CNRS Nantes University US2B US2B
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Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.


***  TRANSFERASE 18-APR-07 2PL0  ***

elNémo ID: 260201014444812257

Job options:

ID        	=	 260201014444812257
JOBID     	=	 TRANSFERASE 18-APR-07 2PL0
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    TRANSFERASE                             18-APR-07   2PL0              
TITLE     LCK BOUND TO IMATINIB                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTO-ONCOGENE TYROSINE-PROTEIN KINASE LCK;                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEIN KINASE;                                            
COMPND   5 SYNONYM: P56-LCK, LYMPHOCYTE CELL-SPECIFIC PROTEIN-TYROSINE KINASE,  
COMPND   6 LSK, T CELL- SPECIFIC PROTEIN-TYROSINE KINASE;                       
COMPND   7 EC: 2.7.10.2;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LCK;                                                           
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PBEV1                                     
KEYWDS    KINASE PHOSPHORYLATION, TRANSFERASE                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.D.JACOBS                                                            
REVDAT   5   21-FEB-24 2PL0    1       REMARK SEQADV HETSYN                     
REVDAT   4   24-FEB-09 2PL0    1       VERSN                                    
REVDAT   3   26-FEB-08 2PL0    1       JRNL                                     
REVDAT   2   20-NOV-07 2PL0    1       JRNL                                     
REVDAT   1   09-OCT-07 2PL0    0                                                
JRNL        AUTH   M.D.JACOBS,P.R.CARON,B.J.HARE                                
JRNL        TITL   CLASSIFYING PROTEIN KINASE STRUCTURES GUIDES USE OF          
JRNL        TITL 2 LIGAND-SELECTIVITY PROFILES TO PREDICT INACTIVE              
JRNL        TITL 3 CONFORMATIONS: STRUCTURE OF LCK/IMATINIB COMPLEX.            
JRNL        REF    PROTEINS                      V.  70  1451 2007              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   17910071                                                     
JRNL        DOI    10.1002/PROT.21633                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.90                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1044136.688                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10474                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.215                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 534                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.011                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.2520               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.2500               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.284                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 5.100                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 534                  
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 10474                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1624                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3060                       
REMARK   3   BIN FREE R VALUE                    : 0.3270                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 68                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.040                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2182                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 37                                      
REMARK   3   SOLVENT ATOMS            : 93                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 55.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -18.32000                                            
REMARK   3    B22 (A**2) : 17.39000                                             
REMARK   3    B33 (A**2) : 0.93000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.42                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.43                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.60                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 20.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.550                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.410 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.520 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.920 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.120 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 47.07                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : INHIB.PAR                                      
REMARK   3  PARAMETER FILE  4  : PARMXRAY.XPL                                   
REMARK   3  PARAMETER FILE  5  : &_1_PARAMETER_INFILE_5                         
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : INHIB.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2PL0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-APR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042493.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-MAR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10512                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.870                              
REMARK 200  R MERGE                    (I) : 0.12000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.99                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.51                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M AMMONIUM SULFATE, 100 MM HEPES     
REMARK 280  PH 7.5, 1% PEG-3350, 10 MM DTT, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-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        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       37.60500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.58500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.60500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.58500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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     GLY A   221                                                      
REMARK 465     SER A   222                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     MET A   224                                                      
REMARK 465     GLN A   225                                                      
REMARK 465     THR A   226                                                      
REMARK 465     GLN A   227                                                      
REMARK 465     LYS A   228                                                      
REMARK 465     PRO A   229                                                      
REMARK 465     GLN A   230                                                      
REMARK 465     THR A   499                                                      
REMARK 465     ALA A   500                                                      
REMARK 465     THR A   501                                                      
REMARK 465     GLU A   502                                                      
REMARK 465     GLY A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     TYR A   505                                                      
REMARK 465     GLN A   506                                                      
REMARK 465     PRO A   507                                                      
REMARK 465     GLN A   508                                                      
REMARK 465     PRO A   509                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 231    CG   CD   CE   NZ                                   
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    PHE A 256       12.07   -149.48                                   
REMARK 500    HIS A 297      145.50   -179.84                                   
REMARK 500    ASN A 359       43.12     70.88                                   
REMARK 500    ARG A 363      -24.94     88.99                                   
REMARK 500    ALA A 396       31.32   -145.94                                   
REMARK 500    ASN A 464      -23.22     72.25                                   
REMARK 500    PRO A 485      176.84    -58.46                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE STI A 200                 
DBREF  2PL0 A  225   509  UNP    P06239   LCK_HUMAN      225    509             
SEQADV 2PL0 GLY A  221  UNP  P06239              EXPRESSION TAG                 
SEQADV 2PL0 SER A  222  UNP  P06239              EXPRESSION TAG                 
SEQADV 2PL0 HIS A  223  UNP  P06239              EXPRESSION TAG                 
SEQADV 2PL0 MET A  224  UNP  P06239              EXPRESSION TAG                 
SEQRES   1 A  289  GLY SER HIS MET GLN THR GLN LYS PRO GLN LYS PRO TRP          
SEQRES   2 A  289  TRP GLU ASP GLU TRP GLU VAL PRO ARG GLU THR LEU LYS          
SEQRES   3 A  289  LEU VAL GLU ARG LEU GLY ALA GLY GLN PHE GLY GLU VAL          
SEQRES   4 A  289  TRP MET GLY TYR TYR ASN GLY HIS THR LYS VAL ALA VAL          
SEQRES   5 A  289  LYS SER LEU LYS GLN GLY SER MET SER PRO ASP ALA PHE          
SEQRES   6 A  289  LEU ALA GLU ALA ASN LEU MET LYS GLN LEU GLN HIS GLN          
SEQRES   7 A  289  ARG LEU VAL ARG LEU TYR ALA VAL VAL THR GLN GLU PRO          
SEQRES   8 A  289  ILE TYR ILE ILE THR GLU TYR MET GLU ASN GLY SER LEU          
SEQRES   9 A  289  VAL ASP PHE LEU LYS THR PRO SER GLY ILE LYS LEU THR          
SEQRES  10 A  289  ILE ASN LYS LEU LEU ASP MET ALA ALA GLN ILE ALA GLU          
SEQRES  11 A  289  GLY MET ALA PHE ILE GLU GLU ARG ASN TYR ILE HIS ARG          
SEQRES  12 A  289  ASP LEU ARG ALA ALA ASN ILE LEU VAL SER ASP THR LEU          
SEQRES  13 A  289  SER CYS LYS ILE ALA ASP PHE GLY LEU ALA ARG LEU ILE          
SEQRES  14 A  289  GLU ASP ASN GLU TYR THR ALA ARG GLU GLY ALA LYS PHE          
SEQRES  15 A  289  PRO ILE LYS TRP THR ALA PRO GLU ALA ILE ASN TYR GLY          
SEQRES  16 A  289  THR PHE THR ILE LYS SER ASP VAL TRP SER PHE GLY ILE          
SEQRES  17 A  289  LEU LEU THR GLU ILE VAL THR HIS GLY ARG ILE PRO TYR          
SEQRES  18 A  289  PRO GLY MET THR ASN PRO GLU VAL ILE GLN ASN LEU GLU          
SEQRES  19 A  289  ARG GLY TYR ARG MET VAL ARG PRO ASP ASN CYS PRO GLU          
SEQRES  20 A  289  GLU LEU TYR GLN LEU MET ARG LEU CYS TRP LYS GLU ARG          
SEQRES  21 A  289  PRO GLU ASP ARG PRO THR PHE ASP TYR LEU ARG SER VAL          
SEQRES  22 A  289  LEU GLU ASP PHE PHE THR ALA THR GLU GLY GLN TYR GLN          
SEQRES  23 A  289  PRO GLN PRO                                                  
HET    STI  A 200      37                                                       
