.960  37.568  1.00 59.85           C  
ANISOU 9601  CA  ASP G  99     4479   6127  12133   1853  -1477  -1783       C  
ATOM   9602  C   ASP G  99      94.803 -78.866  36.686  1.00 60.20           C  
ANISOU 9602  C   ASP G  99     4503   6185  12184   1873  -1459  -1833       C  
ATOM   9603  O   ASP G  99      95.564 -79.668  37.214  1.00 60.10           O  
ANISOU 9603  O   ASP G  99     4502   6167  12166   1870  -1441  -1865       O  
ATOM   9604  CB  ASP G  99      94.898 -77.041  38.350  1.00 59.71           C  
ANISOU 9604  CB  ASP G  99     4461   6097  12129   1839  -1450  -1764       C  
ATOM   9605  CG  ASP G  99      95.897 -76.342  37.466  1.00 60.10           C  
ANISOU 9605  CG  ASP G  99     4472   6157  12207   1850  -1421  -1765       C  
ATOM   9606  OD1 ASP G  99      95.440 -75.637  36.524  1.00 60.36           O  
ANISOU 9606  OD1 ASP G  99     4482   6201  12252   1860  -1430  -1743       O  
ATOM   9607  OD2 ASP G  99      97.127 -76.504  37.707  1.00 60.16           O  
ANISOU 9607  OD2 ASP G  99     4472   6161  12226   1850  -1389  -1789       O  
ATOM   9608  N   PRO G 100      94.687 -78.731  35.351  1.00 51.49           N  
ANISOU 9608  N   PRO G 100     6337   7107   6120   1853   -869   -859       N  
ATOM   9609  CA  PRO G 100      95.226 -79.675  34.364  1.00 53.37           C  
ANISOU 9609  CA  PRO G 100     6577   7358   6344   1868   -813   -897       C  
ATOM   9610  C   PRO G 100      96.725 -79.897  34.502  1.00 54.64           C  
ANISOU 9610  C   PRO G 100     6696   7563   6500   1901   -774   -877       C  
ATOM   9611  O   PRO G 100      97.300 -80.821  33.925  1.00 56.25           O  
ANISOU 9611  O   PRO G 100     6895   7775   6703   1925   -722   -905       O  
ATOM   9612  CB  PRO G 100      94.908 -79.013  33.025  1.00 53.64           C  
ANISOU 9612  CB  PRO G 100     6633   7421   6325   1813   -832   -918       C  
ATOM   9613  CG  PRO G 100      94.604 -77.646  33.341  1.00 52.19           C  
ANISOU 9613  CG  PRO G 100     6449   7257   6124   1773   -893   -882       C  
ATOM   9614  CD  PRO G 100      93.992 -77.633  34.690  1.00 50.64           C  
ANISOU 9614  CD  PRO G 100     6252   7015   5973   1794   -918   -858       C  
ATOM   9615  N   GLU G 101      97.366 -79.029  35.265  1.00 54.12           N  
ANISOU 9615  N   GLU G 101     6600   7529   6433   1900   -800   -828       N  
ATOM   9616  CA  GLU G 101      98.784 -79.171  35.477  1.00 55.08           C  
ANISOU 9616  CA  GLU G 101     6681   7694   6552   1930   -766   -805       C  
ATOM   9617  C   GLU G 101      99.095 -80.348  36.344  1.00 54.42           C  
ANISOU 9617  C   GLU G 101     6584   7575   6518   1991   -724   -808       C  
ATOM   9618  O   GLU G 101     100.195 -80.870  36.264  1.00 56.18           O  
ANISOU 9618  O   GLU G 101     6779   7825   6740   2022   -680   -806       O  
ATOM   9619  CB  GLU G 101      99.371 -77.911  36.103  1.00 53.44           C  
ANISOU 9619  CB  GLU G 101     6446   7529   6331   1914   -806   -751       C  
ATOM   9620  CG  GLU G 101     100.867 -77.850  36.012  1.00 55.33           C  
ANISOU 9620  CG  GLU G 101     6646   7825   6553   1932   -776   -729       C  
ATOM   9621  CD  GLU G 101     101.348 -77.644  34.593  1.00 58.90           C  
ANISOU 9621  CD  GLU G 101     7101   8325   6952   1901   -760   -751       C  
ATOM   9622  OE1 GLU G 101     100.812 -78.237  33.633  1.00 60.72           O  
ANISOU 9622  OE1 GLU G 101     7360   8539   7172   1890   -741   -797       O  
ATOM   9623  OE2 GLU G 101     102.279 -76.854  34.431  1.00 60.04           O  
ANISOU 9623  OE2 GLU G 101     7220   8527   7067   1886   -768   -722       O  
ATOM   9624  N   ASN G 102      98.147 -80.769  37.177  1.00 52.21           N  
ANISOU 9624  N   ASN G 102     6321   7236   6282   2009   -736   -812       N  
ATOM   9625  CA  ASN G 102      98.429 -81.893  38.062  1.00 52.51           C  
ANISOU 9625  CA  ASN G 102     6344   7238   6368   2068   -696   -814       C  
ATOM   9626  C   ASN G 102      98.315 -83.262  37.366  1.00 54.73           C  
ANISOU 9626  C   ASN G 102     6642   7492   6660   2094   -642   -866       C  
ATOM   9627  O   ASN G 102      98.788 -84.270  37.883  1.00 55.55           O  
ANISOU 9627  O   ASN G 102     6731   7577   6798   2144   -599   -870       O  
ATOM   9628  CB  ASN G 102      97.548 -81.816  39.296  1.00 49.98           C  
ANISOU 9628  CB  ASN G 102     6032   6866   6091   2079   -729   -795       C  
ATOM   9629  CG  ASN G 102      98.083 -80.833  40.306  1.00 48.15           C  
ANISOU 9629  CG  ASN G 102     5770   6662   5864   2079   -764   -739       C  
ATOM   9630  OD1 ASN G 102      99.237 -80.433  40.229  1.00 48.95           O  
ANISOU 9630  OD1 ASN G 102     5840   6816   5944   2082   -753   -714       O  
ATOM   9631  ND2 ASN G 102      97.261 -80.449  41.266  1.00 45.71           N  
ANISOU 9631  ND2 ASN G 102     5470   6316   5582   2076   -804   -719       N  
ATOM   9632  N   PHE G 103      97.749 -83.272  36.165  1.00 54.84           N  
ANISOU 9632  N   PHE G 103     6686   7507   6642   2059   -642   -903       N  
ATOM   9633  CA  PHE G 103      97.752 -84.471  35.346  1.00 57.21           C  
ANISOU 9633  CA  PHE G 103     7002   7791   6945   2078   -590   -952       C  
ATOM   9634  C   PHE G 103      99.162 -84.803  34.903  1.00 59.48           C  
ANISOU 9634  C   PHE G 103     7258   8128   7215   2100   -544   -950       C  
ATOM   9635  O   PHE G 103      99.605 -85.941  34.975  1.00 61.08           O  
ANISOU 9635  O   PHE G 103     7452   8315   7441   2144   -493   -969       O  
ATOM   9636  CB  PHE G 103      96.862 -84.308  34.114  1.00 57.83           C  
ANISOU 9636  CB  PHE G 103     7119   7864   6990   2032   -604   -991       C  
ATOM   9637  CG  PHE G 103      95.461 -83.892  34.428  1.00 55.64           C  
ANISOU 9637  CG  PHE G 103     6874   7543   6725   2005   -652   -994       C  
ATOM   9638  CD1 PHE G 103      94.921 -84.080  35.696  1.00 53.70           C  
ANISOU 9638  CD1 PHE G 103     6628   7250   6526   2031   -668   -976       C  
ATOM   9639  CD2 PHE G 103      94.668 -83.311  33.447  1.00 55.55           C  
ANISOU 9639  CD2 PHE G 103     6894   7536   6677   1953   -681  -1016       C  
ATOM   9640  CE1 PHE G 103      93.635 -83.683  35.978  1.00 51.70           C  
ANISOU 9640  CE1 PHE G 103     6403   6956   6283   2005   -713   -979       C  
ATOM   9641  CE2 PHE G 103      93.372 -82.914  33.727  1.00 53.56           C  
ANISOU 9641  CE2 PHE G 103     6671   7243   6436   1927   -726  -1019       C  
ATOM   9642  CZ  PHE G 103      92.864 -83.100  34.995  1.00 51.62           C  
ANISOU 9642  CZ  PHE G 103     6424   6952   6238   1954   -742  -1000       C  
ATOM   9643  N   ARG G 104      99.865 -83.797  34.421  1.00 53.95           N  
ANISOU 9643  N   ARG G 104     6541   7488   6471   2068   -561   -927       N  
ATOM   9644  CA  ARG G 104     101.196 -84.006  33.908  1.00 56.49           C  
ANISOU 9644  CA  ARG G 104     6832   7860   6770   2084   -521   -925       C  
ATOM   9645  C   ARG G 104     102.156 -84.235  35.060  1.00 55.03           C  
ANISOU 9645  C   ARG G 104     6608   7683   6617   2131   -502   -888       C  
ATOM   9646  O   ARG G 104     103.024 -85.113  34.999  1.00 56.96           O  
ANISOU 9646  O   ARG G 104     6833   7936   6872   2171   -451   -898       O  
ATOM   9647  CB  ARG G 104     101.614 -82.819  33.065  1.00 57.51           C  
ANISOU 9647  CB  ARG G 104     6956   8051   6843   2034   -548   -911       C  
ATOM   9648  CG  ARG G 104     100.617 -81.706  33.102  1.00 56.15           C  
ANISOU 9648  CG  ARG G 104     6806   7872   6656   1985   -611   -897       C  
ATOM   9649  CD  ARG G 104     100.802 -80.819  31.902  1.00 57.94           C  
ANISOU 9649  CD  ARG G 104     7040   8151   6825   1932   -629   -902       C  
ATOM   9650  NE  ARG G 104     100.931 -81.597  30.675  1.00 61.98           N  
ANISOU 9650  NE  ARG G 104     7565   8669   7315   1931   -586   -949       N  
ATOM   9651  CZ  ARG G 104     100.332 -81.280  29.529  1.00 63.83           C  
ANISOU 9651  CZ  ARG G 104     7828   8911   7512   1886   -600   -978       C  
ATOM   9652  NH1 ARG G 104      99.544 -80.199  29.452  1.00 61.90           N  
ANISOU 9652  NH1 ARG G 104     7602   8668   7248   1839   -656   -965       N  
ATOM   9653  NH2 ARG G 104     100.520 -82.049  28.458  1.00 67.79           N  
ANISOU 9653  NH2 ARG G 104     8341   9419   7996   1889   -557  -1020       N  
ATOM   9654  N   LEU G 105     101.963 -83.451  36.114  1.00 53.95           N  
ANISOU 9654  N   LEU G 105     6461   7541   6497   2127   -545   -846       N  
ATOM   9655  CA  LEU G 105     102.709 -83.649  37.331  1.00 53.32           C  
ANISOU 9655  CA  LEU G 105     6347   7461   6452   2171   -534   -810       C  
ATOM   9656  C   LEU G 105     102.615 -85.103  37.745  1.00 54.27           C  
ANISOU 9656  C   LEU G 105     6470   7531   6618   2225   -486   -837       C  
ATOM   9657  O   LEU G 105     103.613 -85.680  38.116  1.00 55.54           O  
ANISOU 9657  O   LEU G 105     6601   7706   6794   2267   -447   -827       O  
ATOM   9658  CB  LEU G 105     102.212 -82.735  38.455  1.00 50.40           C  
ANISOU 9658  CB  LEU G 105     5973   7076   6099   2160   -588   -768       C  
ATOM   9659  CG  LEU G 105     102.819 -81.323  38.532  1.00 49.41           C  
ANISOU 9659  CG  LEU G 105     5825   7009   5940   2126   -628   -723       C  
ATOM   9660  CD1 LEU G 105     102.546 -80.659  39.881  1.00 47.00           C  
ANISOU 9660  CD1 LEU G 105     5508   6687   5662   2131   -671   -679       C  
ATOM   9661  CD2 LEU G 105     104.301 -81.324  38.248  1.00 51.10           C  
ANISOU 9661  CD2 LEU G 105     6002   7281   6132   2142   -594   -708       C  
ATOM   9662  N   LEU G 106     101.431 -85.701  37.648  1.00 53.17           N  
ANISOU 9662  N   LEU G 106     6367   7336   6500   2224   -488   -871       N  
ATOM   9663  CA  LEU G 106     101.243 -87.117  38.005  1.00 54.05           C  
ANISOU 9663  CA  LEU G 106     6485   7397   6656   2273   -443   -899       C  
ATOM   9664  C   LEU G 106     101.780 -88.090  36.968  1.00 57.00           C  
ANISOU 9664  C   LEU G 106     6860   7782   7014   2289   -386   -940       C  
ATOM   9665  O   LEU G 106     102.348 -89.109  37.328  1.00 58.20           O  
ANISOU 9665  O   LEU G 106     6997   7921   7196   2338   -340   -948       O  
ATOM   9666  CB  LEU G 106      99.766 -87.427  38.231  1.00 52.70           C  
ANISOU 9666  CB  LEU G 106     6352   7161   6510   2265   -465   -923       C  
ATOM   9667  CG  LEU G 106      99.475 -88.919  38.402  1.00 53.95           C  
ANISOU 9667  CG  LEU G 106     6523   7267   6710   2311   -418   -959       C  
ATOM   9668  CD1 LEU G 106      99.939 -89.402  39.776  1.00 53.27           C  
ANISOU 9668  CD1 LEU G 106     6409   7159   6672   2364   -404   -930       C  
ATOM   9669  CD2 LEU G 106      98.023 -89.192  38.192  1.00 53.14           C  
ANISOU 9669  CD2 LEU G 106     6463   7109   6619   2293   -437   -993       C  
ATOM   9670  N   GLY G 107     101.582 -87.783  35.688  1.00 52.61           N  
ANISOU 9670  N   GLY G 107     6325   7251   6415   2248   -389   -968       N  
ATOM   9671  CA  GLY G 107     102.129 -88.594  34.613  1.00 56.57           C  
ANISOU 9671  CA  GLY G 107     6827   7770   6897   2258   -338  -1006       C  
ATOM   9672  C   GLY G 107     103.650 -88.692  34.697  1.00 57.92           C  
ANISOU 9672  C   GLY G 107     6955   7991   7060   2287   -302   -984       C  
ATOM   9673  O   GLY G 107     104.254 -89.735  34.423  1.00 60.44           O  
ANISOU 9673  O   GLY G 107     7266   8309   7390   2323   -248  -1007       O  
ATOM   9674  N   ASN G 108     104.275 -87.582  35.084  1.00 55.80           N  
ANISOU 9674  N   ASN G 108     6661   7768   6773   2270   -334   -938       N  
ATOM   9675  CA  ASN G 108     105.717 -87.560  35.319  1.00 56.82           C  
ANISOU 9675  CA  ASN G 108     6748   7945   6897   2296   -306   -910       C  
ATOM   9676  C   ASN G 108     106.135 -88.378  36.530  1.00 55.71           C  
ANISOU 9676  C   ASN G 108     6584   7775   6808   2356   -279   -894       C  
ATOM   9677  O   ASN G 108     107.126 -89.081  36.443  1.00 58.01           O  
ANISOU 9677  O   ASN G 108     6852   8085   7105   2391   -231   -899       O  
ATOM   9678  CB  ASN G 108     106.229 -86.125  35.488  1.00 55.64           C  
ANISOU 9678  CB  ASN G 108     6576   7848   6715   2262   -350   -864       C  
ATOM   9679  CG  ASN G 108     106.820 -85.556  34.210  1.00 58.68           C  
ANISOU 9679  CG  ASN G 108     6959   8294   7044   2225   -346   -873       C  
ATOM   9680  OD1 ASN G 108     106.791 -86.187  33.151  1.00 61.68           O  
ANISOU 9680  OD1 ASN G 108     7355   8676   7406   2221   -313   -915       O  
ATOM   9681  ND2 ASN G 108     107.344 -84.342  34.305  1.00 58.09           N  
ANISOU 9681  ND2 ASN G 108     6863   8268   6939   2196   -381   -833       N  
ATOM   9682  N   VAL G 109     105.429 -88.277  37.657  1.00 50.66           N  
ANISOU 9682  N   VAL G 109     5950   7093   6207   2366   -308   -874       N  
ATOM   9683  CA  VAL G 109     105.808 -89.039  38.831  1.00 50.63           C  
ANISOU 9683  CA  VAL G 109     5924   7060   6252   2422   -283   -858       C  
ATOM   9684  C   VAL G 109     105.631 -90.487  38.459  1.00 50.99           C  
ANISOU 9684  C   VAL G 109     5984   7067   6321   2457   -230   -905       C  
ATOM   9685  O   VAL G 109     106.382 -91.359  38.933  1.00 51.22           O  
ANISOU 9685  O   VAL G 109     5991   7092   6379   2507   -187   -903       O  
ATOM   9686  CB  VAL G 109     104.998 -88.671  40.059  1.00 50.08           C  
ANISOU 9686  CB  VAL G 109     5860   6950   6218   2425   -326   -830       C  
ATOM   9687  CG1 VAL G 109     105.153 -89.650  41.155  1.00 50.06           C  
ANISOU 9687  CG1 VAL G 109     5853   6900   6268   2447   -294   -814       C  
ATOM   9688  CG2 VAL G 109     105.458 -87.366  40.562  1.00 49.79           C  
ANISOU 9688  CG2 VAL G 109     5799   6955   6163   2402   -369   -780       C  
ATOM   9689  N   LEU G 110     104.696 -90.764  37.552  1.00 52.47           N  
ANISOU 9689  N   LEU G 110     6210   7230   6495   2431   -231   -948       N  
ATOM   9690  CA  LEU G 110     104.574 -92.132  37.060  1.00 53.97           C  
ANISOU 9690  CA  LEU G 110     6415   7388   6702   2462   -179   -995       C  
ATOM   9691  C   LEU G 110     105.866 -92.543  36.338  1.00 56.60           C  
ANISOU 9691  C   LEU G 110     6723   7769   7012   2479   -129  -1004       C  
ATOM   9692  O   LEU G 110     106.490 -93.547  36.721  1.00 57.93           O  
ANISOU 9692  O   LEU G 110     6874   7926   7211   2529    -83  -1010       O  
ATOM   9693  CB  LEU G 110     103.373 -92.287  36.144  1.00 53.92           C  
ANISOU 9693  CB  LEU G 110     6453   7351   6682   2428   -190  -1039       C  
ATOM   9694  CG  LEU G 110     103.239 -93.653  35.479  1.00 56.01           C  
ANISOU 9694  CG  LEU G 110     6736   7587   6959   2454   -136  -1091       C  
ATOM   9695  CD1 LEU G 110     102.818 -94.693  36.490  1.00 55.54           C  
ANISOU 9695  CD1 LEU G 110     6682   7464   6956   2490   -117  -1092       C  
ATOM   9696  CD2 LEU G 110     102.266 -93.594  34.304  1.00 56.34           C  
ANISOU 9696  CD2 LEU G 110     6819   7617   6972   2411   -148  -1133       C  
ATOM   9697  N   VAL G 111     106.283 -91.753  35.338  1.00 53.94           N  
ANISOU 9697  N   VAL G 111     6384   7487   6624   2439   -140  -1004       N  
ATOM   9698  CA  VAL G 111     107.539 -92.011  34.606  1.00 56.49           C  
ANISOU 9698  CA  VAL G 111     6682   7862   6921   2450    -96  -1010       C  
ATOM   9699  C   VAL G 111     108.735 -92.142  35.537  1.00 56.63           C  
ANISOU 9699  C   VAL G 111     6655   7901   6959   2494    -75   -972       C  
ATOM   9700  O   VAL G 111     109.588 -92.973  35.298  1.00 58.75           O  
ANISOU 9700  O   VAL G 111     6907   8184   7233   2528    -24   -986       O  
ATOM   9701  CB  VAL G 111     107.836 -90.923  33.545  1.00 56.99           C  
ANISOU 9701  CB  VAL G 111     6745   7985   6924   2397   -120  -1005       C  
ATOM   9702  CG1 VAL G 111     109.300 -90.673  33.405  1.00 58.47           C  
ANISOU 9702  CG1 VAL G 111     6893   8235   7089   2408    -96   -981       C  
ATOM   9703  CG2 VAL G 111     107.270 -91.329  32.197  1.00 58.61           C  
ANISOU 9703  CG2 VAL G 111     6985   8184   7102   2371   -104  -1057       C  
ATOM   9704  N   CYS G 112     108.777 -91.367  36.611  1.00 55.59           N  
ANISOU 9704  N   CYS G 112     6506   7773   6842   2493   -113   -926       N  
ATOM   9705  CA  CYS G 112     109.774 -91.573  37.651  1.00 55.48           C  
ANISOU 9705  CA  CYS G 112     6453   7770   6856   2538    -95   -890       C  
ATOM   9706  C   CYS G 112     109.736 -92.965  38.278  1.00 56.18           C  
ANISOU 9706  C   CYS G 112     6546   7804   6996   2574    -51   -901       C  
ATOM   9707  O   CYS G 112     110.774 -93.619  38.442  1.00 57.76           O  
ANISOU 9707  O   CYS G 112     6725   8014   7208   2589     -7   -889       O  
ATOM   9708  CB  CYS G 112     109.597 -90.544  38.747  1.00 52.96           C  
ANISOU 9708  CB  CYS G 112     6121   7453   6548   2527   -147   -840       C  
ATOM   9709  SG  CYS G 112     110.733 -89.178  38.593  1.00 52.98           S  
ANISOU 9709  SG  CYS G 112     6089   7536   6505   2497   -171   -794       S  
ATOM   9710  N   VAL G 113     108.528 -93.400  38.638  1.00 57.55           N  
ANISOU 9710  N   VAL G 113     6755   7911   7199   2554    -64   -912       N  
ATOM   9711  CA  VAL G 113     108.319 -94.708  39.266  1.00 57.70           C  
ANISOU 9711  CA  VAL G 113     6790   7864   7268   2547    -28   -910       C  
ATOM   9712  C   VAL G 113     108.618 -95.849  38.291  1.00 60.38           C  
ANISOU 9712  C   VAL G 113     7138   8201   7604   2567     28   -956       C  
ATOM   9713  O   VAL G 113     109.169 -96.876  38.693  1.00 61.60           O  
ANISOU 9713  O   VAL G 113     7285   8331   7790   2573     71   -947       O  
ATOM   9714  CB  VAL G 113     106.882 -94.834  39.810  1.00 57.22           C  
ANISOU 9714  CB  VAL G 113     6766   7737   7237   2519    -57   -913       C  
ATOM   9715  CG1 VAL G 113     106.671 -96.201  40.438  1.00 57.31           C  
ANISOU 9715  CG1 VAL G 113     6792   7684   7300   2511    -18   -910       C  
ATOM   9716  CG2 VAL G 113     106.606 -93.736  40.834  1.00 56.68           C  
ANISOU 9716  CG2 VAL G 113     6690   7669   7175   2496   -111   -865       C  
ATOM   9717  N   LEU G 114     108.251 -95.654  37.020  1.00 55.24           N  
ANISOU 9717  N   LEU G 114     6501   7574   6913   2575     27  -1006       N  
ATOM   9718  CA  LEU G 114     108.662 -96.542  35.940  1.00 59.39           C  
ANISOU 9718  CA  LEU G 114     7030   8111   7423   2593     78  -1051       C  
ATOM   9719  C   LEU G 114     110.178 -96.715  35.902  1.00 61.29           C  
ANISOU 9719  C   LEU G 114     7232   8400   7656   2616    116  -1032       C  
ATOM   9720  O   LEU G 114     110.709 -97.834  35.888  1.00 63.96           O  
ANISOU 9720  O   LEU G 114     7567   8719   8017   2625    165  -1038       O  
ATOM   9721  CB  LEU G 114     108.193 -96.012  34.592  1.00 61.03           C  
ANISOU 9721  CB  LEU G 114     7256   8352   7582   2588     64  -1098       C  
ATOM   9722  CG  LEU G 114     106.782 -96.363  34.115  1.00 60.96           C  
ANISOU 9722  CG  LEU G 114     7293   8291   7577   2566     52  -1139       C  
ATOM   9723  CD1 LEU G 114     106.711 -96.391  32.601  1.00 64.53           C  
ANISOU 9723  CD1 LEU G 114     7766   8768   7985   2532     66  -1179       C  
ATOM   9724  CD2 LEU G 114     106.317 -97.687  34.671  1.00 61.38           C  
ANISOU 9724  CD2 LEU G 114     7366   8273   7683   2567     83  -1144       C  
ATOM   9725  N   ALA G 115     110.877 -95.590  35.876  1.00 59.94           N  
ANISOU 9725  N   ALA G 115     7030   8294   7452   2624     92  -1008       N  
ATOM   9726  CA  ALA G 115     112.315 -95.614  35.824  1.00 61.49           C  
ANISOU 9726  CA  ALA G 115     7188   8541   7636   2644    124   -989       C  
ATOM   9727  C   ALA G 115     112.860 -96.256  37.105  1.00 61.10           C  
ANISOU 9727  C   ALA G 115     7125   8455   7637   2641    142   -943       C  
ATOM   9728  O   ALA G 115     113.891 -96.919  37.069  1.00 63.00           O  
ANISOU 9728  O   ALA G 115     7345   8709   7885   2656    186   -938       O  
ATOM   9729  CB  ALA G 115     112.857 -94.221  35.621  1.00 60.68           C  
ANISOU 9729  CB  ALA G 115     7060   8505   7489   2626     88   -961       C  
ATOM   9730  N   HIS G 116     112.161 -96.100  38.223  1.00 60.70           N  
ANISOU 9730  N   HIS G 116     7086   8355   7621   2619    110   -911       N  
ATOM   9731  CA  HIS G 116     112.607 -96.713  39.468  1.00 60.38           C  
ANISOU 9731  CA  HIS G 116     7034   8277   7629   2612    127   -869       C  
ATOM   9732  C   HIS G 116     112.581 -98.229  39.435  1.00 61.93           C  
ANISOU 9732  C   HIS G 116     7245   8423   7862   2617    178   -891       C  
ATOM   9733  O   HIS G 116     113.515 -98.870  39.886  1.00 62.76           O  
ANISOU 9733  O   HIS G 116     7329   8526   7990   2626    213   -872       O  
ATOM   9734  CB  HIS G 116     111.756 -96.253  40.624  1.00 57.63           C  
ANISOU 9734  CB  HIS G 116     6699   7886   7310   2585     83   -835       C  
ATOM   9735  CG  HIS G 116     112.239 -96.721  41.956  1.00 57.11           C  
ANISOU 9735  CG  HIS G 116     6620   7788   7291   2575     96   -790       C  
ATOM   9736  ND1 HIS G 116     111.459 -96.662  43.088  1.00 55.16           N  
ANISOU 9736  ND1 HIS G 116     6387   7489   7081   2547     69   -761       N  
ATOM   9737  CD2 HIS G 116     113.427 -97.225  42.349  1.00 58.27           C  
ANISOU 9737  CD2 HIS G 116     6739   7947   7454   2588    132   -768       C  
ATOM   9738  CE1 HIS G 116     112.142 -97.113  44.122  1.00 55.14           C  
ANISOU 9738  CE1 HIS G 116     6366   7469   7115   2543     88   -725       C  
ATOM   9739  NE2 HIS G 116     113.338 -97.469  43.699  1.00 57.01           N  
ANISOU 9739  NE2 HIS G 116     6579   7743   7341   2568    126   -728       N  
ATOM   9740  N   HIS G 117     111.515 -98.821  38.923  1.00 65.33           N  
ANISOU 9740  N   HIS G 117     7711   8811   8299   2609    182   -931       N  
ATOM   9741  CA  HIS G 117     111.444-100.276  38.903  1.00 68.02           C  
ANISOU 9741  CA  HIS G 117     8066   9102   8676   2611    230   -951       C  
ATOM   9742  C   HIS G 117     112.355-100.849  37.824  1.00 72.17           C  
ANISOU 9742  C   HIS G 117     8579   9665   9178   2636    278   -983       C  
ATOM   9743  O   HIS G 117     113.060-101.815  38.076  1.00 74.60           O  
ANISOU 9743  O   HIS G 117     8875   9956   9513   2645    321   -976       O  
ATOM   9744  CB  HIS G 117     109.999-100.761  38.709  1.00 67.70           C  
ANISOU 9744  CB  HIS G 117     8067   9003   8652   2592    220   -982       C  
ATOM   9745  CG  HIS G 117     109.139-100.602  39.930  1.00 64.38           C  
ANISOU 9745  CG  HIS G 117     7660   8532   8270   2565    186   -949       C  
ATOM   9746  ND1 HIS G 117     108.077-101.439  40.212  1.00 63.04           N  
ANISOU 9746  ND1 HIS G 117     7521   8296   8135   2546    192   -962       N  
ATOM   9747  CD2 HIS G 117     109.182 -99.699  40.942  1.00 62.37           C  
ANISOU 9747  CD2 HIS G 117     7391   8284   8021   2552    147   -903       C  
ATOM   9748  CE1 HIS G 117     107.506-101.060  41.345  1.00 60.32           C  
ANISOU 9748  CE1 HIS G 117     7181   7920   7818   2523    158   -925       C  
ATOM   9749  NE2 HIS G 117     108.156-100.005  41.808  1.00 59.81           N  
ANISOU 9749  NE2 HIS G 117     7090   7899   7736   2526    130   -890       N  
ATOM   9750  N   PHE G 118     112.385-100.237  36.644  1.00 63.57           N  
ANISOU 9750  N   PHE G 118     7490   8625   8037   2646    271  -1016       N  
ATOM   9751  CA  PHE G 118     113.077-100.848  35.511  1.00 67.80           C  
ANISOU 9751  CA  PHE G 118     8021   9192   8549   2666    318  -1053       C  
ATOM   9752  C   PHE G 118     114.538-100.472  35.256  1.00 69.32           C  
ANISOU 9752  C   PHE G 118     8172   9452   8713   2687    338  -1037       C  
ATOM   9753  O   PHE G 118     115.093-100.897  34.249  1.00 72.91           O  
ANISOU 9753  O   PHE G 118     8623   9937   9144   2702    376  -1070       O  
ATOM   9754  CB  PHE G 118     112.304-100.568  34.242  1.00 69.11           C  
ANISOU 9754  CB  PHE G 118     8212   9372   8674   2663    309  -1106       C  
ATOM   9755  CG  PHE G 118     111.016-101.291  34.178  1.00 69.17           C  
ANISOU 9755  CG  PHE G 118     8262   9313   8708   2645    307  -1134       C  
ATOM   9756  CD1 PHE G 118     109.859-100.712  34.673  1.00 66.26           C  
ANISOU 9756  CD1 PHE G 118     7915   8913   8348   2624    259  -1126       C  
ATOM   9757  CD2 PHE G 118     110.955-102.559  33.650  1.00 72.27           C  
ANISOU 9757  CD2 PHE G 118     8670   9672   9117   2648    354  -1167       C  
ATOM   9758  CE1 PHE G 118     108.674-101.375  34.624  1.00 66.49           C  
ANISOU 9758  CE1 PHE G 118     7982   8881   8401   2606    258  -1151       C  
ATOM   9759  CE2 PHE G 118     109.771-103.229  33.597  1.00 72.58           C  
ANISOU 9759  CE2 PHE G 118     8746   9650   9180   2630    353  -1191       C  
ATOM   9760  CZ  PHE G 118     108.625-102.636  34.081  1.00 69.69           C  
ANISOU 9760  CZ  PHE G 118     8403   9255   8822   2609    305  -1183       C  
ATOM   9761  N   GLY G 119     115.149 -99.662  36.122  1.00 65.58           N  
ANISOU 9761  N   GLY G 119     7671   9006   8242   2687    314   -988       N  
ATOM   9762  CA  GLY G 119     116.575 -99.382  36.036  1.00 66.87           C  
ANISOU 9762  CA  GLY G 119     7794   9229   8385   2706    334   -967       C  
ATOM   9763  C   GLY G 119     117.067 -99.005  34.652  1.00 69.09           C  
ANISOU 9763  C   GLY G 119     8065   9578   8609   2722    349  -1003       C  
ATOM   9764  O   GLY G 119     116.371 -98.352  33.885  1.00 68.55           O  
ANISOU 9764  O   GLY G 119     8012   9530   8505   2717    324  -1032       O  
ATOM   9765  N   LYS G 120     118.261 -99.473  34.323  1.00 65.93           N  
ANISOU 9765  N   LYS G 120     7639   9210   8202   2739    393  -1003       N  
ATOM   9766  CA  LYS G 120     118.925 -99.179  33.050  1.00 69.04           C  
ANISOU 9766  CA  LYS G 120     8018   9672   8542   2754    414  -1033       C  
ATOM   9767  C   LYS G 120     118.076 -99.546  31.847  1.00 71.26           C  
ANISOU 9767  C   LYS G 120     8332   9943   8800   2750    425  -1094       C  
ATOM   9768  O   LYS G 120     118.318 -99.081  30.742  1.00 73.51           O  
ANISOU 9768  O   LYS G 120     8611  10284   9035   2756    431  -1124       O  
ATOM   9769  CB  LYS G 120     120.264 -99.929  32.969  1.00 72.53           C  
ANISOU 9769  CB  LYS G 120     8433  10133   8991   2772    465  -1025       C  
ATOM   9770  CG  LYS G 120     120.213-101.341  33.547  1.00 74.56           C  
ANISOU 9770  CG  LYS G 120     8705  10320   9305   2771    501  -1025       C  
ATOM   9771  CD  LYS G 120     121.555-102.064  33.451  1.00 78.13           C  
ANISOU 9771  CD  LYS G 120     9129  10792   9764   2789    551  -1018       C  
ATOM   9772  CE  LYS G 120     121.606-103.047  32.263  1.00 82.38           C  
ANISOU 9772  CE  LYS G 120     9682  11326  10291   2797    598  -1070       C  
ATOM   9773  NZ  LYS G 120     122.701-104.056  32.387  1.00 86.17           N  
ANISOU 9773  NZ  LYS G 120    10144  11802  10796   2811    648  -1063       N  
ATOM   9774  N   GLU G 121     117.090-100.400  32.082  1.00 73.32           N  
ANISOU 9774  N   GLU G 121     8628  10131   9099   2739    429  -1111       N  
ATOM   9775  CA  GLU G 121     116.244-100.962  31.039  1.00 75.81           C  
ANISOU 9775  CA  GLU G 121     8979  10425   9402   2733    443  -1167       C  
ATOM   9776  C   GLU G 121     115.199 -99.926  30.625  1.00 73.85           C  
ANISOU 9776  C   GLU G 121     8750  10189   9120   2719    394  -1187       C  
ATOM   9777  O   GLU G 121     114.591-100.043  29.552  1.00 76.18           O  
ANISOU 9777  O   GLU G 121     9072  10484   9389   2707    399  -1234       O  
ATOM   9778  CB  GLU G 121     115.616-102.277  31.549  1.00 76.23           C  
ANISOU 9778  CB  GLU G 121     9059  10394   9511   2724    465  -1173       C  
ATOM   9779  CG  GLU G 121     114.512-102.950  30.729  1.00 78.84           C  
ANISOU 9779  CG  GLU G 121     9431  10682   9841   2712    475  -1226       C  
ATOM   9780  CD  GLU G 121     113.969-104.183  31.456  1.00 78.89           C  
ANISOU 9780  CD  GLU G 121     9458  10608   9908   2702    494  -1220       C  
ATOM   9781  OE1 GLU G 121     114.596-104.580  32.471  1.00 77.55           O  
ANISOU 9781  OE1 GLU G 121     9268  10420   9777   2707    506  -1180       O  
ATOM   9782  OE2 GLU G 121     112.927-104.744  31.035  1.00 80.48           O  
ANISOU 9782  OE2 GLU G 121     9695  10764  10118   2689    496  -1255       O  
ATOM   9783  N   PHE G 122     115.025 -98.887  31.447  1.00 75.32           N  
ANISOU 9783  N   PHE G 122     8925  10386   9308   2713    346  -1148       N  
ATOM   9784  CA  PHE G 122     114.159 -97.779  31.052  1.00 73.35           C  
ANISOU 9784  CA  PHE G 122     8698  10144   9026   2660    292  -1145       C  
ATOM   9785  C   PHE G 122     115.074 -96.772  30.382  1.00 74.32           C  
ANISOU 9785  C   PHE G 122     8799  10341   9098   2627    281  -1124       C  
ATOM   9786  O   PHE G 122     115.638 -95.888  31.024  1.00 71.98           O  
ANISOU 9786  O   PHE G 122     8476  10078   8796   2622    254  -1078       O  
ATOM   9787  CB  PHE G 122     113.462 -97.183  32.291  1.00 68.56           C  
ANISOU 9787  CB  PHE G 122     8094   9505   8449   2658    243  -1109       C  
ATOM   9788  CG  PHE G 122     112.392 -96.158  31.985  1.00 66.11           C  
ANISOU 9788  CG  PHE G 122     7813   9190   8114   2601    185  -1107       C  
ATOM   9789  CD1 PHE G 122     111.080 -96.553  31.744  1.00 66.55           C  
ANISOU 9789  CD1 PHE G 122     7911   9193   8183   2587    174  -1142       C  
ATOM   9790  CD2 PHE G 122     112.688 -94.801  31.987  1.00 63.48           C  
ANISOU 9790  CD2 PHE G 122     7466   8905   7747   2562    142  -1069       C  
ATOM   9791  CE1 PHE G 122     110.092 -95.612  31.475  1.00 64.42           C  
ANISOU 9791  CE1 PHE G 122     7668   8918   7891   2536    121  -1140       C  
ATOM   9792  CE2 PHE G 122     111.718 -93.864  31.712  1.00 61.37           C  
ANISOU 9792  CE2 PHE G 122     7226   8634   7459   2510     89  -1067       C  
ATOM   9793  CZ  PHE G 122     110.416 -94.264  31.455  1.00 61.79           C  
ANISOU 9793  CZ  PHE G 122     7321   8634   7524   2497     79  -1102       C  
ATOM   9794  N   THR G 123     115.122 -96.858  29.060  1.00 70.50           N  
ANISOU 9794  N   THR G 123     8331   9882   8575   2601    299  -1160       N  
ATOM   9795  CA  THR G 123     116.180 -96.219  28.284  1.00 72.89           C  
ANISOU 9795  CA  THR G 123     8610  10255   8830   2580    306  -1148       C  
ATOM   9796  C   THR G 123     115.728 -94.862  27.804  1.00 71.31           C  
ANISOU 9796  C   THR G 123     8423  10084   8587   2518    251  -1133       C  
ATOM   9797  O   THR G 123     114.534 -94.629  27.688  1.00 69.50           O  
ANISOU 9797  O   THR G 123     8227   9820   8358   2489    218  -1147       O  
ATOM   9798  CB  THR G 123     116.616 -97.110  27.088  1.00 78.25           C  
ANISOU 9798  CB  THR G 123     9295  10948   9490   2589    360  -1195       C  
ATOM   9799  OG1 THR G 123     115.746 -96.915  25.972  1.00 79.66           O  
ANISOU 9799  OG1 THR G 123     9510  11121   9635   2543    345  -1231       O  
ATOM   9800  CG2 THR G 123     116.557 -98.548  27.482  1.00 79.68           C  
ANISOU 9800  CG2 THR G 123     9478  11079   9716   2643    407  -1221       C  
ATOM   9801  N   PRO G 124     116.676 -93.965  27.512  1.00 72.16           N  
ANISOU 9801  N   PRO G 124     6901  10358  10158   3341     29    796       N  
ATOM   9802  CA  PRO G 124     116.299 -92.644  27.003  1.00 73.39           C  
ANISOU 9802  CA  PRO G 124     7081  10499  10305   3370    -14    797       C  
ATOM   9803  C   PRO G 124     115.287 -92.675  25.834  1.00 74.27           C  
ANISOU 9803  C   PRO G 124     7212  10602  10407   3390    -14    747       C  
ATOM   9804  O   PRO G 124     114.373 -91.851  25.847  1.00 74.01           O  
ANISOU 9804  O   PRO G 124     7200  10549  10371   3412    -45    709       O  
ATOM   9805  CB  PRO G 124     117.650 -92.050  26.574  1.00 75.80           C  
ANISOU 9805  CB  PRO G 124     7379  10820  10603   3368    -25    882       C  
ATOM   9806  CG  PRO G 124     118.620 -92.666  27.516  1.00 75.01           C  
ANISOU 9806  CG  PRO G 124     7253  10734  10513   3339     -3    922       C  
ATOM   9807  CD  PRO G 124     118.123 -94.058  27.771  1.00 73.15           C  
ANISOU 9807  CD  PRO G 124     7006  10503  10284   3322     39    872       C  
ATOM   9808  N   PRO G 125     115.429 -93.605  24.862  1.00 74.95           N  
ANISOU 9808  N   PRO G 125     7290  10700  10487   3384     20    744       N  
ATOM   9809  CA  PRO G 125     114.366 -93.666  23.845  1.00 75.87           C  
ANISOU 9809  CA  PRO G 125     7425  10805  10596   3402     19    691       C  
ATOM   9810  C   PRO G 125     113.004 -94.120  24.390  1.00 73.76           C  
ANISOU 9810  C   PRO G 125     7166  10520  10339   3401     25    612       C  
ATOM   9811  O   PRO G 125     111.959 -93.646  23.908  1.00 74.36           O  
ANISOU 9811  O   PRO G 125     7263  10579  10410   3420      7    566       O  
ATOM   9812  CB  PRO G 125     114.901 -94.691  22.840  1.00 77.50           C  
ANISOU 9812  CB  PRO G 125     7620  11031  10795   3392     56    708       C  
ATOM   9813  CG  PRO G 125     116.361 -94.671  23.017  1.00 78.44           C  
ANISOU 9813  CG  PRO G 125     7720  11170  10912   3378     63    785       C  
ATOM   9814  CD  PRO G 125     116.594 -94.423  24.474  1.00 76.26           C  
ANISOU 9814  CD  PRO G 125     7436  10891  10650   3365     53    796       C  
ATOM   9815  N   VAL G 126     113.013 -95.022  25.371  1.00 73.63           N  
ANISOU 9815  N   VAL G 126     7133  10507  10337   3376     50    596       N  
ATOM   9816  CA  VAL G 126     111.770 -95.523  25.947  1.00 73.45           C  
ANISOU 9816  CA  VAL G 126     7115  10468  10325   3371     57    526       C  
ATOM   9817  C   VAL G 126     111.048 -94.446  26.779  1.00 73.52           C  
ANISOU 9817  C   VAL G 126     7139  10458  10336   3387     20    500       C  
ATOM   9818  O   VAL G 126     109.824 -94.286  26.663  1.00 73.49           O  
ANISOU 9818  O   VAL G 126     7153  10437  10332   3398     10    442       O  
ATOM   9819  CB  VAL G 126     112.022 -96.774  26.799  1.00 73.23           C  
ANISOU 9819  CB  VAL G 126     7064  10448  10312   3340     93    520       C  
ATOM   9820  CG1 VAL G 126     110.837 -97.058  27.715  1.00 73.07           C  
ANISOU 9820  CG1 VAL G 126     7047  10412  10305   3334     94    457       C  
ATOM   9821  CG2 VAL G 126     112.278 -97.953  25.888  1.00 73.14           C  
ANISOU 9821  CG2 VAL G 126     7042  10448  10299   3328    130    520       C  
ATOM   9822  N   GLN G 127     111.792 -93.712  27.608  1.00 69.55           N  
ANISOU 9822  N   GLN G 127     6632   9959   9834   3387     -2    543       N  
ATOM   9823  CA  GLN G 127     111.229 -92.549  28.283  1.00 70.17           C  
ANISOU 9823  CA  GLN G 127     6728  10021   9911   3405    -44    525       C  
ATOM   9824  C   GLN G 127     110.647 -91.585  27.255  1.00 70.77           C  
ANISOU 9824  C   GLN G 127     6832  10084   9975   3434    -74    511       C  
ATOM   9825  O   GLN G 127     109.472 -91.208  27.343  1.00 70.56           O  
ANISOU 9825  O   GLN G 127     6823  10039   9946   3448    -91    455       O  
ATOM   9826  CB  GLN G 127     112.276 -91.832  29.129  1.00 71.21           C  
ANISOU 9826  CB  GLN G 127     6852  10159  10045   3402    -66    584       C  
ATOM   9827  CG  GLN G 127     111.929 -90.369  29.437  1.00 72.30           C  
ANISOU 9827  CG  GLN G 127     7013  10280  10177   3428   -118    581       C  
ATOM   9828  CD  GLN G 127     112.846 -89.768  30.484  1.00 73.20           C  
ANISOU 9828  CD  GLN G 127     7118  10397  10296   3422   -140    631       C  
ATOM   9829  OE1 GLN G 127     113.817 -90.400  30.884  1.00 73.06           O  
ANISOU 9829  OE1 GLN G 127     7077  10398  10286   3399   -115    674       O  
ATOM   9830  NE2 GLN G 127     112.540 -88.554  30.937  1.00 74.13           N  
ANISOU 9830  NE2 GLN G 127     7255  10499  10411   3442   -186    626       N  
ATOM   9831  N   ALA G 128     111.462 -91.205  26.275  1.00 73.34           N  
ANISOU 9831  N   ALA G 128     7157  10419  10289   3443    -80    562       N  
ATOM   9832  CA  ALA G 128     111.019 -90.299  25.220  1.00 75.43           C  
ANISOU 9832  CA  ALA G 128     7447  10673  10541   3470   -109    555       C  
ATOM   9833  C   ALA G 128     109.712 -90.773  24.564  1.00 75.16           C  
ANISOU 9833  C   ALA G 128     7426  10628  10505   3477    -95    485       C  
ATOM   9834  O   ALA G 128     108.858 -89.964  24.180  1.00 75.88           O  
ANISOU 9834  O   ALA G 128     7541  10702  10588   3500   -124    452       O  
ATOM   9835  CB  ALA G 128     112.094 -90.140  24.183  1.00 78.24           C  
ANISOU 9835  CB  ALA G 128     7797  11045  10887   3473   -106    618       C  
ATOM   9836  N   ALA G 129     109.544 -92.082  24.451  1.00 79.66           N  
ANISOU 9836  N   ALA G 129     7981  11206  11082   3457    -54    461       N  
ATOM   9837  CA  ALA G 129     108.284 -92.607  23.961  1.00 79.59           C  
ANISOU 9837  CA  ALA G 129     7982  11184  11073   3460    -40    395       C  
ATOM   9838  C   ALA G 129     107.201 -92.443  25.023  1.00 77.31           C  
ANISOU 9838  C   ALA G 129     7703  10878  10794   3459    -52    341       C  
ATOM   9839  O   ALA G 129     106.084 -92.013  24.724  1.00 77.58           O  
ANISOU 9839  O   ALA G 129     7757  10896  10823   3475    -68    293       O  
ATOM   9840  CB  ALA G 129     108.431 -94.064  23.557  1.00 79.83           C  
ANISOU 9840  CB  ALA G 129     7994  11226  11110   3438      5    388       C  
ATOM   9841  N   TYR G 130     107.518 -92.772  26.269  1.00 79.21           N  
ANISOU 9841  N   TYR G 130     7928  11123  11047   3441    -44    348       N  
ATOM   9842  CA  TYR G 130     106.511 -92.661  27.326  1.00 77.16           C  
ANISOU 9842  CA  TYR G 130     7674  10848  10794   3440    -53    297       C  
ATOM   9843  C   TYR G 130     106.150 -91.218  27.607  1.00 77.23           C  
ANISOU 9843  C   TYR G 130     7706  10843  10794   3466   -101    292       C  
ATOM   9844  O   TYR G 130     105.023 -90.922  28.009  1.00 76.31           O  
ANISOU 9844  O   TYR G 130     7606  10712  10678   3474   -115    239       O  
ATOM   9845  CB  TYR G 130     106.989 -93.326  28.605  1.00 75.29           C  
ANISOU 9845  CB  TYR G 130     7413  10621  10571   3415    -34    309       C  
ATOM   9846  CG  TYR G 130     106.589 -94.768  28.687  1.00 74.55           C  
ANISOU 9846  CG  TYR G 130     7305  10531  10491   3390      8    278       C  
ATOM   9847  CD1 TYR G 130     105.588 -95.174  29.553  1.00 73.14           C  
ANISOU 9847  CD1 TYR G 130     7125  10342  10322   3380     16    227       C  
ATOM   9848  CD2 TYR G 130     107.202 -95.729  27.883  1.00 75.49           C  
ANISOU 9848  CD2 TYR G 130     7409  10663  10611   3376     41    300       C  
ATOM   9849  CE1 TYR G 130     105.208 -96.498  29.629  1.00 72.75           C  
ANISOU 9849  CE1 TYR G 130     7061  10294  10287   3356     54    200       C  
ATOM   9850  CE2 TYR G 130     106.824 -97.057  27.953  1.00 75.06           C  
ANISOU 9850  CE2 TYR G 130     7341  10609  10570   3353     77    271       C  
ATOM   9851  CZ  TYR G 130     105.826 -97.434  28.830  1.00 73.72           C  
ANISOU 9851  CZ  TYR G 130     7170  10428  10412   3342     83    221       C  
ATOM   9852  OH  TYR G 130     105.446 -98.751  28.911  1.00 73.56           O  
ANISOU 9852  OH  TYR G 130     7136  10408  10407   3318    118    194       O  
ATOM   9853  N   GLN G 131     107.108 -90.320  27.392  1.00 71.62           N  
ANISOU 9853  N   GLN G 131     6999  10137  10075   3478   -128    347       N  
ATOM   9854  CA  GLN G 131     106.832 -88.902  27.570  1.00 72.20           C  
ANISOU 9854  CA  GLN G 131     7097  10196  10141   3504   -177    345       C  
ATOM   9855  C   GLN G 131     105.694 -88.495  26.657  1.00 73.32           C  
ANISOU 9855  C   GLN G 131     7264  10321  10272   3524   -191    297       C  
ATOM   9856  O   GLN G 131     104.810 -87.764  27.083  1.00 72.75           O  
ANISOU 9856  O   GLN G 131     7213  10232  10197   3539   -219    257       O  
ATOM   9857  CB  GLN G 131     108.074 -88.038  27.310  1.00 74.07           C  
ANISOU 9857  CB  GLN G 131     7333  10439  10371   3513   -203    416       C  
ATOM   9858  CG  GLN G 131     109.127 -88.109  28.416  1.00 73.07           C  
ANISOU 9858  CG  GLN G 131     7186  10324  10254   3497   -202    464       C  
ATOM   9859  CD  GLN G 131     108.605 -87.704  29.793  1.00 71.29           C  
ANISOU 9859  CD  GLN G 131     6967  10087  10034   3498   -224    433       C  
ATOM   9860  OE1 GLN G 131     109.228 -88.022  30.811  1.00 70.24           O  
ANISOU 9860  OE1 GLN G 131     6814   9963   9910   3481   -215    456       O  
ATOM   9861  NE2 GLN G 131     107.467 -86.982  29.831  1.00 71.18           N  
ANISOU 9861  NE2 GLN G 131     6978  10053  10014   3519   -253    380       N  
ATOM   9862  N   LYS G 132     105.705 -88.993  25.421  1.00 75.59           N  
ANISOU 9862  N   LYS G 132     7550  10615  10554   3525   -169    299       N  
ATOM   9863  CA  LYS G 132     104.616 -88.728  24.491  1.00 77.02           C  
ANISOU 9863  CA  LYS G 132     7755  10783  10727   3542   -177    253       C  
ATOM   9864  C   LYS G 132     103.301 -89.225  25.089  1.00 75.46           C  
ANISOU 9864  C   LYS G 132     7562  10573  10535   3534   -165    184       C  
ATOM   9865  O   LYS G 132     102.239 -88.574  24.961  1.00 76.15           O  
ANISOU 9865  O   LYS G 132     7674  10644  10616   3551   -188    140       O  
ATOM   9866  CB  LYS G 132     104.877 -89.382  23.135  1.00 79.08           C  
ANISOU 9866  CB  LYS G 132     8010  11055  10982   3540   -151    267       C  
ATOM   9867  CG  LYS G 132     105.861 -88.608  22.283  1.00 82.34           C  
ANISOU 9867  CG  LYS G 132     8427  11476  11384   3556   -171    326       C  
ATOM   9868  CD  LYS G 132     106.198 -89.317  20.976  1.00 81.99           C  
ANISOU 9868  CD  LYS G 132     8375  11446  11332   3553   -142    341       C  
ATOM   9869  CE  LYS G 132     107.537 -88.820  20.423  1.00 83.85           C  
ANISOU 9869  CE  LYS G 132     8603  11696  11559   3559   -153    417       C  
ATOM   9870  NZ  LYS G 132     107.996 -89.570  19.219  1.00 81.96           N  
ANISOU 9870  NZ  LYS G 132     8354  11474  11312   3556   -123    437       N  
ATOM   9871  N   VAL G 133     103.390 -90.362  25.775  1.00 77.13           N  
ANISOU 9871  N   VAL G 133     7751  10793  10761   3508   -130    177       N  
ATOM   9872  CA  VAL G 133     102.205 -90.992  26.341  1.00 75.74           C  
ANISOU 9872  CA  VAL G 133     7576  10609  10594   3496   -114    117       C  
ATOM   9873  C   VAL G 133     101.614 -90.254  27.529  1.00 74.21           C  
ANISOU 9873  C   VAL G 133     7394  10403  10400   3504   -141     90       C  
ATOM   9874  O   VAL G 133     100.424 -89.988  27.521  1.00 74.43           O  
ANISOU 9874  O   VAL G 133     7440  10417  10424   3513   -152     40       O  
ATOM   9875  CB  VAL G 133     102.489 -92.417  26.777  1.00 74.69           C  
ANISOU 9875  CB  VAL G 133     7415  10487  10477   3465    -69    119       C  
ATOM   9876  CG1 VAL G 133     101.203 -93.072  27.232  1.00 72.88           C  
ANISOU 9876  CG1 VAL G 133     7187  10247  10257   3454    -53     58       C  
ATOM   9877  CG2 VAL G 133     103.137 -93.188  25.634  1.00 76.70           C  
ANISOU 9877  CG2 VAL G 133     7658  10754  10731   3458    -42    146       C  
ATOM   9878  N   VAL G 134     102.409 -89.927  28.547  1.00 71.63           N  
ANISOU 9878  N   VAL G 134     7057  10082  10078   3500   -154    124       N  
ATOM   9879  CA  VAL G 134     101.819 -89.292  29.724  1.00 70.22           C  
ANISOU 9879  CA  VAL G 134     6888   9893   9898   3506   -179     95       C  
ATOM   9880  C   VAL G 134     101.405 -87.866  29.409  1.00 71.39           C  
ANISOU 9880  C   VAL G 134     7068  10025  10032   3537   -228     85       C  
ATOM   9881  O   VAL G 134     100.621 -87.261  30.146  1.00 70.70           O  
ANISOU 9881  O   VAL G 134     6997   9926   9941   3547   -252     48       O  
ATOM   9882  CB  VAL G 134     102.748 -89.290  30.938  1.00 68.91           C  
ANISOU 9882  CB  VAL G 134     6705   9738   9741   3495   -182    132       C  
ATOM   9883  CG1 VAL G 134     103.166 -90.703  31.266  1.00 67.96           C  
ANISOU 9883  CG1 VAL G 134     6553   9633   9635   3463   -135    142       C  
ATOM   9884  CG2 VAL G 134     103.957 -88.418  30.699  1.00 70.34           C  
ANISOU 9884  CG2 VAL G 134     6887   9923   9916   3507   -210    193       C  
ATOM   9885  N   ALA G 135     101.901 -87.340  28.296  1.00 70.08           N  
ANISOU 9885  N   ALA G 135     6912   9859   9857   3552   -242    116       N  
ATOM   9886  CA  ALA G 135     101.403 -86.074  27.791  1.00 71.70           C  
ANISOU 9886  CA  ALA G 135     7148  10047  10048   3581   -286    102       C  
ATOM   9887  C   ALA G 135     100.015 -86.296  27.200  1.00 72.27           C  
ANISOU 9887  C   ALA G 135     7237  10109  10115   3586   -276     40       C  
ATOM   9888  O   ALA G 135      99.022 -85.776  27.720  1.00 71.94           O  
ANISOU 9888  O   ALA G 135     7214  10053  10068   3595   -297     -5       O  
ATOM   9889  CB  ALA G 135     102.328 -85.505  26.761  1.00 73.98           C  
ANISOU 9889  CB  ALA G 135     7440  10339  10329   3594   -302    155       C  
ATOM   9890  N   GLY G 136      99.954 -87.099  26.134  1.00 72.89           N  
ANISOU 9890  N   GLY G 136     7307  10194  10193   3578   -245     39       N  
ATOM   9891  CA  GLY G 136      98.717 -87.366  25.414  1.00 73.82           C  
ANISOU 9891  CA  GLY G 136     7440  10303  10307   3582   -234    -13       C  
ATOM   9892  C   GLY G 136      97.596 -87.671  26.370  1.00 72.00           C  
ANISOU 9892  C   GLY G 136     7212  10064  10080   3572   -228    -68       C  
ATOM   9893  O   GLY G 136      96.493 -87.150  26.207  1.00 72.69           O  
ANISOU 9893  O   GLY G 136     7322  10137  10158   3586   -245   -112       O  
ATOM   9894  N   VAL G 137      97.892 -88.466  27.395  1.00 69.97           N  
ANISOU 9894  N   VAL G 137     6931   9816   9837   3550   -204    -63       N  
ATOM   9895  CA  VAL G 137      96.926 -88.724  28.457  1.00 69.86           C  
ANISOU 9895  CA  VAL G 137     6918   9797   9828   3540   -198   -108       C  
ATOM   9896  C   VAL G 137      96.513 -87.443  29.199  1.00 70.02           C  
ANISOU 9896  C   VAL G 137     6962   9804   9837   3562   -244   -126       C  
ATOM   9897  O   VAL G 137      95.310 -87.127  29.306  1.00 70.03           O  
ANISOU 9897  O   VAL G 137     6983   9794   9831   3570   -255   -176       O  
ATOM   9898  CB  VAL G 137      97.461 -89.728  29.472  1.00 69.68           C  
ANISOU 9898  CB  VAL G 137     6866   9788   9822   3513   -168    -93       C  
ATOM   9899  CG1 VAL G 137      96.575 -89.748  30.703  1.00 69.61           C  
ANISOU 9899  CG1 VAL G 137     6859   9774   9816   3507   -170   -134       C  
ATOM   9900  CG2 VAL G 137      97.483 -91.075  28.850  1.00 69.51           C  
ANISOU 9900  CG2 VAL G 137     6824   9773   9812   3490   -123    -93       C  
ATOM   9901  N   ALA G 138      97.511 -86.720  29.713  1.00 69.18           N  
ANISOU 9901  N   ALA G 138     6854   9701   9730   3570   -270    -85       N  
ATOM   9902  CA  ALA G 138      97.262 -85.499  30.486  1.00 68.88           C  
ANISOU 9902  CA  ALA G 138     6839   9651   9683   3590   -317    -97       C  
ATOM   9903  C   ALA G 138      96.413 -84.486  29.695  1.00 70.55           C  
ANISOU 9903  C   ALA G 138     7084   9845   9878   3616   -350   -128       C  
ATOM   9904  O   ALA G 138      95.500 -83.875  30.247  1.00 70.20           O  
ANISOU 9904  O   ALA G 138     7059   9788   9825   3628   -374   -170       O  
ATOM   9905  CB  ALA G 138      98.606 -84.869  30.938  1.00 68.89           C  
ANISOU 9905  CB  ALA G 138     6832   9656   9686   3596   -342    -40       C  
ATOM   9906  N   ASN G 139      96.708 -84.338  28.404  1.00 69.72           N  
ANISOU 9906  N   ASN G 139     6985   9739   9768   3625   -351   -108       N  
ATOM   9907  CA  ASN G 139      95.910 -83.489  27.531  1.00 69.87           C  
ANISOU 9907  CA  ASN G 139     7034   9741   9772   3648   -378   -136       C  
ATOM   9908  C   ASN G 139      94.489 -83.983  27.316  1.00 69.75           C  
ANISOU 9908  C   ASN G 139     7028   9721   9753   3644   -359   -197       C  
ATOM   9909  O   ASN G 139      93.538 -83.260  27.555  1.00 69.87           O  
ANISOU 9909  O   ASN G 139     7068   9722   9757   3658   -385   -238       O  
ATOM   9910  CB  ASN G 139      96.585 -83.349  26.184  1.00 71.76           C  
ANISOU 9910  CB  ASN G 139     7274   9984  10008   3657   -379    -98       C  
ATOM   9911  CG  ASN G 139      97.844 -82.560  26.270  1.00 72.95           C  
ANISOU 9911  CG  ASN G 139     7423  10135  10158   3667   -409    -39       C  
ATOM   9912  OD1 ASN G 139      97.854 -81.442  26.800  1.00 72.28           O  
ANISOU 9912  OD1 ASN G 139     7358  10037  10068   3684   -454    -38       O  
ATOM   9913  ND2 ASN G 139      98.940 -83.140  25.772  1.00 75.00           N  
ANISOU 9913  ND2 ASN G 139     7661  10412  10425   3656   -385     13       N  
ATOM   9914  N   ALA G 140      94.355 -85.216  26.852  1.00 71.20           N  
ANISOU 9914  N   ALA G 140     7192   9915   9945   3623   -314   -201       N  
ATOM   9915  CA  ALA G 140      93.048 -85.795  26.635  1.00 71.08           C  
ANISOU 9915  CA  ALA G 140     7183   9895   9928   3616   -293   -255       C  
ATOM   9916  C   ALA G 140      92.227 -85.700  27.908  1.00 71.03           C  
ANISOU 9916  C   ALA G 140     7181   9885   9922   3612   -299   -294       C  
ATOM   9917  O   ALA G 140      91.035 -85.433  27.868  1.00 71.04           O  
ANISOU 9917  O   ALA G 140     7202   9877   9914   3619   -308   -341       O  
ATOM   9918  CB  ALA G 140      93.183 -87.240  26.187  1.00 70.87           C  
ANISOU 9918  CB  ALA G 140     7131   9882   9916   3591   -243   -249       C  
ATOM   9919  N   LEU G 141      92.876 -85.907  29.045  1.00 68.86           N  
ANISOU 9919  N   LEU G 141     6889   9619   9657   3600   -296   -273       N  
ATOM   9920  CA  LEU G 141      92.181 -85.842  30.315  1.00 67.32           C  
ANISOU 9920  CA  LEU G 141     6696   9422   9462   3596   -301   -307       C  
ATOM   9921  C   LEU G 141      91.738 -84.429  30.592  1.00 67.78           C  
ANISOU 9921  C   LEU G 141     6785   9465   9503   3624   -352   -328       C  
ATOM   9922  O   LEU G 141      90.816 -84.204  31.361  1.00 67.07           O  
ANISOU 9922  O   LEU G 141     6707   9371   9407   3627   -361   -369       O  
ATOM   9923  CB  LEU G 141      93.069 -86.332  31.443  1.00 65.53           C  
ANISOU 9923  CB  LEU G 141     6442   9208   9248   3579   -288   -277       C  
ATOM   9924  CG  LEU G 141      92.369 -86.354  32.793  1.00 65.32           C  
ANISOU 9924  CG  LEU G 141     6415   9181   9221   3574   -291   -310       C  
ATOM   9925  CD1 LEU G 141      91.130 -87.200  32.671  1.00 64.26           C  
ANISOU 9925  CD1 LEU G 141     6279   9047   9089   3560   -260   -356       C  
ATOM   9926  CD2 LEU G 141      93.282 -86.916  33.849  1.00 65.25           C  
ANISOU 9926  CD2 LEU G 141     6378   9187   9226   3556   -274   -278       C  
ATOM   9927  N   ALA G 142      92.419 -83.474  29.963  1.00 68.81           N  
ANISOU 9927  N   ALA G 142     6931   9588   9626   3644   -385   -298       N  
ATOM   9928  CA  ALA G 142      92.137 -82.040  30.123  1.00 69.70           C  
ANISOU 9928  CA  ALA G 142     7075   9684   9724   3672   -438   -312       C  
ATOM   9929  C   ALA G 142      91.246 -81.428  29.016  1.00 71.88           C  
ANISOU 9929  C   ALA G 142     7380   9946   9985   3690   -456   -343       C  
ATOM   9930  O   ALA G 142      91.057 -80.215  28.971  1.00 73.02           O  
ANISOU 9930  O   ALA G 142     7553  10075  10118   3714   -501   -352       O  
ATOM   9931  CB  ALA G 142      93.453 -81.280  30.208  1.00 70.05           C  
ANISOU 9931  CB  ALA G 142     7119   9726   9770   3683   -469   -258       C  
ATOM   9932  N   HIS G 143      90.733 -82.261  28.116  1.00 72.59           N  
ANISOU 9932  N   HIS G 143     7464  10041  10077   3680   -421   -357       N  
ATOM   9933  CA  HIS G 143      90.067 -81.791  26.904  1.00 74.98           C  
ANISOU 9933  CA  HIS G 143     7790  10333  10367   3696   -433   -378       C  
ATOM   9934  C   HIS G 143      88.714 -81.092  27.149  1.00 75.78           C  
ANISOU 9934  C   HIS G 143     7920  10420  10452   3710   -458   -435       C  
ATOM   9935  O   HIS G 143      88.337 -80.167  26.412  1.00 78.19           O  
ANISOU 9935  O   HIS G 143     8252  10711  10744   3732   -488   -447       O  
ATOM   9936  CB  HIS G 143      89.867 -82.961  25.938  1.00 75.65           C  
ANISOU 9936  CB  HIS G 143     7858  10427  10458   3679   -387   -380       C  
ATOM   9937  CG  HIS G 143      89.016 -82.622  24.757  1.00 78.40           C  
ANISOU 9937  CG  HIS G 143     8229  10766  10793   3693   -395   -408       C  
ATOM   9938  ND1 HIS G 143      89.305 -81.575  23.910  1.00 80.24           N  
ANISOU 9938  ND1 HIS G 143     8484  10989  11015   3717   -429   -392       N  
ATOM   9939  CD2 HIS G 143      87.867 -83.172  24.295  1.00 79.88           C  
ANISOU 9939  CD2 HIS G 143     8421  10952  10976   3686   -374   -450       C  
ATOM   9940  CE1 HIS G 143      88.376 -81.498  22.972  1.00 82.72           C  
ANISOU 9940  CE1 HIS G 143     8815  11297  11318   3725   -428   -424       C  
ATOM   9941  NE2 HIS G 143      87.492 -82.458  23.180  1.00 82.57           N  
ANISOU 9941  NE2 HIS G 143     8786  11283  11303   3706   -395   -460       N  
ATOM   9942  N   LYS G 144      87.999 -81.507  28.194  1.00 73.03           N  
ANISOU 9942  N   LYS G 144     7567  10076  10106   3698   -445   -469       N  
ATOM   9943  CA  LYS G 144      86.677 -80.947  28.486  1.00 73.48           C  
ANISOU 9943  CA  LYS G 144     7649  10123  10148   3710   -465   -524       C  
ATOM   9944  C   LYS G 144      86.812 -79.583  29.202  1.00 73.62           C  
ANISOU 9944  C   LYS G 144     7692  10127  10155   3733   -518   -527       C  
ATOM   9945  O   LYS G 144      85.798 -78.969  29.593  1.00 74.42           O  
ANISOU 9945  O   LYS G 144     7816  10219  10242   3745   -541   -571       O  
ATOM   9946  CB  LYS G 144      85.838 -81.928  29.331  1.00 72.01           C  
ANISOU 9946  CB  LYS G 144     7447   9946   9966   3688   -431   -557       C  
ATOM   9947  CG  LYS G 144      85.387 -83.196  28.610  1.00 71.07           C  
ANISOU 9947  CG  LYS G 144     7311   9837   9857   3667   -384   -565       C  
ATOM   9948  CD  LYS G 144      84.237 -82.979  27.636  1.00 73.35           C  
ANISOU 9948  CD  LYS G 144     7622  10116  10132   3676   -388   -604       C  
ATOM   9949  CE  LYS G 144      82.884 -82.938  28.354  1.00 73.03           C  
ANISOU 9949  CE  LYS G 144     7593  10074  10082   3675   -390   -656       C  
ATOM   9950  NZ  LYS G 144      81.841 -82.031  27.698  1.00 71.26           N  
ANISOU 9950  NZ  LYS G 144     7402   9836   9836   3697   -419   -695       N  
ATOM   9951  N   TYR G 145      88.061 -79.141  29.389  1.00 65.70           N  
ANISOU 9951  N   TYR G 145     6683   9122   9158   3739   -538   -480       N  
ATOM   9952  CA  TYR G 145      88.368 -77.823  29.955  1.00 65.93           C  
ANISOU 9952  CA  TYR G 145     6735   9137   9179   3761   -593   -475       C  
ATOM   9953  C   TYR G 145      88.207 -76.703  28.918  1.00 66.15           C  
ANISOU 9953  C   TYR G 145     6794   9145   9194   3786   -632   -477       C  
ATOM   9954  O   TYR G 145      88.162 -75.508  29.259  1.00 66.36           O  
ANISOU 9954  O   TYR G 145     6848   9155   9212   3807   -682   -485       O  
ATOM   9955  CB  TYR G 145      89.789 -77.808  30.535  1.00 65.96           C  
ANISOU 9955  CB  TYR G 145     6720   9146   9196   3756   -599   -420       C  
ATOM   9956  CG  TYR G 145      89.809 -77.962  32.029  1.00 65.91           C  
ANISOU 9956  CG  TYR G 145     6703   9146   9193   3747   -600   -430       C  
ATOM   9957  CD1 TYR G 145      88.904 -77.278  32.821  1.00 66.01           C  
ANISOU 9957  CD1 TYR G 145     6739   9148   9193   3760   -629   -476       C  
ATOM   9958  CD2 TYR G 145      90.704 -78.802  32.642  1.00 65.77           C  
ANISOU 9958  CD2 TYR G 145     6653   9145   9191   3727   -571   -395       C  
ATOM   9959  CE1 TYR G 145      88.900 -77.417  34.178  1.00 65.97           C  
ANISOU 9959  CE1 TYR G 145     6725   9151   9191   3753   -629   -486       C  
ATOM   9960  CE2 TYR G 145      90.699 -78.955  34.005  1.00 65.73           C  
ANISOU 9960  CE2 TYR G 145     6638   9146   9189   3720   -571   -405       C  
ATOM   9961  CZ  TYR G 145      89.796 -78.251  34.769  1.00 65.83           C  
ANISOU 9961  CZ  TYR G 145     6675   9150   9189   3733   -601   -450       C  
ATOM   9962  OH  TYR G 145      89.777 -78.381  36.136  1.00 65.80           O  
ANISOU 9962  OH  TYR G 145     6662   9154   9186   3727   -601   -460       O  
ATOM   9963  N   HIS G 146      88.142 -77.112  27.651  1.00 76.47           N  
ANISOU 9963  N   HIS G 146     8098  10455  10501   3784   -610   -469       N  
ATOM   9964  CA  HIS G 146      87.761 -76.231  26.546  1.00 79.30           C  
ANISOU 9964  CA  HIS G 146     8486  10799  10847   3805   -638   -479       C  
ATOM   9965  C   HIS G 146      86.719 -76.956  25.644  1.00 80.42           C  
ANISOU 9965  C   HIS G 146     8627  10946  10983   3798   -604   -514       C  
ATOM   9966  O   HIS G 146      85.940 -77.817  26.094  1.00 79.34           O  
ANISOU 9966  O   HIS G 146     8479  10819  10848   3781   -571   -547       O  
ATOM   9967  CB  HIS G 146      89.000 -75.775  25.732  1.00 80.60           C  
ANISOU 9967  CB  HIS G 146     8648  10960  11017   3814   -656   -420       C  
ATOM   9968  CG  HIS G 146      90.316 -76.339  26.214  1.00 78.99           C  
ANISOU 9968  CG  HIS G 146     8414  10771  10829   3799   -639   -367       C  
ATOM   9969  ND1 HIS G 146      90.966 -75.872  27.340  1.00 77.70           N  
ANISOU 9969  ND1 HIS G 146     8248  10603  10671   3801   -665   -348       N  
ATOM   9970  CD2 HIS G 146      91.122 -77.299  25.692  1.00 78.67           C  
ANISOU 9970  CD2 HIS G 146     8344  10747  10800   3783   -600   -327       C  
ATOM   9971  CE1 HIS G 146      92.099 -76.538  27.506  1.00 76.64           C  
ANISOU 9971  CE1 HIS G 146     8085  10485  10551   3785   -642   -299       C  
ATOM   9972  NE2 HIS G 146      92.220 -77.408  26.519  1.00 77.16           N  
ANISOU 9972  NE2 HIS G 146     8133  10563  10621   3774   -602   -285       N  
ATOM   9973  OXT HIS G 146      86.595 -76.711  24.438  1.00 82.70           O  
ANISOU 9973  OXT HIS G 146     8927  11229  11265   3808   -608   -511       O  
TER    9974      HIS G 146                                                      
ATOM   9975  N   CYS H  92      56.738 -45.561  27.808  1.00 86.27           N  
ANISOU 9975  N   CYS H  92     7506   8252  17022   1984   -682   -281       N  
ATOM   9976  CA  CYS H  92      55.362 -45.844  28.128  1.00 88.04           C  
ANISOU 9976  CA  CYS H  92     7746   8536  17169   2025   -650   -342       C  
ATOM   9977  C   CYS H  92      54.648 -46.553  26.993  1.00 90.49           C  
ANISOU 9977  C   CYS H  92     8003   8910  17468   2010   -543   -409       C  
ATOM   9978  O   CYS H  92      54.328 -45.932  25.967  1.00 92.02           O  
ANISOU 9978  O   CYS H  92     8196   9133  17633   2019   -539   -446       O  
ATOM   9979  CB  CYS H  92      54.613 -44.567  28.446  1.00 87.62           C  
ANISOU 9979  CB  CYS H  92     7768   8497  17027   2088   -735   -365       C  
ATOM   9980  SG  CYS H  92      54.488 -43.428  27.027  1.00 88.21           S  
ANISOU 9980  SG  CYS H  92     7851   8594  17072   2099   -754   -400       S  
ATOM   9981  N   PRO H  93      54.382 -47.864  27.185  1.00 85.33           N  
ANISOU 9981  N   PRO H  93     7306   8279  16836   1985   -457   -423       N  
ATOM   9982  CA  PRO H  93      53.300 -48.586  26.486  1.00 87.69           C  
ANISOU 9982  CA  PRO H  93     7573   8653  17094   1985   -361   -496       C  
ATOM   9983  C   PRO H  93      51.957 -48.000  26.940  1.00 86.37           C  
ANISOU 9983  C   PRO H  93     7461   8534  16823   2051   -393   -548       C  
ATOM   9984  O   PRO H  93      51.340 -48.567  27.850  1.00 85.98           O  
ANISOU 9984  O   PRO H  93     7423   8501  16743   2070   -379   -558       O  
ATOM   9985  CB  PRO H  93      53.458 -50.024  26.963  1.00 89.17           C  
ANISOU 9985  CB  PRO H  93     7716   8837  17326   1948   -285   -483       C  
ATOM   9986  CG  PRO H  93      54.944 -50.139  27.285  1.00 88.31           C  
ANISOU 9986  CG  PRO H  93     7590   8653  17312   1906   -317   -403       C  
ATOM   9987  CD  PRO H  93      55.380 -48.779  27.777  1.00 85.38           C  
ANISOU 9987  CD  PRO H  93     7278   8236  16925   1940   -436   -364       C  
ATOM   9988  N   LYS H  94      51.521 -46.911  26.287  1.00 84.46           N  
ANISOU 9988  N   LYS H  94     7248   8315  16527   2083   -433   -579       N  
ATOM   9989  CA  LYS H  94      50.626 -45.894  26.845  1.00 82.39           C  
ANISOU 9989  CA  LYS H  94     7056   8072  16175   2150   -506   -604       C  
ATOM   9990  C   LYS H  94      49.467 -46.425  27.670  1.00 82.74           C  
ANISOU 9990  C   LYS H  94     7120   8161  16156   2185   -481   -642       C  
ATOM   9991  O   LYS H  94      48.778 -47.339  27.244  1.00 85.26           O  
ANISOU 9991  O   LYS H  94     7401   8534  16461   2171   -390   -689       O  
ATOM   9992  CB  LYS H  94      50.026 -45.060  25.707  1.00 82.86           C  
ANISOU 9992  CB  LYS H  94     7124   8177  16183   2171   -506   -656       C  
ATOM   9993  CG  LYS H  94      50.920 -43.995  25.072  1.00 80.78           C  
ANISOU 9993  CG  LYS H  94     6872   7871  15948   2163   -570   -623       C  
ATOM   9994  CD  LYS H  94      50.024 -42.999  24.272  1.00 78.11           C  
ANISOU 9994  CD  LYS H  94     6564   7583  15531   2205   -588   -680       C  
ATOM   9995  CE  LYS H  94      50.812 -41.802  23.687  1.00 76.15           C  
ANISOU 9995  CE  LYS H  94     6338   7296  15301   2204   -661   -650       C  
ATOM   9996  NZ  LYS H  94      51.393 -40.884  24.724  1.00 74.39           N  
ANISOU 9996  NZ  LYS H  94     6180   7009  15074   2229   -775   -593       N  
ATOM   9997  N   PRO H  95      49.246 -45.833  28.857  1.00 74.56           N  
ANISOU 9997  N   PRO H  95     6147   7103  15080   2230   -562   -622       N  
ATOM   9998  CA  PRO H  95      48.166 -46.274  29.735  1.00 74.81           C  
ANISOU 9998  CA  PRO H  95     6203   7173  15050   2266   -547   -654       C  
ATOM   9999  C   PRO H  95      46.836 -46.012  29.072  1.00 75.97           C  
ANISOU 9999  C   PRO H  95     6360   7397  15110   2302   -513   -731       C  
ATOM  10000  O   PRO H  95      46.729 -45.101  28.251  1.00 75.83           O  
ANISOU10000  O   PRO H  95     6356   7391  15065   2317   -539   -751       O  
ATOM  10001  CB  PRO H  95      48.336 -45.396  30.976  1.00 72.25           C  
ANISOU10001  CB  PRO H  95     5951   6802  14697   2307   -657   -612       C  
ATOM  10002  CG  PRO H  95      48.832 -44.107  30.423  1.00 70.47           C  
ANISOU10002  CG  PRO H  95     5758   6550  14467   2317   -732   -595       C  
ATOM  10003  CD  PRO H  95      49.777 -44.527  29.289  1.00 71.92           C  
ANISOU10003  CD  PRO H  95     5874   6718  14734   2257   -677   -580       C  
ATOM  10004  N   PRO H  96      45.825 -46.804  29.412  1.00 69.17           N  
ANISOU10004  N   PRO H  96     5491   6586  14204   2316   -454   -774       N  
ATOM  10005  CA  PRO H  96      44.494 -46.519  28.874  1.00 68.99           C  
ANISOU10005  CA  PRO H  96     5483   6639  14091   2354   -426   -846       C  
ATOM  10006  C   PRO H  96      43.883 -45.259  29.498  1.00 69.00           C  
ANISOU10006  C   PRO H  96     5563   6640  14012   2421   -522   -854       C  
ATOM  10007  O   PRO H  96      44.219 -44.919  30.624  1.00 69.12           O  
ANISOU10007  O   PRO H  96     5623   6608  14030   2442   -595   -811       O  
ATOM  10008  CB  PRO H  96      43.699 -47.776  29.241  1.00 68.88           C  
ANISOU10008  CB  PRO H  96     5443   6672  14057   2347   -342   -879       C  
ATOM  10009  CG  PRO H  96      44.419 -48.351  30.417  1.00 69.02           C  
ANISOU10009  CG  PRO H  96     5461   6633  14130   2331   -364   -821       C  
ATOM  10010  CD  PRO H  96      45.845 -47.975  30.301  1.00 69.19           C  
ANISOU10010  CD  PRO H  96     5473   6582  14234   2298   -411   -757       C  
ATOM  10011  N   GLU H  97      43.016 -44.574  28.761  1.00 70.71           N  
ANISOU10011  N   GLU H  97     5799   6910  14159   2454   -521   -908       N  
ATOM  10012  CA  GLU H  97      42.297 -43.403  29.283  1.00 69.20           C  
ANISOU10012  CA  GLU H  97     5683   6727  13881   2520   -605   -923       C  
ATOM  10013  C   GLU H  97      41.114 -43.775  30.163  1.00 69.31           C  
ANISOU10013  C   GLU H  97     5727   6784  13823   2561   -591   -957       C  
ATOM  10014  O   GLU H  97      40.482 -44.816  29.965  1.00 71.92           O  
ANISOU10014  O   GLU H  97     6017   7165  14144   2545   -502   -995       O  
ATOM  10015  CB  GLU H  97      41.775 -42.531  28.146  1.00 69.06           C  
ANISOU10015  CB  GLU H  97     5674   6752  13812   2540   -607   -969       C  
ATOM  10016  CG  GLU H  97      42.320 -42.878  26.782  1.00 71.09           C  
ANISOU10016  CG  GLU H  97     5865   7020  14126   2488   -542   -978       C  
ATOM  10017  CD  GLU H  97      42.787 -41.638  26.040  1.00 73.36           C  
ANISOU10017  CD  GLU H  97     6175   7287  14413   2497   -604   -968       C  
ATOM  10018  OE1 GLU H  97      41.910 -40.825  25.624  1.00 72.09           O  
ANISOU10018  OE1 GLU H  97     6054   7175  14163   2535   -623  -1012       O  
ATOM  10019  OE2 GLU H  97      44.037 -41.461  25.906  1.00 76.78           O  
ANISOU10019  OE2 GLU H  97     6594   7657  14923   2462   -636   -914       O  
ATOM  10020  N   ILE H  98      40.793 -42.925  31.123  1.00 68.07           N  
ANISOU10020  N   ILE H  98     5643   6610  13611   2613   -678   -945       N  
ATOM  10021  CA  ILE H  98      39.545 -43.091  31.821  1.00 67.97           C  
ANISOU10021  CA  ILE H  98     5664   6645  13516   2658   -669   -986       C  
ATOM  10022  C   ILE H  98      38.698 -41.863  31.546  1.00 67.91           C  
ANISOU10022  C   ILE H  98     5715   6672  13416   2715   -721  -1024       C  
ATOM  10023  O   ILE H  98      39.223 -40.792  31.263  1.00 68.00           O  
ANISOU10023  O   ILE H  98     5760   6651  13425   2722   -791  -1001       O  
ATOM  10024  CB  ILE H  98      39.727 -43.298  33.333  1.00 68.08           C  
ANISOU10024  CB  ILE H  98     5716   6616  13534   2673   -717   -943       C  
ATOM  10025  CG1 ILE H  98      40.195 -42.013  34.015  1.00 68.23           C  
ANISOU10025  CG1 ILE H  98     5810   6579  13534   2707   -838   -900       C  
ATOM  10026  CG2 ILE H  98      40.685 -44.419  33.600  1.00 68.16           C  
ANISOU10026  CG2 ILE H  98     5670   6587  13639   2617   -673   -899       C  
ATOM  10027  CD1 ILE H  98      40.380 -42.153  35.518  1.00 68.34           C  
ANISOU10027  CD1 ILE H  98     5866   6551  13549   2721   -890   -857       C  
ATOM  10028  N   ALA H  99      37.380 -42.045  31.609  1.00 67.76           N  
ANISOU10028  N   ALA H  99     5709   6722  13316   2750   -685  -1081       N  
ATOM  10029  CA  ALA H  99      36.408 -40.993  31.360  1.00 67.69           C  
ANISOU10029  CA  ALA H  99     5754   6755  13211   2806   -723  -1124       C  
ATOM  10030  C   ALA H  99      36.632 -39.816  32.278  1.00 67.82           C  
ANISOU10030  C   ALA H  99     5863   6729  13178   2840   -837  -1083       C  
ATOM  10031  O   ALA H  99      36.651 -39.988  33.487  1.00 67.89           O  
ANISOU10031  O   ALA H  99     5903   6706  13188   2858   -874  -1057       O  
ATOM  10032  CB  ALA H  99      35.028 -41.533  31.546  1.00 67.53           C  
ANISOU10032  CB  ALA H  99     5736   6810  13114   2834   -667  -1181       C  
ATOM  10033  N   HIS H 100      36.794 -38.633  31.686  1.00 67.86           N  
ANISOU10033  N   HIS H 100     5913   6733  13138   2846   -891  -1079       N  
ATOM  10034  CA  HIS H 100      37.004 -37.373  32.409  1.00 67.99           C  
ANISOU10034  CA  HIS H 100     6024   6713  13097   2876  -1000  -1043       C  
ATOM  10035  C   HIS H 100      38.210 -37.397  33.333  1.00 68.18           C  
ANISOU10035  C   HIS H 100     6062   6652  13192   2853  -1060   -970       C  
ATOM  10036  O   HIS H 100      38.195 -36.809  34.408  1.00 68.28           O  
ANISOU10036  O   HIS H 100     6146   6634  13164   2883  -1137   -941       O  
ATOM  10037  CB  HIS H 100      35.748 -36.997  33.220  1.00 67.93           C  
ANISOU10037  CB  HIS H 100     6083   6745  12983   2938  -1028  -1075       C  
ATOM  10038  CG  HIS H 100      34.578 -36.618  32.372  1.00 67.78           C  
ANISOU10038  CG  HIS H 100     6071   6805  12876   2968   -993  -1140       C  
ATOM  10039  ND1 HIS H 100      34.328 -35.316  31.992  1.00 67.80           N  
ANISOU10039  ND1 HIS H 100     6139   6821  12800   2994  -1051  -1147       N  
ATOM  10040  CD2 HIS H 100      33.611 -37.371  31.801  1.00 67.60           C  
ANISOU10040  CD2 HIS H 100     5998   6852  12835   2974   -905  -1201       C  
ATOM  10041  CE1 HIS H 100      33.251 -35.279  31.232  1.00 67.64           C  
ANISOU10041  CE1 HIS H 100     6108   6877  12715   3016  -1001  -1208       C  
ATOM  10042  NE2 HIS H 100      32.797 -36.512  31.100  1.00 67.52           N  
ANISOU10042  NE2 HIS H 100     6024   6898  12734   3004   -913  -1242       N  
ATOM  10043  N   GLY H 101      39.280 -38.036  32.906  1.00 68.24           N  
ANISOU10043  N   GLY H 101     6003   6621  13304   2800  -1027   -938       N  
ATOM  10044  CA  GLY H 101      40.423 -38.114  33.785  1.00 68.42           C  
ANISOU10044  CA  GLY H 101     6035   6565  13396   2777  -1081   -868       C  
ATOM  10045  C   GLY H 101      41.777 -38.126  33.098  1.00 68.52           C  
ANISOU10045  C   GLY H 101     6005   6528  13502   2722  -1082   -823       C  
ATOM  10046  O   GLY H 101      41.885 -38.470  31.919  1.00 68.43           O  
ANISOU10046  O   GLY H 101     5933   6543  13526   2692  -1017   -848       O  
ATOM  10047  N   TYR H 102      42.814 -37.756  33.845  1.00 68.71           N  
ANISOU10047  N   TYR H 102     6060   6480  13566   2707  -1156   -756       N  
ATOM  10048  CA  TYR H 102      44.123 -37.616  33.265  1.00 68.83           C  
ANISOU10048  CA  TYR H 102     6045   6444  13662   2658  -1169   -709       C  
ATOM  10049  C   TYR H 102      45.135 -38.313  34.095  1.00 68.97           C  
ANISOU10049  C   TYR H 102     6035   6398  13773   2627  -1180   -649       C  
ATOM  10050  O   TYR H 102      44.894 -38.692  35.237  1.00 69.01           O  
ANISOU10050  O   TYR H 102     6059   6389  13772   2648  -1196   -636       O  
ATOM  10051  CB  TYR H 102      44.518 -36.141  33.090  1.00 68.93           C  
ANISOU10051  CB  TYR H 102     6132   6433  13625   2668  -1262   -684       C  
ATOM  10052  CG  TYR H 102      44.722 -35.315  34.361  1.00 69.10           C  
ANISOU10052  CG  TYR H 102     6241   6408  13604   2696  -1367   -640       C  
ATOM  10053  CD1 TYR H 102      45.933 -35.319  35.040  1.00 69.29           C  
ANISOU10053  CD1 TYR H 102     6270   6358  13698   2666  -1419   -569       C  
ATOM  10054  CD2 TYR H 102      43.722 -34.491  34.841  1.00 69.06           C  
ANISOU10054  CD2 TYR H 102     6316   6434  13488   2750  -1414   -668       C  
ATOM  10055  CE1 TYR H 102      46.124 -34.560  36.186  1.00 69.44           C  
ANISOU10055  CE1 TYR H 102     6370   6336  13678   2690  -1515   -529       C  
ATOM  10056  CE2 TYR H 102      43.907 -33.724  35.981  1.00 69.21           C  
ANISOU10056  CE2 TYR H 102     6416   6412  13468   2774  -1509   -628       C  
ATOM  10057  CZ  TYR H 102      45.105 -33.764  36.653  1.00 69.40           C  
ANISOU10057  CZ  TYR H 102     6443   6363  13563   2744  -1559   -559       C  
ATOM  10058  OH  TYR H 102      45.274 -32.996  37.789  1.00 69.56           O  
ANISOU10058  OH  TYR H 102     6545   6342  13541   2768  -1653   -521       O  
ATOM  10059  N   VAL H 103      46.295 -38.431  33.476  1.00 69.06           N  
ANISOU10059  N   VAL H 103     6001   6368  13870   2578  -1173   -610       N  
ATOM  10060  CA  VAL H 103      47.432 -39.191  33.947  1.00 69.19           C  
ANISOU10060  CA  VAL H 103     5973   6323  13994   2537  -1167   -551       C  
ATOM  10061  C   VAL H 103      48.614 -38.295  34.356  1.00 69.41           C  
ANISOU10061  C   VAL H 103     6047   6279  14046   2520  -1265   -480       C  
ATOM  10062  O   VAL H 103      48.948 -37.340  33.660  1.00 69.44           O  
ANISOU10062  O   VAL H 103     6079   6278  14027   2514  -1305   -474       O  
ATOM  10063  CB  VAL H 103      47.856 -40.152  32.836  1.00 69.12           C  
ANISOU10063  CB  VAL H 103     5865   6325  14073   2489  -1071   -564       C  
ATOM  10064  CG1 VAL H 103      49.353 -40.317  32.781  1.00 69.29           C  
ANISOU10064  CG1 VAL H 103     5857   6280  14191   2434  -1088   -494       C  
ATOM  10065  CG2 VAL H 103      47.127 -41.480  32.994  1.00 68.99           C  
ANISOU10065  CG2 VAL H 103     5799   6356  14058   2482   -974   -602       C  
ATOM  10066  N   GLU H 104      49.226 -38.588  35.498  1.00 70.12           N  
ANISOU10066  N   GLU H 104     6148   6317  14179   2513  -1304   -426       N  
ATOM  10067  CA  GLU H 104      50.466 -37.927  35.886  1.00 70.59           C  
ANISOU10067  CA  GLU H 104     6239   6305  14277   2490  -1387   -354       C  
ATOM  10068  C   GLU H 104      51.661 -38.897  35.847  1.00 70.72           C  
ANISOU10068  C   GLU H 104     6185   6279  14406   2428  -1346   -302       C  
ATOM  10069  O   GLU H 104      51.764 -39.809  36.671  1.00 70.75           O  
ANISOU10069  O   GLU H 104     6169   6273  14439   2414  -1319   -282       O  
ATOM  10070  CB  GLU H 104      50.339 -37.321  37.275  1.00 70.88           C  
ANISOU10070  CB  GLU H 104     6359   6314  14260   2524  -1477   -323       C  
ATOM  10071  CG  GLU H 104      51.633 -36.690  37.700  1.00 71.38           C  
ANISOU10071  CG  GLU H 104     6453   6303  14364   2496  -1561   -248       C  
ATOM  10072  CD  GLU H 104      51.672 -36.319  39.166  1.00 71.71           C  
ANISOU10072  CD  GLU H 104     6567   6313  14366   2517  -1641   -209       C  
ATOM  10073  OE1 GLU H 104      51.578 -37.242  40.014  1.00 71.68           O  
ANISOU10073  OE1 GLU H 104     6544   6309  14382   2511  -1610   -199       O  
ATOM  10074  OE2 GLU H 104      51.819 -35.103  39.461  1.00 72.01           O  
ANISOU10074  OE2 GLU H 104     6682   6326  14352   2539  -1733   -189       O  
ATOM  10075  N   HIS H 105      52.576 -38.691  34.908  1.00 70.32           N  
ANISOU10075  N   HIS H 105     6101   6204  14415   2389  -1342   -279       N  
ATOM  10076  CA  HIS H 105      53.668 -39.646  34.723  1.00 70.43           C  
ANISOU10076  CA  HIS H 105     6044   6184  14531   2327  -1293   -235       C  
ATOM  10077  C   HIS H 105      54.836 -39.597  35.725  1.00 70.90           C  
ANISOU10077  C   HIS H 105     6124   6174  14639   2298  -1357   -153       C  
ATOM  10078  O   HIS H 105      55.323 -38.519  36.070  1.00 71.23           O  
ANISOU10078  O   HIS H 105     6230   6178  14658   2307  -1451   -116       O  
ATOM  10079  CB  HIS H 105      54.241 -39.474  33.330  1.00 70.36           C  
ANISOU10079  CB  HIS H 105     5989   6174  14571   2293  -1262   -239       C  
ATOM  10080  CG  HIS H 105      53.557 -40.303  32.298  1.00 69.91           C  
ANISOU10080  CG  HIS H 105     5864   6177  14522   2285  -1153   -302       C  
ATOM  10081  ND1 HIS H 105      52.420 -39.883  31.651  1.00 69.60           N  
ANISOU10081  ND1 HIS H 105     5839   6196  14410   2325  -1134   -371       N  
ATOM  10082  CD2 HIS H 105      53.851 -41.525  31.799  1.00 69.74           C  
ANISOU10082  CD2 HIS H 105     5762   6166  14571   2239  -1057   -306       C  
ATOM  10083  CE1 HIS H 105      52.039 -40.814  30.796  1.00 69.45           C  
ANISOU10083  CE1 HIS H 105     5751   6223  14415   2303  -1031   -415       C  
ATOM  10084  NE2 HIS H 105      52.888 -41.820  30.868  1.00 69.53           N  
ANISOU10084  NE2 HIS H 105     5703   6204  14510   2251   -982   -377       N  
ATOM  10085  N   SER H 106      55.302 -40.763  36.163  1.00 70.30           N  
ANISOU10085  N   SER H 106     5997   6084  14629   2262  -1305   -126       N  
ATOM  10086  CA  SER H 106      56.511 -40.822  36.953  1.00 70.52           C  
ANISOU10086  CA  SER H 106     6033   6049  14714   2227  -1354    -47       C  
ATOM  10087  C   SER H 106      57.398 -41.844  36.312  1.00 70.55           C  
ANISOU10087  C   SER H 106     5950   6037  14819   2166  -1278    -23       C  
ATOM  10088  O   SER H 106      56.883 -42.727  35.623  1.00 70.39           O  
ANISOU10088  O   SER H 106     5870   6059  14815   2157  -1182    -70       O  
ATOM  10089  CB  SER H 106      56.231 -41.199  38.402  1.00 70.59           C  
ANISOU10089  CB  SER H 106     6075   6049  14698   2245  -1378    -28       C  
ATOM  10090  OG  SER H 106      56.039 -40.054  39.203  1.00 70.68           O  
ANISOU10090  OG  SER H 106     6176   6043  14638   2284  -1481    -13       O  
ATOM  10091  N   VAL H 107      58.717 -41.707  36.497  1.00 70.75           N  
ANISOU10091  N   VAL H 107     5971   6003  14908   2124  -1319     48       N  
ATOM  10092  CA  VAL H 107      59.657 -42.800  36.263  1.00 70.82           C  
ANISOU10092  CA  VAL H 107     5903   5988  15017   2065  -1253     84       C  
ATOM  10093  C   VAL H 107      60.476 -42.961  37.515  1.00 71.03           C  
ANISOU10093  C   VAL H 107     5951   5965  15074   2047  -1305    155       C  
ATOM  10094  O   VAL H 107      60.689 -41.976  38.236  1.00 71.17           O  
ANISOU10094  O   VAL H 107     6039   5952  15049   2066  -1403    187       O  
ATOM  10095  CB  VAL H 107      60.584 -42.553  35.072  1.00 70.86           C  
ANISOU10095  CB  VAL H 107     5869   5971  15082   2024  -1242    104       C  
ATOM  10096  CG1 VAL H 107      59.805 -42.525  33.803  1.00 70.64           C  
ANISOU10096  CG1 VAL H 107     5813   5997  15031   2037  -1181     34       C  
ATOM  10097  CG2 VAL H 107      61.305 -41.274  35.239  1.00 71.02           C  
ANISOU10097  CG2 VAL H 107     5950   5946  15087   2026  -1348    150       C  
ATOM  10098  N   ARG H 108      60.886 -44.203  37.788  1.00 71.07           N  
ANISOU10098  N   ARG H 108     5896   5962  15147   2010  -1239    177       N  
ATOM  10099  CA  ARG H 108      61.851 -44.514  38.839  1.00 71.29           C  
ANISOU10099  CA  ARG H 108     5927   5939  15222   1981  -1276    250       C  
ATOM  10100  C   ARG H 108      63.068 -45.091  38.149  1.00 71.39           C  
ANISOU10100  C   ARG H 108     5871   5919  15335   1918  -1232    293       C  