HETNAM     STI 4-(4-METHYL-PIPERAZIN-1-YLMETHYL)-N-[4-METHYL-3-(4-              
HETNAM   2 STI  PYRIDIN-3-YL-PYRIMIDIN-2-YLAMINO)-PHENYL]-BENZAMIDE             
HETSYN     STI STI-571; IMATINIB                                                
FORMUL   2  STI    C29 H31 N7 O                                                 
FORMUL   3  HOH   *93(H2 O)                                                     
HELIX    1   1 PRO A  232  ASP A  236  5                                   5    
HELIX    2   2 PRO A  241  GLU A  243  5                                   3    
HELIX    3   3 SER A  281  LEU A  295  1                                  15    
HELIX    4   4 SER A  323  THR A  330  1                                   8    
HELIX    5   5 THR A  330  LYS A  335  1                                   6    
HELIX    6   6 THR A  337  ARG A  358  1                                  22    
HELIX    7   7 ARG A  366  ALA A  368  5                                   3    
HELIX    8   8 LEU A  385  ILE A  389  5                                   5    
HELIX    9   9 PRO A  403  THR A  407  5                                   5    
HELIX   10  10 ALA A  408  GLY A  415  1                                   8    
HELIX   11  11 THR A  418  VAL A  434  1                                  17    
HELIX   12  12 THR A  445  ARG A  455  1                                  11    
HELIX   13  13 PRO A  466  TRP A  477  1                                  12    
HELIX   14  14 ARG A  480  ARG A  484  5                                   5    
HELIX   15  15 THR A  486  ASP A  496  1                                  11    
SHEET    1   A 5 LEU A 245  ARG A 250  0                                        
SHEET    2   A 5 VAL A 259  TYR A 264 -1  O  MET A 261   N  VAL A 248           
SHEET    3   A 5 THR A 268  SER A 274 -1  O  VAL A 272   N  TRP A 260           
SHEET    4   A 5 TYR A 313  GLU A 317 -1  O  ILE A 314   N  LYS A 273           
SHEET    5   A 5 LEU A 303  VAL A 307 -1  N  ALA A 305   O  ILE A 315           
SHEET    1   B 2 ILE A 370  VAL A 372  0                                        
SHEET    2   B 2 CYS A 378  ILE A 380 -1  O  LYS A 379   N  LEU A 371           
CISPEP   1 GLU A  310    PRO A  311          0        -9.40                     
SITE     1 AC1 16 HOH A  86  ALA A 271  LYS A 273  GLU A 288                    
SITE     2 AC1 16 LEU A 291  MET A 292  VAL A 301  ILE A 314                    
SITE     3 AC1 16 THR A 316  TYR A 318  MET A 319  ILE A 361                    
SITE     4 AC1 16 HIS A 362  ALA A 381  ASP A 382  PHE A 383                    
CRYST1   75.210  103.170   52.330  90.00  90.00  90.00 P 21 21 2     4          
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      0.013296  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009693  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019109        0.00000                         
ATOM      1  N   LYS A 231      -0.031  16.665   8.457  1.00 94.38           N  
ATOM      2  CA  LYS A 231       0.149  18.061   7.961  1.00 94.74           C  
ATOM      3  C   LYS A 231       0.916  18.069   6.642  1.00 94.56           C  
ATOM      4  O   LYS A 231       1.967  17.437   6.519  1.00 95.24           O  
ATOM      5  CB  LYS A 231       0.894  18.893   9.003  1.00 94.11           C  
ATOM      6  N   PRO A 232       0.398  18.794   5.635  1.00 93.91           N  
ATOM      7  CA  PRO A 232       1.032  18.899   4.314  1.00 92.48           C  
ATOM      8  C   PRO A 232       2.450  19.447   4.404  1.00 91.03           C  
ATOM      9  O   PRO A 232       2.726  20.348   5.196  1.00 90.55           O  
ATOM     10  CB  PRO A 232       0.105  19.837   3.542  1.00 92.58           C  
ATOM     11  CG  PRO A 232      -1.215  19.700   4.223  1.00 93.36           C  
ATOM     12  CD  PRO A 232      -0.891  19.505   5.678  1.00 94.18           C  
ATOM     13  N   TRP A 233       3.348  18.903   3.590  1.00 89.98           N  
ATOM     14  CA  TRP A 233       4.762  19.235   3.705  1.00 89.47           C  
ATOM     15  C   TRP A 233       5.030  20.695   3.354  1.00 89.10           C  
ATOM     16  O   TRP A 233       5.992  21.286   3.847  1.00 88.86           O  
ATOM     17  CB  TRP A 233       5.599  18.322   2.804  1.00 88.91           C  
ATOM     18  CG  TRP A 233       5.349  18.516   1.344  1.00 89.30           C  
ATOM     19  CD1 TRP A 233       4.517  17.781   0.551  1.00 88.85           C  
ATOM     20  CD2 TRP A 233       5.938  19.510   0.497  1.00 90.01           C  
ATOM     21  NE1 TRP A 233       4.550  18.256  -0.738  1.00 89.34           N  
ATOM     22  CE2 TRP A 233       5.415  19.319  -0.798  1.00 90.07           C  
ATOM     23  CE3 TRP A 233       6.857  20.546   0.707  1.00 90.14           C  
ATOM     24  CZ2 TRP A 233       5.780  20.124  -1.878  1.00 90.19           C  
ATOM     25  CZ3 TRP A 233       7.218  21.345  -0.366  1.00 90.04           C  
ATOM     26  CH2 TRP A 233       6.680  21.129  -1.642  1.00 90.36           C  
ATOM     27  N   TRP A 234       4.181  21.270   2.507  1.00 88.46           N  
ATOM     28  CA  TRP A 234       4.364  22.648   2.065  1.00 87.17           C  
ATOM     29  C   TRP A 234       3.908  23.641   3.125  1.00 86.57           C  
ATOM     30  O   TRP A 234       4.173  24.840   3.023  1.00 86.99           O  
ATOM     31  CB  TRP A 234       3.606  22.898   0.757  1.00 87.04           C  
ATOM     32  CG  TRP A 234       2.134  22.629   0.837  1.00 87.12           C  
ATOM     33  CD1 TRP A 234       1.164  23.483   1.284  1.00 86.33           C  
ATOM     34  CD2 TRP A 234       1.458  21.432   0.432  1.00 86.80           C  
ATOM     35  NE1 TRP A 234      -0.072  22.892   1.181  1.00 86.42           N  
ATOM     36  CE2 TRP A 234       0.080  21.633   0.661  1.00 86.72           C  
ATOM     37  CE3 TRP A 234       1.883  20.211  -0.102  1.00 85.53           C  
ATOM     38  CZ2 TRP A 234      -0.876  20.656   0.372  1.00 85.68           C  
ATOM     39  CZ3 TRP A 234       0.933  19.244  -0.388  1.00 85.40           C  
ATOM     40  CH2 TRP A 234      -0.430  19.472  -0.150  1.00 85.18           C  
ATOM     41  N   GLU A 235       3.220  23.136   4.144  1.00 85.53           N  
ATOM     42  CA  GLU A 235       2.864  23.944   5.306  1.00 84.78           C  
ATOM     43  C   GLU A 235       4.100  24.113   6.189  1.00 83.42           C  
ATOM     44  O   GLU A 235       4.207  25.049   6.984  1.00 83.38           O  
ATOM     45  CB  GLU A 235       1.750  23.260   6.108  1.00 85.90           C  
ATOM     46  CG  GLU A 235       0.551  22.863   5.252  1.00 87.04           C  
ATOM     47  CD  GLU A 235      -0.574  23.881   5.291  1.00 86.92           C  
ATOM     48  OE1 GLU A 235      -0.435  24.943   4.648  1.00 87.50           O  
ATOM     49  OE2 GLU A 235      -1.595  23.617   5.962  1.00 86.21           O  
ATOM     50  N   ASP A 236       5.042  23.185   6.032  1.00 80.99           N  
ATOM     51  CA  ASP A 236       6.257  23.156   6.839  1.00 79.09           C  
ATOM     52  C   ASP A 236       7.451  23.707   6.058  1.00 77.79           C  
ATOM     53  O   ASP A 236       7.481  23.638   4.830  1.00 78.79           O  
ATOM     54  CB  ASP A 236       6.542  21.720   7.284  1.00 79.05           C  
ATOM     55  CG  ASP A 236       7.720  21.626   8.226  1.00 79.05           C  
ATOM     56  OD1 ASP A 236       7.562  21.975   9.415  1.00 79.86           O  
ATOM     57  OD2 ASP A 236       8.805  21.201   7.780  1.00 78.70           O  
ATOM     58  N   GLU A 237       8.433  24.249   6.774  1.00 75.29           N  
ATOM     59  CA  GLU A 237       9.591  24.877   6.142  1.00 73.21           C  
ATOM     60  C   GLU A 237      10.721  23.881   5.915  1.00 71.47           C  
ATOM     61  O   GLU A 237      11.727  24.210   5.286  1.00 71.16           O  
ATOM     62  CB  GLU A 237      10.117  26.024   7.006  1.00 73.63           C  
ATOM     63  CG  GLU A 237       9.009  26.766   7.728  1.00 76.79           C  
ATOM     64  CD  GLU A 237       8.666  26.001   8.992  1.00 78.05           C  
ATOM     65  OE1 GLU A 237       9.444  26.079   9.967  1.00 79.21           O  
ATOM     66  OE2 GLU A 237       7.617  25.321   9.014  1.00 79.18           O  
ATOM     67  N   TRP A 238      10.554  22.669   6.438  1.00 69.89           N  
ATOM     68  CA  TRP A 238      11.622  21.674   6.435  1.00 67.56           C  
ATOM     69  C   TRP A 238      11.225  20.422   5.671  1.00 66.36           C  
ATOM     70  O   TRP A 238      12.026  19.854   4.929  1.00 67.13           O  
ATOM     71  CB  TRP A 238      11.987  21.294   7.872  1.00 66.09           C  
ATOM     72  CG  TRP A 238      12.300  22.476   8.717  1.00 64.39           C  
ATOM     73  CD1 TRP A 238      11.551  22.977   9.742  1.00 64.25           C  
ATOM     74  CD2 TRP A 238      13.430  23.341   8.582  1.00 63.58           C  
ATOM     75  NE1 TRP A 238      12.144  24.108  10.251  1.00 63.65           N  
ATOM     76  CE2 TRP A 238      13.299  24.352   9.556  1.00 63.88           C  
ATOM     77  CE3 TRP A 238      14.537  23.362   7.729  1.00 62.92           C  
ATOM     78  CZ2 TRP A 238      14.236  25.371   9.700  1.00 65.10           C  
ATOM     79  CZ3 TRP A 238      15.465  24.374   7.873  1.00 64.04           C  
ATOM     80  CH2 TRP A 238      15.309  25.365   8.850  1.00 65.57           C  
ATOM     81  N   GLU A 239       9.979  19.998   5.858  1.00 64.73           N  
ATOM     82  CA  GLU A 239       9.509  18.733   5.315  1.00 63.87           C  
ATOM     83  C   GLU A 239       9.493  18.756   3.790  1.00 62.32           C  
ATOM     84  O   GLU A 239       8.907  19.641   3.166  1.00 62.17           O  
ATOM     85  CB  GLU A 239       8.106  18.426   5.847  1.00 64.99           C  
ATOM     86  CG  GLU A 239       7.601  17.059   5.407  1.00 67.45           C  
ATOM     87  CD  GLU A 239       8.436  15.955   6.027  1.00 69.18           C  
ATOM     88  OE1 GLU A 239       8.956  16.159   7.145  1.00 70.75           O  
ATOM     89  OE2 GLU A 239       8.573  14.882   5.399  1.00 70.86           O  
ATOM     90  N   VAL A 240      10.153  17.771   3.191  1.00 59.72           N  
ATOM     91  CA  VAL A 240      10.167  17.631   1.742  1.00 58.36           C  
ATOM     92  C   VAL A 240       9.821  16.201   1.343  1.00 58.46           C  
ATOM     93  O   VAL A 240      10.134  15.246   2.054  1.00 58.46           O  
ATOM     94  CB  VAL A 240      11.554  17.978   1.148  1.00 57.86           C  
ATOM     95  CG1 VAL A 240      11.906  19.424   1.458  1.00 57.51           C  
ATOM     96  CG2 VAL A 240      12.614  17.035   1.701  1.00 55.64           C  
ATOM     97  N   PRO A 241       9.149  16.039   0.193  1.00 57.83           N  
ATOM     98  CA  PRO A 241       8.881  14.707  -0.361  1.00 57.72           C  