ATOM  10101  O   ARG H 108      62.957 -46.059  37.406  1.00 71.28           O  
ANISOU10101  O   ARG H 108     5788   5929  15366   1894  -1136    266       O  
ATOM  10102  CB  ARG H 108      61.277 -45.493  39.876  1.00 71.27           C  
ANISOU10102  CB  ARG H 108     5915   5953  15210   1993  -1238    242       C  
ATOM  10103  CG  ARG H 108      62.285 -46.058  40.904  1.00 71.49           C  
ANISOU10103  CG  ARG H 108     5932   5933  15297   1957  -1257    316       C  
ATOM  10104  CD  ARG H 108      61.664 -47.093  41.887  1.00 71.45           C  
ANISOU10104  CD  ARG H 108     5914   5949  15283   1970  -1212    303       C  
ATOM  10105  NE  ARG H 108      61.148 -46.485  43.126  1.00 71.50           N  
ANISOU10105  NE  ARG H 108     5998   5954  15216   2014  -1291    309       N  
ATOM  10106  CZ  ARG H 108      59.844 -46.316  43.446  1.00 71.34           C  
ANISOU10106  CZ  ARG H 108     6016   5978  15113   2068  -1291    251       C  
ATOM  10107  NH1 ARG H 108      58.855 -46.733  42.632  1.00 71.11           N  
ANISOU10107  NH1 ARG H 108     5956   6003  15061   2086  -1214    180       N  
ATOM  10108  NH2 ARG H 108      59.516 -45.730  44.611  1.00 71.42           N  
ANISOU10108  NH2 ARG H 108     6098   5979  15061   2103  -1369    264       N  
ATOM  10109  N   TYR H 109      64.224 -44.470  38.363  1.00 71.60           N  
ANISOU10109  N   TYR H 109     5919   5891  15394   1891  -1303    360       N  
ATOM  10110  CA  TYR H 109      65.466 -44.920  37.754  1.00 71.71           C  
ANISOU10110  CA  TYR H 109     5873   5870  15504   1831  -1272    408       C  
ATOM  10111  C   TYR H 109      66.023 -46.035  38.593  1.00 71.84           C  
ANISOU10111  C   TYR H 109     5851   5864  15580   1798  -1237    453       C  
ATOM  10112  O   TYR H 109      65.974 -45.986  39.818  1.00 71.94           O  
ANISOU10112  O   TYR H 109     5904   5863  15568   1814  -1286    480       O  
ATOM  10113  CB  TYR H 109      66.475 -43.773  37.626  1.00 71.89           C  
ANISOU10113  CB  TYR H 109     5935   5845  15534   1814  -1363    461       C  
ATOM  10114  CG  TYR H 109      66.288 -42.941  36.379  1.00 71.77           C  
ANISOU10114  CG  TYR H 109     5927   5846  15497   1824  -1369    425       C  
ATOM  10115  CD1 TYR H 109      65.652 -41.711  36.427  1.00 71.73           C  
ANISOU10115  CD1 TYR H 109     5996   5852  15405   1871  -1443    398       C  
ATOM  10116  CD2 TYR H 109      66.734 -43.391  35.149  1.00 71.71           C  
ANISOU10116  CD2 TYR H 109     5852   5841  15553   1787  -1300    417       C  
ATOM  10117  CE1 TYR H 109      65.474 -40.954  35.285  1.00 71.62           C  
ANISOU10117  CE1 TYR H 109     5988   5854  15371   1880  -1448    364       C  
ATOM  10118  CE2 TYR H 109      66.554 -42.635  34.002  1.00 71.60           C  
ANISOU10118  CE2 TYR H 109     5843   5844  15519   1796  -1305    383       C  
ATOM  10119  CZ  TYR H 109      65.928 -41.421  34.077  1.00 71.56           C  
ANISOU10119  CZ  TYR H 109     5911   5850  15429   1843  -1379    357       C  
ATOM  10120  OH  TYR H 109      65.760 -40.670  32.941  1.00 71.46           O  
ANISOU10120  OH  TYR H 109     5902   5853  15396   1852  -1384    324       O  
ATOM  10121  N   GLN H 110      66.517 -47.064  37.923  1.00 71.82           N  
ANISOU10121  N   GLN H 110     5770   5860  15658   1753  -1150    459       N  
ATOM  10122  CA  GLN H 110      67.213 -48.146  38.605  1.00 71.96           C  
ANISOU10122  CA  GLN H 110     5744   5852  15744   1715  -1113    508       C  
ATOM  10123  C   GLN H 110      68.419 -48.562  37.781  1.00 72.06           C  
ANISOU10123  C   GLN H 110     5694   5833  15851   1655  -1074    550       C  
ATOM  10124  O   GLN H 110      68.378 -48.516  36.549  1.00 71.94           O  
ANISOU10124  O   GLN H 110     5647   5834  15853   1643  -1029    518       O  
ATOM  10125  CB  GLN H 110      66.283 -49.342  38.840  1.00 71.81           C  
ANISOU10125  CB  GLN H 110     5689   5876  15718   1727  -1023    461       C  
ATOM  10126  CG  GLN H 110      65.073 -49.027  39.689  1.00 71.71           C  
ANISOU10126  CG  GLN H 110     5734   5897  15614   1786  -1056    419       C  
ATOM  10127  CD  GLN H 110      64.297 -50.257  40.005  1.00 71.58           C  
ANISOU10127  CD  GLN H 110     5682   5919  15598   1791   -970    382       C  
ATOM  10128  OE1 GLN H 110      64.835 -51.361  39.918  1.00 71.63           O  
ANISOU10128  OE1 GLN H 110     5625   5915  15676   1749   -900    404       O  
ATOM  10129  NE2 GLN H 110      63.014 -50.097  40.355  1.00 71.42           N  
ANISOU10129  NE2 GLN H 110     5699   5943  15496   1844   -972    325       N  
ATOM  10130  N   CYS H 111      69.488 -48.951  38.469  1.00 72.27           N  
ANISOU10130  N   CYS H 111     5706   5815  15940   1617  -1091    621       N  
ATOM  10131  CA  CYS H 111      70.738 -49.314  37.818  1.00 72.40           C  
ANISOU10131  CA  CYS H 111     5667   5795  16047   1558  -1062    671       C  
ATOM  10132  C   CYS H 111      70.779 -50.824  37.585  1.00 72.35           C  
ANISOU10132  C   CYS H 111     5583   5801  16107   1524   -948    663       C  
ATOM  10133  O   CYS H 111      70.372 -51.610  38.446  1.00 72.35           O  
ANISOU10133  O   CYS H 111     5576   5813  16101   1533   -920    660       O  
ATOM  10134  CB  CYS H 111      71.937 -48.855  38.660  1.00 72.68           C  
ANISOU10134  CB  CYS H 111     5729   5773  16112   1532  -1147    756       C  
ATOM  10135  SG  CYS H 111      72.204 -47.027  38.745  1.00 72.77           S  
ANISOU10135  SG  CYS H 111     5830   5761  16060   1556  -1281    777       S  
ATOM  10136  N   LYS H 112      71.281 -51.234  36.425  1.00 73.23           N  
ANISOU10136  N   LYS H 112     5635   5909  16279   1485   -883    660       N  
ATOM  10137  CA  LYS H 112      71.231 -52.637  36.054  1.00 73.16           C  
ANISOU10137  CA  LYS H 112     5555   5917  16326   1454   -769    644       C  
ATOM  10138  C   LYS H 112      72.166 -53.481  36.898  1.00 73.37           C  
ANISOU10138  C   LYS H 112     5552   5905  16422   1415   -758    713       C  
ATOM  10139  O   LYS H 112      72.831 -53.000  37.811  1.00 73.57           O  
ANISOU10139  O   LYS H 112     5610   5892  16450   1412   -838    772       O  
ATOM  10140  CB  LYS H 112      71.603 -52.835  34.596  1.00 73.09           C  
ANISOU10140  CB  LYS H 112     5494   5912  16365   1418   -705    627       C  
ATOM  10141  CG  LYS H 112      70.932 -51.941  33.619  1.00 72.91           C  
ANISOU10141  CG  LYS H 112     5495   5921  16287   1448   -719    570       C  
ATOM  10142  CD  LYS H 112      70.990 -52.581  32.251  1.00 72.80           C  
ANISOU10142  CD  LYS H 112     5417   5925  16317   1414   -622    537       C  
ATOM  10143  CE  LYS H 112      70.354 -51.717  31.182  1.00 72.62           C  
ANISOU10143  CE  LYS H 112     5414   5936  16243   1439   -630    479       C  
ATOM  10144  NZ  LYS H 112      70.457 -52.406  29.861  1.00 72.52           N  
ANISOU10144  NZ  LYS H 112     5337   5941  16275   1402   -532    449       N  
ATOM  10145  N   ASN H 113      72.217 -54.761  36.563  1.00 73.93           N  
ANISOU10145  N   ASN H 113     5558   5985  16546   1382   -655    704       N  
ATOM  10146  CA  ASN H 113      73.000 -55.721  37.303  1.00 75.34           C  
ANISOU10146  CA  ASN H 113     5701   6132  16791   1345   -629    762       C  
ATOM  10147  C   ASN H 113      74.460 -55.310  37.448  1.00 75.50           C  
ANISOU10147  C   ASN H 113     5719   6094  16875   1305   -687    846       C  
ATOM  10148  O   ASN H 113      75.074 -54.810  36.507  1.00 75.74           O  
ANISOU10148  O   ASN H 113     5736   6108  16934   1283   -696    857       O  
ATOM  10149  CB  ASN H 113      72.885 -57.084  36.630  1.00 77.33           C  
ANISOU10149  CB  ASN H 113     5884   6404  17094   1311   -504    735       C  
ATOM  10150  CG  ASN H 113      71.447 -57.498  36.424  1.00 77.71           C  
ANISOU10150  CG  ASN H 113     5936   6513  17079   1347   -444    651       C  
ATOM  10151  OD1 ASN H 113      70.522 -56.706  36.658  1.00 78.86           O  
ANISOU10151  OD1 ASN H 113     6133   6687  17142   1398   -494    609       O  
ATOM  10152  ND2 ASN H 113      71.240 -58.742  35.978  1.00 77.13           N  
ANISOU10152  ND2 ASN H 113     5808   6459  17038   1319   -335    625       N  
ATOM  10153  N   TYR H 114      74.982 -55.543  38.651  1.00 74.93           N  
ANISOU10153  N   TYR H 114     5656   5993  16821   1297   -725    904       N  
ATOM  10154  CA  TYR H 114      76.337 -55.197  39.083  1.00 75.20           C  
ANISOU10154  CA  TYR H 114     5692   5972  16908   1262   -787    989       C  
ATOM  10155  C   TYR H 114      76.634 -53.679  39.102  1.00 75.27           C  
ANISOU10155  C   TYR H 114     5765   5962  16873   1280   -901   1009       C  
ATOM  10156  O   TYR H 114      77.797 -53.290  39.213  1.00 75.48           O  
ANISOU10156  O   TYR H 114     5792   5946  16942   1247   -951   1075       O  
ATOM  10157  CB  TYR H 114      77.367 -55.917  38.193  1.00 75.28           C  
ANISOU10157  CB  TYR H 114     5632   5957  17014   1202   -718   1023       C  
ATOM  10158  CG  TYR H 114      76.987 -57.341  37.808  1.00 75.17           C  
ANISOU10158  CG  TYR H 114     5556   5966  17038   1183   -595    990       C  
ATOM  10159  CD1 TYR H 114      77.034 -58.378  38.739  1.00 75.25           C  
ANISOU10159  CD1 TYR H 114     5545   5972  17075   1172   -558   1014       C  
ATOM  10160  CD2 TYR H 114      76.584 -57.643  36.510  1.00 74.98           C  
ANISOU10160  CD2 TYR H 114     5498   5970  17022   1174   -517    935       C  
ATOM  10161  CE1 TYR H 114      76.669 -59.672  38.386  1.00 75.15           C  
ANISOU10161  CE1 TYR H 114     5480   5981  17093   1154   -446    982       C  
ATOM  10162  CE2 TYR H 114      76.232 -58.929  36.150  1.00 74.88           C  
ANISOU10162  CE2 TYR H 114     5434   5979  17039   1154   -406    903       C  
ATOM  10163  CZ  TYR H 114      76.276 -59.938  37.086  1.00 74.97           C  
ANISOU10163  CZ  TYR H 114     5427   5984  17074   1144   -370    927       C  
ATOM  10164  OH  TYR H 114      75.927 -61.210  36.702  1.00 74.88           O  
ANISOU10164  OH  TYR H 114     5367   5994  17089   1123   -259    896       O  
ATOM  10165  N   TYR H 115      75.583 -52.845  39.101  1.00 76.24           N  
ANISOU10165  N   TYR H 115     5943   6117  16907   1333   -943    953       N  
ATOM  10166  CA  TYR H 115      75.725 -51.381  39.191  1.00 76.30           C  
ANISOU10166  CA  TYR H 115     6020   6110  16862   1355  -1052    966       C  
ATOM  10167  C   TYR H 115      74.917 -50.799  40.341  1.00 76.31           C  
ANISOU10167  C   TYR H 115     6092   6125  16776   1406  -1124    951       C  
ATOM  10168  O   TYR H 115      74.244 -51.523  41.064  1.00 76.15           O  
ANISOU10168  O   TYR H 115     6068   6127  16738   1425  -1090    931       O  
ATOM  10169  CB  TYR H 115      75.311 -50.696  37.885  1.00 75.98           C  
ANISOU10169  CB  TYR H 115     5983   6091  16794   1369  -1044    913       C  
ATOM  10170  CG  TYR H 115      76.350 -50.825  36.808  1.00 76.11           C  
ANISOU10170  CG  TYR H 115     5948   6082  16889   1318  -1010    943       C  
ATOM  10171  CD1 TYR H 115      77.365 -49.893  36.677  1.00 77.06           C  
ANISOU10171  CD1 TYR H 115     6092   6161  17025   1297  -1087    997       C  
ATOM  10172  CD2 TYR H 115      76.338 -51.903  35.940  1.00 76.62           C  
ANISOU10172  CD2 TYR H 115     5941   6161  17011   1289   -900    919       C  
ATOM  10173  CE1 TYR H 115      78.336 -50.031  35.699  1.00 78.54           C  
ANISOU10173  CE1 TYR H 115     6231   6325  17285   1250  -1056   1025       C  
ATOM  10174  CE2 TYR H 115      77.307 -52.052  34.959  1.00 78.12           C  
ANISOU10174  CE2 TYR H 115     6082   6326  17273   1241   -868    947       C  
ATOM  10175  CZ  TYR H 115      78.301 -51.117  34.841  1.00 79.03           C  
ANISOU10175  CZ  TYR H 115     6221   6402  17405   1222   -945   1001       C  
ATOM  10176  OH  TYR H 115      79.251 -51.274  33.856  1.00 80.79           O  
ANISOU10176  OH  TYR H 115     6395   6600  17700   1175   -912   1028       O  
ATOM  10177  N   LYS H 116      74.973 -49.489  40.510  1.00 75.98           N  
ANISOU10177  N   LYS H 116     6118   6071  16679   1429  -1223    960       N  
ATOM  10178  CA  LYS H 116      74.376 -48.882  41.691  1.00 76.03           C  
ANISOU10178  CA  LYS H 116     6198   6083  16606   1472  -1300    958       C  
ATOM  10179  C   LYS H 116      73.923 -47.419  41.448  1.00 75.99           C  
ANISOU10179  C   LYS H 116     6267   6085  16519   1511  -1385    931       C  
ATOM  10180  O   LYS H 116      74.551 -46.701  40.674  1.00 76.11           O  
ANISOU10180  O   LYS H 116     6288   6082  16550   1492  -1415    947       O  
ATOM  10181  CB  LYS H 116      75.394 -48.989  42.821  1.00 76.59           C  
ANISOU10181  CB  LYS H 116     6278   6112  16711   1442  -1352   1038       C  
ATOM  10182  CG  LYS H 116      75.003 -48.478  44.188  1.00 76.96           C  
ANISOU10182  CG  LYS H 116     6396   6157  16689   1477  -1432   1050       C  
ATOM  10183  CD  LYS H 116      76.151 -48.773  45.186  1.00 78.47           C  
ANISOU10183  CD  LYS H 116     6580   6306  16929   1437  -1467   1134       C  
ATOM  10184  CE  LYS H 116      77.536 -48.405  44.598  1.00 79.86           C  
ANISOU10184  CE  LYS H 116     6735   6440  17168   1385  -1493   1195       C  
ATOM  10185  NZ  LYS H 116      78.674 -48.539  45.550  1.00 81.35           N  
ANISOU10185  NZ  LYS H 116     6923   6589  17398   1346  -1537   1277       N  
ATOM  10186  N   LEU H 117      72.826 -46.983  42.076  1.00 76.08           N  
ANISOU10186  N   LEU H 117     6337   6125  16444   1564  -1420    888       N  
ATOM  10187  CA  LEU H 117      72.385 -45.584  41.958  1.00 76.02           C  
ANISOU10187  CA  LEU H 117     6407   6124  16355   1603  -1504    865       C  
ATOM  10188  C   LEU H 117      73.278 -44.581  42.681  1.00 76.68           C  
ANISOU10188  C   LEU H 117     6551   6163  16422   1590  -1614    931       C  
ATOM  10189  O   LEU H 117      73.545 -44.729  43.872  1.00 77.20           O  
ANISOU10189  O   LEU H 117     6640   6211  16483   1587  -1652    972       O  
ATOM  10190  CB  LEU H 117      70.980 -45.408  42.512  1.00 75.70           C  
ANISOU10190  CB  LEU H 117     6414   6124  16225   1663  -1513    805       C  
ATOM  10191  CG  LEU H 117      69.821 -45.612  41.542  1.00 75.11           C  
ANISOU10191  CG  LEU H 117     6318   6101  16120   1695  -1443    721       C  
ATOM  10192  CD1 LEU H 117      68.517 -45.502  42.299  1.00 74.85           C  
ANISOU10192  CD1 LEU H 117     6334   6106  16001   1752  -1457    672       C  
ATOM  10193  CD2 LEU H 117      69.868 -44.648  40.357  1.00 75.01           C  
ANISOU10193  CD2 LEU H 117     6318   6091  16090   1699  -1465    699       C  
ATOM  10194  N   ARG H 118      73.738 -43.553  41.979  1.00 79.45           N  
ANISOU10194  N   ARG H 118     6929   6497  16763   1582  -1665    940       N  
ATOM  10195  CA  ARG H 118      74.402 -42.455  42.663  1.00 81.25           C  
ANISOU10195  CA  ARG H 118     7226   6689  16955   1578  -1775    992       C  
ATOM  10196  C   ARG H 118      73.609 -41.150  42.487  1.00 80.86           C  
ANISOU10196  C   ARG H 118     7257   6658  16810   1626  -1843    949       C  
ATOM  10197  O   ARG H 118      73.615 -40.572  41.392  1.00 80.47           O  
ANISOU10197  O   ARG H 118     7205   6614  16757   1626  -1842    926       O  
ATOM  10198  CB  ARG H 118      75.836 -42.287  42.141  1.00 82.75           C  
ANISOU10198  CB  ARG H 118     7387   6838  17218   1520  -1791   1055       C  
ATOM  10199  CG  ARG H 118      76.603 -41.170  42.812  1.00 85.17           C  
ANISOU10199  CG  ARG H 118     7763   7107  17491   1509  -1902   1111       C  
ATOM  10200  CD  ARG H 118      77.894 -40.853  42.090  1.00 86.76           C  
ANISOU10200  CD  ARG H 118     7939   7273  17754   1458  -1918   1162       C  
ATOM  10201  NE  ARG H 118      78.704 -39.932  42.881  1.00 89.53           N  
ANISOU10201  NE  ARG H 118     8352   7588  18077   1442  -2021   1222       N  
ATOM  10202  CZ  ARG H 118      79.600 -40.329  43.777  1.00 92.60           C  
ANISOU10202  CZ  ARG H 118     8729   7947  18506   1406  -2041   1287       C  
ATOM  10203  NH1 ARG H 118      79.812 -41.631  43.976  1.00 93.21           N  
ANISOU10203  NH1 ARG H 118     8736   8025  18654   1383  -1965   1303       N  
ATOM  10204  NH2 ARG H 118      80.293 -39.427  44.466  1.00 95.40           N  
ANISOU10204  NH2 ARG H 118     9144   8273  18829   1392  -2135   1338       N  
ATOM  10205  N   THR H 119      72.931 -40.714  43.560  1.00 80.81           N  
ANISOU10205  N   THR H 119     7318   6660  16726   1666  -1899    939       N  
ATOM  10206  CA  THR H 119      72.324 -39.380  43.672  1.00 80.99           C  
ANISOU10206  CA  THR H 119     7428   6691  16652   1709  -1981    913       C  
ATOM  10207  C   THR H 119      71.460 -39.247  44.943  1.00 81.59           C  
ANISOU10207  C   THR H 119     7566   6782  16652   1752  -2021    897       C  
ATOM  10208  O   THR H 119      71.051 -40.251  45.534  1.00 81.41           O  
ANISOU10208  O   THR H 119     7512   6775  16645   1759  -1969    888       O  
ATOM  10209  CB  THR H 119      71.459 -39.037  42.448  1.00 78.84           C  
ANISOU10209  CB  THR H 119     7151   6456  16350   1740  -1945    842       C  
ATOM  10210  OG1 THR H 119      71.064 -37.653  42.495  1.00 79.29           O  
ANISOU10210  OG1 THR H 119     7294   6514  16319   1775  -2030    825       O  
ATOM  10211  CG2 THR H 119      70.254 -39.979  42.371  1.00 76.75           C  
ANISOU10211  CG2 THR H 119     6849   6239  16073   1773  -1860    777       C  
ATOM  10212  N   GLU H 120      71.148 -38.001  45.323  1.00 78.17           N  
ANISOU10212  N   GLU H 120     7222   6346  16133   1783  -2110    892       N  
ATOM  10213  CA  GLU H 120      70.489 -37.695  46.607  1.00 79.54           C  
ANISOU10213  CA  GLU H 120     7464   6526  16230   1821  -2163    887       C  
ATOM  10214  C   GLU H 120      68.956 -37.431  46.713  1.00 77.98           C  
ANISOU10214  C   GLU H 120     7310   6374  15943   1887  -2158    813       C  
ATOM  10215  O   GLU H 120      68.470 -37.271  47.827  1.00 79.38           O  
ANISOU10215  O   GLU H 120     7541   6556  16064   1915  -2199    813       O  
ATOM  10216  CB  GLU H 120      71.203 -36.471  47.208  1.00 82.64           C  
ANISOU10216  CB  GLU H 120     7937   6883  16581   1810  -2274    938       C  
ATOM  10217  CG  GLU H 120      72.484 -36.073  46.451  1.00 84.23           C  
ANISOU10217  CG  GLU H 120     8116   7048  16839   1759  -2295    986       C  
ATOM  10218  CD  GLU H 120      73.311 -34.986  47.153  1.00 87.92           C  
ANISOU10218  CD  GLU H 120     8657   7477  17270   1740  -2401   1043       C  
ATOM  10219  OE1 GLU H 120      72.772 -33.871  47.391  1.00 88.86           O  
ANISOU10219  OE1 GLU H 120     8860   7603  17301   1775  -2470   1021       O  
ATOM  10220  OE2 GLU H 120      74.501 -35.255  47.456  1.00 90.11           O  
ANISOU10220  OE2 GLU H 120     8909   7720  17609   1689  -2414   1108       O  
ATOM  10221  N   GLY H 121      68.168 -37.455  45.638  1.00 81.27           N  
ANISOU10221  N   GLY H 121     7703   6827  16349   1912  -2105    750       N  
ATOM  10222  CA  GLY H 121      68.290 -38.397  44.551  1.00 79.25           C  
ANISOU10222  CA  GLY H 121     7355   6586  16170   1888  -2008    730       C  
ATOM  10223  C   GLY H 121      67.650 -39.711  44.961  1.00 78.20           C  
ANISOU10223  C   GLY H 121     7171   6482  16061   1897  -1926    703       C  
ATOM  10224  O   GLY H 121      68.308 -40.767  44.918  1.00 78.32           O  
ANISOU10224  O   GLY H 121     7115   6484  16159   1856  -1866    733       O  
ATOM  10225  N   ASP H 122      66.394 -39.626  45.424  1.00 79.31           N  
ANISOU10225  N   ASP H 122     7350   6659  16124   1951  -1926    651       N  
ATOM  10226  CA  ASP H 122      65.595 -40.794  45.785  1.00 78.47           C  
ANISOU10226  CA  ASP H 122     7202   6587  16027   1968  -1849    616       C  
ATOM  10227  C   ASP H 122      65.165 -41.536  44.534  1.00 76.49           C  
ANISOU10227  C   ASP H 122     6876   6371  15815   1963  -1747    563       C  
ATOM  10228  O   ASP H 122      64.553 -42.607  44.605  1.00 75.96           O  
ANISOU10228  O   ASP H 122     6762   6335  15764   1970  -1668    530       O  
ATOM  10229  CB  ASP H 122      64.368 -40.410  46.596  1.00 78.71           C  
ANISOU10229  CB  ASP H 122     7299   6647  15960   2027  -1882    573       C  
ATOM  10230  CG  ASP H 122      63.093 -40.274  45.729  1.00 76.68           C  
ANISOU10230  CG  ASP H 122     7041   6444  15651   2072  -1837    490       C  
ATOM  10231  OD1 ASP H 122      63.017 -39.332  44.897  1.00 75.60           O  
ANISOU10231  OD1 ASP H 122     6931   6310  15484   2084  -1867    470       O  
ATOM  10232  OD2 ASP H 122      62.144 -41.083  45.904  1.00 76.41           O  
ANISOU10232  OD2 ASP H 122     6981   6448  15602   2098  -1773    444       O  
ATOM  10233  N   GLY H 123      65.467 -40.951  43.381  1.00 77.38           N  
ANISOU10233  N   GLY H 123     6979   6481  15940   1952  -1749    554       N  
ATOM  10234  CA  GLY H 123      65.416 -41.688  42.132  1.00 76.17           C  
ANISOU10234  CA  GLY H 123     6747   6352  15844   1932  -1653    520       C  
ATOM  10235  C   GLY H 123      64.190 -41.461  41.276  1.00 74.60           C  
ANISOU10235  C   GLY H 123     6550   6206  15589   1975  -1615    438       C  
ATOM  10236  O   GLY H 123      64.239 -41.672  40.070  1.00 73.98           O  
ANISOU10236  O   GLY H 123     6421   6143  15546   1959  -1557    412       O  
ATOM  10237  N   VAL H 124      63.092 -41.027  41.880  1.00 75.24           N  
ANISOU10237  N   VAL H 124     6691   6316  15582   2029  -1646    398       N  
ATOM  10238  CA  VAL H 124      61.852 -40.862  41.118  1.00 73.88           C  
ANISOU10238  CA  VAL H 124     6520   6198  15352   2072  -1607    319       C  
ATOM  10239  C   VAL H 124      61.828 -39.528  40.380  1.00 73.47           C  
ANISOU10239  C   VAL H 124     6517   6144  15255   2090  -1668    305       C  
ATOM  10240  O   VAL H 124      62.429 -38.550  40.834  1.00 74.35           O  
ANISOU10240  O   VAL H 124     6688   6217  15343   2087  -1760    350       O  
ATOM  10241  CB  VAL H 124      60.619 -40.956  42.007  1.00 73.74           C  
ANISOU10241  CB  VAL H 124     6544   6216  15257   2125  -1611    277       C  
ATOM  10242  CG1 VAL H 124      59.409 -41.065  41.152  1.00 72.65           C  
ANISOU10242  CG1 VAL H 124     6390   6138  15077   2160  -1550    196       C  
ATOM  10243  CG2 VAL H 124      60.732 -42.174  42.911  1.00 74.78           C  
ANISOU10243  CG2 VAL H 124     6639   6344  15431   2107  -1565    299       C  
ATOM  10244  N   TYR H 125      61.197 -39.496  39.211  1.00 71.66           N  
ANISOU10244  N   TYR H 125     6259   5955  15014   2104  -1615    246       N  
ATOM  10245  CA  TYR H 125      61.123 -38.252  38.451  1.00 71.68           C  
ANISOU10245  CA  TYR H 125     6305   5959  14972   2122  -1668    230       C  
ATOM  10246  C   TYR H 125      59.735 -38.057  37.829  1.00 71.21           C  
ANISOU10246  C   TYR H 125     6253   5961  14842   2172  -1632    147       C  
ATOM  10247  O   TYR H 125      59.326 -38.881  37.008  1.00 71.00           O  
ANISOU10247  O   TYR H 125     6159   5971  14845   2164  -1539    103       O  
ATOM  10248  CB  TYR H 125      62.216 -38.237  37.368  1.00 71.79           C  
ANISOU10248  CB  TYR H 125     6268   5945  15063   2071  -1649    259       C  
ATOM  10249  CG  TYR H 125      63.616 -38.113  37.910  1.00 72.31           C  
ANISOU10249  CG  TYR H 125     6339   5949  15185   2025  -1703    343       C  
ATOM  10250  CD1 TYR H 125      64.247 -39.192  38.481  1.00 72.44           C  
ANISOU10250  CD1 TYR H 125     6308   5945  15272   1988  -1664    384       C  
ATOM  10251  CD2 TYR H 125      64.308 -36.918  37.842  1.00 72.68           C  
ANISOU10251  CD2 TYR H 125     6441   5960  15214   2018  -1792    381       C  
ATOM  10252  CE1 TYR H 125      65.547 -39.088  38.993  1.00 72.94           C  
ANISOU10252  CE1 TYR H 125     6375   5952  15387   1944  -1713    462       C  
ATOM  10253  CE2 TYR H 125      65.609 -36.794  38.336  1.00 73.18           C  
ANISOU10253  CE2 TYR H 125     6510   5967  15327   1974  -1841    458       C  
ATOM  10254  CZ  TYR H 125      66.232 -37.882  38.913  1.00 73.31           C  
ANISOU10254  CZ  TYR H 125     6476   5964  15414   1937  -1802    499       C  
ATOM  10255  OH  TYR H 125      67.521 -37.777  39.414  1.00 74.20           O  
ANISOU10255  OH  TYR H 125     6594   6024  15575   1892  -1850    576       O  
ATOM  10256  N   THR H 126      59.029 -36.979  38.199  1.00 71.15           N  
ANISOU10256  N   THR H 126     6327   5964  14742   2221  -1703    125       N  
ATOM  10257  CA  THR H 126      57.635 -36.752  37.764  1.00 70.93           C  
ANISOU10257  CA  THR H 126     6315   5996  14638   2274  -1676     47       C  
ATOM  10258  C   THR H 126      57.512 -35.784  36.593  1.00 70.85           C  
ANISOU10258  C   THR H 126     6320   6000  14601   2286  -1694     18       C  
ATOM  10259  O   THR H 126      58.164 -34.759  36.578  1.00 70.99           O  
ANISOU10259  O   THR H 126     6385   5981  14607   2280  -1773     55       O  
ATOM  10260  CB  THR H 126      56.761 -36.185  38.896  1.00 70.94           C  
ANISOU10260  CB  THR H 126     6400   6009  14545   2328  -1738     33       C  
ATOM  10261  OG1 THR H 126      57.026 -36.865  40.129  1.00 71.06           O  
ANISOU10261  OG1 THR H 126     6416   6001  14581   2316  -1744     72       O  
ATOM  10262  CG2 THR H 126      55.293 -36.324  38.542  1.00 70.71           C  
ANISOU10262  CG2 THR H 126     6369   6046  14450   2377  -1688    -48       C  
ATOM  10263  N   LEU H 127      56.661 -36.080  35.627  1.00 70.64           N  
ANISOU10263  N   LEU H 127     6253   6027  14560   2303  -1622    -48       N  
ATOM  10264  CA  LEU H 127      56.531 -35.203  34.469  1.00 70.56           C  
ANISOU10264  CA  LEU H 127     6253   6034  14524   2312  -1633    -77       C  
ATOM  10265  C   LEU H 127      55.739 -33.914  34.798  1.00 70.55           C  
ANISOU10265  C   LEU H 127     6352   6054  14401   2362  -1710   -102       C  
ATOM  10266  O   LEU H 127      54.830 -33.921  35.629  1.00 70.51           O  
ANISOU10266  O   LEU H 127     6388   6072  14330   2403  -1722   -127       O  
ATOM  10267  CB  LEU H 127      55.877 -35.969  33.319  1.00 70.34           C  
ANISOU10267  CB  LEU H 127     6153   6065  14508   2306  -1525   -141       C  
ATOM  10268  CG  LEU H 127      56.029 -35.503  31.872  1.00 70.26           C  
ANISOU10268  CG  LEU H 127     6121   6076  14498   2287  -1501   -165       C  
ATOM  10269  CD1 LEU H 127      54.935 -34.523  31.499  1.00 70.14           C  
ANISOU10269  CD1 LEU H 127     6169   6114  14366   2332  -1525   -222       C  
ATOM  10270  CD2 LEU H 127      57.412 -34.921  31.639  1.00 70.45           C  
ANISOU10270  CD2 LEU H 127     6149   6037  14580   2248  -1559    -99       C  
ATOM  10271  N   ASN H 128      56.105 -32.813  34.141  1.00 72.79           N  
ANISOU10271  N   ASN H 128     6674   6328  14655   2357  -1761    -94       N  
ATOM  10272  CA  ASN H 128      55.594 -31.471  34.446  1.00 72.96           C  
ANISOU10272  CA  ASN H 128     6794   6357  14570   2398  -1845   -104       C  
ATOM  10273  C   ASN H 128      54.386 -31.044  33.611  1.00 72.69           C  
ANISOU10273  C   ASN H 128     6777   6394  14448   2434  -1811   -179       C  
ATOM  10274  O   ASN H 128      54.016 -31.702  32.650  1.00 72.93           O  
ANISOU10274  O   ASN H 128     6742   6468  14501   2423  -1725   -223       O  
ATOM  10275  CB  ASN H 128      56.700 -30.435  34.209  1.00 73.81           C  
ANISOU10275  CB  ASN H 128     6938   6412  14694   2373  -1924    -51       C  
ATOM  10276  CG  ASN H 128      57.291 -29.901  35.478  1.00 76.34           C  
ANISOU10276  CG  ASN H 128     7323   6674  15008   2377  -2019      9       C  
ATOM  10277  OD1 ASN H 128      56.969 -30.362  36.572  1.00 77.44           O  
ANISOU10277  OD1 ASN H 128     7477   6809  15139   2395  -2027     17       O  
ATOM  10278  ND2 ASN H 128      58.180 -28.928  35.346  1.00 77.69           N  
ANISOU10278  ND2 ASN H 128     7534   6801  15183   2359  -2094     54       N  
ATOM  10279  N   ASN H 129      53.809 -29.897  33.919  1.00 74.22           N  
ANISOU10279  N   ASN H 129     7059   6599  14541   2475  -1880   -193       N  
ATOM  10280  CA  ASN H 129      52.954 -29.277  32.933  1.00 74.27           C  
ANISOU10280  CA  ASN H 129     7082   6663  14473   2500  -1860   -253       C  
ATOM  10281  C   ASN H 129      53.888 -28.566  31.962  1.00 75.77           C  
ANISOU10281  C   ASN H 129     7268   6827  14695   2466  -1887   -227       C  
ATOM  10282  O   ASN H 129      53.535 -28.247  30.827  1.00 76.11           O  
ANISOU10282  O   ASN H 129     7296   6910  14711   2468  -1854   -267       O  
ATOM  10283  CB  ASN H 129      51.951 -28.325  33.582  1.00 73.97           C  
ANISOU10283  CB  ASN H 129     7139   6650  14316   2557  -1920   -279       C  
ATOM  10284  CG  ASN H 129      50.816 -29.061  34.264  1.00 72.89           C  
ANISOU10284  CG  ASN H 129     6998   6556  14139   2593  -1877   -321       C  
ATOM  10285  OD1 ASN H 129      50.411 -30.131  33.815  1.00 72.52           O  
ANISOU10285  OD1 ASN H 129     6879   6547  14129   2584  -1786   -356       O  
ATOM  10286  ND2 ASN H 129      50.301 -28.493  35.355  1.00 72.85           N  
ANISOU10286  ND2 ASN H 129     7074   6546  14061   2634  -1941   -317       N  
ATOM  10287  N   GLU H 130      55.104 -28.344  32.446  1.00 73.92           N  
ANISOU10287  N   GLU H 130     7044   6523  14519   2435  -1947   -157       N  
ATOM  10288  CA  GLU H 130      56.224 -27.818  31.676  1.00 75.99           C  
ANISOU10288  CA  GLU H 130     7294   6747  14831   2396  -1974   -119       C  
ATOM  10289  C   GLU H 130      56.879 -28.967  30.915  1.00 76.22           C  
ANISOU10289  C   GLU H 130     7219   6772  14971   2346  -1889   -111       C  
ATOM  10290  O   GLU H 130      57.891 -28.785  30.233  1.00 78.13           O  
ANISOU10290  O   GLU H 130     7432   6979  15273   2306  -1896    -77       O  
ATOM  10291  CB  GLU H 130      57.243 -27.138  32.616  1.00 78.10           C  
ANISOU10291  CB  GLU H 130     7619   6942  15115   2383  -2075    -45       C  
ATOM  10292  CG  GLU H 130      56.958 -25.699  33.042  1.00 77.91           C  
ANISOU10292  CG  GLU H 130     7700   6910  14992   2420  -2171    -42       C  
ATOM  10293  CD  GLU H 130      55.587 -25.468  33.715  1.00 76.75           C  
ANISOU10293  CD  GLU H 130     7612   6809  14741   2479  -2179    -90       C  
ATOM  10294  OE1 GLU H 130      54.633 -26.272  33.565  1.00 75.80           O  
ANISOU10294  OE1 GLU H 130     7452   6742  14605   2497  -2103   -143       O  
ATOM  10295  OE2 GLU H 130      55.462 -24.436  34.409  1.00 77.00           O  
ANISOU10295  OE2 GLU H 130     7732   6822  14702   2507  -2264    -75       O  
ATOM  10296  N   LYS H 131      56.302 -30.156  31.063  1.00 76.69           N  
ANISOU10296  N   LYS H 131     7221   6862  15056   2349  -1809   -142       N  
ATOM  10297  CA  LYS H 131      56.788 -31.370  30.406  1.00 76.81           C  
ANISOU10297  CA  LYS H 131     7135   6878  15173   2305  -1719   -140       C  
ATOM  10298  C   LYS H 131      58.286 -31.551  30.621  1.00 77.86           C  
ANISOU10298  C   LYS H 131     7240   6936  15406   2256  -1749    -63       C  
ATOM  10299  O   LYS H 131      59.039 -31.957  29.740  1.00 79.15           O  
ANISOU10299  O   LYS H 131     7338   7087  15648   2214  -1706    -49       O  
ATOM  10300  CB  LYS H 131      56.399 -31.348  28.926  1.00 77.83           C  
ANISOU10300  CB  LYS H 131     7223   7057  15293   2298  -1654   -193       C  
ATOM  10301  CG  LYS H 131      54.870 -31.384  28.787  1.00 77.15           C  
ANISOU10301  CG  LYS H 131     7154   7047  15114   2345  -1613   -269       C  
ATOM  10302  CD  LYS H 131      54.395 -31.480  27.355  1.00 74.84           C  
ANISOU10302  CD  LYS H 131     6815   6810  14812   2338  -1540   -326       C  
ATOM  10303  CE  LYS H 131      54.584 -30.148  26.638  1.00 73.26           C  
ANISOU10303  CE  LYS H 131     6665   6609  14561   2344  -1599   -325       C  
ATOM  10304  NZ  LYS H 131      53.667 -29.965  25.457  1.00 71.68           N  
ANISOU10304  NZ  LYS H 131     6450   6479  14306   2359  -1544   -394       N  
ATOM  10305  N   GLN H 132      58.673 -31.258  31.852  1.00 72.13           N  
ANISOU10305  N   GLN H 132     6566   6165  14675   2265  -1825    -14       N  
ATOM  10306  CA  GLN H 132      60.013 -31.461  32.356  1.00 72.34           C  
ANISOU10306  CA  GLN H 132     6575   6121  14789   2224  -1861     63       C  
ATOM  10307  C   GLN H 132      60.043 -32.688  33.284  1.00 72.36           C  
ANISOU10307  C   GLN H 132     6534   6111  14849   2217  -1822     81       C  
ATOM  10308  O   GLN H 132      59.034 -33.018  33.896  1.00 72.27           O  
ANISOU10308  O   GLN H 132     6539   6135  14786   2254  -1803     43       O  
ATOM  10309  CB  GLN H 132      60.468 -30.192  33.083  1.00 72.57           C  
ANISOU10309  CB  GLN H 132     6696   6106  14771   2236  -1979    108       C  
ATOM  10310  CG  GLN H 132      60.312 -28.937  32.243  1.00 72.60           C  
ANISOU10310  CG  GLN H 132     6751   6126  14708   2249  -2020     87       C  
ATOM  10311  CD  GLN H 132      60.683 -27.665  32.995  1.00 73.09           C  
ANISOU10311  CD  GLN H 132     6908   6146  14715   2264  -2136    128       C  
ATOM  10312  OE1 GLN H 132      60.891 -27.670  34.214  1.00 73.38           O  
ANISOU10312  OE1 GLN H 132     6982   6148  14751   2271  -2188    166       O  
ATOM  10313  NE2 GLN H 132      60.757 -26.561  32.265  1.00 73.17           N  
ANISOU10313  NE2 GLN H 132     6960   6161  14681   2268  -2176    120       N  
ATOM  10314  N   TRP H 133      61.182 -33.374  33.378  1.00 71.17           N  
ANISOU10314  N   TRP H 133     6333   5919  14788   2163  -1802    136       N  
ATOM  10315  CA  TRP H 133      61.295 -34.559  34.235  1.00 71.21           C  
ANISOU10315  CA  TRP H 133     6301   5918  14836   2144  -1758    156       C  
ATOM  10316  C   TRP H 133      61.964 -34.196  35.535  1.00 71.43           C  
ANISOU10316  C   TRP H 133     6387   5898  14857   2136  -1842    221       C  
ATOM  10317  O   TRP H 133      63.175 -33.954  35.554  1.00 71.62           O  
ANISOU10317  O   TRP H 133     6409   5872  14931   2094  -1881    283       O  
ATOM  10318  CB  TRP H 133      62.082 -35.651  33.535  1.00 71.20           C  
ANISOU10318  CB  TRP H 133     6205   5908  14940   2089  -1675    174       C  
ATOM  10319  CG  TRP H 133      61.282 -36.402  32.559  1.00 70.97           C  
ANISOU10319  CG  TRP H 133     6111   5934  14920   2095  -1574    108       C  
ATOM  10320  CD1 TRP H 133      61.283 -36.251  31.211  1.00 70.86           C  
ANISOU10320  CD1 TRP H 133     6058   5940  14924   2084  -1533     76       C  
ATOM  10321  CD2 TRP H 133      60.332 -37.429  32.850  1.00 70.82           C  
ANISOU10321  CD2 TRP H 133     6060   5960  14890   2113  -1498     62       C  
ATOM  10322  NE1 TRP H 133      60.395 -37.125  30.635  1.00 70.65           N  
ANISOU10322  NE1 TRP H 133     5977   5970  14898   2093  -1436     14       N  
ATOM  10323  CE2 TRP H 133      59.795 -37.862  31.622  1.00 70.63           C  
ANISOU10323  CE2 TRP H 133     5977   5983  14876   2110  -1412      4       C  
ATOM  10324  CE3 TRP H 133      59.887 -38.033  34.031  1.00 70.85           C  
ANISOU10324  CE3 TRP H 133     6076   5968  14874   2129  -1494     65       C  
ATOM  10325  CZ2 TRP H 133      58.829 -38.876  31.537  1.00 70.45           C  
ANISOU10325  CZ2 TRP H 133     5911   6013  14844   2123  -1322    -52       C  
ATOM  10326  CZ3 TRP H 133      58.926 -39.044  33.945  1.00 70.67           C  
ANISOU10326  CZ3 TRP H 133     6010   5997  14843   2143  -1405     10       C  
ATOM  10327  CH2 TRP H 133      58.408 -39.448  32.707  1.00 70.47           C  
ANISOU10327  CH2 TRP H 133     5929   6020  14828   2139  -1321    -48       C  
ATOM  10328  N   ILE H 134      61.198 -34.171  36.624  1.00 71.43           N  
ANISOU10328  N   ILE H 134     6437   5911  14794   2175  -1870    208       N  
ATOM  10329  CA  ILE H 134      61.655 -33.483  37.838  1.00 71.65           C  
ANISOU10329  CA  ILE H 134     6541   5896  14787   2178  -1967    262       C  
ATOM  10330  C   ILE H 134      61.634 -34.246  39.169  1.00 71.74           C  
ANISOU10330  C   ILE H 134     6555   5897  14805   2176  -1965    288       C  
ATOM  10331  O   ILE H 134      60.562 -34.548  39.699  1.00 71.62           O  
ANISOU10331  O   ILE H 134     6556   5918  14739   2217  -1945    246       O  
ATOM  10332  CB  ILE H 134      60.827 -32.210  38.070  1.00 71.62           C  
ANISOU10332  CB  ILE H 134     6630   5909  14675   2233  -2041    231       C  
ATOM  10333  CG1 ILE H 134      60.629 -31.463  36.757  1.00 71.51           C  
ANISOU10333  CG1 ILE H 134     6615   5914  14642   2243  -2038    195       C  
ATOM  10334  CG2 ILE H 134      61.516 -31.315  39.107  1.00 71.87           C  
ANISOU10334  CG2 ILE H 134     6742   5891  14674   2226  -2147    292       C  
ATOM  10335  CD1 ILE H 134      61.905 -30.916  36.198  1.00 71.66           C  
ANISOU10335  CD1 ILE H 134     6629   5887  14711   2198  -2077    247       C  
ATOM  10336  N   ASN H 135      62.820 -34.497  39.734  1.00 73.24           N  
ANISOU10336  N   ASN H 135     6735   6038  15055   2130  -1991    359       N  
ATOM  10337  CA  ASN H 135      62.891 -35.043  41.089  1.00 73.36           C  
ANISOU10337  CA  ASN H 135     6764   6038  15071   2128  -2006    391       C  
ATOM  10338  C   ASN H 135      62.868 -33.960  42.154  1.00 73.52           C  
ANISOU10338  C   ASN H 135     6885   6035  15013   2152  -2112    418       C  
ATOM  10339  O   ASN H 135      63.755 -33.102  42.200  1.00 73.70           O  
ANISOU10339  O   ASN H 135     6947   6018  15036   2129  -2184    465       O  
ATOM  10340  CB  ASN H 135      64.134 -35.885  41.310  1.00 73.52           C  
ANISOU10340  CB  ASN H 135     6726   6018  15189   2068  -1982    455       C  
ATOM  10341  CG  ASN H 135      64.340 -36.206  42.779  1.00 73.68           C  
ANISOU10341  CG  ASN H 135     6775   6016  15203   2065  -2017    498       C  
ATOM  10342  OD1 ASN H 135      65.381 -35.902  43.348  1.00 73.91           O  
ANISOU10342  OD1 ASN H 135     6826   6000  15256   2031  -2075    563       O  
ATOM  10343  ND2 ASN H 135      63.323 -36.789  43.411  1.00 73.56           N  
ANISOU10343  ND2 ASN H 135     6763   6035  15152   2100  -1984    459       N  
ATOM  10344  N   LYS H 136      61.903 -34.061  43.065  1.00 76.39           N  
ANISOU10344  N   LYS H 136     7288   6423  15314   2195  -2120    390       N  
ATOM  10345  CA  LYS H 136      61.673 -33.003  44.033  1.00 78.07           C  
ANISOU10345  CA  LYS H 136     7601   6622  15440   2225  -2217    404       C  
ATOM  10346  C   LYS H 136      62.860 -32.743  44.981  1.00 80.91           C  
ANISOU10346  C   LYS H 136     7992   6927  15824   2186  -2287    484       C  
ATOM  10347  O   LYS H 136      62.834 -31.809  45.766  1.00 83.07           O  
ANISOU10347  O   LYS H 136     8349   7184  16030   2203  -2371    502       O  
ATOM  10348  CB  LYS H 136      60.399 -33.289  44.829  1.00 77.50           C  
ANISOU10348  CB  LYS H 136     7558   6588  15301   2277  -2203    358       C  
ATOM  10349  CG  LYS H 136      60.395 -34.499  45.735  1.00 76.23           C  
ANISOU10349  CG  LYS H 136     7357   6428  15180   2265  -2159    374       C  
ATOM  10350  CD  LYS H 136      59.062 -34.515  46.504  1.00 76.29           C  
ANISOU10350  CD  LYS H 136     7410   6474  15103   2322  -2160    327       C  
ATOM  10351  CE  LYS H 136      58.808 -35.814  47.256  1.00 75.30           C  
ANISOU10351  CE  LYS H 136     7238   6361  15012   2318  -2100    327       C  
ATOM  10352  NZ  LYS H 136      59.955 -36.229  48.118  1.00 76.35           N  
ANISOU10352  NZ  LYS H 136     7359   6446  15205   2272  -2125    401       N  
ATOM  10353  N   ALA H 137      63.902 -33.544  44.897  1.00 74.24           N  
ANISOU10353  N   ALA H 137     7081   6054  15073   2132  -2253    531       N  
ATOM  10354  CA  ALA H 137      65.094 -33.313  45.695  1.00 74.52           C  
ANISOU10354  CA  ALA H 137     7140   6038  15135   2091  -2316    607       C  
ATOM  10355  C   ALA H 137      66.213 -32.650  44.876  1.00 74.64           C  
ANISOU10355  C   ALA H 137     7150   6019  15190   2050  -2349    646       C  
ATOM  10356  O   ALA H 137      66.778 -31.637  45.269  1.00 74.82           O  
ANISOU10356  O   ALA H 137     7239   6012  15178   2041  -2434    684       O  
ATOM  10357  CB  ALA H 137      65.578 -34.616  46.297  1.00 74.58           C  
ANISOU10357  CB  ALA H 137     7084   6035  15219   2058  -2264    641       C  
ATOM  10358  N   VAL H 138      66.609 -33.309  43.798  1.00 74.89           N  
ANISOU10358  N   VAL H 138     7099   6055  15299   2020  -2277    640       N  
ATOM  10359  CA  VAL H 138      67.651 -32.810  42.917  1.00 75.25           C  
ANISOU10359  CA  VAL H 138     7129   6071  15390   1979  -2296    674       C  
ATOM  10360  C   VAL H 138      67.126 -32.113  41.662  1.00 74.80           C  
ANISOU10360  C   VAL H 138     7078   6039  15302   2003  -2287    622       C  
ATOM  10361  O   VAL H 138      67.900 -31.673  40.832  1.00 75.12           O  
ANISOU10361  O   VAL H 138     7105   6060  15377   1973  -2299    643       O  
ATOM  10362  CB  VAL H 138      68.576 -33.959  42.476  1.00 75.16           C  
ANISOU10362  CB  VAL H 138     7021   6043  15492   1924  -2224    707       C  
ATOM  10363  CG1 VAL H 138      69.006 -34.799  43.681  1.00 77.08           C  
ANISOU10363  CG1 VAL H 138     7250   6267  15771   1902  -2221    754       C  
ATOM  10364  CG2 VAL H 138      67.863 -34.826  41.441  1.00 74.49           C  
ANISOU10364  CG2 VAL H 138     6862   6001  15441   1936  -2120    647       C  
ATOM  10365  N   GLY H 139      65.817 -32.029  41.495  1.00 75.11           N  
ANISOU10365  N   GLY H 139     7136   6125  15279   2057  -2264    554       N  
ATOM  10366  CA  GLY H 139      65.308 -31.340  40.324  1.00 74.57           C  
ANISOU10366  CA  GLY H 139     7074   6081  15177   2081  -2257    505       C  
ATOM  10367  C   GLY H 139      65.521 -31.973  38.958  1.00 74.31           C  
ANISOU10367  C   GLY H 139     6953   6063  15218   2055  -2173    484       C  
ATOM  10368  O   GLY H 139      64.928 -33.002  38.605  1.00 74.14           O  
ANISOU10368  O   GLY H 139     6867   6076  15226   2062  -2085    443       O  
ATOM  10369  N   ASP H 140      66.284 -31.248  38.149  1.00 81.00           N  
ANISOU10369  N   ASP H 140     7804   6888  16085   2030  -2204    506       N  
ATOM  10370  CA  ASP H 140      66.566 -31.574  36.754  1.00 80.71           C  
ANISOU10370  CA  ASP H 140     7695   6861  16110   2006  -2139    487       C  
ATOM  10371  C   ASP H 140      67.696 -32.613  36.589  1.00 81.13           C  
ANISOU10371  C   ASP H 140     7667   6885  16273   1944  -2087    537       C  
ATOM  10372  O   ASP H 140      67.906 -33.154  35.496  1.00 80.87           O  
ANISOU10372  O   ASP H 140     7563   6863  16302   1921  -2017    521       O  
ATOM  10373  CB  ASP H 140      66.913 -30.261  36.020  1.00 82.93           C  
ANISOU10373  CB  ASP H 140     8023   7128  16358   2007  -2203    492       C  
ATOM  10374  CG  ASP H 140      67.001 -30.423  34.513  1.00 82.68           C  
ANISOU10374  CG  ASP H 140     7927   7113  16373   1992  -2140    463       C  
ATOM  10375  OD1 ASP H 140      66.302 -31.287  33.955  1.00 80.85           O  
ANISOU10375  OD1 ASP H 140     7635   6922  16163   2003  -2053    412       O  
ATOM  10376  OD2 ASP H 140      67.776 -29.674  33.883  1.00 84.65           O  
ANISOU10376  OD2 ASP H 140     8188   7337  16637   1968  -2179    489       O  
ATOM  10377  N   LYS H 141      68.415 -32.899  37.669  1.00 74.76           N  
ANISOU10377  N   LYS H 141     6872   6043  15492   1918  -2120    596       N  
ATOM  10378  CA  LYS H 141      69.628 -33.705  37.539  1.00 74.97           C  
ANISOU10378  CA  LYS H 141     6830   6035  15619   1857  -2085    651       C  
ATOM  10379  C   LYS H 141      69.335 -35.205  37.595  1.00 74.64           C  
ANISOU10379  C   LYS H 141     6709   6015  15636   1848  -1984    634       C  
ATOM  10380  O   LYS H 141      68.700 -35.713  38.524  1.00 74.56           O  
ANISOU10380  O   LYS H 141     6709   6020  15599   1871  -1974    621       O  
ATOM  10381  CB  LYS H 141      70.656 -33.335  38.616  1.00 76.81           C  
ANISOU10381  CB  LYS H 141     7107   6219  15858   1827  -2164    728       C  
ATOM  10382  CG  LYS H 141      71.959 -34.089  38.475  1.00 77.94           C  
ANISOU10382  CG  LYS H 141     7183   6326  16105   1764  -2133    788       C  
ATOM  10383  CD  LYS H 141      73.034 -33.578  39.435  1.00 79.66           C  
ANISOU10383  CD  LYS H 141     7447   6497  16325   1732  -2218    864       C  
ATOM  10384  CE  LYS H 141      72.628 -33.721  40.902  1.00 82.66           C  
ANISOU10384  CE  LYS H 141     7873   6876  16658   1755  -2253    875       C  
ATOM  10385  NZ  LYS H 141      73.720 -33.280  41.824  1.00 85.26           N  
ANISOU10385  NZ  LYS H 141     8241   7160  16993   1720  -2332    950       N  
ATOM  10386  N   LEU H 142      69.795 -35.919  36.585  1.00 74.12           N  
ANISOU10386  N   LEU H 142     6562   5951  15650   1812  -1909    632       N  
ATOM  10387  CA  LEU H 142      69.587 -37.346  36.561  1.00 74.03           C  
ANISOU10387  CA  LEU H 142     6473   5959  15696   1798  -1811    617       C  
ATOM  10388  C   LEU H 142      70.543 -38.050  37.535  1.00 74.24           C  
ANISOU10388  C   LEU H 142     6479   5947  15783   1757  -1816    686       C  
ATOM  10389  O   LEU H 142      71.477 -37.419  38.052  1.00 74.46           O  
ANISOU10389  O   LEU H 142     6546   5932  15815   1733  -1893    747       O  
ATOM  10390  CB  LEU H 142      69.777 -37.857  35.138  1.00 73.89           C  
ANISOU10390  CB  LEU H 142     6378   5956  15742   1771  -1728    592       C  
ATOM  10391  CG  LEU H 142      68.721 -37.410  34.132  1.00 73.66           C  
ANISOU10391  CG  LEU H 142     6354   5974  15660   1811  -1702    516       C  
ATOM  10392  CD1 LEU H 142      69.128 -37.789  32.725  1.00 73.57           C  
ANISOU10392  CD1 LEU H 142     6270   5968  15714   1777  -1631    503       C  
ATOM  10393  CD2 LEU H 142      67.401 -38.038  34.479  1.00 73.48           C  
ANISOU10393  CD2 LEU H 142     6326   6000  15592   1853  -1649    455       C  
ATOM  10394  N   PRO H 143      70.293 -39.351  37.818  1.00 75.14           N  
ANISOU10394  N   PRO H 143     6534   6077  15939   1748  -1736    676       N  
ATOM  10395  CA  PRO H 143      71.344 -40.138  38.476  1.00 75.66           C  
ANISOU10395  CA  PRO H 143     6563   6106  16080   1700  -1726    743       C  
ATOM  10396  C   PRO H 143      72.283 -40.791  37.473  1.00 75.60           C  
ANISOU10396  C   PRO H 143     6473   6081  16169   1646  -1661    767       C  
ATOM  10397  O   PRO H 143      72.005 -40.781  36.274  1.00 75.17           O  
ANISOU10397  O   PRO H 143     6387   6050  16126   1647  -1612    725       O  
ATOM  10398  CB  PRO H 143      70.553 -41.201  39.234  1.00 75.50           C  
ANISOU10398  CB  PRO H 143     6520   6113  16055   1720  -1669    717       C  
ATOM  10399  CG  PRO H 143      69.326 -41.380  38.433  1.00 74.75           C  
ANISOU10399  CG  PRO H 143     6408   6072  15922   1757  -1606    635       C  
ATOM  10400  CD  PRO H 143      68.993 -40.047  37.832  1.00 74.64           C  
ANISOU10400  CD  PRO H 143     6452   6065  15843   1787  -1667    608       C  
ATOM  10401  N   GLU H 144      73.352 -41.398  37.970  1.00 75.22           N  
ANISOU10401  N   GLU H 144     6393   5996  16192   1600  -1656    832       N  
ATOM  10402  CA  GLU H 144      74.291 -42.106  37.117  1.00 75.26           C  
ANISOU10402  CA  GLU H 144     6320   5983  16294   1546  -1593    860       C  
ATOM  10403  C   GLU H 144      74.498 -43.475  37.743  1.00 75.29           C  
ANISOU10403  C   GLU H 144     6266   5983  16356   1521  -1526    882       C  
ATOM  10404  O   GLU H 144      74.291 -43.641  38.944  1.00 75.44           O  
ANISOU10404  O   GLU H 144     6316   6000  16349   1536  -1556    899       O  
ATOM  10405  CB  GLU H 144      75.600 -41.337  36.986  1.00 75.76           C  
ANISOU10405  CB  GLU H 144     6400   5998  16388   1507  -1662    927       C  
ATOM  10406  CG  GLU H 144      76.245 -41.009  38.330  1.00 76.30           C  
ANISOU10406  CG  GLU H 144     6517   6030  16442   1496  -1744    991       C  
ATOM  10407  CD  GLU H 144      77.337 -39.933  38.244  1.00 77.21           C  
ANISOU10407  CD  GLU H 144     6673   6105  16560   1468  -1831   1048       C  
ATOM  10408  OE1 GLU H 144      78.523 -40.283  38.473  1.00 78.43           O  
ANISOU10408  OE1 GLU H 144     6796   6222  16781   1418  -1836   1114       O  
ATOM  10409  OE2 GLU H 144      77.008 -38.743  37.974  1.00 77.55           O  
ANISOU10409  OE2 GLU H 144     6778   6153  16535   1496  -1895   1026       O  
ATOM  10410  N   CYS H 145      74.862 -44.467  36.943  1.00 75.24           N  
ANISOU10410  N   CYS H 145     6179   5980  16429   1485  -1434    880       N  
ATOM  10411  CA  CYS H 145      75.043 -45.789  37.501  1.00 75.27           C  
ANISOU10411  CA  CYS H 145     6128   5981  16489   1461  -1367    900       C  
ATOM  10412  C   CYS H 145      76.532 -46.153  37.716  1.00 75.76           C  
ANISOU10412  C   CYS H 145     6155   5994  16638   1401  -1375    984       C  
ATOM  10413  O   CYS H 145      77.333 -46.216  36.779  1.00 75.84           O  
ANISOU10413  O   CYS H 145     6123   5985  16709   1362  -1348   1004       O  
ATOM  10414  CB  CYS H 145      74.348 -46.804  36.615  1.00 74.75           C  
ANISOU10414  CB  CYS H 145     5997   5956  16450   1461  -1252    840       C  
ATOM  10415  SG  CYS H 145      72.562 -46.757  36.758  1.00 74.21           S  
ANISOU10415  SG  CYS H 145     5962   5949  16285   1529  -1230    749       S  
ATOM  10416  N   GLU H 146      76.879 -46.400  38.973  1.00 79.90           N  
ANISOU10416  N   GLU H 146     6697   6496  17165   1395  -1411   1031       N  
ATOM  10417  CA  GLU H 146      78.254 -46.629  39.387  1.00 81.59           C  
ANISOU10417  CA  GLU H 146     6888   6664  17449   1343  -1433   1114       C  
ATOM  10418  C   GLU H 146      78.520 -48.097  39.780  1.00 81.90           C  
ANISOU10418  C   GLU H 146     6859   6700  17559   1313  -1350   1135       C  
ATOM  10419  O   GLU H 146      77.763 -48.690  40.546  1.00 81.24           O  
ANISOU10419  O   GLU H 146     6780   6639  17450   1339  -1325   1112       O  
ATOM  10420  CB  GLU H 146      78.563 -45.676  40.539  1.00 82.33           C  
ANISOU10420  CB  GLU H 146     7059   6733  17490   1355  -1546   1158       C  
ATOM  10421  CG  GLU H 146      79.729 -46.034  41.438  1.00 84.77           C  
ANISOU10421  CG  GLU H 146     7355   7001  17852   1311  -1573   1240       C  
ATOM  10422  CD  GLU H 146      79.774 -45.112  42.653  1.00 85.84           C  
ANISOU10422  CD  GLU H 146     7574   7123  17920   1331  -1682   1271       C  
ATOM  10423  OE1 GLU H 146      79.426 -45.589  43.759  1.00 85.68           O  
ANISOU10423  OE1 GLU H 146     7565   7108  17882   1346  -1685   1277       O  
ATOM  10424  OE2 GLU H 146      80.123 -43.912  42.497  1.00 87.17           O  
ANISOU10424  OE2 GLU H 146     7796   7274  18050   1332  -1763   1286       O  
ATOM  10425  N   ALA H 147      79.590 -48.681  39.244  1.00 77.21           N  
ANISOU10425  N   ALA H 147     6203   6079  17054   1259  -1306   1180       N  
ATOM  10426  CA  ALA H 147      79.871 -50.092  39.464  1.00 77.34           C  
ANISOU10426  CA  ALA H 147     6151   6093  17143   1228  -1220   1198       C  
ATOM  10427  C   ALA H 147      80.086 -50.421  40.938  1.00 77.94           C  
ANISOU10427  C   ALA H 147     6245   6153  17215   1228  -1255   1245       C  
ATOM  10428  O   ALA H 147      80.645 -49.636  41.693  1.00 78.49           O  
ANISOU10428  O   ALA H 147     6365   6197  17262   1225  -1348   1293       O  
ATOM  10429  CB  ALA H 147      81.072 -50.516  38.660  1.00 77.58           C  
ANISOU10429  CB  ALA H 147     6118   6092  17267   1170  -1178   1244       C  
ATOM  10430  N   VAL H 148      79.589 -51.579  41.347  1.00 75.81           N  
ANISOU10430  N   VAL H 148     5938   5902  16963   1232  -1182   1226       N  
ATOM  10431  CA  VAL H 148      79.825 -52.092  42.684  1.00 76.80           C  
ANISOU10431  CA  VAL H 148     6069   6015  17097   1226  -1200   1270       C  
ATOM  10432  C   VAL H 148      81.203 -52.708  42.665  1.00 77.67           C  
ANISOU10432  C   VAL H 148     6123   6085  17303   1165  -1177   1345       C  
ATOM  10433  O   VAL H 148      81.702 -53.039  41.586  1.00 77.38           O  
ANISOU10433  O   VAL H 148     6034   6040  17325   1132  -1120   1346       O  
ATOM  10434  CB  VAL H 148      78.772 -53.124  43.090  1.00 76.68           C  
ANISOU10434  CB  VAL H 148     6033   6036  17066   1252  -1126   1222       C  
ATOM  10435  CG1 VAL H 148      78.535 -53.084  44.588  1.00 77.35           C  
ANISOU10435  CG1 VAL H 148     6162   6119  17108   1275  -1182   1245       C  
ATOM  10436  CG2 VAL H 148      77.491 -52.844  42.358  1.00 75.53           C  
ANISOU10436  CG2 VAL H 148     5905   5936  16858   1297  -1098   1135       C  
ATOM  10437  N   CYS H 149      81.827 -52.831  43.838  1.00 74.77           N  
ANISOU10437  N   CYS H 149     5768   5693  16948   1150  -1222   1406       N  
ATOM  10438  CA  CYS H 149      83.140 -53.494  43.970  1.00 75.01           C  
ANISOU10438  CA  CYS H 149     5744   5686  17069   1092  -1200   1482       C  
ATOM  10439  C   CYS H 149      83.161 -54.450  45.169  1.00 75.72           C  
ANISOU10439  C   CYS H 149     5817   5774  17179   1087  -1177   1511       C  
ATOM  10440  O   CYS H 149      82.611 -54.142  46.210  1.00 75.86           O  
ANISOU10440  O   CYS H 149     5886   5802  17135   1121  -1230   1505       O  
ATOM  10441  CB  CYS H 149      84.259 -52.442  44.108  1.00 75.95           C  
ANISOU10441  CB  CYS H 149     5898   5768  17193   1067  -1296   1546       C  
ATOM  10442  SG  CYS H 149      84.249 -51.484  45.672  1.00 77.24           S  
ANISOU10442  SG  CYS H 149     6150   5921  17278   1093  -1422   1581       S  
ATOM  10443  N   GLY H 150      83.781 -55.607  45.041  1.00 75.20           N  
ANISOU10443  N   GLY H 150     5681   5695  17198   1046  -1099   1543       N  
ATOM  10444  CA  GLY H 150      83.874 -56.504  46.183  1.00 75.33           C  
ANISOU10444  CA  GLY H 150     5680   5707  17235   1039  -1079   1575       C  
ATOM  10445  C   GLY H 150      82.661 -57.402  46.345  1.00 75.12           C  
ANISOU10445  C   GLY H 150     5638   5719  17184   1071  -1004   1512       C  
ATOM  10446  O   GLY H 150      82.343 -57.892  47.433  1.00 75.16           O  
ANISOU10446  O   GLY H 150     5653   5732  17174   1085  -1005   1520       O  
ATOM  10447  N   LYS H 151      81.976 -57.604  45.234  1.00 74.87           N  
ANISOU10447  N   LYS H 151     5586   5714  17148   1082   -937   1447       N  
ATOM  10448  CA  LYS H 151      80.784 -58.426  45.175  1.00 74.64           C  
ANISOU10448  CA  LYS H 151     5541   5726  17093   1111   -858   1380       C  
ATOM  10449  C   LYS H 151      80.891 -59.273  43.920  1.00 74.53           C  
ANISOU10449  C   LYS H 151     5459   5718  17140   1080   -751   1355       C  
ATOM  10450  O   LYS H 151      80.321 -58.925  42.893  1.00 74.33           O  
ANISOU10450  O   LYS H 151     5437   5715  17089   1095   -728   1298       O  
ATOM  10451  CB  LYS H 151      79.504 -57.572  45.131  1.00 74.42           C  
ANISOU10451  CB  LYS H 151     5575   5736  16965   1171   -898   1308       C  
ATOM  10452  CG  LYS H 151      79.424 -56.436  46.147  1.00 74.52           C  
ANISOU10452  CG  LYS H 151     5666   5741  16909   1203  -1017   1328       C  
ATOM  10453  CD  LYS H 151      79.235 -56.924  47.572  1.00 74.63           C  
ANISOU10453  CD  LYS H 151     5695   5755  16906   1215  -1033   1351       C  
ATOM  10454  CE  LYS H 151      79.311 -55.773  48.554  1.00 74.76           C  
ANISOU10454  CE  LYS H 151     5789   5759  16859   1240  -1153   1379       C  
ATOM  10455  NZ  LYS H 151      79.240 -56.242  49.957  1.00 74.89           N  
ANISOU10455  NZ  LYS H 151     5819   5772  16864   1247  -1172   1408       N  
ATOM  10456  N   PRO H 152      81.685 -60.347  43.963  1.00 74.67           N  
ANISOU10456  N   PRO H 152     5417   5713  17241   1033   -686   1400       N  
ATOM  10457  CA  PRO H 152      81.682 -61.156  42.750  1.00 74.54           C  
ANISOU10457  CA  PRO H 152     5342   5705  17276   1006   -581   1370       C  
ATOM  10458  C   PRO H 152      80.444 -62.030  42.710  1.00 74.31           C  
ANISOU10458  C   PRO H 152     5302   5720  17214   1032   -498   1299       C  
ATOM  10459  O   PRO H 152      79.989 -62.545  43.742  1.00 74.33           O  
ANISOU10459  O   PRO H 152     5313   5734  17195   1050   -494   1298       O  
ATOM  10460  CB  PRO H 152      82.966 -61.975  42.866  1.00 74.78           C  
ANISOU10460  CB  PRO H 152     5317   5694  17403    948   -544   1446       C  
ATOM  10461  CG  PRO H 152      83.249 -62.022  44.317  1.00 74.98           C  
ANISOU10461  CG  PRO H 152     5363   5704  17421    953   -601   1497       C  
ATOM  10462  CD  PRO H 152      82.596 -60.870  44.991  1.00 74.93           C  
ANISOU10462  CD  PRO H 152     5432   5714  17325   1003   -701   1477       C  
ATOM  10463  N   LYS H 153      79.918 -62.203  41.505  1.00 80.73           N  
ANISOU10463  N   LYS H 153     6094   6557  18022   1032   -432   1239       N  
ATOM  10464  CA  LYS H 153      78.693 -62.943  41.315  1.00 81.13           C  
ANISOU10464  CA  LYS H 153     6137   6655  18035   1057   -354   1164       C  
ATOM  10465  C   LYS H 153      78.790 -64.368  41.817  1.00 83.92           C  
ANISOU10465  C   LYS H 153     6447   7005  18435   1031   -272   1181       C  
ATOM  10466  O   LYS H 153      77.824 -64.858  42.415  1.00 85.02           O  
ANISOU10466  O   LYS H 153     6598   7177  18528   1061   -246   1141       O  
ATOM  10467  CB  LYS H 153      78.299 -62.952  39.850  1.00 80.40           C  
ANISOU10467  CB  LYS H 153     6023   6586  17940   1051   -291   1105       C  
ATOM  10468  CG  LYS H 153      77.009 -63.723  39.594  1.00 80.98           C  
ANISOU10468  CG  LYS H 153     6089   6711  17969   1074   -207   1025       C  
ATOM  10469  CD  LYS H 153      75.866 -63.168  40.429  1.00 82.82           C  
ANISOU10469  CD  LYS H 153     6379   6980  18110   1134   -262    983       C  
ATOM  10470  CE  LYS H 153      74.629 -62.876  39.574  1.00 83.12           C  
ANISOU10470  CE  LYS H 153     6433   7070  18079   1169   -232    893       C  
ATOM  10471  NZ  LYS H 153      73.748 -64.071  39.377  1.00 81.23           N  
ANISOU10471  NZ  LYS H 153     6165   6871  17828   1168   -127    837       N  
ATOM  10472  N   ASN H 154      79.918 -65.037  41.557  1.00 79.86           N  
ANISOU10472  N   ASN H 154     5883   6453  18009    977   -229   1238       N  
ATOM  10473  CA  ASN H 154      80.157 -66.367  42.118  1.00 82.61           C  
ANISOU10473  CA  ASN H 154     6191   6790  18406    950   -158   1265       C  
ATOM  10474  C   ASN H 154      81.493 -66.365  42.825  1.00 83.43           C  
ANISOU10474  C   ASN H 154     6280   6844  18575    915   -203   1360       C  
ATOM  10475  O   ASN H 154      82.531 -66.507  42.182  1.00 84.19           O  
ANISOU10475  O   ASN H 154     6340   6906  18742    870   -182   1403       O  
ATOM  10476  CB  ASN H 154      80.117 -67.505  41.064  1.00 84.56           C  
ANISOU10476  CB  ASN H 154     6386   7044  18698    915    -35   1236       C  
ATOM  10477  CG  ASN H 154      79.676 -67.037  39.679  1.00 83.14           C  
ANISOU10477  CG  ASN H 154     6207   6887  18494    920     -9   1175       C  
ATOM  10478  OD1 ASN H 154      80.509 -66.632  38.860  1.00 81.36           O  
ANISOU10478  OD1 ASN H 154     5966   6635  18313    890    -18   1203       O  
ATOM  10479  ND2 ASN H 154      78.376 -67.120  39.400  1.00 84.32           N  
ANISOU10479  ND2 ASN H 154     6375   7088  18575    955     25   1094       N  
ATOM  10480  N   PRO H 155      81.475 -66.158  44.150  1.00 80.94           N  
ANISOU10480  N   PRO H 155     5995   6524  18234    936   -269   1392       N  
ATOM  10481  CA  PRO H 155      82.668 -66.162  45.021  1.00 82.03           C  
ANISOU10481  CA  PRO H 155     6123   6618  18425    906   -318   1482       C  
ATOM  10482  C   PRO H 155      83.256 -67.555  45.288  1.00 84.88           C  
ANISOU10482  C   PRO H 155     6429   6959  18863    863   -235   1523       C  
ATOM  10483  O   PRO H 155      82.742 -68.552  44.771  1.00 86.02           O  
ANISOU10483  O   PRO H 155     6542   7121  19019    856   -136   1481       O  
ATOM  10484  CB  PRO H 155      82.138 -65.555  46.323  1.00 82.12           C  
ANISOU10484  CB  PRO H 155     6191   6643  18367    950   -405   1484       C  
ATOM  10485  CG  PRO H 155      80.686 -65.931  46.340  1.00 79.77           C  
ANISOU10485  CG  PRO H 155     5910   6394  18004    993   -359   1401       C  
ATOM  10486  CD  PRO H 155      80.228 -65.949  44.906  1.00 79.93           C  
ANISOU10486  CD  PRO H 155     5913   6437  18021    991   -296   1339       C  
ATOM  10487  N   ALA H 156      84.263 -67.609  46.161  1.00 79.79           N  
ANISOU10487  N   ALA H 156     5775   6279  18262    839   -278   1603       N  
ATOM  10488  CA  ALA H 156      84.840 -68.874  46.598  1.00 82.60           C  
ANISOU10488  CA  ALA H 156     6083   6614  18687    801   -209   1649       C  
ATOM  10489  C   ALA H 156      83.837 -69.631  47.450  1.00 85.03           C  
ANISOU10489  C   ALA H 156     6401   6953  18955    831   -174   1612       C  
ATOM  10490  O   ALA H 156      82.684 -69.207  47.576  1.00 87.08           O  
ANISOU10490  O   ALA H 156     6701   7251  19135    879   -194   1548       O  
ATOM  10491  CB  ALA H 156      86.084 -68.644  47.384  1.00 83.76           C  
ANISOU10491  CB  ALA H 156     6223   6721  18882    772   -272   1741       C  
ATOM  10492  N   ASN H 157      84.244 -70.776  48.002  1.00 86.23           N  
ANISOU10492  N   ASN H 157     6515   7088  19159    803   -116   1651       N  
ATOM  10493  CA  ASN H 157      83.416 -71.493  49.001  1.00 86.12           C  
ANISOU10493  CA  ASN H 157     6511   7100  19111    830    -92   1628       C  
ATOM  10494  C   ASN H 157      81.911 -71.637  48.618  1.00 85.87           C  
ANISOU10494  C   ASN H 157     6501   7119  19005    872    -48   1530       C  
ATOM  10495  O   ASN H 157      81.037 -70.908  49.079  1.00 86.07           O  
ANISOU10495  O   ASN H 157     6575   7174  18952    921   -107   1490       O  
ATOM  10496  CB  ASN H 157      83.559 -70.801  50.371  1.00 76.57           C  
ANISOU10496  CB  ASN H 157     5341   5885  17867    853   -196   1669       C  
ATOM  10497  CG  ASN H 157      84.968 -70.968  50.972  1.00 77.19           C  
ANISOU10497  CG  ASN H 157     5391   5918  18019    809   -224   1767       C  
ATOM  10498  OD1 ASN H 157      85.684 -69.986  51.255  1.00 77.54           O  
ANISOU10498  OD1 ASN H 157     5458   5942  18063    805   -316   1814       O  
ATOM  10499  ND2 ASN H 157      85.379 -72.221  51.134  1.00 77.38           N  
ANISOU10499  ND2 ASN H 157     5367   5926  18106    775   -144   1797       N  
ATOM  10500  N   ILE H 158     101.662 -69.216  40.500  1.00 78.20           N  
ANISOU10500  N   ILE H 158     5049   5544  19118    154   -153   2506       N  
ATOM  10501  CA  ILE H 158     101.196 -70.024  41.616  1.00 78.24           C  
ANISOU10501  CA  ILE H 158     5055   5559  19112    169   -130   2508       C  
ATOM  10502  C   ILE H 158     101.592 -71.488  41.397  1.00 78.32           C  
ANISOU10502  C   ILE H 158     5023   5534  19202    133    -15   2536       C  
ATOM  10503  O   ILE H 158     101.294 -72.067  40.358  1.00 78.16           O  
ANISOU10503  O   ILE H 158     4998   5500  19201    128     71   2496       O  
ATOM  10504  CB  ILE H 158      99.657 -69.899  41.797  1.00 77.94           C  
ANISOU10504  CB  ILE H 158     5062   5563  18988    226   -129   2419       C  
ATOM  10505  CG1 ILE H 158      99.243 -68.429  41.765  1.00 77.83           C  
ANISOU10505  CG1 ILE H 158     5097   5577  18897    262   -234   2386       C  
ATOM  10506  CG2 ILE H 158      99.189 -70.574  43.091  1.00 77.99           C  
ANISOU10506  CG2 ILE H 158     5074   5584  18976    245   -122   2425       C  
ATOM  10507  CD1 ILE H 158      97.900 -68.154  42.351  1.00 77.62           C  
ANISOU10507  CD1 ILE H 158     5119   5590  18782    319   -261   2318       C  
ATOM  10508  N   LEU H 159     102.298 -72.073  42.356  1.00 78.58           N  
ANISOU10508  N   LEU H 159     5030   5550  19278    109    -15   2605       N  
ATOM  10509  CA  LEU H 159     102.744 -73.454  42.197  1.00 78.69           C  
ANISOU10509  CA  LEU H 159     5009   5524  19367     75     91   2638       C  
ATOM  10510  C   LEU H 159     101.630 -74.442  42.529  1.00 78.52           C  
ANISOU10510  C   LEU H 159     5003   5516  19315    105    164   2583       C  
ATOM  10511  O   LEU H 159     101.340 -75.395  41.771  1.00 78.40           O  
ANISOU10511  O   LEU H 159     4987   5479  19324    101    266   2552       O  
ATOM  10512  CB  LEU H 159     103.979 -73.726  43.060  1.00 79.05           C  
ANISOU10512  CB  LEU H 159     5017   5545  19474     35     66   2737       C  
ATOM  10513  CG  LEU H 159     105.207 -72.890  42.671  1.00 79.25           C  
ANISOU10513  CG  LEU H 159     5019   5557  19534      0      4   2796       C  
ATOM  10514  CD1 LEU H 159     106.357 -73.157  43.619  1.00 79.60           C  
ANISOU10514  CD1 LEU H 159     5046   5613  19586    -12    -28   2876       C  
ATOM  10515  CD2 LEU H 159     105.609 -73.137  41.240  1.00 79.18           C  
ANISOU10515  CD2 LEU H 159     5022   5548  19515      4     67   2771       C  
ATOM  10516  N   GLY H 160     100.972 -74.189  43.648  1.00 78.49           N  
ANISOU10516  N   GLY H 160     5021   5549  19254    139    110   2567       N  
ATOM  10517  CA  GLY H 160      99.869 -75.030  44.057  1.00 78.33           C  
ANISOU10517  CA  GLY H 160     5016   5548  19197    170    169   2513       C  
ATOM  10518  C   GLY H 160      98.562 -74.733  43.339  1.00 77.98           C  
ANISOU10518  C   GLY H 160     5006   5540  19082    212    188   2412       C  
ATOM  10519  O   GLY H 160      98.551 -74.251  42.203  1.00 77.85           O  
ANISOU10519  O   GLY H 160     4995   5521  19063    209    194   2382       O  
ATOM  10520  N   GLY H 161      97.462 -75.011  44.040  1.00 77.83           N  
ANISOU10520  N   GLY H 161     5011   5557  19004    252    194   2362       N  
ATOM  10521  CA  GLY H 161      96.159 -75.325  43.459  1.00 77.51           C  
ANISOU10521  CA  GLY H 161     4994   5548  18910    286    252   2268       C  
ATOM  10522  C   GLY H 161      95.066 -74.275  43.364  1.00 77.26           C  
ANISOU10522  C   GLY H 161     5004   5565  18787    335    190   2194       C  
ATOM  10523  O   GLY H 161      95.323 -73.111  43.106  1.00 77.26           O  
ANISOU10523  O   GLY H 161     5019   5570  18767    341    111   2200       O  
ATOM  10524  N   HIS H 162      93.826 -74.728  43.555  1.00 58.52           N  
ANISOU10524  N   HIS H 162     4733   5539  11963   1706   -231   2008       N  
ATOM  10525  CA  HIS H 162      92.580 -73.957  43.391  1.00 58.70           C  
ANISOU10525  CA  HIS H 162     4753   5576  11975   1708   -197   2031       C  
ATOM  10526  C   HIS H 162      92.389 -73.441  41.971  1.00 58.60           C  
ANISOU10526  C   HIS H 162     4718   5590  11959   1703   -180   2022       C  
ATOM  10527  O   HIS H 162      92.664 -72.298  41.666  1.00 58.95           O  
ANISOU10527  O   HIS H 162     4762   5640  11998   1707   -164   2017       O  
ATOM  10528  CB  HIS H 162      92.524 -72.836  44.405  1.00 59.47           C  
ANISOU10528  CB  HIS H 162     4870   5661  12065   1719   -182   2043       C  
ATOM  10529  CG  HIS H 162      92.754 -73.296  45.809  1.00 59.78           C  
ANISOU10529  CG  HIS H 162     4932   5674  12107   1725   -200   2051       C  
ATOM  10530  ND1 HIS H 162      91.799 -73.973  46.530  1.00 59.87           N  
ANISOU10530  ND1 HIS H 162     4953   5677  12117   1727   -198   2074       N  
ATOM  10531  CD2 HIS H 162      93.841 -73.211  46.619  1.00 60.03           C  
ANISOU10531  CD2 HIS H 162     4979   5687  12143   1730   -220   2039       C  
ATOM  10532  CE1 HIS H 162      92.275 -74.273  47.727  1.00 60.17           C  
ANISOU10532  CE1 HIS H 162     5013   5690  12157   1733   -216   2077       C  
ATOM  10533  NE2 HIS H 162      93.511 -73.817  47.809  1.00 60.28           N  
ANISOU10533  NE2 HIS H 162     5031   5698  12173   1735   -230   2055       N  
ATOM  10534  N   LEU H 163      92.005 -74.346  41.080  1.00 58.32           N  
ANISOU10534  N   LEU H 163     4664   5568  11928   1694   -185   2019       N  
ATOM  10535  CA  LEU H 163      91.621 -74.002  39.713  1.00 58.22           C  
ANISOU10535  CA  LEU H 163     4629   5582  11910   1690   -168   2014       C  
ATOM  10536  C   LEU H 163      90.416 -73.080  39.751  1.00 58.22           C  
ANISOU10536  C   LEU H 163     4629   5595  11896   1697   -136   2037       C  
ATOM  10537  O   LEU H 163      89.513 -73.264  40.578  1.00 58.30           O  
ANISOU10537  O   LEU H 163     4648   5599  11904   1701   -128   2059       O  
ATOM  10538  CB  LEU H 163      91.310 -75.270  38.914  1.00 58.21           C  
ANISOU10538  CB  LEU H 163     4610   5591  11917   1680   -181   2009       C  
ATOM  10539  CG  LEU H 163      90.829 -75.278  37.459  1.00 58.13           C  
ANISOU10539  CG  LEU H 163     4574   5609  11903   1673   -169   2004       C  
ATOM  10540  CD1 LEU H 163      89.374 -74.999  37.369  1.00 58.15           C  
ANISOU10540  CD1 LEU H 163     4569   5628  11897   1676   -143   2028       C  
ATOM  10541  CD2 LEU H 163      91.546 -74.304  36.615  1.00 58.03           C  
ANISOU10541  CD2 LEU H 163     4556   5608  11886   1674   -161   1986       C  
ATOM  10542  N   ASP H 164      90.371 -72.103  38.848  1.00 60.57           N  
ANISOU10542  N   ASP H 164     4917   5910  12185   1699   -116   2032       N  
ATOM  10543  CA  ASP H 164      89.291 -71.121  38.925  1.00 64.57           C  
ANISOU10543  CA  ASP H 164     5427   6430  12678   1709    -84   2054       C  
ATOM  10544  C   ASP H 164      88.133 -71.587  38.063  1.00 65.13           C  
ANISOU10544  C   ASP H 164     5476   6527  12744   1706    -73   2064       C  
ATOM  10545  O   ASP H 164      88.105 -71.392  36.841  1.00 64.98           O  
ANISOU10545  O   ASP H 164     5440   6529  12720   1703    -66   2054       O  
ATOM  10546  CB  ASP H 164      89.784 -69.740  38.466  1.00 66.54           C  
ANISOU10546  CB  ASP H 164     5680   6683  12919   1716    -66   2046       C  
ATOM  10547  CG  ASP H 164      88.689 -68.715  38.471  1.00 70.84           C  
ANISOU10547  CG  ASP H 164     6229   7240  13447   1728    -34   2068       C  
ATOM  10548  OD1 ASP H 164      87.763 -68.889  39.296  1.00 72.78           O  
ANISOU10548  OD1 ASP H 164     6482   7484  13688   1734    -26   2089       O  
ATOM  10549  OD2 ASP H 164      88.744 -67.766  37.651  1.00 72.39           O  
ANISOU10549  OD2 ASP H 164     6422   7449  13635   1734    -15   2064       O  
ATOM  10550  N   ALA H 165      87.143 -72.156  38.726  1.00 66.14           N  
ANISOU10550  N   ALA H 165     5604   6653  12872   1707    -70   2084       N  
ATOM  10551  CA  ALA H 165      86.149 -72.897  38.004  1.00 64.92           C  
ANISOU10551  CA  ALA H 165     5426   6521  12719   1701    -66   2092       C  
ATOM  10552  C   ALA H 165      85.125 -71.932  37.531  1.00 67.85           C  
ANISOU10552  C   ALA H 165     5789   6918  13073   1712    -35   2106       C  
ATOM  10553  O   ALA H 165      84.673 -71.968  36.380  1.00 67.37           O  
ANISOU10553  O   ALA H 165     5706   6884  13007   1710    -27   2103       O  
ATOM  10554  CB  ALA H 165      85.546 -73.942  38.882  1.00 63.87           C  
ANISOU10554  CB  ALA H 165     5295   6376  12597   1698    -75   2108       C  
ATOM  10555  N   LYS H 166      84.757 -71.079  38.480  1.00 70.68           N  
ANISOU10555  N   LYS H 166     6166   7269  13422   1725    -18   2123       N  
ATOM  10556  CA  LYS H 166      83.650 -70.126  38.377  1.00 74.74           C  
ANISOU10556  CA  LYS H 166     6677   7803  13918   1739     13   2142       C  
ATOM  10557  C   LYS H 166      83.970 -68.749  37.787  1.00 76.36           C  
ANISOU10557  C   LYS H 166     6890   8017  14108   1750     32   2135       C  
ATOM  10558  O   LYS H 166      83.081 -68.071  37.281  1.00 78.70           O  
ANISOU10558  O   LYS H 166     7179   8337  14388   1761     56   2146       O  
ATOM  10559  CB  LYS H 166      83.044 -69.952  39.772  1.00 77.77           C  
ANISOU10559  CB  LYS H 166     7078   8173  14299   1748     22   2164       C  
ATOM  10560  CG  LYS H 166      83.612 -70.962  40.793  1.00 77.02           C  
ANISOU10560  CG  LYS H 166     6995   8047  14221   1739     -4   2163       C  
ATOM  10561  CD  LYS H 166      82.575 -71.362  41.838  1.00 79.89           C  
ANISOU10561  CD  LYS H 166     7361   8406  14586   1743      3   2189       C  
ATOM  10562  CE  LYS H 166      83.175 -72.280  42.895  1.00 78.78           C  
ANISOU10562  CE  LYS H 166     7237   8233  14462   1736    -22   2189       C  
ATOM  10563  NZ  LYS H 166      82.196 -72.539  43.992  1.00 81.56           N  
ANISOU10563  NZ  LYS H 166     7595   8578  14815   1742    -12   2216       N  
ATOM  10564  N   GLY H 167      85.236 -68.347  37.842  1.00 67.34           N  
ANISOU10564  N   GLY H 167     5762   6854  12971   1747     22   2118       N  
ATOM  10565  CA  GLY H 167      85.587 -66.947  37.667  1.00 69.67           C  
ANISOU10565  CA  GLY H 167     6070   7146  13254   1759     41   2116       C  
ATOM  10566  C   GLY H 167      85.315 -66.136  38.923  1.00 72.45           C  
ANISOU10566  C   GLY H 167     6448   7481  13600   1773     56   2133       C  
ATOM  10567  O   GLY H 167      84.706 -65.093  38.841  1.00 75.67           O  
ANISOU10567  O   GLY H 167     6862   7897  13991   1789     82   2146       O  
ATOM  10568  N   SER H 168      85.745 -66.631  40.081  1.00 67.86           N  
ANISOU10568  N   SER H 168     5881   6874  13030   1769     39   2134       N  
ATOM  10569  CA  SER H 168      85.568 -65.990  41.395  1.00 67.96           C  
ANISOU10569  CA  SER H 168     5918   6866  13036   1781     49   2150       C  
ATOM  10570  C   SER H 168      86.458 -64.765  41.627  1.00 67.95           C  
ANISOU10570  C   SER H 168     5938   6846  13034   1789     57   2142       C  
ATOM  10571  O   SER H 168      86.485 -64.193  42.726  1.00 68.03           O  
ANISOU10571  O   SER H 168     5970   6836  13041   1798     64   2152       O  
ATOM  10572  CB  SER H 168      85.806 -66.999  42.524  1.00 68.01           C  
ANISOU10572  CB  SER H 168     5933   6851  13056   1773     26   2153       C  
ATOM  10573  OG  SER H 168      84.829 -68.026  42.516  1.00 68.05           O  
ANISOU10573  OG  SER H 168     5922   6870  13064   1768     23   2166       O  
ATOM  10574  N   PHE H 169      87.260 -64.424  40.631  1.00 66.98           N  
ANISOU10574  N   PHE H 169     5807   6727  12915   1784     55   2123       N  
ATOM  10575  CA  PHE H 169      88.179 -63.311  40.776  1.00 68.38           C  
ANISOU10575  CA  PHE H 169     6002   6886  13095   1789     62   2115       C  
ATOM  10576  C   PHE H 169      88.095 -62.374  39.590  1.00 70.06           C  
ANISOU10576  C   PHE H 169     6208   7113  13299   1796     85   2112       C  
ATOM  10577  O   PHE H 169      88.985 -62.342  38.768  1.00 68.09           O  
ANISOU10577  O   PHE H 169     5948   6864  13058   1788     76   2093       O  
ATOM  10578  CB  PHE H 169      89.597 -63.866  40.969  1.00 65.02           C  
ANISOU10578  CB  PHE H 169     5575   6441  12690   1775     32   2092       C  
ATOM  10579  CG  PHE H 169      89.740 -64.655  42.236  1.00 64.12           C  
ANISOU10579  CG  PHE H 169     5471   6308  12583   1772     11   2096       C  
ATOM  10580  CD1 PHE H 169      90.227 -64.045  43.387  1.00 66.16           C  
ANISOU10580  CD1 PHE H 169     5752   6540  12844   1779     11   2099       C  
ATOM  10581  CD2 PHE H 169      89.310 -65.982  42.300  1.00 62.28           C  
ANISOU10581  CD2 PHE H 169     5226   6083  12354   1763     -7   2098       C  
ATOM  10582  CE1 PHE H 169      90.308 -64.747  44.571  1.00 65.51           C  
ANISOU10582  CE1 PHE H 169     5681   6441  12767   1777     -8   2104       C  
ATOM  10583  CE2 PHE H 169      89.383 -66.691  43.479  1.00 61.92           C  
ANISOU10583  CE2 PHE H 169     5193   6019  12314   1761    -25   2104       C  
ATOM  10584  CZ  PHE H 169      89.887 -66.078  44.620  1.00 63.10           C  
ANISOU10584  CZ  PHE H 169     5366   6143  12466   1769    -26   2107       C  
ATOM  10585  N   PRO H 170      86.994 -61.619  39.491  1.00 66.47           N  
ANISOU10585  N   PRO H 170     5759   6672  12824   1813    113   2131       N  
ATOM  10586  CA  PRO H 170      86.648 -60.813  38.316  1.00 67.30           C  
ANISOU10586  CA  PRO H 170     5858   6796  12917   1822    136   2133       C  
ATOM  10587  C   PRO H 170      87.524 -59.596  38.158  1.00 68.56           C  
ANISOU10587  C   PRO H 170     6034   6936  13080   1829    149   2125       C  
ATOM  10588  O   PRO H 170      87.599 -59.049  37.067  1.00 68.89           O  
ANISOU10588  O   PRO H 170     6070   6989  13117   1833    162   2121       O  
ATOM  10589  CB  PRO H 170      85.205 -60.400  38.590  1.00 69.17           C  
ANISOU10589  CB  PRO H 170     6100   7050  13133   1841    161   2157       C  
ATOM  10590  CG  PRO H 170      84.722 -61.352  39.648  1.00 68.57           C  
ANISOU10590  CG  PRO H 170     6022   6970  13060   1835    147   2167       C  
ATOM  10591  CD  PRO H 170      85.926 -61.541  40.497  1.00 67.75           C  
ANISOU10591  CD  PRO H 170     5933   6834  12976   1825    126   2155       C  
ATOM  10592  N   TRP H 171      88.182 -59.205  39.244  1.00 65.76           N  
ANISOU10592  N   TRP H 171     5699   6551  12735   1830    145   2125       N  
ATOM  10593  CA  TRP H 171      89.125 -58.092  39.264  1.00 67.78           C  
ANISOU10593  CA  TRP H 171     5971   6783  12999   1834    156   2118       C  
ATOM  10594  C   TRP H 171      90.564 -58.473  38.847  1.00 65.09           C  
ANISOU10594  C   TRP H 171     5618   6432  12683   1816    132   2091       C  
ATOM  10595  O   TRP H 171      91.462 -57.653  38.918  1.00 66.46           O  
ANISOU10595  O   TRP H 171     5801   6583  12868   1817    137   2084       O  
ATOM  10596  CB  TRP H 171      89.155 -57.477  40.665  1.00 70.58           C  
ANISOU10596  CB  TRP H 171     6354   7109  13354   1844    163   2129       C  
ATOM  10597  CG  TRP H 171      89.496 -58.456  41.741  1.00 68.65           C  
ANISOU10597  CG  TRP H 171     6110   6853  13121   1833    135   2125       C  
ATOM  10598  CD1 TRP H 171      90.742 -58.921  42.069  1.00 66.56           C  
ANISOU10598  CD1 TRP H 171     5841   6571  12878   1818    108   2106       C  
ATOM  10599  CD2 TRP H 171      88.575 -59.100  42.635  1.00 68.65           C  
ANISOU10599  CD2 TRP H 171     6114   6858  13113   1836    131   2141       C  
ATOM  10600  NE1 TRP H 171      90.650 -59.816  43.109  1.00 65.28           N  