ATOM     99  C   PRO A 241      10.179  13.971  -0.670  1.00 57.53           C  
ATOM    100  O   PRO A 241      11.084  14.533  -1.281  1.00 58.03           O  
ATOM    101  CB  PRO A 241       8.073  15.001  -1.625  1.00 56.12           C  
ATOM    102  CG  PRO A 241       7.454  16.336  -1.368  1.00 55.21           C  
ATOM    103  CD  PRO A 241       8.474  17.098  -0.575  1.00 56.28           C  
ATOM    104  N   ARG A 242      10.264  12.714  -0.245  1.00 59.11           N  
ATOM    105  CA  ARG A 242      11.476  11.921  -0.428  1.00 61.43           C  
ATOM    106  C   ARG A 242      11.987  12.034  -1.855  1.00 61.60           C  
ATOM    107  O   ARG A 242      13.182  11.908  -2.122  1.00 61.13           O  
ATOM    108  CB  ARG A 242      11.196  10.454  -0.112  1.00 64.11           C  
ATOM    109  CG  ARG A 242      12.416   9.566  -0.323  1.00 69.01           C  
ATOM    110  CD  ARG A 242      11.971   8.157   0.037  1.00 73.39           C  
ATOM    111  NE  ARG A 242      11.002   8.175   1.131  1.00 76.07           N  
ATOM    112  CZ  ARG A 242      11.322   8.039   2.414  1.00 77.38           C  
ATOM    113  NH1 ARG A 242      12.591   7.867   2.768  1.00 77.07           N  
ATOM    114  NH2 ARG A 242      10.375   8.095   3.343  1.00 77.38           N  
ATOM    115  N   GLU A 243      11.053  12.276  -2.770  1.00 62.88           N  
ATOM    116  CA  GLU A 243      11.336  12.335  -4.201  1.00 62.58           C  
ATOM    117  C   GLU A 243      12.384  13.386  -4.536  1.00 62.10           C  
ATOM    118  O   GLU A 243      13.148  13.234  -5.490  1.00 62.24           O  
ATOM    119  CB  GLU A 243      10.050  12.638  -4.974  1.00 62.36           C  
ATOM    120  CG  GLU A 243       9.066  11.477  -4.965  1.00 64.17           C  
ATOM    121  CD  GLU A 243       8.605  11.001  -3.596  1.00 65.89           C  
ATOM    122  OE1 GLU A 243       8.257  11.850  -2.746  1.00 65.63           O  
ATOM    123  OE2 GLU A 243       8.591   9.770  -3.373  1.00 67.58           O  
ATOM    124  N   THR A 244      12.418  14.454  -3.747  1.00 60.27           N  
ATOM    125  CA  THR A 244      13.347  15.547  -3.988  1.00 60.39           C  
ATOM    126  C   THR A 244      14.805  15.134  -3.766  1.00 61.63           C  
ATOM    127  O   THR A 244      15.711  15.946  -3.947  1.00 62.20           O  
ATOM    128  CB  THR A 244      13.036  16.754  -3.076  1.00 59.58           C  
ATOM    129  OG1 THR A 244      13.139  16.359  -1.703  1.00 58.45           O  
ATOM    130  CG2 THR A 244      11.631  17.276  -3.341  1.00 58.04           C  
ATOM    131  N   LEU A 245      15.028  13.879  -3.383  1.00 62.32           N  
ATOM    132  CA  LEU A 245      16.361  13.427  -2.988  1.00 63.34           C  
ATOM    133  C   LEU A 245      16.929  12.330  -3.872  1.00 64.50           C  
ATOM    134  O   LEU A 245      16.321  11.276  -4.049  1.00 65.45           O  
ATOM    135  CB  LEU A 245      16.338  12.931  -1.544  1.00 63.18           C  
ATOM    136  CG  LEU A 245      16.106  14.134  -0.634  1.00 62.47           C  
ATOM    137  CD1 LEU A 245      15.767  13.657   0.771  1.00 62.33           C  
ATOM    138  CD2 LEU A 245      17.347  15.015  -0.646  1.00 59.47           C  
ATOM    139  N   LYS A 246      18.115  12.586  -4.415  1.00 66.43           N  
ATOM    140  CA  LYS A 246      18.871  11.577  -5.149  1.00 68.58           C  
ATOM    141  C   LYS A 246      20.205  11.359  -4.437  1.00 69.34           C  
ATOM    142  O   LYS A 246      21.206  12.010  -4.745  1.00 69.68           O  
ATOM    143  CB  LYS A 246      19.118  12.044  -6.589  1.00 70.18           C  
ATOM    144  CG  LYS A 246      19.623  10.932  -7.503  1.00 73.26           C  
ATOM    145  CD  LYS A 246      20.943  11.181  -8.235  1.00 76.04           C  
ATOM    146  CE  LYS A 246      21.049  12.402  -9.143  1.00 76.62           C  
ATOM    147  NZ  LYS A 246      22.369  12.464  -9.838  1.00 75.90           N  
ATOM    148  N   LEU A 247      20.212  10.443  -3.474  1.00 69.77           N  
ATOM    149  CA  LEU A 247      21.406  10.179  -2.680  1.00 70.52           C  
ATOM    150  C   LEU A 247      22.340   9.231  -3.422  1.00 70.86           C  
ATOM    151  O   LEU A 247      21.897   8.210  -3.945  1.00 70.96           O  
ATOM    152  CB  LEU A 247      21.013   9.594  -1.318  1.00 70.34           C  
ATOM    153  CG  LEU A 247      20.105   8.373  -1.137  1.00 70.91           C  
ATOM    154  CD1 LEU A 247      19.919   8.115   0.354  1.00 69.56           C  
ATOM    155  CD2 LEU A 247      18.752   8.601  -1.807  1.00 71.66           C  
ATOM    156  N   VAL A 248      23.626   9.572  -3.470  1.00 71.88           N  
ATOM    157  CA  VAL A 248      24.546   8.926  -4.402  1.00 73.98           C  
ATOM    158  C   VAL A 248      25.706   8.166  -3.756  1.00 75.69           C  
ATOM    159  O   VAL A 248      26.053   7.080  -4.217  1.00 76.52           O  
ATOM    160  CB  VAL A 248      25.156   9.949  -5.386  1.00 73.37           C  
ATOM    161  CG1 VAL A 248      24.053  10.781  -6.012  1.00 72.89           C  
ATOM    162  CG2 VAL A 248      26.160  10.833  -4.674  1.00 73.49           C  
ATOM    163  N   GLU A 249      26.306   8.726  -2.711  1.00 77.60           N  
ATOM    164  CA  GLU A 249      27.477   8.110  -2.096  1.00 79.38           C  
ATOM    165  C   GLU A 249      27.285   7.881  -0.603  1.00 80.10           C  
ATOM    166  O   GLU A 249      26.634   8.672   0.076  1.00 80.80           O  
ATOM    167  CB  GLU A 249      28.708   8.983  -2.325  1.00 79.99           C  
ATOM    168  CG  GLU A 249      29.953   8.391  -1.699  1.00 82.31           C  
ATOM    169  CD  GLU A 249      31.095   9.295  -2.115  1.00 84.66           C  
ATOM    170  OE1 GLU A 249      30.829  10.315  -2.790  1.00 85.70           O  
ATOM    171  OE2 GLU A 249      32.257   8.987  -1.769  1.00 84.46           O  
ATOM    172  N   ARG A 250      27.858   6.795  -0.095  1.00 81.38           N  
ATOM    173  CA  ARG A 250      27.661   6.406   1.297  1.00 82.92           C  
ATOM    174  C   ARG A 250      28.852   6.843   2.146  1.00 83.05           C  
ATOM    175  O   ARG A 250      29.815   6.099   2.326  1.00 83.83           O  
ATOM    176  CB  ARG A 250      27.480   4.888   1.389  1.00 84.74           C  
ATOM    177  CG  ARG A 250      26.459   4.467   2.442  1.00 87.62           C  
ATOM    178  CD  ARG A 250      26.886   4.129   3.866  1.00 89.76           C  
ATOM    179  NE  ARG A 250      27.966   3.142   3.915  1.00 91.85           N  
ATOM    180  CZ  ARG A 250      27.889   1.907   3.424  1.00 92.31           C  
ATOM    181  NH1 ARG A 250      26.776   1.486   2.835  1.00 91.88           N  
ATOM    182  NH2 ARG A 250      28.930   1.090   3.523  1.00 91.71           N  
ATOM    183  N   LEU A 251      28.773   8.060   2.675  1.00 83.22           N  
ATOM    184  CA  LEU A 251      29.882   8.658   3.411  1.00 82.68           C  
ATOM    185  C   LEU A 251      30.272   7.864   4.654  1.00 82.78           C  
ATOM    186  O   LEU A 251      31.446   7.832   5.024  1.00 82.88           O  
ATOM    187  CB  LEU A 251      29.533  10.093   3.815  1.00 82.53           C  
ATOM    188  CG  LEU A 251      29.701  11.187   2.757  1.00 82.74           C  
ATOM    189  CD1 LEU A 251      31.178  11.411   2.483  1.00 82.74           C  
ATOM    190  CD2 LEU A 251      28.973  10.793   1.487  1.00 84.25           C  
ATOM    191  N   GLY A 252      29.294   7.232   5.297  1.00 83.22           N  
ATOM    192  CA  GLY A 252      29.582   6.492   6.512  1.00 84.58           C  
ATOM    193  C   GLY A 252      28.363   5.877   7.172  1.00 86.17           C  
ATOM    194  O   GLY A 252      27.468   6.584   7.636  1.00 85.98           O  
ATOM    195  N   ALA A 253      28.336   4.548   7.221  1.00 87.90           N  
ATOM    196  CA  ALA A 253      27.248   3.820   7.865  1.00 88.66           C  
ATOM    197  C   ALA A 253      27.674   3.282   9.231  1.00 88.92           C  
ATOM    198  O   ALA A 253      28.841   2.971   9.468  1.00 88.78           O  
ATOM    199  CB  ALA A 253      26.787   2.673   6.972  1.00 88.79           C  
ATOM    200  N   GLY A 254      26.704   3.179  10.133  1.00 88.93           N  
ATOM    201  CA  GLY A 254      26.970   2.664  11.463  1.00 88.38           C  
ATOM    202  C   GLY A 254      25.793   1.865  11.982  1.00 88.53           C  
ATOM    203  O   GLY A 254      24.955   1.408  11.204  1.00 88.30           O  
ATOM    204  N   GLN A 255      25.722   1.701  13.299  1.00 89.23           N  
ATOM    205  CA  GLN A 255      24.686   0.878  13.914  1.00 90.05           C  
ATOM    206  C   GLN A 255      23.442   1.677  14.291  1.00 88.57           C  
ATOM    207  O   GLN A 255      22.737   1.319  15.236  1.00 88.45           O  
ATOM    208  CB  GLN A 255      25.234   0.183  15.163  1.00 92.38           C  
ATOM    209  CG  GLN A 255      25.728   1.167  16.211  1.00 96.11           C  
ATOM    210  CD  GLN A 255      25.952   0.400  17.500  1.00 98.91           C  
ATOM    211  OE1 GLN A 255      25.000   0.051  18.201  1.00 99.84           O  
ATOM    212  NE2 GLN A 255      27.216   0.130  17.819  1.00 99.98           N  
ATOM    213  N   PHE A 256      23.177   2.753  13.556  1.00 85.91           N  
ATOM    214  CA  PHE A 256      21.969   3.541  13.765  1.00 83.78           C  
ATOM    215  C   PHE A 256      21.499   4.181  12.469  1.00 82.51           C  
ATOM    216  O   PHE A 256      20.630   5.052  12.458  1.00 82.23           O  
ATOM    217  CB  PHE A 256      22.213   4.623  14.816  1.00 84.13           C  
ATOM    218  CG  PHE A 256      22.156   4.118  16.227  1.00 84.18           C  
ATOM    219  CD1 PHE A 256      23.315   3.957  16.968  1.00 84.24           C  
ATOM    220  CD2 PHE A 256      20.942   3.791  16.808  1.00 84.14           C  
ATOM    221  CE1 PHE A 256      23.264   3.484  18.265  1.00 84.05           C  
ATOM    222  CE2 PHE A 256      20.884   3.318  18.104  1.00 84.02           C  
ATOM    223  CZ  PHE A 256      22.048   3.161  18.832  1.00 83.91           C  
ATOM    224  N   GLY A 257      22.082   3.733  11.364  1.00 81.11           N  
ATOM    225  CA  GLY A 257      21.737   4.291  10.073  1.00 79.91           C  
ATOM    226  C   GLY A 257      22.975   4.774   9.350  1.00 79.06           C  
ATOM    227  O   GLY A 257      24.082   4.687   9.878  1.00 78.97           O  
ATOM    228  N   GLU A 258      22.790   5.289   8.140  1.00 78.36           N  
ATOM    229  CA  GLU A 258      23.916   5.701   7.313  1.00 78.04           C  
ATOM    230  C   GLU A 258      23.948   7.213   7.114  1.00 75.95           C  
ATOM    231  O   GLU A 258      23.058   7.940   7.560  1.00 75.42           O  
ATOM    232  CB  GLU A 258      23.839   5.005   5.953  1.00 80.32           C  
ATOM    233  CG  GLU A 258      23.661   3.499   6.083  1.00 82.85           C  
ATOM    234  CD  GLU A 258      23.147   2.964   4.761  1.00 84.91           C  
ATOM    235  OE1 GLU A 258      23.971   2.487   3.950  1.00 86.01           O  
ATOM    236  OE2 GLU A 258      21.918   3.024   4.536  1.00 84.35           O  
ATOM    237  N   VAL A 259      24.997   7.681   6.446  1.00 73.71           N  
ATOM    238  CA  VAL A 259      25.082   9.071   6.011  1.00 71.01           C  
ATOM    239  C   VAL A 259      25.524   9.138   4.554  1.00 70.14           C  
ATOM    240  O   VAL A 259      26.641   8.768   4.198  1.00 68.89           O  
ATOM    241  CB  VAL A 259      26.090   9.869   6.860  1.00 70.39           C  
ATOM    242  CG1 VAL A 259      26.188  11.291   6.342  1.00 69.43           C  
ATOM    243  CG2 VAL A 259      25.661   9.865   8.318  1.00 70.18           C  
ATOM    244  N   TRP A 260      24.626   9.616   3.702  1.00 69.84           N  
ATOM    245  CA  TRP A 260      24.893   9.689   2.274  1.00 69.10           C  
ATOM    246  C   TRP A 260      25.133  11.123   1.838  1.00 67.26           C  
ATOM    247  O   TRP A 260      24.698  12.074   2.484  1.00 66.90           O  
ATOM    248  CB  TRP A 260      23.717   9.111   1.480  1.00 71.48           C  
ATOM    249  CG  TRP A 260      23.578   7.622   1.589  1.00 75.90           C  
ATOM    250  CD1 TRP A 260      23.151   6.915   2.676  1.00 77.51           C  
ATOM    251  CD2 TRP A 260      23.863   6.654   0.569  1.00 78.63           C  
ATOM    252  NE1 TRP A 260      23.153   5.569   2.398  1.00 79.52           N  
ATOM    253  CE2 TRP A 260      23.586   5.382   1.111  1.00 80.22           C  
ATOM    254  CE3 TRP A 260      24.326   6.740  -0.749  1.00 79.44           C  
ATOM    255  CZ2 TRP A 260      23.756   4.205   0.381  1.00 80.89           C  
ATOM    256  CZ3 TRP A 260      24.496   5.571  -1.472  1.00 79.81           C  
ATOM    257  CH2 TRP A 260      24.212   4.320  -0.905  1.00 81.49           C  
ATOM    258  N   MET A 261      25.844  11.270   0.727  1.00 65.52           N  
ATOM    259  CA  MET A 261      25.858  12.524  -0.008  1.00 63.83           C  
ATOM    260  C   MET A 261      24.967  12.351  -1.231  1.00 61.96           C  
ATOM    261  O   MET A 261      24.969  11.300  -1.865  1.00 61.73           O  
ATOM    262  CB  MET A 261      27.284  12.875  -0.437  1.00 65.06           C  
ATOM    263  CG  MET A 261      27.344  14.114  -1.313  1.00 66.20           C  
ATOM    264  SD  MET A 261      27.224  13.705  -3.063  1.00 68.41           S  
ATOM    265  CE  MET A 261      28.622  12.583  -3.226  1.00 67.73           C  
ATOM    266  N   GLY A 262      24.196  13.382  -1.552  1.00 60.43           N  
ATOM    267  CA  GLY A 262      23.256  13.279  -2.649  1.00 58.59           C  
ATOM    268  C   GLY A 262      22.827  14.649  -3.123  1.00 58.29           C  
ATOM    269  O   GLY A 262      23.457  15.650  -2.783  1.00 58.42           O  
ATOM    270  N   TYR A 263      21.756  14.698  -3.906  1.00 57.16           N  
ATOM    271  CA  TYR A 263      21.289  15.960  -4.451  1.00 58.08           C  
ATOM    272  C   TYR A 263      19.802  16.179  -4.235  1.00 57.82           C  
ATOM    273  O   TYR A 263      18.977  15.303  -4.476  1.00 57.45           O  
ATOM    274  CB  TYR A 263      21.627  16.035  -5.940  1.00 60.64           C  
ATOM    275  CG  TYR A 263      23.114  16.085  -6.191  1.00 64.82           C  
ATOM    276  CD1 TYR A 263      23.762  17.297  -6.405  1.00 65.97           C  
ATOM    277  CD2 TYR A 263      23.882  14.926  -6.161  1.00 66.57           C  
ATOM    278  CE1 TYR A 263      25.133  17.354  -6.577  1.00 66.45           C  
ATOM    279  CE2 TYR A 263      25.252  14.972  -6.330  1.00 67.61           C  
ATOM    280  CZ  TYR A 263      25.874  16.189  -6.536  1.00 68.15           C  
ATOM    281  OH  TYR A 263      27.241  16.242  -6.690  1.00 69.18           O  
ATOM    282  N   TYR A 264      19.469  17.376  -3.764  1.00 57.94           N  
ATOM    283  CA  TYR A 264      18.084  17.766  -3.552  1.00 59.67           C  
ATOM    284  C   TYR A 264      17.564  18.521  -4.768  1.00 62.14           C  
ATOM    285  O   TYR A 264      18.129  19.545  -5.167  1.00 61.91           O  
ATOM    286  CB  TYR A 264      17.974  18.641  -2.302  1.00 59.00           C  
ATOM    287  CG  TYR A 264      16.724  19.483  -2.240  1.00 59.32           C  
ATOM    288  CD1 TYR A 264      15.504  18.931  -1.870  1.00 59.55           C  
ATOM    289  CD2 TYR A 264      16.767  20.839  -2.538  1.00 60.73           C  
ATOM    290  CE1 TYR A 264      14.358  19.710  -1.797  1.00 61.10           C  
ATOM    291  CE2 TYR A 264      15.628  21.625  -2.467  1.00 62.83           C  
ATOM    292  CZ  TYR A 264      14.428  21.057  -2.096  1.00 62.38           C  
ATOM    293  OH  TYR A 264      13.300  21.845  -2.018  1.00 62.91           O  
ATOM    294  N   ASN A 265      16.479  18.008  -5.347  1.00 63.43           N  
ATOM    295  CA  ASN A 265      15.962  18.501  -6.619  1.00 64.74           C  
ATOM    296  C   ASN A 265      17.094  18.765  -7.608  1.00 66.01           C  
ATOM    297  O   ASN A 265      17.055  19.718  -8.388  1.00 64.93           O  
ATOM    298  CB  ASN A 265      15.140  19.779  -6.413  1.00 65.57           C  
ATOM    299  CG  ASN A 265      13.727  19.498  -5.921  1.00 66.40           C  
ATOM    300  OD1 ASN A 265      13.035  20.397  -5.438  1.00 67.57           O  
ATOM    301  ND2 ASN A 265      13.290  18.248  -6.048  1.00 65.47           N  
ATOM    302  N   GLY A 266      18.115  17.911  -7.554  1.00 68.00           N  
ATOM    303  CA  GLY A 266      19.152  17.905  -8.571  1.00 69.08           C  
ATOM    304  C   GLY A 266      20.114  19.079  -8.551  1.00 70.03           C  
ATOM    305  O   GLY A 266      21.241  18.964  -9.036  1.00 71.52           O  
ATOM    306  N   HIS A 267      19.686  20.207  -7.994  1.00 69.98           N  
ATOM    307  CA  HIS A 267      20.468  21.434  -8.102  1.00 70.54           C  
ATOM    308  C   HIS A 267      21.399  21.677  -6.915  1.00 69.85           C  
ATOM    309  O   HIS A 267      22.414  22.361  -7.047  1.00 69.94           O  
ATOM    310  CB  HIS A 267      19.537  22.641  -8.289  1.00 72.74           C  
ATOM    311  CG  HIS A 267      18.654  22.917  -7.112  1.00 74.01           C  
ATOM    312  ND1 HIS A 267      17.426  22.315  -6.944  1.00 74.48           N  
ATOM    313  CD2 HIS A 267      18.819  23.737  -6.047  1.00 75.01           C  
ATOM    314  CE1 HIS A 267      16.872  22.752  -5.827  1.00 75.45           C  
ATOM    315  NE2 HIS A 267      17.697  23.616  -5.264  1.00 75.63           N  
ATOM    316  N   THR A 268      21.054  21.121  -5.759  1.00 68.36           N  
ATOM    317  CA  THR A 268      21.871  21.290  -4.562  1.00 66.04           C  
ATOM    318  C   THR A 268      22.401  19.946  -4.084  1.00 64.86           C  
ATOM    319  O   THR A 268      21.660  18.966  -4.038  1.00 65.56           O  
ATOM    320  CB  THR A 268      21.056  21.905  -3.405  1.00 65.88           C  
ATOM    321  OG1 THR A 268      20.584  23.203  -3.785  1.00 63.74           O  
ATOM    322  CG2 THR A 268      21.918  22.028  -2.157  1.00 66.00           C  
ATOM    323  N   LYS A 269      23.678  19.890  -3.727  1.00 62.48           N  
ATOM    324  CA  LYS A 269      24.194  18.682  -3.105  1.00 60.57           C  
ATOM    325  C   LYS A 269      24.085  18.816  -1.594  1.00 58.76           C  
ATOM    326  O   LYS A 269      24.279  19.890  -1.019  1.00 58.14           O  
ATOM    327  CB  LYS A 269      25.646  18.423  -3.515  1.00 61.34           C  
ATOM    328  CG  LYS A 269      26.643  19.275  -2.766  1.00 62.31           C  
ATOM    329  CD  LYS A 269      28.008  18.706  -3.110  1.00 64.14           C  
ATOM    330  CE  LYS A 269      28.070  17.181  -3.068  1.00 64.34           C  
ATOM    331  NZ  LYS A 269      29.427  16.661  -3.424  1.00 62.46           N  
ATOM    332  N   VAL A 270      23.755  17.702  -0.950  1.00 56.50           N  
ATOM    333  CA  VAL A 270      23.391  17.710   0.458  1.00 52.28           C  
ATOM    334  C   VAL A 270      24.002  16.518   1.180  1.00 51.31           C  
ATOM    335  O   VAL A 270      24.403  15.538   0.554  1.00 50.51           O  
ATOM    336  CB  VAL A 270      21.853  17.643   0.639  1.00 51.60           C  
ATOM    337  CG1 VAL A 270      21.201  18.890   0.058  1.00 47.59           C  
ATOM    338  CG2 VAL A 270      21.303  16.390  -0.036  1.00 48.03           C  
ATOM    339  N   ALA A 271      24.076  16.620   2.504  1.00 50.07           N  
ATOM    340  CA  ALA A 271      24.413  15.483   3.349  1.00 49.23           C  
ATOM    341  C   ALA A 271      23.127  14.931   3.957  1.00 49.44           C  
ATOM    342  O   ALA A 271      22.284  15.677   4.460  1.00 47.86           O  
ATOM    343  CB  ALA A 271      25.376  15.914   4.448  1.00 48.37           C  
ATOM    344  N   VAL A 272      22.974  13.613   3.902  1.00 50.11           N  
ATOM    345  CA  VAL A 272      21.729  12.987   4.318  1.00 51.68           C  
ATOM    346  C   VAL A 272      21.967  11.929   5.384  1.00 52.33           C  
ATOM    347  O   VAL A 272      22.612  10.908   5.141  1.00 53.19           O  
ATOM    348  CB  VAL A 272      21.014  12.332   3.119  1.00 52.66           C  
ATOM    349  CG1 VAL A 272      19.640  11.823   3.541  1.00 54.01           C  
ATOM    350  CG2 VAL A 272      20.884  13.337   1.984  1.00 53.30           C  
ATOM    351  N   LYS A 273      21.442  12.184   6.577  1.00 52.50           N  
ATOM    352  CA  LYS A 273      21.497  11.213   7.659  1.00 52.42           C  
ATOM    353  C   LYS A 273      20.199  10.413   7.653  1.00 54.24           C  
ATOM    354  O   LYS A 273      19.102  10.974   7.713  1.00 53.97           O  
ATOM    355  CB  LYS A 273      21.664  11.931   9.002  1.00 50.62           C  
ATOM    356  CG  LYS A 273      22.026  10.991  10.144  1.00 49.26           C  
ATOM    357  CD  LYS A 273      22.181  11.712  11.478  1.00 48.64           C  
ATOM    358  CE  LYS A 273      23.000  10.969  12.529  1.00 48.69           C  
ATOM    359  NZ  LYS A 273      22.931  11.611  13.876  1.00 47.06           N  
ATOM    360  N   SER A 274      20.324   9.095   7.566  1.00 55.97           N  
ATOM    361  CA  SER A 274      19.152   8.233   7.558  1.00 58.48           C  
ATOM    362  C   SER A 274      19.143   7.338   8.784  1.00 60.08           C  
ATOM    363  O   SER A 274      20.191   6.915   9.270  1.00 59.80           O  
ATOM    364  CB  SER A 274      19.128   7.372   6.293  1.00 56.81           C  
ATOM    365  OG  SER A 274      20.219   6.472   6.273  1.00 57.38           O  
ATOM    366  N   LEU A 275      17.942   7.062   9.281  1.00 62.89           N  