ANISOU10600  NE1 TRP H 171     5682   6402  12719   1814     87   2109       N  
ATOM  10601  CE2 TRP H 171      89.333 -59.944  43.477  1.00 66.52           C  
ANISOU10601  CE2 TRP H 171     5844   6571  12858   1824    101   2131       C  
ATOM  10602  CE3 TRP H 171      87.183 -59.049  42.805  1.00 70.32           C  
ANISOU10602  CE3 TRP H 171     6327   7086  13304   1849    151   2164       C  
ATOM  10603  CZ2 TRP H 171      88.741 -60.729  44.479  1.00 66.02           C  
ANISOU10603  CZ2 TRP H 171     5787   6506  12793   1823     91   2144       C  
ATOM  10604  CZ3 TRP H 171      86.605 -59.819  43.797  1.00 69.82           C  
ANISOU10604  CZ3 TRP H 171     6267   7022  13240   1848    141   2176       C  
ATOM  10605  CH2 TRP H 171      87.382 -60.652  44.619  1.00 67.68           C  
ANISOU10605  CH2 TRP H 171     5999   6732  12985   1835    111   2166       C  
ATOM  10606  N   GLN H 172      90.791 -59.717  38.444  1.00 71.55           N  
ANISOU10606  N   GLN H 172     6413   7264  13508   1800    105   2078       N  
ATOM  10607  CA  GLN H 172      92.115 -60.175  38.054  1.00 68.43           C  
ANISOU10607  CA  GLN H 172     6004   6863  13135   1784     81   2053       C  
ATOM  10608  C   GLN H 172      92.457 -59.914  36.581  1.00 68.05           C  
ANISOU10608  C   GLN H 172     5939   6830  13088   1780     88   2040       C  
ATOM  10609  O   GLN H 172      91.761 -60.391  35.687  1.00 67.37           O  
ANISOU10609  O   GLN H 172     5837   6769  12990   1779     91   2042       O  
ATOM  10610  CB  GLN H 172      92.244 -61.664  38.332  1.00 64.78           C  
ANISOU10610  CB  GLN H 172     5527   6406  12679   1770     49   2043       C  
ATOM  10611  CG  GLN H 172      93.521 -62.247  37.767  1.00 62.28           C  
ANISOU10611  CG  GLN H 172     5194   6089  12382   1755     23   2016       C  
ATOM  10612  CD  GLN H 172      94.743 -61.660  38.428  1.00 62.52           C  
ANISOU10612  CD  GLN H 172     5233   6092  12430   1754     16   2004       C  
ATOM  10613  OE1 GLN H 172      95.070 -62.004  39.565  1.00 62.52           O  
ANISOU10613  OE1 GLN H 172     5243   6075  12436   1753     -1   2004       O  
ATOM  10614  NE2 GLN H 172      95.413 -60.747  37.734  1.00 63.39           N  
ANISOU10614  NE2 GLN H 172     5339   6197  12548   1755     29   1995       N  
ATOM  10615  N   ALA H 173      93.539 -59.177  36.331  1.00 67.11           N  
ANISOU10615  N   ALA H 173     5821   6694  12983   1778     92   2027       N  
ATOM  10616  CA  ALA H 173      93.981 -58.936  34.964  1.00 67.06           C  
ANISOU10616  CA  ALA H 173     5798   6700  12982   1774     98   2015       C  
ATOM  10617  C   ALA H 173      95.340 -59.565  34.643  1.00 67.02           C  
ANISOU10617  C   ALA H 173     5773   6691  13000   1757     70   1987       C  
ATOM  10618  O   ALA H 173      96.276 -59.562  35.447  1.00 67.07           O  
ANISOU10618  O   ALA H 173     5783   6676  13023   1752     55   1976       O  
ATOM  10619  CB  ALA H 173      94.032 -57.470  34.685  1.00 67.14           C  
ANISOU10619  CB  ALA H 173     5824   6696  12990   1788    130   2023       C  
ATOM  10620  N   LYS H 174      95.416 -60.095  33.431  1.00 76.11           N  
ANISOU10620  N   LYS H 174     6904   7865  14151   1749     65   1976       N  
ATOM  10621  CA  LYS H 174      96.599 -60.739  32.909  1.00 72.92           C  
ANISOU10621  CA  LYS H 174     6478   7462  13766   1733     40   1949       C  
ATOM  10622  C   LYS H 174      97.209 -59.834  31.872  1.00 75.10           C  
ANISOU10622  C   LYS H 174     6747   7738  14051   1734     58   1941       C  
ATOM  10623  O   LYS H 174      96.634 -59.650  30.804  1.00 76.13           O  
ANISOU10623  O   LYS H 174     6871   7886  14168   1738     74   1946       O  
ATOM  10624  CB  LYS H 174      96.242 -62.098  32.296  1.00 69.37           C  
ANISOU10624  CB  LYS H 174     6009   7037  13310   1723     20   1941       C  
ATOM  10625  CG  LYS H 174      97.302 -62.687  31.391  1.00 66.26           C  
ANISOU10625  CG  LYS H 174     5592   6652  12932   1710      0   1915       C  
ATOM  10626  CD  LYS H 174      96.845 -64.017  30.807  1.00 63.47           C  
ANISOU10626  CD  LYS H 174     5224   6322  12571   1701    -18   1909       C  
ATOM  10627  CE  LYS H 174      97.887 -64.582  29.825  1.00 60.65           C  
ANISOU10627  CE  LYS H 174     4843   5974  12227   1689    -36   1882       C  
ATOM  10628  NZ  LYS H 174      97.326 -65.707  29.031  1.00 58.24           N  
ANISOU10628  NZ  LYS H 174     4522   5692  11913   1682    -47   1878       N  
ATOM  10629  N   MET H 175      98.369 -59.271  32.188  1.00 71.29           N  
ANISOU10629  N   MET H 175     6264   7234  13590   1731     55   1929       N  
ATOM  10630  CA  MET H 175      99.061 -58.355  31.287  1.00 73.77           C  
ANISOU10630  CA  MET H 175     6570   7542  13917   1731     73   1921       C  
ATOM  10631  C   MET H 175     100.329 -58.989  30.735  1.00 71.10           C  
ANISOU10631  C   MET H 175     6205   7209  13601   1715     49   1892       C  
ATOM  10632  O   MET H 175     101.156 -59.526  31.497  1.00 68.97           O  
ANISOU10632  O   MET H 175     5929   6931  13347   1707     23   1877       O  
ATOM  10633  CB  MET H 175      99.395 -57.055  32.014  1.00 77.75           C  
ANISOU10633  CB  MET H 175     7094   8015  14432   1741     94   1930       C  
ATOM  10634  CG  MET H 175     100.313 -56.147  31.261  1.00 80.23           C  
ANISOU10634  CG  MET H 175     7399   8317  14766   1739    110   1920       C  
ATOM  10635  SD  MET H 175     100.745 -54.699  32.253  1.00 85.18           S  
ANISOU10635  SD  MET H 175     8069   8915  15382   1733    134   1919       S  
ATOM  10636  CE  MET H 175     100.995 -55.397  33.881  1.00 82.84           C  
ANISOU10636  CE  MET H 175     7781   8608  15087   1727    104   1913       C  
ATOM  10637  N   VAL H 176     100.499 -58.938  29.416  1.00 77.74           N  
ANISOU10637  N   VAL H 176     7029   8065  14442   1712     57   1884       N  
ATOM  10638  CA  VAL H 176     101.713 -59.507  28.822  1.00 75.43           C  
ANISOU10638  CA  VAL H 176     6709   7780  14170   1697     35   1856       C  
ATOM  10639  C   VAL H 176     102.594 -58.385  28.259  1.00 78.76           C  
ANISOU10639  C   VAL H 176     7124   8188  14613   1698     56   1849       C  
ATOM  10640  O   VAL H 176     102.133 -57.485  27.545  1.00 82.23           O  
ANISOU10640  O   VAL H 176     7572   8627  15045   1707     86   1863       O  
ATOM  10641  CB  VAL H 176     101.362 -60.579  27.740  1.00 72.56           C  
ANISOU10641  CB  VAL H 176     6329   7448  13794   1690     23   1847       C  
ATOM  10642  CG1 VAL H 176      99.905 -61.059  27.917  1.00 71.65           C  
ANISOU10642  CG1 VAL H 176     6226   7345  13651   1697     26   1868       C  
ATOM  10643  CG2 VAL H 176     101.581 -60.079  26.325  1.00 74.76           C  
ANISOU10643  CG2 VAL H 176     6593   7737  14075   1690     41   1842       C  
ATOM  10644  N   SER H 177     103.864 -58.416  28.628  1.00 80.35           N  
ANISOU10644  N   SER H 177     7310   8377  14841   1689     39   1828       N  
ATOM  10645  CA  SER H 177     104.806 -57.408  28.151  1.00 84.02           C  
ANISOU10645  CA  SER H 177     7773   8832  15317   1679     57   1814       C  
ATOM  10646  C   SER H 177     105.135 -57.647  26.676  1.00 83.70           C  
ANISOU10646  C   SER H 177     7704   8810  15288   1677     60   1804       C  
ATOM  10647  O   SER H 177     104.543 -58.514  26.040  1.00 80.84           O  
ANISOU10647  O   SER H 177     7333   8470  14911   1678     50   1805       O  
ATOM  10648  CB  SER H 177     106.074 -57.392  29.017  1.00 82.89           C  
ANISOU10648  CB  SER H 177     7633   8681  15179   1658     39   1786       C  
ATOM  10649  OG  SER H 177     105.885 -56.504  30.120  1.00 85.68           O  
ANISOU10649  OG  SER H 177     8024   9015  15515   1656     54   1794       O  
ATOM  10650  N   HIS H 178     106.040 -56.855  26.114  1.00 87.89           N  
ANISOU10650  N   HIS H 178     8237   9340  15818   1660     75   1785       N  
ATOM  10651  CA  HIS H 178     106.209 -56.900  24.669  1.00 88.84           C  
ANISOU10651  CA  HIS H 178     8335   9475  15945   1659     84   1779       C  
ATOM  10652  C   HIS H 178     106.697 -58.255  24.219  1.00 83.43           C  
ANISOU10652  C   HIS H 178     7609   8809  15282   1658     50   1762       C  
ATOM  10653  O   HIS H 178     106.280 -58.743  23.176  1.00 82.48           O  
ANISOU10653  O   HIS H 178     7479   8710  15148   1658     50   1762       O  
ATOM  10654  CB  HIS H 178     107.175 -55.827  24.169  1.00 93.33           C  
ANISOU10654  CB  HIS H 178     8914  10039  16509   1638    107   1759       C  
ATOM  10655  CG  HIS H 178     107.108 -55.627  22.687  1.00 95.81           C  
ANISOU10655  CG  HIS H 178     9214  10366  16824   1641    125   1761       C  
ATOM  10656  ND1 HIS H 178     107.728 -56.477  21.794  1.00 92.58           N  
ANISOU10656  ND1 HIS H 178     8768   9977  16433   1635    106   1742       N  
ATOM  10657  CD2 HIS H 178     106.457 -54.701  21.939  1.00101.38           C  
ANISOU10657  CD2 HIS H 178     9939  11068  17514   1650    160   1779       C  
ATOM  10658  CE1 HIS H 178     107.477 -56.071  20.561  1.00 96.10           C  
ANISOU10658  CE1 HIS H 178     9210  10431  16874   1640    128   1748       C  
ATOM  10659  NE2 HIS H 178     106.710 -54.995  20.620  1.00101.47           N  
ANISOU10659  NE2 HIS H 178     9924  11096  17533   1649    161   1771       N  
ATOM  10660  N   HIS H 179     107.583 -58.840  25.020  1.00 86.08           N  
ANISOU10660  N   HIS H 179     7936   9144  15628   1647     21   1740       N  
ATOM  10661  CA  HIS H 179     108.214 -60.135  24.750  1.00 81.10           C  
ANISOU10661  CA  HIS H 179     7276   8532  15007   1640    -14   1717       C  
ATOM  10662  C   HIS H 179     107.548 -61.359  25.403  1.00 76.35           C  
ANISOU10662  C   HIS H 179     6686   7940  14383   1640    -41   1719       C  
ATOM  10663  O   HIS H 179     108.263 -62.152  26.031  1.00 73.39           O  
ANISOU10663  O   HIS H 179     6301   7566  14017   1635    -71   1701       O  
ATOM  10664  CB  HIS H 179     109.723 -60.122  25.041  1.00 80.61           C  
ANISOU10664  CB  HIS H 179     7195   8468  14964   1624    -30   1684       C  
ATOM  10665  CG  HIS H 179     110.104 -59.767  26.440  1.00 80.79           C  
ANISOU10665  CG  HIS H 179     7242   8476  14980   1616    -37   1678       C  
ATOM  10666  ND1 HIS H 179     109.204 -59.317  27.379  1.00 81.63           N  
ANISOU10666  ND1 HIS H 179     7380   8565  15071   1625    -25   1703       N  
ATOM  10667  CD2 HIS H 179     111.313 -59.783  27.050  1.00 80.55           C  
ANISOU10667  CD2 HIS H 179     7206   8447  14954   1599    -54   1649       C  
ATOM  10668  CE1 HIS H 179     109.843 -59.084  28.514  1.00 81.98           C  
ANISOU10668  CE1 HIS H 179     7439   8599  15111   1614    -35   1689       C  
ATOM  10669  NE2 HIS H 179     111.122 -59.357  28.339  1.00 81.25           N  
ANISOU10669  NE2 HIS H 179     7323   8517  15030   1598    -53   1657       N  
ATOM  10670  N   ASN H 180     106.217 -61.383  25.492  1.00 83.86           N  
ANISOU10670  N   ASN H 180     7661   8894  15309   1649    -29   1744       N  
ATOM  10671  CA  ASN H 180     105.484 -62.612  25.832  1.00 79.26           C  
ANISOU10671  CA  ASN H 180     7086   8324  14706   1648    -51   1747       C  
ATOM  10672  C   ASN H 180     105.710 -63.022  27.286  1.00 76.77           C  
ANISOU10672  C   ASN H 180     6781   7994  14395   1649    -73   1746       C  
ATOM  10673  O   ASN H 180     105.600 -64.205  27.642  1.00 72.35           O  
ANISOU10673  O   ASN H 180     6221   7442  13828   1646   -100   1740       O  
ATOM  10674  CB  ASN H 180     105.893 -63.764  24.890  1.00 75.58           C  
ANISOU10674  CB  ASN H 180     6597   7882  14239   1639    -73   1725       C  
ATOM  10675  CG  ASN H 180     104.725 -64.698  24.505  1.00 72.75           C  
ANISOU10675  CG  ASN H 180     6246   7541  13854   1640    -78   1736       C  
ATOM  10676  OD1 ASN H 180     103.549 -64.324  24.541  1.00 74.54           O  
ANISOU10676  OD1 ASN H 180     6490   7769  14064   1648    -59   1760       O  
ATOM  10677  ND2 ASN H 180     105.079 -65.925  24.115  1.00 68.48           N  
ANISOU10677  ND2 ASN H 180     5690   7015  13314   1632   -105   1717       N  
ATOM  10678  N   LEU H 181     106.005 -62.032  28.127  1.00 71.90           N  
ANISOU10678  N   LEU H 181     6174   7354  13791   1654    -61   1753       N  
ATOM  10679  CA  LEU H 181     106.142 -62.277  29.559  1.00 70.34           C  
ANISOU10679  CA  LEU H 181     5989   7141  13596   1657    -79   1755       C  
ATOM  10680  C   LEU H 181     104.868 -61.922  30.310  1.00 72.26           C  
ANISOU10680  C   LEU H 181     6263   7373  13820   1668    -63   1785       C  
ATOM  10681  O   LEU H 181     104.428 -60.767  30.310  1.00 76.99           O  
ANISOU10681  O   LEU H 181     6876   7960  14417   1676    -33   1803       O  
ATOM  10682  CB  LEU H 181     107.316 -61.504  30.134  1.00 72.54           C  
ANISOU10682  CB  LEU H 181     6258   7400  13902   1656    -80   1742       C  
ATOM  10683  CG  LEU H 181     108.658 -62.237  30.106  1.00 68.95           C  
ANISOU10683  CG  LEU H 181     5775   6954  13467   1647   -112   1710       C  
ATOM  10684  CD1 LEU H 181     109.653 -61.555  31.024  1.00 69.19           C  
ANISOU10684  CD1 LEU H 181     5814   6972  13503   1637   -115   1693       C  
ATOM  10685  CD2 LEU H 181     108.463 -63.643  30.534  1.00 66.50           C  
ANISOU10685  CD2 LEU H 181     5469   6656  13143   1646   -144   1704       C  
ATOM  10686  N   THR H 182     104.270 -62.926  30.944  1.00 67.30           N  
ANISOU10686  N   THR H 182     5644   6750  13176   1669    -82   1791       N  
ATOM  10687  CA  THR H 182     102.946 -62.775  31.537  1.00 68.68           C  
ANISOU10687  CA  THR H 182     5845   6921  13331   1678    -68   1819       C  
ATOM  10688  C   THR H 182     103.026 -62.218  32.957  1.00 70.67           C  
ANISOU10688  C   THR H 182     6116   7147  13588   1685    -67   1829       C  
ATOM  10689  O   THR H 182     103.849 -62.654  33.756  1.00 68.22           O  
ANISOU10689  O   THR H 182     5802   6828  13291   1682    -92   1815       O  
ATOM  10690  CB  THR H 182     102.225 -64.116  31.512  1.00 64.31           C  
ANISOU10690  CB  THR H 182     5291   6384  12761   1675    -87   1821       C  
ATOM  10691  OG1 THR H 182     101.929 -64.455  30.151  1.00 63.50           O  
ANISOU10691  OG1 THR H 182     5173   6303  12650   1670    -81   1816       O  
ATOM  10692  CG2 THR H 182     100.948 -64.072  32.319  1.00 65.44           C  
ANISOU10692  CG2 THR H 182     5459   6522  12885   1684    -76   1848       C  
ATOM  10693  N   THR H 183     102.182 -61.241  33.262  1.00 63.36           N  
ANISOU10693  N   THR H 183     5212   6211  12652   1696    -38   1853       N  
ATOM  10694  CA  THR H 183     102.299 -60.498  34.520  1.00 66.14           C  
ANISOU10694  CA  THR H 183     5583   6536  13010   1703    -32   1863       C  
ATOM  10695  C   THR H 183     100.937 -60.007  35.022  1.00 69.39           C  
ANISOU10695  C   THR H 183     6022   6943  13399   1716     -8   1893       C  
ATOM  10696  O   THR H 183     100.039 -59.775  34.229  1.00 70.86           O  
ANISOU10696  O   THR H 183     6211   7143  13568   1721     13   1907       O  
ATOM  10697  CB  THR H 183     103.250 -59.272  34.376  1.00 70.04           C  
ANISOU10697  CB  THR H 183     6074   7013  13524   1702    -15   1854       C  
ATOM  10698  OG1 THR H 183     103.060 -58.639  33.097  1.00 73.09           O  
ANISOU10698  OG1 THR H 183     6452   7408  13910   1704     10   1858       O  
ATOM  10699  CG2 THR H 183     104.709 -59.691  34.542  1.00 66.97           C  
ANISOU10699  CG2 THR H 183     5670   6627  13150   1685    -43   1820       C  
ATOM  10700  N   GLY H 184     100.797 -59.841  36.335  1.00 61.56           N  
ANISOU10700  N   GLY H 184     5050   5933  12407   1722    -12   1904       N  
ATOM  10701  CA  GLY H 184      99.517 -59.513  36.941  1.00 64.13           C  
ANISOU10701  CA  GLY H 184     5401   6255  12711   1735      8   1931       C  
ATOM  10702  C   GLY H 184      99.192 -58.050  37.192  1.00 70.39           C  
ANISOU10702  C   GLY H 184     6215   7028  13501   1748     42   1949       C  
ATOM  10703  O   GLY H 184     100.079 -57.217  37.378  1.00 73.13           O  
ANISOU10703  O   GLY H 184     6574   7362  13851   1738     49   1934       O  
ATOM  10704  N   ALA H 185      97.893 -57.747  37.183  1.00 62.86           N  
ANISOU10704  N   ALA H 185     5279   6082  12524   1759     65   1973       N  
ATOM  10705  CA  ALA H 185      97.354 -56.417  37.491  1.00 68.95           C  
ANISOU10705  CA  ALA H 185     6075   6836  13287   1776     99   1993       C  
ATOM  10706  C   ALA H 185      95.922 -56.556  38.002  1.00 70.17           C  
ANISOU10706  C   ALA H 185     6248   6999  13414   1787    110   2017       C  
ATOM  10707  O   ALA H 185      95.182 -57.446  37.572  1.00 67.22           O  
ANISOU10707  O   ALA H 185     5863   6652  13027   1784    102   2020       O  
ATOM  10708  CB  ALA H 185      97.395 -55.528  36.273  1.00 71.81           C  
ANISOU10708  CB  ALA H 185     6434   7201  13649   1780    126   1994       C  
ATOM  10709  N   THR H 186      95.504 -55.691  38.912  1.00 65.35           N  
ANISOU10709  N   THR H 186     5664   6369  12798   1801    130   2035       N  
ATOM  10710  CA  THR H 186      94.151 -55.837  39.417  1.00 65.36           C  
ANISOU10710  CA  THR H 186     5679   6380  12773   1813    141   2057       C  
ATOM  10711  C   THR H 186      93.292 -54.574  39.233  1.00 65.44           C  
ANISOU10711  C   THR H 186     5712   6386  12765   1834    180   2079       C  
ATOM  10712  O   THR H 186      93.767 -53.454  39.299  1.00 65.66           O  
ANISOU10712  O   THR H 186     5760   6393  12795   1837    199   2077       O  
ATOM  10713  CB  THR H 186      94.161 -56.264  40.892  1.00 65.41           C  
ANISOU10713  CB  THR H 186     5699   6371  12782   1813    124   2062       C  
ATOM  10714  OG1 THR H 186      94.670 -55.206  41.700  1.00 65.53           O  
ANISOU10714  OG1 THR H 186     5745   6361  12792   1812    137   2058       O  
ATOM  10715  CG2 THR H 186      95.022 -57.482  41.065  1.00 65.34           C  
ANISOU10715  CG2 THR H 186     5671   6366  12791   1795     85   2041       C  
ATOM  10716  N   LEU H 187      92.001 -54.785  39.017  1.00 64.84           N  
ANISOU10716  N   LEU H 187     5637   6334  12664   1844    191   2096       N  
ATOM  10717  CA  LEU H 187      91.100 -53.726  38.589  1.00 65.55           C  
ANISOU10717  CA  LEU H 187     5744   6428  12733   1864    227   2114       C  
ATOM  10718  C   LEU H 187      90.475 -53.029  39.769  1.00 67.09           C  
ANISOU10718  C   LEU H 187     5969   6606  12916   1881    245   2134       C  
ATOM  10719  O   LEU H 187      89.640 -53.604  40.472  1.00 66.39           O  
ANISOU10719  O   LEU H 187     5882   6528  12815   1885    239   2146       O  
ATOM  10720  CB  LEU H 187      90.011 -54.308  37.707  1.00 65.25           C  
ANISOU10720  CB  LEU H 187     5689   6428  12674   1868    230   2121       C  
ATOM  10721  CG  LEU H 187      88.884 -53.423  37.233  1.00 66.30           C  
ANISOU10721  CG  LEU H 187     5835   6574  12781   1891    264   2142       C  
ATOM  10722  CD1 LEU H 187      89.317 -52.647  36.034  1.00 67.88           C  
ANISOU10722  CD1 LEU H 187     6034   6774  12983   1896    281   2136       C  
ATOM  10723  CD2 LEU H 187      87.733 -54.318  36.872  1.00 65.58           C  
ANISOU10723  CD2 LEU H 187     5725   6520  12672   1892    258   2149       C  
ATOM  10724  N   ILE H 188      90.900 -51.786  39.973  1.00 65.24           N  
ANISOU10724  N   ILE H 188     5759   6342  12687   1892    267   2138       N  
ATOM  10725  CA  ILE H 188      90.506 -51.003  41.124  1.00 66.01           C  
ANISOU10725  CA  ILE H 188     5893   6421  12766   1902    285   2150       C  
ATOM  10726  C   ILE H 188      89.225 -50.124  40.924  1.00 69.67           C  
ANISOU10726  C   ILE H 188     6374   6891  13206   1933    321   2177       C  
ATOM  10727  O   ILE H 188      88.534 -49.762  41.895  1.00 73.18           O  
ANISOU10727  O   ILE H 188     6843   7329  13633   1946    333   2191       O  
ATOM  10728  CB  ILE H 188      91.716 -50.172  41.522  1.00 66.85           C  
ANISOU10728  CB  ILE H 188     6029   6500  12870   1883    288   2128       C  
ATOM  10729  CG1 ILE H 188      91.493 -49.396  42.809  1.00 72.00           C  
ANISOU10729  CG1 ILE H 188     6724   7132  13502   1887    303   2134       C  
ATOM  10730  CG2 ILE H 188      92.132 -49.238  40.372  1.00 69.42           C  
ANISOU10730  CG2 ILE H 188     6360   6822  13194   1883    311   2121       C  
ATOM  10731  CD1 ILE H 188      92.450 -48.210  42.948  1.00 76.06           C  
ANISOU10731  CD1 ILE H 188     7272   7619  14007   1873    320   2117       C  
ATOM  10732  N   ASN H 189      88.877 -49.834  39.670  1.00 67.73           N  
ANISOU10732  N   ASN H 189     6119   6664  12953   1942    336   2180       N  
ATOM  10733  CA  ASN H 189      87.550 -49.269  39.321  1.00 69.30           C  
ANISOU10733  CA  ASN H 189     6329   6882  13119   1967    364   2200       C  
ATOM  10734  C   ASN H 189      87.281 -49.397  37.824  1.00 68.11           C  
ANISOU10734  C   ASN H 189     6158   6762  12960   1969    369   2197       C  
ATOM  10735  O   ASN H 189      88.024 -50.067  37.125  1.00 67.34           O  
ANISOU10735  O   ASN H 189     6036   6672  12880   1949    348   2179       O  
ATOM  10736  CB  ASN H 189      87.380 -47.804  39.782  1.00 76.31           C  
ANISOU10736  CB  ASN H 189     7257   7740  13997   1992    399   2216       C  
ATOM  10737  CG  ASN H 189      88.222 -46.786  38.989  1.00 78.92           C  
ANISOU10737  CG  ASN H 189     7605   8051  14330   1988    417   2205       C  
ATOM  10738  OD1 ASN H 189      88.468 -46.920  37.787  1.00 76.84           O  
ANISOU10738  OD1 ASN H 189     7319   7799  14076   1987    416   2200       O  
ATOM  10739  ND2 ASN H 189      88.636 -45.732  39.684  1.00 84.05           N  
ANISOU10739  ND2 ASN H 189     8299   8671  14965   1984    435   2200       N  
ATOM  10740  N   GLU H 190      86.232 -48.764  37.324  1.00 73.58           N  
ANISOU10740  N   GLU H 190     6524   6825  14609   1240   1683   3328       N  
ATOM  10741  CA  GLU H 190      85.830 -49.022  35.948  1.00 73.29           C  
ANISOU10741  CA  GLU H 190     6446   6805  14596   1249   1665   3328       C  
ATOM  10742  C   GLU H 190      86.906 -48.662  34.913  1.00 73.04           C  
ANISOU10742  C   GLU H 190     6412   6789  14550   1234   1643   3303       C  
ATOM  10743  O   GLU H 190      86.899 -49.196  33.813  1.00 72.54           O  
ANISOU10743  O   GLU H 190     6312   6744  14506   1235   1617   3297       O  
ATOM  10744  CB  GLU H 190      84.522 -48.281  35.633  1.00 76.80           C  
ANISOU10744  CB  GLU H 190     6887   7242  15050   1273   1697   3353       C  
ATOM  10745  CG  GLU H 190      83.250 -48.920  36.244  1.00 76.84           C  
ANISOU10745  CG  GLU H 190     6876   7240  15081   1290   1711   3379       C  
ATOM  10746  CD  GLU H 190      81.947 -48.339  35.689  1.00 81.32           C  
ANISOU10746  CD  GLU H 190     7429   7805  15662   1315   1736   3401       C  
ATOM  10747  OE1 GLU H 190      81.373 -48.906  34.733  1.00 79.85           O  
ANISOU10747  OE1 GLU H 190     7201   7635  15503   1324   1720   3405       O  
ATOM  10748  OE2 GLU H 190      81.498 -47.303  36.214  1.00 86.48           O  
ANISOU10748  OE2 GLU H 190     8115   8443  16299   1326   1771   3414       O  
ATOM  10749  N   GLN H 191      87.764 -47.696  35.222  1.00 77.36           N  
ANISOU10749  N   GLN H 191     6999   7329  15064   1222   1655   3289       N  
ATOM  10750  CA  GLN H 191      88.822 -47.296  34.285  1.00 76.41           C  
ANISOU10750  CA  GLN H 191     6880   7224  14929   1206   1636   3263       C  
ATOM  10751  C   GLN H 191      90.267 -47.666  34.602  1.00 74.95           C  
ANISOU10751  C   GLN H 191     6705   7047  14724   1181   1610   3233       C  
ATOM  10752  O   GLN H 191      91.155 -47.456  33.761  1.00 74.29           O  
ANISOU10752  O   GLN H 191     6617   6978  14630   1167   1591   3210       O  
ATOM  10753  CB  GLN H 191      88.781 -45.785  34.086  1.00 82.57           C  
ANISOU10753  CB  GLN H 191     7696   7993  15684   1210   1668   3265       C  
ATOM  10754  CG  GLN H 191      88.691 -45.370  32.632  1.00 87.09           C  
ANISOU10754  CG  GLN H 191     8250   8579  16263   1215   1660   3261       C  
ATOM  10755  CD  GLN H 191      87.750 -44.193  32.418  1.00 92.54           C  
ANISOU10755  CD  GLN H 191     8959   9255  16947   1235   1697   3282       C  
ATOM  10756  OE1 GLN H 191      86.935 -43.852  33.286  1.00 94.08           O  
ANISOU10756  OE1 GLN H 191     9173   9433  17142   1250   1728   3303       O  
ATOM  10757  NE2 GLN H 191      87.865 -43.566  31.254  1.00 95.56           N  
ANISOU10757  NE2 GLN H 191     9339   9646  17325   1237   1695   3275       N  
ATOM  10758  N   TRP H 192      90.527 -48.205  35.790  1.00 74.57           N  
ANISOU10758  N   TRP H 192     6672   6992  14671   1175   1609   3233       N  
ATOM  10759  CA  TRP H 192      91.917 -48.305  36.250  1.00 72.52           C  
ANISOU10759  CA  TRP H 192     6431   6737  14386   1151   1591   3204       C  
ATOM  10760  C   TRP H 192      92.255 -49.639  36.874  1.00 66.39           C  
ANISOU10760  C   TRP H 192     5639   5966  13622   1145   1563   3198       C  
ATOM  10761  O   TRP H 192      91.388 -50.316  37.449  1.00 66.18           O  
ANISOU10761  O   TRP H 192     5602   5930  13615   1158   1569   3219       O  
ATOM  10762  CB  TRP H 192      92.244 -47.214  37.277  1.00 77.53           C  
ANISOU10762  CB  TRP H 192     7117   7353  14986   1145   1624   3203       C  
ATOM  10763  CG  TRP H 192      92.073 -45.792  36.795  1.00 83.92           C  
ANISOU10763  CG  TRP H 192     7951   8155  15778   1149   1654   3207       C  
ATOM  10764  CD1 TRP H 192      90.895 -45.110  36.624  1.00 88.58           C  
ANISOU10764  CD1 TRP H 192     8546   8733  16377   1170   1685   3233       C  
ATOM  10765  CD2 TRP H 192      93.119 -44.871  36.466  1.00 86.63           C  
ANISOU10765  CD2 TRP H 192     8321   8503  16090   1131   1656   3183       C  
ATOM  10766  NE1 TRP H 192      91.153 -43.833  36.198  1.00 93.91           N  
ANISOU10766  NE1 TRP H 192     9250   9403  17028   1166   1705   3228       N  
ATOM  10767  CE2 TRP H 192      92.510 -43.663  36.090  1.00 92.88           C  
ANISOU10767  CE2 TRP H 192     9133   9283  16873   1142   1688   3197       C  
ATOM  10768  CE3 TRP H 192      94.512 -44.958  36.444  1.00 84.53           C  
ANISOU10768  CE3 TRP H 192     8063   8251  15804   1106   1633   3151       C  
ATOM  10769  CZ2 TRP H 192      93.244 -42.557  35.695  1.00 97.08           C  
ANISOU10769  CZ2 TRP H 192     9695   9816  17376   1128   1699   3180       C  
ATOM  10770  CZ3 TRP H 192      95.232 -43.862  36.054  1.00 88.75           C  
ANISOU10770  CZ3 TRP H 192     8625   8787  16310   1092   1644   3133       C  
ATOM  10771  CH2 TRP H 192      94.603 -42.681  35.685  1.00 94.96           C  
ANISOU10771  CH2 TRP H 192     9433   9561  17088   1102   1677   3148       C  
ATOM  10772  N   LEU H 193      93.536 -49.989  36.779  1.00 67.43           N  
ANISOU10772  N   LEU H 193     5770   6112  13738   1126   1534   3168       N  
ATOM  10773  CA  LEU H 193      94.072 -51.173  37.405  1.00 67.38           C  
ANISOU10773  CA  LEU H 193     5755   6111  13736   1118   1506   3157       C  
ATOM  10774  C   LEU H 193      95.407 -50.858  38.079  1.00 67.37           C  
ANISOU10774  C   LEU H 193     5786   6112  13701   1098   1500   3129       C  
ATOM  10775  O   LEU H 193      96.267 -50.191  37.500  1.00 67.32           O  
ANISOU10775  O   LEU H 193     5787   6117  13675   1084   1495   3107       O  
ATOM  10776  CB  LEU H 193      94.251 -52.271  36.377  1.00 67.24           C  
ANISOU10776  CB  LEU H 193     5690   6114  13743   1117   1465   3146       C  
ATOM  10777  CG  LEU H 193      93.104 -52.483  35.409  1.00 67.22           C  
ANISOU10777  CG  LEU H 193     5652   6116  13773   1134   1467   3168       C  
ATOM  10778  CD1 LEU H 193      93.514 -52.128  34.016  1.00 67.11           C  
ANISOU10778  CD1 LEU H 193     5618   6120  13759   1128   1451   3152       C  
ATOM  10779  CD2 LEU H 193      92.688 -53.909  35.461  1.00 67.18           C  
ANISOU10779  CD2 LEU H 193     5613   6115  13797   1140   1442   3175       C  
ATOM  10780  N   LEU H 194      95.581 -51.329  39.308  1.00 72.92           N  
ANISOU10780  N   LEU H 194     6506   6804  14396   1097   1500   3130       N  
ATOM  10781  CA  LEU H 194      96.902 -51.336  39.933  1.00 72.33           C  
ANISOU10781  CA  LEU H 194     6454   6735  14292   1079   1486   3102       C  
ATOM  10782  C   LEU H 194      97.812 -52.379  39.290  1.00 66.36           C  
ANISOU10782  C   LEU H 194     5667   6004  13543   1068   1439   3075       C  
ATOM  10783  O   LEU H 194      97.350 -53.340  38.681  1.00 65.02           O  
ANISOU10783  O   LEU H 194     5460   5843  13403   1076   1417   3083       O  
ATOM  10784  CB  LEU H 194      96.808 -51.616  41.434  1.00 72.61           C  
ANISOU10784  CB  LEU H 194     6518   6753  14318   1082   1499   3111       C  
ATOM  10785  CG  LEU H 194      96.675 -50.402  42.351  1.00 78.99           C  
ANISOU10785  CG  LEU H 194     7372   7541  15101   1081   1540   3120       C  
ATOM  10786  CD1 LEU H 194      96.497 -50.854  43.784  1.00 79.19           C  
ANISOU10786  CD1 LEU H 194     7420   7548  15121   1086   1550   3130       C  
ATOM  10787  CD2 LEU H 194      97.904 -49.552  42.250  1.00 82.74           C  
ANISOU10787  CD2 LEU H 194     7871   8025  15542   1062   1539   3090       C  
ATOM  10788  N   THR H 195      99.115 -52.163  39.428  1.00 74.15           N  
ANISOU10788  N   THR H 195     6668   7002  14502   1050   1424   3044       N  
ATOM  10789  CA  THR H 195     100.138 -53.127  39.049  1.00 68.92           C  
ANISOU10789  CA  THR H 195     5982   6363  13840   1038   1379   3015       C  
ATOM  10790  C   THR H 195     101.412 -52.706  39.763  1.00 70.10           C  
ANISOU10790  C   THR H 195     6164   6518  13954   1021   1376   2986       C  
ATOM  10791  O   THR H 195     101.376 -51.857  40.651  1.00 74.43           O  
ANISOU10791  O   THR H 195     6750   7049  14480   1019   1408   2991       O  
ATOM  10792  CB  THR H 195     100.355 -53.201  37.517  1.00 66.99           C  
ANISOU10792  CB  THR H 195     5703   6142  13610   1034   1356   3002       C  
ATOM  10793  OG1 THR H 195     101.368 -54.176  37.201  1.00 64.57           O  
ANISOU10793  OG1 THR H 195     5372   5857  13303   1023   1312   2974       O  
ATOM  10794  CG2 THR H 195     100.759 -51.846  36.982  1.00 71.87           C  
ANISOU10794  CG2 THR H 195     6341   6763  14205   1022   1377   2991       C  
ATOM  10795  N   THR H 196     102.527 -53.320  39.391  1.00 71.28           N  
ANISOU10795  N   THR H 196     6296   6691  14097   1008   1338   2954       N  
ATOM  10796  CA  THR H 196     103.811 -53.007  39.991  1.00 72.72           C  
ANISOU10796  CA  THR H 196     6504   6882  14245    991   1331   2922       C  
ATOM  10797  C   THR H 196     104.623 -52.185  39.033  1.00 75.26           C  
ANISOU10797  C   THR H 196     6824   7221  14549    973   1328   2896       C  
ATOM  10798  O   THR H 196     104.476 -52.313  37.815  1.00 73.76           O  
ANISOU10798  O   THR H 196     6604   7046  14377    973   1314   2895       O  
ATOM  10799  CB  THR H 196     104.617 -54.253  40.320  1.00 67.13           C  
ANISOU10799  CB  THR H 196     5781   6188  13536    988   1290   2901       C  
ATOM  10800  OG1 THR H 196     105.197 -54.761  39.109  1.00 63.55           O  
ANISOU10800  OG1 THR H 196     5291   5762  13093    980   1254   2879       O  
ATOM  10801  CG2 THR H 196     103.732 -55.311  40.942  1.00 63.88           C  
ANISOU10801  CG2 THR H 196     5361   5761  13150   1006   1286   2927       C  
ATOM  10802  N   ALA H 197     105.479 -51.337  39.583  1.00 73.79           N  
ANISOU10802  N   ALA H 197     6671   7036  14328    957   1341   2876       N  
ATOM  10803  CA  ALA H 197     106.459 -50.632  38.766  1.00 76.17           C  
ANISOU10803  CA  ALA H 197     6974   7359  14610    936   1334   2845       C  
ATOM  10804  C   ALA H 197     107.294 -51.625  37.987  1.00 70.70           C  
ANISOU10804  C   ALA H 197     6243   6695  13925    929   1287   2817       C  
ATOM  10805  O   ALA H 197     107.517 -51.466  36.794  1.00 70.81           O  
ANISOU10805  O   ALA H 197     6235   6725  13944    921   1275   2805       O  
ATOM  10806  CB  ALA H 197     107.352 -49.756  39.627  1.00 80.78           C  
ANISOU10806  CB  ALA H 197     7598   7941  15154    920   1352   2824       C  
ATOM  10807  N   LYS H 198     107.732 -52.663  38.679  1.00 74.95           N  
ANISOU10807  N   LYS H 198     6776   7239  14464    932   1260   2807       N  
ATOM  10808  CA  LYS H 198     108.511 -53.731  38.068  1.00 69.44           C  
ANISOU10808  CA  LYS H 198     6043   6567  13774    927   1213   2781       C  
ATOM  10809  C   LYS H 198     107.875 -54.379  36.815  1.00 66.37           C  
ANISOU10809  C   LYS H 198     5611   6187  13421    936   1194   2793       C  
ATOM  10810  O   LYS H 198     108.513 -54.391  35.758  1.00 66.07           O  
ANISOU10810  O   LYS H 198     5550   6172  13382    924   1172   2770       O  
ATOM  10811  CB  LYS H 198     108.802 -54.796  39.121  1.00 66.57           C  
ANISOU10811  CB  LYS H 198     5682   6202  13409    935   1192   2776       C  
ATOM  10812  CG  LYS H 198     110.235 -54.757  39.594  1.00 66.58           C  
ANISOU10812  CG  LYS H 198     5697   6222  13377    918   1173   2736       C  
ATOM  10813  CD  LYS H 198     110.374 -54.721  41.107  1.00 66.96           C  
ANISOU10813  CD  LYS H 198     5782   6255  13406    922   1187   2739       C  
ATOM  10814  CE  LYS H 198     111.833 -54.418  41.480  1.00 68.75           C  
ANISOU10814  CE  LYS H 198     6024   6502  13595    903   1173   2696       C  
ATOM  10815  NZ  LYS H 198     112.100 -54.425  42.945  1.00 69.90           N  
ANISOU10815  NZ  LYS H 198     6204   6634  13719    906   1183   2694       N  
ATOM  10816  N   ASN H 199     106.640 -54.894  36.914  1.00 72.62           N  
ANISOU10816  N   ASN H 199     6391   6960  14241    957   1203   2829       N  
ATOM  10817  CA  ASN H 199     105.991 -55.565  35.769  1.00 69.62           C  
ANISOU10817  CA  ASN H 199     5969   6589  13896    966   1185   2841       C  
ATOM  10818  C   ASN H 199     105.975 -54.679  34.540  1.00 73.15           C  
ANISOU10818  C   ASN H 199     6407   7045  14343    958   1194   2837       C  
ATOM  10819  O   ASN H 199     106.149 -55.148  33.405  1.00 70.81           O  
ANISOU10819  O   ASN H 199     6075   6767  14061    955   1167   2826       O  
ATOM  10820  CB  ASN H 199     104.545 -55.964  36.078  1.00 68.66           C  
ANISOU10820  CB  ASN H 199     5841   6443  13802    988   1202   2882       C  
ATOM  10821  CG  ASN H 199     104.423 -56.912  37.248  1.00 65.27           C  
ANISOU10821  CG  ASN H 199     5420   6002  13376    998   1194   2890       C  
ATOM  10822  OD1 ASN H 199     105.031 -56.692  38.290  1.00 65.77           O  
ANISOU10822  OD1 ASN H 199     5515   6060  13414    992   1200   2878       O  
ATOM  10823  ND2 ASN H 199     103.617 -57.965  37.092  1.00 62.33           N  
ANISOU10823  ND2 ASN H 199     5022   5626  13036   1012   1180   2910       N  
ATOM  10824  N   LEU H 200     105.731 -53.395  34.814  1.00 70.40           N  
ANISOU10824  N   LEU H 200     6091   6681  13976    954   1234   2846       N  
ATOM  10825  CA  LEU H 200     105.650 -52.318  33.841  1.00 71.84           C  
ANISOU10825  CA  LEU H 200     6277   6867  14153    946   1252   2844       C  
ATOM  10826  C   LEU H 200     106.964 -52.140  33.092  1.00 71.20           C  
ANISOU10826  C   LEU H 200     6187   6813  14053    924   1228   2804       C  
ATOM  10827  O   LEU H 200     106.980 -51.962  31.875  1.00 71.01           O  
ANISOU10827  O   LEU H 200     6141   6801  14037    919   1219   2798       O  
ATOM  10828  CB  LEU H 200     105.281 -51.029  34.563  1.00 76.31           C  
ANISOU10828  CB  LEU H 200     6888   7410  14698    946   1298   2859       C  
ATOM  10829  CG  LEU H 200     103.926 -50.336  34.404  1.00 80.11           C  
ANISOU10829  CG  LEU H 200     7377   7868  15194    963   1336   2896       C  
ATOM  10830  CD1 LEU H 200     102.905 -51.149  33.632  1.00 76.71           C  
ANISOU10830  CD1 LEU H 200     6905   7438  14802    982   1323   2920       C  
ATOM  10831  CD2 LEU H 200     103.406 -49.950  35.773  1.00 82.92           C  
ANISOU10831  CD2 LEU H 200     7769   8198  15539    972   1368   2917       C  
ATOM  10832  N   PHE H 201     108.063 -52.225  33.838  1.00 77.05           N  
ANISOU10832  N   PHE H 201     6945   7564  14767    910   1216   2776       N  
ATOM  10833  CA  PHE H 201     109.392 -51.940  33.334  1.00 78.00           C  
ANISOU10833  CA  PHE H 201     7063   7709  14863    886   1197   2735       C  
ATOM  10834  C   PHE H 201     110.024 -53.131  32.597  1.00 72.36           C  
ANISOU10834  C   PHE H 201     6307   7023  14163    883   1148   2712       C  
ATOM  10835  O   PHE H 201     111.199 -53.074  32.189  1.00 72.62           O  
ANISOU10835  O   PHE H 201     6335   7081  14178    864   1127   2675       O  
ATOM  10836  CB  PHE H 201     110.305 -51.526  34.491  1.00 80.08           C  
ANISOU10836  CB  PHE H 201     7363   7973  15091    872   1206   2713       C  
ATOM  10837  CG  PHE H 201     110.340 -50.048  34.758  1.00 87.40           C  
ANISOU10837  CG  PHE H 201     8330   8886  15991    861   1247   2714       C  
ATOM  10838  CD1 PHE H 201     110.842 -49.164  33.811  1.00 91.52           C  
ANISOU10838  CD1 PHE H 201     8855   9421  16499    842   1254   2695       C  
ATOM  10839  CD2 PHE H 201     109.910 -49.542  35.978  1.00 90.36           C  
ANISOU10839  CD2 PHE H 201     8742   9236  16353    868   1280   2733       C  
ATOM  10840  CE1 PHE H 201     110.886 -47.805  34.067  1.00 98.44           C  
ANISOU10840  CE1 PHE H 201     9770  10283  17348    831   1292   2696       C  
ATOM  10841  CE2 PHE H 201     109.954 -48.178  36.237  1.00 97.29           C  
ANISOU10841  CE2 PHE H 201     9659  10101  17205    857   1318   2733       C  
ATOM  10842  CZ  PHE H 201     110.444 -47.314  35.283  1.00101.31           C  
ANISOU10842  CZ  PHE H 201    10171  10622  17700    839   1324   2715       C  
ATOM  10843  N   LEU H 202     109.293 -54.230  32.458  1.00 78.94           N  
ANISOU10843  N   LEU H 202     7111   7852  15029    902   1130   2733       N  
ATOM  10844  CA  LEU H 202     109.872 -55.354  31.747  1.00 73.53           C  
ANISOU10844  CA  LEU H 202     6387   7193  14358    900   1084   2712       C  
ATOM  10845  C   LEU H 202     110.116 -54.979  30.304  1.00 75.02           C  
ANISOU10845  C   LEU H 202     6553   7400  14551    889   1075   2698       C  
ATOM  10846  O   LEU H 202     109.334 -54.264  29.707  1.00 78.47           O  
ANISOU10846  O   LEU H 202     6992   7826  14998    893   1100   2719       O  
ATOM  10847  CB  LEU H 202     108.978 -56.585  31.809  1.00 68.83           C  
ANISOU10847  CB  LEU H 202     5765   6589  13797    922   1067   2737       C  
ATOM  10848  CG  LEU H 202     108.817 -57.423  33.070  1.00 68.90           C  
ANISOU10848  CG  LEU H 202     5785   6585  13808    934   1061   2747       C  
ATOM  10849  CD1 LEU H 202     108.066 -58.649  32.642  1.00 68.82           C  
ANISOU10849  CD1 LEU H 202     5740   6575  13835    951   1038   2766       C  
ATOM  10850  CD2 LEU H 202     110.130 -57.790  33.720  1.00 68.92           C  
ANISOU10850  CD2 LEU H 202     5798   6604  13784    922   1036   2711       C  
ATOM  10851  N   ASN H 203     111.204 -55.493  29.758  1.00 80.49           N  
ANISOU10851  N   ASN H 203     7224   8122  15238    875   1039   2663       N  
ATOM  10852  CA  ASN H 203     111.635 -55.196  28.399  1.00 82.18           C  
ANISOU10852  CA  ASN H 203     7415   8356  15452    861   1026   2644       C  
ATOM  10853  C   ASN H 203     111.777 -53.691  28.140  1.00 89.22           C  
ANISOU10853  C   ASN H 203     8337   9243  16320    846   1062   2639       C  
ATOM  10854  O   ASN H 203     111.494 -53.207  27.045  1.00 91.99           O  
ANISOU10854  O   ASN H 203     8676   9597  16679    842   1068   2644       O  
ATOM  10855  CB  ASN H 203     110.690 -55.834  27.375  1.00 79.41           C  
ANISOU10855  CB  ASN H 203     7028   8006  15140    877   1014   2668       C  
ATOM  10856  CG  ASN H 203     111.340 -55.973  26.013  1.00 79.63           C  
ANISOU10856  CG  ASN H 203     7024   8061  15172    864    986   2642       C  
ATOM  10857  OD1 ASN H 203     110.896 -55.358  25.041  1.00 83.22           O  
ANISOU10857  OD1 ASN H 203     7471   8514  15634    862   1000   2651       O  
ATOM  10858  ND2 ASN H 203     112.424 -56.772  25.940  1.00 76.20           N  
ANISOU10858  ND2 ASN H 203     6570   7652  14730    854    947   2608       N  
ATOM  10859  N   HIS H 204     112.246 -52.968  29.156  1.00 80.14           N  
ANISOU10859  N   HIS H 204     7226   8085  15140    836   1084   2630       N  
ATOM  10860  CA  HIS H 204     112.456 -51.521  29.062  1.00 87.04           C  
ANISOU10860  CA  HIS H 204     8132   8952  15986    820   1119   2624       C  
ATOM  10861  C   HIS H 204     113.641 -51.054  29.922  1.00 89.24           C  
ANISOU10861  C   HIS H 204     8441   9240  16227    799   1122   2591       C  
ATOM  10862  O   HIS H 204     113.976 -51.663  30.940  1.00 86.21           O  
ANISOU10862  O   HIS H 204     8063   8856  15836    803   1110   2585       O  
ATOM  10863  CB  HIS H 204     111.184 -50.762  29.470  1.00 90.82           C  
ANISOU10863  CB  HIS H 204     8638   9398  16473    835   1163   2665       C  
ATOM  10864  CG  HIS H 204     110.152 -50.688  28.388  1.00 91.31           C  
ANISOU10864  CG  HIS H 204     8678   9453  16563    849   1169   2691       C  
ATOM  10865  ND1 HIS H 204     110.426 -50.193  27.131  1.00 93.53           N  
ANISOU10865  ND1 HIS H 204     8948   9748  16842    836   1166   2678       N  
ATOM  10866  CD2 HIS H 204     108.844 -51.036  28.378  1.00 90.13           C  
ANISOU10866  CD2 HIS H 204     8517   9284  16443    873   1179   2730       C  
ATOM  10867  CE1 HIS H 204     109.334 -50.251  26.390  1.00 93.63           C  
ANISOU10867  CE1 HIS H 204     8942   9751  16882    854   1173   2707       C  
ATOM  10868  NE2 HIS H 204     108.359 -50.757  27.123  1.00 91.60           N  
ANISOU10868  NE2 HIS H 204     8684   9475  16645    876   1181   2738       N  
ATOM  10869  N   SER H 205     114.281 -49.975  29.503  1.00 88.96           N  
ANISOU10869  N   SER H 205     8424   9212  16164    777   1138   2569       N  
ATOM  10870  CA  SER H 205     115.389 -49.437  30.272  1.00 91.73           C  
ANISOU10870  CA  SER H 205     8804   9572  16477    756   1144   2538       C  
ATOM  10871  C   SER H 205     114.909 -48.591  31.453  1.00 96.19           C  
ANISOU10871  C   SER H 205     9414  10108  17026    760   1186   2558       C  
ATOM  10872  O   SER H 205     113.797 -48.049  31.443  1.00 98.89           O  
ANISOU10872  O   SER H 205     9770  10423  17379    774   1217   2594       O  
ATOM  10873  CB  SER H 205     116.311 -48.610  29.367  1.00 96.17           C  
ANISOU10873  CB  SER H 205     9370  10155  17017    727   1146   2504       C  
ATOM  10874  OG  SER H 205     116.995 -49.443  28.436  1.00 93.15           O  
ANISOU10874  OG  SER H 205     8946   9803  16645    720   1103   2477       O  
ATOM  10875  N   GLU H 206     115.760 -48.485  32.471  1.00 92.96           N  
ANISOU10875  N   GLU H 206     9028   9705  16589    749   1186   2535       N  
ATOM  10876  CA  GLU H 206     115.498 -47.609  33.608  1.00 98.08           C  
ANISOU10876  CA  GLU H 206     9721  10328  17216    749   1225   2549       C  
ATOM  10877  C   GLU H 206     115.243 -46.195  33.116  1.00105.42           C  
ANISOU10877  C   GLU H 206    10678  11245  18130    737   1264   2555       C  
ATOM  10878  O   GLU H 206     114.550 -45.428  33.771  1.00109.72           O  
ANISOU10878  O   GLU H 206    11256  11762  18669    744   1302   2581       O  
ATOM  10879  CB  GLU H 206     116.674 -47.617  34.584  1.00 99.12           C  
ANISOU10879  CB  GLU H 206     9871  10474  17316    733   1216   2514       C  
ATOM  10880  CG  GLU H 206     117.507 -48.891  34.559  1.00 95.16           C  
ANISOU10880  CG  GLU H 206     9336  10000  16819    734   1167   2486       C  
ATOM  10881  CD  GLU H 206     118.855 -48.722  35.245  1.00 96.49           C  
ANISOU10881  CD  GLU H 206     9520  10190  16952    713   1157   2444       C  
ATOM  10882  OE1 GLU H 206     119.571 -47.742  34.929  1.00 97.98           O  
ANISOU10882  OE1 GLU H 206     9725  10389  17113    688   1172   2418       O  
ATOM  10883  OE2 GLU H 206     119.198 -49.569  36.102  1.00 96.22           O  
ANISOU10883  OE2 GLU H 206     9483  10162  16916    722   1135   2436       O  
ATOM  10884  N   ASN H 207     115.833 -45.867  31.965  1.00 94.67           N  
ANISOU10884  N   ASN H 207     9303   9904  16763    718   1254   2531       N  
ATOM  10885  CA  ASN H 207     115.615 -44.605  31.267  1.00101.22           C  
ANISOU10885  CA  ASN H 207    10155  10724  17580    706   1287   2536       C  
ATOM  10886  C   ASN H 207     114.143 -44.367  30.932  1.00101.50           C  
ANISOU10886  C   ASN H 207    10191  10732  17643    731   1311   2582       C  
ATOM  10887  O   ASN H 207     113.653 -43.228  30.987  1.00107.44           O  
ANISOU10887  O   ASN H 207    10977  11462  18382    729   1350   2598       O  
ATOM  10888  CB  ASN H 207     116.423 -44.569  29.963  1.00101.59           C  
ANISOU10888  CB  ASN H 207    10178  10799  17623    685   1265   2504       C  
ATOM  10889  CG  ASN H 207     117.834 -44.013  30.141  1.00105.90           C  
ANISOU10889  CG  ASN H 207    10742  11367  18130    652   1263   2458       C  
ATOM  10890  OD1 ASN H 207     118.088 -43.195  31.026  1.00109.68           O  
ANISOU10890  OD1 ASN H 207    11259  11834  18581    642   1292   2453       O  
ATOM  10891  ND2 ASN H 207     118.758 -44.454  29.278  1.00105.56           N  
ANISOU10891  ND2 ASN H 207    10668  11356  18085    635   1230   2423       N  
ATOM  10892  N   ALA H 208     113.454 -45.452  30.569  1.00 97.87           N  
ANISOU10892  N   ALA H 208     9694  10273  17219    753   1286   2602       N  
ATOM  10893  CA  ALA H 208     112.111 -45.369  29.993  1.00 97.51           C  
ANISOU10893  CA  ALA H 208     9640  10208  17202    775   1302   2642       C  
ATOM  10894  C   ALA H 208     111.134 -44.652  30.905  1.00101.07           C  
ANISOU10894  C   ALA H 208    10127  10625  17650    791   1344   2676       C  
ATOM  10895  O   ALA H 208     111.169 -44.802  32.126  1.00100.83           O  
ANISOU10895  O   ALA H 208    10115  10584  17610    795   1351   2680       O  
ATOM  10896  CB  ALA H 208     111.590 -46.767  29.653  1.00 90.09           C  
ANISOU10896  CB  ALA H 208     8654   9275  16300    796   1267   2656       C  
ATOM  10897  N   THR H 209     110.288 -43.835  30.295  1.00 95.57           N  
ANISOU10897  N   THR H 209     9442   9912  16960    799   1372   2700       N  
ATOM  10898  CA  THR H 209     109.220 -43.160  31.021  1.00 99.13           C  
ANISOU10898  CA  THR H 209     9924  10331  17411    816   1412   2735       C  
ATOM  10899  C   THR H 209     107.864 -43.765  30.675  1.00 95.85           C  
ANISOU10899  C   THR H 209     9482   9903  17035    847   1411   2774       C  
ATOM  10900  O   THR H 209     107.754 -44.640  29.812  1.00 91.23           O  
ANISOU10900  O   THR H 209     8855   9334  16475    853   1380   2772       O  
ATOM  10901  CB  THR H 209     109.197 -41.624  30.741  1.00106.89           C  
ANISOU10901  CB  THR H 209    10947  11299  18367    805   1452   2736       C  
ATOM  10902  OG1 THR H 209     108.295 -40.982  31.651  1.00110.37           O  
ANISOU10902  OG1 THR H 209    11422  11710  18804    821   1491   2767       O  
ATOM  10903  CG2 THR H 209     108.775 -41.328  29.312  1.00108.85           C  
ANISOU10903  CG2 THR H 209    11178  11551  18628    808   1451   2743       C  
ATOM  10904  N   ALA H 210     106.831 -43.264  31.334  1.00 99.61           N  
ANISOU10904  N   ALA H 210     9982  10351  17514    865   1445   2807       N  
ATOM  10905  CA  ALA H 210     105.509 -43.841  31.209  1.00 96.99           C  
ANISOU10905  CA  ALA H 210     9627  10006  17217    894   1447   2844       C  
ATOM  10906  C   ALA H 210     105.039 -43.878  29.755  1.00 96.25           C  
ANISOU10906  C   ALA H 210     9504   9921  17145    901   1437   2850       C  
ATOM  10907  O   ALA H 210     104.523 -44.902  29.278  1.00 90.98           O  
ANISOU10907  O   ALA H 210     8796   9262  16511    916   1412   2862       O  
ATOM  10908  CB  ALA H 210     104.539 -43.071  32.062  1.00101.77           C  
ANISOU10908  CB  ALA H 210    10268  10582  17819    910   1489   2875       C  
ATOM  10909  N   LYS H 211     105.246 -42.762  29.057  1.00105.81           N  
ANISOU10909  N   LYS H 211    10736  11131  18337    890   1456   2843       N  
ATOM  10910  CA  LYS H 211     104.841 -42.616  27.662  1.00106.09           C  
ANISOU10910  CA  LYS H 211    10749  11173  18388    895   1451   2848       C  
ATOM  10911  C   LYS H 211     105.455 -43.706  26.775  1.00101.09           C  
ANISOU10911  C   LYS H 211    10069  10569  17772    887   1404   2826       C  
ATOM  10912  O   LYS H 211     104.819 -44.187  25.828  1.00 99.00           O  
ANISOU10912  O   LYS H 211     9770  10310  17536    901   1390   2839       O  
ATOM  10913  CB  LYS H 211     105.240 -41.230  27.151  1.00113.03           C  
ANISOU10913  CB  LYS H 211    11664  12047  19237    878   1477   2836       C  
ATOM  10914  CG  LYS H 211     104.739 -40.075  28.019  1.00118.07           C  
ANISOU10914  CG  LYS H 211    12352  12657  19854    884   1523   2855       C  
ATOM  10915  CD  LYS H 211     103.220 -39.908  27.908  1.00125.07           C  
ANISOU10915  CD  LYS H 211    13236  13522  20764    917   1545   2896       C  
ATOM  10916  CE  LYS H 211     102.680 -38.880  28.900  1.00129.38           C  
ANISOU10916  CE  LYS H 211    13829  14039  21290    925   1590   2917       C  
ATOM  10917  NZ  LYS H 211     103.199 -37.504  28.647  1.00131.21           N  
ANISOU10917  NZ  LYS H 211    14105  14263  21487    907   1617   2903       N  
ATOM  10918  N   ASP H 212     106.686 -44.094  27.093  1.00100.08           N  
ANISOU10918  N   ASP H 212     9938  10459  17627    865   1381   2792       N  
ATOM  10919  CA  ASP H 212     107.354 -45.163  26.377  1.00 95.25           C  
ANISOU10919  CA  ASP H 212     9284   9876  17030    856   1336   2769       C  
ATOM  10920  C   ASP H 212     106.687 -46.504  26.593  1.00 88.52           C  
ANISOU10920  C   ASP H 212     8395   9025  16213    878   1312   2788       C  
ATOM  10921  O   ASP H 212     106.546 -47.299  25.663  1.00 85.17           O  
ANISOU10921  O   ASP H 212     7931   8616  15815    884   1283   2787       O  
ATOM  10922  CB  ASP H 212     108.795 -45.288  26.826  1.00 94.75           C  
ANISOU10922  CB  ASP H 212     9228   9832  16939    830   1318   2728       C  
ATOM  10923  CG  ASP H 212     109.545 -43.994  26.747  1.00100.98           C  
ANISOU10923  CG  ASP H 212    10056  10621  17691    805   1343   2707       C  
ATOM  10924  OD1 ASP H 212     108.884 -42.933  26.612  1.00106.01           O  
ANISOU10924  OD1 ASP H 212    10722  11237  18321    811   1379   2727       O  
ATOM  10925  OD2 ASP H 212     110.796 -44.053  26.836  1.00100.96           O  
ANISOU10925  OD2 ASP H 212    10056  10639  17666    781   1325   2669       O  
ATOM  10926  N   ILE H 213     106.300 -46.764  27.837  1.00 94.61           N  
ANISOU10926  N   ILE H 213     9182   9781  16986    889   1323   2804       N  
ATOM  10927  CA  ILE H 213     105.842 -48.094  28.229  1.00 88.18           C  
ANISOU10927  CA  ILE H 213     8336   8967  16200    906   1299   2817       C  
ATOM  10928  C   ILE H 213     104.394 -48.423  27.840  1.00 87.08           C  
ANISOU10928  C   ILE H 213     8176   8815  16096    934   1307   2856       C  
ATOM  10929  O   ILE H 213     104.097 -49.573  27.491  1.00 81.96           O  
ANISOU10929  O   ILE H 213     7488   8176  15476    944   1278   2861       O  
ATOM  10930  CB  ILE H 213     105.981 -48.298  29.744  1.00 87.07           C  
ANISOU10930  CB  ILE H 213     8221   8815  16047    908   1307   2820       C  
ATOM  10931  CG1 ILE H 213     107.366 -47.865  30.222  1.00 88.76           C  
ANISOU10931  CG1 ILE H 213     8459   9040  16224    882   1304   2783       C  
ATOM  10932  CG2 ILE H 213     105.750 -49.748  30.089  1.00 80.33           C  
ANISOU10932  CG2 ILE H 213     7336   7967  15220    921   1277   2827       C  
ATOM  10933  CD1 ILE H 213     107.543 -47.963  31.721  1.00 88.84           C  
ANISOU10933  CD1 ILE H 213     8498   9039  16219    883   1314   2784       C  
ATOM  10934  N   ALA H 214     103.501 -47.431  27.906  1.00 85.09           N  
ANISOU10934  N   ALA H 214     7948   8541  15841    945   1346   2881       N  
ATOM  10935  CA  ALA H 214     102.067 -47.676  27.694  1.00 84.77           C  
ANISOU10935  CA  ALA H 214     7891   8486  15832    973   1357   2918       C  
ATOM  10936  C   ALA H 214     101.711 -48.368  26.368  1.00 81.88           C  
ANISOU10936  C   ALA H 214     7478   8136  15496    980   1330   2921       C  
ATOM  10937  O   ALA H 214     100.918 -49.301  26.377  1.00 77.87           O  
ANISOU10937  O   ALA H 214     6941   7628  15019    998   1318   2941       O  
ATOM  10938  CB  ALA H 214     101.293 -46.384  27.819  1.00 91.35           C  
ANISOU10938  CB  ALA H 214     8758   9296  16653    982   1402   2941       C  
ATOM  10939  N   PRO H 215     102.287 -47.935  25.230  1.00 84.92           N  
ANISOU10939  N   PRO H 215     7856   8537  15873    967   1320   2901       N  
ATOM  10940  CA  PRO H 215     101.920 -48.632  23.986  1.00 82.54           C  
ANISOU10940  CA  PRO H 215     7509   8250  15601    975   1294   2904       C  
ATOM  10941  C   PRO H 215     102.450 -50.075  23.890  1.00 76.01           C  
ANISOU10941  C   PRO H 215     6643   7445  14793    971   1249   2888       C  
ATOM  10942  O   PRO H 215     101.955 -50.872  23.091  1.00 73.50           O  
ANISOU10942  O   PRO H 215     6286   7137  14505    982   1227   2897       O  
ATOM  10943  CB  PRO H 215     102.563 -47.772  22.894  1.00 87.17           C  
ANISOU10943  CB  PRO H 215     8102   8848  16169    958   1295   2883       C  
ATOM  10944  CG  PRO H 215     102.969 -46.508  23.565  1.00 92.01           C  
ANISOU10944  CG  PRO H 215     8766   9446  16746    946   1329   2877       C  
ATOM  10945  CD  PRO H 215     103.250 -46.853  24.974  1.00 89.33           C  
ANISOU10945  CD  PRO H 215     8445   9100  16397    944   1332   2875       C  
ATOM  10946  N   THR H 216     103.464 -50.384  24.689  1.00 88.23           N  
ANISOU10946  N   THR H 216     8203   9000  16321    955   1236   2865       N  
ATOM  10947  CA  THR H 216     104.150 -51.667  24.632  1.00 82.26           C  
ANISOU10947  CA  THR H 216     7414   8264  15576    949   1192   2845       C  
ATOM  10948  C   THR H 216     103.245 -52.783  25.111  1.00 77.54           C  
ANISOU10948  C   THR H 216     6794   7659  15010    970   1183   2870       C  
ATOM  10949  O   THR H 216     103.264 -53.887  24.579  1.00 73.27           O  
ANISOU10949  O   THR H 216     6215   7133  14493    973   1149   2866       O  
ATOM  10950  CB  THR H 216     105.442 -51.640  25.493  1.00 81.45           C  
ANISOU10950  CB  THR H 216     7335   8171  15443    928   1184   2813       C  
ATOM  10951  OG1 THR H 216     106.462 -50.926  24.791  1.00 84.63           O  
ANISOU10951  OG1 THR H 216     7745   8589  15820    905   1180   2782       O  
ATOM  10952  CG2 THR H 216     105.938 -53.055  25.839  1.00 74.65           C  
ANISOU10952  CG2 THR H 216     6446   7324  14593    928   1144   2800       C  
ATOM  10953  N   LEU H 217     102.437 -52.478  26.113  0.71 73.66           N  
ANISOU10953  N   LEU H 217     6352   8096  13539    669    -99   1417       N  
ATOM  10954  CA  LEU H 217     101.710 -53.509  26.820  0.87 73.48           C  
ANISOU10954  CA  LEU H 217     6312   8076  13531    654   -178   1427       C  
ATOM  10955  C   LEU H 217     100.478 -54.010  26.072  0.86 73.78           C  
ANISOU10955  C   LEU H 217     6298   8218  13518    657   -213   1499       C  
ATOM  10956  O   LEU H 217      99.906 -53.327  25.228  0.84 74.13           O  
ANISOU10956  O   LEU H 217     6326   8329  13511    683   -160   1574       O  
ATOM  10957  CB  LEU H 217     101.304 -52.997  28.194  1.00 73.24           C  
ANISOU10957  CB  LEU H 217     6325   7977  13526    685   -150   1481       C  
ATOM  10958  CG  LEU H 217     102.434 -52.313  28.938  1.00 72.97           C  
ANISOU10958  CG  LEU H 217     6347   7841  13539    690   -103   1425       C  
ATOM  10959  CD1 LEU H 217     102.018 -51.879  30.316  1.00 74.14           C  
ANISOU10959  CD1 LEU H 217     6536   7921  13713    719    -81   1476       C  
ATOM  10960  CD2 LEU H 217     103.588 -53.262  29.018  1.00 72.71           C  
ANISOU10960  CD2 LEU H 217     6312   7764  13552    641   -169   1293       C  
ATOM  10961  N   THR H 218     100.113 -55.244  26.387  1.00 77.08           N  
ANISOU10961  N   THR H 218     6689   8648  13951    628   -304   1471       N  
ATOM  10962  CA  THR H 218      98.839 -55.835  26.028  1.00 76.25           C  
ANISOU10962  CA  THR H 218     6538   8626  13807    630   -347   1543       C  
ATOM  10963  C   THR H 218      98.176 -56.148  27.366  1.00 74.81           C  
ANISOU10963  C   THR H 218     6373   8398  13653    640   -378   1581       C  
ATOM  10964  O   THR H 218      98.867 -56.642  28.279  1.00 71.69           O  
ANISOU10964  O   THR H 218     6002   7925  13312    618   -416   1506       O  
ATOM  10965  CB  THR H 218      98.998 -57.126  25.183  1.00 71.61           C  
ANISOU10965  CB  THR H 218     5900   8096  13214    584   -436   1471       C  
ATOM  10966  OG1 THR H 218      99.748 -56.852  23.997  1.00 73.21           O  
ANISOU10966  OG1 THR H 218     6090   8333  13395    573   -408   1425       O  
ATOM  10967  CG2 THR H 218      97.642 -57.672  24.786  1.00 71.38           C  
ANISOU10967  CG2 THR H 218     5823   8155  13143    589   -477   1551       C  
ATOM  10968  N   LEU H 219      96.873 -55.861  27.502  1.00 71.49           N  
ANISOU10968  N   LEU H 219     5940   8023  13199    673   -361   1695       N  
ATOM  10969  CA  LEU H 219      96.165 -56.082  28.772  1.00 70.68           C  
ANISOU10969  CA  LEU H 219     5855   7880  13120    686   -384   1742       C  
ATOM  10970  C   LEU H 219      94.900 -56.908  28.612  1.00 68.94           C  
ANISOU10970  C   LEU H 219     5588   7734  12873    683   -445   1803       C  
ATOM  10971  O   LEU H 219      94.185 -56.780  27.615  1.00 70.53           O  
ANISOU10971  O   LEU H 219     5753   8023  13023    693   -433   1863       O  
ATOM  10972  CB  LEU H 219      95.819 -54.751  29.434  1.00 76.26           C  
ANISOU10972  CB  LEU H 219     6607   8549  13821    737   -292   1829       C  
ATOM  10973  CG  LEU H 219      95.273 -54.797  30.862  1.00 76.19           C  
ANISOU10973  CG  LEU H 219     6626   8481  13842    755   -303   1871       C  
ATOM  10974  CD1 LEU H 219      95.984 -55.796  31.717  1.00 75.13           C  
ANISOU10974  CD1 LEU H 219     6503   8277  13767    717   -377   1772       C  
ATOM  10975  CD2 LEU H 219      95.414 -53.455  31.486  1.00 79.36           C  
ANISOU10975  CD2 LEU H 219     7080   8824  14249    798   -210   1920       C  
ATOM  10976  N   TYR H 220      94.611 -57.738  29.615  1.00 75.76           N  
ANISOU10976  N   TYR H 220     6453   8560  13771    669   -510   1790       N  
ATOM  10977  CA  TYR H 220      93.444 -58.622  29.595  1.00 74.00           C  
ANISOU10977  CA  TYR H 220     6187   8399  13530    662   -576   1842       C  
ATOM  10978  C   TYR H 220      92.630 -58.664  30.884  1.00 74.62           C  
ANISOU10978  C   TYR H 220     6285   8438  13628    684   -585   1906       C  
ATOM  10979  O   TYR H 220      93.182 -58.823  31.980  1.00 73.04           O  
ANISOU10979  O   TYR H 220     6120   8152  13478    676   -600   1857       O  
ATOM  10980  CB  TYR H 220      93.875 -60.041  29.294  1.00 68.19           C  
ANISOU10980  CB  TYR H 220     5416   7677  12816    609   -676   1744       C  
ATOM  10981  CG  TYR H 220      94.404 -60.264  27.910  1.00 67.35           C  
ANISOU10981  CG  TYR H 220     5276   7631  12682    584   -686   1690       C  
ATOM  10982  CD1 TYR H 220      93.539 -60.417  26.841  1.00 68.85           C  
ANISOU10982  CD1 TYR H 220     5419   7922  12819    589   -695   1749       C  
ATOM  10983  CD2 TYR H 220      95.756 -60.375  27.680  1.00 65.13           C  
ANISOU10983  CD2 TYR H 220     5010   7306  12430    556   -689   1580       C  
ATOM  10984  CE1 TYR H 220      94.018 -60.654  25.575  1.00 68.27           C  
ANISOU10984  CE1 TYR H 220     5314   7904  12721    566   -706   1699       C  
ATOM  10985  CE2 TYR H 220      96.238 -60.604  26.423  1.00 64.52           C  
ANISOU10985  CE2 TYR H 220     4903   7284  12329    533   -700   1530       C  
ATOM  10986  CZ  TYR H 220      95.370 -60.749  25.371  1.00 66.20           C  
ANISOU10986  CZ  TYR H 220     5069   7597  12488    538   -708   1589       C  
ATOM  10987  OH  TYR H 220      95.841 -60.985  24.101  1.00 66.15           O  
ANISOU10987  OH  TYR H 220     5031   7647  12456    517   -719   1540       O  
ATOM  10988  N   VAL H 221      91.306 -58.575  30.722  1.00 69.58           N  
ANISOU10988  N   VAL H 221     5620   7866  12950    709   -581   2014       N  
ATOM  10989  CA  VAL H 221      90.332 -58.820  31.795  1.00 69.43           C  
ANISOU10989  CA  VAL H 221     5608   7831  12943    726   -604   2082       C  
ATOM  10990  C   VAL H 221      89.416 -59.981  31.468  1.00 69.55           C  
ANISOU10990  C   VAL H 221     5568   7917  12942    704   -688   2102       C  
ATOM  10991  O   VAL H 221      89.278 -60.375  30.311  1.00 69.82           O  
ANISOU10991  O   VAL H 221     5558   8028  12943    687   -713   2093       O  
ATOM  10992  CB  VAL H 221      89.467 -57.616  32.037  1.00 69.60           C  
ANISOU10992  CB  VAL H 221     5650   7863  12933    781   -520   2204       C  
ATOM  10993  CG1 VAL H 221      90.121 -56.646  32.999  1.00 69.36           C  
ANISOU10993  CG1 VAL H 221     5682   7738  12934    806   -453   2197       C  
ATOM  10994  CG2 VAL H 221      89.203 -56.973  30.728  1.00 70.01           C  
ANISOU10994  CG2 VAL H 221     5678   7996  12928    796   -469   2251       C  
ATOM  10995  N   GLY H 222      88.795 -60.528  32.501  1.00 76.64           N  
ANISOU10995  N   GLY H 222     6468   8788  13865    706   -732   2129       N  
ATOM  10996  CA  GLY H 222      87.762 -61.519  32.286  1.00 75.03           C  
ANISOU10996  CA  GLY H 222     6214   8651  13643    692   -805   2167       C  
ATOM  10997  C   GLY H 222      88.270 -62.751  31.589  1.00 70.02           C  
ANISOU10997  C   GLY H 222     5539   8047  13018    640   -891   2070       C  
ATOM  10998  O   GLY H 222      89.156 -63.419  32.109  1.00 65.99           O  
ANISOU10998  O   GLY H 222     5042   7475  12556    607   -939   1972       O  
ATOM  10999  N   LYS H 223      87.712 -63.072  30.426  1.00 78.86           N  
ANISOU10999  N   LYS H 223     6609   9261  14093    631   -912   2097       N  
ATOM  11000  CA  LYS H 223      88.147 -64.270  29.729  1.00 74.39           C  
ANISOU11000  CA  LYS H 223     6002   8728  13534    582   -996   2008       C  
ATOM  11001  C   LYS H 223      89.311 -64.066  28.767  1.00 73.47           C  
ANISOU11001  C   LYS H 223     5887   8616  13413    562   -976   1922       C  
ATOM  11002  O   LYS H 223      90.498 -64.306  29.103  1.00 70.38           O  
ANISOU11002  O   LYS H 223     5521   8157  13065    536   -992   1819       O  
ATOM  11003  CB  LYS H 223      86.977 -64.822  28.948  1.00 75.45           C  
ANISOU11003  CB  LYS H 223     6079   8963  13624    581  -1037   2074       C  
ATOM  11004  CG  LYS H 223      85.718 -64.865  29.776  1.00 76.80           C  
ANISOU11004  CG  LYS H 223     6247   9141  13793    607  -1045   2174       C  
ATOM  11005  CD  LYS H 223      85.730 -66.028  30.771  1.00 72.76           C  
ANISOU11005  CD  LYS H 223     5733   8583  13331    577  -1132   2125       C  
ATOM  11006  CE  LYS H 223      85.097 -67.285  30.168  1.00 69.27           C  
ANISOU11006  CE  LYS H 223     5230   8214  12875    545  -1224   2118       C  
ATOM  11007  NZ  LYS H 223      83.906 -66.928  29.351  1.00 71.78           N  
ANISOU11007  NZ  LYS H 223     5513   8627  13135    571  -1200   2225       N  
ATOM  11008  N   LYS H 224      88.979 -63.612  27.565  1.00 77.29           N  
ANISOU11008  N   LYS H 224     6344   9178  13844    575   -941   1966       N  
ATOM  11009  CA  LYS H 224      89.997 -63.149  26.627  1.00 77.41           C  
ANISOU11009  CA  LYS H 224     6366   9200  13848    566   -902   1904       C  
ATOM  11010  C   LYS H 224      90.004 -61.633  26.571  1.00 82.56           C  
ANISOU11010  C   LYS H 224     7054   9840  14476    612   -791   1971       C  
ATOM  11011  O   LYS H 224      90.757 -61.046  25.794  1.00 83.86           O  
ANISOU11011  O   LYS H 224     7226  10011  14626    612   -744   1937       O  
ATOM  11012  CB  LYS H 224      89.764 -63.738  25.233  1.00 76.76           C  
ANISOU11012  CB  LYS H 224     6227   9214  13724    544   -941   1892       C  
ATOM  11013  CG  LYS H 224      88.357 -63.479  24.685  1.00 79.75           C  
ANISOU11013  CG  LYS H 224     6571   9682  14047    573   -925   2013       C  
ATOM  11014  CD  LYS H 224      87.795 -64.718  23.992  1.00 75.18           C  
ANISOU11014  CD  LYS H 224     5934   9180  13452    541  -1015   1999       C  
ATOM  11015  CE  LYS H 224      87.967 -65.960  24.854  1.00 71.32           C  
ANISOU11015  CE  LYS H 224     5439   8645  13013    504  -1108   1933       C  
ATOM  11016  NZ  LYS H 224      87.553 -67.188  24.123  1.00 67.19           N  
ANISOU11016  NZ  LYS H 224     4860   8194  12477    470  -1198   1908       N  
ATOM  11017  N   GLN H 225      89.147 -61.010  27.379  1.00 67.15           N  
ANISOU11017  N   GLN H 225     5123   7871  12519    651   -750   2068       N  
ATOM  11018  CA  GLN H 225      88.686 -59.681  27.038  1.00 72.92           C  
ANISOU11018  CA  GLN H 225     5869   8628  13208    698   -654   2163       C  
ATOM  11019  C   GLN H 225      89.849 -58.719  26.965  1.00 74.47           C  
ANISOU11019  C   GLN H 225     6109   8769  13418    706   -581   2115       C  
ATOM  11020  O   GLN H 225      90.535 -58.452  27.953  1.00 74.01           O  
ANISOU11020  O   GLN H 225     6097   8621  13404    708   -564   2075       O  
ATOM  11021  CB  GLN H 225      87.639 -59.189  28.045  1.00 75.83           C  
ANISOU11021  CB  GLN H 225     6258   8979  13575    738   -624   2270       C  
ATOM  11022  CG  GLN H 225      86.558 -58.276  27.442  1.00 79.94           C  
ANISOU11022  CG  GLN H 225     6765   9572  14036    781   -558   2394       C  
ATOM  11023  CD  GLN H 225      85.809 -57.465  28.487  1.00 84.61           C  
ANISOU11023  CD  GLN H 225     7391  10127  14629    826   -504   2492       C  
ATOM  11024  OE1 GLN H 225      85.639 -57.898  29.629  1.00 84.51           O  
ANISOU11024  OE1 GLN H 225     7395  10060  14655    823   -539   2489       O  
ATOM  11025  NE2 GLN H 225      85.362 -56.273  28.098  1.00 88.89           N  
ANISOU11025  NE2 GLN H 225     7945  10699  15131    868   -418   2579       N  
ATOM  11026  N   LEU H 226      90.015 -58.153  25.779  1.00 72.24           N  
ANISOU11026  N   LEU H 226     5812   8543  13094    714   -535   2125       N  
ATOM  11027  CA  LEU H 226      91.133 -57.286  25.484  1.00 74.29           C  
ANISOU11027  CA  LEU H 226     6106   8762  13360    719   -469   2076       C  
ATOM  11028  C   LEU H 226      90.688 -55.869  25.759  1.00 80.33           C  
ANISOU11028  C   LEU H 226     6905   9515  14102    772   -368   2175       C  
ATOM  11029  O   LEU H 226      89.825 -55.326  25.064  1.00 84.42           O  
ANISOU11029  O   LEU H 226     7402  10105  14568    800   -328   2265       O  
ATOM  11030  CB  LEU H 226      91.567 -57.479  24.030  1.00 74.45           C  
ANISOU11030  CB  LEU H 226     6090   8850  13347    698   -476   2031       C  
ATOM  11031  CG  LEU H 226      92.648 -56.622  23.383  1.00 76.76           C  
ANISOU11031  CG  LEU H 226     6406   9124  13635    702   -408   1984       C  
ATOM  11032  CD1 LEU H 226      92.054 -55.372  22.735  1.00 83.60           C  
ANISOU11032  CD1 LEU H 226     7275  10041  14449    747   -316   2086       C  
ATOM  11033  CD2 LEU H 226      93.736 -56.260  24.393  1.00 73.97           C  
ANISOU11033  CD2 LEU H 226     6107   8660  13337    699   -383   1917       C  
ATOM  11034  N   VAL H 227      91.254 -55.275  26.801  1.00 75.24           N  
ANISOU11034  N   VAL H 227     6312   8778  13496    786   -328   2159       N  
ATOM  11035  CA  VAL H 227      90.993 -53.864  27.071  1.00 81.07           C  
ANISOU11035  CA  VAL H 227     7088   9497  14217    836   -228   2243       C  
ATOM  11036  C   VAL H 227      92.166 -53.068  26.556  1.00 83.14           C  
ANISOU11036  C   VAL H 227     7377   9729  14483    836   -166   2186       C  
ATOM  11037  O   VAL H 227      93.324 -53.446  26.784  1.00 80.19           O  
ANISOU11037  O   VAL H 227     7020   9295  14152    806   -191   2079       O  
ATOM  11038  CB  VAL H 227      90.773 -53.569  28.569  1.00 81.58           C  
ANISOU11038  CB  VAL H 227     7197   9480  14318    858   -213   2275       C  
ATOM  11039  CG1 VAL H 227      89.430 -54.103  29.005  1.00 81.30           C  
ANISOU11039  CG1 VAL H 227     7137   9485  14270    869   -256   2357       C  
ATOM  11040  CG2 VAL H 227      91.903 -54.151  29.414  1.00 77.02           C  
ANISOU11040  CG2 VAL H 227     6649   8811  13805    826   -257   2162       C  
ATOM  11041  N   GLU H 228      91.877 -51.993  25.828  1.00 79.88           N  
ANISOU11041  N   GLU H 228     6966   9359  14025    870    -86   2256       N  
ATOM  11042  CA  GLU H 228      92.957 -51.168  25.325  1.00 82.37           C  
ANISOU11042  CA  GLU H 228     7306   9647  14342    873    -22   2209       C  
ATOM  11043  C   GLU H 228      93.429 -50.233  26.423  1.00 84.79           C  
ANISOU11043  C   GLU H 228     7674   9858  14684    900     41   2215       C  
ATOM  11044  O   GLU H 228      92.799 -50.120  27.473  1.00 85.42           O  
ANISOU11044  O   GLU H 228     7774   9903  14778    921     43   2270       O  
ATOM  11045  CB  GLU H 228      92.518 -50.403  24.083  1.00 87.35           C  
ANISOU11045  CB  GLU H 228     7915  10362  14912    898     38   2276       C  
ATOM  11046  CG  GLU H 228      92.315 -51.317  22.875  1.00 85.26           C  
ANISOU11046  CG  GLU H 228     7592  10187  14616    867    -22   2250       C  
ATOM  11047  CD  GLU H 228      92.645 -50.629  21.555  1.00 89.61           C  
ANISOU11047  CD  GLU H 228     8130  10793  15124    875     34   2254       C  
ATOM  11048  OE1 GLU H 228      92.875 -51.360  20.565  1.00 88.09           O  
ANISOU11048  OE1 GLU H 228     7897  10657  14915    844    -13   2202       O  
ATOM  11049  OE2 GLU H 228      92.670 -49.370  21.506  1.00 94.72           O  
ANISOU11049  OE2 GLU H 228     8807  11428  15754    913    126   2309       O  
ATOM  11050  N   ILE H 229      94.523 -49.539  26.165  1.00 83.52           N  
ANISOU11050  N   ILE H 229     7542   9656  14536    900     95   2161       N  
ATOM  11051  CA  ILE H 229      95.277 -48.955  27.257  1.00 84.35           C  
ANISOU11051  CA  ILE H 229     7704   9658  14689    911    132   2130       C  
ATOM  11052  C   ILE H 229      95.743 -47.532  26.887  1.00 90.55           C  
ANISOU11052  C   ILE H 229     8521  10427  15457    943    237   2157       C  
ATOM  11053  O   ILE H 229      96.500 -47.342  25.933  1.00 91.26           O  
ANISOU11053  O   ILE H 229     8602  10537  15536    930    257   2107       O  
ATOM  11054  CB  ILE H 229      96.452 -49.935  27.641  1.00 78.24           C  
ANISOU11054  CB  ILE H 229     6937   8821  13971    862     62   1995       C  
ATOM  11055  CG1 ILE H 229      97.135 -49.552  28.952  1.00 78.26           C  
ANISOU11055  CG1 ILE H 229     6995   8711  14028    869     84   1959       C  
ATOM  11056  CG2 ILE H 229      97.450 -50.156  26.482  1.00 77.10           C  
ANISOU11056  CG2 ILE H 229     6772   8703  13821    830     55   1907       C  
ATOM  11057  CD1 ILE H 229      97.822 -50.745  29.605  1.00 71.96           C  
ANISOU11057  CD1 ILE H 229     6198   7858  13284    825     -4   1853       C  
ATOM  11058  N   GLU H 230      95.266 -46.535  27.638  1.00 80.08           N  
ANISOU11058  N   GLU H 230     7232   9066  14129    987    303   2239       N  
ATOM  11059  CA  GLU H 230      95.452 -45.118  27.286  1.00 86.79           C  
ANISOU11059  CA  GLU H 230     8110   9911  14955   1025    406   2289       C  
ATOM  11060  C   GLU H 230      96.763 -44.580  27.816  1.00 87.69           C  
ANISOU11060  C   GLU H 230     8274   9929  15117   1021    443   2211       C  
ATOM  11061  O   GLU H 230      97.685 -44.317  27.046  1.00 89.07           O  
ANISOU11061  O   GLU H 230     8448  10105  15291   1007    468   2152       O  
ATOM  11062  CB  GLU H 230      94.307 -44.260  27.818  1.00 92.12           C  
ANISOU11062  CB  GLU H 230     8802  10596  15605   1075    462   2416       C  
ATOM  11063  CG  GLU H 230      94.461 -42.775  27.501  1.00 97.07           C  
ANISOU11063  CG  GLU H 230     9458  11216  16207   1116    570   2471       C  
ATOM  11064  CD  GLU H 230      93.395 -41.895  28.158  1.00103.14           C  
ANISOU11064  CD  GLU H 230    10249  11983  16955   1167    627   2593       C  
ATOM  11065  OE1 GLU H 230      93.766 -40.894  28.809  1.00105.64           O  
ANISOU11065  OE1 GLU H 230    10616  12233  17291   1195    694   2609       O  
ATOM  11066  OE2 GLU H 230      92.193 -42.192  28.015  1.00105.58           O  
ANISOU11066  OE2 GLU H 230    10527  12357  17230   1179    605   2673       O  
ATOM  11067  N   LYS H 231      96.860 -44.404  29.129  1.00 85.57           N  
ANISOU11067  N   LYS H 231     8047   9576  14889   1033    448   2211       N  
ATOM  11068  CA  LYS H 231      98.161 -44.050  29.705  1.00 86.10           C  
ANISOU11068  CA  LYS H 231     8160   9547  15006   1024    471   2126       C  
ATOM  11069  C   LYS H 231      98.600 -45.010  30.833  1.00 80.93           C  
ANISOU11069  C   LYS H 231     7521   8818  14410    994    397   2049       C  
ATOM  11070  O   LYS H 231      97.944 -46.018  31.128  1.00 76.61           O  
ANISOU11070  O   LYS H 231     6948   8296  13866    977    323   2055       O  
ATOM  11071  CB  LYS H 231      98.173 -42.578  30.187  1.00 92.12           C  
ANISOU11071  CB  LYS H 231     8972  10262  15767   1072    572   2191       C  
ATOM  11072  CG  LYS H 231      97.118 -42.134  31.216  1.00 96.74           C  
ANISOU11072  CG  LYS H 231     9581  10829  16348   1112    596   2292       C  
ATOM  11073  CD  LYS H 231      96.945 -40.585  31.180  1.00103.42           C  
ANISOU11073  CD  LYS H 231    10461  11665  17170   1162    705   2375       C  
ATOM  11074  CE  LYS H 231      96.064 -40.031  32.315  1.00108.92           C  
ANISOU11074  CE  LYS H 231    11189  12328  17869   1204    736   2467       C  
ATOM  11075  NZ  LYS H 231      95.113 -38.945  31.893  1.00114.53           N  
ANISOU11075  NZ  LYS H 231    11899  13092  18527   1252    814   2590       N  
ATOM  11076  N   VAL H 232      99.744 -44.691  31.418  1.00 83.32           N  
ANISOU11076  N   VAL H 232     7866   9031  14760    987    417   1974       N  
ATOM  11077  CA  VAL H 232     100.363 -45.469  32.468  1.00 79.11           C  
ANISOU11077  CA  VAL H 232     7354   8418  14285    959    357   1891       C  
ATOM  11078  C   VAL H 232     101.003 -44.468  33.421  1.00 83.82           C  
ANISOU11078  C   VAL H 232     8012   8917  14918    985    421   1885       C  
ATOM  11079  O   VAL H 232     101.630 -43.512  32.963  1.00 88.47           O  
ANISOU11079  O   VAL H 232     8621   9492  15500    999    492   1880       O  
ATOM  11080  CB  VAL H 232     101.425 -46.410  31.893  1.00 73.71           C  
ANISOU11080  CB  VAL H 232     6648   7732  13625    907    295   1767       C  
ATOM  11081  CG1 VAL H 232     102.347 -46.923  32.982  1.00 69.80           C  
ANISOU11081  CG1 VAL H 232     6187   7139  13196    882    253   1672       C  
ATOM  11082  CG2 VAL H 232     100.790 -47.544  31.128  1.00 69.51           C  
ANISOU11082  CG2 VAL H 232     6057   7287  13065    878    219   1766       C  
ATOM  11083  N   VAL H 233     100.856 -44.637  34.730  1.00 73.77           N  
ANISOU11083  N   VAL H 233     6771   7577  13683    992    401   1888       N  
ATOM  11084  CA  VAL H 233     101.512 -43.684  35.633  1.00 76.46           C  
ANISOU11084  CA  VAL H 233     7171   7822  14058   1016    462   1879       C  
ATOM  11085  C   VAL H 233     102.182 -44.406  36.796  1.00 74.05           C  
ANISOU11085  C   VAL H 233     6893   7428  13816    991    404   1794       C  
ATOM  11086  O   VAL H 233     101.607 -45.362  37.335  1.00 72.17           O  
ANISOU11086  O   VAL H 233     6637   7196  13588    977    334   1796       O  
ATOM  11087  CB  VAL H 233     100.516 -42.595  36.164  1.00 80.95           C  
ANISOU11087  CB  VAL H 233     7765   8390  14601   1072    534   2004       C  
ATOM  11088  CG1 VAL H 233      99.128 -42.737  35.540  1.00 81.59           C  
ANISOU11088  CG1 VAL H 233     7803   8573  14625   1089    528   2107       C  
ATOM  11089  CG2 VAL H 233     100.446 -42.595  37.686  1.00 81.63           C  
ANISOU11089  CG2 VAL H 233     7895   8390  14730   1086    524   2009       C  
ATOM  11090  N   LEU H 234     103.397 -43.962  37.154  1.00 72.43           N  
ANISOU11090  N   LEU H 234     6727   7140  13652    984    433   1719       N  
ATOM  11091  CA  LEU H 234     104.260 -44.651  38.130  1.00 70.53           C  
ANISOU11091  CA  LEU H 234     6512   6812  13473    955    379   1620       C  
ATOM  11092  C   LEU H 234     104.345 -43.925  39.445  1.00 72.96           C  
ANISOU11092  C   LEU H 234     6877   7029  13814    987    420   1644       C  
ATOM  11093  O   LEU H 234     104.350 -42.718  39.467  1.00 77.19           O  
ANISOU11093  O   LEU H 234     7443   7547  14338   1024    504   1697       O  
ATOM  11094  CB  LEU H 234     105.675 -44.807  37.597  1.00 69.33           C  
ANISOU11094  CB  LEU H 234     6364   6630  13350    920    372   1504       C  
ATOM  11095  CG  LEU H 234     105.999 -45.698  36.406  1.00 68.73           C  
ANISOU11095  CG  LEU H 234     6236   6620  13257    877    319   1441       C  
ATOM  11096  CD1 LEU H 234     105.555 -45.097  35.092  1.00 69.38           C  
ANISOU11096  CD1 LEU H 234     6288   6793  13280    893    370   1503       C  
ATOM  11097  CD2 LEU H 234     107.474 -45.901  36.395  1.00 68.30           C  
ANISOU11097  CD2 LEU H 234     6199   6503  13248    843    306   1318       C  
ATOM  11098  N   HIS H 235     104.449 -44.651  40.543  1.00 72.03           N  
ANISOU11098  N   HIS H 235     6776   6852  13740    973    362   1603       N  
ATOM  11099  CA  HIS H 235     104.534 -44.019  41.845  1.00 72.34           C  
ANISOU11099  CA  HIS H 235     6871   6803  13813   1002    397   1623       C  