ATOM    367  CA  LEU A 275      17.748   6.174  10.420  1.00 65.15           C  
ATOM    368  C   LEU A 275      17.475   4.754   9.938  1.00 67.18           C  
ATOM    369  O   LEU A 275      16.631   4.561   9.061  1.00 68.04           O  
ATOM    370  CB  LEU A 275      16.562   6.659  11.258  1.00 63.94           C  
ATOM    371  CG  LEU A 275      16.113   5.708  12.370  1.00 62.90           C  
ATOM    372  CD1 LEU A 275      17.250   5.508  13.358  1.00 61.53           C  
ATOM    373  CD2 LEU A 275      14.886   6.276  13.066  1.00 62.01           C  
ATOM    374  N   LYS A 276      18.173   3.770  10.499  1.00 69.52           N  
ATOM    375  CA  LYS A 276      17.844   2.375  10.221  1.00 72.56           C  
ATOM    376  C   LYS A 276      16.818   1.868  11.234  1.00 74.31           C  
ATOM    377  O   LYS A 276      16.912   2.133  12.434  1.00 74.57           O  
ATOM    378  CB  LYS A 276      19.102   1.497  10.256  1.00 71.97           C  
ATOM    379  CG  LYS A 276      19.482   1.036  11.652  1.00 72.18           C  
ATOM    380  CD  LYS A 276      20.173  -0.311  11.492  1.00 73.03           C  
ATOM    381  CE  LYS A 276      20.579  -1.027  12.773  1.00 73.24           C  
ATOM    382  NZ  LYS A 276      21.704  -0.344  13.466  1.00 71.35           N  
ATOM    383  N   GLN A 277      15.827   1.138  10.735  1.00 76.41           N  
ATOM    384  CA  GLN A 277      14.676   0.749  11.541  1.00 78.18           C  
ATOM    385  C   GLN A 277      15.088  -0.148  12.701  1.00 78.74           C  
ATOM    386  O   GLN A 277      15.964  -1.006  12.570  1.00 78.72           O  
ATOM    387  CB  GLN A 277      13.639   0.024  10.676  1.00 79.64           C  
ATOM    388  CG  GLN A 277      13.019   0.922   9.610  1.00 82.01           C  
ATOM    389  CD  GLN A 277      13.965   1.251   8.462  1.00 83.73           C  
ATOM    390  OE1 GLN A 277      15.097   0.766   8.414  1.00 84.03           O  
ATOM    391  NE2 GLN A 277      13.500   2.079   7.530  1.00 84.38           N  
ATOM    392  N   GLY A 278      14.448   0.066  13.846  1.00 79.05           N  
ATOM    393  CA  GLY A 278      14.676  -0.792  14.993  1.00 80.02           C  
ATOM    394  C   GLY A 278      15.747  -0.294  15.945  1.00 80.40           C  
ATOM    395  O   GLY A 278      15.568  -0.346  17.162  1.00 81.69           O  
ATOM    396  N   SER A 279      16.858   0.192  15.397  1.00 79.81           N  
ATOM    397  CA  SER A 279      18.001   0.597  16.212  1.00 78.91           C  
ATOM    398  C   SER A 279      17.620   1.622  17.280  1.00 78.14           C  
ATOM    399  O   SER A 279      18.249   1.702  18.336  1.00 77.81           O  
ATOM    400  CB  SER A 279      19.108   1.167  15.321  1.00 78.44           C  
ATOM    401  OG  SER A 279      18.643   2.277  14.575  1.00 78.32           O  
ATOM    402  N   MET A 280      16.584   2.406  17.002  1.00 77.61           N  
ATOM    403  CA  MET A 280      16.121   3.408  17.952  1.00 77.02           C  
ATOM    404  C   MET A 280      14.765   3.988  17.568  1.00 76.52           C  
ATOM    405  O   MET A 280      14.262   3.818  16.456  1.00 74.74           O  
ATOM    406  CB  MET A 280      17.145   4.538  18.061  1.00 78.00           C  
ATOM    407  CG  MET A 280      17.403   5.209  16.724  1.00 79.10           C  
ATOM    408  SD  MET A 280      18.582   6.567  16.835  1.00 80.26           S  
ATOM    409  CE  MET A 280      17.693   7.697  17.907  1.00 79.00           C  
ATOM    410  N   SER A 281      14.171   4.691  18.525  1.00 76.68           N  
ATOM    411  CA  SER A 281      12.877   5.323  18.326  1.00 77.18           C  
ATOM    412  C   SER A 281      12.919   6.301  17.158  1.00 77.18           C  
ATOM    413  O   SER A 281      13.862   7.078  17.004  1.00 76.17           O  
ATOM    414  CB  SER A 281      12.458   6.059  19.602  1.00 77.73           C  
ATOM    415  OG  SER A 281      11.241   6.761  19.415  1.00 79.48           O  
ATOM    416  N   PRO A 282      11.881   6.272  16.310  1.00 77.55           N  
ATOM    417  CA  PRO A 282      11.727   7.256  15.235  1.00 77.74           C  
ATOM    418  C   PRO A 282      11.689   8.669  15.807  1.00 77.86           C  
ATOM    419  O   PRO A 282      12.154   9.618  15.181  1.00 78.68           O  
ATOM    420  CB  PRO A 282      10.401   6.868  14.580  1.00 77.04           C  
ATOM    421  CG  PRO A 282      10.233   5.426  14.906  1.00 77.00           C  
ATOM    422  CD  PRO A 282      10.813   5.259  16.281  1.00 77.66           C  
ATOM    423  N   ASP A 283      11.137   8.797  17.007  1.00 77.64           N  
ATOM    424  CA  ASP A 283      11.022  10.094  17.658  1.00 77.73           C  
ATOM    425  C   ASP A 283      12.357  10.513  18.271  1.00 75.74           C  
ATOM    426  O   ASP A 283      12.639  11.701  18.437  1.00 75.38           O  
ATOM    427  CB  ASP A 283       9.942  10.035  18.742  1.00 80.45           C  
ATOM    428  CG  ASP A 283       8.625   9.481  18.220  1.00 83.96           C  
ATOM    429  OD1 ASP A 283       8.065  10.066  17.266  1.00 84.51           O  
ATOM    430  OD2 ASP A 283       8.153   8.457  18.763  1.00 85.66           O  
ATOM    431  N   ALA A 284      13.179   9.521  18.601  1.00 72.59           N  
ATOM    432  CA  ALA A 284      14.491   9.769  19.188  1.00 68.46           C  
ATOM    433  C   ALA A 284      15.456  10.267  18.121  1.00 66.07           C  
ATOM    434  O   ALA A 284      16.331  11.092  18.381  1.00 66.38           O  
ATOM    435  CB  ALA A 284      15.024   8.492  19.819  1.00 68.73           C  
ATOM    436  N   PHE A 285      15.289   9.751  16.909  1.00 62.46           N  
ATOM    437  CA  PHE A 285      16.076  10.202  15.769  1.00 59.38           C  
ATOM    438  C   PHE A 285      15.682  11.641  15.447  1.00 58.32           C  
ATOM    439  O   PHE A 285      16.526  12.523  15.281  1.00 58.39           O  
ATOM    440  CB  PHE A 285      15.805   9.294  14.563  1.00 57.89           C  
ATOM    441  CG  PHE A 285      16.665   9.591  13.361  1.00 57.30           C  
ATOM    442  CD1 PHE A 285      18.020   9.287  13.364  1.00 56.47           C  
ATOM    443  CD2 PHE A 285      16.110  10.141  12.213  1.00 55.94           C  
ATOM    444  CE1 PHE A 285      18.806   9.522  12.244  1.00 55.18           C  
ATOM    445  CE2 PHE A 285      16.888  10.378  11.092  1.00 55.53           C  
ATOM    446  CZ  PHE A 285      18.238  10.068  11.107  1.00 55.45           C  
ATOM    447  N   LEU A 286      14.375  11.871  15.377  1.00 56.49           N  
ATOM    448  CA  LEU A 286      13.841  13.175  15.018  1.00 54.45           C  
ATOM    449  C   LEU A 286      14.142  14.210  16.086  1.00 52.63           C  
ATOM    450  O   LEU A 286      14.191  15.406  15.803  1.00 52.06           O  
ATOM    451  CB  LEU A 286      12.329  13.089  14.811  1.00 56.80           C  
ATOM    452  CG  LEU A 286      11.923  12.226  13.614  1.00 58.51           C  
ATOM    453  CD1 LEU A 286      10.405  12.219  13.488  1.00 58.41           C  
ATOM    454  CD2 LEU A 286      12.567  12.766  12.343  1.00 57.85           C  
ATOM    455  N   ALA A 287      14.338  13.749  17.317  1.00 51.05           N  
ATOM    456  CA  ALA A 287      14.682  14.649  18.412  1.00 49.71           C  
ATOM    457  C   ALA A 287      15.838  15.547  17.988  1.00 48.87           C  
ATOM    458  O   ALA A 287      15.854  16.741  18.286  1.00 48.86           O  
ATOM    459  CB  ALA A 287      15.068  13.850  19.644  1.00 48.82           C  
ATOM    460  N   GLU A 288      16.800  14.964  17.281  1.00 47.74           N  
ATOM    461  CA  GLU A 288      17.932  15.721  16.776  1.00 47.83           C  
ATOM    462  C   GLU A 288      17.459  16.784  15.793  1.00 49.24           C  
ATOM    463  O   GLU A 288      17.693  17.984  15.970  1.00 49.04           O  
ATOM    464  CB  GLU A 288      18.927  14.793  16.078  1.00 46.90           C  
ATOM    465  CG  GLU A 288      20.108  15.571  15.520  1.00 47.85           C  
ATOM    466  CD  GLU A 288      21.122  14.701  14.811  1.00 48.95           C  
ATOM    467  OE1 GLU A 288      20.885  13.479  14.702  1.00 50.40           O  
ATOM    468  OE2 GLU A 288      22.155  15.243  14.361  1.00 46.54           O  
ATOM    469  N   ALA A 289      16.780  16.330  14.745  1.00 49.41           N  
ATOM    470  CA  ALA A 289      16.275  17.227  13.714  1.00 49.53           C  
ATOM    471  C   ALA A 289      15.546  18.393  14.365  1.00 49.57           C  
ATOM    472  O   ALA A 289      15.572  19.532  13.903  1.00 48.52           O  
ATOM    473  CB  ALA A 289      15.332  16.474  12.790  1.00 48.43           C  
ATOM    474  N   ASN A 290      14.890  18.087  15.475  1.00 50.22           N  
ATOM    475  CA  ASN A 290      14.042  19.057  16.132  1.00 50.29           C  
ATOM    476  C   ASN A 290      14.870  20.134  16.818  1.00 48.93           C  
ATOM    477  O   ASN A 290      14.515  21.309  16.752  1.00 48.69           O  
ATOM    478  CB  ASN A 290      13.146  18.362  17.150  1.00 52.77           C  
ATOM    479  CG  ASN A 290      11.956  19.203  17.527  1.00 56.16           C  
ATOM    480  OD1 ASN A 290      11.258  19.733  16.659  1.00 58.30           O  
ATOM    481  ND2 ASN A 290      11.714  19.340  18.826  1.00 58.27           N  
ATOM    482  N   LEU A 291      15.963  19.740  17.467  1.00 47.65           N  
ATOM    483  CA  LEU A 291      16.885  20.710  18.053  1.00 47.30           C  
ATOM    484  C   LEU A 291      17.434  21.641  16.977  1.00 47.46           C  
ATOM    485  O   LEU A 291      17.524  22.859  17.148  1.00 46.76           O  
ATOM    486  CB  LEU A 291      18.056  20.007  18.740  1.00 46.76           C  
ATOM    487  CG  LEU A 291      17.918  19.544  20.190  1.00 47.85           C  
ATOM    488  CD1 LEU A 291      19.306  19.271  20.744  1.00 45.35           C  
ATOM    489  CD2 LEU A 291      17.216  20.610  21.028  1.00 47.66           C  
ATOM    490  N   MET A 292      17.801  21.044  15.849  1.00 46.87           N  
ATOM    491  CA  MET A 292      18.381  21.790  14.744  1.00 45.76           C  
ATOM    492  C   MET A 292      17.453  22.897  14.251  1.00 46.70           C  
ATOM    493  O   MET A 292      17.923  23.967  13.867  1.00 47.58           O  
ATOM    494  CB  MET A 292      18.727  20.833  13.604  1.00 42.58           C  
ATOM    495  CG  MET A 292      19.702  19.766  14.068  1.00 43.32           C  
ATOM    496  SD  MET A 292      20.155  18.589  12.794  1.00 43.02           S  
ATOM    497  CE  MET A 292      21.007  19.664  11.618  1.00 44.26           C  
ATOM    498  N   LYS A 293      16.147  22.652  14.267  1.00 46.58           N  
ATOM    499  CA  LYS A 293      15.194  23.687  13.892  1.00 45.64           C  
ATOM    500  C   LYS A 293      15.306  24.827  14.890  1.00 45.67           C  