ATOM  11100  C   HIS H 235     105.873 -43.307  41.953  1.00 72.56           C  
ANISOU11100  C   HIS H 235     6939   6753  13876    999    445   1549       C  
ATOM  11101  O   HIS H 235     106.914 -43.877  41.603  1.00 71.99           O  
ANISOU11101  O   HIS H 235     6859   6662  13831    959    408   1444       O  
ATOM  11102  CB  HIS H 235     104.376 -45.059  42.935  1.00 71.60           C  
ANISOU11102  CB  HIS H 235     6780   6666  13758    983    318   1588       C  
ATOM  11103  CG  HIS H 235     104.211 -44.505  44.315  1.00 71.93           C  
ANISOU11103  CG  HIS H 235     6875   6628  13829   1017    346   1624       C  
ATOM  11104  ND1 HIS H 235     105.272 -44.052  45.068  1.00 71.99           N  
ANISOU11104  ND1 HIS H 235     6932   6536  13884   1018    372   1560       N  
ATOM  11105  CD2 HIS H 235     103.121 -44.412  45.111  1.00 72.18           C  
ANISOU11105  CD2 HIS H 235     6915   6661  13850   1048    348   1713       C  
ATOM  11106  CE1 HIS H 235     104.835 -43.673  46.255  1.00 72.28           C  
ANISOU11106  CE1 HIS H 235     7008   6519  13938   1050    390   1609       C  
ATOM  11107  NE2 HIS H 235     103.533 -43.884  46.309  1.00 72.41           N  
ANISOU11107  NE2 HIS H 235     6999   6594  13918   1069    376   1702       N  
ATOM  11108  N   PRO H 236     105.855 -42.041  42.417  1.00 76.87           N  
ANISOU11108  N   PRO H 236     7530   7255  14421   1043    529   1606       N  
ATOM  11109  CA  PRO H 236     107.043 -41.190  42.569  1.00 78.74           C  
ANISOU11109  CA  PRO H 236     7811   7418  14690   1048    585   1550       C  
ATOM  11110  C   PRO H 236     108.175 -41.884  43.320  1.00 76.67           C  
ANISOU11110  C   PRO H 236     7572   7069  14492   1012    532   1430       C  
ATOM  11111  O   PRO H 236     109.331 -41.522  43.145  1.00 77.93           O  
ANISOU11111  O   PRO H 236     7752   7181  14678    999    557   1356       O  
ATOM  11112  CB  PRO H 236     106.514 -40.010  43.378  1.00 86.09           C  
ANISOU11112  CB  PRO H 236     8786   8308  15615   1102    660   1642       C  
ATOM  11113  CG  PRO H 236     105.094 -39.931  43.008  1.00 86.09           C  
ANISOU11113  CG  PRO H 236     8756   8395  15561   1128    669   1756       C  
ATOM  11114  CD  PRO H 236     104.631 -41.338  42.842  1.00 78.29           C  
ANISOU11114  CD  PRO H 236     7721   7457  14569   1092    574   1731       C  
ATOM  11115  N   ASN H 237     107.817 -42.816  44.196  1.00 85.15           N  
ANISOU11115  N   ASN H 237     8644   8121  15590    999    461   1416       N  
ATOM  11116  CA  ASN H 237     108.751 -43.674  44.925  1.00 81.29           C  
ANISOU11116  CA  ASN H 237     8170   7558  15159    961    396   1304       C  
ATOM  11117  C   ASN H 237     108.942 -45.096  44.330  1.00 73.06           C  
ANISOU11117  C   ASN H 237     7077   6561  14120    908    304   1228       C  
ATOM  11118  O   ASN H 237     109.265 -46.033  45.076  1.00 69.07           O  
ANISOU11118  O   ASN H 237     6576   6010  13656    881    234   1161       O  
ATOM  11119  CB  ASN H 237     108.380 -43.757  46.407  1.00 82.89           C  
ANISOU11119  CB  ASN H 237     8409   7692  15394    981    380   1327       C  
ATOM  11120  CG  ASN H 237     109.574 -43.451  47.324  1.00 84.85           C  
ANISOU11120  CG  ASN H 237     8711   7828  15702    976    393   1245       C  
ATOM  11121  OD1 ASN H 237     110.679 -43.177  46.857  1.00 85.78           O  
ANISOU11121  OD1 ASN H 237     8838   7918  15837    959    414   1172       O  
ATOM  11122  ND2 ASN H 237     109.334 -43.501  48.635  1.00 85.58           N  
ANISOU11122  ND2 ASN H 237     8837   7854  15824    993    380   1260       N  
ATOM  11123  N   TYR H 238     108.677 -45.268  43.029  1.00 83.64           N  
ANISOU11123  N   TYR H 238     8370   7992  15416    896    301   1243       N  
ATOM  11124  CA  TYR H 238     108.715 -46.572  42.333  1.00 76.34           C  
ANISOU11124  CA  TYR H 238     7394   7125  14487    849    217   1184       C  
ATOM  11125  C   TYR H 238     109.776 -47.545  42.866  1.00 71.66           C  
ANISOU11125  C   TYR H 238     6810   6465  13952    804    146   1058       C  
ATOM  11126  O   TYR H 238     109.487 -48.722  43.048  1.00 67.40           O  
ANISOU11126  O   TYR H 238     6243   5944  13422    775     63   1028       O  
ATOM  11127  CB  TYR H 238     109.002 -46.338  40.834  1.00 76.39           C  
ANISOU11127  CB  TYR H 238     7367   7203  14456    838    244   1174       C  
ATOM  11128  CG  TYR H 238     110.280 -45.534  40.628  1.00 80.72           C  
ANISOU11128  CG  TYR H 238     7948   7694  15028    836    301   1110       C  
ATOM  11129  CD1 TYR H 238     110.353 -44.184  41.029  1.00 87.71           C  
ANISOU11129  CD1 TYR H 238     8879   8534  15914    879    391   1164       C  
ATOM  11130  CD2 TYR H 238     111.430 -46.107  40.088  1.00 78.22           C  
ANISOU11130  CD2 TYR H 238     7619   7365  14736    793    266    997       C  
ATOM  11131  CE1 TYR H 238     111.519 -43.418  40.901  1.00 92.15           C  
ANISOU11131  CE1 TYR H 238     9473   9040  16500    879    444   1107       C  
ATOM  11132  CE2 TYR H 238     112.620 -45.325  39.947  1.00 82.69           C  
ANISOU11132  CE2 TYR H 238     8218   7875  15327    793    321    940       C  
ATOM  11133  CZ  TYR H 238     112.638 -43.976  40.358  1.00 89.68           C  
ANISOU11133  CZ  TYR H 238     9148   8716  16212    837    410    997       C  
ATOM  11134  OH  TYR H 238     113.757 -43.177  40.247  1.00 94.47           O  
ANISOU11134  OH  TYR H 238     9786   9266  16841    839    466    947       O  
ATOM  11135  N   SER H 239     110.969 -47.061  43.182  1.00 77.36           N  
ANISOU11135  N   SER H 239     7572   7108  14714    799    177    985       N  
ATOM  11136  CA  SER H 239     112.038 -47.933  43.666  1.00 73.44           C  
ANISOU11136  CA  SER H 239     7084   6546  14273    757    113    863       C  
ATOM  11137  C   SER H 239     111.860 -48.373  45.129  1.00 72.68           C  
ANISOU11137  C   SER H 239     7018   6378  14218    760     72    855       C  
ATOM  11138  O   SER H 239     112.559 -49.288  45.607  1.00 68.97           O  
ANISOU11138  O   SER H 239     6552   5861  13794    724      5    760       O  
ATOM  11139  CB  SER H 239     113.397 -47.249  43.504  1.00 77.00           C  
ANISOU11139  CB  SER H 239     7568   6935  14754    750    161    788       C  
ATOM  11140  OG  SER H 239     113.775 -46.610  44.711  1.00 81.38           O  
ANISOU11140  OG  SER H 239     8180   7393  15349    774    195    784       O  
ATOM  11141  N   GLN H 240     110.926 -47.733  45.822  1.00 74.34           N  
ANISOU11141  N   GLN H 240     7251   6582  14414    804    111    955       N  
ATOM  11142  CA  GLN H 240     110.640 -48.029  47.219  1.00 74.37           C  
ANISOU11142  CA  GLN H 240     7284   6520  14452    815     81    963       C  
ATOM  11143  C   GLN H 240     109.235 -48.604  47.339  1.00 71.90           C  
ANISOU11143  C   GLN H 240     6939   6273  14107    825     41   1048       C  
ATOM  11144  O   GLN H 240     109.007 -49.681  47.906  1.00 69.99           O  
ANISOU11144  O   GLN H 240     6684   6023  13886    802    -36   1018       O  
ATOM  11145  CB  GLN H 240     110.785 -46.785  48.069  1.00 81.79           C  
ANISOU11145  CB  GLN H 240     8282   7386  15407    858    159   1004       C  
ATOM  11146  CG  GLN H 240     112.206 -46.293  48.164  1.00 84.48           C  
ANISOU11146  CG  GLN H 240     8660   7651  15789    847    191    914       C  
ATOM  11147  CD  GLN H 240     112.945 -46.925  49.311  1.00 82.30           C  
ANISOU11147  CD  GLN H 240     8414   7282  15575    825    138    827       C  
ATOM  11148  OE1 GLN H 240     112.332 -47.415  50.260  1.00 78.20           O  
ANISOU11148  OE1 GLN H 240     7902   6741  15068    832     98    852       O  
ATOM  11149  NE2 GLN H 240     114.272 -46.924  49.233  1.00 85.22           N  
ANISOU11149  NE2 GLN H 240     8802   7595  15983    799    137    723       N  
ATOM  11150  N   VAL H 241     108.268 -47.831  46.867  1.00 75.41           N  
ANISOU11150  N   VAL H 241     7374   6779  14501    862     98   1158       N  
ATOM  11151  CA  VAL H 241     106.926 -48.348  46.715  1.00 73.07           C  
ANISOU11151  CA  VAL H 241     7038   6559  14165    871     65   1241       C  
ATOM  11152  C   VAL H 241     106.790 -48.899  45.297  1.00 68.74           C  
ANISOU11152  C   VAL H 241     6432   6107  13579    842     36   1229       C  
ATOM  11153  O   VAL H 241     106.718 -48.112  44.330  1.00 71.62           O  
ANISOU11153  O   VAL H 241     6786   6521  13904    858     97   1270       O  
ATOM  11154  CB  VAL H 241     105.896 -47.253  46.979  1.00 79.21           C  
ANISOU11154  CB  VAL H 241     7835   7354  14908    927    139   1369       C  
ATOM  11155  CG1 VAL H 241     104.473 -47.803  46.846  1.00 77.19           C  
ANISOU11155  CG1 VAL H 241     7538   7178  14613    935    103   1458       C  
ATOM  11156  CG2 VAL H 241     106.144 -46.657  48.353  1.00 83.37           C  
ANISOU11156  CG2 VAL H 241     8421   7781  15474    954    170   1374       C  
ATOM  11157  N   ASP H 242     106.708 -50.234  45.173  1.00 80.19           N  
ANISOU11157  N   ASP H 242     7844   7585  15038    801    -55   1177       N  
ATOM  11158  CA  ASP H 242     106.716 -50.845  43.845  1.00 75.90           C  
ANISOU11158  CA  ASP H 242     7247   7128  14465    770    -88   1151       C  
ATOM  11159  C   ASP H 242     105.286 -50.982  43.306  1.00 75.20           C  
ANISOU11159  C   ASP H 242     7117   7137  14320    788    -94   1258       C  
ATOM  11160  O   ASP H 242     104.618 -51.992  43.502  1.00 71.01           O  
ANISOU11160  O   ASP H 242     6555   6637  13787    771   -165   1266       O  
ATOM  11161  CB  ASP H 242     107.389 -52.209  43.944  1.00 69.38           C  
ANISOU11161  CB  ASP H 242     6402   6284  13677    716   -183   1039       C  
ATOM  11162  CG  ASP H 242     107.509 -52.900  42.610  1.00 64.89           C  
ANISOU11162  CG  ASP H 242     5779   5797  13081    681   -223   1000       C  
ATOM  11163  OD1 ASP H 242     107.680 -52.180  41.596  1.00 67.35           O  
ANISOU11163  OD1 ASP H 242     6081   6150  13358    691   -166   1019       O  
ATOM  11164  OD2 ASP H 242     107.451 -54.167  42.583  1.00 63.64           O  
ANISOU11164  OD2 ASP H 242     5588   5658  12934    643   -310    949       O  
ATOM  11165  N   ILE H 243     104.876 -49.958  42.552  1.00 70.76           N  
ANISOU11165  N   ILE H 243     6550   6624  13712    820    -18   1335       N  
ATOM  11166  CA  ILE H 243     103.475 -49.741  42.192  1.00 71.38           C  
ANISOU11166  CA  ILE H 243     6601   6784  13737    849     -1   1455       C  
ATOM  11167  C   ILE H 243     103.294 -48.949  40.884  1.00 72.23           C  
ANISOU11167  C   ILE H 243     6687   6966  13791    865     62   1504       C  
ATOM  11168  O   ILE H 243     103.902 -47.913  40.711  1.00 73.78           O  
ANISOU11168  O   ILE H 243     6913   7131  13988    884    135   1502       O  
ATOM  11169  CB  ILE H 243     102.745 -48.998  43.333  1.00 73.25           C  
ANISOU11169  CB  ILE H 243     6878   6978  13977    897     43   1544       C  
ATOM  11170  CG1 ILE H 243     102.411 -49.960  44.484  1.00 72.11           C  
ANISOU11170  CG1 ILE H 243     6737   6793  13867    884    -30   1528       C  
ATOM  11171  CG2 ILE H 243     101.495 -48.306  42.812  1.00 75.10           C  
ANISOU11171  CG2 ILE H 243     7093   7290  14152    937     95   1673       C  
ATOM  11172  CD1 ILE H 243     101.606 -51.147  44.069  1.00 70.58           C  
ANISOU11172  CD1 ILE H 243     6489   6676  13654    859   -110   1540       C  
ATOM  11173  N   GLY H 244     102.460 -49.423  39.969  1.00 72.22           N  
ANISOU11173  N   GLY H 244     7074   6899  13469    458   -714   1916       N  
ATOM  11174  CA  GLY H 244     102.007 -48.600  38.859  1.00 75.12           C  
ANISOU11174  CA  GLY H 244     7405   7308  13831    443   -762   1918       C  
ATOM  11175  C   GLY H 244     100.520 -48.252  38.898  1.00 77.92           C  
ANISOU11175  C   GLY H 244     7750   7669  14187    442   -770   1861       C  
ATOM  11176  O   GLY H 244      99.770 -48.770  39.740  1.00 77.28           O  
ANISOU11176  O   GLY H 244     7689   7562  14111    451   -730   1815       O  
ATOM  11177  N   LEU H 245     100.071 -47.416  37.960  1.00 72.13           N  
ANISOU11177  N   LEU H 245     6986   6971  13451    430   -818   1863       N  
ATOM  11178  CA  LEU H 245      98.631 -47.291  37.692  1.00 74.07           C  
ANISOU11178  CA  LEU H 245     7216   7234  13695    423   -815   1804       C  
ATOM  11179  C   LEU H 245      98.367 -47.353  36.199  1.00 73.52           C  
ANISOU11179  C   LEU H 245     7106   7218  13611    398   -813   1796       C  
ATOM  11180  O   LEU H 245      99.052 -46.685  35.408  1.00 75.81           O  
ANISOU11180  O   LEU H 245     7375   7531  13897    391   -861   1843       O  
ATOM  11181  CB  LEU H 245      98.057 -45.999  38.269  1.00 80.87           C  
ANISOU11181  CB  LEU H 245     8081   8077  14568    438   -884   1807       C  
ATOM  11182  CG  LEU H 245      97.518 -46.149  39.684  1.00 81.37           C  
ANISOU11182  CG  LEU H 245     8179   8094  14644    459   -867   1776       C  
ATOM  11183  CD1 LEU H 245      96.598 -45.014  40.035  1.00 88.21           C  
ANISOU11183  CD1 LEU H 245     9043   8952  15519    468   -925   1760       C  
ATOM  11184  CD2 LEU H 245      96.796 -47.447  39.767  1.00 77.90           C  
ANISOU11184  CD2 LEU H 245     7744   7655  14199    451   -783   1716       C  
ATOM  11185  N   ILE H 246      97.393 -48.165  35.808  1.00 77.61           N  
ANISOU11185  N   ILE H 246     7612   7754  14121    385   -758   1737       N  
ATOM  11186  CA  ILE H 246      96.994 -48.200  34.413  1.00 77.46           C  
ANISOU11186  CA  ILE H 246     7555   7787  14089    362   -757   1722       C  
ATOM  11187  C   ILE H 246      95.655 -47.495  34.200  1.00 81.80           C  
ANISOU11187  C   ILE H 246     8088   8351  14642    359   -789   1681       C  
ATOM  11188  O   ILE H 246      94.683 -47.754  34.916  1.00 81.24           O  
ANISOU11188  O   ILE H 246     8030   8260  14577    366   -763   1631       O  
ATOM  11189  CB  ILE H 246      96.892 -49.621  33.899  1.00 71.04           C  
ANISOU11189  CB  ILE H 246     6736   6992  13264    346   -674   1688       C  
ATOM  11190  CG1 ILE H 246      98.279 -50.254  33.818  1.00 66.21           C  
ANISOU11190  CG1 ILE H 246     6134   6376  12648    344   -649   1734       C  
ATOM  11191  CG2 ILE H 246      96.279 -49.623  32.533  1.00 71.45           C  
ANISOU11191  CG2 ILE H 246     6749   7096  13304    323   -674   1665       C  
ATOM  11192  CD1 ILE H 246      98.275 -51.707  33.271  1.00 65.92           C  
ANISOU11192  CD1 ILE H 246     6090   6358  12597    328   -565   1703       C  
ATOM  11193  N   LYS H 247      95.600 -46.589  33.225  1.00 78.32           N  
ANISOU11193  N   LYS H 247     7616   7945  14196    349   -845   1701       N  
ATOM  11194  CA  LYS H 247      94.328 -46.019  32.813  1.00 82.06           C  
ANISOU11194  CA  LYS H 247     8069   8441  14670    342   -870   1660       C  
ATOM  11195  C   LYS H 247      93.861 -46.685  31.521  1.00 79.26           C  
ANISOU11195  C   LYS H 247     7682   8134  14300    317   -831   1628       C  
ATOM  11196  O   LYS H 247      94.595 -46.709  30.531  1.00 78.55           O  
ANISOU11196  O   LYS H 247     7572   8075  14200    304   -839   1662       O  
ATOM  11197  CB  LYS H 247      94.434 -44.502  32.627  1.00 89.04           C  
ANISOU11197  CB  LYS H 247     8940   9330  15560    348   -960   1699       C  
ATOM  11198  CG  LYS H 247      93.096 -43.839  32.288  1.00 93.53           C  
ANISOU11198  CG  LYS H 247     9489   9918  16130    343   -990   1657       C  
ATOM  11199  CD  LYS H 247      93.222 -42.336  32.177  1.00100.34           C  
ANISOU11199  CD  LYS H 247    10341  10783  16999    351  -1079   1696       C  
ATOM  11200  CE  LYS H 247      91.909 -41.675  31.832  1.00104.90           C  
ANISOU11200  CE  LYS H 247    10900  11381  17578    346  -1109   1655       C  
ATOM  11201  NZ  LYS H 247      92.027 -40.197  31.955  1.00111.63           N  
ANISOU11201  NZ  LYS H 247    11748  12227  18439    357  -1196   1693       N  
ATOM  11202  N   LEU H 248      92.642 -47.232  31.546  1.00 84.70           N  
ANISOU11202  N   LEU H 248     8366   8828  14987    311   -789   1563       N  
ATOM  11203  CA  LEU H 248      92.006 -47.807  30.355  1.00 82.98           C  
ANISOU11203  CA  LEU H 248     8117   8656  14755    288   -754   1525       C  
ATOM  11204  C   LEU H 248      91.342 -46.722  29.490  1.00 88.64           C  
ANISOU11204  C   LEU H 248     8802   9407  15470    279   -816   1523       C  
ATOM  11205  O   LEU H 248      90.668 -45.819  30.008  1.00 93.52           O  
ANISOU11205  O   LEU H 248     9425  10011  16098    291   -862   1512       O  
ATOM  11206  CB  LEU H 248      90.973 -48.868  30.756  1.00 79.57           C  
ANISOU11206  CB  LEU H 248     7694   8215  14323    285   -682   1455       C  
ATOM  11207  CG  LEU H 248      91.480 -50.092  31.519  1.00 73.40           C  
ANISOU11207  CG  LEU H 248     6943   7404  13543    291   -611   1448       C  
ATOM  11208  CD1 LEU H 248      90.341 -51.002  31.904  1.00 71.64           C  
ANISOU11208  CD1 LEU H 248     6727   7173  13320    289   -547   1377       C  
ATOM  11209  CD2 LEU H 248      92.504 -50.855  30.688  1.00 68.73           C  
ANISOU11209  CD2 LEU H 248     6341   6836  12938    277   -578   1477       C  
ATOM  11210  N   LYS H 249      91.528 -46.839  28.174  1.00 84.93           N  
ANISOU11210  N   LYS H 249     8301   8983  14987    259   -815   1531       N  
ATOM  11211  CA  LYS H 249      91.100 -45.847  27.187  1.00 90.13           C  
ANISOU11211  CA  LYS H 249     8927   9679  15641    249   -873   1538       C  
ATOM  11212  C   LYS H 249      89.650 -45.434  27.397  1.00 93.51           C  
ANISOU11212  C   LYS H 249     9349  10108  16074    251   -885   1483       C  
ATOM  11213  O   LYS H 249      89.285 -44.284  27.212  1.00 98.91           O  
ANISOU11213  O   LYS H 249    10020  10800  16762    254   -951   1494       O  
ATOM  11214  CB  LYS H 249      91.291 -46.405  25.770  1.00 87.96           C  
ANISOU11214  CB  LYS H 249     8619   9452  15348    225   -847   1537       C  
ATOM  11215  CG  LYS H 249      91.334 -45.364  24.671  1.00 93.19           C  
ANISOU11215  CG  LYS H 249     9249  10154  16005    215   -912   1565       C  
ATOM  11216  CD  LYS H 249      92.018 -45.911  23.425  1.00 90.92           C  
ANISOU11216  CD  LYS H 249     8937   9906  15701    196   -890   1586       C  
ATOM  11217  CE  LYS H 249      93.513 -46.088  23.646  1.00 89.08           C  
ANISOU11217  CE  LYS H 249     8720   9657  15468    202   -890   1647       C  
ATOM  11218  NZ  LYS H 249      94.127 -46.799  22.495  1.00 86.93           N  
ANISOU11218  NZ  LYS H 249     8427   9423  15181    183   -856   1660       N  
ATOM  11219  N   GLN H 250      88.836 -46.386  27.810  1.00 87.91           N  
ANISOU11219  N   GLN H 250     8649   9387  15364    249   -822   1425       N  
ATOM  11220  CA  GLN H 250      87.464 -46.110  28.182  1.00 91.08           C  
ANISOU11220  CA  GLN H 250     9051   9784  15773    253   -826   1371       C  
ATOM  11221  C   GLN H 250      87.145 -46.913  29.444  1.00 87.94           C  
ANISOU11221  C   GLN H 250     8687   9343  15384    266   -772   1336       C  
ATOM  11222  O   GLN H 250      88.006 -47.622  29.965  1.00 83.96           O  
ANISOU11222  O   GLN H 250     8205   8815  14880    272   -735   1356       O  
ATOM  11223  CB  GLN H 250      86.522 -46.471  27.037  1.00 91.07           C  
ANISOU11223  CB  GLN H 250     9016   9828  15759    231   -802   1324       C  
ATOM  11224  CG  GLN H 250      86.891 -47.807  26.385  1.00 86.16           C  
ANISOU11224  CG  GLN H 250     8387   9227  15124    214   -729   1311       C  
ATOM  11225  CD  GLN H 250      85.873 -48.275  25.365  1.00 86.20           C  
ANISOU11225  CD  GLN H 250     8361   9273  15118    193   -698   1259       C  
ATOM  11226  OE1 GLN H 250      84.687 -47.937  25.456  1.00 89.75           O  
ANISOU11226  OE1 GLN H 250     8803   9726  15572    194   -708   1214       O  
ATOM  11227  NE2 GLN H 250      86.332 -49.056  24.381  1.00 82.48           N  
ANISOU11227  NE2 GLN H 250     7872   8834  14633    176   -660   1263       N  
ATOM  11228  N   LYS H 251      85.923 -46.804  29.949  1.00 84.88           N  
ANISOU11228  N   LYS H 251     8303   8943  15003    271   -766   1284       N  
ATOM  11229  CA  LYS H 251      85.539 -47.629  31.084  1.00 81.82           C  
ANISOU11229  CA  LYS H 251     7946   8518  14623    283   -710   1247       C  
ATOM  11230  C   LYS H 251      85.215 -49.027  30.567  1.00 76.54           C  
ANISOU11230  C   LYS H 251     7270   7869  13944    266   -628   1202       C  
ATOM  11231  O   LYS H 251      84.810 -49.162  29.411  1.00 76.62           O  
ANISOU11231  O   LYS H 251     7249   7922  13943    246   -622   1184       O  
ATOM  11232  CB  LYS H 251      84.349 -47.015  31.817  1.00 86.29           C  
ANISOU11232  CB  LYS H 251     8521   9065  15201    295   -734   1207       C  
ATOM  11233  CG  LYS H 251      84.604 -45.633  32.367  1.00 92.21           C  
ANISOU11233  CG  LYS H 251     9280   9794  15962    312   -815   1248       C  
ATOM  11234  CD  LYS H 251      83.730 -45.365  33.572  1.00 96.15           C  
ANISOU11234  CD  LYS H 251     9802  10255  16475    330   -819   1214       C  
ATOM  11235  CE  LYS H 251      82.283 -45.120  33.171  1.00 97.12           C  
ANISOU11235  CE  LYS H 251     9904  10401  16597    322   -823   1158       C  
ATOM  11236  NZ  LYS H 251      81.388 -45.068  34.358  1.00 99.52           N  
ANISOU11236  NZ  LYS H 251    10233  10667  16914    338   -814   1118       N  
ATOM  11237  N   VAL H 252      85.408 -50.060  31.392  1.00 82.74           N  
ANISOU11237  N   VAL H 252     8082   8623  14732    273   -565   1186       N  
ATOM  11238  CA  VAL H 252      85.052 -51.435  31.003  1.00 78.00           C  
ANISOU11238  CA  VAL H 252     7476   8037  14122    257   -483   1140       C  
ATOM  11239  C   VAL H 252      83.694 -51.841  31.609  1.00 78.79           C  
ANISOU11239  C   VAL H 252     7584   8123  14228    261   -446   1071       C  
ATOM  11240  O   VAL H 252      83.399 -51.501  32.754  1.00 80.38           O  
ANISOU11240  O   VAL H 252     7812   8286  14444    280   -459   1064       O  
ATOM  11241  CB  VAL H 252      86.136 -52.456  31.432  1.00 72.02           C  
ANISOU11241  CB  VAL H 252     6743   7260  13363    261   -430   1163       C  
ATOM  11242  CG1 VAL H 252      86.306 -52.481  32.947  1.00 71.75           C  
ANISOU11242  CG1 VAL H 252     6748   7170  13343    285   -424   1167       C  
ATOM  11243  CG2 VAL H 252      85.808 -53.855  30.902  1.00 67.00           C  
ANISOU11243  CG2 VAL H 252     6098   6642  12716    243   -347   1118       C  
ATOM  11244  N   SER H 253      82.853 -52.542  30.853  1.00 77.98           N  
ANISOU11244  N   SER H 253     7460   8051  14117    242   -401   1020       N  
ATOM  11245  CA  SER H 253      81.540 -52.907  31.374  1.00 79.11           C  
ANISOU11245  CA  SER H 253     7610   8183  14267    244   -367    954       C  
ATOM  11246  C   SER H 253      81.681 -53.963  32.453  1.00 74.84           C  
ANISOU11246  C   SER H 253     7102   7601  13731    255   -301    934       C  
ATOM  11247  O   SER H 253      82.266 -55.027  32.223  1.00 69.78           O  
ANISOU11247  O   SER H 253     6465   6965  13083    247   -244    936       O  
ATOM  11248  CB  SER H 253      80.638 -53.403  30.252  1.00 79.09           C  
ANISOU11248  CB  SER H 253     7574   8224  14253    221   -336    905       C  
ATOM  11249  OG  SER H 253      81.347 -53.377  29.030  1.00 77.21           O  
ANISOU11249  OG  SER H 253     7310   8025  14002    205   -349    939       O  
ATOM  11250  N   VAL H 254      81.156 -53.670  33.634  1.00 75.71           N  
ANISOU11250  N   VAL H 254     7238   7674  13856    274   -309    916       N  
ATOM  11251  CA  VAL H 254      81.217 -54.607  34.753  1.00 72.29           C  
ANISOU11251  CA  VAL H 254     6839   7200  13429    286   -249    896       C  
ATOM  11252  C   VAL H 254      80.193 -55.752  34.608  1.00 72.14           C  
ANISOU11252  C   VAL H 254     6814   7190  13407    274   -174    827       C  
ATOM  11253  O   VAL H 254      79.058 -55.514  34.195  1.00 73.77           O  
ANISOU11253  O   VAL H 254     7001   7417  13613    265   -181    784       O  
ATOM  11254  CB  VAL H 254      80.977 -53.861  36.081  1.00 75.92           C  
ANISOU11254  CB  VAL H 254     7327   7614  13905    311   -285    900       C  
ATOM  11255  CG1 VAL H 254      80.888 -54.830  37.244  1.00 73.88           C  
ANISOU11255  CG1 VAL H 254     7103   7314  13653    324   -222    873       C  
ATOM  11256  CG2 VAL H 254      82.056 -52.863  36.312  1.00 77.30           C  
ANISOU11256  CG2 VAL H 254     7511   7776  14083    324   -352    969       C  
ATOM  11257  N   ASN H 255      80.591 -56.985  34.924  1.00 80.70           N  
ANISOU11257  N   ASN H 255     7915   8259  14487    272   -103    816       N  
ATOM  11258  CA  ASN H 255      79.659 -58.126  35.018  1.00 78.96           C  
ANISOU11258  CA  ASN H 255     7696   8039  14266    264    -27    750       C  
ATOM  11259  C   ASN H 255      80.223 -59.233  35.908  1.00 74.11           C  
ANISOU11259  C   ASN H 255     7115   7390  13655    273     38    748       C  
ATOM  11260  O   ASN H 255      81.160 -59.012  36.668  1.00 73.47           O  
ANISOU11260  O   ASN H 255     7058   7277  13579    290     21    792       O  
ATOM  11261  CB  ASN H 255      79.309 -58.690  33.643  1.00 77.85           C  
ANISOU11261  CB  ASN H 255     7520   7948  14111    238      2    724       C  
ATOM  11262  CG  ASN H 255      80.522 -59.081  32.862  1.00 74.03           C  
ANISOU11262  CG  ASN H 255     7027   7485  13615    227     11    769       C  
ATOM  11263  OD1 ASN H 255      81.170 -60.089  33.164  1.00 68.95           O  
ANISOU11263  OD1 ASN H 255     6401   6827  12969    227     67    774       O  
ATOM  11264  ND2 ASN H 255      80.858 -58.282  31.852  1.00 76.60           N  
ANISOU11264  ND2 ASN H 255     7326   7846  13934    217    -43    802       N  
ATOM  11265  N   GLU H 256      79.642 -60.420  35.850  1.00 82.65           N  
ANISOU11265  N   GLU H 256     8196   8475  14733    263    112    697       N  
ATOM  11266  CA  GLU H 256      80.071 -61.467  36.765  1.00 78.35           C  
ANISOU11266  CA  GLU H 256     7683   7894  14191    273    175    691       C  
ATOM  11267  C   GLU H 256      81.571 -61.814  36.614  1.00 73.40           C  
ANISOU11267  C   GLU H 256     7065   7265  13558    273    183    748       C  
ATOM  11268  O   GLU H 256      82.228 -62.157  37.607  1.00 70.68           O  
ANISOU11268  O   GLU H 256     6753   6883  13221    289    203    767       O  
ATOM  11269  CB  GLU H 256      79.188 -62.717  36.593  1.00 76.27           C  
ANISOU11269  CB  GLU H 256     7415   7640  13925    260    256    625       C  
ATOM  11270  CG  GLU H 256      79.484 -63.631  35.402  1.00 73.80           C  
ANISOU11270  CG  GLU H 256     7078   7366  13596    236    301    619       C  
ATOM  11271  CD  GLU H 256      78.639 -63.345  34.160  1.00 76.32           C  
ANISOU11271  CD  GLU H 256     7357   7734  13907    215    285    590       C  
ATOM  11272  OE1 GLU H 256      77.615 -62.604  34.243  1.00 79.10           O  
ANISOU11272  OE1 GLU H 256     7700   8089  14266    218    250    562       O  
ATOM  11273  OE2 GLU H 256      79.011 -63.873  33.084  1.00 75.66           O  
ANISOU11273  OE2 GLU H 256     7252   7686  13811    196    307    595       O  
ATOM  11274  N   ARG H 257      82.119 -61.756  35.397  1.00 80.03           N  
ANISOU11274  N   ARG H 257     7877   8145  14385    255    169    774       N  
ATOM  11275  CA  ARG H 257      83.524 -62.138  35.217  1.00 75.61           C  
ANISOU11275  CA  ARG H 257     7325   7585  13819    255    179    827       C  
ATOM  11276  C   ARG H 257      84.523 -60.958  35.232  1.00 77.48           C  
ANISOU11276  C   ARG H 257     7563   7817  14057    265    101    896       C  
ATOM  11277  O   ARG H 257      85.742 -61.155  35.390  1.00 74.54           O  
ANISOU11277  O   ARG H 257     7204   7433  13683    270    104    944       O  
ATOM  11278  CB  ARG H 257      83.673 -62.925  33.911  1.00 72.89           C  
ANISOU11278  CB  ARG H 257     6952   7285  13458    230    218    817       C  
ATOM  11279  CG  ARG H 257      83.343 -62.113  32.672  1.00 76.54           C  
ANISOU11279  CG  ARG H 257     7376   7793  13912    214    167    823       C  
ATOM  11280  CD  ARG H 257      83.010 -62.971  31.461  1.00 74.59           C  
ANISOU11280  CD  ARG H 257     7099   7589  13651    189    214    791       C  
ATOM  11281  NE  ARG H 257      81.822 -63.793  31.669  1.00 73.31           N  
ANISOU11281  NE  ARG H 257     6938   7424  13491    183    273    720       N  
ATOM  11282  CZ  ARG H 257      81.865 -65.101  31.962  1.00 70.49           C  
ANISOU11282  CZ  ARG H 257     6596   7056  13132    180    351    692       C  
ATOM  11283  NH1 ARG H 257      83.046 -65.706  32.079  1.00 68.62           N  
ANISOU11283  NH1 ARG H 257     6374   6808  12891    182    378    730       N  
ATOM  11284  NH2 ARG H 257      80.740 -65.814  32.146  1.00 69.72           N  
ANISOU11284  NH2 ARG H 257     6498   6956  13037    175    403    627       N  
ATOM  11285  N   VAL H 258      84.009 -59.735  35.111  1.00 70.79           N  
ANISOU11285  N   VAL H 258     6703   6978  13215    269     33    901       N  
ATOM  11286  CA  VAL H 258      84.864 -58.546  35.033  1.00 70.74           C  
ANISOU11286  CA  VAL H 258     6695   6971  13211    277    -45    965       C  
ATOM  11287  C   VAL H 258      84.324 -57.493  35.968  1.00 70.69           C  
ANISOU11287  C   VAL H 258     6704   6936  13220    297    -98    964       C  
ATOM  11288  O   VAL H 258      83.260 -56.972  35.720  1.00 71.84           O  
ANISOU11288  O   VAL H 258     6833   7096  13367    293   -122    930       O  
ATOM  11289  CB  VAL H 258      84.908 -57.948  33.602  1.00 70.84           C  
ANISOU11289  CB  VAL H 258     6668   7035  13213    258    -87    983       C  
ATOM  11290  CG1 VAL H 258      85.617 -56.596  33.588  1.00 70.79           C  
ANISOU11290  CG1 VAL H 258     6660   7027  13211    268   -173   1044       C  
ATOM  11291  CG2 VAL H 258      85.527 -58.919  32.623  1.00 70.88           C  
ANISOU11291  CG2 VAL H 258     6658   7071  13204    239    -39    989       C  
ATOM  11292  N   MET H 259      85.070 -57.131  36.996  1.00 67.04           N  
ANISOU11292  N   MET H 259     6271   6434  12767    318   -121   1002       N  
ATOM  11293  CA  MET H 259      84.532 -56.229  37.988  1.00 66.99           C  
ANISOU11293  CA  MET H 259     6283   6396  12775    338   -166    997       C  
ATOM  11294  C   MET H 259      85.548 -55.807  39.048  1.00 66.86           C  
ANISOU11294  C   MET H 259     6298   6337  12767    360   -195   1049       C  
ATOM  11295  O   MET H 259      86.358 -56.599  39.479  1.00 66.78           O  
ANISOU11295  O   MET H 259     6310   6308  12757    365   -153   1065       O  
ATOM  11296  CB  MET H 259      83.319 -56.884  38.629  1.00 67.02           C  
ANISOU11296  CB  MET H 259     6297   6382  12784    341   -114    930       C  
ATOM  11297  CG  MET H 259      83.540 -57.499  39.946  1.00 66.91           C  
ANISOU11297  CG  MET H 259     6323   6321  12780    359    -73    923       C  
ATOM  11298  SD  MET H 259      82.014 -57.370  40.875  1.00 66.93           S  
ANISOU11298  SD  MET H 259     6338   6299  12794    371    -63    859       S  
ATOM  11299  CE  MET H 259      82.740 -56.855  42.403  1.00 67.01           C  
ANISOU11299  CE  MET H 259     6391   6252  12818    401    -93    900       C  
ATOM  11300  N   PRO H 260      85.527 -54.529  39.448  1.00 66.41           N  
ANISOU11300  N   PRO H 260     6246   6268  12720    374   -268   1075       N  
ATOM  11301  CA  PRO H 260      86.610 -54.016  40.293  1.00 66.29           C  
ANISOU11301  CA  PRO H 260     6258   6218  12713    394   -304   1132       C  
ATOM  11302  C   PRO H 260      86.561 -54.515  41.730  1.00 66.20           C  
ANISOU11302  C   PRO H 260     6285   6155  12712    415   -268   1116       C  
ATOM  11303  O   PRO H 260      85.513 -54.956  42.189  1.00 66.22           O  
ANISOU11303  O   PRO H 260     6296   6147  12719    417   -231   1060       O  
ATOM  11304  CB  PRO H 260      86.396 -52.493  40.245  1.00 71.72           C  
ANISOU11304  CB  PRO H 260     6934   6909  13406    402   -393   1156       C  
ATOM  11305  CG  PRO H 260      84.951 -52.326  39.958  1.00 74.87           C  
ANISOU11305  CG  PRO H 260     7316   7326  13807    394   -392   1099       C  
ATOM  11306  CD  PRO H 260      84.606 -53.453  39.033  1.00 70.64           C  
ANISOU11306  CD  PRO H 260     6759   6823  13258    371   -326   1060       C  
ATOM  11307  N   ILE H 261      87.680 -54.385  42.432  1.00 68.03           N  
ANISOU11307  N   ILE H 261     6543   6357  12949    430   -283   1165       N  
ATOM  11308  CA  ILE H 261      87.818 -54.815  43.816  1.00 67.93           C  
ANISOU11308  CA  ILE H 261     6570   6295  12946    451   -253   1159       C  
ATOM  11309  C   ILE H 261      87.755 -53.584  44.707  1.00 67.87           C  
ANISOU11309  C   ILE H 261     6579   6257  12951    473   -322   1182       C  
ATOM  11310  O   ILE H 261      88.033 -52.495  44.244  1.00 67.88           O  
ANISOU11310  O   ILE H 261     6565   6274  12953    473   -391   1218       O  
ATOM  11311  CB  ILE H 261      89.156 -55.576  44.044  1.00 67.85           C  
ANISOU11311  CB  ILE H 261     6578   6269  12932    454   -218   1199       C  
ATOM  11312  CG1 ILE H 261      89.102 -56.405  45.328  1.00 67.77           C  
ANISOU11312  CG1 ILE H 261     6605   6214  12929    471   -163   1176       C  
ATOM  11313  CG2 ILE H 261      90.336 -54.616  44.092  1.00 67.78           C  
ANISOU11313  CG2 ILE H 261     6573   6254  12926    464   -285   1271       C  
ATOM  11314  CD1 ILE H 261      90.385 -57.029  45.704  1.00 67.68           C  
ANISOU11314  CD1 ILE H 261     6616   6183  12916    477   -135   1217       C  
ATOM  11315  N   CYS H 262      87.319 -53.725  45.954  1.00 67.30           N  
ANISOU11315  N   CYS H 262     6537   6143  12890    492   -304   1158       N  
ATOM  11316  CA  CYS H 262      87.232 -52.566  46.850  1.00 71.90           C  
ANISOU11316  CA  CYS H 262     7138   6695  13486    514   -369   1177       C  
ATOM  11317  C   CYS H 262      88.554 -52.161  47.485  1.00 72.28           C  
ANISOU11317  C   CYS H 262     7210   6715  13540    531   -402   1241       C  
ATOM  11318  O   CYS H 262      89.285 -53.034  47.950  1.00 68.41           O  
ANISOU11318  O   CYS H 262     6741   6204  13048    536   -355   1252       O  
ATOM  11319  CB  CYS H 262      86.237 -52.841  47.959  1.00 74.07           C  
ANISOU11319  CB  CYS H 262     7437   6937  13771    529   -339   1127       C  
ATOM  11320  SG  CYS H 262      84.591 -52.459  47.442  1.00 77.89           S  
ANISOU11320  SG  CYS H 262     7894   7447  14255    518   -349   1066       S  
ATOM  11321  N   LEU H 263      88.863 -50.855  47.522  1.00 71.65           N  
ANISOU11321  N   LEU H 263     7126   6633  13466    540   -483   1283       N  
ATOM  11322  CA  LEU H 263      90.018 -50.388  48.304  1.00 71.54           C  
ANISOU11322  CA  LEU H 263     7138   6585  13459    559   -518   1340       C  
ATOM  11323  C   LEU H 263      89.571 -50.246  49.732  1.00 71.47           C  
ANISOU11323  C   LEU H 263     7164   6528  13463    583   -517   1321       C  
ATOM  11324  O   LEU H 263      88.489 -49.745  49.992  1.00 71.51           O  
ANISOU11324  O   LEU H 263     7166   6530  13473    588   -536   1286       O  
ATOM  11325  CB  LEU H 263      90.572 -49.064  47.814  1.00 71.54           C  
ANISOU11325  CB  LEU H 263     7122   6600  13461    560   -604   1394       C  
ATOM  11326  CG  LEU H 263      91.010 -48.934  46.369  1.00 71.62           C  
ANISOU11326  CG  LEU H 263     7096   6658  13458    537   -621   1419       C  
ATOM  11327  CD1 LEU H 263      89.814 -48.523  45.525  1.00 71.73           C  
ANISOU11327  CD1 LEU H 263     7078   6709  13469    522   -638   1379       C  
ATOM  11328  CD2 LEU H 263      92.104 -47.905  46.312  1.00 71.57           C  
ANISOU11328  CD2 LEU H 263     7089   6648  13455    545   -693   1488       C  
ATOM  11329  N   PRO H 264      90.378 -50.732  50.663  1.00 74.60           N  
ANISOU11329  N   PRO H 264     6408   7652  14283   1172   -444    785       N  
ATOM  11330  CA  PRO H 264      89.987 -50.841  52.060  1.00 75.59           C  
ANISOU11330  CA  PRO H 264     6565   7741  14414   1196   -428    733       C  
ATOM  11331  C   PRO H 264      90.050 -49.541  52.803  1.00 78.29           C  
ANISOU11331  C   PRO H 264     6920   8068  14757   1200   -481    724       C  
ATOM  11332  O   PRO H 264      90.997 -48.790  52.628  1.00 78.83           O  
ANISOU11332  O   PRO H 264     7003   8139  14811   1197   -523    760       O  
ATOM  11333  CB  PRO H 264      91.019 -51.808  52.619  1.00 73.58           C  
ANISOU11333  CB  PRO H 264     6363   7459  14136   1221   -393    735       C  
ATOM  11334  CG  PRO H 264      92.249 -51.475  51.870  1.00 73.34           C  
ANISOU11334  CG  PRO H 264     6339   7442  14084   1213   -424    792       C  
ATOM  11335  CD  PRO H 264      91.778 -51.125  50.464  1.00 73.38           C  
ANISOU11335  CD  PRO H 264     6289   7491  14102   1181   -442    823       C  
ATOM  11336  N   SER H 265      89.051 -49.288  53.635  1.00 80.29           N  
ANISOU11336  N   SER H 265     7170   8307  15028   1207   -477    677       N  
ATOM  11337  CA  SER H 265      89.150 -48.219  54.609  1.00 86.92           C  
ANISOU11337  CA  SER H 265     8034   9125  15868   1217   -519    662       C  
ATOM  11338  C   SER H 265      90.046 -48.746  55.710  1.00 85.74           C  
ANISOU11338  C   SER H 265     7943   8938  15697   1246   -500    648       C  
ATOM  11339  O   SER H 265      91.095 -48.185  56.003  1.00 87.61           O  
ANISOU11339  O   SER H 265     8210   9162  15914   1252   -533    671       O  
ATOM  11340  CB  SER H 265      87.776 -47.818  55.160  1.00 91.57           C  
ANISOU11340  CB  SER H 265     8600   9711  16482   1217   -518    615       C  
ATOM  11341  OG  SER H 265      86.786 -47.772  54.144  1.00 90.96           O  
ANISOU11341  OG  SER H 265     8467   9670  16424   1192   -515    620       O  
ATOM  11342  N   LYS H 266      89.656 -49.884  56.264  1.00 91.37           N  
ANISOU11342  N   LYS H 266     8673   9632  16410   1262   -444    611       N  
ATOM  11343  CA  LYS H 266      90.442 -50.548  57.286  1.00 89.98           C  
ANISOU11343  CA  LYS H 266     8556   9420  16211   1289   -418    596       C  
ATOM  11344  C   LYS H 266      91.722 -51.074  56.647  1.00 84.09           C  
ANISOU11344  C   LYS H 266     7829   8681  15441   1289   -412    642       C  
ATOM  11345  O   LYS H 266      91.849 -51.088  55.425  1.00 80.74           O  
ANISOU11345  O   LYS H 266     7370   8288  15020   1269   -419    681       O  
ATOM  11346  CB  LYS H 266      89.649 -51.683  57.943  1.00 88.75           C  
ANISOU11346  CB  LYS H 266     8414   9245  16062   1305   -354    544       C  
ATOM  11347  CG  LYS H 266      90.103 -51.994  59.364  1.00 87.60           C  
ANISOU11347  CG  LYS H 266     8330   9057  15896   1333   -337    511       C  
ATOM  11348  CD  LYS H 266      89.879 -53.458  59.777  1.00 84.48           C  
ANISOU11348  CD  LYS H 266     7964   8642  15494   1350   -265    477       C  
ATOM  11349  CE  LYS H 266      88.394 -53.774  59.977  1.00 85.96           C  
ANISOU11349  CE  LYS H 266     8126   8832  15703   1345   -230    426       C  
ATOM  11350  NZ  LYS H 266      88.170 -54.965  60.854  1.00 83.68           N  
ANISOU11350  NZ  LYS H 266     7908   8530  15355   1343   -163    376       N  
ATOM  11351  N   ASP H 267      92.704 -51.436  57.459  1.00 90.29           N  
ANISOU11351  N   ASP H 267     8669   9438  16200   1311   -402    641       N  
ATOM  11352  CA  ASP H 267      93.881 -52.089  56.912  1.00 84.65           C  
ANISOU11352  CA  ASP H 267     7974   8727  15461   1314   -388    682       C  
ATOM  11353  C   ASP H 267      94.024 -53.519  57.416  1.00 79.24           C  
ANISOU11353  C   ASP H 267     7328   8018  14761   1335   -322    657       C  
ATOM  11354  O   ASP H 267      94.394 -53.729  58.574  1.00 80.36           O  
ANISOU11354  O   ASP H 267     7520   8127  14886   1357   -310    631       O  
ATOM  11355  CB  ASP H 267      95.121 -51.283  57.272  1.00 87.54           C  
ANISOU11355  CB  ASP H 267     8372   9086  15804   1318   -435    711       C  
ATOM  11356  CG  ASP H 267      96.399 -52.048  57.039  1.00 82.11           C  
ANISOU11356  CG  ASP H 267     7718   8395  15086   1328   -415    744       C  
ATOM  11357  OD1 ASP H 267      96.793 -52.196  55.857  1.00 77.80           O  
ANISOU11357  OD1 ASP H 267     7147   7876  14537   1312   -418    788       O  
ATOM  11358  OD2 ASP H 267      97.009 -52.488  58.043  1.00 82.35           O  
ANISOU11358  OD2 ASP H 267     7800   8395  15093   1350   -397    727       O  
ATOM  11359  N   TYR H 268      93.771 -54.519  56.576  1.00 85.07           N  
ANISOU11359  N   TYR H 268     8046   8771  15504   1329   -277    666       N  
ATOM  11360  CA  TYR H 268      94.068 -55.838  57.081  1.00 79.95           C  
ANISOU11360  CA  TYR H 268     7443   8097  14838   1351   -215    646       C  
ATOM  11361  C   TYR H 268      95.398 -56.280  56.494  1.00 75.16           C  
ANISOU11361  C   TYR H 268     6858   7497  14204   1354   -212    696       C  
ATOM  11362  O   TYR H 268      95.453 -57.085  55.570  1.00 70.29           O  
ANISOU11362  O   TYR H 268     6243   6907  13557   1333   -177    714       O  
ATOM  11363  CB  TYR H 268      92.984 -56.839  56.669  1.00 76.27           C  
ANISOU11363  CB  TYR H 268     6992   7663  14325   1314   -153    610       C  
ATOM  11364  CG  TYR H 268      91.581 -56.301  56.486  1.00 80.24           C  
ANISOU11364  CG  TYR H 268     7450   8187  14852   1292   -163    581       C  
ATOM  11365  CD1 TYR H 268      90.620 -56.497  57.463  1.00 82.49           C  
ANISOU11365  CD1 TYR H 268     7759   8458  15127   1293   -136    521       C  
ATOM  11366  CD2 TYR H 268      91.196 -55.643  55.315  1.00 81.76           C  
ANISOU11366  CD2 TYR H 268     7577   8414  15074   1270   -197    614       C  
ATOM  11367  CE1 TYR H 268      89.314 -56.019  57.303  1.00 86.37           C  
ANISOU11367  CE1 TYR H 268     8208   8968  15639   1273   -144    495       C  
ATOM  11368  CE2 TYR H 268      89.878 -55.158  55.144  1.00 85.56           C  
ANISOU11368  CE2 TYR H 268     8017   8916  15577   1250   -206    588       C  
ATOM  11369  CZ  TYR H 268      88.952 -55.356  56.148  1.00 87.82           C  
ANISOU11369  CZ  TYR H 268     8327   9187  15853   1252   -179    528       C  
ATOM  11370  OH  TYR H 268      87.664 -54.908  56.023  1.00 91.71           O  
ANISOU11370  OH  TYR H 268     8780   9699  16365   1233   -185    501       O  
ATOM  11371  N   ALA H 269      96.473 -55.820  57.118  1.00 82.12           N  
ANISOU11371  N   ALA H 269     7779   8363  15060   1365   -243    711       N  
ATOM  11372  CA  ALA H 269      97.824 -56.275  56.846  1.00 77.79           C  
ANISOU11372  CA  ALA H 269     7263   7814  14480   1373   -237    752       C  
ATOM  11373  C   ALA H 269      98.350 -57.035  58.036  1.00 77.33           C  
ANISOU11373  C   ALA H 269     7270   7718  14394   1400   -201    724       C  
ATOM  11374  O   ALA H 269      99.514 -57.399  58.061  1.00 74.96           O  
ANISOU11374  O   ALA H 269     7005   7412  14063   1410   -196    752       O  
ATOM  11375  CB  ALA H 269      98.732 -55.107  56.509  1.00 80.15           C  
ANISOU11375  CB  ALA H 269     7554   8130  14770   1361   -303    797       C  
ATOM  11376  N   GLU H 270      97.530 -57.181  59.065  1.00 80.61           N  
ANISOU11376  N   GLU H 270     7703   8108  14817   1412   -179    668       N  
ATOM  11377  CA  GLU H 270      98.004 -57.723  60.331  1.00 80.92           C  
ANISOU11377  CA  GLU H 270     7807   8110  14828   1437   -152    638       C  
ATOM  11378  C   GLU H 270      98.057 -59.244  60.322  1.00 74.72           C  
ANISOU11378  C   GLU H 270     7056   7311  14023   1449    -77    623       C  
ATOM  11379  O   GLU H 270      97.318 -59.880  59.573  1.00 71.30           O  
ANISOU11379  O   GLU H 270     6622   6913  13555   1413    -38    612       O  
ATOM  11380  CB  GLU H 270      97.120 -57.234  61.473  1.00 87.12           C  
ANISOU11380  CB  GLU H 270     8601   8875  15626   1443   -160    583       C  
ATOM  11381  CG  GLU H 270      96.907 -55.733  61.461  1.00 92.52           C  
ANISOU11381  CG  GLU H 270     9250   9574  16328   1429   -230    593       C  
ATOM  11382  CD  GLU H 270      96.465 -55.191  62.803  1.00 99.06           C  
ANISOU11382  CD  GLU H 270    10104  10377  17158   1441   -243    547       C  
ATOM  11383  OE1 GLU H 270      97.005 -55.658  63.836  1.00 99.73           O  
ANISOU11383  OE1 GLU H 270    10245  10433  17214   1462   -222    526       O  
ATOM  11384  OE2 GLU H 270      95.582 -54.300  62.815  1.00103.69           O  
ANISOU11384  OE2 GLU H 270    10654  10972  17772   1430   -275    532       O  
ATOM  11385  N   VAL H 271      98.939 -59.834  61.129  1.00 82.48           N  
ANISOU11385  N   VAL H 271     8099   8266  14973   1471    -54    618       N  
ATOM  11386  CA  VAL H 271      98.969 -61.284  61.200  1.00 76.99           C  
ANISOU11386  CA  VAL H 271     7466   7576  14210   1460     21    595       C  
ATOM  11387  C   VAL H 271      97.727 -61.709  61.971  1.00 78.82           C  
ANISOU11387  C   VAL H 271     7724   7803  14420   1448     62    526       C  
ATOM  11388  O   VAL H 271      97.279 -61.023  62.893  1.00 84.34           O  
ANISOU11388  O   VAL H 271     8415   8476  15156   1466     36    496       O  
ATOM  11389  CB  VAL H 271     100.286 -61.869  61.836  1.00 75.00           C  
ANISOU11389  CB  VAL H 271     7270   7294  13932   1490     37    609       C  
ATOM  11390  CG1 VAL H 271     101.317 -60.785  62.074  1.00 79.06           C  
ANISOU11390  CG1 VAL H 271     7775   7804  14462   1504    -30    647       C  
ATOM  11391  CG2 VAL H 271     100.013 -62.685  63.116  1.00 72.86           C  
ANISOU11391  CG2 VAL H 271     7067   6995  13622   1501     88    551       C  
ATOM  11392  N   GLY H 272      97.193 -62.855  61.565  1.00 79.44           N  
ANISOU11392  N   GLY H 272     7836   7908  14438   1417    126    503       N  
ATOM  11393  CA  GLY H 272      95.898 -63.334  61.979  1.00 80.76           C  
ANISOU11393  CA  GLY H 272     8022   8083  14581   1395    168    443       C  
ATOM  11394  C   GLY H 272      94.905 -63.156  60.848  1.00 79.37           C  
ANISOU11394  C   GLY H 272     7796   7951  14409   1356    166    447       C  
ATOM  11395  O   GLY H 272      93.971 -63.954  60.748  1.00 77.72           O  
ANISOU11395  O   GLY H 272     7609   7763  14159   1326    218    409       O  
ATOM  11396  N   ARG H 273      95.127 -62.191  59.954  1.00 74.92           N  
ANISOU11396  N   ARG H 273     7168   7405  13893   1353    109    495       N  
ATOM  11397  CA  ARG H 273      94.293 -62.108  58.755  1.00 73.54           C  
ANISOU11397  CA  ARG H 273     6948   7275  13719   1314    110    506       C  
ATOM  11398  C   ARG H 273      94.742 -63.139  57.725  1.00 66.64           C  
ANISOU11398  C   ARG H 273     6098   6433  12791   1289    152    533       C  
ATOM  11399  O   ARG H 273      95.902 -63.602  57.745  1.00 64.65           O  
ANISOU11399  O   ARG H 273     5880   6168  12516   1307    162    561       O  
ATOM  11400  CB  ARG H 273      94.323 -60.712  58.131  1.00 77.42           C  
ANISOU11400  CB  ARG H 273     7361   7775  14280   1319     35    547       C  
ATOM  11401  CG  ARG H 273      93.445 -59.650  58.820  1.00 84.58           C  
ANISOU11401  CG  ARG H 273     8230   8666  15241   1331     -5    517       C  
ATOM  11402  CD  ARG H 273      92.049 -60.178  59.165  1.00 85.54           C  
ANISOU11402  CD  ARG H 273     8367   8800  15333   1305     41    456       C  
ATOM  11403  NE  ARG H 273      91.138 -59.143  59.665  1.00 92.07           N  
ANISOU11403  NE  ARG H 273     9153   9618  16213   1313      3    431       N  
ATOM  11404  CZ  ARG H 273      91.332 -58.419  60.767  1.00 97.27           C  
ANISOU11404  CZ  ARG H 273     9813  10236  16910   1349    -31    416       C  
ATOM  11405  NH1 ARG H 273      92.427 -58.565  61.505  1.00 96.88           N  
ANISOU11405  NH1 ARG H 273     9803  10150  16857   1381    -34    426       N  
ATOM  11406  NH2 ARG H 273      90.425 -57.527  61.129  1.00103.10           N  
ANISOU11406  NH2 ARG H 273    10512  10969  17692   1352    -62    393       N  
ATOM  11407  N   VAL H 274      93.821 -63.510  56.837  1.00 64.79           N  
ANISOU11407  N   VAL H 274     5846   6238  12533   1249    177    524       N  
ATOM  11408  CA  VAL H 274      94.099 -64.445  55.749  1.00 63.99           C  
ANISOU11408  CA  VAL H 274     5761   6171  12381   1221    216    549       C  
ATOM  11409  C   VAL H 274      93.716 -63.756  54.458  1.00 64.16           C  
ANISOU11409  C   VAL H 274     5713   6231  12433   1196    179    585       C  
ATOM  11410  O   VAL H 274      92.880 -62.856  54.479  1.00 64.84           O  
ANISOU11410  O   VAL H 274     5749   6322  12565   1191    143    574       O  
ATOM  11411  CB  VAL H 274      93.328 -65.740  55.932  1.00 63.55           C  
ANISOU11411  CB  VAL H 274     5761   6128  12258   1193    292    499       C  
ATOM  11412  CG1 VAL H 274      93.375 -66.581  54.696  1.00 62.85           C  
ANISOU11412  CG1 VAL H 274     5680   6079  12122   1158    328    523       C  
ATOM  11413  CG2 VAL H 274      93.883 -66.501  57.120  1.00 63.30           C  
ANISOU11413  CG2 VAL H 274     5801   6058  12191   1219    330    470       C  
ATOM  11414  N   GLY H 275      94.291 -64.156  53.334  1.00 60.53           N  
ANISOU11414  N   GLY H 275     5250   5799  11951   1180    187    629       N  
ATOM  11415  CA  GLY H 275      94.072 -63.418  52.113  1.00 60.62           C  
ANISOU11415  CA  GLY H 275     5193   5843  11996   1160    146    669       C  
ATOM  11416  C   GLY H 275      93.959 -64.375  50.966  1.00 60.62           C  
ANISOU11416  C   GLY H 275     5206   5883  11942   1123    190    683       C  
ATOM  11417  O   GLY H 275      94.181 -65.543  51.129  1.00 60.54           O  
ANISOU11417  O   GLY H 275     5258   5872  11872   1116    248    667       O  
ATOM  11418  N   TYR H 276      93.564 -63.876  49.812  1.00 68.09           N  
ANISOU11418  N   TYR H 276     6095   6866  12910   1098    163    712       N  
ATOM  11419  CA  TYR H 276      93.378 -64.697  48.631  1.00 63.68           C  
ANISOU11419  CA  TYR H 276     5544   6349  12304   1060    201    727       C  
ATOM  11420  C   TYR H 276      94.217 -64.104  47.509  1.00 62.90           C  
ANISOU11420  C   TYR H 276     5398   6267  12233   1063    156    795       C  
ATOM  11421  O   TYR H 276      94.019 -62.953  47.128  1.00 66.95           O  
ANISOU11421  O   TYR H 276     5845   6788  12805   1065     98    819       O  
ATOM  11422  CB  TYR H 276      91.899 -64.736  48.214  1.00 65.31           C  
ANISOU11422  CB  TYR H 276     5724   6587  12504   1020    217    694       C  
ATOM  11423  CG  TYR H 276      91.013 -65.704  48.988  1.00 64.71           C  
ANISOU11423  CG  TYR H 276     5701   6506  12379   1004    279    629       C  
ATOM  11424  CD1 TYR H 276      91.016 -65.731  50.379  1.00 66.86           C  
ANISOU11424  CD1 TYR H 276     6010   6739  12655   1033    288    589       C  
ATOM  11425  CD2 TYR H 276      90.145 -66.570  48.321  1.00 62.30           C  
ANISOU11425  CD2 TYR H 276     5411   6237  12025    961    328    608       C  
ATOM  11426  CE1 TYR H 276      90.205 -66.610  51.082  1.00 66.56           C  
ANISOU11426  CE1 TYR H 276     6021   6696  12572   1018    345    530       C  
ATOM  11427  CE2 TYR H 276      89.339 -67.448  49.012  1.00 61.98           C  
ANISOU11427  CE2 TYR H 276     5419   6192  11940    946    384    550       C  
ATOM  11428  CZ  TYR H 276      89.370 -67.468  50.395  1.00 64.12           C  
ANISOU11428  CZ  TYR H 276     5726   6423  12215    975    393    511       C  
ATOM  11429  OH  TYR H 276      88.555 -68.350  51.091  1.00 64.08           O  
ANISOU11429  OH  TYR H 276     5769   6414  12165    960    450    453       O  
ATOM  11430  N   VAL H 277      95.149 -64.857  46.957  1.00 56.90           N  
ANISOU11430  N   VAL H 277     4671   5515  11434   1062    182    828       N  
ATOM  11431  CA  VAL H 277      95.864 -64.312  45.825  1.00 56.89           C  
ANISOU11431  CA  VAL H 277     4624   5535  11458   1062    141    892       C  
ATOM  11432  C   VAL H 277      95.489 -65.062  44.563  1.00 56.94           C  
ANISOU11432  C   VAL H 277     4630   5585  11419   1020    177    904       C  
ATOM  11433  O   VAL H 277      95.566 -66.275  44.511  1.00 56.89           O  
ANISOU11433  O   VAL H 277     4682   5585  11348   1006    238    888       O  
ATOM  11434  CB  VAL H 277      97.376 -64.359  46.040  1.00 56.75           C  
ANISOU11434  CB  VAL H 277     4631   5492  11441   1097    129    933       C  
ATOM  11435  CG1 VAL H 277      98.062 -63.705  44.894  1.00 56.76           C  
ANISOU11435  CG1 VAL H 277     4579   5514  11473   1097     83    998       C  
ATOM  11436  CG2 VAL H 277      97.732 -63.661  47.329  1.00 56.71           C  
ANISOU11436  CG2 VAL H 277     4629   5442  11478   1138     95    918       C  
ATOM  11437  N   SER H 278      95.050 -64.337  43.548  1.00 59.25           N  
ANISOU11437  N   SER H 278     4858   5909  11745    999    140    931       N  
ATOM  11438  CA  SER H 278      94.822 -64.956  42.265  1.00 58.82           C  
ANISOU11438  CA  SER H 278     4800   5897  11652    962    167    951       C  
ATOM  11439  C   SER H 278      96.118 -64.854  41.557  1.00 58.46           C  
ANISOU11439  C   SER H 278     4747   5854  11611    978    146   1014       C  
ATOM  11440  O   SER H 278      96.989 -64.175  42.049  1.00 58.66           O  
ANISOU11440  O   SER H 278     4761   5852  11676   1014    105   1038       O  
ATOM  11441  CB  SER H 278      93.704 -64.254  41.474  1.00 59.37           C  
ANISOU11441  CB  SER H 278     4803   6000  11754    931    139    950       C  
ATOM  11442  OG  SER H 278      93.389 -62.954  41.977  1.00 60.18           O  
ANISOU11442  OG  SER H 278     4852   6087  11927    950     79    947       O  
ATOM  11443  N   GLY H 279      96.259 -65.499  40.403  1.00 65.92           N  
ANISOU11443  N   GLY H 279     5696   6833  12516    951    171   1041       N  
ATOM  11444  CA  GLY H 279      97.432 -65.271  39.573  1.00 64.57           C  
ANISOU11444  CA  GLY H 279     5508   6671  12356    964    145   1106       C  
ATOM  11445  C   GLY H 279      97.514 -65.910  38.193  1.00 61.59           C  
ANISOU11445  C   GLY H 279     5130   6334  11939    932    170   1138       C  
ATOM  11446  O   GLY H 279      96.971 -66.982  37.946  1.00 58.83           O  
ANISOU11446  O   GLY H 279     4822   6002  11530    903    229   1110       O  
ATOM  11447  N   TRP H 280      98.220 -65.229  37.291  1.00 63.69           N  
ANISOU11447  N   TRP H 280     5348   6613  12237    939    124   1198       N  
ATOM  11448  CA  TRP H 280      98.508 -65.747  35.957  1.00 60.92           C  
ANISOU11448  CA  TRP H 280     4995   6298  11852    914    142   1237       C  
ATOM  11449  C   TRP H 280      99.913 -66.272  35.850  1.00 57.81           C  
ANISOU11449  C   TRP H 280     4639   5893  11432    939    156   1277       C  
ATOM  11450  O   TRP H 280     100.347 -66.643  34.769  1.00 57.43           O  
ANISOU11450  O   TRP H 280     4590   5872  11359    925    166   1317       O  
ATOM  11451  CB  TRP H 280      98.236 -64.673  34.893  1.00 64.51           C  
ANISOU11451  CB  TRP H 280     5369   6782  12359    901     85   1277       C  
ATOM  11452  CG  TRP H 280      96.761 -64.518  34.699  1.00 67.19           C  
ANISOU11452  CG  TRP H 280     5680   7144  12704    865     90   1237       C  
ATOM  11453  CD1 TRP H 280      95.954 -63.565  35.251  1.00 71.83           C  
ANISOU11453  CD1 TRP H 280     6224   7723  13344    869     51   1211       C  
ATOM  11454  CD2 TRP H 280      95.899 -65.399  33.962  1.00 65.51           C  
ANISOU11454  CD2 TRP H 280     5484   6967  12439    821    139   1216       C  
ATOM  11455  NE1 TRP H 280      94.660 -63.775  34.872  1.00 73.12           N  
ANISOU11455  NE1 TRP H 280     6375   7915  13492    830     72   1178       N  
ATOM  11456  CE2 TRP H 280      94.597 -64.903  34.086  1.00 69.33           C  
ANISOU11456  CE2 TRP H 280     5931   7462  12948    799    126   1180       C  
ATOM  11457  CE3 TRP H 280      96.107 -66.556  33.198  1.00 61.34           C  
ANISOU11457  CE3 TRP H 280     4999   6462  11845    797    192   1226       C  
ATOM  11458  CZ2 TRP H 280      93.507 -65.521  33.477  1.00 69.14           C  
ANISOU11458  CZ2 TRP H 280     5912   7472  12886    755    164   1153       C  
ATOM  11459  CZ3 TRP H 280      95.019 -67.147  32.583  1.00 61.25           C  
ANISOU11459  CZ3 TRP H 280     4991   6484  11797    753    228   1199       C  
ATOM  11460  CH2 TRP H 280      93.743 -66.635  32.733  1.00 65.12           C  
ANISOU11460  CH2 TRP H 280     5445   6985  12314    732    214   1163       C  
ATOM  11461  N   GLY H 281     100.635 -66.268  36.961  1.00 65.10           N  
ANISOU11461  N   GLY H 281     5595   6777  12362    976    154   1269       N  
ATOM  11462  CA  GLY H 281     102.047 -66.619  36.935  1.00 62.43           C  
ANISOU11462  CA  GLY H 281     5289   6426  12007   1004    159   1311       C  
ATOM  11463  C   GLY H 281     102.339 -68.088  36.717  1.00 58.49           C  
ANISOU11463  C   GLY H 281     4861   5935  11428    992    231   1303       C  
ATOM  11464  O   GLY H 281     101.418 -68.884  36.573  1.00 58.27           O  
ANISOU11464  O   GLY H 281     4862   5924  11355    959    280   1263       O  
ATOM  11465  N   ARG H 282     103.626 -68.430  36.742  1.00 66.22           N  
ANISOU11465  N   ARG H 282     5870   6901  12390   1019    237   1340       N  
ATOM  11466  CA  ARG H 282     104.152 -69.769  36.456  1.00 61.08           C  
ANISOU11466  CA  ARG H 282     5285   6256  11665   1013    301   1344       C  
ATOM  11467  C   ARG H 282     103.742 -70.825  37.486  1.00 59.58           C  
ANISOU11467  C   ARG H 282     5170   6046  11423   1012    364   1283       C  
ATOM  11468  O   ARG H 282     103.320 -70.486  38.589  1.00 60.86           O  
ANISOU11468  O   ARG H 282     5335   6180  11608   1025    354   1242       O  
ATOM  11469  CB  ARG H 282     105.681 -69.708  36.358  1.00 59.87           C  
ANISOU11469  CB  ARG H 282     5141   6091  11517   1049    284   1400       C  
ATOM  11470  CG  ARG H 282     106.180 -69.236  34.980  1.00 60.56           C  
ANISOU11470  CG  ARG H 282     5178   6210  11623   1041    250   1465       C  
ATOM  11471  CD  ARG H 282     107.687 -68.956  34.858  1.00 60.46           C  
ANISOU11471  CD  ARG H 282     5161   6185  11627   1077    222   1525       C  
ATOM  11472  NE  ARG H 282     108.056 -68.804  33.448  1.00 61.27           N  
ANISOU11472  NE  ARG H 282     5226   6322  11730   1063    205   1581       N  
ATOM  11473  CZ  ARG H 282     108.442 -67.661  32.879  1.00 64.97           C  
ANISOU11473  CZ  ARG H 282     5627   6799  12259   1072    140   1630       C  
ATOM  11474  NH1 ARG H 282     108.548 -66.545  33.600  1.00 68.25           N  
ANISOU11474  NH1 ARG H 282     6003   7190  12739   1097     83   1632       N  
ATOM  11475  NH2 ARG H 282     108.734 -67.640  31.582  1.00 65.60           N  
ANISOU11475  NH2 ARG H 282     5679   6912  12333   1057    132   1679       N  
ATOM  11476  N   ASN H 283     103.850 -72.101  37.123  1.00 65.00           N  
ANISOU11476  N   ASN H 283     5914   6745  12038    995    427   1276       N  
ATOM  11477  CA  ASN H 283     103.592 -73.193  38.060  1.00 62.26           C  
ANISOU11477  CA  ASN H 283     5642   6378  11636    995    490   1222       C  
ATOM  11478  C   ASN H 283     104.802 -74.142  38.212  1.00 57.98           C  
ANISOU11478  C   ASN H 283     5164   5821  11044   1018    530   1243       C  
ATOM  11479  O   ASN H 283     105.936 -73.786  37.875  1.00 57.78           O  
ANISOU11479  O   ASN H 283     5123   5793  11037   1044    501   1298       O  
ATOM  11480  CB  ASN H 283     102.364 -73.984  37.642  1.00 61.19           C  
ANISOU11480  CB  ASN H 283     5527   6270  11454    949    540   1180       C  
ATOM  11481  CG  ASN H 283     102.411 -74.405  36.195  1.00 59.45           C  
ANISOU11481  CG  ASN H 283     5298   6089  11203    919    555   1216       C  
ATOM  11482  OD1 ASN H 283     103.481 -74.449  35.587  1.00 57.92           O  
ANISOU11482  OD1 ASN H 283     5103   5901  11004    935    546   1269       O  
ATOM  11483  ND2 ASN H 283     101.239 -74.716  35.626  1.00 59.92           N  
ANISOU11483  ND2 ASN H 283     5349   6177  11239    876    578   1188       N  
ATOM  11484  N   ALA H 284     104.578 -75.310  38.816  1.00 62.74           N  
ANISOU11484  N   ALA H 284     5840   6414  11586   1012    595   1199       N  
ATOM  11485  CA  ALA H 284     105.662 -76.234  39.142  1.00 58.96           C  
ANISOU11485  CA  ALA H 284     5426   5916  11059   1037    636   1212       C  
ATOM  11486  C   ALA H 284     106.316 -76.863  37.929  1.00 55.94           C  
ANISOU11486  C   ALA H 284     5056   5562  10636   1026    659   1259       C  
ATOM  11487  O   ALA H 284     107.313 -77.527  38.076  1.00 53.43           O  
ANISOU11487  O   ALA H 284     4786   5233  10283   1048    686   1278       O  
ATOM  11488  CB  ALA H 284     105.168 -77.301  40.066  1.00 56.87           C  
ANISOU11488  CB  ALA H 284     5233   5634  10740   1031    699   1151       C  
ATOM  11489  N   ASN H 285     105.773 -76.675  36.734  1.00 60.20           N  
ANISOU11489  N   ASN H 285     5556   6139  11178    992    648   1277       N  
ATOM  11490  CA  ASN H 285     106.545 -76.956  35.521  1.00 58.38           C  
ANISOU11490  CA  ASN H 285     5321   5934  10925    988    652   1334       C  
ATOM  11491  C   ASN H 285     107.218 -75.685  35.025  1.00 61.43           C  
ANISOU11491  C   ASN H 285     5635   6326  11381   1008    579   1393       C  
ATOM  11492  O   ASN H 285     107.755 -75.663  33.919  1.00 61.20           O  
ANISOU11492  O   ASN H 285     5586   6322  11347   1003    569   1444       O  
ATOM  11493  CB  ASN H 285     105.689 -77.540  34.393  1.00 57.64           C  
ANISOU11493  CB  ASN H 285     5227   5880  10792    940    685   1327       C  
ATOM  11494  CG  ASN H 285     105.033 -78.877  34.767  1.00 54.72           C  
ANISOU11494  CG  ASN H 285     4932   5510  10349    917    761   1272       C  
ATOM  11495  OD1 ASN H 285     105.521 -79.604  35.641  1.00 52.10           O  
ANISOU11495  OD1 ASN H 285     4662   5150   9983    939    799   1252       O  
ATOM  11496  ND2 ASN H 285     103.929 -79.211  34.088  1.00 55.35           N  
ANISOU11496  ND2 ASN H 285     5006   5619  10405    872    783   1248       N  
ATOM  11497  N   PHE H 286     107.125 -74.612  35.815  1.00 56.05           N  
ANISOU11497  N   PHE H 286     4913   5621  10763   1029    526   1384       N  
ATOM  11498  CA  PHE H 286     107.647 -73.285  35.448  1.00 59.83           C  
ANISOU11498  CA  PHE H 286     5318   6101  11313   1048    451   1435       C  
ATOM  11499  C   PHE H 286     107.054 -72.839  34.112  1.00 61.57           C  
ANISOU11499  C   PHE H 286     5480   6363  11549   1014    428   1460       C  
ATOM  11500  O   PHE H 286     107.612 -71.992  33.413  1.00 63.17           O  
ANISOU11500  O   PHE H 286     5629   6578  11796   1023    376   1514       O  
ATOM  11501  CB  PHE H 286     109.186 -73.262  35.398  1.00 58.95           C  
ANISOU11501  CB  PHE H 286     5217   5978  11204   1086    437   1491       C  
ATOM  11502  CG  PHE H 286     109.847 -72.967  36.737  1.00 59.72           C  
ANISOU11502  CG  PHE H 286     5333   6031  11325   1128    421   1481       C  
ATOM  11503  CD1 PHE H 286     109.089 -72.652  37.856  1.00 61.46           C  
ANISOU11503  CD1 PHE H 286     5556   6227  11568   1131    415   1427       C  
ATOM  11504  CD2 PHE H 286     111.224 -73.000  36.868  1.00 58.95           C  
ANISOU11504  CD2 PHE H 286     5251   5919  11229   1164    412   1526       C  
ATOM  11505  CE1 PHE H 286     109.697 -72.393  39.080  1.00 62.40           C  
ANISOU11505  CE1 PHE H 286     5694   6306  11709   1169    400   1417       C  
ATOM  11506  CE2 PHE H 286     111.827 -72.743  38.088  1.00 59.86           C  
ANISOU11506  CE2 PHE H 286     5385   5995  11365   1201    397   1516       C  
ATOM  11507  CZ  PHE H 286     111.056 -72.439  39.193  1.00 61.58           C  
ANISOU11507  CZ  PHE H 286     5606   6188  11605   1204    391   1462       C  
ATOM  11508  N   LYS H 287     105.890 -73.404  33.793  1.00 60.74           N  
ANISOU11508  N   LYS H 287     5388   6279  11410    974    465   1420       N  
ATOM  11509  CA  LYS H 287     105.022 -72.937  32.706  1.00 62.85           C  
ANISOU11509  CA  LYS H 287     5599   6584  11696    937    443   1429       C  
ATOM  11510  C   LYS H 287     104.091 -71.845  33.192  1.00 67.16           C  
ANISOU11510  C   LYS H 287     6090   7123  12304    933    396   1401       C  
ATOM  11511  O   LYS H 287     103.510 -71.943  34.278  1.00 67.45           O  
ANISOU11511  O   LYS H 287     6150   7137  12341    937    410   1349       O  
ATOM  11512  CB  LYS H 287     104.169 -74.085  32.142  1.00 60.19           C  
ANISOU11512  CB  LYS H 287     5304   6274  11292    894    507   1397       C  
ATOM  11513  CG  LYS H 287     104.737 -74.848  30.921  1.00 58.19           C  
ANISOU11513  CG  LYS H 287     5070   6049  10989    880    538   1439       C  
ATOM  11514  CD  LYS H 287     103.656 -75.769  30.285  1.00 58.41           C  
ANISOU11514  CD  LYS H 287     5125   6107  10961    831    591   1405       C  
ATOM  11515  CE  LYS H 287     103.584 -77.147  30.969  1.00 56.96           C  
ANISOU11515  CE  LYS H 287     5030   5908  10705    828    665   1360       C  
ATOM  11516  NZ  LYS H 287     102.574 -78.132  30.370  1.00 58.51           N  
ANISOU11516  NZ  LYS H 287     5258   6132  10840    780    721   1326       N  
ATOM  11517  N   PHE H 288     103.954 -70.807  32.381  1.00 55.58           N  
ANISOU11517  N   PHE H 288     4550   5678  10890    925    340   1437       N  
ATOM  11518  CA  PHE H 288     102.926 -69.786  32.623  1.00 59.57           C  
ANISOU11518  CA  PHE H 288     4998   6185  11451    915    297   1412       C  
ATOM  11519  C   PHE H 288     101.578 -70.531  32.630  1.00 58.76           C  
ANISOU11519  C   PHE H 288     4921   6098  11306    874    346   1355       C  
ATOM  11520  O   PHE H 288     101.318 -71.342  31.745  1.00 56.78           O  
ANISOU11520  O   PHE H 288     4691   5877  11006    843    386   1358       O  
ATOM  11521  CB  PHE H 288     102.963 -68.663  31.559  1.00 63.25           C  
ANISOU11521  CB  PHE H 288     5383   6677  11973    908    234   1463       C  
ATOM  11522  CG  PHE H 288     103.977 -67.577  31.837  1.00 66.05           C  
ANISOU11522  CG  PHE H 288     5698   7009  12390    948    170   1507       C  
ATOM  11523  CD1 PHE H 288     104.093 -67.013  33.102  1.00 67.67           C  
ANISOU11523  CD1 PHE H 288     5903   7176  12632    979    145   1484       C  
ATOM  11524  CD2 PHE H 288     104.810 -67.106  30.829  1.00 67.35           C  
ANISOU11524  CD2 PHE H 288     5823   7191  12575    955    135   1573       C  
ATOM  11525  CE1 PHE H 288     105.024 -65.996  33.348  1.00 70.56           C  
ANISOU11525  CE1 PHE H 288     6232   7522  13056   1015     85   1526       C  
ATOM  11526  CE2 PHE H 288     105.735 -66.099  31.073  1.00 70.21           C  
ANISOU11526  CE2 PHE H 288     6147   7534  12995    991     75   1614       C  
ATOM  11527  CZ  PHE H 288     105.840 -65.553  32.330  1.00 71.80           C  
ANISOU11527  CZ  PHE H 288     6351   7698  13233   1020     51   1590       C  
ATOM  11528  N   THR H 289     100.744 -70.282  33.635  1.00 56.85           N  
ANISOU11528  N   THR H 289     4680   5837  11082    875    345   1302       N  
ATOM  11529  CA  THR H 289      99.591 -71.142  33.860  1.00 56.37           C  
ANISOU11529  CA  THR H 289     4657   5786  10975    841    399   1243       C  
ATOM  11530  C   THR H 289      98.499 -71.036  32.800  1.00 57.16           C  
ANISOU11530  C   THR H 289     4717   5928  11074    796    398   1240       C  
ATOM  11531  O   THR H 289      98.236 -69.960  32.256  1.00 60.89           O  
ANISOU11531  O   THR H 289     5118   6415  11601    791    343   1265       O  
ATOM  11532  CB  THR H 289      98.942 -70.878  35.223  1.00 57.70           C  
ANISOU11532  CB  THR H 289     4835   5924  11164    853    397   1187       C  
ATOM  11533  OG1 THR H 289      97.718 -71.628  35.300  1.00 57.40           O  
ANISOU11533  OG1 THR H 289     4825   5901  11085    816    446   1133       O  
ATOM  11534  CG2 THR H 289      98.641 -69.410  35.399  1.00 62.16           C  
ANISOU11534  CG2 THR H 289     5326   6483  11810    866    326   1197       C  
ATOM  11535  N   ASP H 290      97.856 -72.164  32.526  1.00 55.26           N  
ANISOU11535  N   ASP H 290     4523   5706  10769    762    459   1208       N  
ATOM  11536  CA  ASP H 290      96.790 -72.228  31.527  1.00 56.86           C  
ANISOU11536  CA  ASP H 290     4695   5949  10960    715    466   1201       C  
ATOM  11537  C   ASP H 290      95.435 -71.739  32.021  1.00 60.51           C  
ANISOU11537  C   ASP H 290     5127   6413  11450    697    455   1152       C  
ATOM  11538  O   ASP H 290      94.538 -71.460  31.239  1.00 63.41           O  
ANISOU11538  O   ASP H 290     5452   6813  11827    663    444   1151       O  
ATOM  11539  CB  ASP H 290      96.638 -73.661  31.028  1.00 53.47           C  
ANISOU11539  CB  ASP H 290     4329   5538  10449    685    538   1187       C  
ATOM  11540  CG  ASP H 290      97.686 -74.012  30.016  1.00 52.99           C  
ANISOU11540  CG  ASP H 290     4277   5492  10363    689    543   1244       C  
ATOM  11541  OD1 ASP H 290      98.243 -73.040  29.447  1.00 53.59           O  
ANISOU11541  OD1 ASP H 290     4296   5576  10491    704    486   1294       O  
ATOM  11542  OD2 ASP H 290      97.944 -75.233  29.799  1.00 52.35           O  
ANISOU11542  OD2 ASP H 290     4260   5416  10214    678    602   1238       O  
ATOM  11543  N   HIS H 291      95.296 -71.677  33.333  1.00 56.09           N  
ANISOU11543  N   HIS H 291     4591   5819  10901    719    459   1111       N  
ATOM  11544  CA  HIS H 291      94.047 -71.321  33.976  1.00 56.18           C  
ANISOU11544  CA  HIS H 291     4584   5828  10934    705    455   1060       C  
ATOM  11545  C   HIS H 291      94.357 -70.490  35.182  1.00 57.00           C  
ANISOU11545  C   HIS H 291     4675   5893  11091    746    416   1049       C  
ATOM  11546  O   HIS H 291      95.280 -70.816  35.934  1.00 55.99           O  
ANISOU11546  O   HIS H 291     4592   5733  10950    779    429   1051       O  
ATOM  11547  CB  HIS H 291      93.274 -72.544  34.422  1.00 56.21           C  
ANISOU11547  CB  HIS H 291     4651   5833  10872    679    525   1002       C  
ATOM  11548  CG  HIS H 291      92.843 -73.437  33.308  1.00 56.28           C  
ANISOU11548  CG  HIS H 291     4678   5880  10826    635    567   1006       C  
ATOM  11549  ND1 HIS H 291      93.720 -74.250  32.626  1.00 56.22           N  
ANISOU11549  ND1 HIS H 291     4709   5881  10770    634    598   1039       N  
ATOM  11550  CD2 HIS H 291      91.624 -73.657  32.766  1.00 56.42           C  
ANISOU11550  CD2 HIS H 291     4681   5930  10827    591    585    980       C  
ATOM  11551  CE1 HIS H 291      93.057 -74.928  31.704  1.00 56.31           C  
ANISOU11551  CE1 HIS H 291     4730   5928  10739    590    632   1034       C  
ATOM  11552  NE2 HIS H 291      91.786 -74.579  31.764  1.00 56.44           N  
ANISOU11552  NE2 HIS H 291     4713   5959  10772    563    625    998       N  
ATOM  11553  N   LEU H 292      93.582 -69.426  35.373  1.00 57.09           N  
ANISOU11553  N   LEU H 292     4626   5905  11159    744    370   1037       N  
ATOM  11554  CA  LEU H 292      93.752 -68.575  36.540  1.00 58.82           C  
ANISOU11554  CA  LEU H 292     4831   6087  11431    781    332   1022       C  
ATOM  11555  C   LEU H 292      93.700 -69.494  37.775  1.00 57.21           C  
ANISOU11555  C   LEU H 292     4702   5853  11184    793    385    970       C  
ATOM  11556  O   LEU H 292      92.947 -70.478  37.800  1.00 56.96           O  
ANISOU11556  O   LEU H 292     4711   5833  11097    763    441    930       O  
ATOM  11557  CB  LEU H 292      92.684 -67.475  36.557  1.00 64.17           C  
ANISOU11557  CB  LEU H 292     5442   6775  12166    771    286   1007       C  
ATOM  11558  CG  LEU H 292      92.741 -66.493  37.719  1.00 67.61           C  
ANISOU11558  CG  LEU H 292     5855   7173  12660    807    242    992       C  
ATOM  11559  CD1 LEU H 292      94.106 -65.933  37.770  1.00 67.25           C  
ANISOU11559  CD1 LEU H 292     5800   7105  12646    846    201   1042       C  
ATOM  11560  CD2 LEU H 292      91.727 -65.381  37.586  1.00 72.94           C  
ANISOU11560  CD2 LEU H 292     6461   7862  13392    796    195    983       C  
ATOM  11561  N   LYS H 293      94.561 -69.259  38.754  1.00 58.45           N  
ANISOU11561  N   LYS H 293     4174   4544  13492    778    685   1308       N  
ATOM  11562  CA  LYS H 293      94.490 -70.063  39.968  1.00 58.61           C  
ANISOU11562  CA  LYS H 293     4196   4602  13470    821    686   1301       C  
ATOM  11563  C   LYS H 293      94.540 -69.113  41.133  1.00 59.30           C  
ANISOU11563  C   LYS H 293     4285   4670  13577    882    686   1247       C  
ATOM  11564  O   LYS H 293      94.658 -67.907  40.948  1.00 59.62           O  
ANISOU11564  O   LYS H 293     4323   4668  13661    886    684   1217       O  
ATOM  11565  CB  LYS H 293      95.620 -71.093  40.057  1.00 58.25           C  
ANISOU11565  CB  LYS H 293     4147   4572  13414    793    655   1303       C  
ATOM  11566  CG  LYS H 293      95.931 -71.848  38.773  1.00 57.56           C  
ANISOU11566  CG  LYS H 293     4059   4489  13322    723    647   1347       C  
ATOM  11567  CD  LYS H 293      96.724 -73.116  39.081  1.00 57.22           C  
ANISOU11567  CD  LYS H 293     4016   4476  13250    708    624   1356       C  
ATOM  11568  CE  LYS H 293      98.127 -73.123  38.504  1.00 56.97           C  
ANISOU11568  CE  LYS H 293     3975   4414  13256    658    588   1339       C  
ATOM  11569  NZ  LYS H 293      99.034 -73.813  39.453  1.00 57.04           N  
ANISOU11569  NZ  LYS H 293     3981   4441  13251    676    560   1313       N  
ATOM  11570  N   TYR H 294      94.455 -69.655  42.334  1.00 58.68           N  
ANISOU11570  N   TYR H 294     4210   4621  13465    930    689   1235       N  
ATOM  11571  CA  TYR H 294      94.418 -68.808  43.505  1.00 59.95           C  
ANISOU11571  CA  TYR H 294     4374   4765  13638    993    691   1184       C  
ATOM  11572  C   TYR H 294      94.875 -69.602  44.696  1.00 59.88           C  
ANISOU11572  C   TYR H 294     4368   4786  13599   1032    679   1166       C  
ATOM  11573  O   TYR H 294      94.801 -70.811  44.674  1.00 58.97           O  
ANISOU11573  O   TYR H 294     4253   4711  13442   1019    682   1202       O  
ATOM  11574  CB  TYR H 294      92.996 -68.220  43.719  1.00 60.83           C  
ANISOU11574  CB  TYR H 294     4494   4882  13738   1033    733   1194       C  
ATOM  11575  CG  TYR H 294      91.950 -69.093  44.403  1.00 60.78           C  
ANISOU11575  CG  TYR H 294     4493   4923  13676   1071    766   1224       C  
ATOM  11576  CD1 TYR H 294      91.889 -69.192  45.790  1.00 61.48           C  
ANISOU11576  CD1 TYR H 294     4589   5026  13743   1134    774   1195       C  
ATOM  11577  CD2 TYR H 294      90.994 -69.766  43.658  1.00 60.12           C  
ANISOU11577  CD2 TYR H 294     4410   4869  13564   1044    793   1278       C  
ATOM  11578  CE1 TYR H 294      90.936 -69.976  46.420  1.00 61.48           C  
ANISOU11578  CE1 TYR H 294     4594   5068  13696   1169    808   1222       C  
ATOM  11579  CE2 TYR H 294      90.006 -70.558  44.278  1.00 60.12           C  
ANISOU11579  CE2 TYR H 294     4414   4911  13518   1078    827   1304       C  
ATOM  11580  CZ  TYR H 294      89.981 -70.662  45.663  1.00 60.80           C  
ANISOU11580  CZ  TYR H 294     4506   5011  13584   1140    836   1277       C  
ATOM  11581  OH  TYR H 294      89.002 -71.439  46.273  1.00 60.84           O  
ANISOU11581  OH  TYR H 294     4516   5056  13545   1173    874   1303       O  
ATOM  11582  N   VAL H 295      95.338 -68.938  45.741  1.00 59.77           N  
ANISOU11582  N   VAL H 295     4358   4751  13602   1081    664   1110       N  
ATOM  11583  CA  VAL H 295      95.803 -69.664  46.909  1.00 59.97           C  
ANISOU11583  CA  VAL H 295     4388   4802  13597   1123    650   1090       C  
ATOM  11584  C   VAL H 295      95.493 -68.784  48.104  1.00 60.71           C  
ANISOU11584  C   VAL H 295     4493   4879  13696   1196    660   1041       C  
ATOM  11585  O   VAL H 295      95.499 -67.574  47.984  1.00 61.04           O  
ANISOU11585  O   VAL H 295     4534   4879  13778   1202    658   1009       O  
ATOM  11586  CB  VAL H 295      97.373 -70.063  46.795  1.00 59.76           C  
ANISOU11586  CB  VAL H 295     4350   4763  13592   1089    598   1063       C  
ATOM  11587  CG1 VAL H 295      98.254 -68.918  46.283  1.00 59.89           C  
ANISOU11587  CG1 VAL H 295     4358   4724  13675   1060    570   1020       C  
ATOM  11588  CG2 VAL H 295      97.932 -70.613  48.091  1.00 60.08           C  
ANISOU11588  CG2 VAL H 295     4397   4824  13607   1141    578   1030       C  
ATOM  11589  N   MET H 296      95.160 -69.393  49.231  1.00 61.29           N  
ANISOU11589  N   MET H 296     4577   4985  13727   1252    674   1039       N  
ATOM  11590  CA  MET H 296      95.041 -68.681  50.487  1.00 62.62           C  
ANISOU11590  CA  MET H 296     4759   5137  13896   1326    678    989       C  
ATOM  11591  C   MET H 296      96.399 -68.646  51.160  1.00 62.81           C  
ANISOU11591  C   MET H 296     4784   5144  13938   1342    628    933       C  
ATOM  11592  O   MET H 296      97.134 -69.636  51.110  1.00 61.91           O  
ANISOU11592  O   MET H 296     4663   5052  13807   1320    602    943       O  
ATOM  11593  CB  MET H 296      93.999 -69.350  51.372  1.00 62.88           C  
ANISOU11593  CB  MET H 296     4806   5211  13875   1381    720   1013       C  
ATOM  11594  CG  MET H 296      92.570 -69.204  50.805  1.00 62.94           C  
ANISOU11594  CG  MET H 296     4813   5231  13872   1372    770   1059       C  
ATOM  11595  SD  MET H 296      91.506 -70.646  50.876  1.00 62.18           S  
ANISOU11595  SD  MET H 296     4718   5195  13713   1375    815   1125       S  
ATOM  11596  CE  MET H 296      91.923 -71.267  52.500  1.00 62.95           C  
ANISOU11596  CE  MET H 296     4833   5313  13774   1450    812   1094       C  
ATOM  11597  N   LEU H 297      96.784 -67.503  51.728  1.00 62.51           N  
ANISOU11597  N   LEU H 297     4751   5063  13936   1376    611    872       N  
ATOM  11598  CA  LEU H 297      98.077 -67.389  52.445  1.00 62.81           C  
ANISOU11598  CA  LEU H 297     4791   5081  13994   1397    560    810       C  