ATOM    501  O   LYS A 293      15.322  26.008  14.533  1.00 45.15           O  
ATOM    502  CB  LYS A 293      13.768  23.138  13.909  1.00 46.25           C  
ATOM    503  CG  LYS A 293      13.627  21.864  13.101  1.00 50.21           C  
ATOM    504  CD  LYS A 293      12.188  21.516  12.753  1.00 52.36           C  
ATOM    505  CE  LYS A 293      12.051  20.023  12.499  1.00 54.85           C  
ATOM    506  NZ  LYS A 293      10.699  19.643  12.006  1.00 55.61           N  
ATOM    507  N   GLN A 294      15.400  24.449  16.161  1.00 45.23           N  
ATOM    508  CA  GLN A 294      15.333  25.397  17.265  1.00 45.91           C  
ATOM    509  C   GLN A 294      16.633  26.151  17.480  1.00 47.46           C  
ATOM    510  O   GLN A 294      16.638  27.261  18.011  1.00 47.63           O  
ATOM    511  CB  GLN A 294      14.965  24.665  18.552  1.00 44.29           C  
ATOM    512  CG  GLN A 294      13.612  24.010  18.455  1.00 42.57           C  
ATOM    513  CD  GLN A 294      13.362  23.284  19.752  1.00 43.22           C  
ATOM    514  OE1 GLN A 294      12.291  22.719  19.956  1.00 44.68           O  
ATOM    515  NE2 GLN A 294      14.350  23.295  20.642  1.00 43.38           N  
ATOM    516  N   LEU A 295      17.737  25.533  17.075  1.00 48.49           N  
ATOM    517  CA  LEU A 295      19.059  26.084  17.329  1.00 48.18           C  
ATOM    518  C   LEU A 295      19.703  26.586  16.046  1.00 50.50           C  
ATOM    519  O   LEU A 295      20.906  26.421  15.838  1.00 52.03           O  
ATOM    520  CB  LEU A 295      19.952  25.022  17.974  1.00 45.40           C  
ATOM    521  CG  LEU A 295      19.508  24.629  19.385  1.00 43.26           C  
ATOM    522  CD1 LEU A 295      20.340  23.458  19.893  1.00 41.14           C  
ATOM    523  CD2 LEU A 295      19.657  25.829  20.305  1.00 42.46           C  
ATOM    524  N   GLN A 296      18.903  27.197  15.179  1.00 52.32           N  
ATOM    525  CA  GLN A 296      19.440  27.739  13.938  1.00 52.34           C  
ATOM    526  C   GLN A 296      20.304  28.944  14.249  1.00 50.83           C  
ATOM    527  O   GLN A 296      20.017  29.715  15.165  1.00 50.58           O  
ATOM    528  CB  GLN A 296      18.309  28.128  12.983  1.00 55.38           C  
ATOM    529  CG  GLN A 296      17.538  26.911  12.480  1.00 64.15           C  
ATOM    530  CD  GLN A 296      18.393  25.880  11.736  1.00 68.71           C  
ATOM    531  OE1 GLN A 296      18.149  25.590  10.563  1.00 71.73           O  
ATOM    532  NE2 GLN A 296      19.394  25.321  12.417  1.00 69.64           N  
ATOM    533  N   HIS A 297      21.378  29.096  13.485  1.00 49.83           N  
ATOM    534  CA  HIS A 297      22.374  30.116  13.778  1.00 47.42           C  
ATOM    535  C   HIS A 297      23.475  30.049  12.734  1.00 46.04           C  
ATOM    536  O   HIS A 297      23.816  28.969  12.252  1.00 46.33           O  
ATOM    537  CB  HIS A 297      22.957  29.881  15.172  1.00 46.56           C  
ATOM    538  CG  HIS A 297      23.770  31.025  15.688  1.00 46.78           C  
ATOM    539  ND1 HIS A 297      25.059  31.272  15.266  1.00 46.75           N  
ATOM    540  CD2 HIS A 297      23.483  31.983  16.600  1.00 44.82           C  
ATOM    541  CE1 HIS A 297      25.531  32.332  15.897  1.00 45.58           C  
ATOM    542  NE2 HIS A 297      24.594  32.781  16.713  1.00 45.20           N  
ATOM    543  N   GLN A 298      24.031  31.202  12.385  1.00 44.99           N  
ATOM    544  CA  GLN A 298      25.007  31.272  11.307  1.00 46.80           C  
ATOM    545  C   GLN A 298      26.231  30.405  11.584  1.00 46.63           C  
ATOM    546  O   GLN A 298      26.872  29.924  10.651  1.00 47.50           O  
ATOM    547  CB  GLN A 298      25.451  32.717  11.096  1.00 49.47           C  
ATOM    548  CG  GLN A 298      26.154  33.275  12.317  1.00 53.22           C  
ATOM    549  CD  GLN A 298      26.689  34.642  11.960  1.00 54.59           C  
ATOM    550  OE1 GLN A 298      26.938  34.936  10.788  1.00 54.57           O  
ATOM    551  NE2 GLN A 298      26.871  35.491  12.970  1.00 54.20           N  
ATOM    552  N   ARG A 299      26.550  30.212  12.862  1.00 45.49           N  
ATOM    553  CA  ARG A 299      27.723  29.442  13.258  1.00 44.34           C  
ATOM    554  C   ARG A 299      27.403  27.970  13.529  1.00 44.03           C  
ATOM    555  O   ARG A 299      28.280  27.193  13.905  1.00 43.97           O  
ATOM    556  CB  ARG A 299      28.357  30.058  14.503  1.00 44.69           C  
ATOM    557  CG  ARG A 299      28.710  31.516  14.307  1.00 45.30           C  
ATOM    558  CD  ARG A 299      29.363  31.801  12.975  1.00 45.83           C  
ATOM    559  NE  ARG A 299      29.852  33.174  12.916  1.00 50.38           N  
ATOM    560  CZ  ARG A 299      30.246  33.786  11.803  1.00 53.10           C  
ATOM    561  NH1 ARG A 299      30.212  33.146  10.640  1.00 53.66           N  
ATOM    562  NH2 ARG A 299      30.675  35.041  11.855  1.00 53.83           N  
ATOM    563  N   LEU A 300      26.141  27.594  13.352  1.00 43.53           N  
ATOM    564  CA  LEU A 300      25.735  26.197  13.462  1.00 43.24           C  
ATOM    565  C   LEU A 300      25.458  25.656  12.070  1.00 43.71           C  
ATOM    566  O   LEU A 300      25.075  26.418  11.187  1.00 45.04           O  
ATOM    567  CB  LEU A 300      24.471  26.074  14.316  1.00 42.28           C  
ATOM    568  CG  LEU A 300      24.631  25.944  15.832  1.00 40.74           C  
ATOM    569  CD1 LEU A 300      25.107  24.552  16.160  1.00 41.73           C  
ATOM    570  CD2 LEU A 300      25.610  26.980  16.354  1.00 39.59           C  
ATOM    571  N   VAL A 301      25.657  24.359  11.867  1.00 43.69           N  
ATOM    572  CA  VAL A 301      25.245  23.740  10.619  1.00 44.39           C  
ATOM    573  C   VAL A 301      23.732  23.875  10.541  1.00 47.43           C  
ATOM    574  O   VAL A 301      23.020  23.546  11.491  1.00 48.94           O  
ATOM    575  CB  VAL A 301      25.640  22.244  10.564  1.00 42.24           C  
ATOM    576  CG1 VAL A 301      25.031  21.498  11.736  1.00 44.02           C  
ATOM    577  CG2 VAL A 301      25.174  21.630   9.259  1.00 38.10           C  
ATOM    578  N   ARG A 302      23.240  24.378   9.415  1.00 49.66           N  
ATOM    579  CA  ARG A 302      21.814  24.622   9.275  1.00 51.72           C  
ATOM    580  C   ARG A 302      21.109  23.402   8.702  1.00 51.14           C  
ATOM    581  O   ARG A 302      21.536  22.798   7.714  1.00 49.18           O  
ATOM    582  CB  ARG A 302      21.566  25.840   8.381  1.00 55.70           C  
ATOM    583  CG  ARG A 302      20.092  26.223   8.309  1.00 62.63           C  
ATOM    584  CD  ARG A 302      19.832  27.726   8.179  1.00 69.69           C  
ATOM    585  NE  ARG A 302      18.478  28.020   7.707  1.00 75.49           N  
ATOM    586  CZ  ARG A 302      17.485  28.459   8.480  1.00 77.44           C  
ATOM    587  NH1 ARG A 302      17.687  28.662   9.778  1.00 77.14           N  
ATOM    588  NH2 ARG A 302      16.287  28.695   7.954  1.00 77.32           N  
ATOM    589  N   LEU A 303      20.014  23.031   9.356  1.00 51.14           N  
ATOM    590  CA  LEU A 303      19.128  22.003   8.839  1.00 50.75           C  
ATOM    591  C   LEU A 303      18.585  22.470   7.496  1.00 50.78           C  
ATOM    592  O   LEU A 303      18.160  23.614   7.335  1.00 49.33           O  
ATOM    593  CB  LEU A 303      17.973  21.766   9.813  1.00 50.25           C  
ATOM    594  CG  LEU A 303      16.901  20.765   9.377  1.00 50.16           C  
ATOM    595  CD1 LEU A 303      17.506  19.377   9.233  1.00 48.95           C  
ATOM    596  CD2 LEU A 303      15.780  20.754  10.402  1.00 50.05           C  
ATOM    597  N   TYR A 304      18.609  21.570   6.523  1.00 52.43           N  
ATOM    598  CA  TYR A 304      18.189  21.905   5.172  1.00 54.41           C  
ATOM    599  C   TYR A 304      16.780  21.379   4.902  1.00 54.91           C  
ATOM    600  O   TYR A 304      15.913  22.099   4.399  1.00 54.69           O  
ATOM    601  CB  TYR A 304      19.181  21.313   4.171  1.00 55.23           C  
ATOM    602  CG  TYR A 304      19.009  21.818   2.760  1.00 57.53           C  
ATOM    603  CD1 TYR A 304      18.455  21.006   1.779  1.00 60.13           C  
ATOM    604  CD2 TYR A 304      19.404  23.104   2.406  1.00 57.72           C  
ATOM    605  CE1 TYR A 304      18.298  21.458   0.480  1.00 62.50           C  
ATOM    606  CE2 TYR A 304      19.250  23.567   1.110  1.00 60.49           C  
ATOM    607  CZ  TYR A 304      18.695  22.738   0.148  1.00 62.62           C  
ATOM    608  OH  TYR A 304      18.533  23.177  -1.149  1.00 62.12           O  
ATOM    609  N   ALA A 305      16.558  20.115   5.249  1.00 54.75           N  
ATOM    610  CA  ALA A 305      15.270  19.470   5.034  1.00 54.05           C  
ATOM    611  C   ALA A 305      15.158  18.221   5.890  1.00 54.31           C  
ATOM    612  O   ALA A 305      16.147  17.703   6.410  1.00 53.09           O  
ATOM    613  CB  ALA A 305      15.110  19.104   3.571  1.00 54.35           C  
ATOM    614  N   VAL A 306      13.934  17.732   6.034  1.00 54.00           N  
ATOM    615  CA  VAL A 306      13.716  16.474   6.724  1.00 56.09           C  
ATOM    616  C   VAL A 306      12.615  15.658   6.065  1.00 56.41           C  
ATOM    617  O   VAL A 306      11.619  16.195   5.583  1.00 54.93           O  
ATOM    618  CB  VAL A 306      13.331  16.701   8.195  1.00 56.80           C  
ATOM    619  CG1 VAL A 306      12.028  17.479   8.277  1.00 56.86           C  
ATOM    620  CG2 VAL A 306      13.203  15.362   8.908  1.00 56.85           C  
ATOM    621  N   VAL A 307      12.815  14.345   6.043  1.00 58.61           N  
ATOM    622  CA  VAL A 307      11.784  13.406   5.623  1.00 61.59           C  
ATOM    623  C   VAL A 307      11.340  12.579   6.827  1.00 63.71           C  
ATOM    624  O   VAL A 307      12.138  11.834   7.392  1.00 64.82           O  
ATOM    625  CB  VAL A 307      12.319  12.454   4.543  1.00 60.97           C  
ATOM    626  CG1 VAL A 307      11.261  11.436   4.176  1.00 62.05           C  
ATOM    627  CG2 VAL A 307      12.744  13.248   3.323  1.00 61.37           C  
ATOM    628  N   THR A 308      10.075  12.704   7.215  1.00 66.65           N  
ATOM    629  CA  THR A 308       9.603  12.084   8.450  1.00 70.50           C  
ATOM    630  C   THR A 308       9.282  10.590   8.330  1.00 72.91           C  
ATOM    631  O   THR A 308       9.705   9.809   9.182  1.00 74.04           O  
ATOM    632  CB  THR A 308       8.347  12.789   8.989  1.00 70.49           C  
ATOM    633  OG1 THR A 308       8.629  14.180   9.187  1.00 70.14           O  
ATOM    634  CG2 THR A 308       7.928  12.175  10.316  1.00 70.24           C  
ATOM    635  N   GLN A 309       8.546  10.196   7.294  1.00 74.45           N  
ATOM    636  CA  GLN A 309       8.190   8.789   7.103  1.00 76.39           C  
ATOM    637  C   GLN A 309       9.449   7.934   7.059  1.00 76.35           C  
ATOM    638  O   GLN A 309      10.531   8.442   6.768  1.00 77.21           O  
ATOM    639  CB  GLN A 309       7.417   8.605   5.793  1.00 79.14           C  
ATOM    640  CG  GLN A 309       6.354   9.674   5.577  1.00 83.41           C  
ATOM    641  CD  GLN A 309       5.342   9.708   6.708  1.00 85.07           C  
ATOM    642  OE1 GLN A 309       5.150  10.740   7.356  1.00 85.67           O  
ATOM    643  NE2 GLN A 309       4.686   8.577   6.950  1.00 85.70           N  
ATOM    644  N   GLU A 310       9.311   6.643   7.346  1.00 75.94           N  
ATOM    645  CA  GLU A 310      10.433   5.718   7.222  1.00 76.36           C  
ATOM    646  C   GLU A 310      10.697   5.414   5.751  1.00 74.61           C  
ATOM    647  O   GLU A 310       9.760   5.315   4.961  1.00 75.50           O  
ATOM    648  CB  GLU A 310      10.137   4.409   7.960  1.00 79.29           C  
ATOM    649  CG  GLU A 310      10.150   4.557   9.477  1.00 84.03           C  
ATOM    650  CD  GLU A 310      10.491   3.213  10.118  1.00 86.69           C  
ATOM    651  OE1 GLU A 310       9.999   2.170   9.630  1.00 86.48           O  
ATOM    652  OE2 GLU A 310      11.256   3.204  11.109  1.00 87.21           O  
ATOM    653  N   PRO A 311      11.976   5.279   5.362  1.00 73.32           N  
ATOM    654  CA  PRO A 311      13.139   5.595   6.202  1.00 71.67           C  
ATOM    655  C   PRO A 311      13.308   7.102   6.416  1.00 68.95           C  
ATOM    656  O   PRO A 311      13.220   7.890   5.471  1.00 67.93           O  
ATOM    657  CB  PRO A 311      14.315   4.987   5.436  1.00 72.41           C  
ATOM    658  CG  PRO A 311      13.863   4.964   4.011  1.00 72.20           C  
ATOM    659  CD  PRO A 311      12.375   4.725   4.054  1.00 72.76           C  
ATOM    660  N   ILE A 312      13.555   7.494   7.661  1.00 65.36           N  
ATOM    661  CA  ILE A 312      13.627   8.904   8.015  1.00 62.69           C  
ATOM    662  C   ILE A 312      14.967   9.508   7.611  1.00 60.58           C  
ATOM    663  O   ILE A 312      16.018   8.899   7.815  1.00 60.78           O  
ATOM    664  CB  ILE A 312      13.484   9.103   9.526  1.00 64.05           C  
ATOM    665  CG1 ILE A 312      12.247   8.362  10.030  1.00 64.28           C  
ATOM    666  CG2 ILE A 312      13.377  10.586   9.847  1.00 63.40           C  
ATOM    667  CD1 ILE A 312      12.101   8.389  11.536  1.00 64.93           C  
ATOM    668  N   TYR A 313      14.925  10.708   7.038  1.00 57.74           N  
ATOM    669  CA  TYR A 313      16.142  11.437   6.700  1.00 55.02           C  
ATOM    670  C   TYR A 313      16.185  12.785   7.404  1.00 52.71           C  
ATOM    671  O   TYR A 313      15.188  13.508   7.473  1.00 50.21           O  
ATOM    672  CB  TYR A 313      16.237  11.681   5.192  1.00 57.06           C  
ATOM    673  CG  TYR A 313      16.170  10.440   4.339  1.00 59.79           C  
ATOM    674  CD1 TYR A 313      16.831   9.277   4.711  1.00 60.81           C  
ATOM    675  CD2 TYR A 313      15.447  10.434   3.156  1.00 61.13           C  
ATOM    676  CE1 TYR A 313      16.769   8.141   3.925  1.00 63.46           C  
ATOM    677  CE2 TYR A 313      15.380   9.306   2.364  1.00 63.93           C  
ATOM    678  CZ  TYR A 313      16.042   8.163   2.751  1.00 64.74           C  
ATOM    679  OH  TYR A 313      15.972   7.041   1.957  1.00 66.72           O  
ATOM    680  N   ILE A 314      17.361  13.119   7.925  1.00 50.06           N  
ATOM    681  CA  ILE A 314      17.691  14.503   8.235  1.00 47.22           C  
ATOM    682  C   ILE A 314      18.668  14.991   7.170  1.00 47.12           C  
ATOM    683  O   ILE A 314      19.712  14.382   6.939  1.00 45.60           O  
ATOM    684  CB  ILE A 314      18.353  14.634   9.622  1.00 46.19           C  
ATOM    685  CG1 ILE A 314      17.446  14.030  10.699  1.00 44.69           C  
ATOM    686  CG2 ILE A 314      18.612  16.100   9.934  1.00 44.78           C  
ATOM    687  CD1 ILE A 314      18.051  14.047  12.093  1.00 42.74           C  
ATOM    688  N   ILE A 315      18.317  16.086   6.506  1.00 47.63           N  
ATOM    689  CA  ILE A 315      19.157  16.622   5.445  1.00 48.20           C  
ATOM    690  C   ILE A 315      19.747  17.978   5.813  1.00 48.50           C  
ATOM    691  O   ILE A 315      19.036  18.894   6.222  1.00 47.75           O  
ATOM    692  CB  ILE A 315      18.369  16.827   4.134  1.00 48.48           C  
ATOM    693  CG1 ILE A 315      17.730  15.511   3.688  1.00 49.23           C  
ATOM    694  CG2 ILE A 315      19.293  17.352   3.050  1.00 48.40           C  
ATOM    695  CD1 ILE A 315      16.375  15.253   4.305  1.00 48.54           C  
ATOM    696  N   THR A 316      21.061  18.100   5.664  1.00 49.15           N  
ATOM    697  CA  THR A 316      21.709  19.407   5.647  1.00 49.79           C  
ATOM    698  C   THR A 316      22.387  19.603   4.297  1.00 50.70           C  
ATOM    699  O   THR A 316      22.445  18.673   3.495  1.00 49.45           O  
ATOM    700  CB  THR A 316      22.795  19.535   6.736  1.00 48.43           C  
ATOM    701  OG1 THR A 316      23.819  18.558   6.511  1.00 46.79           O  
ATOM    702  CG2 THR A 316      22.190  19.346   8.121  1.00 46.89           C  
ATOM    703  N   GLU A 317      22.895  20.807   4.050  1.00 53.24           N  
ATOM    704  CA  GLU A 317      23.652  21.073   2.835  1.00 55.42           C  
ATOM    705  C   GLU A 317      25.076  20.563   2.935  1.00 55.45           C  
ATOM    706  O   GLU A 317      25.649  20.475   4.019  1.00 56.20           O  
ATOM    707  CB  GLU A 317      23.669  22.568   2.532  1.00 58.77           C  
ATOM    708  CG  GLU A 317      22.710  22.913   1.412  1.00 65.89           C  
ATOM    709  CD  GLU A 317      22.415  24.393   1.478  1.00 70.28           C  
ATOM    710  OE1 GLU A 317      22.116  24.888   2.587  1.00 73.17           O  
ATOM    711  OE2 GLU A 317      22.484  25.060   0.422  1.00 73.20           O  
ATOM    712  N   TYR A 318      25.644  20.228   1.782  1.00 56.14           N  
ATOM    713  CA  TYR A 318      26.986  19.671   1.721  1.00 56.02           C  
ATOM    714  C   TYR A 318      28.029  20.773   1.580  1.00 56.02           C  
ATOM    715  O   TYR A 318      27.872  21.727   0.816  1.00 56.13           O  
ATOM    716  CB  TYR A 318      27.095  18.706   0.542  1.00 56.29           C  
ATOM    717  CG  TYR A 318      28.312  17.818   0.590  1.00 56.35           C  
ATOM    718  CD1 TYR A 318      28.260  16.578   1.212  1.00 56.66           C  
ATOM    719  CD2 TYR A 318      29.514  18.218   0.019  1.00 57.09           C  
ATOM    720  CE1 TYR A 318      29.369  15.758   1.268  1.00 57.69           C  
ATOM    721  CE2 TYR A 318      30.633  17.404   0.067  1.00 57.82           C  
ATOM    722  CZ  TYR A 318      30.554  16.175   0.694  1.00 58.81           C  
ATOM    723  OH  TYR A 318      31.662  15.361   0.756  1.00 62.30           O  
ATOM    724  N   MET A 319      29.109  20.628   2.337  1.00 55.95           N  
ATOM    725  CA  MET A 319      30.197  21.592   2.330  1.00 56.84           C  
ATOM    726  C   MET A 319      31.418  21.006   1.635  1.00 56.40           C  
ATOM    727  O   MET A 319      32.068  20.093   2.144  1.00 54.98           O  
ATOM    728  CB  MET A 319      30.552  21.980   3.764  1.00 57.26           C  
ATOM    729  CG  MET A 319      29.344  22.486   4.532  1.00 59.38           C  
ATOM    730  SD  MET A 319      29.148  24.283   4.470  1.00 64.47           S  
ATOM    731  CE  MET A 319      29.146  24.592   2.670  1.00 63.55           C  
ATOM    732  N   GLU A 320      31.727  21.546   0.462  1.00 56.29           N  
ATOM    733  CA  GLU A 320      32.826  21.038  -0.346  1.00 56.84           C  
ATOM    734  C   GLU A 320      34.175  21.136   0.359  1.00 55.92           C  
ATOM    735  O   GLU A 320      35.117  20.447  -0.031  1.00 55.73           O  
ATOM    736  CB  GLU A 320      32.893  21.788  -1.680  1.00 59.73           C  
ATOM    737  CG  GLU A 320      31.823  21.328  -2.659  1.00 64.52           C  
ATOM    738  CD  GLU A 320      32.042  19.863  -3.015  1.00 67.72           C  
ATOM    739  OE1 GLU A 320      33.198  19.391  -2.944  1.00 67.88           O  
ATOM    740  OE2 GLU A 320      31.053  19.183  -3.367  1.00 69.82           O  
ATOM    741  N   ASN A 321      34.274  21.985   1.380  1.00 54.23           N  
ATOM    742  CA  ASN A 321      35.527  22.134   2.113  1.00 51.31           C  
ATOM    743  C   ASN A 321      35.660  21.096   3.220  1.00 50.00           C  
ATOM    744  O   ASN A 321      36.759  20.849   3.716  1.00 49.75           O  
ATOM    745  CB  ASN A 321      35.636  23.539   2.700  1.00 51.53           C  
ATOM    746  CG  ASN A 321      35.956  24.580   1.650  1.00 52.75           C  
ATOM    747  OD1 ASN A 321      36.438  24.253   0.568  1.00 52.05           O  
ATOM    748  ND2 ASN A 321      35.688  25.844   1.964  1.00 54.46           N  
ATOM    749  N   GLY A 322      34.535  20.494   3.599  1.00 47.96           N  
ATOM    750  CA  GLY A 322      34.559  19.391   4.543  1.00 45.33           C  
ATOM    751  C   GLY A 322      34.701  19.825   5.989  1.00 44.16           C  
ATOM    752  O   GLY A 322      34.277  20.917   6.367  1.00 43.80           O  
ATOM    753  N   SER A 323      35.300  18.964   6.806  1.00 43.41           N  
ATOM    754  CA  SER A 323      35.506  19.279   8.214  1.00 41.63           C  
ATOM    755  C   SER A 323      36.778  20.091   8.404  1.00 39.45           C  
ATOM    756  O   SER A 323      37.711  20.044   7.601  1.00 37.90           O  
ATOM    757  CB  SER A 323      35.588  17.997   9.046  1.00 41.60           C  
ATOM    758  OG  SER A 323      36.797  17.302   8.799  1.00 44.88           O  
ATOM    759  N   LEU A 324      36.803  20.844   9.495  1.00 38.49           N  
ATOM    760  CA  LEU A 324      37.921  21.719   9.800  1.00 39.31           C  
ATOM    761  C   LEU A 324      39.235  20.940   9.848  1.00 40.14           C  
ATOM    762  O   LEU A 324      40.238  21.366   9.273  1.00 40.93           O  
ATOM    763  CB  LEU A 324      37.676  22.421  11.141  1.00 36.99           C  
ATOM    764  CG  LEU A 324      38.748  23.468  11.438  1.00 32.52           C  
ATOM    765  CD1 LEU A 324      38.886  24.405  10.256  1.00 32.92           C  
ATOM    766  CD2 LEU A 324      38.374  24.233  12.682  1.00 31.54           C  
ATOM    767  N   VAL A 325      39.220  19.796  10.525  1.00 40.38           N  