ATOM  11599  C   LEU H 297      97.874 -66.548  53.681  1.00 64.18           C  
ANISOU11599  C   LEU H 297     4984   5232  14169   1474    564    754       C  
ATOM  11600  O   LEU H 297      97.103 -65.590  53.654  1.00 66.77           O  
ANISOU11600  O   LEU H 297     5319   5539  14512   1491    593    749       O  
ATOM  11601  CB  LEU H 297      99.166 -66.755  51.571  1.00 62.64           C  
ANISOU11601  CB  LEU H 297     4750   5015  14034   1338    520    781       C  
ATOM  11602  CG  LEU H 297      99.160 -67.177  50.102  1.00 61.91           C  
ANISOU11602  CG  LEU H 297     4641   4930  13952   1256    526    836       C  
ATOM  11603  CD1 LEU H 297      99.636 -66.049  49.220  1.00 61.91           C  
ANISOU11603  CD1 LEU H 297     4629   4877  14017   1212    513    813       C  
ATOM  11604  CD2 LEU H 297      99.987 -68.416  49.884  1.00 61.44           C  
ANISOU11604  CD2 LEU H 297     4571   4899  13873   1222    497    855       C  
ATOM  11605  N   PRO H 298      98.535 -66.890  54.782  1.00 64.48           N  
ANISOU11605  N   PRO H 298     5034   5276  14191   1524    535    713       N  
ATOM  11606  CA  PRO H 298      98.374 -66.028  55.949  1.00 65.25           C  
ANISOU11606  CA  PRO H 298     5153   5348  14290   1599    537    656       C  
ATOM  11607  C   PRO H 298      99.235 -64.796  55.758  1.00 65.96           C  
ANISOU11607  C   PRO H 298     5236   5381  14445   1583    500    592       C  
ATOM  11608  O   PRO H 298     100.131 -64.856  54.910  1.00 65.23           O  
ANISOU11608  O   PRO H 298     5122   5274  14389   1521    467    589       O  
ATOM  11609  CB  PRO H 298      98.863 -66.904  57.099  1.00 65.49           C  
ANISOU11609  CB  PRO H 298     5200   5403  14280   1654    515    634       C  
ATOM  11610  CG  PRO H 298      99.781 -67.774  56.494  1.00 64.96           C  
ANISOU11610  CG  PRO H 298     5114   5352  14217   1601    479    649       C  
ATOM  11611  CD  PRO H 298      99.387 -68.028  55.075  1.00 64.27           C  
ANISOU11611  CD  PRO H 298     5004   5276  14139   1522    502    713       C  
ATOM  11612  N   VAL H 299      98.974 -63.696  56.461  1.00 65.62           N  
ANISOU11612  N   VAL H 299     5209   5304  14418   1633    506    544       N  
ATOM  11613  CA  VAL H 299      99.949 -62.600  56.402  1.00 66.31           C  
ANISOU11613  CA  VAL H 299     5290   5337  14568   1621    464    475       C  
ATOM  11614  C   VAL H 299     100.958 -62.860  57.506  1.00 67.14           C  
ANISOU11614  C   VAL H 299     5407   5438  14667   1669    415    412       C  
ATOM  11615  O   VAL H 299     100.613 -63.374  58.572  1.00 68.58           O  
ANISOU11615  O   VAL H 299     5613   5645  14801   1734    424    408       O  
ATOM  11616  CB  VAL H 299      99.327 -61.165  56.544  1.00 73.28           C  
ANISOU11616  CB  VAL H 299     6184   6179  15480   1646    489    445       C  
ATOM  11617  CG1 VAL H 299      97.776 -61.162  56.378  1.00 74.24           C  
ANISOU11617  CG1 VAL H 299     6315   6325  15566   1661    553    504       C  
ATOM  11618  CG2 VAL H 299      99.775 -60.515  57.830  1.00 79.07           C  
ANISOU11618  CG2 VAL H 299     6940   6884  16220   1716    462    366       C  
ATOM  11619  N   ALA H 300     102.208 -62.521  57.247  1.00 69.40           N  
ANISOU11619  N   ALA H 300     5676   5689  15003   1636    363    361       N  
ATOM  11620  CA  ALA H 300     103.283 -62.951  58.117  1.00 69.59           C  
ANISOU11620  CA  ALA H 300     5706   5713  15023   1669    309    305       C  
ATOM  11621  C   ALA H 300     103.890 -61.839  58.960  1.00 75.52           C  
ANISOU11621  C   ALA H 300     6469   6415  15810   1714    274    213       C  
ATOM  11622  O   ALA H 300     103.883 -60.666  58.573  1.00 79.31           O  
ANISOU11622  O   ALA H 300     6943   6851  16340   1695    279    185       O  
ATOM  11623  CB  ALA H 300     104.362 -63.603  57.298  1.00 68.43           C  
ANISOU11623  CB  ALA H 300     5530   5569  14900   1601    269    312       C  
ATOM  11624  N   ASP H 301     104.422 -62.236  60.116  1.00 73.61           N  
ANISOU11624  N   ASP H 301     6246   6180  15542   1775    238    164       N  
ATOM  11625  CA  ASP H 301     105.064 -61.309  61.036  1.00 79.85           C  
ANISOU11625  CA  ASP H 301     7052   6927  16361   1824    198     70       C  
ATOM  11626  C   ASP H 301     106.167 -60.545  60.320  1.00 80.60           C  
ANISOU11626  C   ASP H 301     7118   6974  16533   1764    155     20       C  
ATOM  11627  O   ASP H 301     107.049 -61.147  59.727  1.00 75.92           O  
ANISOU11627  O   ASP H 301     6500   6386  15960   1712    122     24       O  
ATOM  11628  CB  ASP H 301     105.630 -62.058  62.248  1.00 79.81           C  
ANISOU11628  CB  ASP H 301     7070   6941  16315   1890    156     28       C  
ATOM  11629  CG  ASP H 301     106.452 -61.157  63.144  1.00 86.24           C  
ANISOU11629  CG  ASP H 301     7899   7709  17161   1935    104    -76       C  
ATOM  11630  OD1 ASP H 301     107.627 -60.921  62.812  1.00 87.26           O  
ANISOU11630  OD1 ASP H 301     8004   7810  17342   1896     50   -127       O  
ATOM  11631  OD2 ASP H 301     105.933 -60.668  64.168  1.00 90.48           O  
ANISOU11631  OD2 ASP H 301     8469   8236  17672   2009    116   -109       O  
ATOM  11632  N   GLN H 302     106.115 -59.214  60.376  1.00 79.19           N  
ANISOU11632  N   GLN H 302     6943   6747  16399   1770    159    -27       N  
ATOM  11633  CA  GLN H 302     107.044 -58.391  59.589  1.00 80.31           C  
ANISOU11633  CA  GLN H 302     7056   6839  16618   1708    130    -69       C  
ATOM  11634  C   GLN H 302     108.513 -58.593  59.982  1.00 80.58           C  
ANISOU11634  C   GLN H 302     7079   6856  16683   1706     57   -145       C  
ATOM  11635  O   GLN H 302     109.385 -58.550  59.126  1.00 78.64           O  
ANISOU11635  O   GLN H 302     6801   6589  16490   1639     32   -155       O  
ATOM  11636  CB  GLN H 302     106.678 -56.902  59.683  1.00 87.20           C  
ANISOU11636  CB  GLN H 302     7939   7663  17530   1722    149   -110       C  
ATOM  11637  CG  GLN H 302     106.064 -56.313  58.401  1.00 85.74           C  
ANISOU11637  CG  GLN H 302     7737   7463  17378   1659    196    -55       C  
ATOM  11638  CD  GLN H 302     107.059 -56.150  57.260  1.00 84.87           C  
ANISOU11638  CD  GLN H 302     7591   7321  17333   1575    172    -61       C  
ATOM  11639  OE1 GLN H 302     108.182 -56.617  57.342  1.00 85.80           O  
ANISOU11639  OE1 GLN H 302     7693   7436  17471   1558    122    -99       O  
ATOM  11640  NE2 GLN H 302     106.644 -55.480  56.192  1.00 83.33           N  
ANISOU11640  NE2 GLN H 302     7385   7104  17173   1524    208    -26       N  
ATOM  11641  N   ASP H 303     108.794 -58.831  61.258  1.00 85.59           N  
ANISOU11641  N   ASP H 303     7738   7498  17284   1780     22   -200       N  
ATOM  11642  CA  ASP H 303     110.183 -58.989  61.690  1.00 86.13           C  
ANISOU11642  CA  ASP H 303     7796   7548  17380   1783    -52   -279       C  
ATOM  11643  C   ASP H 303     110.761 -60.331  61.241  1.00 78.59           C  
ANISOU11643  C   ASP H 303     6822   6633  16407   1745    -75   -239       C  
ATOM  11644  O   ASP H 303     111.850 -60.364  60.672  1.00 76.65           O  
ANISOU11644  O   ASP H 303     6545   6366  16212   1690   -116   -269       O  
ATOM  11645  CB  ASP H 303     110.306 -58.824  63.211  1.00 91.33           C  
ANISOU11645  CB  ASP H 303     8493   8203  18007   1877    -85   -353       C  
ATOM  11646  CG  ASP H 303     110.212 -57.354  63.662  1.00 99.87           C  
ANISOU11646  CG  ASP H 303     9588   9232  19126   1907    -85   -422       C  
ATOM  11647  OD1 ASP H 303     109.860 -56.470  62.844  1.00101.89           O  
ANISOU11647  OD1 ASP H 303     9828   9459  19426   1860    -50   -404       O  
ATOM  11648  OD2 ASP H 303     110.481 -57.088  64.854  1.00104.83           O  
ANISOU11648  OD2 ASP H 303    10245   9848  19737   1979   -121   -496       O  
ATOM  11649  N   GLN H 304     110.039 -61.427  61.479  1.00 88.67           N  
ANISOU11649  N   GLN H 304     8114   7963  17612   1772    -47   -172       N  
ATOM  11650  CA  GLN H 304     110.433 -62.756  60.978  1.00 81.29           C  
ANISOU11650  CA  GLN H 304     7163   7071  16654   1733    -60   -122       C  
ATOM  11651  C   GLN H 304     110.762 -62.710  59.494  1.00 76.84           C  
ANISOU11651  C   GLN H 304     6559   6495  16142   1633    -50    -82       C  
ATOM  11652  O   GLN H 304     111.722 -63.307  59.048  1.00 72.85           O  
ANISOU11652  O   GLN H 304     6029   5993  15657   1588    -88    -89       O  
ATOM  11653  CB  GLN H 304     109.318 -63.797  61.206  1.00 77.92           C  
ANISOU11653  CB  GLN H 304     6757   6702  16146   1764    -11    -39       C  
ATOM  11654  CG  GLN H 304     109.032 -64.167  62.662  1.00 80.90           C  
ANISOU11654  CG  GLN H 304     7177   7100  16463   1863    -20    -67       C  
ATOM  11655  CD  GLN H 304     110.034 -65.170  63.257  1.00 78.48           C  
ANISOU11655  CD  GLN H 304     6873   6813  16131   1887    -81   -100       C  
ATOM  11656  OE1 GLN H 304     111.255 -65.155  62.948  1.00 76.90           O  
ANISOU11656  OE1 GLN H 304     6648   6593  15977   1848   -139   -149       O  
ATOM  11657  NE2 GLN H 304     109.520 -66.054  64.128  1.00 78.40           N  
ANISOU11657  NE2 GLN H 304     6897   6844  16049   1953    -68    -75       N  
ATOM  11658  N   CYS H 305     109.948 -61.992  58.737  1.00 74.59           N  
ANISOU11658  N   CYS H 305     6269   6194  15877   1601      3    -41       N  
ATOM  11659  CA  CYS H 305     110.131 -61.865  57.302  1.00 73.00           C  
ANISOU11659  CA  CYS H 305     6036   5979  15723   1510     19      1       C  
ATOM  11660  C   CYS H 305     111.381 -61.085  56.986  1.00 73.84           C  
ANISOU11660  C   CYS H 305     6117   6029  15910   1470    -27    -74       C  
ATOM  11661  O   CYS H 305     112.091 -61.411  56.037  1.00 71.91           O  
ANISOU11661  O   CYS H 305     5843   5778  15702   1400    -40    -59       O  
ATOM  11662  CB  CYS H 305     108.928 -61.172  56.657  1.00 73.89           C  
ANISOU11662  CB  CYS H 305     6154   6084  15836   1494     85     55       C  
ATOM  11663  SG  CYS H 305     109.118 -60.819  54.880  1.00 72.56           S  
ANISOU11663  SG  CYS H 305     5952   5889  15730   1388    107    100       S  
ATOM  11664  N   ILE H 306     111.619 -60.025  57.756  1.00 73.13           N  
ANISOU11664  N   ILE H 306     6039   5898  15849   1514    -47   -154       N  
ATOM  11665  CA  ILE H 306     112.786 -59.180  57.562  1.00 73.77           C  
ANISOU11665  CA  ILE H 306     6097   5922  16010   1481    -90   -234       C  
ATOM  11666  C   ILE H 306     114.022 -60.004  57.840  1.00 73.34           C  
ANISOU11666  C   ILE H 306     6027   5877  15962   1474   -154   -277       C  
ATOM  11667  O   ILE H 306     114.860 -60.182  56.968  1.00 72.98           O  
ANISOU11667  O   ILE H 306     5949   5816  15965   1405   -173   -278       O  
ATOM  11668  CB  ILE H 306     112.761 -57.942  58.469  1.00 80.63           C  
ANISOU11668  CB  ILE H 306     6986   6749  16902   1537   -101   -315       C  
ATOM  11669  CG1 ILE H 306     111.716 -56.970  57.970  1.00 83.94           C  
ANISOU11669  CG1 ILE H 306     7413   7148  17332   1528    -40   -279       C  
ATOM  11670  CG2 ILE H 306     114.111 -57.239  58.480  1.00 84.53           C  
ANISOU11670  CG2 ILE H 306     7456   7188  17473   1512   -156   -411       C  
ATOM  11671  CD1 ILE H 306     111.716 -56.843  56.496  1.00 81.00           C  
ANISOU11671  CD1 ILE H 306     7013   6761  17002   1441     -9   -224       C  
ATOM  11672  N   ARG H 307     114.097 -60.550  59.046  1.00 79.33           N  
ANISOU11672  N   ARG H 307     6809   6662  16669   1547   -187   -310       N  
ATOM  11673  CA  ARG H 307     115.195 -61.413  59.420  1.00 76.66           C  
ANISOU11673  CA  ARG H 307     6461   6339  16326   1551   -251   -350       C  
ATOM  11674  C   ARG H 307     115.413 -62.527  58.408  1.00 68.73           C  
ANISOU11674  C   ARG H 307     5432   5369  15314   1483   -243   -278       C  
ATOM  11675  O   ARG H 307     116.515 -63.015  58.269  1.00 67.75           O  
ANISOU11675  O   ARG H 307     5285   5241  15215   1454   -293   -312       O  
ATOM  11676  CB  ARG H 307     114.952 -62.004  60.803  1.00 78.16           C  
ANISOU11676  CB  ARG H 307     6689   6565  16445   1644   -273   -373       C  
ATOM  11677  CG  ARG H 307     115.155 -61.018  61.907  1.00 85.92           C  
ANISOU11677  CG  ARG H 307     7694   7510  17441   1711   -305   -468       C  
ATOM  11678  CD  ARG H 307     115.046 -61.690  63.253  1.00 89.28           C  
ANISOU11678  CD  ARG H 307     8160   7969  17795   1802   -333   -493       C  
ATOM  11679  NE  ARG H 307     114.205 -60.895  64.130  1.00 92.56           N  
ANISOU11679  NE  ARG H 307     8612   8371  18185   1874   -308   -516       N  
ATOM  11680  CZ  ARG H 307     112.922 -61.162  64.371  1.00 91.99           C  
ANISOU11680  CZ  ARG H 307     8569   8331  18052   1912   -247   -447       C  
ATOM  11681  NH1 ARG H 307     112.343 -62.232  63.815  1.00 88.23           N  
ANISOU11681  NH1 ARG H 307     8086   7903  17533   1886   -208   -352       N  
ATOM  11682  NH2 ARG H 307     112.218 -60.359  65.176  1.00 95.38           N  
ANISOU11682  NH2 ARG H 307     9032   8743  18464   1976   -225   -475       N  
ATOM  11683  N   HIS H 308     114.370 -62.929  57.699  1.00 80.20           N  
ANISOU11683  N   HIS H 308     6888   6853  16732   1457   -182   -181       N  
ATOM  11684  CA  HIS H 308     114.523 -63.966  56.694  1.00 72.91           C  
ANISOU11684  CA  HIS H 308     5943   5961  15799   1391   -172   -110       C  
ATOM  11685  C   HIS H 308     115.302 -63.445  55.489  1.00 72.25           C  
ANISOU11685  C   HIS H 308     5822   5832  15796   1303   -177   -120       C  
ATOM  11686  O   HIS H 308     116.260 -64.056  55.071  1.00 68.78           O  
ANISOU11686  O   HIS H 308     5359   5395  15380   1259   -213   -129       O  
ATOM  11687  CB  HIS H 308     113.150 -64.515  56.258  1.00 69.30           C  
ANISOU11687  CB  HIS H 308     5501   5549  15281   1388   -104     -6       C  
ATOM  11688  CG  HIS H 308     113.224 -65.712  55.351  1.00 65.19           C  
ANISOU11688  CG  HIS H 308     4964   5068  14737   1329    -94     68       C  
ATOM  11689  ND1 HIS H 308     113.078 -65.623  53.982  1.00 64.60           N  
ANISOU11689  ND1 HIS H 308     4869   4983  14694   1249    -62    123       N  
ATOM  11690  CD2 HIS H 308     113.427 -67.024  55.618  1.00 64.90           C  
ANISOU11690  CD2 HIS H 308     4930   5080  14648   1339   -113     96       C  
ATOM  11691  CE1 HIS H 308     113.187 -66.825  53.445  1.00 63.98           C  
ANISOU11691  CE1 HIS H 308     4781   4945  14583   1211    -61    181       C  
ATOM  11692  NE2 HIS H 308     113.403 -67.692  54.416  1.00 64.14           N  
ANISOU11692  NE2 HIS H 308     4815   5003  14553   1264    -92    166       N  
ATOM  11693  N   TYR H 309     114.887 -62.328  54.925  1.00 70.35           N  
ANISOU11693  N   TYR H 309     5578   5551  15600   1279   -141   -118       N  
ATOM  11694  CA  TYR H 309     115.426 -61.864  53.644  1.00 69.44           C  
ANISOU11694  CA  TYR H 309     5431   5396  15557   1194   -132   -110       C  
ATOM  11695  C   TYR H 309     116.767 -61.098  53.682  1.00 73.54           C  
ANISOU11695  C   TYR H 309     5926   5856  16161   1170   -181   -207       C  
ATOM  11696  O   TYR H 309     117.602 -61.173  52.778  1.00 71.88           O  
ANISOU11696  O   TYR H 309     5684   5621  16005   1100   -193   -209       O  
ATOM  11697  CB  TYR H 309     114.365 -60.988  52.988  1.00 71.62           C  
ANISOU11697  CB  TYR H 309     5717   5654  15843   1178    -69    -64       C  
ATOM  11698  CG  TYR H 309     113.404 -61.786  52.178  1.00 66.06           C  
ANISOU11698  CG  TYR H 309     5017   4995  15088   1149    -19     41       C  
ATOM  11699  CD1 TYR H 309     113.791 -62.315  50.959  1.00 64.52           C  
ANISOU11699  CD1 TYR H 309     4799   4801  14914   1071    -13     89       C  
ATOM  11700  CD2 TYR H 309     112.127 -62.044  52.630  1.00 65.93           C  
ANISOU11700  CD2 TYR H 309     5029   5020  15002   1199     20     92       C  
ATOM  11701  CE1 TYR H 309     112.924 -63.046  50.189  1.00 63.87           C  
ANISOU11701  CE1 TYR H 309     4722   4759  14786   1042     30    182       C  
ATOM  11702  CE2 TYR H 309     111.249 -62.782  51.865  1.00 64.50           C  
ANISOU11702  CE2 TYR H 309     4851   4880  14777   1169     64    186       C  
ATOM  11703  CZ  TYR H 309     111.663 -63.276  50.645  1.00 63.87           C  
ANISOU11703  CZ  TYR H 309     4749   4799  14719   1091     68    229       C  
ATOM  11704  OH  TYR H 309     110.826 -64.016  49.866  1.00 63.24           O  
ANISOU11704  OH  TYR H 309     4673   4759  14595   1061    108    318       O  
ATOM  11705  N   GLU H 310     116.892 -60.287  54.718  1.00 67.47           N  
ANISOU11705  N   GLU H 310     5171   5061  15403   1230   -206   -285       N  
ATOM  11706  CA  GLU H 310     118.084 -59.555  55.091  1.00 72.67           C  
ANISOU11706  CA  GLU H 310     5812   5668  16131   1228   -259   -390       C  
ATOM  11707  C   GLU H 310     118.387 -60.252  56.395  1.00 73.37           C  
ANISOU11707  C   GLU H 310     5919   5791  16168   1301   -312   -436       C  
ATOM  11708  O   GLU H 310     117.736 -61.250  56.691  1.00 68.95           O  
ANISOU11708  O   GLU H 310     5379   5287  15533   1332   -298   -377       O  
ATOM  11709  CB  GLU H 310     117.771 -58.065  55.197  1.00 79.72           C  
ANISOU11709  CB  GLU H 310     6713   6509  17069   1241   -236   -433       C  
ATOM  11710  CG  GLU H 310     116.927 -57.632  53.972  1.00 78.67           C  
ANISOU11710  CG  GLU H 310     6576   6365  16949   1188   -167   -353       C  
ATOM  11711  CD  GLU H 310     116.025 -56.434  54.181  1.00 84.86           C  
ANISOU11711  CD  GLU H 310     7382   7123  17737   1220   -127   -359       C  
ATOM  11712  OE1 GLU H 310     115.665 -56.127  55.336  1.00 89.77           O  
ANISOU11712  OE1 GLU H 310     8032   7751  18326   1294   -138   -400       O  
ATOM  11713  OE2 GLU H 310     115.665 -55.808  53.165  1.00 84.82           O  
ANISOU11713  OE2 GLU H 310     7369   7092  17767   1170    -82   -320       O  
ATOM  11714  N   GLY H 311     119.351 -59.830  57.182  1.00 72.99           N  
ANISOU11714  N   GLY H 311     5866   5711  16155   1329   -372   -539       N  
ATOM  11715  CA  GLY H 311     119.622 -60.683  58.324  1.00 72.78           C  
ANISOU11715  CA  GLY H 311     5859   5724  16070   1396   -422   -572       C  
ATOM  11716  C   GLY H 311     119.017 -60.164  59.599  1.00 75.76           C  
ANISOU11716  C   GLY H 311     6276   6103  16406   1488   -426   -614       C  
ATOM  11717  O   GLY H 311     119.002 -60.853  60.630  1.00 75.41           O  
ANISOU11717  O   GLY H 311     6258   6094  16300   1556   -458   -632       O  
ATOM  11718  N   SER H 312     118.431 -58.977  59.475  1.00 79.02           N  
ANISOU11718  N   SER H 312     6698   6479  16848   1490   -387   -621       N  
ATOM  11719  CA  SER H 312     118.591 -57.937  60.470  1.00 85.90           C  
ANISOU11719  CA  SER H 312     7588   7314  17737   1548   -414   -714       C  
ATOM  11720  C   SER H 312     117.494 -57.616  61.491  1.00 92.41           C  
ANISOU11720  C   SER H 312     8459   8154  18499   1634   -388   -710       C  
ATOM  11721  O   SER H 312     117.605 -58.048  62.644  1.00 95.92           O  
ANISOU11721  O   SER H 312     8931   8620  18893   1708   -428   -751       O  
ATOM  11722  CB  SER H 312     118.902 -56.650  59.712  1.00 86.55           C  
ANISOU11722  CB  SER H 312     7645   7333  17908   1491   -397   -747       C  
ATOM  11723  OG  SER H 312     117.743 -56.149  59.039  1.00 90.16           O  
ANISOU11723  OG  SER H 312     8111   7788  18357   1472   -322   -671       O  
ATOM  11724  N   THR H 313     116.410 -56.952  61.051  1.00 85.00           N  
ANISOU11724  N   THR H 313     7531   7208  17558   1626   -321   -655       N  
ATOM  11725  CA  THR H 313     115.900 -55.739  61.722  1.00 92.10           C  
ANISOU11725  CA  THR H 313     8456   8073  18463   1676   -307   -703       C  
ATOM  11726  C   THR H 313     117.003 -54.700  61.491  1.00 98.16           C  
ANISOU11726  C   THR H 313     9197   8778  19323   1637   -345   -794       C  
ATOM  11727  O   THR H 313     117.106 -54.190  60.374  1.00 99.38           O  
ANISOU11727  O   THR H 313     9323   8902  19536   1564   -315   -769       O  
ATOM  11728  CB  THR H 313     115.587 -55.906  63.219  1.00 94.46           C  
ANISOU11728  CB  THR H 313     8799   8393  18697   1778   -332   -746       C  
ATOM  11729  OG1 THR H 313     114.793 -57.077  63.405  1.00 90.25           O  
ANISOU11729  OG1 THR H 313     8286   7921  18084   1808   -304   -665       O  
ATOM  11730  CG2 THR H 313     114.801 -54.727  63.733  1.00101.90           C  
ANISOU11730  CG2 THR H 313     9770   9307  19639   1823   -300   -770       C  
ATOM  11731  N   VAL H 314     117.801 -54.372  62.511  1.00 92.59           N  
ANISOU11731  N   VAL H 314     8501   8051  18629   1684   -408   -899       N  
ATOM  11732  CA  VAL H 314     118.804 -53.283  62.445  1.00 99.21           C  
ANISOU11732  CA  VAL H 314     9315   8826  19553   1656   -444   -996       C  
ATOM  11733  C   VAL H 314     119.703 -53.223  61.183  1.00 97.19           C  
ANISOU11733  C   VAL H 314     9009   8541  19379   1557   -446   -992       C  
ATOM  11734  O   VAL H 314     120.358 -54.207  60.828  1.00 93.35           O  
ANISOU11734  O   VAL H 314     8499   8076  18892   1524   -474   -976       O  
ATOM  11735  CB  VAL H 314     119.736 -53.366  63.682  1.00103.35           C  
ANISOU11735  CB  VAL H 314     9853   9346  20071   1716   -526  -1106       C  
ATOM  11736  CG1 VAL H 314     119.938 -54.809  64.100  1.00 98.85           C  
ANISOU11736  CG1 VAL H 314     9290   8831  19436   1745   -561  -1082       C  
ATOM  11737  CG2 VAL H 314     121.073 -52.673  63.413  1.00104.23           C  
ANISOU11737  CG2 VAL H 314     9925   9402  20274   1667   -575  -1201       C  
ATOM  11738  N   PRO H 315     119.760 -52.039  60.530  1.00 97.28           N  
ANISOU11738  N   PRO H 315     9004   8498  19460   1511   -417  -1010       N  
ATOM  11739  CA  PRO H 315     120.299 -51.902  59.169  1.00 94.36           C  
ANISOU11739  CA  PRO H 315     8592   8099  19162   1416   -397   -983       C  
ATOM  11740  C   PRO H 315     121.807 -52.144  59.030  1.00 94.64           C  
ANISOU11740  C   PRO H 315     8588   8110  19259   1374   -459  -1057       C  
ATOM  11741  O   PRO H 315     122.305 -52.311  57.912  1.00 91.99           O  
ANISOU11741  O   PRO H 315     8217   7759  18976   1295   -446  -1027       O  
ATOM  11742  CB  PRO H 315     119.951 -50.459  58.801  1.00100.02           C  
ANISOU11742  CB  PRO H 315     9310   8762  19930   1397   -355  -1000       C  
ATOM  11743  CG  PRO H 315     118.854 -50.095  59.714  1.00105.34           C  
ANISOU11743  CG  PRO H 315    10029   9454  20542   1475   -333   -993       C  
ATOM  11744  CD  PRO H 315     119.173 -50.778  60.994  1.00104.27           C  
ANISOU11744  CD  PRO H 315     9914   9350  20353   1548   -393  -1046       C  
ATOM  11745  N   GLU H 316     122.532 -52.142  60.138  1.00 99.53           N  
ANISOU11745  N   GLU H 316     9214   8725  19876   1426   -528  -1153       N  
ATOM  11746  CA  GLU H 316     123.980 -52.299  60.068  1.00100.04           C  
ANISOU11746  CA  GLU H 316     9242   8766  20004   1389   -590  -1233       C  
ATOM  11747  C   GLU H 316     124.351 -53.785  59.990  1.00 91.70           C  
ANISOU11747  C   GLU H 316     8175   7760  18907   1382   -621  -1195       C  
ATOM  11748  O   GLU H 316     125.459 -54.163  59.569  1.00 89.82           O  
ANISOU11748  O   GLU H 316     7899   7509  18719   1332   -660  -1229       O  
ATOM  11749  CB  GLU H 316     124.643 -51.609  61.270  1.00107.32           C  
ANISOU11749  CB  GLU H 316    10175   9659  20943   1446   -654  -1360       C  
ATOM  11750  CG  GLU H 316     123.791 -50.486  61.905  1.00115.15           C  
ANISOU11750  CG  GLU H 316    11203  10630  21918   1500   -625  -1381       C  
ATOM  11751  CD  GLU H 316     123.411 -49.373  60.925  1.00118.46           C  
ANISOU11751  CD  GLU H 316    11609  11004  22398   1441   -560  -1352       C  
ATOM  11752  OE1 GLU H 316     124.137 -49.192  59.922  1.00118.03           O  
ANISOU11752  OE1 GLU H 316    11512  10916  22418   1361   -553  -1354       O  
ATOM  11753  OE2 GLU H 316     122.385 -48.683  61.156  1.00121.66           O  
ANISOU11753  OE2 GLU H 316    12045  11406  22775   1476   -515  -1326       O  
ATOM  11754  N   LYS H 317     123.411 -54.625  60.401  1.00100.68           N  
ANISOU11754  N   LYS H 317     9347   8955  19953   1432   -603  -1124       N  
ATOM  11755  CA  LYS H 317     123.590 -56.072  60.351  1.00 93.03           C  
ANISOU11755  CA  LYS H 317     8374   8039  18933   1431   -625  -1076       C  
ATOM  11756  C   LYS H 317     122.925 -56.675  59.106  1.00 85.72           C  
ANISOU11756  C   LYS H 317     7435   7139  17994   1368   -559   -953       C  
ATOM  11757  O   LYS H 317     122.879 -57.886  58.930  1.00 79.25           O  
ANISOU11757  O   LYS H 317     6615   6368  17127   1362   -564   -895       O  
ATOM  11758  CB  LYS H 317     123.047 -56.679  61.640  1.00 92.95           C  
ANISOU11758  CB  LYS H 317     8410   8077  18830   1528   -649  -1080       C  
ATOM  11759  CG  LYS H 317     123.418 -55.831  62.855  1.00101.33           C  
ANISOU11759  CG  LYS H 317     9493   9109  19900   1596   -699  -1195       C  
ATOM  11760  CD  LYS H 317     123.665 -56.680  64.088  1.00101.21           C  
ANISOU11760  CD  LYS H 317     9508   9133  19814   1677   -761  -1237       C  
ATOM  11761  CE  LYS H 317     124.664 -56.005  65.026  1.00108.69           C  
ANISOU11761  CE  LYS H 317    10458  10044  20797   1716   -838  -1373       C  
ATOM  11762  NZ  LYS H 317     125.016 -56.850  66.203  1.00108.90           N  
ANISOU11762  NZ  LYS H 317    10514  10106  20756   1794   -906  -1420       N  
ATOM  11763  N   LYS H 318     122.391 -55.803  58.255  1.00 90.32           N  
ANISOU11763  N   LYS H 318     8011   7690  18616   1324   -499   -915       N  
ATOM  11764  CA  LYS H 318     121.741 -56.226  57.016  1.00 84.14           C  
ANISOU11764  CA  LYS H 318     7219   6926  17825   1264   -437   -804       C  
ATOM  11765  C   LYS H 318     122.737 -56.878  56.058  1.00 79.16           C  
ANISOU11765  C   LYS H 318     6547   6289  17242   1185   -455   -793       C  
ATOM  11766  O   LYS H 318     123.810 -56.320  55.799  1.00 82.45           O  
ANISOU11766  O   LYS H 318     6931   6656  17740   1144   -485   -865       O  
ATOM  11767  CB  LYS H 318     121.052 -55.031  56.330  1.00 87.85           C  
ANISOU11767  CB  LYS H 318     7691   7355  18332   1235   -374   -778       C  
ATOM  11768  CG  LYS H 318     119.694 -54.661  56.910  1.00 91.58           C  
ANISOU11768  CG  LYS H 318     8206   7848  18742   1299   -332   -741       C  
ATOM  11769  CD  LYS H 318     118.714 -54.307  55.804  1.00 89.07           C  
ANISOU11769  CD  LYS H 318     7889   7526  18426   1255   -256   -650       C  
ATOM  11770  CE  LYS H 318     117.414 -53.752  56.351  1.00 93.80           C  
ANISOU11770  CE  LYS H 318     8527   8137  18975   1315   -214   -623       C  
ATOM  11771  NZ  LYS H 318     116.585 -54.797  57.018  1.00 92.73           N  
ANISOU11771  NZ  LYS H 318     8420   8067  18745   1373   -207   -569       N  
ATOM  11772  N   THR H 319     122.372 -58.053  55.549  1.00 82.41           N  
ANISOU11772  N   THR H 319     6958   6751  17603   1164   -436   -704       N  
ATOM  11773  CA  THR H 319     123.113 -58.743  54.488  1.00 77.01           C  
ANISOU11773  CA  THR H 319     6238   6066  16955   1084   -441   -673       C  
ATOM  11774  C   THR H 319     122.117 -59.443  53.576  1.00 70.43           C  
ANISOU11774  C   THR H 319     5413   5274  16072   1052   -380   -549       C  
ATOM  11775  O   THR H 319     121.000 -59.702  54.002  1.00 68.78           O  
ANISOU11775  O   THR H 319     5238   5106  15790   1102   -350   -496       O  
ATOM  11776  CB  THR H 319     124.108 -59.764  55.052  1.00 74.23           C  
ANISOU11776  CB  THR H 319     5874   5740  16589   1098   -511   -717       C  
ATOM  11777  OG1 THR H 319     123.479 -60.539  56.085  1.00 72.74           O  
ANISOU11777  OG1 THR H 319     5722   5610  16307   1176   -525   -698       O  
ATOM  11778  CG2 THR H 319     125.300 -59.054  55.624  1.00 80.47           C  
ANISOU11778  CG2 THR H 319     6644   6481  17449   1105   -572   -842       C  
ATOM  11779  N   PRO H 320     122.492 -59.722  52.315  1.00 67.13           N  
ANISOU11779  N   PRO H 320     4968   4845  15695    970   -359   -504       N  
ATOM  11780  CA  PRO H 320     121.549 -60.404  51.422  1.00 66.36           C  
ANISOU11780  CA  PRO H 320     4880   4786  15549    938   -303   -388       C  
ATOM  11781  C   PRO H 320     121.378 -61.887  51.702  1.00 65.92           C  
ANISOU11781  C   PRO H 320     4834   4798  15413    957   -319   -336       C  
ATOM  11782  O   PRO H 320     122.109 -62.659  51.114  1.00 65.50           O  
ANISOU11782  O   PRO H 320     4759   4752  15376    906   -338   -322       O  
ATOM  11783  CB  PRO H 320     122.155 -60.177  50.033  1.00 65.97           C  
ANISOU11783  CB  PRO H 320     4797   4696  15574    846   -283   -369       C  
ATOM  11784  CG  PRO H 320     122.898 -58.920  50.169  1.00 66.61           C  
ANISOU11784  CG  PRO H 320     4860   4710  15740    837   -300   -461       C  
ATOM  11785  CD  PRO H 320     123.514 -59.001  51.546  1.00 67.25           C  
ANISOU11785  CD  PRO H 320     4945   4796  15810    902   -366   -554       C  
ATOM  11786  N   LYS H 321     120.464 -62.263  52.598  1.00 66.63           N  
ANISOU11786  N   LYS H 321     4960   4935  15423   1029   -312   -312       N  
ATOM  11787  CA  LYS H 321     120.217 -63.666  52.964  1.00 66.26           C  
ANISOU11787  CA  LYS H 321     4926   4955  15294   1054   -324   -262       C  
ATOM  11788  C   LYS H 321     119.201 -64.386  52.069  1.00 65.49           C  
ANISOU11788  C   LYS H 321     4838   4899  15145   1021   -264   -146       C  
ATOM  11789  O   LYS H 321     118.814 -65.516  52.351  1.00 65.16           O  
ANISOU11789  O   LYS H 321     4812   4915  15032   1043   -264    -96       O  
ATOM  11790  CB  LYS H 321     119.732 -63.754  54.419  1.00 66.79           C  
ANISOU11790  CB  LYS H 321     5028   5052  15298   1152   -343   -294       C  
ATOM  11791  CG  LYS H 321     120.448 -62.834  55.383  1.00 67.64           C  
ANISOU11791  CG  LYS H 321     5136   5116  15449   1197   -393   -408       C  
ATOM  11792  CD  LYS H 321     121.816 -63.363  55.790  1.00 67.84           C  
ANISOU11792  CD  LYS H 321     5141   5138  15498   1195   -469   -482       C  
ATOM  11793  CE  LYS H 321     121.678 -64.604  56.672  1.00 67.79           C  
ANISOU11793  CE  LYS H 321     5158   5194  15405   1254   -498   -465       C  
ATOM  11794  NZ  LYS H 321     122.962 -65.368  56.808  1.00 67.78           N  
ANISOU11794  NZ  LYS H 321     5135   5199  15421   1238   -566   -514       N  
ATOM  11795  N   SER H 322     118.733 -63.715  51.020  1.00 70.16           N  
ANISOU11795  N   SER H 322     5423   5463  15773    970   -214   -103       N  
ATOM  11796  CA  SER H 322     117.583 -64.206  50.243  1.00 65.91           C  
ANISOU11796  CA  SER H 322     4898   4961  15183    948   -154      3       C  
ATOM  11797  C   SER H 322     117.832 -65.537  49.557  1.00 63.63           C  
ANISOU11797  C   SER H 322     4600   4712  14864    900   -157     64       C  
ATOM  11798  O   SER H 322     118.726 -65.622  48.746  1.00 63.11           O  
ANISOU11798  O   SER H 322     4508   4619  14851    835   -172     56       O  
ATOM  11799  CB  SER H 322     117.181 -63.168  49.187  1.00 68.37           C  
ANISOU11799  CB  SER H 322     5203   5228  15546    900   -106     27       C  
ATOM  11800  OG  SER H 322     116.166 -63.684  48.345  1.00 64.54           O  
ANISOU11800  OG  SER H 322     4729   4777  15016    872    -54    126       O  
ATOM  11801  N   PRO H 323     117.037 -66.567  49.879  1.00 65.89           N  
ANISOU11801  N   PRO H 323     4909   5062  15066    931   -142    126       N  
ATOM  11802  CA  PRO H 323     117.078 -67.905  49.252  1.00 62.22           C  
ANISOU11802  CA  PRO H 323     4440   4641  14558    889   -138    195       C  
ATOM  11803  C   PRO H 323     117.089 -67.999  47.710  1.00 61.55           C  
ANISOU11803  C   PRO H 323     4341   4542  14505    801   -105    256       C  
ATOM  11804  O   PRO H 323     117.825 -68.873  47.208  1.00 61.12           O  
ANISOU11804  O   PRO H 323     4273   4498  14453    755   -127    271       O  
ATOM  11805  CB  PRO H 323     115.827 -68.563  49.812  1.00 62.10           C  
ANISOU11805  CB  PRO H 323     4455   4686  14453    943   -105    255       C  
ATOM  11806  CG  PRO H 323     115.822 -68.052  51.224  1.00 62.86           C  
ANISOU11806  CG  PRO H 323     4568   4778  14539   1027   -132    185       C  
ATOM  11807  CD  PRO H 323     116.343 -66.621  51.173  1.00 68.13           C  
ANISOU11807  CD  PRO H 323     5221   5377  15289   1019   -143    112       C  
ATOM  11808  N   VAL H 324     116.338 -67.172  46.979  1.00 62.18           N  
ANISOU11808  N   VAL H 324     4424   4596  14605    779    -56    289       N  
ATOM  11809  CA  VAL H 324     116.579 -67.080  45.534  1.00 61.40           C  
ANISOU11809  CA  VAL H 324     4309   4468  14551    697    -33    329       C  
ATOM  11810  C   VAL H 324     117.669 -66.029  45.301  1.00 62.22           C  
ANISOU11810  C   VAL H 324     4386   4503  14753    666    -56    253       C  
ATOM  11811  O   VAL H 324     118.174 -65.454  46.258  1.00 63.76           O  
ANISOU11811  O   VAL H 324     4576   4675  14974    710    -91    174       O  
ATOM  11812  CB  VAL H 324     115.316 -66.724  44.751  1.00 61.19           C  
ANISOU11812  CB  VAL H 324     4298   4448  14504    683     29    402       C  
ATOM  11813  CG1 VAL H 324     114.117 -67.473  45.307  1.00 60.85           C  
ANISOU11813  CG1 VAL H 324     4282   4469  14369    733     53    457       C  
ATOM  11814  CG2 VAL H 324     115.049 -65.250  44.819  1.00 62.49           C  
ANISOU11814  CG2 VAL H 324     4462   4563  14719    700     48    362       C  
ATOM  11815  N   GLY H 325     118.046 -65.762  44.055  1.00 61.03           N  
ANISOU11815  N   GLY H 325     4217   4314  14656    594    -37    275       N  
ATOM  11816  CA  GLY H 325     119.100 -64.777  43.809  1.00 61.42           C  
ANISOU11816  CA  GLY H 325     4239   4296  14801    562    -56    202       C  
ATOM  11817  C   GLY H 325     118.840 -63.314  44.202  1.00 62.07           C  
ANISOU11817  C   GLY H 325     4324   4334  14927    595    -43    150       C  
ATOM  11818  O   GLY H 325     119.760 -62.586  44.543  1.00 62.59           O  
ANISOU11818  O   GLY H 325     4369   4353  15059    595    -73     67       O  
ATOM  11819  N   VAL H 326     117.577 -62.888  44.159  1.00 62.20           N  
ANISOU11819  N   VAL H 326     4365   4365  14905    623      2    196       N  
ATOM  11820  CA  VAL H 326     117.253 -61.462  44.198  1.00 63.48           C  
ANISOU11820  CA  VAL H 326     4529   4480  15109    639     26    161       C  
ATOM  11821  C   VAL H 326     116.498 -61.021  45.454  1.00 64.54           C  
ANISOU11821  C   VAL H 326     4689   4630  15202    722     24    132       C  
ATOM  11822  O   VAL H 326     115.814 -61.812  46.085  1.00 64.15           O  
ANISOU11822  O   VAL H 326     4661   4636  15078    767     25    166       O  
ATOM  11823  CB  VAL H 326     116.442 -61.045  42.961  1.00 63.11           C  
ANISOU11823  CB  VAL H 326     4489   4423  15067    598     84    232       C  
ATOM  11824  CG1 VAL H 326     116.717 -61.970  41.808  1.00 61.67           C  
ANISOU11824  CG1 VAL H 326     4294   4256  14882    530     93    294       C  
ATOM  11825  CG2 VAL H 326     115.002 -61.053  43.262  1.00 63.19           C  
ANISOU11825  CG2 VAL H 326     4530   4473  15007    645    120    284       C  
ATOM  11826  N   GLN H 327     116.677 -59.754  45.826  1.00 64.04           N  
ANISOU11826  N   GLN H 327     4624   4517  15190    743     23     66       N  
ATOM  11827  CA  GLN H 327     116.171 -59.236  47.087  1.00 65.20           C  
ANISOU11827  CA  GLN H 327     4794   4670  15309    822     14     22       C  
ATOM  11828  C   GLN H 327     114.820 -58.545  46.928  1.00 65.64           C  
ANISOU11828  C   GLN H 327     4875   4729  15335    846     69     68       C  
ATOM  11829  O   GLN H 327     114.595 -57.768  45.992  1.00 66.62           O  
ANISOU11829  O   GLN H 327     4996   4819  15499    807    104     88       O  
ATOM  11830  CB  GLN H 327     117.181 -58.270  47.702  1.00 67.08           C  
ANISOU11830  CB  GLN H 327     5018   4853  15618    835    -24    -84       C  
ATOM  11831  CG  GLN H 327     118.416 -58.912  48.254  1.00 66.40           C  
ANISOU11831  CG  GLN H 327     4911   4768  15549    834    -87   -145       C  
ATOM  11832  CD  GLN H 327     118.178 -59.649  49.564  1.00 66.52           C  
ANISOU11832  CD  GLN H 327     4948   4833  15493    909   -120   -161       C  
ATOM  11833  OE1 GLN H 327     117.340 -59.248  50.377  1.00 68.18           O  
ANISOU11833  OE1 GLN H 327     5186   5056  15663    973   -106   -166       O  
ATOM  11834  NE2 GLN H 327     118.919 -60.751  49.769  1.00 65.73           N  
ANISOU11834  NE2 GLN H 327     4837   4763  15376    902   -163   -168       N  
ATOM  11835  N   PRO H 328     113.897 -58.828  47.846  1.00 64.54           N  
ANISOU11835  N   PRO H 328     4763   4632  15126    913     76     84       N  
ATOM  11836  CA  PRO H 328     112.615 -58.127  47.808  1.00 64.65           C  
ANISOU11836  CA  PRO H 328     4801   4648  15115    942    125    119       C  
ATOM  11837  C   PRO H 328     112.804 -56.734  48.369  1.00 70.93           C  
ANISOU11837  C   PRO H 328     5602   5390  15960    972    120     42       C  
ATOM  11838  O   PRO H 328     113.789 -56.491  49.072  1.00 73.52           O  
ANISOU11838  O   PRO H 328     5920   5692  16324    988     74    -39       O  
ATOM  11839  CB  PRO H 328     111.737 -58.967  48.715  1.00 64.61           C  
ANISOU11839  CB  PRO H 328     4821   4705  15024   1004    129    152       C  
ATOM  11840  CG  PRO H 328     112.735 -59.407  49.793  1.00 64.97           C  
ANISOU11840  CG  PRO H 328     4860   4755  15070   1039     70     81       C  
ATOM  11841  CD  PRO H 328     114.072 -59.600  49.088  1.00 64.76           C  
ANISOU11841  CD  PRO H 328     4801   4699  15105    972     37     54       C  
ATOM  11842  N   ILE H 329     111.863 -55.841  48.065  1.00 66.39           N  
ANISOU11842  N   ILE H 329     5043   4799  15385    981    164     66       N  
ATOM  11843  CA  ILE H 329     111.835 -54.495  48.616  1.00 67.09           C  
ANISOU11843  CA  ILE H 329     5141   4840  15510   1015    166      0       C  
ATOM  11844  C   ILE H 329     111.129 -54.532  49.947  1.00 67.51           C  
ANISOU11844  C   ILE H 329     5222   4922  15506   1099    162    -19       C  
ATOM  11845  O   ILE H 329     109.972 -54.930  50.007  1.00 67.28           O  
ANISOU11845  O   ILE H 329     5213   4936  15415   1125    196     44       O  
ATOM  11846  CB  ILE H 329     111.109 -53.548  47.690  1.00 67.02           C  
ANISOU11846  CB  ILE H 329     5139   4803  15523    989    217     37       C  
ATOM  11847  CG1 ILE H 329     111.638 -53.704  46.270  1.00 66.50           C  
ANISOU11847  CG1 ILE H 329     5049   4718  15500    907    229     74       C  
ATOM  11848  CG2 ILE H 329     111.246 -52.144  48.185  1.00 67.73           C  
ANISOU11848  CG2 ILE H 329     5237   4839  15659   1016    217    -35       C  
ATOM  11849  CD1 ILE H 329     111.337 -52.537  45.388  1.00 66.60           C  
ANISOU11849  CD1 ILE H 329     5063   4685  15556    877    268     82       C  
ATOM  11850  N   LEU H 330     111.809 -54.153  51.023  1.00 69.31           N  
ANISOU11850  N   LEU H 330     5452   5129  15753   1141    120   -105       N  
ATOM  11851  CA  LEU H 330     111.177 -54.247  52.337  1.00 70.30           C  
ANISOU11851  CA  LEU H 330     5607   5284  15821   1224    114   -124       C  
ATOM  11852  C   LEU H 330     111.266 -52.980  53.188  1.00 78.59           C  
ANISOU11852  C   LEU H 330     6671   6289  16902   1271    104   -206       C  
ATOM  11853  O   LEU H 330     112.340 -52.602  53.651  1.00 81.74           O  
ANISOU11853  O   LEU H 330     7059   6653  17347   1274     58   -290       O  
ATOM  11854  CB  LEU H 330     111.768 -55.422  53.107  1.00 69.68           C  
ANISOU11854  CB  LEU H 330     5525   5245  15705   1251     68   -141       C  
ATOM  11855  CG  LEU H 330     111.196 -56.795  52.732  1.00 68.99           C  
ANISOU11855  CG  LEU H 330     5439   5221  15553   1238     86    -52       C  
ATOM  11856  CD1 LEU H 330     112.041 -57.889  53.304  1.00 68.92           C  
ANISOU11856  CD1 LEU H 330     5423   5242  15523   1250     36    -76       C  
ATOM  11857  CD2 LEU H 330     109.790 -56.938  53.241  1.00 69.02           C  
ANISOU11857  CD2 LEU H 330     5473   5264  15486   1294    128     -3       C  
ATOM  11858  N   ASN H 331     110.110 -52.361  53.426  1.00 75.10           N  
ANISOU11858  N   ASN H 331     6254   5849  16430   1310    145   -183       N  
ATOM  11859  CA  ASN H 331     110.024 -51.129  54.187  1.00 77.72           C  
ANISOU11859  CA  ASN H 331     6604   6141  16785   1355    143   -253       C  
ATOM  11860  C   ASN H 331     108.737 -51.123  54.977  1.00 79.50           C  
ANISOU11860  C   ASN H 331     6863   6399  16943   1425    174   -225       C  
ATOM  11861  O   ASN H 331     108.137 -52.166  55.184  1.00 76.35           O  
ANISOU11861  O   ASN H 331     6473   6055  16481   1447    186   -169       O  
ATOM  11862  CB  ASN H 331     110.129 -49.909  53.272  1.00 81.97           C  
ANISOU11862  CB  ASN H 331     7132   6622  17390   1307    168   -263       C  
ATOM  11863  CG  ASN H 331     109.187 -49.973  52.091  1.00 78.70           C  
ANISOU11863  CG  ASN H 331     6719   6223  16962   1266    223   -170       C  
ATOM  11864  OD1 ASN H 331     108.009 -50.252  52.243  1.00 77.83           O  
ANISOU11864  OD1 ASN H 331     6628   6150  16793   1299    258   -114       O  
ATOM  11865  ND2 ASN H 331     109.707 -49.698  50.903  1.00 77.24           N  
ANISOU11865  ND2 ASN H 331     6511   6005  16831   1195    233   -156       N  
ATOM  11866  N   GLU H 332     108.345 -49.958  55.477  1.00 79.15           N  
ANISOU11866  N   GLU H 332     6838   6322  16913   1463    188   -267       N  
ATOM  11867  CA  GLU H 332     107.066 -49.808  56.190  1.00 81.55           C  
ANISOU11867  CA  GLU H 332     7175   6652  17158   1528    223   -242       C  
ATOM  11868  C   GLU H 332     105.840 -49.732  55.277  1.00 79.90           C  
ANISOU11868  C   GLU H 332     6970   6460  16928   1505    284   -155       C  
ATOM  11869  O   GLU H 332     104.721 -49.770  55.760  1.00 81.47           O  
ANISOU11869  O   GLU H 332     7192   6686  17075   1553    317   -123       O  
ATOM  11870  CB  GLU H 332     107.104 -48.567  57.084  1.00 90.23           C  
ANISOU11870  CB  GLU H 332     8295   7708  18281   1578    214   -323       C  
ATOM  11871  CG  GLU H 332     107.109 -47.244  56.331  1.00 95.52           C  
ANISOU11871  CG  GLU H 332     8958   8322  19012   1539    237   -339       C  
ATOM  11872  CD  GLU H 332     108.434 -46.945  55.639  1.00 95.64           C  
ANISOU11872  CD  GLU H 332     8943   8293  19104   1474    205   -383       C  
ATOM  11873  OE1 GLU H 332     109.406 -47.719  55.822  1.00 93.24           O  
ANISOU11873  OE1 GLU H 332     8620   7999  18807   1461    160   -409       O  
ATOM  11874  OE2 GLU H 332     108.495 -45.923  54.915  1.00 98.37           O  
ANISOU11874  OE2 GLU H 332     9282   8593  19503   1436    226   -391       O  
ATOM  11875  N   HIS H 333     106.060 -49.622  53.969  1.00 84.19           N  
ANISOU11875  N   HIS H 333     7491   6986  17511   1432    299   -117       N  
ATOM  11876  CA  HIS H 333     104.976 -49.689  52.994  1.00 81.96           C  
ANISOU11876  CA  HIS H 333     7211   6723  17206   1404    351    -32       C  
ATOM  11877  C   HIS H 333     104.742 -51.115  52.442  1.00 73.67           C  
ANISOU11877  C   HIS H 333     6150   5730  16112   1376    358     46       C  
ATOM  11878  O   HIS H 333     103.940 -51.293  51.520  1.00 71.17           O  
ANISOU11878  O   HIS H 333     5832   5431  15779   1345    396    118       O  
ATOM  11879  CB  HIS H 333     105.243 -48.736  51.826  1.00 83.94           C  
ANISOU11879  CB  HIS H 333     7449   6924  17522   1343    367    -31       C  
ATOM  11880  CG  HIS H 333     105.338 -47.292  52.223  1.00 92.04           C  
ANISOU11880  CG  HIS H 333     8487   7894  18590   1366    369    -98       C  
ATOM  11881  ND1 HIS H 333     106.155 -46.393  51.567  1.00 94.60           N  
ANISOU11881  ND1 HIS H 333     8797   8161  18987   1319    362   -137       N  
ATOM  11882  CD2 HIS H 333     104.722 -46.589  53.205  1.00 98.39           C  
ANISOU11882  CD2 HIS H 333     9317   8691  19375   1431    378   -133       C  
ATOM  11883  CE1 HIS H 333     106.050 -45.204  52.135  1.00102.11           C  
ANISOU11883  CE1 HIS H 333     9764   9072  19960   1353    366   -194       C  
ATOM  11884  NE2 HIS H 333     105.191 -45.298  53.134  1.00104.57           N  
ANISOU11884  NE2 HIS H 333    10101   9414  20218   1421    375   -193       N  
ATOM  11885  N   THR H 334     105.438 -52.120  52.980  1.00 79.96           N  
ANISOU11885  N   THR H 334     6939   6554  16890   1385    319     31       N  
ATOM  11886  CA  THR H 334     105.267 -53.489  52.525  1.00 76.72           C  
ANISOU11886  CA  THR H 334     6518   6197  16436   1359    324    100       C  
ATOM  11887  C   THR H 334     104.794 -54.393  53.651  1.00 76.27           C  
ANISOU11887  C   THR H 334     6479   6191  16308   1424    320    109       C  
ATOM  11888  O   THR H 334     104.919 -54.035  54.824  1.00 78.16           O  
ANISOU11888  O   THR H 334     6736   6421  16540   1486    301     49       O  
ATOM  11889  CB  THR H 334     106.572 -54.088  51.973  1.00 74.48           C  
ANISOU11889  CB  THR H 334     6206   5904  16188   1302    283     87       C  
ATOM  11890  OG1 THR H 334     107.620 -53.897  52.927  1.00 75.71           O  
ANISOU11890  OG1 THR H 334     6359   6037  16369   1331    232      0       O  
ATOM  11891  CG2 THR H 334     106.970 -53.468  50.641  1.00 74.11           C  
ANISOU11891  CG2 THR H 334     6139   5815  16204   1227    295     99       C  
ATOM  11892  N   PHE H 335     104.244 -55.557  53.287  1.00 82.36           N  
ANISOU11892  N   PHE H 335     7248   7016  17029   1410    339    183       N  
ATOM  11893  CA  PHE H 335     103.988 -56.636  54.249  1.00 79.82           C  
ANISOU11893  CA  PHE H 335     6940   6746  16642   1462    332    195       C  
ATOM  11894  C   PHE H 335     104.248 -58.009  53.617  1.00 71.89           C  
ANISOU11894  C   PHE H 335     5918   5785  15611   1417    325    253       C  
ATOM  11895  O   PHE H 335     104.234 -58.143  52.391  1.00 68.38           O  
ANISOU11895  O   PHE H 335     5456   5338  15186   1351    340    301       O  
ATOM  11896  CB  PHE H 335     102.557 -56.568  54.802  1.00 82.37           C  
ANISOU11896  CB  PHE H 335     7289   7097  16911   1518    380    230       C  
ATOM  11897  CG  PHE H 335     101.484 -56.883  53.794  1.00 79.16           C  
ANISOU11897  CG  PHE H 335     6878   6718  16482   1482    430    316       C  
ATOM  11898  CD1 PHE H 335     101.204 -58.186  53.435  1.00 73.09           C  
ANISOU11898  CD1 PHE H 335     6102   6001  15668   1461    440    381       C  
ATOM  11899  CD2 PHE H 335     100.721 -55.877  53.247  1.00 82.50           C  
ANISOU11899  CD2 PHE H 335     7305   7115  16925   1473    465    329       C  
ATOM  11900  CE1 PHE H 335     100.222 -58.470  52.522  1.00 70.45           C  
ANISOU11900  CE1 PHE H 335     5763   5691  15312   1428    482    455       C  
ATOM  11901  CE2 PHE H 335      99.725 -56.158  52.338  1.00 79.87           C  
ANISOU11901  CE2 PHE H 335     6969   6808  16571   1442    507    404       C  
ATOM  11902  CZ  PHE H 335      99.478 -57.454  51.975  1.00 73.89           C  
ANISOU11902  CZ  PHE H 335     6203   6100  15770   1420    515    466       C  
ATOM  11903  N   CYS H 336     104.458 -59.033  54.438  1.00 72.90           N  
ANISOU11903  N   CYS H 336     6053   5952  15693   1454    304    251       N  
ATOM  11904  CA  CYS H 336     104.773 -60.330  53.878  1.00 69.83           C  
ANISOU11904  CA  CYS H 336     5648   5603  15280   1411    295    301       C  
ATOM  11905  C   CYS H 336     103.696 -61.375  54.142  1.00 69.19           C  
ANISOU11905  C   CYS H 336     5583   5583  15124   1440    332    369       C  
ATOM  11906  O   CYS H 336     103.177 -61.482  55.251  1.00 69.88           O  
ANISOU11906  O   CYS H 336     5693   5689  15169   1510    341    355       O  
ATOM  11907  CB  CYS H 336     106.104 -60.830  54.432  1.00 69.73           C  
ANISOU11907  CB  CYS H 336     5627   5586  15280   1416    234    245       C  
ATOM  11908  SG  CYS H 336     107.550 -59.880  53.968  1.00 70.18           S  
ANISOU11908  SG  CYS H 336     5660   5577  15430   1368    187    169       S  
ATOM  11909  N   ALA H 337     103.382 -62.168  53.122  1.00 67.76           N  
ANISOU11909  N   ALA H 337     5388   5432  14926   1384    352    441       N  
ATOM  11910  CA  ALA H 337     102.460 -63.275  53.293  1.00 67.45           C  
ANISOU11910  CA  ALA H 337     5359   5451  14818   1403    385    506       C  
ATOM  11911  C   ALA H 337     103.199 -64.608  53.284  1.00 67.04           C  
ANISOU11911  C   ALA H 337     5298   5436  14740   1383    354    523       C  
ATOM  11912  O   ALA H 337     104.028 -64.875  52.407  1.00 66.62           O  
ANISOU11912  O   ALA H 337     5223   5372  14718   1319    330    530       O  
ATOM  11913  CB  ALA H 337     101.405 -63.250  52.223  1.00 67.00           C  
ANISOU11913  CB  ALA H 337     5297   5407  14752   1362    433    577       C  
ATOM  11914  N   GLY H 338     102.840 -65.467  54.236  1.00 72.70           N  
ANISOU11914  N   GLY H 338     6031   6194  15397   1438    361    534       N  
ATOM  11915  CA  GLY H 338     103.505 -66.742  54.436  1.00 67.96           C  
ANISOU11915  CA  GLY H 338     5426   5630  14765   1432    331    546       C  
ATOM  11916  C   GLY H 338     103.285 -67.723  53.298  1.00 64.09           C  
ANISOU11916  C   GLY H 338     4921   5175  14257   1364    349    622       C  
ATOM  11917  O   GLY H 338     102.802 -67.349  52.220  1.00 63.72           O  
ANISOU11917  O   GLY H 338     4864   5117  14231   1313    377    660       O  
ATOM  11918  N   MET H 339     103.702 -68.972  53.501  1.00 73.84           N  
ANISOU11918  N   MET H 339     6154   6448  15453   1362    331    641       N  
ATOM  11919  CA  MET H 339     103.418 -69.983  52.498  1.00 68.87           C  
ANISOU11919  CA  MET H 339     5514   5855  14799   1303    351    715       C  
ATOM  11920  C   MET H 339     102.045 -70.646  52.783  1.00 68.38           C  
ANISOU11920  C   MET H 339     5469   5840  14674   1335    406    775       C  
ATOM  11921  O   MET H 339     101.461 -70.480  53.858  1.00 71.41           O  
ANISOU11921  O   MET H 339     5872   6231  15028   1407    424    758       O  
ATOM  11922  CB  MET H 339     104.549 -71.029  52.452  1.00 64.22           C  
ANISOU11922  CB  MET H 339     4915   5285  14202   1276    305    710       C  
ATOM  11923  CG  MET H 339     105.783 -70.631  51.636  1.00 63.20           C  
ANISOU11923  CG  MET H 339     4761   5116  14137   1213    262    677       C  
ATOM  11924  SD  MET H 339     106.953 -72.021  51.159  1.00 60.95           S  
ANISOU11924  SD  MET H 339     4460   4858  13840   1158    218    694       S  
ATOM  11925  CE  MET H 339     107.582 -72.624  52.736  1.00 61.47           C  
ANISOU11925  CE  MET H 339     4540   4945  13869   1238    176    641       C  
ATOM  11926  N   SER H 340     101.596 -71.475  51.849  1.00 69.50           N  
ANISOU11926  N   SER H 340     5602   6013  14791   1283    430    843       N  
ATOM  11927  CA  SER H 340     100.287 -72.086  51.935  1.00 68.77           C  
ANISOU11927  CA  SER H 340     5521   5962  14646   1302    483    902       C  
ATOM  11928  C   SER H 340     100.246 -73.139  53.035  1.00 67.33           C  
ANISOU11928  C   SER H 340     5355   5822  14407   1358    484    906       C  
ATOM  11929  O   SER H 340     101.245 -73.380  53.700  1.00 67.01           O  
ANISOU11929  O   SER H 340     5316   5778  14367   1381    441    863       O  
ATOM  11930  CB  SER H 340      99.906 -72.696  50.584  1.00 64.61           C  
ANISOU11930  CB  SER H 340     4981   5455  14112   1227    503    969       C  
ATOM  11931  OG  SER H 340      99.100 -73.848  50.738  1.00 62.40           O  
ANISOU11931  OG  SER H 340     4710   5227  13773   1238    537   1024       O  
ATOM  11932  N   LYS H 341      99.079 -73.744  53.241  1.00 71.40           N  
ANISOU11932  N   LYS H 341     5880   6374  14873   1381    535    956       N  
ATOM  11933  CA  LYS H 341      98.942 -74.829  54.206  1.00 70.17           C  
ANISOU11933  CA  LYS H 341     5741   6260  14662   1431    544    968       C  
ATOM  11934  C   LYS H 341      99.662 -76.028  53.651  1.00 63.91           C  
ANISOU11934  C   LYS H 341     4936   5496  13850   1380    519    999       C  
ATOM  11935  O   LYS H 341     100.303 -76.770  54.388  1.00 62.15           O  
ANISOU11935  O   LYS H 341     4722   5292  13602   1411    493    983       O  
ATOM  11936  CB  LYS H 341      97.470 -75.150  54.448  1.00 72.46           C  
ANISOU11936  CB  LYS H 341     6042   6580  14910   1460    610   1016       C  
ATOM  11937  CG  LYS H 341      97.144 -76.166  55.540  1.00 69.90           C  
ANISOU11937  CG  LYS H 341     5738   6293  14528   1522    632   1030       C  
ATOM  11938  CD  LYS H 341      95.646 -76.518  55.462  1.00 72.27           C  
ANISOU11938  CD  LYS H 341     6043   6622  14795   1530    701   1086       C  
ATOM  11939  CE  LYS H 341      95.132 -77.227  56.707  1.00 76.20           C  
ANISOU11939  CE  LYS H 341     6565   7147  15241   1605    736   1093       C  
ATOM  11940  NZ  LYS H 341      94.804 -76.281  57.811  1.00 80.20           N  
ANISOU11940  NZ  LYS H 341     7093   7626  15753   1683    750   1046       N  
ATOM  11941  N   TYR H 342      99.513 -76.196  52.337  1.00 70.45           N  
ANISOU11941  N   TYR H 342     5749   6327  14693   1304    527   1042       N  
ATOM  11942  CA  TYR H 342     100.098 -77.280  51.533  1.00 64.49           C  
ANISOU11942  CA  TYR H 342     4982   5596  13924   1242    507   1079       C  
ATOM  11943  C   TYR H 342     101.394 -76.922  50.781  1.00 62.26           C  
ANISOU11943  C   TYR H 342     4683   5281  13693   1184    454   1048       C  
ATOM  11944  O   TYR H 342     101.711 -77.551  49.775  1.00 58.63           O  
ANISOU11944  O   TYR H 342     4212   4831  13233   1118    445   1084       O  
ATOM  11945  CB  TYR H 342      99.062 -77.827  50.563  1.00 62.42           C  
ANISOU11945  CB  TYR H 342     4717   5361  13640   1195    552   1150       C  
ATOM  11946  CG  TYR H 342      97.840 -78.366  51.294  1.00 64.14           C  
ANISOU11946  CG  TYR H 342     4949   5615  13807   1247    605   1182       C  
ATOM  11947  CD1 TYR H 342      97.799 -79.676  51.782  1.00 61.38           C  
ANISOU11947  CD1 TYR H 342     4607   5309  13404   1264    614   1211       C  
ATOM  11948  CD2 TYR H 342      96.727 -77.542  51.521  1.00 68.86           C  
ANISOU11948  CD2 TYR H 342     5553   6200  14410   1281    647   1182       C  
ATOM  11949  CE1 TYR H 342      96.693 -80.143  52.464  1.00 63.34           C  
ANISOU11949  CE1 TYR H 342     4869   5587  13610   1313    666   1239       C  
ATOM  11950  CE2 TYR H 342      95.622 -78.000  52.191  1.00 70.82           C  
ANISOU11950  CE2 TYR H 342     5813   6478  14616   1327    698   1209       C  
ATOM  11951  CZ  TYR H 342      95.604 -79.292  52.665  1.00 68.11           C  
ANISOU11951  CZ  TYR H 342     5478   6177  14224   1344    708   1237       C  
ATOM  11952  OH  TYR H 342      94.469 -79.708  53.338  1.00 70.50           O  
ANISOU11952  OH  TYR H 342     5793   6505  14488   1391    764   1264       O  
ATOM  11953  N   GLN H 343     102.055 -75.845  51.186  1.00 67.54           N  
ANISOU11953  N   GLN H 343     5348   5906  14408   1207    422    984       N  
ATOM  11954  CA  GLN H 343     103.303 -75.375  50.562  1.00 66.28           C  
ANISOU11954  CA  GLN H 343     5172   5708  14305   1157    373    946       C  
ATOM  11955  C   GLN H 343     103.097 -74.852  49.147  1.00 65.52           C  
ANISOU11955  C   GLN H 343     5062   5587  14247   1084    388    976       C  
ATOM  11956  O   GLN H 343     104.005 -74.886  48.335  1.00 62.84           O  
ANISOU11956  O   GLN H 343     4709   5227  13942   1025    358    971       O  
ATOM  11957  CB  GLN H 343     104.391 -76.468  50.497  1.00 61.33           C  
ANISOU11957  CB  GLN H 343     4537   5102  13663   1130    331    946       C  
ATOM  11958  CG  GLN H 343     104.512 -77.424  51.675  1.00 60.73           C  
ANISOU11958  CG  GLN H 343     4476   5066  13534   1190    321    939       C  
ATOM  11959  CD  GLN H 343     104.774 -76.740  53.013  1.00 65.41           C  
ANISOU11959  CD  GLN H 343     5081   5637  14133   1271    300    871       C  
ATOM  11960  OE1 GLN H 343     103.858 -76.155  53.610  1.00 69.77           O  
ANISOU11960  OE1 GLN H 343     5648   6185  14676   1323    335    867       O  
ATOM  11961  NE2 GLN H 343     106.009 -76.843  53.509  1.00 64.72           N  
ANISOU11961  NE2 GLN H 343     4990   5538  14063   1284    242    816       N  
ATOM  11962  N   GLU H 344     101.904 -74.373  48.843  1.00 61.12           N  
ANISOU11962  N   GLU H 344     4511   5029  13684   1089    435   1007       N  
ATOM  11963  CA  GLU H 344     101.693 -73.694  47.584  1.00 61.35           C  
ANISOU11963  CA  GLU H 344     4531   5028  13753   1030    447   1027       C  
ATOM  11964  C   GLU H 344     102.329 -72.337  47.750  1.00 65.64           C  
ANISOU11964  C   GLU H 344     5068   5515  14359   1040    423    962       C  
ATOM  11965  O   GLU H 344     102.423 -71.819  48.859  1.00 69.20           O  
ANISOU11965  O   GLU H 344     5525   5954  14812   1102    413    912       O  
ATOM  11966  CB  GLU H 344     100.212 -73.596  47.268  1.00 62.72           C  
ANISOU11966  CB  GLU H 344     4713   5218  13900   1037    502   1076       C  
ATOM  11967  CG  GLU H 344      99.461 -74.900  47.558  1.00 60.32           C  
ANISOU11967  CG  GLU H 344     4418   4972  13529   1051    530   1128       C  
ATOM  11968  CD  GLU H 344      97.956 -74.737  47.540  1.00 62.73           C  
ANISOU11968  CD  GLU H 344     4732   5292  13809   1074    584   1164       C  
ATOM  11969  OE1 GLU H 344      97.345 -74.847  46.458  1.00 61.58           O  
ANISOU11969  OE1 GLU H 344     4584   5151  13664   1026    606   1210       O  
ATOM  11970  OE2 GLU H 344      97.387 -74.488  48.617  1.00 66.29           O  
ANISOU11970  OE2 GLU H 344     5194   5752  14243   1141    605   1145       O  
ATOM  11971  N   ASP H 345     102.812 -71.769  46.665  1.00 60.55           N  
ANISOU11971  N   ASP H 345     4410   4833  13765    980    412    961       N  
ATOM  11972  CA  ASP H 345     103.310 -70.423  46.748  1.00 61.02           C  
ANISOU11972  CA  ASP H 345     4462   4836  13885    987    395    902       C  
ATOM  11973  C   ASP H 345     103.219 -69.787  45.388  1.00 60.69           C  
ANISOU11973  C   ASP H 345     4413   4761  13887    924    409    926       C  
ATOM  11974  O   ASP H 345     102.735 -70.386  44.419  1.00 60.13           O  
ANISOU11974  O   ASP H 345     4342   4710  13795    879    431    986       O  
ATOM  11975  CB  ASP H 345     104.743 -70.382  47.285  1.00 61.26           C  
ANISOU11975  CB  ASP H 345     4483   4845  13949    991    341    839       C  
ATOM  11976  CG  ASP H 345     105.234 -68.956  47.580  1.00 61.85           C  
ANISOU11976  CG  ASP H 345     4552   4861  14087   1009    323    769       C  
ATOM  11977  OD1 ASP H 345     104.396 -68.104  47.999  1.00 62.27           O  
ANISOU11977  OD1 ASP H 345     4617   4902  14140   1052    351    758       O  
ATOM  11978  OD2 ASP H 345     106.439 -68.675  47.353  1.00 61.89           O  
ANISOU11978  OD2 ASP H 345     4541   4830  14143    978    283    725       O  
ATOM  11979  N   THR H 346     103.712 -68.559  45.350  1.00 60.53           N  
ANISOU11979  N   THR H 346     4385   4687  13926    924    396    874       N  
ATOM  11980  CA  THR H 346     103.408 -67.606  44.323  1.00 60.75           C  
ANISOU11980  CA  THR H 346     4409   4677  13997    887    417    886       C  
ATOM  11981  C   THR H 346     104.730 -67.313  43.633  1.00 60.48           C  
ANISOU11981  C   THR H 346     4356   4598  14024    831    383    856       C  
ATOM  11982  O   THR H 346     105.679 -66.980  44.284  1.00 61.03           O  
ANISOU11982  O   THR H 346     4418   4643  14126    848    348    795       O  
ATOM  11983  CB  THR H 346     102.711 -66.380  44.953  1.00 62.17           C  
ANISOU11983  CB  THR H 346     4599   4832  14191    941    437    852       C  
ATOM  11984  OG1 THR H 346     102.471 -65.383  43.967  1.00 64.04           O  
ANISOU11984  OG1 THR H 346     4832   5028  14471    906    455    859       O  
ATOM  11985  CG2 THR H 346     103.495 -65.831  46.144  1.00 64.91           C  
ANISOU11985  CG2 THR H 346     4945   5154  14562    990    403    775       C  
ATOM  11986  N   CYS H 347     104.776 -67.490  42.317  1.00 60.97           N  
ANISOU11986  N   CYS H 347     4412   4651  14102    765    393    899       N  
ATOM  11987  CA  CYS H 347     106.004 -67.496  41.542  1.00 60.44           C  
ANISOU11987  CA  CYS H 347     4328   4551  14086    705    365    884       C  
ATOM  11988  C   CYS H 347     105.935 -66.432  40.438  1.00 60.77           C  
ANISOU11988  C   CYS H 347     4363   4543  14182    664    385    889       C  
ATOM  11989  O   CYS H 347     105.066 -65.552  40.484  1.00 61.59           O  
ANISOU11989  O   CYS H 347     4477   4636  14290    692    413    889       O  
ATOM  11990  CB  CYS H 347     106.271 -68.879  40.957  1.00 58.98           C  
ANISOU11990  CB  CYS H 347     4141   4402  13865    660    358    934       C  
ATOM  11991  SG  CYS H 347     108.043 -69.350  40.989  1.00 58.47           S  
ANISOU11991  SG  CYS H 347     4057   4317  13842    623    303    889       S  
ATOM  11992  N   TYR H 348     106.876 -66.488  39.493  1.00 60.48           N  
ANISOU11992  N   TYR H 348     4312   4478  14191    601    370    889       N  
ATOM  11993  CA  TYR H 348     107.037 -65.496  38.439  1.00 60.80           C  
ANISOU11993  CA  TYR H 348     4343   4468  14289    560    386    888       C  
ATOM  11994  C   TYR H 348     105.725 -65.169  37.668  1.00 60.82           C  
ANISOU11994  C   TYR H 348     4360   4480  14267    557    430    943       C  
ATOM  11995  O   TYR H 348     105.111 -66.031  37.059  1.00 59.86           O  
ANISOU11995  O   TYR H 348     4247   4395  14101    535    446   1004       O  
ATOM  11996  CB  TYR H 348     108.069 -66.001  37.435  1.00 60.00           C  
ANISOU11996  CB  TYR H 348     4226   4349  14221    489    369    901       C  
ATOM  11997  CG  TYR H 348     109.393 -66.555  38.006  1.00 60.05           C  
ANISOU11997  CG  TYR H 348     4217   4350  14248    480    324    855       C  
ATOM  11998  CD1 TYR H 348     109.786 -66.352  39.340  1.00 60.59           C  
ANISOU11998  CD1 TYR H 348     4283   4419  14319    535    295    792       C  
ATOM  11999  CD2 TYR H 348     110.275 -67.254  37.190  1.00 59.57           C  
ANISOU11999  CD2 TYR H 348     4144   4283  14205    419    308    872       C  
ATOM  12000  CE1 TYR H 348     110.981 -66.843  39.825  1.00 60.64           C  
ANISOU12000  CE1 TYR H 348     4276   4421  14345    528    251    749       C  
ATOM  12001  CE2 TYR H 348     111.459 -67.728  37.671  1.00 59.62           C  
ANISOU12001  CE2 TYR H 348     4137   4283  14233    411    266    830       C  
ATOM  12002  CZ  TYR H 348     111.804 -67.524  38.982  1.00 60.16           C  
ANISOU12002  CZ  TYR H 348     4203   4353  14302    465    237    768       C  
ATOM  12003  OH  TYR H 348     113.005 -68.029  39.438  1.00 60.22           O  
ANISOU12003  OH  TYR H 348     4195   4356  14329    457    192    724       O  
ATOM  12004  N   GLY H 349     105.326 -63.905  37.631  1.00 61.68           N  
ANISOU12004  N   GLY H 349     4472   4555  14410    577    449    920       N  
ATOM  12005  CA  GLY H 349     104.130 -63.521  36.912  1.00 62.22           C  
ANISOU12005  CA  GLY H 349     4553   4630  14458    577    488    966       C  
ATOM  12006  C   GLY H 349     103.053 -63.106  37.877  1.00 64.26           C  
ANISOU12006  C   GLY H 349     4828   4906  14682    645    505    957       C  
ATOM  12007  O   GLY H 349     102.057 -62.463  37.500  1.00 65.63           O  
ANISOU12007  O   GLY H 349     5012   5075  14848    657    536    978       O  
ATOM  12008  N   ASP H 350     103.268 -63.442  39.144  1.00 61.66           N  
ANISOU12008  N   ASP H 350     4500   4595  14332    690    486    923       N  
ATOM  12009  CA  ASP H 350     102.228 -63.236  40.150  1.00 64.23           C  
ANISOU12009  CA  ASP H 350     4842   4945  14618    758    504    917       C  
ATOM  12010  C   ASP H 350     102.272 -61.871  40.792  1.00 70.46           C  
ANISOU12010  C   ASP H 350     5634   5690  15447    798    504    858       C  
ATOM  12011  O   ASP H 350     101.492 -61.601  41.674  1.00 73.38           O  
ANISOU12011  O   ASP H 350     6017   6074  15789    856    518    846       O  
ATOM  12012  CB  ASP H 350     102.332 -64.290  41.258  1.00 62.08           C  
ANISOU12012  CB  ASP H 350     4573   4718  14297    794    486    912       C  
ATOM  12013  CG  ASP H 350     101.816 -65.654  40.847  1.00 60.81           C  
ANISOU12013  CG  ASP H 350     4416   4611  14078    772    498    978       C  
ATOM  12014  OD1 ASP H 350     101.824 -66.546  41.717  1.00 60.52           O  
ANISOU12014  OD1 ASP H 350     4383   4614  13997    803    487    978       O  
ATOM  12015  OD2 ASP H 350     101.392 -65.834  39.689  1.00 60.14           O  
ANISOU12015  OD2 ASP H 350     4333   4530  13989    727    517   1028       O  
ATOM  12016  N   ALA H 351     103.213 -61.032  40.401  1.00 62.63           N  
ANISOU12016  N   ALA H 351     4631   4646  14521    770    489    817       N  
ATOM  12017  CA  ALA H 351     103.220 -59.660  40.892  1.00 65.97           C  
ANISOU12017  CA  ALA H 351     5058   5022  14984    804    493    761       C  
ATOM  12018  C   ALA H 351     102.092 -58.885  40.243  1.00 69.37           C  
ANISOU12018  C   ALA H 351     5502   5445  15410    808    532    793       C  
ATOM  12019  O   ALA H 351     101.756 -59.138  39.090  1.00 67.58           O  
ANISOU12019  O   ALA H 351     5273   5225  15178    765    550    845       O  
ATOM  12020  CB  ALA H 351     104.533 -58.984  40.614  1.00 67.78           C  
ANISOU12020  CB  ALA H 351     5271   5197  15287    770    468    708       C  
ATOM  12021  N   GLY H 352     101.506 -57.941  40.975  1.00 66.01           N  
ANISOU12021  N   GLY H 352     5090   5003  14987    861    545    761       N  
ATOM  12022  CA  GLY H 352     100.401 -57.159  40.447  1.00 69.76           C  
ANISOU12022  CA  GLY H 352     5578   5469  15457    871    582    787       C  
ATOM  12023  C   GLY H 352      99.054 -57.805  40.716  1.00 68.28           C  
ANISOU12023  C   GLY H 352     5405   5336  15204    904    607    836       C  
ATOM  12024  O   GLY H 352      98.012 -57.147  40.663  1.00 71.77           O  
ANISOU12024  O   GLY H 352     5860   5775  15633    931    636    847       O  
ATOM  12025  N   SER H 353      99.077 -59.099  40.995  1.00 65.11           N  
ANISOU12025  N   SER H 353     5000   4982  14758    902    598    864       N  
ATOM  12026  CA  SER H 353      97.902 -59.789  41.498  1.00 64.62           C  
ANISOU12026  CA  SER H 353     4948   4972  14632    939    620    901       C  
ATOM  12027  C   SER H 353      97.649 -59.327  42.939  1.00 68.40           C  
ANISOU12027  C   SER H 353     5438   5450  15101   1011    620    853       C  
ATOM  12028  O   SER H 353      98.592 -59.091  43.689  1.00 69.80           O  
ANISOU12028  O   SER H 353     5612   5606  15303   1028    592    798       O  
ATOM  12029  CB  SER H 353      98.086 -61.309  41.424  1.00 63.28           C  
ANISOU12029  CB  SER H 353     4772   4851  14420    916    609    941       C  
ATOM  12030  OG  SER H 353      98.229 -61.775  40.083  1.00 62.22           O  
ANISOU12030  OG  SER H 353     4630   4720  14291    852    611    988       O  
ATOM  12031  N   ALA H 354      96.380 -59.194  43.319  1.00 63.48           N  
ANISOU12031  N   ALA H 354     4829   4850  14442   1054    652    873       N  
ATOM  12032  CA  ALA H 354      96.019 -58.565  44.586  1.00 66.13           C  
ANISOU12032  CA  ALA H 354     5178   5179  14771   1123    659    828       C  
ATOM  12033  C   ALA H 354      95.939 -59.561  45.710  1.00 64.49           C  
ANISOU12033  C   ALA H 354     4973   5015  14514   1164    654    827       C  
ATOM  12034  O   ALA H 354      95.390 -60.639  45.541  1.00 63.60           O  
ANISOU12034  O   ALA H 354     4859   4950  14356   1156    668    878       O  
ATOM  12035  CB  ALA H 354      94.698 -57.851  44.461  1.00 69.88           C  
ANISOU12035  CB  ALA H 354     5665   5652  15234   1150    697    846       C  
ATOM  12036  N   PHE H 355      96.420 -59.172  46.879  1.00 63.27           N  
ANISOU12036  N   PHE H 355     4825   4845  14368   1213    637    769       N  
ATOM  12037  CA  PHE H 355      96.255 -60.014  48.034  1.00 63.41           C  
ANISOU12037  CA  PHE H 355     4851   4904  14339   1262    636    765       C  
ATOM  12038  C   PHE H 355      94.923 -59.549  48.546  1.00 63.77           C  
ANISOU12038  C   PHE H 355     4913   4960  14358   1314    677    774       C  
ATOM  12039  O   PHE H 355      94.839 -58.529  49.199  1.00 64.34           O  
ANISOU12039  O   PHE H 355     4997   5001  14450   1356    679    728       O  
ATOM  12040  CB  PHE H 355      97.393 -59.783  49.028  1.00 63.84           C  
ANISOU12040  CB  PHE H 355     4907   4936  14415   1292    597    696       C  
ATOM  12041  CG  PHE H 355      97.248 -60.489  50.361  1.00 64.13           C  
ANISOU12041  CG  PHE H 355     4955   5007  14403   1355    595    682       C  
ATOM  12042  CD1 PHE H 355      97.798 -61.733  50.576  1.00 63.81           C  
ANISOU12042  CD1 PHE H 355     4909   5003  14333   1346    574    697       C  
ATOM  12043  CD2 PHE H 355      96.655 -59.868  51.424  1.00 64.74           C  
ANISOU12043  CD2 PHE H 355     5052   5078  14468   1423    612    650       C  
ATOM  12044  CE1 PHE H 355      97.689 -62.345  51.812  1.00 64.11           C  
ANISOU12044  CE1 PHE H 355     4960   5070  14327   1407    573    683       C  
ATOM  12045  CE2 PHE H 355      96.567 -60.486  52.656  1.00 65.03           C  
ANISOU12045  CE2 PHE H 355     5103   5144  14462   1483    611    635       C  
ATOM  12046  CZ  PHE H 355      97.072 -61.709  52.845  1.00 64.72           C  
ANISOU12046  CZ  PHE H 355     5058   5141  14392   1476    592    652       C  
ATOM  12047  N   ALA H 356      93.884 -60.344  48.286  1.00 63.45           N  
ANISOU12047  N   ALA H 356     4873   4964  14272   1312    709    833       N  
ATOM  12048  CA  ALA H 356      92.490 -59.924  48.439  1.00 63.69           C  
ANISOU12048  CA  ALA H 356     4914   5003  14281   1347    752    852       C  
ATOM  12049  C   ALA H 356      91.869 -60.516  49.677  1.00 63.98           C  
ANISOU12049  C   ALA H 356     4963   5078  14270   1410    773    852       C  
ATOM  12050  O   ALA H 356      91.672 -61.713  49.749  1.00 63.66           O  
ANISOU12050  O   ALA H 356     4918   5080  14188   1405    781    890       O  
ATOM  12051  CB  ALA H 356      91.700 -60.323  47.224  1.00 63.15           C  
ANISOU12051  CB  ALA H 356     4838   4956  14201   1301    775    916       C  
ATOM  12052  N   VAL H 357      91.569 -59.685  50.662  1.00 67.24           N  
ANISOU12052  N   VAL H 357     5391   5470  14686   1470    784    809       N  
ATOM  12053  CA  VAL H 357      90.989 -60.187  51.902  1.00 67.58           C  
ANISOU12053  CA  VAL H 357     5449   5545  14685   1535    806    805       C  
ATOM  12054  C   VAL H 357      89.471 -59.977  51.948  1.00 67.74           C  
ANISOU12054  C   VAL H 357     5476   5580  14681   1563    858    835       C  
ATOM  12055  O   VAL H 357      88.971 -58.892  51.777  1.00 68.52           O  
ANISOU12055  O   VAL H 357     5580   5650  14805   1572    872    820       O  
ATOM  12056  CB  VAL H 357      91.629 -59.540  53.117  1.00 68.26           C  
ANISOU12056  CB  VAL H 357     5551   5602  14783   1592    786    736       C  
ATOM  12057  CG1 VAL H 357      91.893 -58.107  52.814  1.00 69.16           C  
ANISOU12057  CG1 VAL H 357     5667   5662  14950   1585    774    694       C  
ATOM  12058  CG2 VAL H 357      90.711 -59.656  54.329  1.00 69.11           C  
ANISOU12058  CG2 VAL H 357     5678   5730  14849   1666    822    730       C  
ATOM  12059  N   HIS H 358      88.764 -61.071  52.165  1.00 70.60           N  
ANISOU12059  N   HIS H 358     5837   5990  14997   1573    886    879       N  
ATOM  12060  CA  HIS H 358      87.326 -61.112  52.193  1.00 73.29           C  
ANISOU12060  CA  HIS H 358     6181   6353  15314   1595    935    912       C  
ATOM  12061  C   HIS H 358      86.885 -60.773  53.614  1.00 78.77           C  
ANISOU12061  C   HIS H 358     6896   7045  15988   1674    959    877       C  
ATOM  12062  O   HIS H 358      87.342 -61.381  54.584  1.00 77.84           O  
ANISOU12062  O   HIS H 358     6789   6942  15846   1710    952    860       O  
ATOM  12063  CB  HIS H 358      86.858 -62.501  51.736  1.00 68.02           C  
ANISOU12063  CB  HIS H 358     5502   5735  14607   1565    952    973       C  
ATOM  12064  CG  HIS H 358      85.375 -62.684  51.698  1.00 70.54           C  
ANISOU12064  CG  HIS H 358     5821   6079  14901   1581   1003   1010       C  
ATOM  12065  ND1 HIS H 358      84.795 -63.791  51.126  1.00 67.34           N  
ANISOU12065  ND1 HIS H 358     5404   5714  14467   1549   1022   1065       N  
ATOM  12066  CD2 HIS H 358      84.353 -61.923  52.162  1.00 76.06           C  
ANISOU12066  CD2 HIS H 358     6529   6768  15601   1626   1038    998       C  
ATOM  12067  CE1 HIS H 358      83.478 -63.707  51.239  1.00 70.85           C  
ANISOU12067  CE1 HIS H 358     5849   6172  14898   1573   1066   1085       C  
ATOM  12068  NE2 HIS H 358      83.184 -62.579  51.860  1.00 76.11           N  
ANISOU12068  NE2 HIS H 358     6529   6809  15582   1619   1077   1045       N  
ATOM  12069  N   ASP H 359      86.022 -59.768  53.724  1.00 75.24           N  
ANISOU12069  N   ASP H 359     6457   6577  15554   1701    986    864       N  
ATOM  12070  CA  ASP H 359      85.530 -59.278  55.005  1.00 81.23           C  
ANISOU12070  CA  ASP H 359     7237   7327  16299   1776   1012    829       C  
ATOM  12071  C   ASP H 359      84.189 -59.908  55.231  1.00 81.87           C  
ANISOU12071  C   ASP H 359     7317   7446  16342   1798   1065    871       C  
ATOM  12072  O   ASP H 359      83.248 -59.587  54.514  1.00 82.94           O  
ANISOU12072  O   ASP H 359     7444   7583  16486   1778   1089    898       O  
ATOM  12073  CB  ASP H 359      85.411 -57.748  54.990  1.00 87.69           C  
ANISOU12073  CB  ASP H 359     8064   8097  17156   1791   1009    787       C  
ATOM  12074  CG  ASP H 359      85.157 -57.156  56.369  1.00 94.09           C  
ANISOU12074  CG  ASP H 359     8900   8893  17956   1869   1027    740       C  
ATOM  12075  OD1 ASP H 359      84.423 -57.773  57.176  1.00 94.12           O  
ANISOU12075  OD1 ASP H 359     8914   8927  17921   1913   1064    754       O  
ATOM  12076  OD2 ASP H 359      85.696 -56.061  56.643  1.00 99.30           O  
ANISOU12076  OD2 ASP H 359     9571   9510  18649   1885   1005    687       O  
ATOM  12077  N   LEU H 360      84.072 -60.789  56.217  1.00 86.74           N  
ANISOU12077  N   LEU H 360     7946   8093  16920   1840   1084    875       N  
ATOM  12078  CA  LEU H 360      82.853 -61.594  56.297  1.00 86.67           C  
ANISOU12078  CA  LEU H 360     7933   8123  16876   1851   1136    922       C  
ATOM  12079  C   LEU H 360      81.633 -60.811  56.809  1.00 93.78           C  
ANISOU12079  C   LEU H 360     8844   9013  17775   1898   1183    912       C  
ATOM  12080  O   LEU H 360      80.504 -61.104  56.414  1.00 94.47           O  
ANISOU12080  O   LEU H 360     8920   9121  17852   1888   1221    950       O  
ATOM  12081  CB  LEU H 360      83.087 -62.841  57.154  1.00 83.65           C  
ANISOU12081  CB  LEU H 360     7558   7775  16449   1879   1146    934       C  
ATOM  12082  CG  LEU H 360      83.993 -63.869  56.472  1.00 76.02           C  
ANISOU12082  CG  LEU H 360     6577   6832  15477   1824   1110    961       C  
ATOM  12083  CD1 LEU H 360      83.800 -65.294  57.031  1.00 71.46           C  
ANISOU12083  CD1 LEU H 360     6002   6298  14851   1841   1135    994       C  
ATOM  12084  CD2 LEU H 360      83.776 -63.835  54.962  1.00 73.83           C  
ANISOU12084  CD2 LEU H 360     6275   6555  15222   1749   1100    999       C  
ATOM  12085  N   GLU H 361      81.861 -59.805  57.653  1.00 86.63           N  
ANISOU12085  N   GLU H 361     7959   8073  16883   1949   1178    858       N  
ATOM  12086  CA  GLU H 361      80.768 -59.003  58.212  1.00 93.69           C  
ANISOU12086  CA  GLU H 361     8866   8954  17777   1997   1221    843       C  
ATOM  12087  C   GLU H 361      80.043 -58.205  57.136  1.00 95.46           C  
ANISOU12087  C   GLU H 361     9075   9164  18032   1960   1227    859       C  
ATOM  12088  O   GLU H 361      78.816 -58.253  57.050  1.00 98.21           O  
ANISOU12088  O   GLU H 361     9418   9528  18371   1969   1271    885       O  
ATOM  12089  CB  GLU H 361      81.297 -58.063  59.300  1.00 98.95           C  
ANISOU12089  CB  GLU H 361     9560   9584  18453   2056   1209    779       C  
ATOM  12090  CG  GLU H 361      81.882 -58.799  60.513  1.00 98.60           C  
ANISOU12090  CG  GLU H 361     9538   9552  18374   2106   1207    759       C  
ATOM  12091  CD  GLU H 361      80.811 -59.487  61.359  1.00102.17           C  
ANISOU12091  CD  GLU H 361    10002  10034  18784   2156   1269    782       C  
ATOM  12092  OE1 GLU H 361      80.049 -58.771  62.055  1.00108.95           O  
ANISOU12092  OE1 GLU H 361    10879  10877  19640   2207   1305    760       O  
ATOM  12093  OE2 GLU H 361      80.737 -60.741  61.332  1.00 98.36           O  
ANISOU12093  OE2 GLU H 361     9512   9590  18270   2144   1283    822       O  
ATOM  12094  N   GLU H 362      80.799 -57.476  56.315  1.00 87.98           N  
ANISOU12094  N   GLU H 362     8120   8185  17122   1919   1185    843       N  
ATOM  12095  CA  GLU H 362      80.206 -56.704  55.219  1.00 89.45           C  
ANISOU12095  CA  GLU H 362     8294   8355  17338   1882   1186    858       C  
ATOM  12096  C   GLU H 362      80.221 -57.422  53.869  1.00 83.33           C  
ANISOU12096  C   GLU H 362     7495   7601  16565   1811   1173    909       C  
ATOM  12097  O   GLU H 362      79.856 -56.829  52.846  1.00 84.08           O  
ANISOU12097  O   GLU H 362     7581   7681  16685   1776   1168    922       O  
ATOM  12098  CB  GLU H 362      80.903 -55.355  55.074  1.00 92.76           C  
ANISOU12098  CB  GLU H 362     8722   8723  17799   1881   1154    810       C  
ATOM  12099  CG  GLU H 362      82.303 -55.277  55.650  1.00 93.30           C  
ANISOU12099  CG  GLU H 362     8801   8770  17877   1890   1113    765       C  
ATOM  12100  CD  GLU H 362      82.862 -53.868  55.563  1.00 97.01           C  
ANISOU12100  CD  GLU H 362     9281   9188  18392   1892   1087    715       C  
ATOM  12101  OE1 GLU H 362      82.172 -52.983  55.000  1.00 98.33           O  
ANISOU12101  OE1 GLU H 362     9446   9335  18579   1884   1101    718       O  
ATOM  12102  OE2 GLU H 362      83.989 -53.645  56.052  1.00 98.81           O  
ANISOU12102  OE2 GLU H 362     9518   9393  18633   1902   1051    671       O  
ATOM  12103  N   ASP H 363      80.667 -58.682  53.874  1.00 88.97           N  
ANISOU12103  N   ASP H 363     8202   8350  17254   1791   1165    936       N  
ATOM  12104  CA  ASP H 363      80.691 -59.536  52.679  1.00 82.88           C  
ANISOU12104  CA  ASP H 363     7410   7603  16478   1726   1153    986       C  
ATOM  12105  C   ASP H 363      81.266 -58.811  51.448  1.00 81.58           C  
ANISOU12105  C   ASP H 363     7237   7407  16354   1671   1116    984       C  
ATOM  12106  O   ASP H 363      80.715 -58.862  50.349  1.00 80.24           O  
ANISOU12106  O   ASP H 363     7055   7243  16191   1629   1120   1019       O  
ATOM  12107  CB  ASP H 363      79.288 -60.057  52.378  1.00 83.58           C  
ANISOU12107  CB  ASP H 363     7488   7723  16546   1724   1197   1030       C  
ATOM  12108  CG  ASP H 363      79.296 -61.217  51.416  1.00 77.20           C  
ANISOU12108  CG  ASP H 363     6662   6948  15722   1666   1190   1082       C  
ATOM  12109  OD1 ASP H 363      79.575 -62.341  51.872  1.00 73.93           O  
ANISOU12109  OD1 ASP H 363     6247   6566  15278   1669   1195   1099       O  
ATOM  12110  OD2 ASP H 363      79.016 -61.016  50.214  1.00 75.65           O  
ANISOU12110  OD2 ASP H 363     6454   6747  15544   1620   1180   1106       O  
ATOM  12111  N   THR H 364      82.386 -58.130  51.636  1.00 78.87           N  
ANISOU12111  N   THR H 364     6901   7028  16038   1671   1080    941       N  
ATOM  12112  CA  THR H 364      83.010 -57.421  50.533  1.00 77.94           C  
ANISOU12112  CA  THR H 364     6777   6876  15960   1621   1048    936       C  
ATOM  12113  C   THR H 364      84.470 -57.807  50.393  1.00 73.15           C  
ANISOU12113  C   THR H 364     6166   6262  15366   1588   1004    922       C  
ATOM  12114  O   THR H 364      85.117 -58.158  51.382  1.00 72.67           O  
ANISOU12114  O   THR H 364     6113   6206  15292   1620    992    895       O  
ATOM  12115  CB  THR H 364      82.887 -55.931  50.732  1.00 84.64           C  
ANISOU12115  CB  THR H 364     7638   7679  16842   1649   1049    892       C  
ATOM  12116  OG1 THR H 364      81.493 -55.610  50.926  1.00 89.32           O  
ANISOU12116  OG1 THR H 364     8235   8281  17422   1683   1091    904       O  
ATOM  12117  CG2 THR H 364      83.462 -55.169  49.526  1.00 84.11           C  
ANISOU12117  CG2 THR H 364     7565   7575  16817   1597   1020    890       C  
ATOM  12118  N   TRP H 365      84.970 -57.767  49.159  1.00 73.66           N  
ANISOU12118  N   TRP H 365     6219   6314  15455   1526    979    941       N  
ATOM  12119  CA  TRP H 365      86.345 -58.138  48.853  1.00 72.07           C  
ANISOU12119  CA  TRP H 365     6011   6104  15270   1487    937    931       C  
ATOM  12120  C   TRP H 365      87.252 -56.923  48.713  1.00 73.20           C  
ANISOU12120  C   TRP H 365     6158   6191  15463   1479    909    882       C  
ATOM  12121  O   TRP H 365      87.141 -56.169  47.753  1.00 73.87           O  
ANISOU12121  O   TRP H 365     6240   6248  15578   1448    907    888       O  
ATOM  12122  CB  TRP H 365      86.381 -58.963  47.568  1.00 70.72           C  
ANISOU12122  CB  TRP H 365     5824   5953  15093   1420    930    985       C  
ATOM  12123  CG  TRP H 365      85.767 -60.334  47.710  1.00 69.89           C  
ANISOU12123  CG  TRP H 365     5713   5902  14940   1420    951   1031       C  
ATOM  12124  CD1 TRP H 365      84.425 -60.651  47.700  1.00 70.02           C  
ANISOU12124  CD1 TRP H 365     5728   5947  14928   1437    990   1064       C  
ATOM  12125  CD2 TRP H 365      86.463 -61.578  47.876  1.00 68.82           C  
ANISOU12125  CD2 TRP H 365     5571   5798  14780   1402    934   1048       C  
ATOM  12126  NE1 TRP H 365      84.258 -62.001  47.851  1.00 69.12           N  
ANISOU12126  NE1 TRP H 365     5608   5879  14774   1429   1000   1100       N  
ATOM  12127  CE2 TRP H 365      85.490 -62.595  47.958  1.00 68.36           C  
ANISOU12127  CE2 TRP H 365     5509   5786  14678   1408    966   1092       C  
ATOM  12128  CE3 TRP H 365      87.798 -61.924  47.970  1.00 68.25           C  
ANISOU12128  CE3 TRP H 365     5495   5719  14718   1381    896   1028       C  
ATOM  12129  CZ2 TRP H 365      85.819 -63.924  48.115  1.00 67.34           C  
ANISOU12129  CZ2 TRP H 365     5375   5695  14516   1394    962   1118       C  
ATOM  12130  CZ3 TRP H 365      88.119 -63.249  48.135  1.00 67.24           C  
ANISOU12130  CZ3 TRP H 365     5362   5630  14556   1368    890   1054       C  
ATOM  12131  CH2 TRP H 365      87.134 -64.232  48.204  1.00 66.79           C  
ANISOU12131  CH2 TRP H 365     5303   5619  14455   1375    923   1100       C  
ATOM  12132  N   TYR H 366      88.173 -56.750  49.648  1.00 68.70           N  
ANISOU12132  N   TYR H 366     5595   5604  14902   1507    885    833       N  
ATOM  12133  CA  TYR H 366      89.091 -55.616  49.601  1.00 69.38           C  
ANISOU12133  CA  TYR H 366     5685   5637  15038   1502    857    780       C  
ATOM  12134  C   TYR H 366      90.456 -55.998  49.046  1.00 68.47           C  
ANISOU12134  C   TYR H 366     5557   5510  14949   1449    816    773       C  
ATOM  12135  O   TYR H 366      90.899 -57.120  49.243  1.00 67.58           O  
ANISOU12135  O   TYR H 366     5437   5429  14810   1439    802    789       O  
ATOM  12136  CB  TYR H 366      89.255 -55.017  50.994  1.00 71.28           C  
ANISOU12136  CB  TYR H 366     5944   5861  15280   1568    855    721       C  
ATOM  12137  CG  TYR H 366      87.968 -54.475  51.535  1.00 74.53           C  
ANISOU12137  CG  TYR H 366     6370   6276  15673   1620    897    722       C  
ATOM  12138  CD1 TYR H 366      87.452 -53.252  51.073  1.00 79.53           C  
ANISOU12138  CD1 TYR H 366     7008   6873  16335   1620    910    711       C  
ATOM  12139  CD2 TYR H 366      87.245 -55.182  52.495  1.00 75.05           C  
ANISOU12139  CD2 TYR H 366     6444   6380  15692   1669    924    734       C  
ATOM  12140  CE1 TYR H 366      86.261 -52.749  51.556  1.00 84.82           C  
ANISOU12140  CE1 TYR H 366     7690   7547  16989   1666    947    712       C  
ATOM  12141  CE2 TYR H 366      86.036 -54.673  52.987  1.00 80.48           C  
ANISOU12141  CE2 TYR H 366     7143   7070  16365   1716    965    734       C  
ATOM  12142  CZ  TYR H 366      85.565 -53.459  52.512  1.00 85.26           C  
ANISOU12142  CZ  TYR H 366     7753   7641  17001   1714    975    722       C  
ATOM  12143  OH  TYR H 366      84.392 -52.971  52.996  1.00 90.58           O  
ANISOU12143  OH  TYR H 366     8438   8317  17660   1759   1013    722       O  
ATOM  12144  N   ALA H 367      91.129 -55.085  48.354  1.00 65.25           N  
ANISOU12144  N   ALA H 367     5145   5055  14591   1415    796    749       N  
ATOM  12145  CA  ALA H 367      92.512 -55.353  48.020  1.00 65.00           C  
ANISOU12145  CA  ALA H 367     5101   5007  14588   1373    756    731       C  
ATOM  12146  C   ALA H 367      93.369 -54.789  49.126  1.00 65.56           C  
ANISOU12146  C   ALA H 367     5180   5047  14681   1412    730    660       C  
ATOM  12147  O   ALA H 367      93.628 -53.618  49.183  1.00 65.95           O  
ANISOU12147  O   ALA H 367     5237   5051  14771   1421    725    616       O  
ATOM  12148  CB  ALA H 367      92.889 -54.738  46.685  1.00 64.73           C  
ANISOU12148  CB  ALA H 367     5058   4936  14599   1313    749    741       C  
ATOM  12149  N   THR H 368      93.879 -55.655  49.974  1.00 68.75           N  
ANISOU12149  N   THR H 368     5584   5478  15060   1435    712    646       N  
ATOM  12150  CA  THR H 368      94.732 -55.213  51.053  1.00 70.21           C  
ANISOU12150  CA  THR H 368     5778   5637  15263   1475    683    576       C  
ATOM  12151  C   THR H 368      96.132 -54.923  50.523  1.00 69.46           C  
ANISOU12151  C   THR H 368     5668   5503  15222   1426    641    541       C  
ATOM  12152  O   THR H 368      96.762 -53.956  50.937  1.00 71.50           O  
ANISOU12152  O   THR H 368     5931   5715  15520   1442    621    479       O  
ATOM  12153  CB  THR H 368      94.798 -56.259  52.183  1.00 69.30           C  
ANISOU12153  CB  THR H 368     5669   5562  15098   1521    676    572       C  
ATOM  12154  OG1 THR H 368      93.862 -55.900  53.214  1.00 71.60           O  
ANISOU12154  OG1 THR H 368     5982   5861  15361   1590    706    558       O  
ATOM  12155  CG2 THR H 368      96.237 -56.360  52.753  1.00 68.96           C  
ANISOU12155  CG2 THR H 368     5622   5499  15079   1524    625    513       C  
ATOM  12156  N   GLY H 369      96.604 -55.733  49.583  1.00 69.25           N  
ANISOU12156  N   GLY H 369     5623   5492  15198   1366    628    580       N  
ATOM  12157  CA  GLY H 369      97.903 -55.488  49.002  1.00 68.24           C  
ANISOU12157  CA  GLY H 369     5479   5326  15123   1316    592    550       C  
ATOM  12158  C   GLY H 369      98.063 -55.858  47.540  1.00 67.09           C  
ANISOU12158  C   GLY H 369     5316   5182  14992   1242    595    602       C  
ATOM  12159  O   GLY H 369      97.231 -56.559  46.965  1.00 66.28           O  
ANISOU12159  O   GLY H 369     5213   5118  14853   1225    620    666       O  
ATOM  12160  N   ILE H 370      99.146 -55.364  46.939  1.00 69.50           N  
ANISOU12160  N   ILE H 370     5608   5443  15354   1197    570    572       N  
ATOM  12161  CA  ILE H 370      99.559 -55.802  45.612  1.00 68.36           C  
ANISOU12161  CA  ILE H 370     5447   5298  15229   1124    567    614       C  
ATOM  12162  C   ILE H 370     100.902 -56.551  45.680  1.00 67.62           C  
ANISOU12162  C   ILE H 370     5335   5204  15152   1094    525    591       C  
ATOM  12163  O   ILE H 370     101.821 -56.131  46.393  1.00 68.28           O  
ANISOU12163  O   ILE H 370     5416   5259  15269   1111    494    525       O  
ATOM  12164  CB  ILE H 370      99.668 -54.625  44.663  1.00 68.88           C  
ANISOU12164  CB  ILE H 370     5511   5311  15348   1090    578    605       C  
ATOM  12165  CG1 ILE H 370      98.316 -53.930  44.559  1.00 69.57           C  
ANISOU12165  CG1 ILE H 370     5617   5401  15417   1120    618    629       C  
ATOM  12166  CG2 ILE H 370     100.123 -55.073  43.288  1.00 67.74           C  
ANISOU12166  CG2 ILE H 370     5351   5164  15223   1017    576    647       C  
ATOM  12167  CD1 ILE H 370      97.408 -54.563  43.567  1.00 68.64           C  
ANISOU12167  CD1 ILE H 370     5498   5318  15264   1091    645    704       C  
ATOM  12168  N   LEU H 371     101.025 -57.659  44.951  1.00 68.40           N  
ANISOU12168  N   LEU H 371     5422   5336  15229   1049    522    644       N  
ATOM  12169  CA  LEU H 371     102.248 -58.456  45.010  1.00 67.63           C  
ANISOU12169  CA  LEU H 371     5309   5243  15144   1020    483    627       C  
ATOM  12170  C   LEU H 371     103.420 -57.769  44.334  1.00 67.77           C  
ANISOU12170  C   LEU H 371     5310   5205  15235    970    461    588       C  
ATOM  12171  O   LEU H 371     103.353 -57.455  43.153  1.00 67.44           O  
ANISOU12171  O   LEU H 371     5262   5144  15218    921    479    619       O  
ATOM  12172  CB  LEU H 371     102.018 -59.829  44.361  1.00 66.13           C  
ANISOU12172  CB  LEU H 371     5113   5104  14910    983    489    696       C  
ATOM  12173  CG  LEU H 371     102.818 -61.059  44.820  1.00 65.26           C  
ANISOU12173  CG  LEU H 371     4994   5026  14777    978    455    693       C  
ATOM  12174  CD1 LEU H 371     103.575 -61.677  43.718  1.00 64.08           C  
ANISOU12174  CD1 LEU H 371     4827   4874  14647    906    441    721       C  
ATOM  12175  CD2 LEU H 371     103.747 -60.772  45.984  1.00 66.07           C  
ANISOU12175  CD2 LEU H 371     5094   5108  14900   1017    417    616       C  
ATOM  12176  N   SER H 372     104.501 -57.559  45.078  1.00 68.87           N  
ANISOU12176  N   SER H 372     5441   5319  15408    984    423    520       N  
ATOM  12177  CA  SER H 372     105.734 -57.012  44.500  1.00 69.78           C  
ANISOU12177  CA  SER H 372     5537   5382  15595    935    400    479       C  
ATOM  12178  C   SER H 372     106.678 -58.122  44.121  1.00 64.74           C  
ANISOU12178  C   SER H 372     4878   4761  14959    889    370    492       C  
ATOM  12179  O   SER H 372     107.046 -58.259  42.956  1.00 63.99           O  
ANISOU12179  O   SER H 372     4770   4653  14892    826    376    522       O  
ATOM  12180  CB  SER H 372     106.445 -56.062  45.460  1.00 75.71           C  
ANISOU12180  CB  SER H 372     6287   6089  16390    971    373    390       C  
ATOM  12181  OG  SER H 372     107.441 -55.335  44.765  1.00 77.83           O  
ANISOU12181  OG  SER H 372     6538   6301  16733    921    361    353       O  
ATOM  12182  N   PHE H 373     107.085 -58.900  45.121  1.00 74.19           N  
ANISOU12182  N   PHE H 373     6075   5987  16127    922    338    467       N  
ATOM  12183  CA  PHE H 373     108.081 -59.943  44.925  1.00 68.82           C  
ANISOU12183  CA  PHE H 373     5376   5322  15449    884    304    469       C  
ATOM  12184  C   PHE H 373     107.431 -61.290  44.639  1.00 63.62           C  
ANISOU12184  C   PHE H 373     4724   4727  14722    874    319    546       C  
ATOM  12185  O   PHE H 373     106.932 -61.984  45.543  1.00 63.54           O  
ANISOU12185  O   PHE H 373     4727   4762  14653    924    317    556       O  
ATOM  12186  CB  PHE H 373     108.926 -60.002  46.192  1.00 70.13           C  
ANISOU12186  CB  PHE H 373     5540   5484  15623    928    258    394       C  
ATOM  12187  CG  PHE H 373     110.125 -60.885  46.129  1.00 65.99           C  
ANISOU12187  CG  PHE H 373     4995   4966  15113    895    215    377       C  
ATOM  12188  CD1 PHE H 373     111.285 -60.457  45.505  1.00 66.56           C  
ANISOU12188  CD1 PHE H 373     5043   4989  15259    842    193    339       C  
ATOM  12189  CD2 PHE H 373     110.125 -62.096  46.783  1.00 64.08           C  
ANISOU12189  CD2 PHE H 373     4758   4776  14812    921    196    394       C  
ATOM  12190  CE1 PHE H 373     112.399 -61.261  45.475  1.00 64.06           C  
ANISOU12190  CE1 PHE H 373     4707   4677  14957    812    152    320       C  
ATOM  12191  CE2 PHE H 373     111.238 -62.900  46.763  1.00 63.37           C  
ANISOU12191  CE2 PHE H 373     4651   4693  14734    893    154    375       C  
ATOM  12192  CZ  PHE H 373     112.379 -62.488  46.106  1.00 63.35           C  
ANISOU12192  CZ  PHE H 373     4624   4642  14806    838    131    338       C  
ATOM  12193  N   ASP H 374     107.456 -61.660  43.368  1.00 67.91           N  
ANISOU12193  N   ASP H 374     5258   5272  15274    810    334    599       N  
ATOM  12194  CA  ASP H 374     106.901 -62.922  42.907  1.00 63.44           C  
ANISOU12194  CA  ASP H 374     4696   4760  14648    790    348    673       C  
ATOM  12195  C   ASP H 374     107.984 -63.960  42.674  1.00 62.38           C  
ANISOU12195  C   ASP H 374     4546   4637  14518    748    313    674       C  
ATOM  12196  O   ASP H 374     107.740 -64.941  41.990  1.00 61.19           O  
ANISOU12196  O   ASP H 374     4397   4521  14333    713    324    735       O  
ATOM  12197  CB  ASP H 374     106.099 -62.714  41.644  1.00 63.00           C  
ANISOU12197  CB  ASP H 374     4645   4702  14592    749    388    735       C  
ATOM  12198  CG  ASP H 374     106.755 -61.744  40.729  1.00 64.35           C  
ANISOU12198  CG  ASP H 374     4802   4814  14835    702    389    713       C  
ATOM  12199  OD1 ASP H 374     107.774 -61.166  41.143  1.00 66.98           O  
ANISOU12199  OD1 ASP H 374     5122   5107  15221    704    361    647       O  
ATOM  12200  OD2 ASP H 374     106.245 -61.537  39.615  1.00 63.88           O  
ANISOU12200  OD2 ASP H 374     4744   4748  14779    666    419    760       O  
ATOM  12201  N   LYS H 375     109.205 -63.685  43.114  1.00 64.99           N  
ANISOU12201  N   LYS H 375     4861   4935  14897    746    273    607       N  
ATOM  12202  CA  LYS H 375     110.306 -64.590  42.849  1.00 62.82           C  
ANISOU12202  CA  LYS H 375     4569   4666  14634    704    238    603       C  
ATOM  12203  C   LYS H 375     110.418 -65.826  43.778  1.00 62.28           C  
ANISOU12203  C   LYS H 375     4507   4652  14504    739    211    606       C  
ATOM  12204  O   LYS H 375     111.155 -66.763  43.449  1.00 61.29           O  
ANISOU12204  O   LYS H 375     4371   4541  14374    701    188    618       O  
ATOM  12205  CB  LYS H 375     111.611 -63.811  42.915  1.00 63.51           C  
ANISOU12205  CB  LYS H 375     4635   4695  14802    685    203    526       C  
ATOM  12206  CG  LYS H 375     111.609 -62.549  42.112  1.00 66.02           C  
ANISOU12206  CG  LYS H 375     4945   4957  15183    655    228    514       C  
ATOM  12207  CD  LYS H 375     111.452 -62.818  40.629  1.00 63.18           C  
ANISOU12207  CD  LYS H 375     4579   4594  14831    587    256    580       C  
ATOM  12208  CE  LYS H 375     111.956 -61.605  39.837  1.00 65.87           C  
ANISOU12208  CE  LYS H 375     4904   4871  15252    548    268    551       C  
ATOM  12209  NZ  LYS H 375     111.780 -61.769  38.373  1.00 64.08           N  
ANISOU12209  NZ  LYS H 375     4672   4640  15034    485    299    613       N  
ATOM  12210  N   SER H 376     109.705 -65.835  44.912  1.00 63.99           N  
ANISOU12210  N   SER H 376     4742   4898  14674    810    216    595       N  
ATOM  12211  CA  SER H 376     110.039 -66.727  46.043  1.00 63.23           C  
ANISOU12211  CA  SER H 376     4651   4841  14534    856    183    572       C  
ATOM  12212  C   SER H 376     109.775 -68.213  45.830  1.00 61.78           C  
ANISOU12212  C   SER H 376     4472   4716  14285    840    188    637       C  
ATOM  12213  O   SER H 376     110.614 -69.054  46.198  1.00 61.28           O  
ANISOU12213  O   SER H 376     4403   4672  14210    838    150    619       O  
ATOM  12214  CB  SER H 376     109.297 -66.287  47.311  1.00 65.58           C  
ANISOU12214  CB  SER H 376     4968   5151  14799    940    192    544       C  
ATOM  12215  OG  SER H 376     107.900 -66.296  47.142  1.00 65.82           O  
ANISOU12215  OG  SER H 376     5017   5209  14784    957    243    603       O  
ATOM  12216  N   CYS H 377     108.607 -68.550  45.304  1.00 62.30           N  
ANISOU12216  N   CYS H 377     4551   4813  14307    832    234    708       N  
ATOM  12217  CA  CYS H 377     108.333 -69.936  44.883  1.00 60.05           C  
ANISOU12217  CA  CYS H 377     4272   4581  13965    806    243    775       C  
ATOM  12218  C   CYS H 377     108.555 -71.094  45.897  1.00 59.71           C  
ANISOU12218  C   CYS H 377     4235   4587  13864    846    219    771       C  
ATOM  12219  O   CYS H 377     108.158 -71.063  47.062  1.00 60.45           O  
ANISOU12219  O   CYS H 377     4342   4701  13927    916    219    748       O  
ATOM  12220  CB  CYS H 377     109.162 -70.221  43.637  1.00 59.07           C  
ANISOU12220  CB  CYS H 377     4131   4434  13878    725    230    794       C  
ATOM  12221  SG  CYS H 377     109.174 -68.760  42.570  1.00 59.68           S  
ANISOU12221  SG  CYS H 377     4198   4444  14032    682    251    782       S  
ATOM  12222  N   ALA H 378     109.143 -72.160  45.436  1.00 66.10           N  
ANISOU12222  N   ALA H 378     5039   5419  14658    804    201    797       N  
ATOM  12223  CA  ALA H 378     109.387 -73.203  46.399  1.00 63.71           C  
ANISOU12223  CA  ALA H 378     4742   5161  14302    844    177    791       C  
ATOM  12224  C   ALA H 378     110.282 -72.659  47.516  1.00 67.28           C  
ANISOU12224  C   ALA H 378     5189   5588  14786    893    131    705       C  
ATOM  12225  O   ALA H 378     109.988 -72.783  48.717  1.00 69.30           O  
ANISOU12225  O   ALA H 378     5459   5868  15005    965    126    681       O  
ATOM  12226  CB  ALA H 378     110.062 -74.462  45.718  1.00 58.78           C  
ANISOU12226  CB  ALA H 378     4113   4562  13660    787    158    827       C  
ATOM  12227  N   VAL H 379     111.354 -72.011  47.081  1.00 60.33           N  
ANISOU12227  N   VAL H 379     4289   4658  13977    854     99    656       N  
ATOM  12228  CA  VAL H 379     112.570 -71.972  47.865  1.00 60.83           C  
ANISOU12228  CA  VAL H 379     4341   4704  14068    876     41    580       C  
ATOM  12229  C   VAL H 379     112.612 -70.903  48.953  1.00 66.88           C  
ANISOU12229  C   VAL H 379     5112   5441  14859    943     26    506       C  
ATOM  12230  O   VAL H 379     113.395 -71.039  49.900  1.00 67.78           O  
ANISOU12230  O   VAL H 379     5224   5554  14975    982    -22    445       O  
ATOM  12231  CB  VAL H 379     113.789 -71.807  46.927  1.00 60.37           C  
ANISOU12231  CB  VAL H 379     4257   4603  14078    803     12    557       C  
ATOM  12232  CG1 VAL H 379     113.370 -72.101  45.503  1.00 59.27           C  
ANISOU12232  CG1 VAL H 379     4116   4464  13938    731     51    632       C  
ATOM  12233  CG2 VAL H 379     114.391 -70.416  47.027  1.00 65.15           C  
ANISOU12233  CG2 VAL H 379     4848   5143  14764    804     -5    482       C  
ATOM  12234  N   ALA H 380     111.769 -69.875  48.848  1.00 63.39           N  
ANISOU12234  N   ALA H 380     4677   4975  14432    957     64    511       N  
ATOM  12235  CA  ALA H 380     111.927 -68.692  49.678  1.00 64.13           C  
ANISOU12235  CA  ALA H 380     4774   5029  14564   1007     49    436       C  
ATOM  12236  C   ALA H 380     110.674 -68.393  50.472  1.00 64.48           C  
ANISOU12236  C   ALA H 380     4844   5094  14560   1076     86    451       C  
ATOM  12237  O   ALA H 380     109.626 -68.039  49.906  1.00 64.29           O  
ANISOU12237  O   ALA H 380     4829   5072  14527   1065    136    501       O  
ATOM  12238  CB  ALA H 380     112.286 -67.529  48.822  1.00 64.20           C  
ANISOU12238  CB  ALA H 380     4766   4976  14651    958     55    412       C  
ATOM  12239  N   GLU H 381     110.790 -68.455  51.791  1.00 65.32           N  
ANISOU12239  N   GLU H 381     4966   5212  14641   1150     61    402       N  
ATOM  12240  CA  GLU H 381     109.597 -68.529  52.651  1.00 67.32           C  
ANISOU12240  CA  GLU H 381     5248   5498  14834   1220     97    425       C  
ATOM  12241  C   GLU H 381     108.489 -67.432  52.574  1.00 71.92           C  
ANISOU12241  C   GLU H 381     5842   6058  15425   1240    145    436       C  
ATOM  12242  O   GLU H 381     107.375 -67.688  53.015  1.00 72.56           O  
ANISOU12242  O   GLU H 381     5944   6172  15453   1283    185    475       O  
ATOM  12243  CB  GLU H 381     110.083 -68.649  54.093  1.00 70.03           C  
ANISOU12243  CB  GLU H 381     5607   5846  15157   1297     55    359       C  
ATOM  12244  CG  GLU H 381     111.024 -69.840  54.267  1.00 65.53           C  
ANISOU12244  CG  GLU H 381     5029   5305  14566   1288      9    354       C  
ATOM  12245  CD  GLU H 381     111.117 -70.345  55.706  1.00 67.77           C  
ANISOU12245  CD  GLU H 381     5337   5614  14799   1374    -18    317       C  
ATOM  12246  OE1 GLU H 381     111.789 -69.683  56.534  1.00 73.24           O  
ANISOU12246  OE1 GLU H 381     6034   6274  15520   1417    -61    234       O  
ATOM  12247  OE2 GLU H 381     110.521 -71.411  56.005  1.00 64.19           O  
ANISOU12247  OE2 GLU H 381     4899   5212  14277   1398      4    371       O  
ATOM  12248  N   TYR H 382     108.751 -66.242  52.032  1.00 63.58           N  
ANISOU12248  N   TYR H 382     4775   4948  14435   1210    145    404       N  
ATOM  12249  CA  TYR H 382     107.682 -65.224  51.988  1.00 64.42           C  
ANISOU12249  CA  TYR H 382     4894   5036  14547   1231    191    414       C  
ATOM  12250  C   TYR H 382     107.565 -64.402  50.708  1.00 64.27           C  
ANISOU12250  C   TYR H 382     4861   4979  14581   1166    215    435       C  
ATOM  12251  O   TYR H 382     108.495 -63.722  50.341  1.00 64.58           O  
ANISOU12251  O   TYR H 382     4883   4970  14685   1132    188    388       O  
ATOM  12252  CB  TYR H 382     107.848 -64.227  53.130  1.00 69.38           C  
ANISOU12252  CB  TYR H 382     5537   5631  15195   1297    172    335       C  
ATOM  12253  CG  TYR H 382     108.006 -64.836  54.493  1.00 70.06           C  
ANISOU12253  CG  TYR H 382     5641   5745  15233   1371    145    301       C  
ATOM  12254  CD1 TYR H 382     106.928 -64.987  55.341  1.00 71.63           C  
ANISOU12254  CD1 TYR H 382     5868   5974  15374   1438    179    322       C  
ATOM  12255  CD2 TYR H 382     109.236 -65.235  54.938  1.00 69.46           C  
ANISOU12255  CD2 TYR H 382     5556   5664  15171   1375     86    247       C  
ATOM  12256  CE1 TYR H 382     107.087 -65.528  56.593  1.00 72.57           C  
ANISOU12256  CE1 TYR H 382     6008   6115  15450   1509    156    291       C  
ATOM  12257  CE2 TYR H 382     109.403 -65.785  56.176  1.00 70.33           C  
ANISOU12257  CE2 TYR H 382     5687   5799  15238   1445     59    215       C  
ATOM  12258  CZ  TYR H 382     108.335 -65.927  57.007  1.00 71.92           C  
ANISOU12258  CZ  TYR H 382     5919   6028  15381   1512     95    237       C  
ATOM  12259  OH  TYR H 382     108.524 -66.474  58.256  1.00 73.10           O  
ANISOU12259  OH  TYR H 382     6091   6199  15486   1585     68    204       O  
ATOM  12260  N   GLY H 383     106.412 -64.426  50.059  1.00 63.87           N  
ANISOU12260  N   GLY H 383     4816   4946  14504   1151    266    503       N  
ATOM  12261  CA  GLY H 383     106.147 -63.481  49.000  1.00 64.01           C  
ANISOU12261  CA  GLY H 383     4827   4925  14568   1105    292    517       C  
ATOM  12262  C   GLY H 383     105.829 -62.221  49.756  1.00 65.86           C  
ANISOU12262  C   GLY H 383     5075   5125  14825   1159    299    463       C  
ATOM  12263  O   GLY H 383     105.413 -62.288  50.914  1.00 68.29           O  
ANISOU12263  O   GLY H 383     5401   5451  15094   1228    299    442       O  
ATOM  12264  N   VAL H 384     106.033 -61.072  49.125  1.00 64.46           N  
ANISOU12264  N   VAL H 384     4890   4894  14708   1129    304    439       N  
ATOM  12265  CA  VAL H 384     105.925 -59.809  49.849  1.00 69.40           C  
ANISOU12265  CA  VAL H 384     5528   5480  15362   1176    305    378       C  
ATOM  12266  C   VAL H 384     105.070 -58.765  49.089  1.00 72.60           C  
ANISOU12266  C   VAL H 384     5938   5857  15789   1159    348    403       C  
ATOM  12267  O   VAL H 384     105.210 -58.574  47.874  1.00 70.76           O  
ANISOU12267  O   VAL H 384     5691   5604  15589   1097    360    433       O  
ATOM  12268  CB  VAL H 384     107.322 -59.252  50.156  1.00 72.07           C  
ANISOU12268  CB  VAL H 384     5851   5769  15763   1168    255    294       C  
ATOM  12269  CG1 VAL H 384     107.923 -58.693  48.945  1.00 73.52           C  
ANISOU12269  CG1 VAL H 384     6013   5909  16012   1096    256    294       C  
ATOM  12270  CG2 VAL H 384     107.220 -58.189  51.170  1.00 76.72           C  
ANISOU12270  CG2 VAL H 384     6456   6327  16366   1229    249    226       C  
ATOM  12271  N   TYR H 385     104.170 -58.104  49.814  1.00 69.77           N  
ANISOU12271  N   TYR H 385     5601   5497  15410   1218    373    390       N  
ATOM  12272  CA  TYR H 385     103.182 -57.223  49.212  1.00 72.91           C  
ANISOU12272  CA  TYR H 385     6008   5878  15817   1212    416    419       C  
ATOM  12273  C   TYR H 385     103.354 -55.821  49.760  1.00 80.35           C  
ANISOU12273  C   TYR H 385     6960   6767  16803   1245    412    349       C  
ATOM  12274  O   TYR H 385     103.792 -55.665  50.899  1.00 83.25           O  
ANISOU12274  O   TYR H 385     7335   7127  17169   1294    384    288       O  
ATOM  12275  CB  TYR H 385     101.772 -57.753  49.497  1.00 72.03           C  
ANISOU12275  CB  TYR H 385     5914   5817  15638   1250    457    476       C  
ATOM  12276  CG  TYR H 385     101.578 -59.188  49.048  1.00 65.42           C  
ANISOU12276  CG  TYR H 385     5069   5034  14754   1221    462    543       C  
ATOM  12277  CD1 TYR H 385     102.049 -60.250  49.809  1.00 64.94           C  
ANISOU12277  CD1 TYR H 385     5008   5009  14658   1244    436    535       C  
ATOM  12278  CD2 TYR H 385     100.922 -59.481  47.863  1.00 64.55           C  
ANISOU12278  CD2 TYR H 385     4954   4940  14633   1173    492    611       C  
ATOM  12279  CE1 TYR H 385     101.878 -61.562  49.389  1.00 63.62           C  
ANISOU12279  CE1 TYR H 385     4834   4891  14447   1216    442    596       C  
ATOM  12280  CE2 TYR H 385     100.740 -60.790  47.446  1.00 63.24           C  
ANISOU12280  CE2 TYR H 385     4782   4823  14424   1146    497    670       C  
ATOM  12281  CZ  TYR H 385     101.225 -61.823  48.206  1.00 62.89           C  
ANISOU12281  CZ  TYR H 385     4737   4812  14347   1166    472    663       C  
ATOM  12282  OH  TYR H 385     101.071 -63.125  47.781  1.00 62.30           O  
ANISOU12282  OH  TYR H 385     4657   4785  14230   1138    477    721       O  
ATOM  12283  N   VAL H 386     103.033 -54.813  48.939  1.00 71.83           N  
ANISOU12283  N   VAL H 386     5880   5651  15761   1217    437    357       N  
ATOM  12284  CA  VAL H 386     102.904 -53.411  49.398  1.00 72.48           C  
ANISOU12284  CA  VAL H 386     5976   5686  15877   1251    443    301       C  
ATOM  12285  C   VAL H 386     101.459 -53.094  49.832  1.00 72.69           C  
ANISOU12285  C   VAL H 386     6026   5734  15859   1303    485    329       C  
ATOM  12286  O   VAL H 386     100.501 -53.264  49.065  1.00 72.32           O  
ANISOU12286  O   VAL H 386     5982   5708  15788   1285    522    393       O  
ATOM  12287  CB  VAL H 386     103.349 -52.365  48.322  1.00 72.47           C  
ANISOU12287  CB  VAL H 386     5964   5628  15945   1196    450    288       C  
ATOM  12288  CG1 VAL H 386     102.951 -52.790  46.941  1.00 71.82           C  
ANISOU12288  CG1 VAL H 386     5871   5560  15856   1137    476    364       C  
ATOM  12289  CG2 VAL H 386     102.741 -51.021  48.613  1.00 73.03           C  
ANISOU12289  CG2 VAL H 386     6053   5662  16032   1231    473    258       C  
ATOM  12290  N   LYS H 387     101.331 -52.669  51.085  1.00 72.50           N  
ANISOU12290  N   LYS H 387     6020   5704  15822   1369    478    277       N  
ATOM  12291  CA  LYS H 387     100.053 -52.369  51.677  1.00 74.22           C  
ANISOU12291  CA  LYS H 387     6261   5940  15999   1426    515    293       C  
ATOM  12292  C   LYS H 387      99.325 -51.350  50.809  1.00 75.72           C  
ANISOU12292  C   LYS H 387     6456   6102  16214   1404    551    316       C  
ATOM  12293  O   LYS H 387      99.942 -50.387  50.339  1.00 76.99           O  
ANISOU12293  O   LYS H 387     6611   6211  16432   1375    541    280       O  
ATOM  12294  CB  LYS H 387     100.251 -51.840  53.091  1.00 76.68           C  
ANISOU12294  CB  LYS H 387     6592   6236  16308   1495    497    221       C  
ATOM  12295  CG  LYS H 387     101.371 -52.543  53.799  1.00 75.55           C  
ANISOU12295  CG  LYS H 387     6441   6100  16163   1506    449    177       C  
ATOM  12296  CD  LYS H 387     101.834 -51.808  55.035  1.00 78.34           C  
ANISOU12296  CD  LYS H 387     6811   6422  16531   1565    421     91       C  
ATOM  12297  CE  LYS H 387     101.099 -52.262  56.276  1.00 79.26           C  
ANISOU12297  CE  LYS H 387     6954   6576  16584   1643    433     91       C  
ATOM  12298  NZ  LYS H 387     102.033 -52.314  57.444  1.00 82.32           N  
ANISOU12298  NZ  LYS H 387     7351   6953  16975   1689    385     13       N  
ATOM  12299  N   VAL H 388      98.032 -51.570  50.559  1.00 71.67           N  
ANISOU12299  N   VAL H 388     5952   5622  15658   1416    592    375       N  
ATOM  12300  CA  VAL H 388      97.317 -50.686  49.653  1.00 74.82           C  
ANISOU12300  CA  VAL H 388     6354   5997  16076   1394    624    401       C  
ATOM  12301  C   VAL H 388      96.941 -49.431  50.403  1.00 82.72           C  
ANISOU12301  C   VAL H 388     7375   6963  17092   1446    635    350       C  
ATOM  12302  O   VAL H 388      96.979 -48.345  49.842  1.00 87.02           O  
ANISOU12302  O   VAL H 388     7922   7462  17678   1427    644    334       O  
ATOM  12303  CB  VAL H 388      96.091 -51.373  49.037  1.00 71.43           C  
ANISOU12303  CB  VAL H 388     5925   5614  15600   1386    661    480       C  
ATOM  12304  CG1 VAL H 388      94.876 -50.452  49.033  1.00 76.98           C  
ANISOU12304  CG1 VAL H 388     6646   6308  16296   1417    699    490       C  
ATOM  12305  CG2 VAL H 388      96.431 -51.860  47.623  1.00 68.48           C  
ANISOU12305  CG2 VAL H 388     5533   5244  15242   1311    658    529       C  
ATOM  12306  N   THR H 389      96.631 -49.573  51.687  1.00 75.56           N  
ANISOU12306  N   THR H 389     6484   6074  16151   1511    635    322       N  
ATOM  12307  CA  THR H 389      96.339 -48.421  52.542  1.00 83.21           C  
ANISOU12307  CA  THR H 389     7474   7011  17132   1565    643    268       C  
ATOM  12308  C   THR H 389      97.436 -47.348  52.494  1.00 87.85           C  
ANISOU12308  C   THR H 389     8059   7536  17785   1547    614    198       C  
ATOM  12309  O   THR H 389      97.151 -46.166  52.650  1.00 94.54           O  
ANISOU12309  O   THR H 389     8920   8345  18655   1567    627    165       O  
ATOM  12310  CB  THR H 389      96.149 -48.858  53.993  1.00 84.05           C  
ANISOU12310  CB  THR H 389     7598   7144  17195   1636    638    240       C  
ATOM  12311  OG1 THR H 389      97.419 -49.208  54.553  1.00 84.82           O  
ANISOU12311  OG1 THR H 389     7689   7232  17308   1637    590    188       O  
ATOM  12312  CG2 THR H 389      95.251 -50.059  54.043  1.00 77.47           C  
ANISOU12312  CG2 THR H 389     6764   6372  16300   1648    664    306       C  
ATOM  12313  N   SER H 390      98.681 -47.760  52.269  1.00 81.25           N  
ANISOU12313  N   SER H 390     7205   6689  16979   1509    575    175       N  
ATOM  12314  CA  SER H 390      99.789 -46.816  52.186  1.00 85.38           C  
ANISOU12314  CA  SER H 390     7721   7153  17568   1487    547    107       C  
ATOM  12315  C   SER H 390      99.902 -46.083  50.850  1.00 86.20           C  
ANISOU12315  C   SER H 390     7814   7218  17719   1425    563    127       C  
ATOM  12316  O   SER H 390     100.459 -45.002  50.814  1.00 91.41           O  
ANISOU12316  O   SER H 390     8476   7825  18432   1417    555     74       O  
ATOM  12317  CB  SER H 390     101.112 -47.517  52.476  1.00 81.94           C  
ANISOU12317  CB  SER H 390     7267   6716  17149   1469    498     70       C  
ATOM  12318  OG  SER H 390     101.289 -47.700  53.867  1.00 84.11           O  
ANISOU12318  OG  SER H 390     7557   7003  17398   1533    474     19       O  
ATOM  12319  N   ILE H 391      99.408 -46.658  49.759  1.00 82.18           N  
ANISOU12319  N   ILE H 391     7296   6735  17194   1383    585    201       N  
ATOM  12320  CA  ILE H 391      99.314 -45.941  48.479  1.00 82.59           C  
ANISOU12320  CA  ILE H 391     7343   6753  17283   1332    607    227       C  
ATOM  12321  C   ILE H 391      97.960 -45.268  48.247  1.00 86.55           C  
ANISOU12321  C   ILE H 391     7865   7258  17763   1357    649    260       C  
ATOM  12322  O   ILE H 391      97.642 -44.915  47.116  1.00 86.61           O  
ANISOU12322  O   ILE H 391     7871   7253  17785   1318    671    298       O  
ATOM  12323  CB  ILE H 391      99.583 -46.837  47.269  1.00 79.32           C  
ANISOU12323  CB  ILE H 391     6909   6360  16869   1267    606    286       C  
ATOM  12324  CG1 ILE H 391      98.819 -48.157  47.400  1.00 76.94           C  
ANISOU12324  CG1 ILE H 391     6606   6126  16501   1280    616    348       C  
ATOM  12325  CG2 ILE H 391     101.046 -47.078  47.128  1.00 78.15           C  
ANISOU12325  CG2 ILE H 391     6739   6187  16766   1226    568    248       C  
ATOM  12326  CD1 ILE H 391      98.251 -48.698  46.090  1.00 74.82           C  
ANISOU12326  CD1 ILE H 391     6330   5882  16216   1232    639    426       C  
ATOM  12327  N   GLN H 392      97.129 -45.203  49.283  1.00 82.29           N  
ANISOU12327  N   GLN H 392     7344   6740  17184   1421    662    251       N  
ATOM  12328  CA  GLN H 392      95.790 -44.614  49.195  1.00 85.98           C  
ANISOU12328  CA  GLN H 392     7829   7213  17627   1450    702    280       C  
ATOM  12329  C   GLN H 392      95.730 -43.212  48.608  1.00 92.03           C  
ANISOU12329  C   GLN H 392     8605   7925  18438   1437    717    259       C  
ATOM  12330  O   GLN H 392      95.196 -42.994  47.523  1.00 91.38           O  
ANISOU12330  O   GLN H 392     8522   7839  18358   1406    740    305       O  
ATOM  12331  CB  GLN H 392      95.149 -44.580  50.584  1.00 89.77           C  
ANISOU12331  CB  GLN H 392     8327   7712  18068   1525    709    253       C  
ATOM  12332  CG  GLN H 392      94.371 -45.832  50.932  1.00 84.85           C  
ANISOU12332  CG  GLN H 392     7703   7153  17382   1548    723    305       C  
ATOM  12333  CD  GLN H 392      93.118 -45.966  50.106  1.00 82.88           C  
ANISOU12333  CD  GLN H 392     7455   6931  17106   1536    761    374       C  
ATOM  12334  OE1 GLN H 392      92.775 -45.062  49.342  1.00 84.42           O  
ANISOU12334  OE1 GLN H 392     7654   7094  17326   1518    778    381       O  
ATOM  12335  NE2 GLN H 392      92.412 -47.090  50.256  1.00 79.74           N  
ANISOU12335  NE2 GLN H 392     7053   6588  16655   1548    776    424       N  
ATOM  12336  N   ASP H 393      96.268 -42.252  49.341  1.00 85.01           N  
ANISOU12336  N   ASP H 393     7726   6992  17582   1463    704    187       N  
ATOM  12337  CA  ASP H 393      96.118 -40.860  48.951  1.00 91.73           C  
ANISOU12337  CA  ASP H 393     8590   7791  18472   1459    721    163       C  
ATOM  12338  C   ASP H 393      96.784 -40.558  47.619  1.00 90.42           C  
ANISOU12338  C   ASP H 393     8411   7592  18352   1391    720    178       C  
ATOM  12339  O   ASP H 393      96.504 -39.533  47.002  1.00 95.00           O  
ANISOU12339  O   ASP H 393     9003   8136  18958   1380    741    178       O  
ATOM  12340  CB  ASP H 393      96.666 -39.944  50.042  1.00 98.52           C  
ANISOU12340  CB  ASP H 393     9462   8611  19360   1498    703     79       C  
ATOM  12341  CG  ASP H 393      95.825 -39.986  51.300  1.00101.27           C  
ANISOU12341  CG  ASP H 393     9830   8987  19662   1571    713     65       C  
ATOM  12342  OD1 ASP H 393      94.664 -39.504  51.245  1.00103.31           O  
ANISOU12342  OD1 ASP H 393    10104   9251  19897   1598    747     91       O  
ATOM  12343  OD2 ASP H 393      96.317 -40.494  52.335  1.00101.52           O  
ANISOU12343  OD2 ASP H 393     9861   9033  19680   1603    686     27       O  
ATOM  12344  N   TRP H 394      97.665 -41.445  47.173  1.00 93.81           N  
ANISOU12344  N   TRP H 394     8818   8033  18793   1345    697    191       N  
ATOM  12345  CA  TRP H 394      98.271 -41.265  45.867  1.00 92.13           C  
ANISOU12345  CA  TRP H 394     8593   7793  18621   1280    699    210       C  
ATOM  12346  C   TRP H 394      97.361 -41.751  44.744  1.00 88.11           C  
ANISOU12346  C   TRP H 394     8084   7315  18080   1254    727    293       C  
ATOM  12347  O   TRP H 394      97.333 -41.139  43.675  1.00 89.71           O  
ANISOU12347  O   TRP H 394     8288   7489  18307   1219    744    311       O  
ATOM  12348  CB  TRP H 394      99.618 -41.977  45.770  1.00 87.48           C  
ANISOU12348  CB  TRP H 394     7978   7199  18061   1238    664    189       C  
ATOM  12349  CG  TRP H 394     100.143 -41.925  44.370  1.00 85.48           C  
ANISOU12349  CG  TRP H 394     7711   6924  17843   1170    671    219       C  
ATOM  12350  CD1 TRP H 394     100.672 -40.841  43.740  1.00 90.42           C  
ANISOU12350  CD1 TRP H 394     8339   7493  18523   1140    680    190       C  
ATOM  12351  CD2 TRP H 394     100.152 -42.994  43.406  1.00 78.37           C  
ANISOU12351  CD2 TRP H 394     6795   6058  16924   1124    672    284       C  
ATOM  12352  NE1 TRP H 394     101.025 -41.161  42.452  1.00 86.88           N  
ANISOU12352  NE1 TRP H 394     7877   7042  18091   1080    687    233       N  
ATOM  12353  CE2 TRP H 394     100.720 -42.476  42.218  1.00 79.45           C  
ANISOU12353  CE2 TRP H 394     6925   6156  17106   1069    682    290       C  
ATOM  12354  CE3 TRP H 394      99.747 -44.341  43.434  1.00 71.43           C  
ANISOU12354  CE3 TRP H 394     5908   5240  15993   1124    667    336       C  
ATOM  12355  CZ2 TRP H 394     100.892 -43.256  41.066  1.00 73.82           C  
ANISOU12355  CZ2 TRP H 394     6198   5463  16389   1015    685    347       C  
ATOM  12356  CZ3 TRP H 394      99.916 -45.110  42.291  1.00 68.37           C  
ANISOU12356  CZ3 TRP H 394     5505   4870  15601   1070    670    392       C  
ATOM  12357  CH2 TRP H 394     100.481 -44.566  41.123  1.00 68.32           C  
ANISOU12357  CH2 TRP H 394     5492   4825  15641   1016    679    397       C  
ATOM  12358  N   VAL H 395      96.638 -42.852  44.970  1.00 90.81           N  
ANISOU12358  N   VAL H 395     8422   7715  18365   1271    730    340       N  
ATOM  12359  CA  VAL H 395      95.862 -43.450  43.885  1.00 86.68           C  
ANISOU12359  CA  VAL H 395     7896   7227  17812   1243    752    417       C  
ATOM  12360  C   VAL H 395      94.661 -42.567  43.673  1.00 91.78           C  
ANISOU12360  C   VAL H 395     8564   7865  18445   1271    785    433       C  
ATOM  12361  O   VAL H 395      94.301 -42.270  42.536  1.00 91.56           O  
ANISOU12361  O   VAL H 395     8540   7827  18423   1241    803    471       O  
ATOM  12362  CB  VAL H 395      95.427 -44.957  44.135  1.00 79.42           C  
ANISOU12362  CB  VAL H 395     6966   6374  16837   1249    747    465       C  
ATOM  12363  CG1 VAL H 395      96.557 -45.930  43.765  1.00 73.44           C  
ANISOU12363  CG1 VAL H 395     6185   5626  16092   1199    719    472       C  
ATOM  12364  CG2 VAL H 395      94.950 -45.199  45.547  1.00 80.29           C  
ANISOU12364  CG2 VAL H 395     7086   6512  16910   1313    746    441       C  
ATOM  12365  N   GLN H 396      94.075 -42.104  44.771  1.00 84.57           N  
ANISOU12365  N   GLN H 396     7666   6952  17515   1331    792    402       N  
ATOM  12366  CA  GLN H 396      92.960 -41.164  44.690  1.00 90.52           C  
ANISOU12366  CA  GLN H 396     8440   7694  18259   1363    823    409       C  
ATOM  12367  C   GLN H 396      93.365 -39.930  43.903  1.00 95.40           C  
ANISOU12367  C   GLN H 396     9068   8253  18927   1336    830    387       C  
ATOM  12368  O   GLN H 396      92.649 -39.516  42.992  1.00 97.12           O  
ANISOU12368  O   GLN H 396     9296   8467  19140   1325    852    424       O  
ATOM  12369  CB  GLN H 396      92.478 -40.770  46.085  1.00 95.53           C  
ANISOU12369  CB  GLN H 396     9090   8332  18876   1430    827    367       C  
ATOM  12370  CG  GLN H 396      91.716 -41.876  46.810  1.00 96.04           C  
ANISOU12370  CG  GLN H 396     9151   8457  18882   1465    833    398       C  
ATOM  12371  CD  GLN H 396      90.792 -41.319  47.868  1.00 96.42           C  
ANISOU12371  CD  GLN H 396     9219   8510  18907   1532    852    374       C  
ATOM  12372  OE1 GLN H 396      90.961 -40.182  48.317  1.00101.63           O  
ANISOU12372  OE1 GLN H 396     9894   9127  19595   1556    853    322       O  
ATOM  12373  NE2 GLN H 396      89.789 -42.101  48.253  1.00 91.14           N  
ANISOU12373  NE2 GLN H 396     8550   7892  18187   1562    870    412       N  
ATOM  12374  N   LYS H 397      94.529 -39.380  44.249  1.00 86.55           N  
ANISOU12374  N   LYS H 397     7943   7088  17853   1325    809    327       N  
ATOM  12375  CA  LYS H 397      95.106 -38.213  43.586  1.00 91.56           C  
ANISOU12375  CA  LYS H 397     8585   7662  18541   1297    815    298       C  
ATOM  12376  C   LYS H 397      95.299 -38.404  42.078  1.00 88.11           C  
ANISOU12376  C   LYS H 397     8141   7221  18117   1237    824    347       C  
ATOM  12377  O   LYS H 397      95.021 -37.511  41.289  1.00 91.96           O  
ANISOU12377  O   LYS H 397     8643   7676  18620   1226    845    356       O  
ATOM  12378  CB  LYS H 397      96.453 -37.854  44.231  1.00 94.05           C  
ANISOU12378  CB  LYS H 397     8892   7937  18905   1289    787    224       C  
ATOM  12379  CG  LYS H 397      96.960 -36.436  43.917  1.00101.18           C  
ANISOU12379  CG  LYS H 397     9807   8774  19863   1276    795    178       C  
ATOM  12380  CD  LYS H 397      98.438 -36.280  44.238  1.00103.23           C  
ANISOU12380  CD  LYS H 397    10051   8996  20177   1250    766    113       C  
ATOM  12381  CE  LYS H 397      99.320 -36.932  43.176  1.00 97.65           C  
ANISOU12381  CE  LYS H 397     9320   8288  19494   1183    757    141       C  
ATOM  12382  NZ  LYS H 397      99.192 -36.283  41.838  1.00 98.55           N  
ANISOU12382  NZ  LYS H 397     9443   8374  19628   1145    785    173       N  
ATOM  12383  N   THR H 398      95.778 -39.567  41.673  1.00 89.16           N  
ANISOU12383  N   THR H 398     8252   7385  18240   1200    808    380       N  
ATOM  12384  CA  THR H 398      96.068 -39.799  40.266  1.00 87.39           C  
ANISOU12384  CA  THR H 398     8020   7156  18029   1143    814    423       C  
ATOM  12385  C   THR H 398      94.789 -39.930  39.450  1.00 87.06           C  
ANISOU12385  C   THR H 398     7990   7144  17945   1148    840    489       C  
ATOM  12386  O   THR H 398      94.719 -39.434  38.324  1.00 87.32           O  
ANISOU12386  O   THR H 398     8031   7154  17991   1120    856    512       O  
ATOM  12387  CB  THR H 398      96.941 -41.073  40.077  1.00 84.06           C  
ANISOU12387  CB  THR H 398     7571   6762  17607   1102    789    440       C  
ATOM  12388  OG1 THR H 398      98.154 -40.950  40.836  1.00 84.42           O  
ANISOU12388  OG1 THR H 398     7604   6780  17693   1098    762    375       O  
ATOM  12389  CG2 THR H 398      97.297 -41.281  38.611  1.00 82.29           C  
ANISOU12389  CG2 THR H 398     7338   6532  17398   1042    797    483       C  
ATOM  12390  N   ILE H 399      93.792 -40.597  40.039  1.00 88.56           N  
ANISOU12390  N   ILE H 399     8181   7383  18083   1186    844    516       N  
ATOM  12391  CA  ILE H 399      92.490 -40.874  39.408  1.00 87.08           C  
ANISOU12391  CA  ILE H 399     8003   7232  17853   1195    866    576       C  
ATOM  12392  C   ILE H 399      91.840 -39.613  38.872  1.00 93.69           C  
ANISOU12392  C   ILE H 399     8864   8034  18701   1209    890    574       C  
ATOM  12393  O   ILE H 399      91.163 -39.631  37.839  1.00 93.06           O  
ANISOU12393  O   ILE H 399     8791   7964  18603   1195    905    621       O  
ATOM  12394  CB  ILE H 399      91.492 -41.545  40.397  1.00 85.75           C  
ANISOU12394  CB  ILE H 399     7835   7114  17633   1244    871    590       C  
ATOM  12395  CG1 ILE H 399      91.905 -42.980  40.747  1.00 82.96           C  
ANISOU12395  CG1 ILE H 399     7459   6806  17255   1230    851    608       C  
ATOM  12396  CG2 ILE H 399      90.100 -41.596  39.792  1.00 89.73           C  
ANISOU12396  CG2 ILE H 399     8349   7646  18099   1258    895    642       C  
ATOM  12397  CD1 ILE H 399      91.747 -43.928  39.623  1.00 79.96           C  
ANISOU12397  CD1 ILE H 399     7067   6459  16855   1185    852    671       C  
ATOM  12398  N   ALA H 400      92.067 -38.526  39.604  1.00 84.33           N  
ANISOU12398  N   ALA H 400     7692   6805  17543   1238    892    517       N  
ATOM  12399  CA  ALA H 400      91.622 -37.183  39.257  1.00 91.57           C  
ANISOU12399  CA  ALA H 400     8634   7680  18478   1254    914    502       C  
ATOM  12400  C   ALA H 400      92.113 -36.690  37.892  1.00 92.56           C  
ANISOU12400  C   ALA H 400     8766   7771  18633   1207    921    518       C  
ATOM  12401  O   ALA H 400      91.555 -35.760  37.345  1.00 97.25           O  
ANISOU12401  O   ALA H 400     9382   8340  19229   1217    941    524       O  
ATOM  12402  CB  ALA H 400      92.041 -36.226  40.341  1.00 97.99           C  
ANISOU12402  CB  ALA H 400     9457   8454  19321   1287    910    432       C  
ATOM  12403  N   GLU H 401      93.146 -37.307  37.335  1.00 93.28           N  
ANISOU12403  N   GLU H 401     8837   7860  18744   1156    907    526       N  
ATOM  12404  CA  GLU H 401      93.586 -36.960  35.986  1.00 93.99           C  
ANISOU12404  CA  GLU H 401     8932   7923  18856   1110    916    547       C  
ATOM  12405  C   GLU H 401      93.494 -38.143  35.009  1.00 86.92           C  
ANISOU12405  C   GLU H 401     8021   7070  17933   1072    912    610       C  
ATOM  12406  O   GLU H 401      92.597 -38.204  34.159  1.00 86.27           O  
ANISOU12406  O   GLU H 401     7951   7008  17821   1074    926    658       O  
ATOM  12407  CB  GLU H 401      95.014 -36.432  36.024  1.00 96.23           C  
ANISOU12407  CB  GLU H 401     9208   8156  19199   1078    907    495       C  
ATOM  12408  CG  GLU H 401      95.185 -35.134  36.806  1.00101.74           C  
ANISOU12408  CG  GLU H 401     9923   8804  19930   1109    913    430       C  
ATOM  12409  CD  GLU H 401      95.671 -35.349  38.236  1.00103.31           C  
ANISOU12409  CD  GLU H 401    10108   9005  20139   1135    890    377       C  
ATOM  12410  OE1 GLU H 401      94.817 -35.714  39.076  1.00104.23           O  
ANISOU12410  OE1 GLU H 401    10227   9158  20217   1179    888    384       O  
ATOM  12411  OE2 GLU H 401      96.888 -35.137  38.516  1.00103.82           O  
ANISOU12411  OE2 GLU H 401    10160   9036  20251   1111    875    326       O  
TER   12412      GLU H 401                                                      
ATOM  12413  N   ALA I  86     129.204 -84.572  75.044  1.00 90.52           N  
ANISOU12413  N   ALA I  86     9236  10977  14180   1075    661  -2338       N  
ATOM  12414  CA  ALA I  86     129.261 -83.703  73.873  1.00 88.29           C  
ANISOU12414  CA  ALA I  86     8979  10666  13901   1061    584  -2358       C  
ATOM  12415  C   ALA I  86     129.208 -84.499  72.567  1.00 81.67           C  
ANISOU12415  C   ALA I  86     8090   9821  13121   1078    641  -2356       C  
ATOM  12416  O   ALA I  86     128.418 -84.191  71.663  1.00 77.85           O  
ANISOU12416  O   ALA I  86     7615   9300  12666   1098    626  -2433       O  
ATOM  12417  CB  ALA I  86     130.516 -82.854  73.923  1.00 92.34           C  
ANISOU12417  CB  ALA I  86     9523  11197  14364   1009    492  -2272       C  
ATOM  12418  N   ASP I  87     130.064 -85.518  72.472  1.00 86.49           N  
ANISOU12418  N   ASP I  87     8647  10468  13748   1068    707  -2266       N  
ATOM  12419  CA  ASP I  87     130.193 -86.314  71.244  1.00 80.94           C  
ANISOU12419  CA  ASP I  87     7893   9764  13098   1078    761  -2248       C  
ATOM  12420  C   ASP I  87     129.347 -87.609  71.259  1.00 79.83           C  
ANISOU12420  C   ASP I  87     7699   9622  13011   1125    881  -2291       C  
ATOM  12421  O   ASP I  87     129.407 -88.440  70.327  1.00 76.07           O  
ANISOU12421  O   ASP I  87     7174   9147  12581   1138    941  -2276       O  
ATOM  12422  CB  ASP I  87     131.677 -86.625  70.961  1.00 80.80           C  
ANISOU12422  CB  ASP I  87     7847   9784  13069   1038    757  -2122       C  
ATOM  12423  CG  ASP I  87     132.352 -87.505  72.036  1.00 84.98           C  
ANISOU12423  CG  ASP I  87     8344  10359  13584   1030    821  -2042       C  
ATOM  12424  OD1 ASP I  87     131.751 -88.499  72.522  1.00 87.53           O  
ANISOU12424  OD1 ASP I  87     8632  10690  13936   1063    915  -2068       O  
ATOM  12425  OD2 ASP I  87     133.535 -87.212  72.362  1.00 85.78           O  
ANISOU12425  OD2 ASP I  87     8454  10490  13647    988    778  -1949       O  
ATOM  12426  N   GLU I  88     128.570 -87.778  72.328  1.00 82.75           N  
ANISOU12426  N   GLU I  88     8078   9990  13372   1149    915  -2344       N  
ATOM  12427  CA  GLU I  88     127.618 -88.874  72.401  1.00 82.75           C  
ANISOU12427  CA  GLU I  88     8036   9985  13421   1196   1021  -2400       C  
ATOM  12428  C   GLU I  88     126.400 -88.510  71.543  1.00 79.81           C  
ANISOU12428  C   GLU I  88     7678   9565  13082   1229   1010  -2513       C  
ATOM  12429  O   GLU I  88     125.939 -89.320  70.739  1.00 77.14           O  
ANISOU12429  O   GLU I  88     7297   9216  12797   1257   1079  -2540       O  
ATOM  12430  CB  GLU I  88     127.229 -89.199  73.861  1.00 88.21           C  
ANISOU12430  CB  GLU I  88     8732  10693  14091   1210   1063  -2415       C  
ATOM  12431  CG  GLU I  88     126.621 -88.059  74.680  1.00 91.03           C  
ANISOU12431  CG  GLU I  88     9155  11029  14405   1210    988  -2482       C  
ATOM  12432  CD  GLU I  88     127.636 -86.981  75.101  1.00 97.15           C  
ANISOU12432  CD  GLU I  88     9977  11817  15118   1161    885  -2418       C  
ATOM  12433  OE1 GLU I  88     128.810 -87.318  75.392  1.00 99.21           O  
ANISOU12433  OE1 GLU I  88    10219  12117  15361   1130    892  -2313       O  
ATOM  12434  OE2 GLU I  88     127.256 -85.783  75.144  1.00100.07           O  
ANISOU12434  OE2 GLU I  88    10404  12159  15458   1154    796  -2472       O  
ATOM  12435  N   SER I  89     125.883 -87.296  71.697  1.00 82.53           N  
ANISOU12435  N   SER I  89     8083   9879  13396   1225    923  -2578       N  
ATOM  12436  CA  SER I  89     124.862 -86.807  70.772  1.00 79.88           C  
ANISOU12436  CA  SER I  89     7765   9497  13088   1250    897  -2678       C  
ATOM  12437  C   SER I  89     125.090 -85.343  70.398  1.00 78.37           C  
ANISOU12437  C   SER I  89     7635   9283  12858   1221    773  -2691       C  
ATOM  12438  O   SER I  89     124.974 -84.441  71.248  1.00 81.56           O  
ANISOU12438  O   SER I  89     8091   9682  13216   1210    707  -2713       O  
ATOM  12439  CB  SER I  89     123.465 -86.971  71.364  1.00 83.00           C  
ANISOU12439  CB  SER I  89     8169   9869  13498   1295    940  -2785       C  
ATOM  12440  OG  SER I  89     122.538 -86.174  70.648  1.00 81.10           O  
ANISOU12440  OG  SER I  89     7962   9583  13269   1312    888  -2882       O  
ATOM  12441  N   LEU I  90     125.360 -85.109  69.113  1.00 75.37           N  
ANISOU12441  N   LEU I  90     7250   8888  12499   1212    741  -2683       N  
ATOM  12442  CA  LEU I  90     125.713 -83.780  68.618  1.00 73.97           C  
ANISOU12442  CA  LEU I  90     7125   8691  12288   1181    625  -2684       C  
ATOM  12443  C   LEU I  90     124.486 -82.913  68.393  1.00 74.07           C  
ANISOU12443  C   LEU I  90     7183   8656  12303   1206    577  -2803       C  
ATOM  12444  O   LEU I  90     124.534 -81.702  68.596  1.00 75.09           O  
ANISOU12444  O   LEU I  90     7370   8770  12390   1185    479  -2822       O  
ATOM  12445  CB  LEU I  90     126.525 -83.903  67.333  1.00 70.31           C  
ANISOU12445  CB  LEU I  90     6636   8231  11846   1160    613  -2623       C  
ATOM  12446  CG  LEU I  90     127.185 -82.651  66.785  1.00 69.70           C  
ANISOU12446  CG  LEU I  90     6607   8143  11734   1120    497  -2597       C  
ATOM  12447  CD1 LEU I  90     128.664 -82.879  66.569  1.00 71.01           C  
ANISOU12447  CD1 LEU I  90     6749   8346  11886   1078    487  -2473       C  
ATOM  12448  CD2 LEU I  90     126.527 -82.322  65.488  1.00 67.64           C  
ANISOU12448  CD2 LEU I  90     6350   7841  11508   1138    475  -2667       C  
ATOM  12449  N   LYS I  91     123.384 -83.530  67.980  1.00 71.88           N  
ANISOU12449  N   LYS I  91     6880   8356  12075   1250    644  -2884       N  
ATOM  12450  CA  LYS I  91     122.155 -82.768  67.718  1.00 72.40           C  
ANISOU12450  CA  LYS I  91     6985   8375  12147   1277    604  -3002       C  
ATOM  12451  C   LYS I  91     121.434 -82.388  69.007  1.00 76.15           C  
ANISOU12451  C   LYS I  91     7497   8845  12591   1292    594  -3060       C  
ATOM  12452  O   LYS I  91     120.622 -81.474  69.007  1.00 76.52           O  
ANISOU12452  O   LYS I  91     7592   8858  12626   1303    535  -3145       O  
ATOM  12453  CB  LYS I  91     121.209 -83.544  66.797  1.00 71.81           C  
ANISOU12453  CB  LYS I  91     6871   8277  12137   1320    678  -3071       C  
ATOM  12454  CG  LYS I  91     120.617 -84.801  67.406  1.00 70.23           C  
ANISOU12454  CG  LYS I  91     6623   8091  11969   1356    794  -3090       C  
ATOM  12455  CD  LYS I  91     120.030 -85.714  66.334  1.00 70.75           C  
ANISOU12455  CD  LYS I  91     6639   8142  12101   1390    871  -3128       C  
ATOM  12456  CE  LYS I  91     118.636 -86.220  66.734  1.00 70.05           C  
ANISOU12456  CE  LYS I  91     6539   8033  12042   1440    940  -3230       C  
ATOM  12457  NZ  LYS I  91     118.073 -87.170  65.725  1.00 71.17           N  
ANISOU12457  NZ  LYS I  91     6630   8162  12249   1474   1020  -3264       N  
ATOM  12458  N   ASP I  92     121.732 -83.092  70.099  1.00 73.70           N  
ANISOU12458  N   ASP I  92     7164   8569  12268   1291    652  -3014       N  
ATOM  12459  CA  ASP I  92     121.291 -82.659  71.424  1.00 78.80           C  
ANISOU12459  CA  ASP I  92     7849   9217  12876   1296    633  -3050       C  
ATOM  12460  C   ASP I  92     122.209 -81.547  71.913  1.00 81.05           C  
ANISOU12460  C   ASP I  92     8184   9512  13098   1250    529  -2993       C  
ATOM  12461  O   ASP I  92     121.783 -80.630  72.620  1.00 84.75           O  
ANISOU12461  O   ASP I  92     8706   9966  13528   1248    467  -3042       O  
ATOM  12462  CB  ASP I  92     121.285 -83.823  72.418  1.00 81.92           C  
ANISOU12462  CB  ASP I  92     8201   9644  13279   1313    733  -3020       C  
ATOM  12463  CG  ASP I  92     120.091 -84.744  72.228  1.00 81.06           C  
ANISOU12463  CG  ASP I  92     8055   9519  13225   1364    828  -3101       C  
ATOM  12464  OD1 ASP I  92     118.932 -84.246  72.310  1.00 81.17           O  
ANISOU12464  OD1 ASP I  92     8099   9498  13243   1392    810  -3206       O  
ATOM  12465  OD2 ASP I  92     120.312 -85.959  71.982  1.00 80.84           O  
ANISOU12465  OD2 ASP I  92     7968   9512  13236   1375    921  -3060       O  
ATOM  12466  N   ALA I  93     123.478 -81.639  71.523  1.00 77.48           N  
ANISOU12466  N   ALA I  93     7716   9088  12636   1212    511  -2890       N  
ATOM  12467  CA  ALA I  93     124.479 -80.683  71.962  1.00 79.61           C  
ANISOU12467  CA  ALA I  93     8028   9372  12847   1166    418  -2824       C  
ATOM  12468  C   ALA I  93     124.160 -79.281  71.469  1.00 78.49           C  
ANISOU12468  C   ALA I  93     7948   9193  12682   1155    308  -2881       C  
ATOM  12469  O   ALA I  93     124.313 -78.322  72.223  1.00 82.27           O  
ANISOU12469  O   ALA I  93     8479   9670  13110   1134    232  -2883       O  
ATOM  12470  CB  ALA I  93     125.848 -81.102  71.496  1.00 77.52           C  
ANISOU12470  CB  ALA I  93     7730   9141  12582   1130    424  -2706       C  
ATOM  12471  N   ILE I  94     123.702 -79.149  70.224  1.00 76.28           N  
ANISOU12471  N   ILE I  94     7663   8881  12438   1169    298  -2930       N  
ATOM  12472  CA  ILE I  94     123.483 -77.813  69.665  1.00 76.44           C  
ANISOU12472  CA  ILE I  94     7740   8866  12436   1156    191  -2979       C  
ATOM  12473  C   ILE I  94     122.261 -77.113  70.297  1.00 78.08           C  
ANISOU12473  C   ILE I  94     7996   9042  12630   1183    161  -3089       C  
ATOM  12474  O   ILE I  94     122.022 -75.926  70.053  1.00 78.60           O  
ANISOU12474  O   ILE I  94     8116   9079  12670   1173     68  -3134       O  
ATOM  12475  CB  ILE I  94     123.329 -77.847  68.124  1.00 74.75           C  
ANISOU12475  CB  ILE I  94     7509   8628  12266   1164    188  -3001       C  
ATOM  12476  CG1 ILE I  94     122.030 -78.516  67.696  1.00 73.44           C  
ANISOU12476  CG1 ILE I  94     7314   8434  12154   1216    263  -3097       C  
ATOM  12477  CG2 ILE I  94     124.465 -78.592  67.504  1.00 74.07           C  
ANISOU12477  CG2 ILE I  94     7374   8573  12198   1141    223  -2897       C  
ATOM  12478  CD1 ILE I  94     121.857 -78.603  66.178  1.00 71.71           C  
ANISOU12478  CD1 ILE I  94     7076   8191  11980   1225    264  -3120       C  
ATOM  12479  N   LYS I  95     121.516 -77.840  71.131  1.00 78.09           N  
ANISOU12479  N   LYS I  95     7977   9049  12644   1217    238  -3130       N  
ATOM  12480  CA  LYS I  95     120.331 -77.299  71.795  1.00 81.22           C  
ANISOU12480  CA  LYS I  95     8414   9418  13029   1245    220  -3234       C  
ATOM  12481  C   LYS I  95     120.646 -76.311  72.926  1.00 86.52           C  
ANISOU12481  C   LYS I  95     9141  10096  13635   1219    141  -3220       C  
ATOM  12482  O   LYS I  95     119.783 -75.528  73.326  1.00 88.38           O  
ANISOU12482  O   LYS I  95     9424  10305  13853   1234     96  -3304       O  
ATOM  12483  CB  LYS I  95     119.472 -78.439  72.340  1.00 82.77           C  
ANISOU12483  CB  LYS I  95     8568   9620  13261   1288    331  -3278       C  
ATOM  12484  CG  LYS I  95     118.738 -79.222  71.266  1.00 78.45           C  
ANISOU12484  CG  LYS I  95     7977   9053  12778   1325    402  -3330       C  
ATOM  12485  CD  LYS I  95     117.961 -80.381  71.866  1.00 80.69           C  
ANISOU12485  CD  LYS I  95     8218   9345  13095   1365    514  -3367       C  
ATOM  12486  CE  LYS I  95     117.370 -81.282  70.791  1.00 77.61           C  
ANISOU12486  CE  LYS I  95     7777   8940  12770   1399    591  -3405       C  
ATOM  12487  NZ  LYS I  95     116.721 -82.492  71.381  1.00 75.03           N  
ANISOU12487  NZ  LYS I  95     7405   8626  12476   1436    704  -3429       N  
ATOM  12488  N   ASP I  96     121.870 -76.344  73.440  1.00 80.20           N  
ANISOU12488  N   ASP I  96     8338   9333  12801   1180    124  -3115       N  
ATOM  12489  CA  ASP I  96     122.304 -75.372  74.439  1.00 85.57           C  
ANISOU12489  CA  ASP I  96     9072  10022  13418   1150     43  -3092       C  
ATOM  12490  C   ASP I  96     122.280 -73.970  73.823  1.00 84.84           C  
ANISOU12490  C   ASP I  96     9038   9897  13300   1130    -74  -3127       C  
ATOM  12491  O   ASP I  96     122.982 -73.693  72.848  1.00 81.36           O  
ANISOU12491  O   ASP I  96     8595   9454  12863   1105   -115  -3081       O  
ATOM  12492  CB  ASP I  96     123.699 -75.742  74.964  1.00 87.09           C  
ANISOU12492  CB  ASP I  96     9244  10262  13583   1111     50  -2967       C  
ATOM  12493  CG  ASP I  96     124.256 -74.737  75.965  1.00 92.90           C  
ANISOU12493  CG  ASP I  96    10035  11009  14253   1076    -36  -2934       C  
ATOM  12494  OD1 ASP I  96     125.461 -74.867  76.292  1.00 95.55           O  
ANISOU12494  OD1 ASP I  96    10361  11381  14563   1040    -46  -2831       O  
ATOM  12495  OD2 ASP I  96     123.515 -73.830  76.418  1.00 94.96           O  
ANISOU12495  OD2 ASP I  96    10348  11243  14488   1086    -93  -3011       O  
ATOM  12496  N   PRO I  97     121.438 -73.086  74.381  1.00 87.46           N  
ANISOU12496  N   PRO I  97     9424  10202  13606   1143   -127  -3210       N  
ATOM  12497  CA  PRO I  97     121.243 -71.732  73.848  1.00 87.38           C  
ANISOU12497  CA  PRO I  97     9473  10157  13572   1129   -236  -3257       C  
ATOM  12498  C   PRO I  97     122.465 -70.838  74.021  1.00 89.59           C  
ANISOU12498  C   PRO I  97     9789  10453  13799   1076   -331  -3173       C  
ATOM  12499  O   PRO I  97     122.557 -69.813  73.347  1.00 89.26           O  
ANISOU12499  O   PRO I  97     9788  10386  13741   1059   -419  -3190       O  
ATOM  12500  CB  PRO I  97     120.069 -71.196  74.672  1.00 92.01           C  
ANISOU12500  CB  PRO I  97    10101  10717  14141   1158   -253  -3359       C  
ATOM  12501  CG  PRO I  97     120.126 -71.976  75.942  1.00 95.64           C  
ANISOU12501  CG  PRO I  97    10537  11210  14591   1167   -184  -3330       C  
ATOM  12502  CD  PRO I  97     120.563 -73.348  75.536  1.00 92.18           C  
ANISOU12502  CD  PRO I  97    10028  10800  14197   1174    -83  -3269       C  
ATOM  12503  N   ALA I  98     123.385 -71.218  74.904  1.00 86.03           N  
ANISOU12503  N   ALA I  98     9325  10043  13320   1052   -312  -3084       N  
ATOM  12504  CA  ALA I  98     124.539 -70.374  75.191  1.00 89.31           C  
ANISOU12504  CA  ALA I  98     9775  10476  13682   1001   -400  -3004       C  
ATOM  12505  C   ALA I  98     125.508 -70.347  74.017  1.00 85.41           C  
ANISOU12505  C   ALA I  98     9263   9988  13200    971   -427  -2932       C  
ATOM  12506  O   ALA I  98     126.416 -69.520  73.961  1.00 87.78           O  
ANISOU12506  O   ALA I  98     9596  10296  13461    929   -511  -2874       O  
ATOM  12507  CB  ALA I  98     125.245 -70.855  76.453  1.00 94.29           C  
ANISOU12507  CB  ALA I  98    10393  11150  14282    985   -367  -2928       C  
ATOM  12508  N   LEU I  99     125.317 -71.267  73.084  1.00 88.71           N  
ANISOU12508  N   LEU I  99     9628  10404  13673    992   -354  -2936       N  
ATOM  12509  CA  LEU I  99     126.298 -71.474  72.026  1.00 85.12           C  
ANISOU12509  CA  LEU I  99     9145   9961  13234    965   -361  -2857       C  
ATOM  12510  C   LEU I  99     125.957 -70.804  70.695  1.00 82.06           C  
ANISOU12510  C   LEU I  99     8777   9536  12867    967   -416  -2908       C  
ATOM  12511  O   LEU I  99     126.710 -70.956  69.727  1.00 78.87           O  
ANISOU12511  O   LEU I  99     8350   9138  12479    947   -423  -2849       O  
ATOM  12512  CB  LEU I  99     126.510 -72.977  71.791  1.00 81.36           C  
ANISOU12512  CB  LEU I  99     8595   9513  12806    982   -244  -2812       C  
ATOM  12513  CG  LEU I  99     127.357 -73.808  72.764  1.00 84.57           C  
ANISOU12513  CG  LEU I  99     8967   9969  13198    967   -187  -2719       C  
ATOM  12514  CD1 LEU I  99     127.489 -73.184  74.150  1.00 91.04           C  
ANISOU12514  CD1 LEU I  99     9830  10800  13960    951   -232  -2712       C  
ATOM  12515  CD2 LEU I  99     126.780 -75.215  72.887  1.00 82.94           C  
ANISOU12515  CD2 LEU I  99     8700   9773  13040   1007    -61  -2738       C  
ATOM  12516  N   GLU I 100     124.842 -70.083  70.613  1.00 82.72           N  
ANISOU12516  N   GLU I 100     8901   9578  12950    992   -455  -3014       N  
ATOM  12517  CA  GLU I 100     124.395 -69.654  69.288  1.00 79.79           C  
ANISOU12517  CA  GLU I 100     8539   9170  12609   1002   -489  -3068       C  
ATOM  12518  C   GLU I 100     125.025 -68.344  68.832  1.00 82.13           C  
ANISOU12518  C   GLU I 100     8888   9452  12866    961   -609  -3045       C  
ATOM  12519  O   GLU I 100     124.910 -67.305  69.489  1.00 86.92           O  
ANISOU12519  O   GLU I 100     9552  10047  13425    948   -688  -3071       O  
ATOM  12520  CB  GLU I 100     122.862 -69.560  69.211  1.00 79.18           C  
ANISOU12520  CB  GLU I 100     8475   9053  12558   1050   -469  -3197       C  
ATOM  12521  CG  GLU I 100     122.164 -68.751  70.278  1.00 83.90           C  
ANISOU12521  CG  GLU I 100     9128   9635  13116   1059   -516  -3264       C  
ATOM  12522  CD  GLU I 100     120.655 -68.794  70.102  1.00 83.12           C  
ANISOU12522  CD  GLU I 100     9035   9498  13050   1109   -486  -3389       C  
ATOM  12523  OE1 GLU I 100     120.201 -69.541  69.203  1.00 78.91           O  
ANISOU12523  OE1 GLU I 100     8458   8953  12570   1136   -422  -3418       O  
ATOM  12524  OE2 GLU I 100     119.927 -68.084  70.845  1.00 87.02           O  
ANISOU12524  OE2 GLU I 100     9575   9973  13516   1121   -526  -3459       O  
ATOM  12525  N   ASN I 101     125.703 -68.430  67.689  1.00 81.02           N  
ANISOU12525  N   ASN I 101     8726   9313  12744    942   -621  -2995       N  
ATOM  12526  CA  ASN I 101     126.400 -67.308  67.077  1.00 83.01           C  
ANISOU12526  CA  ASN I 101     9020   9554  12965    903   -728  -2964       C  
ATOM  12527  C   ASN I 101     127.444 -66.734  68.027  1.00 87.99           C  
ANISOU12527  C   ASN I 101     9682  10215  13537    858   -789  -2883       C  
ATOM  12528  O   ASN I 101     127.790 -65.552  67.971  1.00 91.93           O  
ANISOU12528  O   ASN I 101    10234  10700  13995    828   -892  -2878       O  
ATOM  12529  CB  ASN I 101     125.397 -66.251  66.632  1.00 84.18           C  
ANISOU12529  CB  ASN I 101     9221   9652  13111    920   -798  -3070       C  
ATOM  12530  CG  ASN I 101     124.385 -66.807  65.639  1.00 79.48           C  
ANISOU12530  CG  ASN I 101     8595   9028  12575    963   -740  -3149       C  
ATOM  12531  OD1 ASN I 101     123.292 -67.262  66.016  1.00 78.96           O  
ANISOU12531  OD1 ASN I 101     8518   8949  12533   1005   -681  -3228       O  
ATOM  12532  ND2 ASN I 101     124.760 -66.808  64.361  1.00 77.50           N  
ANISOU12532  ND2 ASN I 101     8328   8769  12351    952   -754  -3127       N  
ATOM  12533  N   LYS I 102     127.946 -67.606  68.898  1.00 83.62           N  
ANISOU12533  N   LYS I 102     9092   9700  12978    855   -722  -2819       N  
ATOM  12534  CA  LYS I 102     129.044 -67.290  69.788  1.00 85.09           C  
ANISOU12534  CA  LYS I 102     9297   9922  13113    813   -763  -2729       C  
ATOM  12535  C   LYS I 102     130.310 -67.188  68.945  1.00 84.73           C  
ANISOU12535  C   LYS I 102     9237   9894  13063    771   -799  -2632       C  
ATOM  12536  O   LYS I 102     130.384 -67.791  67.873  1.00 83.28           O  
ANISOU12536  O   LYS I 102     9012   9706  12923    780   -757  -2620       O  
ATOM  12537  CB  LYS I 102     129.164 -68.364  70.868  1.00 85.50           C  
ANISOU12537  CB  LYS I 102     9308  10010  13168    825   -672  -2691       C  
ATOM  12538  CG  LYS I 102     130.163 -68.077  71.962  1.00 87.17           C  
ANISOU12538  CG  LYS I 102     9539  10258  13325    787   -708  -2607       C  
ATOM  12539  CD  LYS I 102     130.059 -69.125  73.046  1.00 87.55           C  
ANISOU12539  CD  LYS I 102     9550  10336  13379    806   -615  -2588       C  
ATOM  12540  CE  LYS I 102     131.263 -69.109  73.957  1.00 88.92           C  
ANISOU12540  CE  LYS I 102     9726  10552  13507    766   -634  -2483       C  
ATOM  12541  NZ  LYS I 102     131.407 -70.414  74.654  1.00 88.73           N  
ANISOU12541  NZ  LYS I 102     9647  10564  13502    781   -527  -2441       N  
ATOM  12542  N   GLU I 103     131.294 -66.416  69.405  1.00 88.25           N  
ANISOU12542  N   GLU I 103     9718  10357  13457    726   -877  -2563       N  
ATOM  12543  CA  GLU I 103     132.527 -66.237  68.646  1.00 88.97           C  
ANISOU12543  CA  GLU I 103     9800  10465  13540    684   -918  -2469       C  
ATOM  12544  C   GLU I 103     133.509 -67.369  68.892  1.00 87.14           C  
ANISOU12544  C   GLU I 103     9510  10281  13318    670   -843  -2365       C  
ATOM  12545  O   GLU I 103     133.882 -67.640  70.030  1.00 90.05           O  
ANISOU12545  O   GLU I 103     9875  10680  13659    661   -822  -2322       O  
ATOM  12546  CB  GLU I 103     133.203 -64.923  69.004  1.00 96.03           C  
ANISOU12546  CB  GLU I 103    10756  11358  14373    640  -1036  -2437       C  
ATOM  12547  CG  GLU I 103     132.311 -63.724  69.037  1.00 99.13           C  
ANISOU12547  CG  GLU I 103    11212  11707  14744    649  -1117  -2534       C  
ATOM  12548  CD  GLU I 103     133.060 -62.504  69.536  1.00106.82           C  
ANISOU12548  CD  GLU I 103    12245  12685  15655    604  -1228  -2493       C  
ATOM  12549  OE1 GLU I 103     134.300 -62.597  69.700  1.00110.12           O  
ANISOU12549  OE1 GLU I 103    12652  13138  16051    565  -1242  -2388       O  
ATOM  12550  OE2 GLU I 103     132.412 -61.457  69.767  1.00109.97           O  
ANISOU12550  OE2 GLU I 103    12702  13052  16029    608  -1300  -2566       O  
ATOM  12551  N   HIS I 104     133.861 -68.077  67.829  1.00 91.00           N  
ANISOU12551  N   HIS I 104     9950  10776  13848    671   -798  -2328       N  
ATOM  12552  CA  HIS I 104     134.961 -69.028  67.858  1.00 89.67           C  
ANISOU12552  CA  HIS I 104     9728  10653  13688    651   -740  -2219       C  
ATOM  12553  C   HIS I 104     136.250 -68.546  67.145  1.00 91.79           C  
ANISOU12553  C   HIS I 104    10002  10936  13937    602   -806  -2127       C  
ATOM  12554  O   HIS I 104     137.234 -69.295  67.081  1.00 91.21           O  
ANISOU12554  O   HIS I 104     9885  10901  13871    583   -764  -2032       O  
ATOM  12555  CB  HIS I 104     134.484 -70.358  67.270  1.00 83.29           C  
ANISOU12555  CB  HIS I 104     8855   9848  12944    689   -627  -2236       C  
ATOM  12556  CG  HIS I 104     133.685 -70.204  66.019  1.00 79.68           C  
ANISOU12556  CG  HIS I 104     8396   9350  12527    714   -631  -2313       C  
ATOM  12557  ND1 HIS I 104     132.450 -69.589  65.997  1.00 78.61           N  
ANISOU12557  ND1 HIS I 104     8300   9173  12397    744   -659  -2427       N  
ATOM  12558  CD2 HIS I 104     133.944 -70.572  64.744  1.00 77.34           C  
ANISOU12558  CD2 HIS I 104     8067   9049  12270    714   -613  -2292       C  
ATOM  12559  CE1 HIS I 104     131.983 -69.581  64.762  1.00 75.82           C  
ANISOU12559  CE1 HIS I 104     7936   8790  12082    761   -658  -2473       C  
ATOM  12560  NE2 HIS I 104     132.871 -70.176  63.981  1.00 74.93           N  
ANISOU12560  NE2 HIS I 104     7780   8699  11992    743   -629  -2393       N  
ATOM  12561  N   ASP I 105     136.249 -67.327  66.596  1.00 91.92           N  
ANISOU12561  N   ASP I 105    10071  10924  13931    582   -908  -2154       N  
ATOM  12562  CA  ASP I 105     137.324 -66.910  65.676  1.00 93.42           C  
ANISOU12562  CA  ASP I 105    10261  11121  14112    541   -966  -2079       C  
ATOM  12563  C   ASP I 105     138.481 -66.111  66.288  1.00100.36           C  
ANISOU12563  C   ASP I 105    11177  12025  14932    489  -1049  -1996       C  
ATOM  12564  O   ASP I 105     139.382 -65.665  65.571  1.00102.51           O  
ANISOU12564  O   ASP I 105    11454  12302  15192    453  -1105  -1935       O  
ATOM  12565  CB  ASP I 105     136.735 -66.098  64.522  1.00 91.98           C  
ANISOU12565  CB  ASP I 105    10110  10893  13945    548  -1027  -2151       C  
ATOM  12566  CG  ASP I 105     136.308 -64.701  64.941  1.00 97.48           C  
ANISOU12566  CG  ASP I 105    10881  11560  14597    539  -1131  -2210       C  
ATOM  12567  OD1 ASP I 105     136.388 -64.367  66.149  1.00101.38           O  
ANISOU12567  OD1 ASP I 105    11404  12067  15050    529  -1153  -2203       O  
ATOM  12568  OD2 ASP I 105     135.864 -63.933  64.054  1.00 98.24           O  
ANISOU12568  OD2 ASP I 105    11008  11619  14700    541  -1190  -2267       O  
ATOM  12569  N   ILE I 106     138.445 -65.908  67.597  1.00 91.25           N  
ANISOU12569  N   ILE I 106    10047  10884  13740    486  -1058  -1995       N  
ATOM  12570  CA  ILE I 106     139.487 -65.137  68.275  1.00 98.24           C  
ANISOU12570  CA  ILE I 106    10968  11792  14566    438  -1136  -1920       C  
ATOM  12571  C   ILE I 106     140.809 -65.887  68.341  1.00 97.64           C  
ANISOU12571  C   ILE I 106    10847  11765  14487    407  -1099  -1796       C  
ATOM  12572  O   ILE I 106     140.848 -67.035  68.757  1.00 93.18           O  
ANISOU12572  O   ILE I 106    10232  11227  13946    425  -1005  -1768       O  
ATOM  12573  CB  ILE I 106     139.051 -64.764  69.706  1.00103.03           C  
ANISOU12573  CB  ILE I 106    11612  12400  15133    444  -1152  -1954       C  
ATOM  12574  CG1 ILE I 106     137.964 -63.689  69.658  1.00103.69           C  
ANISOU12574  CG1 ILE I 106    11756  12437  15206    462  -1220  -2065       C  
ATOM  12575  CG2 ILE I 106     140.243 -64.308  70.541  1.00110.96           C  
ANISOU12575  CG2 ILE I 106    12639  13439  16082    397  -1207  -1860       C  
ATOM  12576  CD1 ILE I 106     137.105 -63.642  70.897  1.00107.66           C  
ANISOU12576  CD1 ILE I 106    12281  12933  15690    488  -1202  -2129       C  
ATOM  12577  N   GLY I 107     141.890 -65.226  67.948  1.00 94.30           N  
ANISOU12577  N   GLY I 107    10442  11353  14035    361  -1175  -1722       N  
ATOM  12578  CA  GLY I 107     143.222 -65.793  68.075  1.00 94.52           C  
ANISOU12578  CA  GLY I 107    10433  11427  14052    327  -1152  -1601       C  
ATOM  12579  C   GLY I 107     143.913 -66.208  66.789  1.00 93.26           C  
ANISOU12579  C   GLY I 107    10233  11275  13925    313  -1137  -1544       C  
ATOM  12580  O   GLY I 107     143.346 -66.078  65.704  1.00 92.07           O  
ANISOU12580  O   GLY I 107    10082  11093  13808    330  -1143  -1599       O  
ATOM  12581  N   PRO I 108     145.165 -66.684  66.910  1.00 95.83           N  
ANISOU12581  N   PRO I 108    10527  11645  14239    280  -1121  -1431       N  
ATOM  12582  CA  PRO I 108     146.016 -67.146  65.804  1.00 93.92           C  
ANISOU12582  CA  PRO I 108    10244  11419  14024    261  -1104  -1359       C  
ATOM  12583  C   PRO I 108     145.587 -68.522  65.308  1.00 86.03           C  
ANISOU12583  C   PRO I 108     9177  10425  13085    300   -987  -1370       C  
ATOM  12584  O   PRO I 108     145.171 -69.363  66.113  1.00 83.44           O  
ANISOU12584  O   PRO I 108     8822  10112  12769    328   -907  -1384       O  
ATOM  12585  CB  PRO I 108     147.409 -67.200  66.432  1.00 98.96           C  
ANISOU12585  CB  PRO I 108    10875  12104  14623    216  -1122  -1240       C  
ATOM  12586  CG  PRO I 108     147.144 -67.532  67.859  1.00 99.78           C  
ANISOU12586  CG  PRO I 108    10981  12226  14706    229  -1083  -1247       C  
ATOM  12587  CD  PRO I 108     145.824 -66.868  68.217  1.00 99.81           C  
ANISOU12587  CD  PRO I 108    11032  12187  14705    260  -1112  -1366       C  
ATOM  12588  N   ARG I 109     145.697 -68.748  64.003  1.00 93.02           N  
ANISOU12588  N   ARG I 109    10036  11300  14008    302   -977  -1365       N  
ATOM  12589  CA  ARG I 109     145.133 -69.947  63.395  1.00 85.70           C  
ANISOU12589  CA  ARG I 109     9050  10371  13142    342   -873  -1392       C  
ATOM  12590  C   ARG I 109     145.874 -70.323  62.125  1.00 83.58           C  
ANISOU12590  C   ARG I 109     8744  10112  12902    327   -862  -1331       C  
ATOM  12591  O   ARG I 109     146.436 -69.463  61.458  1.00 87.42           O  
ANISOU12591  O   ARG I 109     9258  10589  13369    294   -944  -1306       O  
ATOM  12592  CB  ARG I 109     143.643 -69.732  63.087  1.00 82.27           C  
ANISOU12592  CB  ARG I 109     8635   9889  12735    387   -865  -1520       C  
ATOM  12593  CG  ARG I 109     143.365 -68.902  61.837  1.00 82.63           C  
ANISOU12593  CG  ARG I 109     8709   9895  12792    384   -933  -1567       C  
ATOM  12594  CD  ARG I 109     141.976 -68.303  61.908  1.00 79.10           C  
ANISOU12594  CD  ARG I 109     8302   9401  12350    418   -956  -1692       C  
ATOM  12595  NE  ARG I 109     141.366 -68.083  60.595  1.00 77.85           N  
ANISOU12595  NE  ARG I 109     8145   9206  12230    436   -969  -1754       N  
ATOM  12596  CZ  ARG I 109     140.111 -67.665  60.414  1.00 75.15           C  
ANISOU12596  CZ  ARG I 109     7831   8821  11903    470   -981  -1867       C  
ATOM  12597  NH1 ARG I 109     139.336 -67.417  61.463  1.00 73.46           N  
ANISOU12597  NH1 ARG I 109     7647   8597  11669    490   -982  -1929       N  
ATOM  12598  NH2 ARG I 109     139.631 -67.496  59.185  1.00 74.49           N  
ANISOU12598  NH2 ARG I 109     7746   8705  11853    485   -993  -1917       N  
ATOM  12599  N   GLU I 110     145.863 -71.603  61.782  1.00 81.85           N  
ANISOU12599  N   GLU I 110     8460   9909  12729    350   -760  -1310       N  
ATOM  12600  CA  GLU I 110     146.422 -72.060  60.518  1.00 79.39           C  
ANISOU12600  CA  GLU I 110     8108   9604  12453    342   -739  -1263       C  
ATOM  12601  C   GLU I 110     145.285 -72.636  59.703  1.00 73.17           C  
ANISOU12601  C   GLU I 110     7294   8785  11722    390   -676  -1350       C  
ATOM  12602  O   GLU I 110     144.306 -73.117  60.269  1.00 69.91           O  
ANISOU12602  O   GLU I 110     6873   8362  11328    430   -617  -1418       O  
ATOM  12603  CB  GLU I 110     147.512 -73.113  60.745  1.00 79.34           C  
ANISOU12603  CB  GLU I 110     8045   9649  12451    326   -673  -1152       C  
ATOM  12604  CG  GLU I 110     148.357 -73.431  59.526  1.00 77.36           C  
ANISOU12604  CG  GLU I 110     7758   9410  12225    306   -668  -1084       C  
ATOM  12605  CD  GLU I 110     149.399 -74.498  59.810  1.00 80.13           C  
ANISOU12605  CD  GLU I 110     8054   9812  12581    292   -599   -976       C  
ATOM  12606  OE1 GLU I 110     150.590 -74.280  59.492  1.00 80.37           O  
ANISOU12606  OE1 GLU I 110     8079   9867  12591    250   -640   -885       O  
ATOM  12607  OE2 GLU I 110     149.021 -75.556  60.354  1.00 82.44           O  
ANISOU12607  OE2 GLU I 110     8306  10120  12898    322   -505   -984       O  
ATOM  12608  N   GLN I 111     145.396 -72.601  58.382  1.00 77.50           N  
ANISOU12608  N   GLN I 111     7828   9318  12300    388   -687  -1350       N  
ATOM  12609  CA  GLN I 111     144.381 -73.244  57.552  1.00 72.02           C  
ANISOU12609  CA  GLN I 111     7103   8597  11665    434   -621  -1426       C  
ATOM  12610  C   GLN I 111     144.920 -74.475  56.839  1.00 69.41           C  
ANISOU12610  C   GLN I 111     6702   8292  11378    440   -535  -1363       C  
ATOM  12611  O   GLN I 111     145.735 -74.366  55.928  1.00 71.26           O  
ANISOU12611  O   GLN I 111     6925   8534  11617    413   -563  -1303       O  
ATOM  12612  CB  GLN I 111     143.844 -72.250  56.542  1.00 72.52           C  
ANISOU12612  CB  GLN I 111     7206   8614  11733    435   -697  -1495       C  
ATOM  12613  CG  GLN I 111     143.368 -70.994  57.205  1.00 78.37           C  
ANISOU12613  CG  GLN I 111     8018   9329  12429    427   -786  -1554       C  
ATOM  12614  CD  GLN I 111     142.669 -70.092  56.250  1.00 77.89           C  
ANISOU12614  CD  GLN I 111     7996   9222  12378    436   -851  -1635       C  
ATOM  12615  OE1 GLN I 111     141.433 -70.045  56.224  1.00 73.97           O  
ANISOU12615  OE1 GLN I 111     7512   8691  11904    475   -833  -1738       O  
ATOM  12616  NE2 GLN I 111     143.441 -69.371  55.439  1.00 82.24           N  
ANISOU12616  NE2 GLN I 111     8565   9769  12913    399   -927  -1590       N  
ATOM  12617  N   VAL I 112     144.470 -75.654  57.250  1.00 66.35           N  
ANISOU12617  N   VAL I 112     6268   7919  11024    474   -430  -1375       N  
ATOM  12618  CA  VAL I 112     144.993 -76.892  56.675  1.00 66.11           C  
ANISOU12618  CA  VAL I 112     6169   7915  11034    481   -343  -1312       C  
ATOM  12619  C   VAL I 112     143.933 -77.662  55.881  1.00 65.78           C  
ANISOU12619  C   VAL I 112     6091   7847  11054    529   -266  -1389       C  
ATOM  12620  O   VAL I 112     142.968 -78.170  56.459  1.00 65.76           O  
ANISOU12620  O   VAL I 112     6080   7835  11070    568   -205  -1455       O  
ATOM  12621  CB  VAL I 112     145.548 -77.809  57.769  1.00 66.24           C  
ANISOU12621  CB  VAL I 112     6150   7977  11040    477   -274  -1242       C  
ATOM  12622  CG1 VAL I 112     146.318 -78.934  57.154  1.00 66.02           C  
ANISOU12622  CG1 VAL I 112     6056   7981  11046    474   -201  -1161       C  
ATOM  12623  CG2 VAL I 112     146.407 -77.020  58.721  1.00 66.58           C  
ANISOU12623  CG2 VAL I 112     6234   8044  11021    434   -348  -1181       C  
ATOM  12624  N   ASN I 113     144.087 -77.761  54.564  1.00 70.36           N  
ANISOU12624  N   ASN I 113     6651   8416  11666    528   -269  -1381       N  
ATOM  12625  CA  ASN I 113     143.155 -78.604  53.823  1.00 66.23           C  
ANISOU12625  CA  ASN I 113     6086   7875  11205    573   -187  -1440       C  
ATOM  12626  C   ASN I 113     143.352 -80.043  54.247  1.00 63.65           C  
ANISOU12626  C   ASN I 113     5697   7581  10905    593    -72  -1400       C  
ATOM  12627  O   ASN I 113     144.449 -80.448  54.658  1.00 64.91           O  
ANISOU12627  O   ASN I 113     5834   7783  11045    566    -55  -1302       O  
ATOM  12628  CB  ASN I 113     143.329 -78.494  52.312  1.00 66.31           C  
ANISOU12628  CB  ASN I 113     6077   7875  11243    564   -201  -1418       C  
ATOM  12629  CG  ASN I 113     143.871 -77.161  51.891  1.00 69.62           C  
ANISOU12629  CG  ASN I 113     6553   8260  11640    544   -311  -1456       C  
ATOM  12630  OD1 ASN I 113     143.140 -76.169  51.870  1.00 71.31           O  
ANISOU12630  OD1 ASN I 113     6799   8486  11808    500   -393  -1397       O  
ATOM  12631  ND2 ASN I 113     145.164 -77.119  51.549  1.00 70.96           N  
ANISOU12631  ND2 ASN I 113     6734   8386  11840    576   -313  -1555       N  
ATOM  12632  N   PHE I 114     142.279 -80.811  54.143  1.00 59.57           N  
ANISOU12632  N   PHE I 114     5154   7046  10434    641      7  -1476       N  
ATOM  12633  CA  PHE I 114     142.287 -82.221  54.481  1.00 59.45           C  
ANISOU12633  CA  PHE I 114     5077   7059  10452    665    121  -1446       C  
ATOM  12634  C   PHE I 114     141.494 -83.001  53.457  1.00 59.10           C  
ANISOU12634  C   PHE I 114     4992   6992  10470    705    192  -1503       C  
ATOM  12635  O   PHE I 114     140.780 -82.417  52.646  1.00 58.97           O  
ANISOU12635  O   PHE I 114     4999   6936  10470    719    154  -1578       O  
ATOM  12636  CB  PHE I 114     141.713 -82.448  55.870  1.00 59.65           C  
ANISOU12636  CB  PHE I 114     5113   7092  10461    684    157  -1480       C  
ATOM  12637  CG  PHE I 114     140.326 -81.947  56.022  1.00 59.66           C  
ANISOU12637  CG  PHE I 114     5149   7049  10469    718    142  -1603       C  
ATOM  12638  CD1 PHE I 114     139.257 -82.664  55.532  1.00 59.40           C  
ANISOU12638  CD1 PHE I 114     5087   6994  10489    765    216  -1680       C  
ATOM  12639  CD2 PHE I 114     140.078 -80.741  56.650  1.00 59.93           C  
ANISOU12639  CD2 PHE I 114     5248   7065  10456    704     54  -1642       C  
ATOM  12640  CE1 PHE I 114     137.979 -82.199  55.675  1.00 59.41           C  
ANISOU12640  CE1 PHE I 114     5121   6955  10497    797    203  -1793       C  
ATOM  12641  CE2 PHE I 114     138.794 -80.271  56.801  1.00 59.93           C  
ANISOU12641  CE2 PHE I 114     5283   7026  10463    736     40  -1756       C  
ATOM  12642  CZ  PHE I 114     137.752 -81.002  56.314  1.00 59.68           C  
ANISOU12642  CZ  PHE I 114     5219   6972  10484    782    114  -1831       C  
ATOM  12643  N   GLN I 115     141.628 -84.323  53.498  1.00 59.29           N  
ANISOU12643  N   GLN I 115     4955   7043  10530    724    296  -1467       N  
ATOM  12644  CA  GLN I 115     140.731 -85.199  52.775  1.00 58.98           C  
ANISOU12644  CA  GLN I 115     4875   6984  10551    769    378  -1529       C  
ATOM  12645  C   GLN I 115     139.971 -86.038  53.786  1.00 59.02           C  
ANISOU12645  C   GLN I 115     4859   6996  10570    805    464  -1568       C  
ATOM  12646  O   GLN I 115     140.465 -86.279  54.896  1.00 59.23           O  
ANISOU12646  O   GLN I 115     4883   7055  10568    792    480  -1516       O  
ATOM  12647  CB  GLN I 115     141.466 -86.082  51.788  1.00 58.72           C  
ANISOU12647  CB  GLN I 115     4785   6972  10555    764    430  -1458       C  
ATOM  12648  CG  GLN I 115     141.685 -85.439  50.427  1.00 58.55           C  
ANISOU12648  CG  GLN I 115     4776   6928  10544    749    368  -1461       C  
ATOM  12649  CD  GLN I 115     142.195 -86.421  49.358  1.00 58.25           C  
ANISOU12649  CD  GLN I 115     4677   6906  10551    753    431  -1407       C  
ATOM  12650  OE1 GLN I 115     142.811 -87.450  49.673  1.00 58.23           O  
ANISOU12650  OE1 GLN I 115     4625   6940  10558    752    504  -1335       O  
ATOM  12651  NE2 GLN I 115     141.943 -86.099  48.086  1.00 58.04           N  
ANISOU12651  NE2 GLN I 115     4652   6849  10550    759    403  -1443       N  
ATOM  12652  N   LEU I 116     138.747 -86.421  53.405  1.00 58.47           N  
ANISOU12652  N   LEU I 116     4777   6895  10544    851    514  -1664       N  
ATOM  12653  CA  LEU I 116     137.885 -87.301  54.183  1.00 58.45           C  
ANISOU12653  CA  LEU I 116     4750   6895  10565    891    604  -1713       C  
ATOM  12654  C   LEU I 116     137.651 -88.565  53.361  1.00 58.12           C  
ANISOU12654  C   LEU I 116     4643   6855  10585    921    705  -1713       C  
ATOM  12655  O   LEU I 116     137.013 -88.495  52.295  1.00 57.88           O  
ANISOU12655  O   LEU I 116     4609   6792  10591    942    705  -1774       O  
ATOM  12656  CB  LEU I 116     136.560 -86.619  54.507  1.00 58.53           C  
ANISOU12656  CB  LEU I 116     4804   6862  10571    919    575  -1833       C  
ATOM  12657  CG  LEU I 116     136.516 -85.639  55.671  1.00 58.88           C  
ANISOU12657  CG  LEU I 116     4907   6905  10558    901    504  -1847       C  
ATOM  12658  CD1 LEU I 116     135.278 -84.841  55.560  1.00 58.88           C  
ANISOU12658  CD1 LEU I 116     4952   6859  10561    926    462  -1965       C  
ATOM  12659  CD2 LEU I 116     136.513 -86.346  57.006  1.00 59.05           C  
ANISOU12659  CD2 LEU I 116     4911   6956  10568    910    568  -1825       C  
ATOM  12660  N   LEU I 117     138.172 -89.703  53.842  1.00 61.92           N  
ANISOU12660  N   LEU I 117     5074   7375  11077    924    789  -1646       N  
ATOM  12661  CA  LEU I 117     138.075 -90.974  53.113  1.00 61.49           C  
ANISOU12661  CA  LEU I 117     4955   7328  11080    951    888  -1634       C  
ATOM  12662  C   LEU I 117     137.451 -92.131  53.927  1.00 61.54           C  
ANISOU12662  C   LEU I 117     4923   7347  11112    987    995  -1658       C  
ATOM  12663  O   LEU I 117     137.536 -92.139  55.161  1.00 62.21           O  
ANISOU12663  O   LEU I 117     5020   7451  11165    982   1001  -1642       O  
ATOM  12664  CB  LEU I 117     139.458 -91.390  52.642  1.00 62.59           C  
ANISOU12664  CB  LEU I 117     5059   7505  11217    917    893  -1516       C  
ATOM  12665  CG  LEU I 117     140.475 -90.339  52.204  1.00 63.58           C  
ANISOU12665  CG  LEU I 117     5219   7635  11304    868    789  -1456       C  
ATOM  12666  CD1 LEU I 117     141.848 -90.926  52.401  1.00 64.31           C  
ANISOU12666  CD1 LEU I 117     5276   7777  11382    836    812  -1331       C  
ATOM  12667  CD2 LEU I 117     140.288 -89.947  50.748  1.00 64.00           C  
ANISOU12667  CD2 LEU I 117     5275   7657  11384    871    753  -1488       C  
ATOM  12668  N   ASP I 118     136.851 -93.108  53.240  1.00 63.34           N  
ANISOU12668  N   ASP I 118     8033   8350   7685   1323   -690    123       N  
ATOM  12669  CA  ASP I 118     136.317 -94.303  53.901  1.00 62.63           C  
ANISOU12669  CA  ASP I 118     7993   8271   7532   1310   -784    141       C  
ATOM  12670  C   ASP I 118     137.388 -95.401  54.007  1.00 63.15           C  
ANISOU12670  C   ASP I 118     8076   8342   7575   1336   -861    101       C  
ATOM  12671  O   ASP I 118     138.557 -95.144  53.757  1.00 64.18           O  
ANISOU12671  O   ASP I 118     8176   8469   7741   1358   -839     54       O  
ATOM  12672  CB  ASP I 118     135.082 -94.826  53.163  1.00 60.86           C  
ANISOU12672  CB  ASP I 118     7816   8042   7266   1313   -805    216       C  
ATOM  12673  CG  ASP I 118     135.417 -95.496  51.825  1.00 60.16           C  
ANISOU12673  CG  ASP I 118     7753   7941   7165   1357   -824    236       C  
ATOM  12674  OD1 ASP I 118     136.508 -95.244  51.260  1.00 61.02           O  
ANISOU12674  OD1 ASP I 118     7834   8043   7309   1386   -795    198       O  
ATOM  12675  OD2 ASP I 118     134.565 -96.272  51.331  1.00 59.59           O  
ANISOU12675  OD2 ASP I 118     7728   7866   7046   1362   -867    290       O  
ATOM  12676  N   LYS I 119     137.004 -96.621  54.374  1.00 62.02           N  
ANISOU12676  N   LYS I 119     7983   8207   7374   1332   -952    120       N  
ATOM  12677  CA  LYS I 119     137.986 -97.662  54.670  1.00 64.13           C  
ANISOU12677  CA  LYS I 119     8267   8481   7617   1352  -1028     79       C  
ATOM  12678  C   LYS I 119     138.627 -98.270  53.435  1.00 65.26           C  
ANISOU12678  C   LYS I 119     8427   8613   7757   1399  -1045     83       C  
ATOM  12679  O   LYS I 119     139.564 -99.056  53.551  1.00 67.05           O  
ANISOU12679  O   LYS I 119     8663   8844   7970   1420  -1100     46       O  
ATOM  12680  CB  LYS I 119     137.364 -98.776  55.506  1.00 65.24           C  
ANISOU12680  CB  LYS I 119     8457   8635   7697   1332  -1121     97       C  
ATOM  12681  CG  LYS I 119     136.562 -99.804  54.722  1.00 65.33           C  
ANISOU12681  CG  LYS I 119     8526   8641   7655   1348  -1176    158       C  
ATOM  12682  CD  LYS I 119     135.766-100.698  55.659  1.00 67.16           C  
ANISOU12682  CD  LYS I 119     8802   8886   7831   1320  -1256    180       C  
ATOM  12683  CE  LYS I 119     134.976-101.721  54.871  1.00 68.40           C  
ANISOU12683  CE  LYS I 119     9017   9038   7935   1336  -1311    240       C  
ATOM  12684  NZ  LYS I 119     134.244-102.689  55.758  1.00 68.43           N  
ANISOU12684  NZ  LYS I 119     9065   9054   7880   1311  -1395    262       N  
ATOM  12685  N   ASN I 120     138.122 -97.932  52.256  1.00 66.56           N  
ANISOU12685  N   ASN I 120     8596   8764   7931   1416   -998    128       N  
ATOM  12686  CA  ASN I 120     138.800 -98.291  51.009  1.00 68.02           C  
ANISOU12686  CA  ASN I 120     8787   8936   8121   1462   -997    128       C  
ATOM  12687  C   ASN I 120     139.640 -97.147  50.409  1.00 67.93           C  
ANISOU12687  C   ASN I 120     8721   8915   8176   1479   -907     95       C  
ATOM  12688  O   ASN I 120     140.124 -97.253  49.285  1.00 69.30           O  
ANISOU12688  O   ASN I 120     8894   9077   8360   1516   -891    100       O  
ATOM  12689  CB  ASN I 120     137.782 -98.799  49.994  1.00 68.45           C  
ANISOU12689  CB  ASN I 120     8888   8981   8140   1475  -1011    198       C  
ATOM  12690  CG  ASN I 120     137.084-100.082  50.458  1.00 69.46           C  
ANISOU12690  CG  ASN I 120     9075   9118   8200   1464  -1109    229       C  
ATOM  12691  OD1 ASN I 120     137.163-100.467  51.631  1.00 69.15           O  
ANISOU12691  OD1 ASN I 120     9041   9092   8141   1441  -1159    203       O  
ATOM  12692  ND2 ASN I 120     136.399-100.747  49.536  1.00 71.18           N  
ANISOU12692  ND2 ASN I 120     9337   9327   8381   1482  -1136    284       N  
ATOM  12693  N   ASN I 121     139.759 -96.046  51.152  1.00 68.64           N  
ANISOU12693  N   ASN I 121     8763   9009   8308   1451   -847     66       N  
ATOM  12694  CA  ASN I 121     140.494 -94.833  50.742  1.00 68.95           C  
ANISOU12694  CA  ASN I 121     8744   9040   8412   1461   -756     33       C  
ATOM  12695  C   ASN I 121     139.925 -94.139  49.496  1.00 68.91           C  
ANISOU12695  C   ASN I 121     8732   9019   8430   1475   -684     79       C  
ATOM  12696  O   ASN I 121     140.659 -93.598  48.665  1.00 70.47           O  
ANISOU12696  O   ASN I 121     8899   9207   8669   1502   -630     62       O  
ATOM  12697  CB  ASN I 121     141.978 -95.143  50.538  1.00 71.03           C  
ANISOU12697  CB  ASN I 121     8990   9304   8695   1494   -773    -23       C  
ATOM  12698  CG  ASN I 121     142.801 -94.882  51.791  1.00 71.56           C  
ANISOU12698  CG  ASN I 121     9024   9384   8783   1474   -781    -88       C  
ATOM  12699  OD1 ASN I 121     142.254 -94.577  52.861  1.00 70.40           O  
ANISOU12699  OD1 ASN I 121     8871   9246   8631   1435   -782    -90       O  
ATOM  12700  ND2 ASN I 121     144.120 -95.007  51.666  1.00 73.70           N  
ANISOU12700  ND2 ASN I 121     9272   9654   9075   1500   -787   -140       N  
ATOM  12701  N   GLU I 122     138.598 -94.157  49.394  1.00 68.67           N  
ANISOU12701  N   GLU I 122     8731   8988   8374   1456   -683    139       N  
ATOM  12702  CA  GLU I 122     137.860 -93.281  48.483  1.00 68.45           C  
ANISOU12702  CA  GLU I 122     8690   8947   8370   1457   -605    184       C  
ATOM  12703  C   GLU I 122     137.047 -92.318  49.335  1.00 66.39           C  
ANISOU12703  C   GLU I 122     8406   8692   8127   1413   -557    193       C  
ATOM  12704  O   GLU I 122     136.715 -92.617  50.488  1.00 65.37           O  
ANISOU12704  O   GLU I 122     8288   8575   7973   1382   -601    185       O  
ATOM  12705  CB  GLU I 122     136.954 -94.074  47.532  1.00 68.87           C  
ANISOU12705  CB  GLU I 122     8796   8992   8378   1473   -640    250       C  
ATOM  12706  CG  GLU I 122     137.700 -94.752  46.383  1.00 71.34           C  
ANISOU12706  CG  GLU I 122     9125   9296   8684   1521   -663    248       C  
ATOM  12707  CD  GLU I 122     136.898 -95.874  45.750  1.00 72.57           C  
ANISOU12707  CD  GLU I 122     9343   9449   8782   1534   -727    305       C  
ATOM  12708  OE1 GLU I 122     135.652 -95.852  45.896  1.00 71.78           O  
ANISOU12708  OE1 GLU I 122     9266   9351   8658   1509   -729    357       O  
ATOM  12709  OE2 GLU I 122     137.512 -96.780  45.124  1.00 74.70           O  
ANISOU12709  OE2 GLU I 122     9638   9715   9031   1569   -775    299       O  
ATOM  12710  N   THR I 123     136.755 -91.154  48.765  1.00 64.81           N  
ANISOU12710  N   THR I 123     8173   8481   7971   1410   -467    209       N  
ATOM  12711  CA  THR I 123     136.216 -90.044  49.538  1.00 63.36           C  
ANISOU12711  CA  THR I 123     7956   8302   7817   1372   -407    207       C  
ATOM  12712  C   THR I 123     134.938 -90.461  50.244  1.00 61.70           C  
ANISOU12712  C   THR I 123     7783   8100   7559   1338   -449    251       C  
ATOM  12713  O   THR I 123     134.112 -91.172  49.671  1.00 61.69           O  
ANISOU12713  O   THR I 123     7826   8096   7516   1346   -486    305       O  
ATOM  12714  CB  THR I 123     135.952 -88.802  48.651  1.00 63.77           C  
ANISOU12714  CB  THR I 123     7973   8339   7917   1377   -305    228       C  
ATOM  12715  OG1 THR I 123     135.316 -89.201  47.424  1.00 64.83           O  
ANISOU12715  OG1 THR I 123     8140   8462   8029   1400   -307    286       O  
ATOM  12716  CG2 THR I 123     137.273 -88.058  48.348  1.00 64.84           C  
ANISOU12716  CG2 THR I 123     8057   8469   8112   1397   -249    172       C  
ATOM  12717  N   GLN I 124     134.773 -90.016  51.484  1.00 57.03           N  
ANISOU12717  N   GLN I 124     7173   7521   6976   1302   -444    227       N  
ATOM  12718  CA  GLN I 124     133.543 -90.310  52.162  1.00 56.20           C  
ANISOU12718  CA  GLN I 124     7100   7425   6830   1269   -477    269       C  
ATOM  12719  C   GLN I 124     132.619 -89.193  51.772  1.00 55.81           C  
ANISOU12719  C   GLN I 124     7030   7367   6808   1253   -393    309       C  
ATOM  12720  O   GLN I 124     132.624 -88.133  52.372  1.00 56.64           O  
ANISOU12720  O   GLN I 124     7094   7474   6952   1229   -333    287       O  
ATOM  12721  CB  GLN I 124     133.758 -90.340  53.668  1.00 57.14           C  
ANISOU12721  CB  GLN I 124     7207   7559   6943   1236   -510    226       C  
ATOM  12722  CG  GLN I 124     132.491 -90.592  54.447  1.00 56.35           C  
ANISOU12722  CG  GLN I 124     7138   7471   6803   1200   -542    267       C  
ATOM  12723  CD  GLN I 124     132.086 -92.065  54.431  1.00 55.22           C  
ANISOU12723  CD  GLN I 124     7055   7333   6593   1208   -642    298       C  
ATOM  12724  OE1 GLN I 124     132.491 -92.834  55.312  1.00 55.58           O  
ANISOU12724  OE1 GLN I 124     7116   7391   6611   1201   -712    267       O  
ATOM  12725  NE2 GLN I 124     131.300 -92.470  53.425  1.00 53.87           N  
ANISOU12725  NE2 GLN I 124     6919   7154   6396   1223   -649    358       N  
ATOM  12726  N   TYR I 125     131.744 -89.448  50.822  1.00 56.71           N  
ANISOU12726  N   TYR I 125     7175   7473   6899   1264   -391    370       N  
ATOM  12727  CA  TYR I 125     131.035 -88.327  50.205  1.00 56.50           C  
ANISOU12727  CA  TYR I 125     7125   7436   6906   1257   -302    406       C  
ATOM  12728  C   TYR I 125     130.039 -87.630  51.129  1.00 55.14           C  
ANISOU12728  C   TYR I 125     6943   7272   6736   1214   -272    425       C  
ATOM  12729  O   TYR I 125     129.801 -86.455  50.975  1.00 55.05           O  
ANISOU12729  O   TYR I 125     6896   7254   6767   1203   -189    429       O  
ATOM  12730  CB  TYR I 125     130.301 -88.781  48.954  1.00 57.27           C  
ANISOU12730  CB  TYR I 125     7259   7523   6978   1279   -307    470       C  
ATOM  12731  CG  TYR I 125     131.176 -89.007  47.743  1.00 59.04           C  
ANISOU12731  CG  TYR I 125     7480   7734   7217   1324   -299    460       C  
ATOM  12732  CD1 TYR I 125     131.564 -87.939  46.946  1.00 59.71           C  
ANISOU12732  CD1 TYR I 125     7523   7806   7358   1339   -210    452       C  
ATOM  12733  CD2 TYR I 125     131.578 -90.289  47.370  1.00 60.45           C  
ANISOU12733  CD2 TYR I 125     7699   7914   7355   1351   -379    460       C  
ATOM  12734  CE1 TYR I 125     132.341 -88.135  45.823  1.00 61.70           C  
ANISOU12734  CE1 TYR I 125     7773   8047   7624   1380   -201    444       C  
ATOM  12735  CE2 TYR I 125     132.341 -90.488  46.249  1.00 62.35           C  
ANISOU12735  CE2 TYR I 125     7938   8143   7609   1393   -370    453       C  
ATOM  12736  CZ  TYR I 125     132.722 -89.406  45.481  1.00 62.97           C  
ANISOU12736  CZ  TYR I 125     7973   8208   7743   1407   -281    444       C  
ATOM  12737  OH  TYR I 125     133.492 -89.594  44.362  1.00 65.29           O  
ANISOU12737  OH  TYR I 125     8264   8492   8051   1448   -271    436       O  
ATOM  12738  N   TYR I 126     129.444 -88.330  52.083  1.00 51.97           N  
ANISOU12738  N   TYR I 126     6574   6884   6289   1188   -339    436       N  
ATOM  12739  CA  TYR I 126     128.566 -87.630  52.995  1.00 52.00           C  
ANISOU12739  CA  TYR I 126     6565   6895   6296   1147   -309    450       C  
ATOM  12740  C   TYR I 126     129.351 -86.699  53.890  1.00 53.65           C  
ANISOU12740  C   TYR I 126     6723   7109   6554   1130   -263    387       C  
ATOM  12741  O   TYR I 126     128.965 -85.545  54.068  1.00 54.01           O  
ANISOU12741  O   TYR I 126     6734   7151   6635   1110   -188    390       O  
ATOM  12742  CB  TYR I 126     127.741 -88.571  53.858  1.00 51.17           C  
ANISOU12742  CB  TYR I 126     6505   6806   6132   1122   -389    476       C  
ATOM  12743  CG  TYR I 126     126.765 -87.775  54.699  1.00 51.18           C  
ANISOU12743  CG  TYR I 126     6492   6814   6139   1081   -351    494       C  
ATOM  12744  CD1 TYR I 126     125.605 -87.215  54.134  1.00 50.17           C  
ANISOU12744  CD1 TYR I 126     6370   6680   6013   1072   -301    555       C  
ATOM  12745  CD2 TYR I 126     127.016 -87.548  56.041  1.00 52.21           C  
ANISOU12745  CD2 TYR I 126     6604   6958   6275   1052   -362    452       C  
ATOM  12746  CE1 TYR I 126     124.750 -86.480  54.888  1.00 50.21           C  
ANISOU12746  CE1 TYR I 126     6362   6692   6025   1036   -264    571       C  
ATOM  12747  CE2 TYR I 126     126.148 -86.825  56.799  1.00 52.24           C  
ANISOU12747  CE2 TYR I 126     6595   6968   6285   1016   -327    468       C  
ATOM  12748  CZ  TYR I 126     125.027 -86.290  56.227  1.00 51.25           C  
ANISOU12748  CZ  TYR I 126     6476   6837   6161   1008   -278    527       C  
ATOM  12749  OH  TYR I 126     124.195 -85.553  57.038  1.00 51.37           O  
ANISOU12749  OH  TYR I 126     6477   6859   6182    971   -243    541       O  
ATOM  12750  N   HIS I 127     130.446 -87.190  54.455  1.00 51.81           N  
ANISOU12750  N   HIS I 127     6482   6882   6320   1138   -309    329       N  
ATOM  12751  CA  HIS I 127     131.285 -86.344  55.292  1.00 52.01           C  
ANISOU12751  CA  HIS I 127     6458   6911   6391   1123   -269    266       C  
ATOM  12752  C   HIS I 127     131.983 -85.261  54.464  1.00 52.11           C  
ANISOU12752  C   HIS I 127     6424   6910   6467   1143   -180    245       C  
ATOM  12753  O   HIS I 127     132.193 -84.132  54.928  1.00 52.60           O  
ANISOU12753  O   HIS I 127     6441   6971   6574   1125   -113    216       O  
ATOM  12754  CB  HIS I 127     132.314 -87.180  56.042  1.00 52.17           C  
ANISOU12754  CB  HIS I 127     6485   6943   6395   1128   -342    211       C  
ATOM  12755  CG  HIS I 127     131.735 -87.999  57.150  1.00 52.11           C  
ANISOU12755  CG  HIS I 127     6511   6951   6336   1101   -419    219       C  
ATOM  12756  ND1 HIS I 127     130.981 -89.126  56.921  1.00 51.94           N  
ANISOU12756  ND1 HIS I 127     6545   6933   6256   1105   -491    268       N  
ATOM  12757  CD2 HIS I 127     131.810 -87.861  58.495  1.00 52.19           C  
ANISOU12757  CD2 HIS I 127     6510   6975   6345   1069   -437    185       C  
ATOM  12758  CE1 HIS I 127     130.611 -89.647  58.078  1.00 51.92           C  
ANISOU12758  CE1 HIS I 127     6562   6947   6218   1077   -549    263       C  
ATOM  12759  NE2 HIS I 127     131.106 -88.901  59.047  1.00 52.07           N  
ANISOU12759  NE2 HIS I 127     6542   6972   6271   1055   -518    213       N  
ATOM  12760  N   PHE I 128     132.334 -85.620  53.235  1.00 49.14           N  
ANISOU12760  N   PHE I 128     6059   6522   6091   1181   -180    260       N  
ATOM  12761  CA  PHE I 128     133.009 -84.701  52.330  1.00 49.82           C  
ANISOU12761  CA  PHE I 128     6103   6593   6232   1203   -100    242       C  
ATOM  12762  C   PHE I 128     132.216 -83.444  52.203  1.00 49.78           C  
ANISOU12762  C   PHE I 128     6071   6582   6262   1183    -11    270       C  
ATOM  12763  O   PHE I 128     132.768 -82.359  52.255  1.00 50.96           O  
ANISOU12763  O   PHE I 128     6172   6726   6466   1180     60    235       O  
ATOM  12764  CB  PHE I 128     133.197 -85.325  50.950  1.00 50.30           C  
ANISOU12764  CB  PHE I 128     6188   6643   6281   1245   -114    270       C  
ATOM  12765  CG  PHE I 128     133.558 -84.336  49.877  1.00 51.97           C  
ANISOU12765  CG  PHE I 128     6362   6838   6545   1266    -26    270       C  
ATOM  12766  CD1 PHE I 128     132.598 -83.825  49.027  1.00 51.05           C  
ANISOU12766  CD1 PHE I 128     6250   6711   6434   1267     27    327       C  
ATOM  12767  CD2 PHE I 128     134.861 -83.938  49.705  1.00 54.91           C  
ANISOU12767  CD2 PHE I 128     6696   7207   6962   1286      3    214       C  
ATOM  12768  CE1 PHE I 128     132.922 -82.935  48.035  1.00 53.09           C  
ANISOU12768  CE1 PHE I 128     6475   6955   6741   1287    106    328       C  
ATOM  12769  CE2 PHE I 128     135.199 -83.044  48.710  1.00 57.01           C  
ANISOU12769  CE2 PHE I 128     6927   7458   7276   1306     83    214       C  
ATOM  12770  CZ  PHE I 128     134.220 -82.548  47.867  1.00 56.13           C  
ANISOU12770  CZ  PHE I 128     6821   7336   7169   1307    135    272       C  
ATOM  12771  N   PHE I 129     130.906 -83.652  52.045  1.00 49.62           N  
ANISOU12771  N   PHE I 129     6084   6563   6208   1169    -21    333       N  
ATOM  12772  CA  PHE I 129     129.883 -82.658  51.790  1.00 49.49           C  
ANISOU12772  CA  PHE I 129     6054   6540   6211   1151     53    376       C  
ATOM  12773  C   PHE I 129     129.489 -81.907  53.034  1.00 49.53           C  
ANISOU12773  C   PHE I 129     6035   6554   6229   1110     79    359       C  
ATOM  12774  O   PHE I 129     129.041 -80.786  52.969  1.00 49.50           O  
ANISOU12774  O   PHE I 129     6003   6545   6261   1095    157    371       O  
ATOM  12775  CB  PHE I 129     128.671 -83.347  51.221  1.00 49.26           C  
ANISOU12775  CB  PHE I 129     6074   6509   6132   1152     18    448       C  
ATOM  12776  CG  PHE I 129     128.789 -83.683  49.785  1.00 49.19           C  
ANISOU12776  CG  PHE I 129     6081   6487   6121   1191     24    478       C  
ATOM  12777  CD1 PHE I 129     129.458 -82.862  48.929  1.00 49.28           C  
ANISOU12777  CD1 PHE I 129     6055   6485   6185   1213     97    460       C  
ATOM  12778  CD2 PHE I 129     128.175 -84.810  49.275  1.00 49.03           C  
ANISOU12778  CD2 PHE I 129     6114   6468   6047   1203    -42    526       C  
ATOM  12779  CE1 PHE I 129     129.541 -83.178  47.586  1.00 49.22           C  
ANISOU12779  CE1 PHE I 129     6062   6465   6174   1249    102    489       C  
ATOM  12780  CE2 PHE I 129     128.257 -85.134  47.929  1.00 48.97           C  
ANISOU12780  CE2 PHE I 129     6122   6448   6036   1239    -37    555       C  
ATOM  12781  CZ  PHE I 129     128.943 -84.324  47.087  1.00 49.06           C  
ANISOU12781  CZ  PHE I 129     6096   6446   6099   1262     34    536       C  
ATOM  12782  N   SER I 130     129.624 -82.549  54.177  1.00 51.61           N  
ANISOU12782  N   SER I 130     6315   6833   6463   1091     12    333       N  
ATOM  12783  CA  SER I 130     129.181 -81.955  55.418  1.00 51.67           C  
ANISOU12783  CA  SER I 130     6305   6850   6476   1050     28    320       C  
ATOM  12784  C   SER I 130     130.222 -81.145  56.164  1.00 53.02           C  
ANISOU12784  C   SER I 130     6426   7024   6697   1041     67    250       C  
ATOM  12785  O   SER I 130     129.858 -80.418  57.075  1.00 53.60           O  
ANISOU12785  O   SER I 130     6478   7102   6784   1008     98    240       O  
ATOM  12786  CB  SER I 130     128.666 -83.049  56.356  1.00 51.17           C  
ANISOU12786  CB  SER I 130     6285   6804   6353   1031    -64    332       C  
ATOM  12787  OG  SER I 130     127.695 -83.861  55.726  1.00 50.35           O  
ANISOU12787  OG  SER I 130     6230   6700   6201   1038   -105    396       O  
ATOM  12788  N   ILE I 131     131.505 -81.261  55.808  1.00 52.17           N  
ANISOU12788  N   ILE I 131     6299   6911   6613   1068     64    202       N  
ATOM  12789  CA  ILE I 131     132.570 -80.561  56.564  1.00 53.89           C  
ANISOU12789  CA  ILE I 131     6469   7131   6876   1059     95    132       C  
ATOM  12790  C   ILE I 131     133.450 -79.649  55.731  1.00 54.78           C  
ANISOU12790  C   ILE I 131     6537   7229   7048   1082    172    105       C  
ATOM  12791  O   ILE I 131     134.068 -80.097  54.768  1.00 54.48           O  
ANISOU12791  O   ILE I 131     6505   7184   7012   1118    160    103       O  
ATOM  12792  CB  ILE I 131     133.526 -81.517  57.272  1.00 54.47           C  
ANISOU12792  CB  ILE I 131     6554   7216   6927   1065     15     83       C  
ATOM  12793  CG1 ILE I 131     132.769 -82.650  57.961  1.00 53.44           C  
ANISOU12793  CG1 ILE I 131     6473   7099   6731   1048    -75    110       C  
ATOM  12794  CG2 ILE I 131     134.319 -80.753  58.282  1.00 56.14           C  
ANISOU12794  CG2 ILE I 131     6720   7433   7178   1045     44     19       C  
ATOM  12795  CD1 ILE I 131     133.574 -83.357  59.023  1.00 54.12           C  
ANISOU12795  CD1 ILE I 131     6563   7200   6799   1041   -145     57       C  
ATOM  12796  N   LYS I 132     133.535 -78.386  56.151  1.00 55.80           N  
ANISOU12796  N   LYS I 132     6620   7355   7226   1062    248     81       N  
ATOM  12797  CA  LYS I 132     134.241 -77.333  55.422  1.00 57.35           C  
ANISOU12797  CA  LYS I 132     6770   7537   7484   1079    332     58       C  
ATOM  12798  C   LYS I 132     135.731 -77.556  55.276  1.00 59.26           C  
ANISOU12798  C   LYS I 132     6990   7778   7748   1105    317     -2       C  
ATOM  12799  O   LYS I 132     136.435 -77.780  56.258  1.00 60.13           O  
ANISOU12799  O   LYS I 132     7091   7899   7858   1093    281    -53       O  
ATOM  12800  CB  LYS I 132     134.022 -75.993  56.112  1.00 59.85           C  
ANISOU12800  CB  LYS I 132     7045   7853   7844   1047    408     41       C  
ATOM  12801  CG  LYS I 132     134.886 -74.847  55.595  1.00 61.65           C  
ANISOU12801  CG  LYS I 132     7219   8068   8139   1060    494      5       C  
ATOM  12802  CD  LYS I 132     134.803 -73.630  56.527  1.00 61.88           C  
ANISOU12802  CD  LYS I 132     7207   8097   8207   1025    556    -23       C  
ATOM  12803  CE  LYS I 132     135.985 -72.684  56.293  1.00 62.66           C  
ANISOU12803  CE  LYS I 132     7252   8187   8369   1037    621    -76       C  
ATOM  12804  NZ  LYS I 132     136.051 -71.548  57.275  1.00 63.10           N  
ANISOU12804  NZ  LYS I 132     7268   8244   8464   1004    676   -111       N  
ATOM  12805  N   ASP I 133     136.190 -77.477  54.031  1.00 58.19           N  
ANISOU12805  N   ASP I 133     6847   7629   7634   1140    347      6       N  
ATOM  12806  CA  ASP I 133     137.594 -77.644  53.657  1.00 60.32           C  
ANISOU12806  CA  ASP I 133     7095   7896   7929   1169    342    -44       C  
ATOM  12807  C   ASP I 133     138.164 -76.377  53.025  1.00 64.27           C  
ANISOU12807  C   ASP I 133     7543   8382   8495   1180    438    -65       C  
ATOM  12808  O   ASP I 133     137.685 -75.972  51.961  1.00 64.48           O  
ANISOU12808  O   ASP I 133     7569   8396   8535   1194    488    -23       O  
ATOM  12809  CB  ASP I 133     137.728 -78.790  52.676  1.00 58.14           C  
ANISOU12809  CB  ASP I 133     6858   7616   7616   1206    285    -19       C  
ATOM  12810  CG  ASP I 133     139.130 -78.980  52.210  1.00 60.98           C  
ANISOU12810  CG  ASP I 133     7197   7972   8000   1239    280    -66       C  
ATOM  12811  OD1 ASP I 133     139.999 -79.190  53.076  1.00 62.76           O  
ANISOU12811  OD1 ASP I 133     7409   8208   8230   1233    247   -122       O  
ATOM  12812  OD2 ASP I 133     139.365 -78.907  50.988  1.00 61.73           O  
ANISOU12812  OD2 ASP I 133     7289   8055   8110   1271    309    -49       O  
ATOM  12813  N   PRO I 134     139.212 -75.763  53.614  1.00 59.67           N  
ANISOU12813  N   PRO I 134     6917   7801   7955   1174    465   -128       N  
ATOM  12814  CA  PRO I 134     140.150 -76.140  54.673  1.00 60.71           C  
ANISOU12814  CA  PRO I 134     7038   7945   8084   1165    416   -189       C  
ATOM  12815  C   PRO I 134     139.667 -75.988  56.093  1.00 61.10           C  
ANISOU12815  C   PRO I 134     7089   8008   8120   1123    398   -202       C  
ATOM  12816  O   PRO I 134     138.599 -75.459  56.306  1.00 60.70           O  
ANISOU12816  O   PRO I 134     7042   7956   8066   1098    431   -166       O  
ATOM  12817  CB  PRO I 134     141.304 -75.186  54.437  1.00 62.20           C  
ANISOU12817  CB  PRO I 134     7173   8126   8336   1176    482   -240       C  
ATOM  12818  CG  PRO I 134     140.661 -74.017  53.900  1.00 62.26           C  
ANISOU12818  CG  PRO I 134     7156   8121   8379   1168    572   -210       C  
ATOM  12819  CD  PRO I 134     139.650 -74.530  52.959  1.00 60.61           C  
ANISOU12819  CD  PRO I 134     6988   7906   8136   1182    560   -141       C  
ATOM  12820  N   ALA I 135     140.485 -76.408  57.050  1.00 60.69           N  
ANISOU12820  N   ALA I 135     7031   7967   8061   1115    349   -255       N  
ATOM  12821  CA  ALA I 135     140.078 -76.473  58.440  1.00 61.00           C  
ANISOU12821  CA  ALA I 135     7077   8021   8081   1077    317   -269       C  
ATOM  12822  C   ALA I 135     140.874 -75.511  59.286  1.00 62.77           C  
ANISOU12822  C   ALA I 135     7250   8246   8352   1058    361   -330       C  
ATOM  12823  O   ALA I 135     142.104 -75.516  59.259  1.00 63.82           O  
ANISOU12823  O   ALA I 135     7357   8379   8511   1074    359   -382       O  
ATOM  12824  CB  ALA I 135     140.239 -77.868  58.967  1.00 60.54           C  
ANISOU12824  CB  ALA I 135     7059   7976   7966   1081    213   -277       C  
ATOM  12825  N   ASP I 136     140.175 -74.682  60.045  1.00 62.90           N  
ANISOU12825  N   ASP I 136     7252   8265   8382   1022    402   -325       N  
ATOM  12826  CA  ASP I 136     140.852 -73.734  60.909  1.00 68.07           C  
ANISOU12826  CA  ASP I 136     7860   8921   9081   1001    445   -382       C  
ATOM  12827  C   ASP I 136     141.483 -74.513  62.054  1.00 69.11           C  
ANISOU12827  C   ASP I 136     8001   9069   9188    989    368   -428       C  
ATOM  12828  O   ASP I 136     140.807 -75.295  62.710  1.00 66.37           O  
ANISOU12828  O   ASP I 136     7691   8734   8791    973    305   -408       O  
ATOM  12829  CB  ASP I 136     139.878 -72.657  61.432  1.00 69.43           C  
ANISOU12829  CB  ASP I 136     8017   9092   9272    965    508   -362       C  
ATOM  12830  CG  ASP I 136     139.240 -71.812  60.310  1.00 69.41           C  
ANISOU12830  CG  ASP I 136     8003   9072   9297    975    589   -316       C  
ATOM  12831  OD1 ASP I 136     139.381 -72.153  59.116  1.00 69.66           O  
ANISOU12831  OD1 ASP I 136     8045   9094   9327   1008    590   -291       O  
ATOM  12832  OD2 ASP I 136     138.572 -70.806  60.625  1.00 69.47           O  
ANISOU12832  OD2 ASP I 136     7991   9075   9328    949    650   -303       O  
ATOM  12833  N   VAL I 137     142.782 -74.323  62.264  1.00 70.82           N  
ANISOU12833  N   VAL I 137     8184   9287   9438    999    374   -489       N  
ATOM  12834  CA  VAL I 137     143.477 -74.928  63.390  1.00 71.62           C  
ANISOU12834  CA  VAL I 137     8287   9403   9521    987    309   -539       C  
ATOM  12835  C   VAL I 137     143.997 -73.863  64.331  1.00 73.33           C  
ANISOU12835  C   VAL I 137     8456   9622   9783    959    358   -592       C  
ATOM  12836  O   VAL I 137     144.862 -73.077  63.968  1.00 74.48           O  
ANISOU12836  O   VAL I 137     8560   9759   9980    970    415   -626       O  
ATOM  12837  CB  VAL I 137     144.653 -75.764  62.947  1.00 71.86           C  
ANISOU12837  CB  VAL I 137     8321   9435   9546   1021    260   -571       C  
ATOM  12838  CG1 VAL I 137     145.137 -76.612  64.105  1.00 72.42           C  
ANISOU12838  CG1 VAL I 137     8406   9524   9586   1009    179   -611       C  
ATOM  12839  CG2 VAL I 137     144.270 -76.602  61.755  1.00 70.28           C  
ANISOU12839  CG2 VAL I 137     8160   9230   9315   1054    231   -521       C  
ATOM  12840  N   TYR I 138     143.489 -73.847  65.553  1.00 77.16           N  
ANISOU12840  N   TYR I 138     8950  10119  10250    924    335   -599       N  
ATOM  12841  CA  TYR I 138     143.785 -72.757  66.465  1.00 83.20           C  
ANISOU12841  CA  TYR I 138     9672  10885  11057    894    386   -642       C  
ATOM  12842  C   TYR I 138     144.916 -73.105  67.393  1.00 87.33           C  
ANISOU12842  C   TYR I 138    10179  11419  11582    889    341   -708       C  
ATOM  12843  O   TYR I 138     144.998 -74.220  67.883  1.00 85.14           O  
ANISOU12843  O   TYR I 138     9934  11155  11259    890    258   -713       O  
ATOM  12844  CB  TYR I 138     142.530 -72.370  67.246  1.00 82.79           C  
ANISOU12844  CB  TYR I 138     9632  10838  10987    857    399   -611       C  
ATOM  12845  CG  TYR I 138     141.616 -71.521  66.397  1.00 80.93           C  
ANISOU12845  CG  TYR I 138     9391  10588  10772    857    475   -560       C  
ATOM  12846  CD1 TYR I 138     140.915 -72.078  65.339  1.00 75.00           C  
ANISOU12846  CD1 TYR I 138     8674   9830   9993    880    462   -501       C  
ATOM  12847  CD2 TYR I 138     141.498 -70.157  66.613  1.00 85.54           C  
ANISOU12847  CD2 TYR I 138     9934  11162  11404    837    561   -572       C  
ATOM  12848  CE1 TYR I 138     140.101 -71.318  64.548  1.00 73.55           C  
ANISOU12848  CE1 TYR I 138     8485   9634   9828    881    531   -455       C  
ATOM  12849  CE2 TYR I 138     140.690 -69.387  65.820  1.00 84.11           C  
ANISOU12849  CE2 TYR I 138     9747  10968  11242    839    630   -526       C  
ATOM  12850  CZ  TYR I 138     139.993 -69.975  64.787  1.00 78.03           C  
ANISOU12850  CZ  TYR I 138     9011  10193  10442    861    615   -467       C  
ATOM  12851  OH  TYR I 138     139.177 -69.219  63.981  1.00 76.76           O  
ANISOU12851  OH  TYR I 138     8846  10020  10301    862    684   -421       O  
ATOM  12852  N   TYR I 139     145.801 -72.139  67.611  1.00 79.55           N  
ANISOU12852  N   TYR I 139     9145  10429  10651    884    397   -758       N  
ATOM  12853  CA  TYR I 139     147.004 -72.345  68.415  1.00 84.44           C  
ANISOU12853  CA  TYR I 139     9743  11058  11281    881    364   -825       C  
ATOM  12854  C   TYR I 139     146.719 -72.122  69.895  1.00 87.87           C  
ANISOU12854  C   TYR I 139    10174  11505  11707    840    348   -849       C  
ATOM  12855  O   TYR I 139     145.943 -71.245  70.257  1.00 89.21           O  
ANISOU12855  O   TYR I 139    10333  11672  11892    813    400   -833       O  
ATOM  12856  CB  TYR I 139     148.130 -71.418  67.931  1.00 90.43           C  
ANISOU12856  CB  TYR I 139    10451  11806  12103    896    431   -868       C  
ATOM  12857  CG  TYR I 139     148.668 -71.783  66.562  1.00 88.38           C  
ANISOU12857  CG  TYR I 139    10193  11536  11850    939    435   -855       C  
ATOM  12858  CD1 TYR I 139     148.926 -73.107  66.234  1.00 83.50           C  
ANISOU12858  CD1 TYR I 139     9612  10926  11190    965    355   -846       C  
ATOM  12859  CD2 TYR I 139     148.899 -70.812  65.594  1.00 91.90           C  
ANISOU12859  CD2 TYR I 139    10605  11966  12347    955    518   -850       C  
ATOM  12860  CE1 TYR I 139     149.409 -73.458  64.982  1.00 82.15           C  
ANISOU12860  CE1 TYR I 139     9444  10745  11023   1006    357   -834       C  
ATOM  12861  CE2 TYR I 139     149.387 -71.149  64.336  1.00 90.65           C  
ANISOU12861  CE2 TYR I 139    10450  11799  12195    995    521   -838       C  
ATOM  12862  CZ  TYR I 139     149.641 -72.476  64.035  1.00 85.78           C  
ANISOU12862  CZ  TYR I 139     9869  11189  11533   1020    440   -830       C  
ATOM  12863  OH  TYR I 139     150.123 -72.837  62.790  1.00 85.00           O  
ANISOU12863  OH  TYR I 139     9775  11083  11440   1061    442   -817       O  
ATOM  12864  N   THR I 140     147.331 -72.936  70.746  1.00 89.18           N  
ANISOU12864  N   THR I 140    10351  11686  11848    836    275   -887       N  
ATOM  12865  CA  THR I 140     147.164 -72.803  72.190  1.00 93.81           C  
ANISOU12865  CA  THR I 140    10933  12285  12424    798    254   -915       C  
ATOM  12866  C   THR I 140     148.486 -72.923  72.938  1.00 99.68           C  
ANISOU12866  C   THR I 140    11651  13038  13185    796    226   -985       C  
ATOM  12867  O   THR I 140     149.556 -72.979  72.329  1.00100.04           O  
ANISOU12867  O   THR I 140    11677  13078  13255    824    232  -1015       O  
ATOM  12868  CB  THR I 140     146.217 -73.865  72.759  1.00 89.57           C  
ANISOU12868  CB  THR I 140    10448  11762  11822    785    175   -879       C  
ATOM  12869  OG1 THR I 140     146.801 -75.167  72.593  1.00 86.23           O  
ANISOU12869  OG1 THR I 140    10054  11348  11363    809     92   -888       O  
ATOM  12870  CG2 THR I 140     144.872 -73.804  72.071  1.00 84.11           C  
ANISOU12870  CG2 THR I 140     9784  11063  11110    785    198   -808       C  
ATOM  12871  N   LYS I 141     148.391 -72.962  74.266  1.00 97.47           N  
ANISOU12871  N   LYS I 141    11372  12771  12891    764    196  -1012       N  
ATOM  12872  CA  LYS I 141     149.550 -73.195  75.120  1.00103.33           C  
ANISOU12872  CA  LYS I 141    12094  13524  13641    759    159  -1077       C  
ATOM  12873  C   LYS I 141     150.065 -74.621  74.966  1.00 99.75           C  
ANISOU12873  C   LYS I 141    11675  13081  13145    784     68  -1082       C  
ATOM  12874  O   LYS I 141     151.274 -74.852  74.866  1.00103.05           O  
ANISOU12874  O   LYS I 141    12074  13501  13580    803     51  -1127       O  
ATOM  12875  CB  LYS I 141     149.206 -72.931  76.592  1.00109.21           C  
ANISOU12875  CB  LYS I 141    12836  14282  14377    717    146  -1100       C  
ATOM  12876  CG  LYS I 141     148.657 -71.541  76.888  1.00116.46           C  
ANISOU12876  CG  LYS I 141    13724  15191  15334    688    232  -1097       C  
ATOM  12877  CD  LYS I 141     149.723 -70.473  76.706  1.00123.46           C  
ANISOU12877  CD  LYS I 141    14556  16068  16286    693    302  -1146       C  
ATOM  12878  CE  LYS I 141     150.954 -70.770  77.551  1.00124.23           C  
ANISOU12878  CE  LYS I 141    14634  16176  16390    689    260  -1213       C  
ATOM  12879  NZ  LYS I 141     151.974 -69.687  77.444  1.00124.94           N  
ANISOU12879  NZ  LYS I 141    14671  16257  16545    690    329  -1262       N  
ATOM  12880  N   LYS I 142     149.145 -75.580  74.936  1.00102.94           N  
ANISOU12880  N   LYS I 142    12128  13492  13494    785      9  -1035       N  
ATOM  12881  CA  LYS I 142     149.541 -76.985  75.022  1.00100.11           C  
ANISOU12881  CA  LYS I 142    11805  13145  13089    803    -86  -1041       C  
ATOM  12882  C   LYS I 142     149.517 -77.728  73.671  1.00 93.35           C  
ANISOU12882  C   LYS I 142    10975  12281  12214    843   -106  -1002       C  
ATOM  12883  O   LYS I 142     150.579 -77.995  73.105  1.00 93.94           O  
ANISOU12883  O   LYS I 142    11037  12352  12304    873   -114  -1030       O  
ATOM  12884  CB  LYS I 142     148.666 -77.684  76.063  1.00 99.37           C  
ANISOU12884  CB  LYS I 142    11748  13067  12942    775   -151  -1022       C  
ATOM  12885  CG  LYS I 142     148.687 -76.949  77.404  1.00106.59           C  
ANISOU12885  CG  LYS I 142    12637  13990  13874    735   -131  -1061       C  
ATOM  12886  CD  LYS I 142     148.214 -77.823  78.550  1.00106.33           C  
ANISOU12886  CD  LYS I 142    12638  13975  13788    711   -211  -1059       C  
ATOM  12887  CE  LYS I 142     148.341 -77.098  79.882  1.00114.02           C  
ANISOU12887  CE  LYS I 142    13584  14957  14782    673   -192  -1102       C  
ATOM  12888  NZ  LYS I 142     149.730 -76.625  80.131  1.00119.72           N  
ANISOU12888  NZ  LYS I 142    14261  15678  15548    678   -171  -1169       N  
ATOM  12889  N   LYS I 143     148.338 -78.057  73.145  1.00 94.11           N  
ANISOU12889  N   LYS I 143    11108  12373  12277    846   -113   -938       N  
ATOM  12890  CA  LYS I 143     148.273 -78.626  71.796  1.00 87.93           C  
ANISOU12890  CA  LYS I 143    10349  11581  11481    884   -122   -900       C  
ATOM  12891  C   LYS I 143     147.352 -77.792  70.901  1.00 84.47           C  
ANISOU12891  C   LYS I 143     9905  11127  11063    885    -46   -849       C  
ATOM  12892  O   LYS I 143     146.447 -77.113  71.392  1.00 85.23           O  
ANISOU12892  O   LYS I 143     9998  11223  11162    855    -10   -828       O  
ATOM  12893  CB  LYS I 143     147.798 -80.078  71.828  1.00 83.73           C  
ANISOU12893  CB  LYS I 143     9872  11059  10882    893   -217   -868       C  
ATOM  12894  CG  LYS I 143     148.365 -80.922  72.961  1.00 87.48           C  
ANISOU12894  CG  LYS I 143    10359  11552  11328    882   -297   -910       C  
ATOM  12895  CD  LYS I 143     148.024 -82.400  72.773  1.00 83.70           C  
ANISOU12895  CD  LYS I 143     9936  11081  10787    898   -390   -878       C  
ATOM  12896  CE  LYS I 143     148.202 -83.191  74.059  1.00 87.82           C  
ANISOU12896  CE  LYS I 143    10475  11621  11272    878   -469   -908       C  
ATOM  12897  NZ  LYS I 143     148.158 -84.656  73.805  1.00 84.85           N  
ANISOU12897  NZ  LYS I 143    10148  11252  10840    899   -560   -887       N  
ATOM  12898  N   ALA I 144     147.600 -77.839  69.591  1.00 89.48           N  
ANISOU12898  N   ALA I 144    10216  11308  12473    135    813  -1633       N  
ATOM  12899  CA  ALA I 144     146.790 -77.105  68.621  1.00 86.42           C  
ANISOU12899  CA  ALA I 144     9849  10897  12089    139    869  -1607       C  
ATOM  12900  C   ALA I 144     145.407 -77.700  68.586  1.00 80.98           C  
ANISOU12900  C   ALA I 144     9171  10193  11403    171    860  -1541       C  
ATOM  12901  O   ALA I 144     145.268 -78.916  68.588  1.00 77.24           O  
ANISOU12901  O   ALA I 144     8673   9728  10945    193    805  -1523       O  
ATOM  12902  CB  ALA I 144     147.409 -77.162  67.247  1.00 84.29           C  
ANISOU12902  CB  ALA I 144     9551  10631  11843    135    872  -1636       C  
ATOM  12903  N   GLU I 145     144.377 -76.864  68.539  1.00 82.14           N  
ANISOU12903  N   GLU I 145     9354  10317  11537    173    913  -1505       N  
ATOM  12904  CA  GLU I 145     143.009 -77.368  68.524  1.00 77.26           C  
ANISOU12904  CA  GLU I 145     8750   9684  10922    203    908  -1441       C  
ATOM  12905  C   GLU I 145     142.381 -77.183  67.159  1.00 72.25           C  
ANISOU12905  C   GLU I 145     8115   9032  10304    215    940  -1418       C  
ATOM  12906  O   GLU I 145     142.200 -76.062  66.701  1.00 73.47           O  
ANISOU12906  O   GLU I 145     8292   9171  10451    201    999  -1422       O  
ATOM  12907  CB  GLU I 145     142.172 -76.669  69.584  1.00 80.14           C  
ANISOU12907  CB  GLU I 145     9157  10035  11259    201    941  -1409       C  
ATOM  12908  CG  GLU I 145     142.410 -77.165  70.996  1.00 84.42           C  
ANISOU12908  CG  GLU I 145     9699  10591  11785    201    900  -1412       C  
ATOM  12909  CD  GLU I 145     141.451 -76.525  71.988  1.00 87.18           C  
ANISOU12909  CD  GLU I 145    10092  10926  12108    203    933  -1375       C  
ATOM  12910  OE1 GLU I 145     141.420 -75.272  72.072  1.00 88.97           O  
ANISOU12910  OE1 GLU I 145    10347  11140  12316    182    991  -1386       O  
ATOM  12911  OE2 GLU I 145     140.707 -77.273  72.667  1.00 87.82           O  
ANISOU12911  OE2 GLU I 145    10177  11006  12186    224    901  -1333       O  
ATOM  12912  N   VAL I 146     142.055 -78.290  66.505  1.00 74.25           N  
ANISOU12912  N   VAL I 146     8342   9287  10581    240    899  -1394       N  
ATOM  12913  CA  VAL I 146     141.407 -78.222  65.205  1.00 70.02           C  
ANISOU12913  CA  VAL I 146     7804   8736  10063    254    924  -1369       C  
ATOM  12914  C   VAL I 146     139.935 -77.825  65.358  1.00 68.30           C  
ANISOU12914  C   VAL I 146     7623   8494   9833    270    961  -1309       C  
ATOM  12915  O   VAL I 146     139.274 -78.251  66.302  1.00 68.29           O  
ANISOU12915  O   VAL I 146     7635   8492   9821    283    940  -1274       O  
ATOM  12916  CB  VAL I 146     141.535 -79.563  64.471  1.00 68.28           C  
ANISOU12916  CB  VAL I 146     7545   8527   9873    276    867  -1363       C  
ATOM  12917  CG1 VAL I 146     140.641 -79.601  63.240  1.00 68.01           C  
ANISOU12917  CG1 VAL I 146     7511   8474   9855    294    890  -1326       C  
ATOM  12918  CG2 VAL I 146     142.970 -79.806  64.092  1.00 68.42           C  
ANISOU12918  CG2 VAL I 146     7527   8566   9904    259    841  -1423       C  
ATOM  12919  N   GLU I 147     139.434 -76.980  64.460  1.00 71.39           N  
ANISOU12919  N   GLU I 147     8032   8867  10225    267   1017  -1298       N  
ATOM  12920  CA  GLU I 147     138.013 -76.630  64.480  1.00 69.38           C  
ANISOU12920  CA  GLU I 147     7810   8589   9961    284   1052  -1239       C  
ATOM  12921  C   GLU I 147     137.307 -77.089  63.202  1.00 64.82           C  
ANISOU12921  C   GLU I 147     7220   8001   9408    307   1053  -1207       C  
ATOM  12922  O   GLU I 147     137.728 -76.746  62.089  1.00 64.87           O  
ANISOU12922  O   GLU I 147     7214   8005   9427    299   1075  -1231       O  
ATOM  12923  CB  GLU I 147     137.805 -75.128  64.675  1.00 73.17           C  
ANISOU12923  CB  GLU I 147     8330   9054  10418    263   1123  -1245       C  
ATOM  12924  CG  GLU I 147     136.361 -74.708  64.450  1.00 71.17           C  
ANISOU12924  CG  GLU I 147     8109   8776  10158    280   1165  -1186       C  
ATOM  12925  CD  GLU I 147     136.151 -73.196  64.452  1.00 75.31           C  
ANISOU12925  CD  GLU I 147     8671   9283  10662    260   1239  -1192       C  
ATOM  12926  OE1 GLU I 147     136.031 -72.598  63.350  1.00 74.89           O  
ANISOU12926  OE1 GLU I 147     8620   9218  10617    257   1280  -1195       O  
ATOM  12927  OE2 GLU I 147     136.089 -72.617  65.562  1.00 79.30           O  
ANISOU12927  OE2 GLU I 147     9203   9787  11142    248   1256  -1193       O  
ATOM  12928  N   LEU I 148     136.233 -77.858  63.379  1.00 65.95           N  
ANISOU12928  N   LEU I 148     7367   8137   9555    335   1029  -1152       N  
ATOM  12929  CA  LEU I 148     135.501 -78.441  62.266  1.00 64.12           C  
ANISOU12929  CA  LEU I 148     7123   7896   9345    360   1023  -1117       C  
ATOM  12930  C   LEU I 148     134.143 -77.758  62.012  1.00 63.45           C  
ANISOU12930  C   LEU I 148     7073   7785   9250    371   1076  -1065       C  
ATOM  12931  O   LEU I 148     133.367 -77.470  62.941  1.00 63.83           O  
ANISOU12931  O   LEU I 148     7151   7823   9277    375   1090  -1033       O  
ATOM  12932  CB  LEU I 148     135.295 -79.930  62.513  1.00 62.99           C  
ANISOU12932  CB  LEU I 148     6953   7764   9218    385    953  -1093       C  
ATOM  12933  CG  LEU I 148     136.502 -80.827  62.230  1.00 63.10           C  
ANISOU12933  CG  LEU I 148     6923   7802   9252    381    898  -1137       C  
ATOM  12934  CD1 LEU I 148     136.229 -82.266  62.617  1.00 62.17           C  
ANISOU12934  CD1 LEU I 148     6782   7693   9145    406    830  -1111       C  
ATOM  12935  CD2 LEU I 148     136.894 -80.752  60.768  1.00 62.36           C  
ANISOU12935  CD2 LEU I 148     6807   7706   9180    379    911  -1158       C  
ATOM  12936  N   ASP I 149     133.860 -77.501  60.738  1.00 63.22           N  
ANISOU12936  N   ASP I 149     7040   7744   9236    376   1105  -1058       N  
ATOM  12937  CA  ASP I 149     132.662 -76.777  60.332  1.00 62.54           C  
ANISOU12937  CA  ASP I 149     6986   7635   9143    386   1159  -1014       C  
ATOM  12938  C   ASP I 149     131.653 -77.756  59.724  1.00 58.72           C  
ANISOU12938  C   ASP I 149     6490   7143   8677    419   1133   -963       C  
ATOM  12939  O   ASP I 149     131.805 -78.184  58.587  1.00 57.23           O  
ANISOU12939  O   ASP I 149     6276   6955   8512    427   1122   -968       O  
ATOM  12940  CB  ASP I 149     133.085 -75.703  59.331  1.00 64.39           C  
ANISOU12940  CB  ASP I 149     7226   7861   9380    366   1215  -1045       C  
ATOM  12941  CG  ASP I 149     132.025 -74.660  59.068  1.00 64.78           C  
ANISOU12941  CG  ASP I 149     7314   7886   9415    368   1281  -1010       C  
ATOM  12942  OD1 ASP I 149     130.822 -75.007  58.963  1.00 65.82           O  
ANISOU12942  OD1 ASP I 149     7456   8004   9549    393   1281   -954       O  
ATOM  12943  OD2 ASP I 149     132.425 -73.474  58.937  1.00 64.43           O  
ANISOU12943  OD2 ASP I 149     7287   7834   9358    345   1333  -1039       O  
ATOM  12944  N   ILE I 150     130.600 -78.096  60.450  1.00 59.23           N  
ANISOU12944  N   ILE I 150     6573   7200   8732    437   1123   -912       N  
ATOM  12945  CA  ILE I 150     129.718 -79.156  59.961  1.00 57.99           C  
ANISOU12945  CA  ILE I 150     6402   7038   8594    469   1090   -865       C  
ATOM  12946  C   ILE I 150     128.277 -78.682  59.740  1.00 57.46           C  
ANISOU12946  C   ILE I 150     6367   6947   8518    485   1134   -807       C  
ATOM  12947  O   ILE I 150     127.643 -78.198  60.670  1.00 57.63           O  
ANISOU12947  O   ILE I 150     6420   6960   8517    484   1155   -782       O  
ATOM  12948  CB  ILE I 150     129.683 -80.368  60.932  1.00 57.90           C  
ANISOU12948  CB  ILE I 150     6376   7041   8584    484   1024   -849       C  
ATOM  12949  CG1 ILE I 150     131.003 -80.533  61.680  1.00 58.65           C  
ANISOU12949  CG1 ILE I 150     6452   7157   8674    463    991   -903       C  
ATOM  12950  CG2 ILE I 150     129.356 -81.631  60.182  1.00 57.14           C  
ANISOU12950  CG2 ILE I 150     6248   6948   8515    511    976   -825       C  
ATOM  12951  CD1 ILE I 150     130.895 -81.446  62.885  1.00 58.80           C  
ANISOU12951  CD1 ILE I 150     6467   7188   8687    475    937   -887       C  
ATOM  12952  N   ASN I 151     127.750 -78.824  58.524  1.00 56.46           N  
ANISOU12952  N   ASN I 151     6232   6811   8411    500   1146   -786       N  
ATOM  12953  CA  ASN I 151     126.368 -78.435  58.304  1.00 56.29           C  
ANISOU12953  CA  ASN I 151     6239   6766   8381    516   1185   -730       C  
ATOM  12954  C   ASN I 151     125.434 -79.568  58.735  1.00 56.14           C  
ANISOU12954  C   ASN I 151     6215   6747   8368    546   1140   -678       C  
ATOM  12955  O   ASN I 151     125.893 -80.630  59.153  1.00 56.18           O  
ANISOU12955  O   ASN I 151     6193   6768   8383    553   1079   -687       O  
ATOM  12956  CB  ASN I 151     126.112 -78.000  56.837  1.00 56.11           C  
ANISOU12956  CB  ASN I 151     6213   6731   8374    520   1224   -727       C  
ATOM  12957  CG  ASN I 151     126.106 -79.154  55.837  1.00 55.91           C  
ANISOU12957  CG  ASN I 151     6151   6713   8379    540   1179   -718       C  
ATOM  12958  OD1 ASN I 151     126.032 -80.320  56.207  1.00 55.87           O  
ANISOU12958  OD1 ASN I 151     6125   6718   8384    557   1122   -703       O  
ATOM  12959  ND2 ASN I 151     126.165 -78.820  54.544  1.00 55.79           N  
ANISOU12959  ND2 ASN I 151     6127   6691   8379    540   1207   -727       N  
ATOM  12960  N   THR I 152     124.128 -79.309  58.637  1.00 58.50           N  
ANISOU12960  N   THR I 152     6541   7027   8661    563   1170   -624       N  
ATOM  12961  CA  THR I 152     123.052 -80.191  59.112  1.00 57.42           C  
ANISOU12961  CA  THR I 152     6407   6886   8525    590   1138   -568       C  
ATOM  12962  C   THR I 152     123.342 -80.776  60.483  1.00 58.29           C  
ANISOU12962  C   THR I 152     6515   7009   8623    589   1093   -572       C  
ATOM  12963  O   THR I 152     123.052 -81.925  60.730  1.00 57.47           O  
ANISOU12963  O   THR I 152     6393   6912   8531    609   1040   -548       O  
ATOM  12964  CB  THR I 152     122.745 -81.359  58.132  1.00 55.63           C  
ANISOU12964  CB  THR I 152     6148   6662   8328    615   1097   -546       C  
ATOM  12965  OG1 THR I 152     123.862 -82.236  58.054  1.00 55.82           O  
ANISOU12965  OG1 THR I 152     6133   6707   8369    611   1042   -587       O  
ATOM  12966  CG2 THR I 152     122.429 -80.864  56.745  1.00 54.70           C  
ANISOU12966  CG2 THR I 152     6031   6531   8223    618   1138   -541       C  
ATOM  12967  N   ALA I 153     123.895 -79.975  61.376  1.00 57.63           N  
ANISOU12967  N   ALA I 153     6450   6928   8517    566   1115   -601       N  
ATOM  12968  CA  ALA I 153     124.235 -80.431  62.710  1.00 57.80           C  
ANISOU12968  CA  ALA I 153     6471   6964   8526    562   1075   -608       C  
ATOM  12969  C   ALA I 153     123.065 -81.073  63.422  1.00 57.69           C  
ANISOU12969  C   ALA I 153     6470   6943   8506    587   1054   -549       C  
ATOM  12970  O   ALA I 153     123.240 -81.969  64.234  1.00 57.75           O  
ANISOU12970  O   ALA I 153     6464   6963   8514    595   1001   -546       O  
ATOM  12971  CB  ALA I 153     124.761 -79.285  63.529  1.00 58.04           C  
ANISOU12971  CB  ALA I 153     6528   6994   8530    535   1114   -639       C  
ATOM  12972  N   SER I 154     121.859 -80.611  63.116  1.00 62.05           N  
ANISOU12972  N   SER I 154     7050   7475   9053    600   1094   -502       N  
ATOM  12973  CA  SER I 154     120.654 -81.148  63.762  1.00 62.75           C  
ANISOU12973  CA  SER I 154     7152   7555   9134    624   1079   -442       C  
ATOM  12974  C   SER I 154     120.388 -82.603  63.371  1.00 61.45           C  
ANISOU12974  C   SER I 154     6956   7398   8995    651   1018   -418       C  
ATOM  12975  O   SER I 154     119.764 -83.325  64.124  1.00 62.58           O  
ANISOU12975  O   SER I 154     7101   7541   9134    668    985   -382       O  
ATOM  12976  CB  SER I 154     119.441 -80.298  63.427  1.00 62.99           C  
ANISOU12976  CB  SER I 154     7218   7562   9154    632   1138   -398       C  
ATOM  12977  OG  SER I 154     119.094 -80.465  62.071  1.00 63.76           O  
ANISOU12977  OG  SER I 154     7302   7652   9273    644   1148   -385       O  
ATOM  12978  N   THR I 155     120.856 -83.040  62.204  1.00 61.33           N  
ANISOU12978  N   THR I 155     6910   7388   9005    654   1003   -438       N  
ATOM  12979  CA  THR I 155     120.732 -84.452  61.833  1.00 60.01           C  
ANISOU12979  CA  THR I 155     6709   7230   8863    677    942   -420       C  
ATOM  12980  C   THR I 155     121.991 -85.285  62.146  1.00 60.70           C  
ANISOU12980  C   THR I 155     6762   7341   8961    669    883   -466       C  
ATOM  12981  O   THR I 155     121.989 -86.491  61.926  1.00 59.77           O  
ANISOU12981  O   THR I 155     6614   7232   8863    687    829   -455       O  
ATOM  12982  CB  THR I 155     120.395 -84.613  60.333  1.00 58.50           C  
ANISOU12982  CB  THR I 155     6503   7030   8695    690    953   -408       C  
ATOM  12983  OG1 THR I 155     121.588 -84.466  59.540  1.00 58.94           O  
ANISOU12983  OG1 THR I 155     6533   7097   8765    673    952   -464       O  
ATOM  12984  CG2 THR I 155     119.374 -83.587  59.913  1.00 58.05           C  
ANISOU12984  CG2 THR I 155     6480   6951   8627    692   1019   -375       C  
ATOM  12985  N   TRP I 156     123.059 -84.656  62.643  1.00 58.47           N  
ANISOU12985  N   TRP I 156     6481   7069   8666    642    893   -517       N  
ATOM  12986  CA  TRP I 156     124.231 -85.402  63.123  1.00 59.29           C  
ANISOU12986  CA  TRP I 156     6556   7196   8777    634    838   -559       C  
ATOM  12987  C   TRP I 156     123.997 -85.949  64.542  1.00 59.85           C  
ANISOU12987  C   TRP I 156     6634   7274   8833    641    802   -540       C  
ATOM  12988  O   TRP I 156     123.434 -85.259  65.396  1.00 60.51           O  
ANISOU12988  O   TRP I 156     6752   7348   8892    636    833   -520       O  
ATOM  12989  CB  TRP I 156     125.492 -84.525  63.109  1.00 60.84           C  
ANISOU12989  CB  TRP I 156     6750   7401   8966    602    863   -623       C  
ATOM  12990  CG  TRP I 156     126.088 -84.354  61.764  1.00 60.32           C  
ANISOU12990  CG  TRP I 156     6663   7337   8920    595    876   -654       C  
ATOM  12991  CD1 TRP I 156     125.871 -83.337  60.898  1.00 60.11           C  
ANISOU12991  CD1 TRP I 156     6652   7295   8891    586    935   -656       C  
ATOM  12992  CD2 TRP I 156     126.999 -85.240  61.118  1.00 59.93           C  
ANISOU12992  CD2 TRP I 156     6571   7303   8895    597    829   -686       C  
ATOM  12993  NE1 TRP I 156     126.588 -83.526  59.747  1.00 59.60           N  
ANISOU12993  NE1 TRP I 156     6558   7237   8849    582    928   -688       N  
ATOM  12994  CE2 TRP I 156     127.289 -84.693  59.858  1.00 59.48           C  
ANISOU12994  CE2 TRP I 156     6507   7242   8851    589    863   -708       C  
ATOM  12995  CE3 TRP I 156     127.586 -86.454  61.479  1.00 59.90           C  
ANISOU12995  CE3 TRP I 156     6536   7320   8905    605    761   -699       C  
ATOM  12996  CZ2 TRP I 156     128.140 -85.307  58.964  1.00 59.03           C  
ANISOU12996  CZ2 TRP I 156     6413   7198   8819    588    832   -741       C  
ATOM  12997  CZ3 TRP I 156     128.418 -87.065  60.593  1.00 59.45           C  
ANISOU12997  CZ3 TRP I 156     6442   7275   8872    604    730   -732       C  
ATOM  12998  CH2 TRP I 156     128.692 -86.493  59.345  1.00 59.01           C  
ANISOU12998  CH2 TRP I 156     6379   7213   8828    596    765   -753       C  
ATOM  12999  N   LYS I 157     124.430 -87.177  64.812  1.00 64.07           N  
ANISOU12999  N   LYS I 157     7138   7825   9382    651    736   -546       N  
ATOM  13000  CA  LYS I 157     124.246 -87.721  66.157  1.00 66.93           C  
ANISOU13000  CA  LYS I 157     7506   8194   9730    658    700   -529       C  
ATOM  13001  C   LYS I 157     125.564 -88.026  66.867  1.00 68.87           C  
ANISOU13001  C   LYS I 157     7732   8463   9974    641    661   -582       C  
ATOM  13002  O   LYS I 157     125.958 -87.324  67.792  1.00 71.55           O  
ANISOU13002  O   LYS I 157     8091   8805  10291    621    680   -603       O  
ATOM  13003  CB  LYS I 157     123.394 -88.986  66.106  1.00 67.27           C  
ANISOU13003  CB  LYS I 157     7535   8236   9789    689    653   -480       C  
ATOM  13004  CG  LYS I 157     123.039 -89.556  67.477  1.00 70.65           C  
ANISOU13004  CG  LYS I 157     7972   8668  10202    699    618   -455       C  
ATOM  13005  CD  LYS I 157     122.083 -90.739  67.335  1.00 71.68           C  
ANISOU13005  CD  LYS I 157     8091   8795  10348    731    577   -403       C  
ATOM  13006  CE  LYS I 157     121.167 -90.902  68.550  1.00 75.38           C  
ANISOU13006  CE  LYS I 157     8585   9259  10798    743    570   -358       C  
ATOM  13007  NZ  LYS I 157     119.905 -91.629  68.195  1.00 76.65           N  
ANISOU13007  NZ  LYS I 157     8746   9407  10970    773    557   -297       N  
ATOM  13008  N   LYS I 158     126.232 -89.090  66.448  1.00 67.10           N  
ANISOU13008  N   LYS I 158     7469   8254   9773    648    607   -602       N  
ATOM  13009  CA  LYS I 158     127.464 -89.495  67.097  1.00 69.03           C  
ANISOU13009  CA  LYS I 158     7692   8521  10017    634    566   -649       C  
ATOM  13010  C   LYS I 158     128.596 -88.899  66.306  1.00 67.42           C  
ANISOU13010  C   LYS I 158     7473   8324   9820    610    586   -706       C  
ATOM  13011  O   LYS I 158     128.664 -89.106  65.105  1.00 65.07           O  
ANISOU13011  O   LYS I 158     7156   8024   9544    616    587   -711       O  
ATOM  13012  CB  LYS I 158     127.586 -91.019  67.146  1.00 69.88           C  
ANISOU13012  CB  LYS I 158     7765   8642  10144    655    493   -639       C  
ATOM  13013  CG  LYS I 158     128.826 -91.529  67.859  1.00 71.43           C  
ANISOU13013  CG  LYS I 158     7937   8862  10340    642    446   -686       C  
ATOM  13014  CD  LYS I 158     129.285 -92.863  67.287  1.00 71.88           C  
ANISOU13014  CD  LYS I 158     7952   8933  10426    657    383   -695       C  
ATOM  13015  CE  LYS I 158     128.268 -93.978  67.508  1.00 73.84           C  
ANISOU13015  CE  LYS I 158     8195   9177  10682    688    343   -639       C  
ATOM  13016  NZ  LYS I 158     128.686 -95.230  66.788  1.00 74.18           N  
ANISOU13016  NZ  LYS I 158     8197   9232  10755    703    287   -647       N  
ATOM  13017  N   PHE I 159     129.437 -88.087  66.924  1.00 63.69           N  
ANISOU13017  N   PHE I 159     7011   7859   9329    584    606   -749       N  
ATOM  13018  CA  PHE I 159     130.628 -87.655  66.216  1.00 64.14           C  
ANISOU13018  CA  PHE I 159     7050   7926   9396    562    617   -807       C  
ATOM  13019  C   PHE I 159     131.805 -87.806  67.145  1.00 65.67           C  
ANISOU13019  C   PHE I 159     7230   8140   9580    543    586   -854       C  
ATOM  13020  O   PHE I 159     132.030 -86.947  68.005  1.00 67.11           O  
ANISOU13020  O   PHE I 159     7438   8323   9739    524    614   -870       O  
ATOM  13021  CB  PHE I 159     130.483 -86.204  65.762  1.00 64.71           C  
ANISOU13021  CB  PHE I 159     7150   7982   9454    543    691   -816       C  
ATOM  13022  CG  PHE I 159     131.388 -85.813  64.629  1.00 64.88           C  
ANISOU13022  CG  PHE I 159     7152   8008   9490    527    709   -862       C  
ATOM  13023  CD1 PHE I 159     132.653 -85.329  64.869  1.00 66.40           C  
ANISOU13023  CD1 PHE I 159     7337   8215   9677    500    712   -921       C  
ATOM  13024  CD2 PHE I 159     130.948 -85.887  63.322  1.00 63.59           C  
ANISOU13024  CD2 PHE I 159     6981   7835   9347    539    724   -845       C  
ATOM  13025  CE1 PHE I 159     133.462 -84.958  63.823  1.00 66.54           C  
ANISOU13025  CE1 PHE I 159     7338   8237   9708    486    729   -962       C  
ATOM  13026  CE2 PHE I 159     131.761 -85.513  62.275  1.00 63.66           C  
ANISOU13026  CE2 PHE I 159     6972   7847   9370    525    741   -887       C  
ATOM  13027  CZ  PHE I 159     133.016 -85.051  62.526  1.00 65.17           C  
ANISOU13027  CZ  PHE I 159     7155   8052   9554    498    744   -945       C  
ATOM  13028  N   GLU I 160     132.612 -88.837  66.902  1.00 69.58           N  
ANISOU13028  N   GLU I 160     7687   8655  10096    548    529   -879       N  
ATOM  13029  CA  GLU I 160     133.741 -89.163  67.763  1.00 72.68           C  
ANISOU13029  CA  GLU I 160     8064   9069  10483    534    491   -922       C  
ATOM  13030  C   GLU I 160     134.992 -89.014  66.934  1.00 71.64           C  
ANISOU13030  C   GLU I 160     7904   8950  10365    515    489   -980       C  
ATOM  13031  O   GLU I 160     135.026 -89.483  65.787  1.00 69.03           O  
ANISOU13031  O   GLU I 160     7550   8619  10059    526    478   -980       O  
ATOM  13032  CB  GLU I 160     133.627 -90.589  68.321  1.00 73.99           C  
ANISOU13032  CB  GLU I 160     8207   9248  10659    556    420   -902       C  
ATOM  13033  CG  GLU I 160     132.564 -90.774  69.398  1.00 75.93           C  
ANISOU13033  CG  GLU I 160     8478   9484  10887    571    416   -851       C  
ATOM  13034  CD  GLU I 160     132.438 -92.225  69.848  1.00 77.91           C  
ANISOU13034  CD  GLU I 160     8705   9746  11150    594    346   -830       C  
ATOM  13035  OE1 GLU I 160     133.192 -93.075  69.322  1.00 77.03           O  
ANISOU13035  OE1 GLU I 160     8557   9649  11060    598    302   -855       O  
ATOM  13036  OE2 GLU I 160     131.583 -92.519  70.718  1.00 80.85           O  
ANISOU13036  OE2 GLU I 160     9096  10113  11511    608    335   -787       O  
ATOM  13037  N   VAL I 161     136.011 -88.353  67.483  1.00 70.70           N  
ANISOU13037  N   VAL I 161     7788   8842  10232    488    501  -1029       N  
ATOM  13038  CA  VAL I 161     137.273 -88.241  66.759  1.00 70.27           C  
ANISOU13038  CA  VAL I 161     7707   8802  10191    470    496  -1087       C  
ATOM  13039  C   VAL I 161     138.451 -88.854  67.522  1.00 73.82           C  
ANISOU13039  C   VAL I 161     8131   9277  10640    460    444  -1130       C  
ATOM  13040  O   VAL I 161     138.707 -88.543  68.687  1.00 78.14           O  
ANISOU13040  O   VAL I 161     8694   9830  11166    447    444  -1141       O  
ATOM  13041  CB  VAL I 161     137.583 -86.785  66.418  1.00 70.87           C  
ANISOU13041  CB  VAL I 161     7805   8869  10253    444    563  -1116       C  
ATOM  13042  CG1 VAL I 161     138.780 -86.715  65.491  1.00 70.87           C  
ANISOU13042  CG1 VAL I 161     7776   8882  10271    428    560  -1170       C  
ATOM  13043  CG2 VAL I 161     136.391 -86.149  65.756  1.00 68.19           C  
ANISOU13043  CG2 VAL I 161     7492   8504   9912    454    615  -1072       C  
ATOM  13044  N   TYR I 162     139.167 -89.734  66.832  1.00 74.12           N  
ANISOU13044  N   TYR I 162     8130   9329  10702    465    401  -1154       N  
ATOM  13045  CA  TYR I 162     140.222 -90.543  67.437  1.00 76.99           C  
ANISOU13045  CA  TYR I 162     8465   9717  11070    461    343  -1189       C  
ATOM  13046  C   TYR I 162     141.622 -90.230  66.874  1.00 77.77           C  
ANISOU13046  C   TYR I 162     8540   9831  11177    437    345  -1254       C  
ATOM  13047  O   TYR I 162     141.804 -90.082  65.663  1.00 75.30           O  
ANISOU13047  O   TYR I 162     8214   9515  10882    436    361  -1267       O  
ATOM  13048  CB  TYR I 162     139.907 -92.036  67.244  1.00 75.73           C  
ANISOU13048  CB  TYR I 162     8277   9564  10933    490    280  -1161       C  
ATOM  13049  CG  TYR I 162     138.729 -92.550  68.050  1.00 76.31           C  
ANISOU13049  CG  TYR I 162     8369   9628  10997    512    264  -1103       C  
ATOM  13050  CD1 TYR I 162     138.837 -92.754  69.418  1.00 80.59           C  
ANISOU13050  CD1 TYR I 162     8921  10180  11521    510    240  -1102       C  
ATOM  13051  CD2 TYR I 162     137.519 -92.857  67.439  1.00 73.46           C  
ANISOU13051  CD2 TYR I 162     8015   9249  10646    537    272  -1050       C  
ATOM  13052  CE1 TYR I 162     137.772 -93.231  70.158  1.00 81.66           C  
ANISOU13052  CE1 TYR I 162     9072  10307  11648    531    225  -1049       C  
ATOM  13053  CE2 TYR I 162     136.448 -93.333  68.176  1.00 74.42           C  
ANISOU13053  CE2 TYR I 162     8154   9363  10760    558    257   -997       C  
ATOM  13054  CZ  TYR I 162     136.584 -93.518  69.531  1.00 78.31           C  
ANISOU13054  CZ  TYR I 162     8655   9865  11235    555    234   -997       C  
ATOM  13055  OH  TYR I 162     135.530 -93.995  70.264  1.00 79.77           O  
ANISOU13055  OH  TYR I 162     8856  10042  11412    575    219   -945       O  
ATOM  13056  N   GLU I 163     142.598 -90.135  67.768  1.00 74.32           N  
ANISOU13056  N   GLU I 163     8098   9412  10728    418    327  -1295       N  
ATOM  13057  CA  GLU I 163     143.991 -89.960  67.387  1.00 75.60           C  
ANISOU13057  CA  GLU I 163     8235   9591  10897    396    320  -1358       C  
ATOM  13058  C   GLU I 163     144.814 -91.119  67.933  1.00 77.81           C  
ANISOU13058  C   GLU I 163     8482   9896  11186    401    250  -1380       C  
ATOM  13059  O   GLU I 163     144.892 -91.308  69.147  1.00 81.34           O  
ANISOU13059  O   GLU I 163     8937  10352  11617    399    228  -1379       O  
ATOM  13060  CB  GLU I 163     144.517 -88.617  67.902  1.00 78.78           C  
ANISOU13060  CB  GLU I 163     8663   9993  11276    365    370  -1393       C  
ATOM  13061  CG  GLU I 163     146.033 -88.516  68.109  1.00 81.28           C  
ANISOU13061  CG  GLU I 163     8958  10333  11592    340    353  -1459       C  
ATOM  13062  CD  GLU I 163     146.437 -87.129  68.563  1.00 84.45           C  
ANISOU13062  CD  GLU I 163     9387  10732  11970    310    407  -1489       C  
ATOM  13063  OE1 GLU I 163     146.502 -86.884  69.789  1.00 87.99           O  
ANISOU13063  OE1 GLU I 163     9853  11185  12396    301    405  -1492       O  
ATOM  13064  OE2 GLU I 163     146.661 -86.275  67.684  1.00 83.71           O  
ANISOU13064  OE2 GLU I 163     9297  10629  11879    295    452  -1510       O  
ATOM  13065  N   ASN I 164     145.417 -91.887  67.026  1.00 83.64           N  
ANISOU13065  N   ASN I 164     9184  10645  11951    407    216  -1401       N  
ATOM  13066  CA  ASN I 164     146.091 -93.143  67.373  1.00 85.45           C  
ANISOU13066  CA  ASN I 164     9378  10896  12192    417    146  -1416       C  
ATOM  13067  C   ASN I 164     145.181 -94.118  68.128  1.00 85.71           C  
ANISOU13067  C   ASN I 164     9415  10927  12224    444    105  -1365       C  
ATOM  13068  O   ASN I 164     145.601 -94.754  69.102  1.00 88.73           O  
ANISOU13068  O   ASN I 164     9787  11325  12600    445     61  -1374       O  
ATOM  13069  CB  ASN I 164     147.351 -92.871  68.196  1.00 89.38           C  
ANISOU13069  CB  ASN I 164     9869  11415  12677    392    133  -1471       C  
ATOM  13070  CG  ASN I 164     148.547 -92.575  67.334  1.00 89.69           C  
ANISOU13070  CG  ASN I 164     9884  11467  12729    372    140  -1527       C  
ATOM  13071  OD1 ASN I 164     149.111 -91.478  67.386  1.00 91.35           O  
ANISOU13071  OD1 ASN I 164    10107  11676  12925    346    182  -1563       O  
ATOM  13072  ND2 ASN I 164     148.949 -93.555  66.528  1.00 88.53           N  
ANISOU13072  ND2 ASN I 164     9700  11329  12608    385     97  -1537       N  
ATOM  13073  N   ASN I 165     143.943 -94.232  67.657  1.00 87.74           N  
ANISOU13073  N   ASN I 165     9686  11164  12487    465    121  -1312       N  
ATOM  13074  CA  ASN I 165     142.933 -95.082  68.275  1.00 88.10           C  
ANISOU13074  CA  ASN I 165     9738  11204  12531    491     89  -1258       C  
ATOM  13075  C   ASN I 165     142.683 -94.809  69.747  1.00 90.85           C  
ANISOU13075  C   ASN I 165    10113  11553  12852    486     91  -1246       C  
ATOM  13076  O   ASN I 165     142.422 -95.735  70.505  1.00 92.95           O  
ANISOU13076  O   ASN I 165    10372  11826  13117    503     44  -1223       O  
ATOM  13077  CB  ASN I 165     143.287 -96.563  68.124  1.00 89.55           C  
ANISOU13077  CB  ASN I 165     9883  11404  12738    511     18  -1259       C  
ATOM  13078  CG  ASN I 165     142.964 -97.105  66.753  1.00 88.73           C  
ANISOU13078  CG  ASN I 165     9759  11293  12662    528     11  -1243       C  
ATOM  13079  OD1 ASN I 165     141.822 -97.486  66.467  1.00 85.87           O  
ANISOU13079  OD1 ASN I 165     9405  10916  12306    551     12  -1191       O  
ATOM  13080  ND2 ASN I 165     143.979 -97.156  65.891  1.00 91.68           N  
ANISOU13080  ND2 ASN I 165    10104  11678  13052    517      4  -1289       N  
ATOM  13081  N   GLN I 166     142.753 -93.554  70.165  1.00 83.44           N  
ANISOU13081  N   GLN I 166     9204  10608  11891    464    143  -1261       N  
ATOM  13082  CA  GLN I 166     142.221 -93.201  71.480  1.00 87.07           C  
ANISOU13082  CA  GLN I 166     9695  11063  12323    462    153  -1238       C  
ATOM  13083  C   GLN I 166     141.383 -91.908  71.427  1.00 86.21           C  
ANISOU13083  C   GLN I 166     9627  10931  12196    453    225  -1215       C  
ATOM  13084  O   GLN I 166     141.591 -91.037  70.582  1.00 83.55           O  
ANISOU13084  O   GLN I 166     9296  10587  11862    439    271  -1235       O  
ATOM  13085  CB  GLN I 166     143.348 -93.087  72.498  1.00 91.95           C  
ANISOU13085  CB  GLN I 166    10307  11702  12927    441    133  -1285       C  
ATOM  13086  CG  GLN I 166     144.478 -92.228  72.041  1.00 96.71           C  
ANISOU13086  CG  GLN I 166    10903  12313  13529    412    162  -1344       C  
ATOM  13087  CD  GLN I 166     145.639 -92.260  73.004  1.00 97.74           C  
ANISOU13087  CD  GLN I 166    11023  12466  13647    392    135  -1391       C  
ATOM  13088  OE1 GLN I 166     146.237 -93.323  73.248  1.00 98.77           O  
ANISOU13088  OE1 GLN I 166    11123  12616  13789    401     76  -1405       O  
ATOM  13089  NE2 GLN I 166     145.972 -91.090  73.566  1.00 97.91           N  
ANISOU13089  NE2 GLN I 166    11070  12486  13646    367    179  -1417       N  
ATOM  13090  N   LYS I 167     140.416 -91.804  72.330  1.00 83.20           N  
ANISOU13090  N   LYS I 167     9275  10539  11797    463    234  -1172       N  
ATOM  13091  CA  LYS I 167     139.360 -90.811  72.207  1.00 82.06           C  
ANISOU13091  CA  LYS I 167     9169  10371  11639    463    295  -1137       C  
ATOM  13092  C   LYS I 167     139.863 -89.409  72.491  1.00 84.52           C  
ANISOU13092  C   LYS I 167     9505  10679  11928    433    350  -1172       C  
ATOM  13093  O   LYS I 167     140.476 -89.169  73.528  1.00 89.28           O  
ANISOU13093  O   LYS I 167    10114  11295  12513    417    342  -1199       O  
ATOM  13094  CB  LYS I 167     138.208 -91.162  73.154  1.00 83.71           C  
ANISOU13094  CB  LYS I 167     9401  10570  11834    483    285  -1081       C  
ATOM  13095  CG  LYS I 167     136.882 -90.499  72.834  1.00 81.74           C  
ANISOU13095  CG  LYS I 167     9185  10295  11577    493    336  -1031       C  
ATOM  13096  CD  LYS I 167     135.870 -90.776  73.945  1.00 83.53           C  
ANISOU13096  CD  LYS I 167     9435  10514  11787    509    326   -982       C  
ATOM  13097  CE  LYS I 167     134.510 -90.107  73.696  1.00 82.49           C  
ANISOU13097  CE  LYS I 167     9339  10356  11647    520    378   -930       C  
ATOM  13098  NZ  LYS I 167     133.597 -90.941  72.862  1.00 77.42           N  
ANISOU13098  NZ  LYS I 167     8685   9704  11027    548    360   -884       N  
ATOM  13099  N   LEU I 168     139.611 -88.485  71.566  1.00 81.37           N  
ANISOU13099  N   LEU I 168     9120  10265  11531    424    405  -1173       N  
ATOM  13100  CA  LEU I 168     139.856 -87.070  71.829  1.00 83.04           C  
ANISOU13100  CA  LEU I 168     9361  10469  11720    397    465  -1198       C  
ATOM  13101  C   LEU I 168     138.631 -86.458  72.489  1.00 84.13           C  
ANISOU13101  C   LEU I 168     9542  10588  11837    404    503  -1149       C  
ATOM  13102  O   LEU I 168     137.508 -86.802  72.130  1.00 81.46           O  
ANISOU13102  O   LEU I 168     9211  10235  11505    427    506  -1098       O  
ATOM  13103  CB  LEU I 168     140.188 -86.313  70.543  1.00 79.41           C  
ANISOU13103  CB  LEU I 168     8897  10002  11272    384    508  -1223       C  
ATOM  13104  CG  LEU I 168     141.349 -86.826  69.693  1.00 77.97           C  
ANISOU13104  CG  LEU I 168     8675   9838  11113    377    478  -1270       C  
ATOM  13105  CD1 LEU I 168     141.658 -85.819  68.593  1.00 75.12           C  
ANISOU13105  CD1 LEU I 168     8318   9467  10757    360    531  -1296       C  
ATOM  13106  CD2 LEU I 168     142.563 -87.089  70.557  1.00 82.14           C  
ANISOU13106  CD2 LEU I 168     9185  10390  11634    361    440  -1318       C  
ATOM  13107  N   PRO I 169     138.843 -85.544  73.446  1.00 78.79           N  
ANISOU13107  N   PRO I 169     8892   9912  11134    383    533  -1166       N  
ATOM  13108  CA  PRO I 169     137.763 -84.852  74.155  1.00 80.00           C  
ANISOU13108  CA  PRO I 169     9086  10046  11263    386    572  -1124       C  
ATOM  13109  C   PRO I 169     137.099 -83.779  73.294  1.00 77.28           C  
ANISOU13109  C   PRO I 169     8767   9679  10915    382    640  -1108       C  
ATOM  13110  O   PRO I 169     137.483 -82.613  73.385  1.00 79.16           O  
ANISOU13110  O   PRO I 169     9026   9914  11139    357    688  -1137       O  
ATOM  13111  CB  PRO I 169     138.480 -84.218  75.341  1.00 85.36           C  
ANISOU13111  CB  PRO I 169     9780  10736  11917    362    580  -1159       C  
ATOM  13112  CG  PRO I 169     139.830 -83.932  74.817  1.00 86.02           C  
ANISOU13112  CG  PRO I 169     9841  10834  12009    338    580  -1222       C  
ATOM  13113  CD  PRO I 169     140.163 -85.089  73.904  1.00 82.56           C  
ANISOU13113  CD  PRO I 169     9361  10406  11601    355    531  -1226       C  
ATOM  13114  N   VAL I 170     136.139 -84.170  72.459  1.00 77.45           N  
ANISOU13114  N   VAL I 170     8788   9686  10953    405    643  -1064       N  
ATOM  13115  CA  VAL I 170     135.505 -83.233  71.538  1.00 77.19           C  
ANISOU13115  CA  VAL I 170     8776   9632  10920    403    704  -1049       C  
ATOM  13116  C   VAL I 170     134.492 -82.344  72.255  1.00 77.28           C  
ANISOU13116  C   VAL I 170     8833   9625  10906    402    752  -1012       C  
ATOM  13117  O   VAL I 170     133.737 -82.816  73.103  1.00 76.98           O  
ANISOU13117  O   VAL I 170     8806   9584  10857    419    732   -972       O  
ATOM  13118  CB  VAL I 170     134.818 -83.975  70.386  1.00 76.12           C  
ANISOU13118  CB  VAL I 170     8624   9489  10811    429    691  -1014       C  
ATOM  13119  CG1 VAL I 170     134.233 -82.994  69.399  1.00 75.90           C  
ANISOU13119  CG1 VAL I 170     8616   9440  10783    425    754  -1001       C  
ATOM  13120  CG2 VAL I 170     135.813 -84.874  69.686  1.00 76.01           C  
ANISOU13120  CG2 VAL I 170     8565   9493  10823    430    643  -1050       C  
ATOM  13121  N   ARG I 171     134.487 -81.052  71.931  1.00 74.86           N  
ANISOU13121  N   ARG I 171     6413   8681  13349    979    -78  -2240       N  
ATOM  13122  CA  ARG I 171     133.493 -80.139  72.503  1.00 76.85           C  
ANISOU13122  CA  ARG I 171     6709   8924  13565    980    -28  -2254       C  
ATOM  13123  C   ARG I 171     132.949 -79.136  71.474  1.00 73.75           C  
ANISOU13123  C   ARG I 171     6304   8541  13175   1032     18  -2267       C  
ATOM  13124  O   ARG I 171     133.620 -78.791  70.495  1.00 71.71           O  
ANISOU13124  O   ARG I 171     6019   8286  12940   1057     12  -2263       O  
ATOM  13125  CB  ARG I 171     134.082 -79.391  73.699  1.00 82.74           C  
ANISOU13125  CB  ARG I 171     7518   9641  14279    928    -33  -2248       C  
ATOM  13126  CG  ARG I 171     134.872 -78.170  73.321  1.00 83.99           C  
ANISOU13126  CG  ARG I 171     7693   9785  14435    933    -23  -2245       C  
ATOM  13127  CD  ARG I 171     135.834 -77.787  74.413  1.00 90.19           C  
ANISOU13127  CD  ARG I 171     8527  10542  15198    877    -48  -2232       C  
ATOM  13128  NE  ARG I 171     137.122 -77.444  73.824  1.00 91.19           N  
ANISOU13128  NE  ARG I 171     8640  10662  15345    877    -74  -2220       N  
ATOM  13129  CZ  ARG I 171     137.446 -76.228  73.397  1.00 92.04           C  
ANISOU13129  CZ  ARG I 171     8763  10761  15447    892    -51  -2222       C  
ATOM  13130  NH1 ARG I 171     136.582 -75.218  73.511  1.00 91.87           N  
ANISOU13130  NH1 ARG I 171     8773  10735  15400    908      0  -2237       N  
ATOM  13131  NH2 ARG I 171     138.641 -76.024  72.860  1.00 93.42           N  
ANISOU13131  NH2 ARG I 171     8923  10930  15642    892    -78  -2210       N  
ATOM  13132  N   LEU I 172     131.722 -78.686  71.704  1.00 72.97           N  
ANISOU13132  N   LEU I 172     6226   8446  13054   1047     64  -2283       N  
ATOM  13133  CA  LEU I 172     131.058 -77.766  70.801  1.00 72.89           C  
ANISOU13133  CA  LEU I 172     6206   8444  13044   1096    111  -2296       C  
ATOM  13134  C   LEU I 172     131.310 -76.330  71.251  1.00 73.09           C  
ANISOU13134  C   LEU I 172     6283   8445  13041   1082    138  -2299       C  
ATOM  13135  O   LEU I 172     131.111 -75.988  72.421  1.00 73.32           O  
ANISOU13135  O   LEU I 172     6365   8457  13038   1043    147  -2300       O  
ATOM  13136  CB  LEU I 172     129.558 -78.068  70.759  1.00 72.85           C  
ANISOU13136  CB  LEU I 172     6192   8457  13032   1123    148  -2312       C  
ATOM  13137  CG  LEU I 172     128.596 -77.331  69.825  1.00 72.75           C  
ANISOU13137  CG  LEU I 172     6164   8458  13021   1178    198  -2328       C  
ATOM  13138  CD1 LEU I 172     128.856 -77.627  68.354  1.00 72.47           C  
ANISOU13138  CD1 LEU I 172     6068   8444  13025   1225    190  -2327       C  
ATOM  13139  CD2 LEU I 172     127.180 -77.714  70.195  1.00 72.79           C  
ANISOU13139  CD2 LEU I 172     6172   8474  13011   1188    229  -2342       C  
ATOM  13140  N   VAL I 173     131.758 -75.486  70.332  1.00 73.55           N  
ANISOU13140  N   VAL I 173     6330   8504  13112   1111    150  -2299       N  
ATOM  13141  CA  VAL I 173     132.024 -74.098  70.686  1.00 77.44           C  
ANISOU13141  CA  VAL I 173     6871   8975  13579   1099    176  -2301       C  
ATOM  13142  C   VAL I 173     130.902 -73.168  70.171  1.00 76.30           C  
ANISOU13142  C   VAL I 173     6730   8837  13423   1143    235  -2319       C  
ATOM  13143  O   VAL I 173     130.263 -72.490  70.985  1.00 79.97           O  
ANISOU13143  O   VAL I 173     7242   9288  13854   1127    267  -2328       O  
ATOM  13144  CB  VAL I 173     133.418 -73.647  70.213  1.00 79.50           C  
ANISOU13144  CB  VAL I 173     7125   9225  13856   1094    148  -2288       C  
ATOM  13145  CG1 VAL I 173     134.457 -74.229  71.134  1.00 83.40           C  
ANISOU13145  CG1 VAL I 173     7638   9703  14347   1039     99  -2271       C  
ATOM  13146  CG2 VAL I 173     133.707 -74.089  68.799  1.00 75.10           C  
ANISOU13146  CG2 VAL I 173     6505   8689  13339   1139    135  -2285       C  
ATOM  13147  N   SER I 174     130.646 -73.097  68.865  1.00 78.49           N  
ANISOU13147  N   SER I 174     6962   9134  13726   1196    249  -2324       N  
ATOM  13148  CA  SER I 174     129.488 -72.311  68.420  1.00 78.13           C  
ANISOU13148  CA  SER I 174     6919   9096  13669   1236    305  -2341       C  
ATOM  13149  C   SER I 174     128.507 -73.129  67.608  1.00 73.79           C  
ANISOU13149  C   SER I 174     6319   8575  13141   1280    316  -2350       C  
ATOM  13150  O   SER I 174     128.879 -74.163  67.050  1.00 70.94           O  
ANISOU13150  O   SER I 174     5913   8231  12811   1288    281  -2343       O  
ATOM  13151  CB  SER I 174     129.913 -71.096  67.594  1.00 79.17           C  
ANISOU13151  CB  SER I 174     7053   9223  13806   1264    326  -2343       C  
ATOM  13152  OG  SER I 174     128.768 -70.411  67.086  1.00 78.91           O  
ANISOU13152  OG  SER I 174     7018   9199  13766   1307    379  -2359       O  
ATOM  13153  N   TYR I 175     127.260 -72.662  67.547  1.00 72.13           N  
ANISOU13153  N   TYR I 175     6118   8372  12916   1306    364  -2366       N  
ATOM  13154  CA  TYR I 175     126.269 -73.228  66.640  1.00 71.93           C  
ANISOU13154  CA  TYR I 175     6045   8374  12910   1354    382  -2376       C  
ATOM  13155  C   TYR I 175     125.547 -72.128  65.868  1.00 71.89           C  
ANISOU13155  C   TYR I 175     6039   8375  12902   1400    433  -2389       C  
ATOM  13156  O   TYR I 175     125.288 -71.061  66.409  1.00 72.08           O  
ANISOU13156  O   TYR I 175     6109   8382  12898   1391    466  -2395       O  
ATOM  13157  CB  TYR I 175     125.249 -74.075  67.395  1.00 71.99           C  
ANISOU13157  CB  TYR I 175     6058   8390  12905   1341    388  -2382       C  
ATOM  13158  CG  TYR I 175     124.111 -74.550  66.508  1.00 71.80           C  
ANISOU13158  CG  TYR I 175     5990   8394  12898   1391    412  -2394       C  
ATOM  13159  CD1 TYR I 175     124.367 -75.341  65.397  1.00 71.54           C  
ANISOU13159  CD1 TYR I 175     5897   8383  12902   1423    389  -2390       C  
ATOM  13160  CD2 TYR I 175     122.790 -74.207  66.773  1.00 71.89           C  
ANISOU13160  CD2 TYR I 175     6017   8409  12889   1407    458  -2409       C  
ATOM  13161  CE1 TYR I 175     123.344 -75.771  64.570  1.00 71.37           C  
ANISOU13161  CE1 TYR I 175     5834   8387  12896   1468    410  -2400       C  
ATOM  13162  CE2 TYR I 175     121.759 -74.652  65.946  1.00 71.72           C  
ANISOU13162  CE2 TYR I 175     5954   8413  12883   1453    479  -2420       C  
ATOM  13163  CZ  TYR I 175     122.051 -75.434  64.848  1.00 71.46           C  
ANISOU13163  CZ  TYR I 175     5862   8402  12887   1483    455  -2415       C  
ATOM  13164  OH  TYR I 175     121.075 -75.889  64.006  1.00 71.28           O  
ANISOU13164  OH  TYR I 175     5798   8405  12881   1528    474  -2424       O  
ATOM  13165  N   SER I 176     125.224 -72.381  64.603  1.00 72.17           N  
ANISOU13165  N   SER I 176     6023   8434  12966   1450    441  -2393       N  
ATOM  13166  CA  SER I 176     124.505 -71.400  63.794  1.00 72.61           C  
ANISOU13166  CA  SER I 176     6073   8496  13020   1497    489  -2405       C  
ATOM  13167  C   SER I 176     123.117 -71.910  63.406  1.00 70.84           C  
ANISOU13167  C   SER I 176     5820   8295  12801   1533    517  -2418       C  
ATOM  13168  O   SER I 176     123.011 -72.876  62.659  1.00 70.41           O  
ANISOU13168  O   SER I 176     5715   8262  12774   1557    498  -2417       O  
ATOM  13169  CB  SER I 176     125.316 -71.055  62.544  1.00 71.69           C  
ANISOU13169  CB  SER I 176     5921   8386  12932   1528    478  -2400       C  
ATOM  13170  OG  SER I 176     126.551 -70.458  62.899  1.00 74.00           O  
ANISOU13170  OG  SER I 176     6242   8656  13219   1497    457  -2388       O  
ATOM  13171  N   PRO I 177     122.052 -71.245  63.895  1.00 70.60           N  
ANISOU13171  N   PRO I 177     5823   8260  12743   1538    563  -2432       N  
ATOM  13172  CA  PRO I 177     120.665 -71.730  63.855  1.00 70.57           C  
ANISOU13172  CA  PRO I 177     5803   8273  12736   1562    591  -2444       C  
ATOM  13173  C   PRO I 177     120.089 -71.921  62.458  1.00 70.32           C  
ANISOU13173  C   PRO I 177     5716   8269  12733   1621    606  -2451       C  
ATOM  13174  O   PRO I 177     120.736 -71.615  61.474  1.00 70.17           O  
ANISOU13174  O   PRO I 177     5671   8255  12736   1646    598  -2446       O  
ATOM  13175  CB  PRO I 177     119.895 -70.652  64.607  1.00 70.80           C  
ANISOU13175  CB  PRO I 177     5885   8287  12730   1555    638  -2456       C  
ATOM  13176  CG  PRO I 177     120.934 -69.945  65.434  1.00 71.00           C  
ANISOU13176  CG  PRO I 177     5958   8283  12734   1510    624  -2447       C  
ATOM  13177  CD  PRO I 177     122.149 -69.941  64.571  1.00 70.83           C  
ANISOU13177  CD  PRO I 177     5909   8264  12741   1519    591  -2435       C  
ATOM  13178  N   VAL I 178     118.840 -72.381  62.411  1.00 77.56           N  
ANISOU13178  N   VAL I 178     6618   9203  13647   1642    631  -2462       N  
ATOM  13179  CA  VAL I 178     118.400 -73.414  61.440  1.00 74.88           C  
ANISOU13179  CA  VAL I 178     6218   8893  13339   1679    620  -2463       C  
ATOM  13180  C   VAL I 178     118.447 -73.197  59.902  1.00 73.60           C  
ANISOU13180  C   VAL I 178     6007   8751  13208   1733    629  -2465       C  
ATOM  13181  O   VAL I 178     118.597 -74.204  59.157  1.00 71.31           O  
ANISOU13181  O   VAL I 178     5666   8481  12947   1751    601  -2461       O  
ATOM  13182  CB  VAL I 178     116.998 -73.881  61.772  1.00 75.20           C  
ANISOU13182  CB  VAL I 178     6257   8947  13369   1690    648  -2476       C  
ATOM  13183  CG1 VAL I 178     116.823 -75.318  61.264  1.00 73.12           C  
ANISOU13183  CG1 VAL I 178     5940   8708  13133   1703    618  -2473       C  
ATOM  13184  CG2 VAL I 178     116.799 -73.828  63.284  1.00 76.45           C  
ANISOU13184  CG2 VAL I 178     6470   9085  13493   1640    651  -2477       C  
ATOM  13185  N   PRO I 179     118.274 -71.952  59.401  1.00 68.60           N  
ANISOU13185  N   PRO I 179     5386   8112  12568   1760    666  -2471       N  
ATOM  13186  CA  PRO I 179     118.624 -71.835  57.976  1.00 68.37           C  
ANISOU13186  CA  PRO I 179     5310   8098  12570   1804    663  -2469       C  
ATOM  13187  C   PRO I 179     120.125 -72.153  57.722  1.00 68.28           C  
ANISOU13187  C   PRO I 179     5284   8081  12578   1784    613  -2454       C  
ATOM  13188  O   PRO I 179     120.526 -72.525  56.612  1.00 68.06           O  
ANISOU13188  O   PRO I 179     5209   8069  12581   1814    596  -2449       O  
ATOM  13189  CB  PRO I 179     118.305 -70.390  57.662  1.00 68.45           C  
ANISOU13189  CB  PRO I 179     5344   8099  12566   1828    708  -2478       C  
ATOM  13190  CG  PRO I 179     118.529 -69.714  58.949  1.00 68.72           C  
ANISOU13190  CG  PRO I 179     5440   8106  12566   1783    715  -2477       C  
ATOM  13191  CD  PRO I 179     117.992 -70.648  59.994  1.00 68.82           C  
ANISOU13191  CD  PRO I 179     5466   8119  12565   1752    705  -2478       C  
ATOM  13192  N   GLU I 180     120.927 -72.024  58.776  1.00 69.00           N  
ANISOU13192  N   GLU I 180     5417   8148  12652   1734    591  -2445       N  
ATOM  13193  CA  GLU I 180     122.353 -72.292  58.735  1.00 68.96           C  
ANISOU13193  CA  GLU I 180     5405   8134  12661   1709    544  -2430       C  
ATOM  13194  C   GLU I 180     122.667 -73.727  59.195  1.00 68.90           C  
ANISOU13194  C   GLU I 180     5380   8134  12666   1680    498  -2421       C  
ATOM  13195  O   GLU I 180     123.235 -74.511  58.438  1.00 68.70           O  
ANISOU13195  O   GLU I 180     5310   8122  12672   1692    465  -2414       O  
ATOM  13196  CB  GLU I 180     123.101 -71.266  59.600  1.00 69.18           C  
ANISOU13196  CB  GLU I 180     5491   8132  12663   1671    546  -2425       C  
ATOM  13197  CG  GLU I 180     124.432 -70.798  59.012  1.00 69.11           C  
ANISOU13197  CG  GLU I 180     5474   8114  12671   1670    521  -2414       C  
ATOM  13198  CD  GLU I 180     124.322 -70.404  57.535  1.00 68.90           C  
ANISOU13198  CD  GLU I 180     5405   8105  12669   1725    539  -2418       C  
ATOM  13199  OE1 GLU I 180     123.332 -69.711  57.168  1.00 68.91           O  
ANISOU13199  OE1 GLU I 180     5409   8113  12662   1759    585  -2431       O  
ATOM  13200  OE2 GLU I 180     125.218 -70.803  56.745  1.00 68.73           O  
ANISOU13200  OE2 GLU I 180     5346   8091  12676   1734    506  -2408       O  
ATOM  13201  N   ASP I 181     122.336 -74.042  60.448  1.00 68.55           N  
ANISOU13201  N   ASP I 181     5371   8077  12596   1641    496  -2422       N  
ATOM  13202  CA  ASP I 181     122.428 -75.403  60.957  1.00 68.51           C  
ANISOU13202  CA  ASP I 181     5351   8079  12599   1614    458  -2416       C  
ATOM  13203  C   ASP I 181     123.854 -75.908  60.848  1.00 68.43           C  
ANISOU13203  C   ASP I 181     5327   8064  12611   1590    405  -2399       C  
ATOM  13204  O   ASP I 181     124.060 -77.042  60.427  1.00 68.27           O  
ANISOU13204  O   ASP I 181     5264   8059  12615   1596    373  -2394       O  
ATOM  13205  CB  ASP I 181     121.462 -76.306  60.173  1.00 68.31           C  
ANISOU13205  CB  ASP I 181     5275   8084  12595   1654    465  -2423       C  
ATOM  13206  CG  ASP I 181     121.070 -77.580  60.913  1.00 68.33           C  
ANISOU13206  CG  ASP I 181     5272   8093  12596   1629    443  -2422       C  
ATOM  13207  OD1 ASP I 181     121.332 -77.716  62.136  1.00 68.52           O  
ANISOU13207  OD1 ASP I 181     5337   8099  12598   1580    428  -2417       O  
ATOM  13208  OD2 ASP I 181     120.455 -78.433  60.236  1.00 68.14           O  
ANISOU13208  OD2 ASP I 181     5204   8094  12593   1659    441  -2426       O  
ATOM  13209  N   HIS I 182     124.834 -75.056  61.181  1.00 68.56           N  
ANISOU13209  N   HIS I 182     5376   8057  12615   1566    397  -2392       N  
ATOM  13210  CA  HIS I 182     126.258 -75.454  61.249  1.00 68.52           C  
ANISOU13210  CA  HIS I 182     5366   8043  12627   1536    347  -2375       C  
ATOM  13211  C   HIS I 182     126.742 -75.576  62.687  1.00 68.76           C  
ANISOU13211  C   HIS I 182     5444   8049  12631   1476    325  -2367       C  
ATOM  13212  O   HIS I 182     126.575 -74.650  63.474  1.00 68.97           O  
ANISOU13212  O   HIS I 182     5522   8057  12627   1455    349  -2372       O  
ATOM  13213  CB  HIS I 182     127.171 -74.455  60.554  1.00 68.49           C  
ANISOU13213  CB  HIS I 182     5362   8030  12631   1549    348  -2370       C  
ATOM  13214  CG  HIS I 182     127.172 -74.537  59.065  1.00 68.23           C  
ANISOU13214  CG  HIS I 182     5275   8019  12631   1601    352  -2372       C  
ATOM  13215  ND1 HIS I 182     128.293 -74.261  58.316  1.00 68.13           N  
ANISOU13215  ND1 HIS I 182     5243   8003  12639   1608    330  -2363       N  
ATOM  13216  CD2 HIS I 182     126.190 -74.809  58.180  1.00 68.07           C  
ANISOU13216  CD2 HIS I 182     5216   8022  12624   1648    376  -2383       C  
ATOM  13217  CE1 HIS I 182     128.004 -74.372  57.033  1.00 67.90           C  
ANISOU13217  CE1 HIS I 182     5167   7996  12637   1658    340  -2367       C  
ATOM  13218  NE2 HIS I 182     126.735 -74.713  56.922  1.00 67.86           N  
ANISOU13218  NE2 HIS I 182     5149   8008  12628   1682    368  -2379       N  
ATOM  13219  N   ALA I 183     127.365 -76.695  63.035  1.00 68.72           N  
ANISOU13219  N   ALA I 183     5424   8046  12639   1447    278  -2356       N  
ATOM  13220  CA  ALA I 183     127.958 -76.802  64.360  1.00 68.93           C  
ANISOU13220  CA  ALA I 183     5496   8051  12645   1389    253  -2347       C  
ATOM  13221  C   ALA I 183     129.470 -76.654  64.285  1.00 68.93           C  
ANISOU13221  C   ALA I 183     5497   8036  12656   1366    213  -2331       C  
ATOM  13222  O   ALA I 183     130.119 -77.096  63.331  1.00 68.73           O  
ANISOU13222  O   ALA I 183     5427   8022  12664   1386    188  -2324       O  
ATOM  13223  CB  ALA I 183     127.586 -78.112  65.015  1.00 68.93           C  
ANISOU13223  CB  ALA I 183     5487   8059  12646   1366    228  -2345       C  
ATOM  13224  N   TYR I 184     130.027 -76.028  65.310  1.00 69.68           N  
ANISOU13224  N   TYR I 184     5645   8105  12725   1322    208  -2326       N  
ATOM  13225  CA  TYR I 184     131.458 -75.776  65.366  1.00 69.71           C  
ANISOU13225  CA  TYR I 184     5657   8092  12737   1296    173  -2311       C  
ATOM  13226  C   TYR I 184     132.088 -76.502  66.560  1.00 69.85           C  
ANISOU13226  C   TYR I 184     5700   8096  12745   1238    132  -2298       C  
ATOM  13227  O   TYR I 184     131.746 -76.249  67.715  1.00 70.07           O  
ANISOU13227  O   TYR I 184     5776   8108  12741   1204    143  -2301       O  
ATOM  13228  CB  TYR I 184     131.707 -74.256  65.406  1.00 69.84           C  
ANISOU13228  CB  TYR I 184     5713   8090  12733   1297    204  -2314       C  
ATOM  13229  CG  TYR I 184     131.292 -73.596  64.108  1.00 69.67           C  
ANISOU13229  CG  TYR I 184     5662   8084  12727   1354    238  -2323       C  
ATOM  13230  CD1 TYR I 184     132.077 -73.714  62.968  1.00 69.47           C  
ANISOU13230  CD1 TYR I 184     5592   8068  12734   1380    217  -2317       C  
ATOM  13231  CD2 TYR I 184     130.103 -72.894  64.010  1.00 69.72           C  
ANISOU13231  CD2 TYR I 184     5681   8094  12715   1382    290  -2339       C  
ATOM  13232  CE1 TYR I 184     131.706 -73.136  61.779  1.00 69.31           C  
ANISOU13232  CE1 TYR I 184     5545   8062  12729   1431    247  -2325       C  
ATOM  13233  CE2 TYR I 184     129.713 -72.305  62.805  1.00 69.56           C  
ANISOU13233  CE2 TYR I 184     5633   8088  12710   1434    320  -2348       C  
ATOM  13234  CZ  TYR I 184     130.525 -72.435  61.688  1.00 69.36           C  
ANISOU13234  CZ  TYR I 184     5565   8072  12717   1459    298  -2340       C  
ATOM  13235  OH  TYR I 184     130.172 -71.870  60.474  1.00 69.21           O  
ANISOU13235  OH  TYR I 184     5516   8067  12712   1511    327  -2348       O  
ATOM  13236  N   ILE I 185     132.986 -77.435  66.270  1.00 69.20           N  
ANISOU13236  N   ILE I 185     5584   8019  12691   1229     84  -2285       N  
ATOM  13237  CA  ILE I 185     133.617 -78.238  67.317  1.00 69.32           C  
ANISOU13237  CA  ILE I 185     5616   8022  12700   1176     41  -2273       C  
ATOM  13238  C   ILE I 185     135.136 -78.142  67.304  1.00 69.33           C  
ANISOU13238  C   ILE I 185     5618   8009  12714   1150     -1  -2256       C  
ATOM  13239  O   ILE I 185     135.760 -77.963  66.254  1.00 69.16           O  
ANISOU13239  O   ILE I 185     5564   7995  12720   1178     -9  -2252       O  
ATOM  13240  CB  ILE I 185     133.247 -79.722  67.201  1.00 69.18           C  
ANISOU13240  CB  ILE I 185     5557   8025  12703   1180     15  -2271       C  
ATOM  13241  CG1 ILE I 185     133.676 -80.253  65.843  1.00 68.90           C  
ANISOU13241  CG1 ILE I 185     5460   8010  12710   1219     -4  -2267       C  
ATOM  13242  CG2 ILE I 185     131.760 -79.921  67.378  1.00 69.19           C  
ANISOU13242  CG2 ILE I 185     5560   8039  12690   1199     52  -2287       C  
ATOM  13243  CD1 ILE I 185     133.796 -81.733  65.801  1.00 68.77           C  
ANISOU13243  CD1 ILE I 185     5405   8008  12718   1212    -44  -2260       C  
ATOM  13244  N   ARG I 186     135.717 -78.282  68.492  1.00 71.24           N  
ANISOU13244  N   ARG I 186     5899   8231  12938   1096    -27  -2246       N  
ATOM  13245  CA  ARG I 186     137.169 -78.259  68.674  1.00 72.39           C  
ANISOU13245  CA  ARG I 186     6052   8361  13093   1063    -70  -2228       C  
ATOM  13246  C   ARG I 186     137.682 -79.429  69.513  1.00 73.87           C  
ANISOU13246  C   ARG I 186     6240   8544  13285   1019   -118  -2215       C  
ATOM  13247  O   ARG I 186     137.035 -79.870  70.463  1.00 75.56           O  
ANISOU13247  O   ARG I 186     6478   8755  13478    993   -115  -2219       O  
ATOM  13248  CB  ARG I 186     137.604 -76.948  69.332  1.00 77.38           C  
ANISOU13248  CB  ARG I 186     6740   8966  13694   1037    -53  -2227       C  
ATOM  13249  CG  ARG I 186     137.630 -75.752  68.391  1.00 76.86           C  
ANISOU13249  CG  ARG I 186     6671   8901  13632   1076    -19  -2234       C  
ATOM  13250  CD  ARG I 186     137.453 -74.462  69.173  1.00 82.32           C  
ANISOU13250  CD  ARG I 186     7423   9570  14285   1056     14  -2240       C  
ATOM  13251  NE  ARG I 186     137.508 -73.282  68.321  1.00 82.52           N  
ANISOU13251  NE  ARG I 186     7448   9594  14312   1091     46  -2246       N  
ATOM  13252  CZ  ARG I 186     138.578 -72.510  68.220  1.00 86.76           C  
ANISOU13252  CZ  ARG I 186     8001  10115  14850   1079     35  -2237       C  
ATOM  13253  NH1 ARG I 186     139.664 -72.807  68.923  1.00 91.00           N  
ANISOU13253  NH1 ARG I 186     8555  10636  15386   1032     -8  -2222       N  
ATOM  13254  NH2 ARG I 186     138.557 -71.450  67.421  1.00 87.31           N  
ANISOU13254  NH2 ARG I 186     8068  10184  14920   1113     66  -2244       N  
ATOM  13255  N   PHE I 187     138.853 -79.927  69.144  1.00 72.73           N  
ANISOU13255  N   PHE I 187     6068   8399  13168   1009   -163  -2200       N  
ATOM  13256  CA  PHE I 187     139.535 -80.962  69.901  1.00 72.79           C  
ANISOU13256  CA  PHE I 187     6076   8399  13181    965   -213  -2186       C  
ATOM  13257  C   PHE I 187     141.053 -80.787  69.775  1.00 72.79           C  
ANISOU13257  C   PHE I 187     6075   8386  13197    944   -252  -2169       C  
ATOM  13258  O   PHE I 187     141.539 -80.327  68.737  1.00 72.65           O  
ANISOU13258  O   PHE I 187     6030   8373  13200    975   -249  -2168       O  
ATOM  13259  CB  PHE I 187     139.105 -82.315  69.391  1.00 72.59           C  
ANISOU13259  CB  PHE I 187     5998   8399  13184    986   -231  -2186       C  
ATOM  13260  CG  PHE I 187     139.017 -82.376  67.902  1.00 72.32           C  
ANISOU13260  CG  PHE I 187     5910   8387  13183   1042   -221  -2192       C  
ATOM  13261  CD1 PHE I 187     137.798 -82.250  67.263  1.00 72.21           C  
ANISOU13261  CD1 PHE I 187     5877   8392  13169   1087   -179  -2208       C  
ATOM  13262  CD2 PHE I 187     140.153 -82.543  67.136  1.00 72.19           C  
ANISOU13262  CD2 PHE I 187     5860   8371  13197   1049   -254  -2180       C  
ATOM  13263  CE1 PHE I 187     137.718 -82.305  65.885  1.00 71.97           C  
ANISOU13263  CE1 PHE I 187     5796   8381  13168   1138   -171  -2213       C  
ATOM  13264  CE2 PHE I 187     140.080 -82.592  65.763  1.00 71.95           C  
ANISOU13264  CE2 PHE I 187     5779   8360  13197   1100   -245  -2184       C  
ATOM  13265  CZ  PHE I 187     138.871 -82.472  65.135  1.00 71.83           C  
ANISOU13265  CZ  PHE I 187     5747   8365  13182   1144   -204  -2201       C  
ATOM  13266  N   PRO I 188     141.813 -81.148  70.825  1.00 77.45           N  
ANISOU13266  N   PRO I 188     6692   8958  13777    890   -289  -2155       N  
ATOM  13267  CA  PRO I 188     143.283 -81.058  70.774  1.00 79.67           C  
ANISOU13267  CA  PRO I 188     6972   9226  14074    867   -330  -2138       C  
ATOM  13268  C   PRO I 188     143.890 -82.133  69.909  1.00 75.95           C  
ANISOU13268  C   PRO I 188     6441   8771  13646    884   -369  -2128       C  
ATOM  13269  O   PRO I 188     143.376 -83.241  69.938  1.00 73.17           O  
ANISOU13269  O   PRO I 188     6062   8434  13305    887   -381  -2130       O  
ATOM  13270  CB  PRO I 188     143.703 -81.261  72.232  1.00 84.96           C  
ANISOU13270  CB  PRO I 188     7689   9874  14719    804   -356  -2127       C  
ATOM  13271  CG  PRO I 188     142.621 -82.075  72.813  1.00 84.13           C  
ANISOU13271  CG  PRO I 188     7586   9779  14602    799   -348  -2135       C  
ATOM  13272  CD  PRO I 188     141.341 -81.612  72.139  1.00 80.67           C  
ANISOU13272  CD  PRO I 188     7137   9357  14158    848   -295  -2155       C  
ATOM  13273  N   VAL I 189     144.933 -81.834  69.147  1.00 76.56           N  
ANISOU13273  N   VAL I 189     6496   8846  13746    895   -387  -2119       N  
ATOM  13274  CA  VAL I 189     145.666 -82.894  68.462  1.00 76.22           C  
ANISOU13274  CA  VAL I 189     6401   8816  13744    903   -430  -2108       C  
ATOM  13275  C   VAL I 189     147.165 -82.800  68.796  1.00 76.49           C  
ANISOU13275  C   VAL I 189     6447   8831  13786    865   -473  -2089       C  
ATOM  13276  O   VAL I 189     147.749 -81.702  68.910  1.00 76.76           O  
ANISOU13276  O   VAL I 189     6512   8847  13805    854   -464  -2087       O  
ATOM  13277  CB  VAL I 189     145.439 -82.870  66.926  1.00 75.66           C  
ANISOU13277  CB  VAL I 189     6276   8768  13704    963   -413  -2116       C  
ATOM  13278  CG1 VAL I 189     144.053 -82.357  66.601  1.00 75.50           C  
ANISOU13278  CG1 VAL I 189     6259   8759  13667   1001   -359  -2136       C  
ATOM  13279  CG2 VAL I 189     146.471 -82.033  66.221  1.00 75.64           C  
ANISOU13279  CG2 VAL I 189     6268   8756  13714    974   -418  -2110       C  
ATOM  13280  N   SER I 190     147.776 -83.964  69.003  1.00 75.67           N  
ANISOU13280  N   SER I 190     6319   8729  13703    842   -521  -2076       N  
ATOM  13281  CA  SER I 190     149.179 -84.028  69.376  1.00 78.87           C  
ANISOU13281  CA  SER I 190     6734   9117  14117    804   -566  -2057       C  
ATOM  13282  C   SER I 190     150.035 -83.617  68.195  1.00 78.28           C  
ANISOU13282  C   SER I 190     6625   9045  14072    834   -573  -2053       C  
ATOM  13283  O   SER I 190     149.767 -84.052  67.068  1.00 75.33           O  
ANISOU13283  O   SER I 190     6201   8694  13728    878   -568  -2058       O  
ATOM  13284  CB  SER I 190     149.553 -85.434  69.842  1.00 79.35           C  
ANISOU13284  CB  SER I 190     6774   9180  14195    775   -615  -2044       C  
ATOM  13285  OG  SER I 190     149.183 -85.632  71.195  1.00 81.81           O  
ANISOU13285  OG  SER I 190     7129   9479  14475    731   -618  -2043       O  
ATOM  13286  N   ASP I 191     151.064 -82.796  68.468  1.00 76.52           N  
ANISOU13286  N   ASP I 191     6431   8802  13841    809   -584  -2043       N  
ATOM  13287  CA  ASP I 191     152.013 -82.313  67.454  1.00 77.08           C  
ANISOU13287  CA  ASP I 191     6476   8874  13938    831   -593  -2037       C  
ATOM  13288  C   ASP I 191     152.520 -83.506  66.654  1.00 73.88           C  
ANISOU13288  C   ASP I 191     6010   8485  13576    847   -631  -2029       C  
ATOM  13289  O   ASP I 191     152.968 -84.500  67.231  1.00 73.57           O  
ANISOU13289  O   ASP I 191     5964   8442  13546    815   -672  -2016       O  
ATOM  13290  CB  ASP I 191     153.192 -81.568  68.107  1.00 83.45           C  
ANISOU13290  CB  ASP I 191     7322   9653  14731    789   -613  -2023       C  
ATOM  13291  CG  ASP I 191     153.100 -80.037  67.970  1.00 86.97           C  
ANISOU13291  CG  ASP I 191     7803  10088  15153    801   -572  -2031       C  
ATOM  13292  OD1 ASP I 191     152.005 -79.500  67.701  1.00 84.54           O  
ANISOU13292  OD1 ASP I 191     7502   9789  14829    832   -526  -2048       O  
ATOM  13293  OD2 ASP I 191     154.135 -79.360  68.151  1.00 92.58           O  
ANISOU13293  OD2 ASP I 191     8535  10780  15860    778   -587  -2021       O  
ATOM  13294  N   GLY I 192     152.423 -83.420  65.331  1.00 78.73           N  
ANISOU13294  N   GLY I 192     6580   9118  14217    897   -616  -2035       N  
ATOM  13295  CA  GLY I 192     152.858 -84.510  64.473  1.00 76.30           C  
ANISOU13295  CA  GLY I 192     6213   8827  13952    917   -649  -2029       C  
ATOM  13296  C   GLY I 192     151.755 -85.354  63.846  1.00 72.87           C  
ANISOU13296  C   GLY I 192     5737   8418  13532    956   -633  -2041       C  
ATOM  13297  O   GLY I 192     152.015 -86.095  62.888  1.00 72.66           O  
ANISOU13297  O   GLY I 192     5657   8409  13542    983   -651  -2039       O  
ATOM  13298  N   THR I 193     150.540 -85.252  64.386  1.00 71.95           N  
ANISOU13298  N   THR I 193     5645   8305  13387    958   -600  -2054       N  
ATOM  13299  CA  THR I 193     149.367 -85.935  63.841  1.00 71.79           C  
ANISOU13299  CA  THR I 193     5591   8310  13376    995   -579  -2068       C  
ATOM  13300  C   THR I 193     149.060 -85.534  62.405  1.00 71.57           C  
ANISOU13300  C   THR I 193     5523   8300  13369   1053   -551  -2078       C  
ATOM  13301  O   THR I 193     149.159 -84.374  62.047  1.00 71.59           O  
ANISOU13301  O   THR I 193     5543   8296  13361   1069   -523  -2083       O  
ATOM  13302  CB  THR I 193     148.117 -85.647  64.703  1.00 71.94           C  
ANISOU13302  CB  THR I 193     5650   8326  13357    987   -543  -2080       C  
ATOM  13303  OG1 THR I 193     148.357 -86.059  66.055  1.00 72.15           O  
ANISOU13303  OG1 THR I 193     5713   8336  13363    932   -569  -2071       O  
ATOM  13304  CG2 THR I 193     146.884 -86.361  64.163  1.00 71.77           C  
ANISOU13304  CG2 THR I 193     5594   8331  13345   1025   -521  -2094       C  
ATOM  13305  N   GLN I 194     148.690 -86.501  61.580  1.00 71.74           N  
ANISOU13305  N   GLN I 194     5492   8345  13420   1086   -558  -2082       N  
ATOM  13306  CA  GLN I 194     148.178 -86.207  60.249  1.00 71.28           C  
ANISOU13306  CA  GLN I 194     5396   8307  13379   1143   -527  -2094       C  
ATOM  13307  C   GLN I 194     146.842 -86.913  60.028  1.00 70.97           C  
ANISOU13307  C   GLN I 194     5334   8290  13340   1171   -505  -2108       C  
ATOM  13308  O   GLN I 194     145.851 -86.278  59.684  1.00 70.85           O  
ANISOU13308  O   GLN I 194     5325   8283  13311   1202   -460  -2123       O  
ATOM  13309  CB  GLN I 194     149.178 -86.570  59.155  1.00 70.96           C  
ANISOU13309  CB  GLN I 194     5306   8274  13380   1163   -556  -2085       C  
ATOM  13310  CG  GLN I 194     149.398 -85.415  58.181  1.00 70.82           C  
ANISOU13310  CG  GLN I 194     5284   8257  13366   1198   -528  -2091       C  
ATOM  13311  CD  GLN I 194     150.270 -85.760  56.970  1.00 70.45           C  
ANISOU13311  CD  GLN I 194     5185   8222  13361   1224   -552  -2084       C  
ATOM  13312  OE1 GLN I 194     150.907 -86.822  56.909  1.00 70.35           O  
ANISOU13312  OE1 GLN I 194     5142   8213  13375   1211   -594  -2073       O  
ATOM  13313  NE2 GLN I 194     150.302 -84.850  55.995  1.00 70.26           N  
ANISOU13313  NE2 GLN I 194     5150   8202  13343   1261   -524  -2091       N  
ATOM  13314  N   GLU I 195     146.828 -88.233  60.154  1.00 75.22           N  
ANISOU13314  N   GLU I 195     8004   8385  12191    626   -142    265       N  
ATOM  13315  CA  GLU I 195     145.584 -89.002  60.035  1.00 73.27           C  
ANISOU13315  CA  GLU I 195     7771   8105  11964    635   -181    345       C  
ATOM  13316  C   GLU I 195     144.665 -88.858  61.250  1.00 72.86           C  
ANISOU13316  C   GLU I 195     7730   8029  11924    640   -166    404       C  
ATOM  13317  O   GLU I 195     145.134 -88.747  62.382  1.00 74.53           O  
ANISOU13317  O   GLU I 195     7941   8252  12126    649   -157    375       O  
ATOM  13318  CB  GLU I 195     145.892 -90.488  59.828  1.00 74.16           C  
ANISOU13318  CB  GLU I 195     7885   8222  12071    660   -265    326       C  
ATOM  13319  CG  GLU I 195     146.504 -90.815  58.490  1.00 74.50           C  
ANISOU13319  CG  GLU I 195     7920   8281  12106    656   -289    287       C  
ATOM  13320  CD  GLU I 195     146.222 -92.241  58.065  1.00 75.42           C  
ANISOU13320  CD  GLU I 195     8043   8387  12227    676   -369    305       C  
ATOM  13321  OE1 GLU I 195     145.656 -93.020  58.888  1.00 75.20           O  
ANISOU13321  OE1 GLU I 195     8025   8342  12205    695   -408    343       O  
ATOM  13322  OE2 GLU I 195     146.561 -92.576  56.900  1.00 76.69           O  
ANISOU13322  OE2 GLU I 195     8198   8556  12384    673   -393    283       O  
ATOM  13323  N   LEU I 196     143.357 -88.886  61.018  1.00 68.10           N  
ANISOU13323  N   LEU I 196     7138   7392  11343    635   -165    487       N  
ATOM  13324  CA  LEU I 196     142.409 -88.911  62.122  1.00 68.08           C  
ANISOU13324  CA  LEU I 196     7148   7365  11354    642   -160    548       C  
ATOM  13325  C   LEU I 196     141.226 -89.850  61.856  1.00 67.99           C  
ANISOU13325  C   LEU I 196     7149   7321  11362    652   -210    624       C  
ATOM  13326  O   LEU I 196     140.728 -89.952  60.728  1.00 67.75           O  
ANISOU13326  O   LEU I 196     7121   7279  11342    643   -218    655       O  
ATOM  13327  CB  LEU I 196     141.915 -87.501  62.410  1.00 67.79           C  
ANISOU13327  CB  LEU I 196     7112   7319  11326    618    -80    578       C  
ATOM  13328  CG  LEU I 196     142.769 -86.668  63.366  1.00 67.96           C  
ANISOU13328  CG  LEU I 196     7126   7364  11333    615    -33    524       C  
ATOM  13329  CD1 LEU I 196     142.242 -85.249  63.500  1.00 67.66           C  
ANISOU13329  CD1 LEU I 196     7087   7315  11304    590     48    556       C  
ATOM  13330  CD2 LEU I 196     142.835 -87.321  64.727  1.00 68.49           C  
ANISOU13330  CD2 LEU I 196     7199   7430  11394    637    -64    521       C  
ATOM  13331  N   LYS I 197     140.776 -90.532  62.905  1.00 70.96           N  
ANISOU13331  N   LYS I 197     7535   7684  11742    671   -242    654       N  
ATOM  13332  CA  LYS I 197     139.666 -91.492  62.810  1.00 70.52           C  
ANISOU13332  CA  LYS I 197     7492   7598  11704    684   -292    725       C  
ATOM  13333  C   LYS I 197     138.323 -90.882  63.241  1.00 69.82           C  
ANISOU13333  C   LYS I 197     7415   7477  11638    673   -253    810       C  
ATOM  13334  O   LYS I 197     138.216 -90.358  64.357  1.00 70.93           O  
ANISOU13334  O   LYS I 197     7558   7615  11778    673   -220    817       O  
ATOM  13335  CB  LYS I 197     139.974 -92.708  63.684  1.00 72.64           C  
ANISOU13335  CB  LYS I 197     7765   7871  11965    713   -357    707       C  
ATOM  13336  CG  LYS I 197     139.038 -93.890  63.521  1.00 73.31           C  
ANISOU13336  CG  LYS I 197     7861   7929  12064    729   -420    768       C  
ATOM  13337  CD  LYS I 197     139.367 -94.967  64.552  1.00 75.91           C  
ANISOU13337  CD  LYS I 197     8195   8264  12385    757   -477    749       C  
ATOM  13338  CE  LYS I 197     138.463 -96.176  64.427  1.00 76.96           C  
ANISOU13338  CE  LYS I 197     8339   8371  12531    774   -542    807       C  
ATOM  13339  NZ  LYS I 197     138.661 -97.086  65.584  1.00 79.61           N  
ANISOU13339  NZ  LYS I 197     8680   8709  12860    800   -588    797       N  
ATOM  13340  N   ILE I 198     137.295 -90.942  62.393  1.00 67.56           N  
ANISOU13340  N   ILE I 198     7135   7164  11371    664   -257    875       N  
ATOM  13341  CA  ILE I 198     135.986 -90.420  62.804  1.00 67.19           C  
ANISOU13341  CA  ILE I 198     7099   7085  11346    655   -223    958       C  
ATOM  13342  C   ILE I 198     134.908 -91.490  62.808  1.00 67.87           C  
ANISOU13342  C   ILE I 198     7199   7141  11449    670   -279   1028       C  
ATOM  13343  O   ILE I 198     134.529 -92.011  61.753  1.00 67.41           O  
ANISOU13343  O   ILE I 198     7142   7072  11399    669   -311   1052       O  
ATOM  13344  CB  ILE I 198     135.480 -89.271  61.904  1.00 65.35           C  
ANISOU13344  CB  ILE I 198     6864   6842  11124    626   -162    989       C  
ATOM  13345  CG1 ILE I 198     136.416 -88.069  61.935  1.00 64.97           C  
ANISOU13345  CG1 ILE I 198     6804   6821  11061    609    -98    928       C  
ATOM  13346  CG2 ILE I 198     134.144 -88.803  62.386  1.00 65.29           C  
ANISOU13346  CG2 ILE I 198     6868   6802  11139    618   -131   1073       C  
ATOM  13347  CD1 ILE I 198     135.946 -86.957  61.020  1.00 63.53           C  
ANISOU13347  CD1 ILE I 198     6619   6629  10890    580    -39    956       C  
ATOM  13348  N   VAL I 199     134.408 -91.800  64.002  1.00 66.54           N  
ANISOU13348  N   VAL I 199     7039   6959  11286    684   -290   1061       N  
ATOM  13349  CA  VAL I 199     133.234 -92.656  64.162  1.00 67.55           C  
ANISOU13349  CA  VAL I 199     7180   7055  11432    696   -334   1137       C  
ATOM  13350  C   VAL I 199     131.987 -91.778  64.292  1.00 66.89           C  
ANISOU13350  C   VAL I 199     7104   6941  11369    679   -281   1215       C  
ATOM  13351  O   VAL I 199     131.798 -91.109  65.309  1.00 67.58           O  
ANISOU13351  O   VAL I 199     7195   7025  11458    676   -239   1227       O  
ATOM  13352  CB  VAL I 199     133.373 -93.561  65.403  1.00 70.48           C  
ANISOU13352  CB  VAL I 199     7556   7426  11796    723   -379   1130       C  
ATOM  13353  CG1 VAL I 199     132.236 -94.542  65.497  1.00 71.96           C  
ANISOU13353  CG1 VAL I 199     7758   7583  12002    737   -430   1203       C  
ATOM  13354  CG2 VAL I 199     134.682 -94.296  65.349  1.00 72.23           C  
ANISOU13354  CG2 VAL I 199     7770   7680  11995    738   -424   1047       C  
ATOM  13355  N   SER I 200     131.128 -91.796  63.279  1.00 64.99           N  
ANISOU13355  N   SER I 200     6869   6680  11146    668   -284   1269       N  
ATOM  13356  CA  SER I 200     129.976 -90.900  63.266  1.00 64.16           C  
ANISOU13356  CA  SER I 200     6770   6547  11062    650   -231   1342       C  
ATOM  13357  C   SER I 200     128.640 -91.581  62.950  1.00 65.25           C  
ANISOU13357  C   SER I 200     6921   6649  11222    655   -267   1427       C  
ATOM  13358  O   SER I 200     128.624 -92.728  62.513  1.00 66.73           O  
ANISOU13358  O   SER I 200     7111   6833  11409    670   -332   1429       O  
ATOM  13359  CB  SER I 200     130.218 -89.759  62.265  1.00 61.87           C  
ANISOU13359  CB  SER I 200     6472   6266  10771    622   -173   1324       C  
ATOM  13360  OG  SER I 200     130.944 -90.231  61.134  1.00 61.36           O  
ANISOU13360  OG  SER I 200     6398   6219  10696    623   -206   1278       O  
ATOM  13361  N   SER I 201     127.527 -90.876  63.187  1.00 63.30           N  
ANISOU13361  N   SER I 201     6681   6375  10994    641   -224   1497       N  
ATOM  13362  CA  SER I 201     126.208 -91.330  62.736  1.00 63.21           C  
ANISOU13362  CA  SER I 201     6681   6329  11006    642   -247   1582       C  
ATOM  13363  C   SER I 201     125.217 -90.198  62.463  1.00 63.12           C  
ANISOU13363  C   SER I 201     6673   6295  11013    617   -183   1643       C  
ATOM  13364  O   SER I 201     125.219 -89.180  63.153  1.00 63.11           O  
ANISOU13364  O   SER I 201     6671   6297  11012    606   -124   1642       O  
ATOM  13365  CB  SER I 201     125.596 -92.275  63.760  1.00 63.20           C  
ANISOU13365  CB  SER I 201     6692   6311  11012    664   -293   1623       C  
ATOM  13366  OG  SER I 201     125.230 -91.575  64.931  1.00 63.19           O  
ANISOU13366  OG  SER I 201     6694   6301  11015    661   -249   1646       O  
ATOM  13367  N   THR I 202     124.348 -90.395  61.472  1.00 60.18           N  
ANISOU13367  N   THR I 202     6307   5901  10659    610   -196   1698       N  
ATOM  13368  CA  THR I 202     123.314 -89.418  61.135  1.00 60.09           C  
ANISOU13368  CA  THR I 202     6300   5865  10667    587   -141   1763       C  
ATOM  13369  C   THR I 202     121.887 -90.002  61.227  1.00 60.01           C  
ANISOU13369  C   THR I 202     6304   5817  10681    594   -169   1855       C  
ATOM  13370  O   THR I 202     121.568 -91.005  60.593  1.00 60.00           O  
ANISOU13370  O   THR I 202     6306   5805  10685    605   -226   1876       O  
ATOM  13371  CB  THR I 202     123.538 -88.819  59.709  1.00 60.07           C  
ANISOU13371  CB  THR I 202     6289   5870  10664    566   -115   1747       C  
ATOM  13372  OG1 THR I 202     123.051 -89.698  58.690  1.00 60.03           O  
ANISOU13372  OG1 THR I 202     6288   5851  10670    571   -167   1778       O  
ATOM  13373  CG2 THR I 202     124.988 -88.566  59.474  1.00 60.15           C  
ANISOU13373  CG2 THR I 202     6286   5918  10651    564   -106   1654       C  
ATOM  13374  N   GLN I 203     121.033 -89.341  62.009  1.00 63.27           N  
ANISOU13374  N   GLN I 203     6723   6210  11107    587   -127   1909       N  
ATOM  13375  CA  GLN I 203     119.625 -89.726  62.190  1.00 65.66           C  
ANISOU13375  CA  GLN I 203     7040   6476  11433    591   -143   1999       C  
ATOM  13376  C   GLN I 203     118.648 -88.550  62.073  1.00 64.99           C  
ANISOU13376  C   GLN I 203     6958   6369  11367    567    -76   2060       C  
ATOM  13377  O   GLN I 203     118.767 -87.585  62.809  1.00 64.46           O  
ANISOU13377  O   GLN I 203     6889   6306  11296    558    -20   2051       O  
ATOM  13378  CB  GLN I 203     119.444 -90.387  63.560  1.00 68.31           C  
ANISOU13378  CB  GLN I 203     7382   6805  11767    613   -173   2012       C  
ATOM  13379  CG  GLN I 203     118.076 -90.129  64.199  1.00 70.84           C  
ANISOU13379  CG  GLN I 203     7715   7091  12110    610   -152   2100       C  
ATOM  13380  CD  GLN I 203     118.019 -90.527  65.667  1.00 73.67           C  
ANISOU13380  CD  GLN I 203     8080   7448  12465    629   -167   2105       C  
ATOM  13381  OE1 GLN I 203     118.343 -89.726  66.556  1.00 73.60           O  
ANISOU13381  OE1 GLN I 203     8067   7448  12448    624   -120   2083       O  
ATOM  13382  NE2 GLN I 203     117.598 -91.766  65.930  1.00 76.64           N  
ANISOU13382  NE2 GLN I 203     8464   7810  12847    651   -233   2133       N  
ATOM  13383  N   ILE I 204     117.675 -88.638  61.173  1.00 63.59           N  
ANISOU13383  N   ILE I 204     6667   6435  11060     33   1453    486       N  
ATOM  13384  CA  ILE I 204     116.682 -87.570  61.035  1.00 63.45           C  
ANISOU13384  CA  ILE I 204     6629   6408  11073     12   1521    473       C  
ATOM  13385  C   ILE I 204     115.517 -87.760  62.004  1.00 63.91           C  
ANISOU13385  C   ILE I 204     6720   6455  11108      2   1582    517       C  
ATOM  13386  O   ILE I 204     114.773 -88.740  61.905  1.00 63.99           O  
ANISOU13386  O   ILE I 204     6735   6436  11143      1   1590    571       O  
ATOM  13387  CB  ILE I 204     116.096 -87.490  59.618  1.00 62.87           C  
ANISOU13387  CB  ILE I 204     6501   6299  11088      2   1530    476       C  
ATOM  13388  CG1 ILE I 204     117.164 -87.747  58.562  1.00 62.43           C  
ANISOU13388  CG1 ILE I 204     6414   6245  11062     16   1461    450       C  
ATOM  13389  CG2 ILE I 204     115.447 -86.144  59.422  1.00 62.68           C  
ANISOU13389  CG2 ILE I 204     6452   6275  11087    -17   1589    445       C  
ATOM  13390  CD1 ILE I 204     116.623 -87.811  57.171  1.00 61.88           C  
ANISOU13390  CD1 ILE I 204     6293   6139  11078      8   1464    457       C  
ATOM  13391  N   ASP I 205     115.343 -86.814  62.922  1.00 66.42           N  
ANISOU13391  N   ASP I 205     7060   6796  11379     -6   1626    495       N  
ATOM  13392  CA  ASP I 205     114.317 -86.923  63.963  1.00 70.16           C  
ANISOU13392  CA  ASP I 205     7570   7266  11823    -15   1684    534       C  
ATOM  13393  C   ASP I 205     114.408 -88.251  64.738  1.00 73.97           C  
ANISOU13393  C   ASP I 205     8096   7747  12264      0   1659    584       C  
ATOM  13394  O   ASP I 205     115.410 -88.523  65.389  1.00 73.72           O  
ANISOU13394  O   ASP I 205     8095   7743  12173     15   1616    571       O  
ATOM  13395  CB  ASP I 205     112.927 -86.745  63.344  1.00 71.73           C  
ANISOU13395  CB  ASP I 205     7738   7428  12088    -34   1742    561       C  
ATOM  13396  CG  ASP I 205     112.785 -85.425  62.610  1.00 68.64           C  
ANISOU13396  CG  ASP I 205     7306   7038  11736    -48   1770    513       C  
ATOM  13397  OD1 ASP I 205     113.221 -84.406  63.175  1.00 68.01           O  
ANISOU13397  OD1 ASP I 205     7238   6988  11614    -49   1784    470       O  
ATOM  13398  OD2 ASP I 205     112.260 -85.405  61.475  1.00 67.25           O  
ANISOU13398  OD2 ASP I 205     7086   6833  11634    -56   1778    519       O  
ATOM  13399  N   ASP I 206     113.359 -89.062  64.688  1.00 74.20           N  
ANISOU13399  N   ASP I 206     8127   7742  12322     -6   1686    640       N  
ATOM  13400  CA  ASP I 206     113.347 -90.353  65.386  1.00 78.42           C  
ANISOU13400  CA  ASP I 206     8702   8272  12823      6   1665    691       C  
ATOM  13401  C   ASP I 206     113.684 -91.534  64.496  1.00 79.68           C  
ANISOU13401  C   ASP I 206     8843   8407  13023     17   1609    717       C  
ATOM  13402  O   ASP I 206     113.715 -92.669  64.960  1.00 83.78           O  
ANISOU13402  O   ASP I 206     9393   8920  13519     28   1587    760       O  
ATOM  13403  CB  ASP I 206     111.981 -90.589  66.024  1.00 83.07           C  
ANISOU13403  CB  ASP I 206     9310   8840  13412     -7   1731    742       C  
ATOM  13404  CG  ASP I 206     111.652 -89.534  67.066  1.00 82.49           C  
ANISOU13404  CG  ASP I 206     9263   8792  13289    -15   1787    721       C  
ATOM  13405  OD1 ASP I 206     112.631 -89.093  67.742  1.00 80.01           O  
ANISOU13405  OD1 ASP I 206     8973   8515  12913     -4   1763    684       O  
ATOM  13406  OD2 ASP I 206     110.445 -89.145  67.187  1.00 84.85           O  
ANISOU13406  OD2 ASP I 206     9555   9073  13610    -32   1853    742       O  
ATOM  13407  N   GLY I 207     113.966 -91.258  63.228  1.00 74.25           N  
ANISOU13407  N   GLY I 207     8108   7708  12396     15   1584    690       N  
ATOM  13408  CA  GLY I 207     114.025 -92.296  62.218  1.00 75.81           C  
ANISOU13408  CA  GLY I 207     8281   7875  12647     21   1541    717       C  
ATOM  13409  C   GLY I 207     115.247 -93.187  62.269  1.00 75.60           C  
ANISOU13409  C   GLY I 207     8273   7863  12588     45   1466    716       C  
ATOM  13410  O   GLY I 207     115.912 -93.310  63.303  1.00 75.50           O  
ANISOU13410  O   GLY I 207     8301   7880  12504     57   1449    711       O  
ATOM  13411  N   GLU I 208     115.513 -93.842  61.144  1.00 75.91           N  
ANISOU13411  N   GLU I 208     8281   7879  12681     51   1422    723       N  
ATOM  13412  CA  GLU I 208     116.673 -94.708  60.990  1.00 76.16           C  
ANISOU13412  CA  GLU I 208     8323   7921  12692     74   1348    722       C  
ATOM  13413  C   GLU I 208     118.003 -93.982  61.273  1.00 71.64           C  
ANISOU13413  C   GLU I 208     7756   7392  12071     86   1311    664       C  
ATOM  13414  O   GLU I 208     118.319 -92.938  60.685  1.00 67.45           O  
ANISOU13414  O   GLU I 208     7192   6873  11562     80   1313    615       O  
ATOM  13415  CB  GLU I 208     116.685 -95.291  59.572  1.00 77.41           C  
ANISOU13415  CB  GLU I 208     8439   8047  12926     77   1312    731       C  
ATOM  13416  CG  GLU I 208     117.718 -96.384  59.327  1.00 83.04           C  
ANISOU13416  CG  GLU I 208     9163   8763  13627    100   1237    741       C  
ATOM  13417  CD  GLU I 208     117.164 -97.784  59.580  1.00 86.54           C  
ANISOU13417  CD  GLU I 208     9631   9178  14071    105   1231    805       C  
ATOM  13418  OE1 GLU I 208     115.943 -97.909  59.853  1.00 85.03           O  
ANISOU13418  OE1 GLU I 208     9446   8963  13898     89   1286    843       O  
ATOM  13419  OE2 GLU I 208     117.951 -98.758  59.505  1.00 91.14           O  
ANISOU13419  OE2 GLU I 208    10229   9762  14639    125   1173    818       O  
ATOM  13420  N   GLU I 209     118.784 -94.547  62.181  1.00 73.17           N  
ANISOU13420  N   GLU I 209     7993   7611  12198    103   1276    671       N  
ATOM  13421  CA  GLU I 209     120.123 -94.041  62.463  1.00 69.58           C  
ANISOU13421  CA  GLU I 209     7546   7198  11695    117   1232    620       C  
ATOM  13422  C   GLU I 209     121.114 -94.628  61.460  1.00 68.15           C  
ANISOU13422  C   GLU I 209     7339   7013  11542    134   1161    609       C  
ATOM  13423  O   GLU I 209     121.206 -95.844  61.322  1.00 71.22           O  
ANISOU13423  O   GLU I 209     7739   7385  11935    147   1126    648       O  
ATOM  13424  CB  GLU I 209     120.527 -94.391  63.900  1.00 72.12           C  
ANISOU13424  CB  GLU I 209     7925   7549  11930    129   1226    632       C  
ATOM  13425  CG  GLU I 209     121.962 -94.076  64.271  1.00 69.39           C  
ANISOU13425  CG  GLU I 209     7592   7246  11528    146   1175    587       C  
ATOM  13426  CD  GLU I 209     122.151 -93.992  65.785  1.00 72.26           C  
ANISOU13426  CD  GLU I 209     8009   7641  11806    151   1189    590       C  
ATOM  13427  OE1 GLU I 209     121.144 -93.855  66.507  1.00 75.69           O  
ANISOU13427  OE1 GLU I 209     8466   8067  12227    139   1247    616       O  
ATOM  13428  OE2 GLU I 209     123.304 -94.057  66.265  1.00 71.48           O  
ANISOU13428  OE2 GLU I 209     7931   7576  11652    168   1142    566       O  
ATOM  13429  N   THR I 210     121.839 -93.779  60.742  1.00 64.91           N  
ANISOU13429  N   THR I 210     6893   6618  11150    134   1139    556       N  
ATOM  13430  CA  THR I 210     122.818 -94.292  59.798  1.00 64.36           C  
ANISOU13430  CA  THR I 210     6800   6547  11106    151   1071    542       C  
ATOM  13431  C   THR I 210     124.215 -94.214  60.393  1.00 64.56           C  
ANISOU13431  C   THR I 210     6848   6616  11066    170   1019    509       C  
ATOM  13432  O   THR I 210     124.768 -93.131  60.555  1.00 64.34           O  
ANISOU13432  O   THR I 210     6813   6618  11017    166   1023    458       O  
ATOM  13433  CB  THR I 210     122.799 -93.525  58.480  1.00 63.45           C  
ANISOU13433  CB  THR I 210     6628   6419  11060    142   1072    507       C  
ATOM  13434  OG1 THR I 210     121.531 -93.681  57.849  1.00 63.24           O  
ANISOU13434  OG1 THR I 210     6579   6351  11098    126   1115    540       O  
ATOM  13435  CG2 THR I 210     123.858 -94.051  57.557  1.00 63.00           C  
ANISOU13435  CG2 THR I 210     6548   6363  11025    161   1001    493       C  
ATOM  13436  N   ASN I 211     124.790 -95.364  60.720  1.00 65.70           N  
ANISOU13436  N   ASN I 211     7021   6763  11178    190    971    537       N  
ATOM  13437  CA  ASN I 211     126.102 -95.380  61.330  1.00 66.05           C  
ANISOU13437  CA  ASN I 211     7089   6849  11158    209    921    509       C  
ATOM  13438  C   ASN I 211     127.161 -95.331  60.264  1.00 65.18           C  
ANISOU13438  C   ASN I 211     6942   6746  11078    222    862    475       C  
ATOM  13439  O   ASN I 211     127.062 -96.050  59.264  1.00 64.96           O  
ANISOU13439  O   ASN I 211     6889   6688  11104    228    837    496       O  
ATOM  13440  CB  ASN I 211     126.281 -96.616  62.199  1.00 67.49           C  
ANISOU13440  CB  ASN I 211     7320   7034  11290    227    896    554       C  
ATOM  13441  CG  ASN I 211     125.471 -96.547  63.476  1.00 68.40           C  
ANISOU13441  CG  ASN I 211     7477   7153  11357    217    951    580       C  
ATOM  13442  OD1 ASN I 211     125.904 -95.946  64.469  1.00 68.65           O  
ANISOU13442  OD1 ASN I 211     7538   7221  11326    218    959    555       O  
ATOM  13443  ND2 ASN I 211     124.284 -97.159  63.460  1.00 70.24           N  
ANISOU13443  ND2 ASN I 211     7717   7350  11621    207    989    632       N  
ATOM  13444  N   TYR I 212     128.149 -94.457  60.472  1.00 64.54           N  
ANISOU13444  N   TYR I 212     6858   6703  10962    226    842    422       N  
ATOM  13445  CA  TYR I 212     129.320 -94.359  59.612  1.00 64.17           C  
ANISOU13445  CA  TYR I 212     6779   6670  10932    240    782    385       C  
ATOM  13446  C   TYR I 212     130.512 -94.847  60.403  1.00 64.54           C  
ANISOU13446  C   TYR I 212     6862   6754  10908    262    728    378       C  
ATOM  13447  O   TYR I 212     131.010 -94.164  61.284  1.00 64.84           O  
ANISOU13447  O   TYR I 212     6921   6828  10888    261    733    347       O  
ATOM  13448  CB  TYR I 212     129.507 -92.928  59.135  1.00 63.82           C  
ANISOU13448  CB  TYR I 212     6699   6641  10910    225    801    327       C  
ATOM  13449  CG  TYR I 212     128.505 -92.529  58.082  1.00 63.35           C  
ANISOU13449  CG  TYR I 212     6597   6544  10930    207    842    331       C  
ATOM  13450  CD1 TYR I 212     128.785 -92.701  56.741  1.00 62.81           C  
ANISOU13450  CD1 TYR I 212     6484   6457  10925    213    809    323       C  
ATOM  13451  CD2 TYR I 212     127.269 -92.006  58.424  1.00 63.45           C  
ANISOU13451  CD2 TYR I 212     6613   6540  10955    185    912    345       C  
ATOM  13452  CE1 TYR I 212     127.875 -92.352  55.758  1.00 62.38           C  
ANISOU13452  CE1 TYR I 212     6390   6369  10944    197    844    326       C  
ATOM  13453  CE2 TYR I 212     126.331 -91.653  57.439  1.00 63.01           C  
ANISOU13453  CE2 TYR I 212     6517   6451  10974    168    949    349       C  
ATOM  13454  CZ  TYR I 212     126.641 -91.832  56.106  1.00 62.48           C  
ANISOU13454  CZ  TYR I 212     6406   6365  10968    174    915    340       C  
ATOM  13455  OH  TYR I 212     125.726 -91.488  55.123  1.00 62.05           O  
ANISOU13455  OH  TYR I 212     6312   6278  10987    159    950    344       O  
ATOM  13456  N   ASP I 213     130.976 -96.037  60.061  1.00 70.28           N  
ANISOU13456  N   ASP I 213     7594   7470  11640    283    676    407       N  
ATOM  13457  CA  ASP I 213     131.827 -96.819  60.949  1.00 72.92           C  
ANISOU13457  CA  ASP I 213     7970   7830  11905    305    632    420       C  
ATOM  13458  C   ASP I 213     133.166 -96.213  61.192  1.00 71.00           C  
ANISOU13458  C   ASP I 213     7726   7632  11617    316    590    368       C  
ATOM  13459  O   ASP I 213     133.594 -96.019  62.328  1.00 72.22           O  
ANISOU13459  O   ASP I 213     7918   7820  11702    321    589    358       O  
ATOM  13460  CB  ASP I 213     132.036 -98.205  60.373  1.00 75.85           C  
ANISOU13460  CB  ASP I 213     8343   8178  12300    324    584    460       C  
ATOM  13461  CG  ASP I 213     130.999 -99.150  60.839  1.00 76.06           C  
ANISOU13461  CG  ASP I 213     8400   8174  12327    321    614    521       C  
ATOM  13462  OD1 ASP I 213     129.866 -98.659  61.101  1.00 73.79           O  
ANISOU13462  OD1 ASP I 213     8113   7870  12054    299    678    532       O  
ATOM  13463  OD2 ASP I 213     131.311-100.362  60.971  1.00 78.79           O  
ANISOU13463  OD2 ASP I 213     8768   8513  12656    341    574    557       O  
ATOM  13464  N   TYR I 214     133.823 -95.945  60.080  1.00 64.27           N  
ANISOU13464  N   TYR I 214     6831   6779  10808    321    554    337       N  
ATOM  13465  CA  TYR I 214     135.173 -95.488  60.060  1.00 64.22           C  
ANISOU13465  CA  TYR I 214     6816   6813  10771    334    505    290       C  
ATOM  13466  C   TYR I 214     135.236 -94.403  59.017  1.00 63.68           C  
ANISOU13466  C   TYR I 214     6695   6741  10758    320    515    245       C  
ATOM  13467  O   TYR I 214     134.780 -94.596  57.891  1.00 63.22           O  
ANISOU13467  O   TYR I 214     6602   6650  10770    317    517    256       O  
ATOM  13468  CB  TYR I 214     136.098 -96.648  59.730  1.00 64.21           C  
ANISOU13468  CB  TYR I 214     6820   6814  10762    362    434    308       C  
ATOM  13469  CG  TYR I 214     137.502 -96.285  59.337  1.00 64.02           C  
ANISOU13469  CG  TYR I 214     6775   6824  10726    377    377    261       C  
ATOM  13470  CD1 TYR I 214     138.473 -96.017  60.305  1.00 64.41           C  
ANISOU13470  CD1 TYR I 214     6852   6919  10702    387    351    234       C  
ATOM  13471  CD2 TYR I 214     137.871 -96.237  57.999  1.00 63.47           C  
ANISOU13471  CD2 TYR I 214     6657   6740  10717    382    347    244       C  
ATOM  13472  CE1 TYR I 214     139.778 -95.682  59.944  1.00 64.25           C  
ANISOU13472  CE1 TYR I 214     6811   6930  10670    400    298    192       C  
ATOM  13473  CE2 TYR I 214     139.171 -95.902  57.629  1.00 63.30           C  
ANISOU13473  CE2 TYR I 214     6616   6750  10685    395    294    201       C  
ATOM  13474  CZ  TYR I 214     140.118 -95.632  58.604  1.00 63.69           C  
ANISOU13474  CZ  TYR I 214     6693   6845  10662    404    270    176       C  
ATOM  13475  OH  TYR I 214     141.393 -95.321  58.225  1.00 63.53           O  
ANISOU13475  OH  TYR I 214     6651   6855  10632    418    217    135       O  
ATOM  13476  N   THR I 215     135.760 -93.246  59.398  1.00 63.67           N  
ANISOU13476  N   THR I 215     6690   6774  10726    312    523    194       N  
ATOM  13477  CA  THR I 215     136.037 -92.195  58.438  1.00 62.01           C  
ANISOU13477  CA  THR I 215     6431   6567  10563    302    524    146       C  
ATOM  13478  C   THR I 215     137.435 -91.689  58.729  1.00 63.17           C  
ANISOU13478  C   THR I 215     6579   6761  10663    314    478     98       C  
ATOM  13479  O   THR I 215     137.726 -91.307  59.867  1.00 65.20           O  
ANISOU13479  O   THR I 215     6869   7049  10854    312    486     83       O  
ATOM  13480  CB  THR I 215     135.009 -91.048  58.521  1.00 61.92           C  
ANISOU13480  CB  THR I 215     6408   6545  10574    274    597    129       C  
ATOM  13481  OG1 THR I 215     133.679 -91.570  58.348  1.00 61.89           O  
ANISOU13481  OG1 THR I 215     6406   6499  10609    263    641    178       O  
ATOM  13482  CG2 THR I 215     135.283 -90.032  57.438  1.00 61.38           C  
ANISOU13482  CG2 THR I 215     6287   6477  10558    264    596     82       C  
ATOM  13483  N   LYS I 216     138.315 -91.724  57.728  1.00 63.39           N  
ANISOU13483  N   LYS I 216     6571   6793  10723    326    428     74       N  
ATOM  13484  CA  LYS I 216     139.707 -91.314  57.929  1.00 63.47           C  
ANISOU13484  CA  LYS I 216     6578   6846  10691    338    378     30       C  
ATOM  13485  C   LYS I 216     139.850 -89.876  57.494  1.00 63.16           C  
ANISOU13485  C   LYS I 216     6503   6819  10676    320    401    -26       C  
ATOM  13486  O   LYS I 216     139.557 -89.561  56.337  1.00 62.65           O  
ANISOU13486  O   LYS I 216     6394   6730  10679    313    409    -35       O  
ATOM  13487  CB  LYS I 216     140.671 -92.204  57.138  1.00 63.24           C  
ANISOU13487  CB  LYS I 216     6532   6817  10679    364    308     37       C  
ATOM  13488  CG  LYS I 216     142.149 -92.000  57.457  1.00 63.90           C  
ANISOU13488  CG  LYS I 216     6619   6948  10713    380    251     -2       C  
ATOM  13489  CD  LYS I 216     143.046 -92.471  56.309  1.00 63.12           C  
ANISOU13489  CD  LYS I 216     6485   6846  10652    400    190     -9       C  
ATOM  13490  CE  LYS I 216     143.647 -93.850  56.544  1.00 63.68           C  
ANISOU13490  CE  LYS I 216     6583   6922  10692    429    135     27       C  
ATOM  13491  NZ  LYS I 216     144.257 -94.411  55.301  1.00 62.78           N  
ANISOU13491  NZ  LYS I 216     6432   6794  10626    447     84     29       N  
ATOM  13492  N   LEU I 217     140.267 -89.004  58.412  1.00 62.15           N  
ANISOU13492  N   LEU I 217     6394   6728  10493    312    411    -62       N  
ATOM  13493  CA  LEU I 217     140.564 -87.621  58.056  1.00 61.89           C  
ANISOU13493  CA  LEU I 217     6329   6711  10476    296    426   -118       C  
ATOM  13494  C   LEU I 217     142.058 -87.433  57.873  1.00 61.84           C  
ANISOU13494  C   LEU I 217     6308   6742  10446    312    363   -159       C  
ATOM  13495  O   LEU I 217     142.841 -87.659  58.800  1.00 62.27           O  
ANISOU13495  O   LEU I 217     6395   6830  10433    324    332   -164       O  
ATOM  13496  CB  LEU I 217     140.049 -86.649  59.112  1.00 62.24           C  
ANISOU13496  CB  LEU I 217     6399   6771  10478    276    482   -137       C  
ATOM  13497  CG  LEU I 217     140.340 -85.164  58.855  1.00 62.02           C  
ANISOU13497  CG  LEU I 217     6342   6761  10462    258    500   -197       C  
ATOM  13498  CD1 LEU I 217     139.062 -84.400  58.781  1.00 61.90           C  
ANISOU13498  CD1 LEU I 217     6318   6720  10480    233    574   -195       C  
ATOM  13499  CD2 LEU I 217     141.195 -84.587  59.955  1.00 62.46           C  
ANISOU13499  CD2 LEU I 217     6427   6863  10442    259    486   -232       C  
ATOM  13500  N   VAL I 218     142.442 -87.017  56.670  1.00 62.33           N  
ANISOU13500  N   VAL I 218     6321   6798  10565    312    345   -186       N  
ATOM  13501  CA  VAL I 218     143.843 -86.825  56.329  1.00 63.14           C  
ANISOU13501  CA  VAL I 218     6403   6932  10655    326    285   -224       C  
ATOM  13502  C   VAL I 218     144.219 -85.378  56.037  1.00 63.53           C  
ANISOU13502  C   VAL I 218     6421   7000  10716    309    299   -284       C  
ATOM  13503  O   VAL I 218     143.931 -84.875  54.954  1.00 62.09           O  
ANISOU13503  O   VAL I 218     6196   6797  10600    300    314   -299       O  
ATOM  13504  CB  VAL I 218     144.195 -87.646  55.092  1.00 61.65           C  
ANISOU13504  CB  VAL I 218     6182   6722  10521    345    239   -207       C  
ATOM  13505  CG1 VAL I 218     145.610 -87.379  54.674  1.00 62.27           C  
ANISOU13505  CG1 VAL I 218     6235   6833  10590    359    180   -248       C  
ATOM  13506  CG2 VAL I 218     144.002 -89.086  55.383  1.00 61.64           C  
ANISOU13506  CG2 VAL I 218     6212   6705  10503    364    217   -152       C  
ATOM  13507  N   PHE I 219     144.920 -84.728  56.958  1.00 61.96           N  
ANISOU13507  N   PHE I 219     6243   6842  10456    306    291   -319       N  
ATOM  13508  CA  PHE I 219     145.365 -83.364  56.706  1.00 62.91           C  
ANISOU13508  CA  PHE I 219     6335   6983  10586    291    300   -377       C  
ATOM  13509  C   PHE I 219     146.393 -83.366  55.592  1.00 63.94           C  
ANISOU13509  C   PHE I 219     6421   7121  10753    304    246   -402       C  
ATOM  13510  O   PHE I 219     147.259 -84.250  55.546  1.00 64.47           O  
ANISOU13510  O   PHE I 219     6493   7201  10800    328    187   -389       O  
ATOM  13511  CB  PHE I 219     145.946 -82.740  57.961  1.00 66.85           C  
ANISOU13511  CB  PHE I 219     6867   7524  11008    286    299   -408       C  
ATOM  13512  CG  PHE I 219     144.932 -82.439  59.003  1.00 66.39           C  
ANISOU13512  CG  PHE I 219     6848   7461  10917    269    360   -394       C  
ATOM  13513  CD1 PHE I 219     143.993 -81.435  58.796  1.00 65.06           C  
ANISOU13513  CD1 PHE I 219     6664   7274  10783    244    423   -409       C  
ATOM  13514  CD2 PHE I 219     144.915 -83.138  60.196  1.00 67.62           C  
ANISOU13514  CD2 PHE I 219     7055   7631  11007    278    355   -365       C  
ATOM  13515  CE1 PHE I 219     143.043 -81.134  59.765  1.00 64.99           C  
ANISOU13515  CE1 PHE I 219     6690   7259  10743    228    480   -396       C  
ATOM  13516  CE2 PHE I 219     143.975 -82.847  61.173  1.00 67.64           C  
ANISOU13516  CE2 PHE I 219     7093   7628  10978    263    411   -352       C  
ATOM  13517  CZ  PHE I 219     143.033 -81.841  60.958  1.00 66.24           C  
ANISOU13517  CZ  PHE I 219     6900   7432  10835    238    475   -368       C  
ATOM  13518  N   ALA I 220     146.310 -82.393  54.689  1.00 65.45           N  
ANISOU13518  N   ALA I 220     6568   7303  10997    290    265   -436       N  
ATOM  13519  CA  ALA I 220     147.265 -82.335  53.579  1.00 64.98           C  
ANISOU13519  CA  ALA I 220     6464   7250  10976    302    216   -461       C  
ATOM  13520  C   ALA I 220     148.699 -82.070  54.062  1.00 66.46           C  
ANISOU13520  C   ALA I 220     6656   7485  11109    313    163   -499       C  
ATOM  13521  O   ALA I 220     149.641 -82.259  53.311  1.00 66.29           O  
ANISOU13521  O   ALA I 220     6606   7475  11108    328    112   -513       O  
ATOM  13522  CB  ALA I 220     146.843 -81.284  52.566  1.00 63.90           C  
ANISOU13522  CB  ALA I 220     6280   7094  10906    284    251   -491       C  
ATOM  13523  N   LYS I 221     148.849 -81.620  55.304  1.00 66.96           N  
ANISOU13523  N   LYS I 221     6757   7579  11107    304    176   -515       N  
ATOM  13524  CA  LYS I 221     150.147 -81.527  55.948  1.00 67.29           C  
ANISOU13524  CA  LYS I 221     6812   7667  11087    315    125   -544       C  
ATOM  13525  C   LYS I 221     150.002 -81.782  57.453  1.00 67.93           C  
ANISOU13525  C   LYS I 221     6951   7768  11090    315    137   -529       C  
ATOM  13526  O   LYS I 221     148.944 -81.566  58.010  1.00 68.10           O  
ANISOU13526  O   LYS I 221     6996   7773  11105    299    193   -513       O  
ATOM  13527  CB  LYS I 221     150.783 -80.164  55.663  1.00 67.11           C  
ANISOU13527  CB  LYS I 221     6758   7668  11073    300    126   -605       C  
ATOM  13528  CG  LYS I 221     150.229 -78.978  56.432  1.00 67.33           C  
ANISOU13528  CG  LYS I 221     6801   7703  11077    273    183   -634       C  
ATOM  13529  CD  LYS I 221     150.950 -77.711  55.959  1.00 67.09           C  
ANISOU13529  CD  LYS I 221     6734   7694  11063    260    177   -694       C  
ATOM  13530  CE  LYS I 221     150.467 -76.433  56.651  1.00 67.28           C  
ANISOU13530  CE  LYS I 221     6771   7727  11066    233    233   -728       C  
ATOM  13531  NZ  LYS I 221     151.051 -75.208  56.011  1.00 66.97           N  
ANISOU13531  NZ  LYS I 221     6691   7701  11055    219    231   -785       N  
ATOM  13532  N   PRO I 222     151.073 -82.246  58.122  1.00 67.84           N  
ANISOU13532  N   PRO I 222     6963   7794  11020    333     84   -533       N  
ATOM  13533  CA  PRO I 222     150.979 -82.510  59.571  1.00 69.51           C  
ANISOU13533  CA  PRO I 222     7230   8025  11154    334     92   -519       C  
ATOM  13534  C   PRO I 222     150.543 -81.289  60.391  1.00 71.83           C  
ANISOU13534  C   PRO I 222     7541   8332  11419    308    145   -552       C  
ATOM  13535  O   PRO I 222     150.661 -80.167  59.907  1.00 73.71           O  
ANISOU13535  O   PRO I 222     7746   8574  11685    291    161   -595       O  
ATOM  13536  CB  PRO I 222     152.408 -82.923  59.935  1.00 73.91           C  
ANISOU13536  CB  PRO I 222     7797   8625  11661    356     22   -533       C  
ATOM  13537  CG  PRO I 222     152.945 -83.516  58.660  1.00 72.65           C  
ANISOU13537  CG  PRO I 222     7595   8452  11555    374    -24   -525       C  
ATOM  13538  CD  PRO I 222     152.368 -82.687  57.561  1.00 70.57           C  
ANISOU13538  CD  PRO I 222     7286   8162  11367    356     12   -545       C  
ATOM  13539  N   ILE I 223     150.021 -81.504  61.595  1.00 70.44           N  
ANISOU13539  N   ILE I 223     7415   8162  11188    305    172   -530       N  
ATOM  13540  CA  ILE I 223     149.632 -80.391  62.463  1.00 71.53           C  
ANISOU13540  CA  ILE I 223     7573   8314  11292    282    221   -560       C  
ATOM  13541  C   ILE I 223     150.671 -80.150  63.544  1.00 77.02           C  
ANISOU13541  C   ILE I 223     8299   9058  11908    288    186   -589       C  
ATOM  13542  O   ILE I 223     151.014 -81.074  64.274  1.00 78.38           O  
ANISOU13542  O   ILE I 223     8506   9245  12029    307    156   -562       O  
ATOM  13543  CB  ILE I 223     148.256 -80.630  63.160  1.00 71.16           C  
ANISOU13543  CB  ILE I 223     7563   8240  11234    272    283   -521       C  
ATOM  13544  CG1 ILE I 223     147.101 -80.758  62.145  1.00 68.86           C  
ANISOU13544  CG1 ILE I 223     7242   7899  11021    263    325   -493       C  
ATOM  13545  CG2 ILE I 223     147.954 -79.509  64.158  1.00 72.52           C  
ANISOU13545  CG2 ILE I 223     7760   8431  11362    250    329   -552       C  
ATOM  13546  CD1 ILE I 223     146.728 -79.480  61.414  1.00 67.99           C  
ANISOU13546  CD1 ILE I 223     7093   7778  10964    239    365   -532       C  
ATOM  13547  N   TYR I 224     151.169 -78.916  63.646  1.00 72.78           N  
ANISOU13547  N   TYR I 224     7747   8546  11360    272    191   -644       N  
ATOM  13548  CA  TYR I 224     152.118 -78.542  64.704  1.00 79.51           C  
ANISOU13548  CA  TYR I 224     8627   9445  12137    274    163   -677       C  
ATOM  13549  C   TYR I 224     151.710 -77.264  65.418  1.00 83.04           C  
ANISOU13549  C   TYR I 224     9089   9903  12559    248    214   -713       C  
ATOM  13550  O   TYR I 224     151.546 -76.215  64.790  1.00 83.11           O  
ANISOU13550  O   TYR I 224     9064   9903  12610    229    241   -748       O  
ATOM  13551  CB  TYR I 224     153.534 -78.346  64.153  1.00 83.34           C  
ANISOU13551  CB  TYR I 224     9080   9961  12626    284     99   -715       C  
ATOM  13552  CG  TYR I 224     154.284 -79.611  63.866  1.00 82.31           C  
ANISOU13552  CG  TYR I 224     8948   9837  12490    314     35   -685       C  
ATOM  13553  CD1 TYR I 224     154.599 -80.499  64.883  1.00 83.77           C  
ANISOU13553  CD1 TYR I 224     9179  10042  12608    332      8   -658       C  
ATOM  13554  CD2 TYR I 224     154.696 -79.910  62.576  1.00 80.42           C  
ANISOU13554  CD2 TYR I 224     8662   9584  12311    324      2   -684       C  
ATOM  13555  CE1 TYR I 224     155.302 -81.679  64.616  1.00 83.13           C  
ANISOU13555  CE1 TYR I 224     9097   9967  12522    360    -51   -630       C  
ATOM  13556  CE2 TYR I 224     155.395 -81.084  62.291  1.00 79.77           C  
ANISOU13556  CE2 TYR I 224     8578   9507  12223    352    -57   -657       C  
ATOM  13557  CZ  TYR I 224     155.702 -81.968  63.314  1.00 81.09           C  
ANISOU13557  CZ  TYR I 224     8792   9694  12324    370    -83   -630       C  
ATOM  13558  OH  TYR I 224     156.390 -83.133  63.035  1.00 80.71           O  
ANISOU13558  OH  TYR I 224     8743   9651  12271    399   -141   -602       O  
ATOM  13559  N   ASN I 225     151.581 -77.350  66.737  1.00 77.96           N  
ANISOU13559  N   ASN I 225     8497   9278  11845    249    227   -705       N  
ATOM  13560  CA  ASN I 225     151.267 -76.185  67.556  1.00 82.44           C  
ANISOU13560  CA  ASN I 225     9085   9860  12378    226    272   -740       C  
ATOM  13561  C   ASN I 225     152.374 -75.136  67.472  1.00 88.65           C  
ANISOU13561  C   ASN I 225     9849  10681  13152    217    242   -803       C  
ATOM  13562  O   ASN I 225     153.548 -75.465  67.276  1.00 91.00           O  
ANISOU13562  O   ASN I 225    10134  11006  13436    233    179   -816       O  
ATOM  13563  CB  ASN I 225     151.046 -76.606  69.013  1.00 85.83           C  
ANISOU13563  CB  ASN I 225     9576  10306  12729    232    282   -718       C  
ATOM  13564  CG  ASN I 225     150.376 -75.526  69.850  1.00 88.19           C  
ANISOU13564  CG  ASN I 225     9901  10609  13000    209    342   -741       C  
ATOM  13565  OD1 ASN I 225     149.623 -74.700  69.335  1.00 85.99           O  
ANISOU13565  OD1 ASN I 225     9599  10306  12768    188    392   -755       O  
ATOM  13566  ND2 ASN I 225     150.644 -75.534  71.152  1.00 92.98           N  
ANISOU13566  ND2 ASN I 225    10555  11245  13528    213    338   -745       N  
ATOM  13567  N   ASP I 226     151.990 -73.872  67.616  1.00 84.38           N  
ANISOU13567  N   ASP I 226     9304  10141  12616    192    288   -840       N  
ATOM  13568  CA  ASP I 226     152.938 -72.753  67.586  1.00 91.41           C  
ANISOU13568  CA  ASP I 226    10174  11062  13494    181    268   -902       C  
ATOM  13569  C   ASP I 226     152.622 -71.752  68.697  1.00 96.65           C  
ANISOU13569  C   ASP I 226    10874  11743  14107    161    311   -931       C  
ATOM  13570  O   ASP I 226     152.110 -70.667  68.429  1.00 96.96           O  
ANISOU13570  O   ASP I 226    10896  11770  14175    138    357   -959       O  
ATOM  13571  CB  ASP I 226     152.905 -72.065  66.210  1.00 89.74           C  
ANISOU13571  CB  ASP I 226     9904  10830  13363    168    277   -927       C  
ATOM  13572  CG  ASP I 226     153.856 -70.881  66.111  1.00 97.35           C  
ANISOU13572  CG  ASP I 226    10845  11824  14320    155    258   -991       C  
ATOM  13573  OD1 ASP I 226     154.736 -70.756  66.980  1.00102.58           O  
ANISOU13573  OD1 ASP I 226    11532  12527  14918    159    224  -1014       O  
ATOM  13574  OD2 ASP I 226     153.726 -70.079  65.159  1.00 98.43           O  
ANISOU13574  OD2 ASP I 226    10939  11945  14515    140    276  -1017       O  
ATOM  13575  N   PRO I 227     152.939 -72.108  69.953  1.00 91.10           N  
ANISOU13575  N   PRO I 227    10219  11068  13325    171    295   -924       N  
ATOM  13576  CA  PRO I 227     152.625 -71.246  71.103  1.00 96.82           C  
ANISOU13576  CA  PRO I 227    10983  11809  13995    154    335   -948       C  
ATOM  13577  C   PRO I 227     153.271 -69.853  71.009  1.00104.01           C  
ANISOU13577  C   PRO I 227    11872  12743  14905    134    333  -1014       C  
ATOM  13578  O   PRO I 227     152.893 -68.938  71.748  1.00108.78           O  
ANISOU13578  O   PRO I 227    12501  13354  15478    116    375  -1039       O  
ATOM  13579  CB  PRO I 227     153.187 -72.031  72.295  1.00100.98           C  
ANISOU13579  CB  PRO I 227    11559  12368  14441    173    298   -931       C  
ATOM  13580  CG  PRO I 227     153.251 -73.453  71.827  1.00 94.82           C  
ANISOU13580  CG  PRO I 227    10774  11574  13680    198    262   -880       C  
ATOM  13581  CD  PRO I 227     153.577 -73.372  70.368  1.00 91.08           C  
ANISOU13581  CD  PRO I 227    10240  11083  13282    198    240   -891       C  
ATOM  13582  N   SER I 228     154.231 -69.701  70.097  1.00 99.42           N  
ANISOU13582  N   SER I 228    11246  12172  14357    137    286  -1041       N  
ATOM  13583  CA  SER I 228     154.982 -68.457  69.932  1.00106.64           C  
ANISOU13583  CA  SER I 228    12137  13110  15273    120    276  -1103       C  
ATOM  13584  C   SER I 228     154.122 -67.263  69.468  1.00106.22           C  
ANISOU13584  C   SER I 228    12062  13030  15266     93    341  -1128       C  
ATOM  13585  O   SER I 228     154.606 -66.124  69.441  1.00113.23           O  
ANISOU13585  O   SER I 228    12935  13935  16152     76    342  -1181       O  
ATOM  13586  CB  SER I 228     156.140 -68.683  68.946  1.00107.25           C  
ANISOU13586  CB  SER I 228    12167  13200  15383    132    212  -1120       C  
ATOM  13587  OG  SER I 228     157.115 -67.656  69.027  1.00114.48           O  
ANISOU13587  OG  SER I 228    13068  14149  16282    119    188  -1179       O  
ATOM  13588  N   LEU I 229     152.860 -67.514  69.108  1.00108.27           N  
ANISOU13588  N   LEU I 229    12320  13248  15568     89    393  -1091       N  
ATOM  13589  CA  LEU I 229     151.972 -66.450  68.614  1.00107.22           C  
ANISOU13589  CA  LEU I 229    12167  13088  15484     65    456  -1111       C  
ATOM  13590  C   LEU I 229     150.948 -65.979  69.654  1.00107.97           C  
ANISOU13590  C   LEU I 229    12307  13176  15541     51    521  -1105       C  
ATOM  13591  O   LEU I 229     150.225 -65.000  69.435  1.00108.75           O  
ANISOU13591  O   LEU I 229    12395  13257  15669     30    576  -1124       O  
ATOM  13592  CB  LEU I 229     151.243 -66.915  67.344  1.00 98.72           C  
ANISOU13592  CB  LEU I 229    11051  11969  14490     68    474  -1078       C  
ATOM  13593  CG  LEU I 229     151.927 -66.580  66.013  1.00 98.61           C  
ANISOU13593  CG  LEU I 229    10977  11952  14539     66    443  -1105       C  
ATOM  13594  CD1 LEU I 229     151.131 -67.097  64.813  1.00 90.31           C  
ANISOU13594  CD1 LEU I 229     9891  10857  13567     70    462  -1069       C  
ATOM  13595  CD2 LEU I 229     152.183 -65.070  65.907  1.00105.74           C  
ANISOU13595  CD2 LEU I 229    11861  12866  15449     42    464  -1166       C  
TER   13596      LEU I 229                                                      



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: april 24th, 2026.