ATOM    768  CA  VAL A 325      40.423  18.985  10.683  1.00 41.90           C  
ATOM    769  C   VAL A 325      40.935  18.477   9.338  1.00 43.36           C  
ATOM    770  O   VAL A 325      42.142  18.342   9.124  1.00 44.57           O  
ATOM    771  CB  VAL A 325      40.167  17.762  11.588  1.00 40.89           C  
ATOM    772  CG1 VAL A 325      39.046  16.920  11.013  1.00 39.79           C  
ATOM    773  CG2 VAL A 325      41.436  16.939  11.714  1.00 39.80           C  
ATOM    774  N   ASP A 326      40.012  18.194   8.427  1.00 42.26           N  
ATOM    775  CA  ASP A 326      40.396  17.784   7.087  1.00 42.69           C  
ATOM    776  C   ASP A 326      40.963  18.972   6.336  1.00 42.57           C  
ATOM    777  O   ASP A 326      42.071  18.938   5.798  1.00 42.46           O  
ATOM    778  CB  ASP A 326      39.188  17.238   6.331  1.00 43.63           C  
ATOM    779  CG  ASP A 326      38.874  15.810   6.699  1.00 44.33           C  
ATOM    780  OD1 ASP A 326      39.696  15.193   7.408  1.00 47.31           O  
ATOM    781  OD2 ASP A 326      37.811  15.304   6.280  1.00 44.81           O  
ATOM    782  N   PHE A 327      40.178  20.042   6.312  1.00 41.75           N  
ATOM    783  CA  PHE A 327      40.507  21.218   5.526  1.00 40.35           C  
ATOM    784  C   PHE A 327      41.863  21.791   5.903  1.00 40.78           C  
ATOM    785  O   PHE A 327      42.612  22.259   5.042  1.00 39.63           O  
ATOM    786  CB  PHE A 327      39.440  22.285   5.721  1.00 39.10           C  
ATOM    787  CG  PHE A 327      39.707  23.540   4.958  1.00 39.67           C  
ATOM    788  CD1 PHE A 327      39.591  23.559   3.579  1.00 40.52           C  
ATOM    789  CD2 PHE A 327      40.073  24.703   5.618  1.00 39.47           C  
ATOM    790  CE1 PHE A 327      39.834  24.717   2.868  1.00 41.50           C  
ATOM    791  CE2 PHE A 327      40.318  25.861   4.919  1.00 38.72           C  
ATOM    792  CZ  PHE A 327      40.198  25.871   3.540  1.00 42.49           C  
ATOM    793  N   LEU A 328      42.172  21.758   7.196  1.00 41.34           N  
ATOM    794  CA  LEU A 328      43.422  22.316   7.697  1.00 43.06           C  
ATOM    795  C   LEU A 328      44.630  21.652   7.043  1.00 44.42           C  
ATOM    796  O   LEU A 328      45.641  22.305   6.774  1.00 45.98           O  
ATOM    797  CB  LEU A 328      43.501  22.153   9.219  1.00 42.09           C  
ATOM    798  CG  LEU A 328      42.511  23.017  10.010  1.00 42.10           C  
ATOM    799  CD1 LEU A 328      42.589  22.641  11.479  1.00 42.23           C  
ATOM    800  CD2 LEU A 328      42.817  24.504   9.814  1.00 39.14           C  
ATOM    801  N   LYS A 329      44.512  20.352   6.779  1.00 44.34           N  
ATOM    802  CA  LYS A 329      45.606  19.573   6.212  1.00 43.57           C  
ATOM    803  C   LYS A 329      45.735  19.741   4.697  1.00 44.88           C  
ATOM    804  O   LYS A 329      46.753  19.342   4.125  1.00 45.78           O  
ATOM    805  CB  LYS A 329      45.422  18.090   6.544  1.00 43.52           C  
ATOM    806  CG  LYS A 329      45.396  17.813   8.038  1.00 42.83           C  
ATOM    807  CD  LYS A 329      44.996  16.363   8.240  1.00 43.74           C  
ATOM    808  CE  LYS A 329      44.588  15.993   9.656  1.00 45.95           C  
ATOM    809  NZ  LYS A 329      43.614  14.859   9.659  1.00 49.21           N  
ATOM    810  N   THR A 330      44.720  20.314   4.051  1.00 44.92           N  
ATOM    811  CA  THR A 330      44.802  20.568   2.615  1.00 44.90           C  
ATOM    812  C   THR A 330      45.804  21.681   2.347  1.00 46.20           C  
ATOM    813  O   THR A 330      46.105  22.493   3.222  1.00 44.57           O  
ATOM    814  CB  THR A 330      43.453  21.016   2.007  1.00 43.51           C  
ATOM    815  OG1 THR A 330      43.076  22.290   2.545  1.00 44.12           O  
ATOM    816  CG2 THR A 330      42.375  19.994   2.303  1.00 41.08           C  
ATOM    817  N   PRO A 331      46.343  21.725   1.121  1.00 48.72           N  
ATOM    818  CA  PRO A 331      47.346  22.727   0.751  1.00 50.19           C  
ATOM    819  C   PRO A 331      46.821  24.153   0.887  1.00 51.68           C  
ATOM    820  O   PRO A 331      47.559  25.060   1.275  1.00 52.58           O  
ATOM    821  CB  PRO A 331      47.689  22.371  -0.693  1.00 49.30           C  
ATOM    822  CG  PRO A 331      47.348  20.922  -0.808  1.00 48.58           C  
ATOM    823  CD  PRO A 331      46.132  20.740   0.046  1.00 48.30           C  
ATOM    824  N   SER A 332      45.546  24.350   0.570  1.00 52.23           N  
ATOM    825  CA  SER A 332      44.936  25.662   0.733  1.00 54.55           C  
ATOM    826  C   SER A 332      44.658  25.926   2.211  1.00 54.59           C  
ATOM    827  O   SER A 332      44.707  27.068   2.672  1.00 54.89           O  
ATOM    828  CB  SER A 332      43.638  25.755  -0.077  1.00 54.16           C  
ATOM    829  OG  SER A 332      42.741  24.718   0.274  1.00 57.62           O  
ATOM    830  N   GLY A 333      44.378  24.857   2.953  1.00 54.88           N  
ATOM    831  CA  GLY A 333      44.178  24.983   4.385  1.00 53.74           C  
ATOM    832  C   GLY A 333      45.465  25.370   5.085  1.00 53.20           C  
ATOM    833  O   GLY A 333      45.459  26.159   6.031  1.00 54.03           O  
ATOM    834  N   ILE A 334      46.577  24.822   4.608  1.00 52.54           N  
ATOM    835  CA  ILE A 334      47.881  25.083   5.204  1.00 50.56           C  
ATOM    836  C   ILE A 334      48.358  26.502   4.917  1.00 49.74           C  
ATOM    837  O   ILE A 334      49.247  27.021   5.586  1.00 48.81           O  
ATOM    838  CB  ILE A 334      48.929  24.088   4.682  1.00 49.29           C  
ATOM    839  CG1 ILE A 334      48.503  22.662   5.032  1.00 49.50           C  
ATOM    840  CG2 ILE A 334      50.281  24.383   5.300  1.00 50.59           C  
ATOM    841  CD1 ILE A 334      49.512  21.606   4.646  1.00 47.83           C  
ATOM    842  N   LYS A 335      47.750  27.134   3.920  1.00 50.76           N  
ATOM    843  CA  LYS A 335      48.113  28.497   3.547  1.00 51.35           C  
ATOM    844  C   LYS A 335      47.478  29.541   4.456  1.00 50.29           C  
ATOM    845  O   LYS A 335      47.904  30.696   4.460  1.00 49.38           O  
ATOM    846  CB  LYS A 335      47.709  28.774   2.098  1.00 53.78           C  
ATOM    847  CG  LYS A 335      48.529  27.963   1.120  1.00 56.43           C  
ATOM    848  CD  LYS A 335      48.262  28.340  -0.319  1.00 61.23           C  
ATOM    849  CE  LYS A 335      49.069  27.423  -1.223  1.00 63.56           C  
ATOM    850  NZ  LYS A 335      48.980  27.838  -2.650  1.00 67.20           N  
ATOM    851  N   LEU A 336      46.467  29.132   5.217  1.00 49.59           N  
ATOM    852  CA  LEU A 336      45.779  30.029   6.143  1.00 48.14           C  
ATOM    853  C   LEU A 336      46.740  30.793   7.052  1.00 47.78           C  
ATOM    854  O   LEU A 336      47.731  30.247   7.548  1.00 48.50           O  
ATOM    855  CB  LEU A 336      44.800  29.234   7.002  1.00 47.83           C  
ATOM    856  CG  LEU A 336      43.646  28.706   6.151  1.00 48.20           C  
ATOM    857  CD1 LEU A 336      42.727  27.846   7.011  1.00 46.99           C  
ATOM    858  CD2 LEU A 336      42.888  29.881   5.550  1.00 47.06           C  
ATOM    859  N   THR A 337      46.437  32.069   7.274  1.00 45.76           N  
ATOM    860  CA  THR A 337      47.249  32.896   8.156  1.00 46.43           C  
ATOM    861  C   THR A 337      46.734  32.790   9.579  1.00 46.84           C  
ATOM    862  O   THR A 337      45.546  32.551   9.801  1.00 48.13           O  
ATOM    863  CB  THR A 337      47.173  34.392   7.809  1.00 47.82           C  
ATOM    864  OG1 THR A 337      45.854  34.880   8.087  1.00 48.89           O  
ATOM    865  CG2 THR A 337      47.504  34.619   6.340  1.00 48.60           C  
ATOM    866  N   ILE A 338      47.632  32.979  10.539  1.00 45.99           N  
ATOM    867  CA  ILE A 338      47.264  32.958  11.947  1.00 44.92           C  
ATOM    868  C   ILE A 338      46.035  33.837  12.192  1.00 44.20           C  
ATOM    869  O   ILE A 338      45.195  33.533  13.040  1.00 42.06           O  
ATOM    870  CB  ILE A 338      48.445  33.443  12.825  1.00 45.24           C  
ATOM    871  CG1 ILE A 338      48.057  33.393  14.303  1.00 43.81           C  
ATOM    872  CG2 ILE A 338      48.852  34.855  12.422  1.00 44.91           C  
ATOM    873  CD1 ILE A 338      47.742  32.004  14.796  1.00 44.91           C  
ATOM    874  N   ASN A 339      45.924  34.923  11.433  1.00 44.59           N  
ATOM    875  CA  ASN A 339      44.787  35.825  11.567  1.00 46.34           C  
ATOM    876  C   ASN A 339      43.499  35.130  11.154  1.00 46.32           C  
ATOM    877  O   ASN A 339      42.478  35.247  11.827  1.00 45.22           O  
ATOM    878  CB  ASN A 339      44.984  37.069  10.705  1.00 49.54           C  
ATOM    879  CG  ASN A 339      46.252  37.821  11.048  1.00 54.31           C  
ATOM    880  OD1 ASN A 339      46.211  38.865  11.704  1.00 55.10           O  
ATOM    881  ND2 ASN A 339      47.391  37.293  10.605  1.00 55.73           N  
ATOM    882  N   LYS A 340      43.547  34.402  10.044  1.00 47.07           N  
ATOM    883  CA  LYS A 340      42.368  33.700   9.558  1.00 47.89           C  
ATOM    884  C   LYS A 340      42.025  32.520  10.461  1.00 46.15           C  
ATOM    885  O   LYS A 340      40.855  32.185  10.657  1.00 45.41           O  
ATOM    886  CB  LYS A 340      42.591  33.201   8.129  1.00 50.88           C  
ATOM    887  CG  LYS A 340      41.316  32.628   7.533  1.00 54.14           C  
ATOM    888  CD  LYS A 340      40.217  33.681   7.606  1.00 55.86           C  
ATOM    889  CE  LYS A 340      38.812  33.167   7.906  1.00 58.40           C  
ATOM    890  NZ  LYS A 340      38.266  32.309   6.817  1.00 58.32           N  
ATOM    891  N   LEU A 341      43.057  31.892  11.013  1.00 44.06           N  
ATOM    892  CA  LEU A 341      42.868  30.792  11.949  1.00 42.69           C  
ATOM    893  C   LEU A 341      42.144  31.274  13.198  1.00 42.25           C  
ATOM    894  O   LEU A 341      41.229  30.627  13.710  1.00 41.30           O  
ATOM    895  CB  LEU A 341      44.221  30.191  12.341  1.00 41.90           C  
ATOM    896  CG  LEU A 341      44.895  29.481  11.162  1.00 42.45           C  
ATOM    897  CD1 LEU A 341      46.182  28.811  11.632  1.00 41.27           C  
ATOM    898  CD2 LEU A 341      43.935  28.452  10.570  1.00 39.68           C  
ATOM    899  N   LEU A 342      42.563  32.435  13.688  1.00 41.35           N  
ATOM    900  CA  LEU A 342      41.996  32.985  14.906  1.00 39.88           C  
ATOM    901  C   LEU A 342      40.559  33.427  14.698  1.00 39.39           C  
ATOM    902  O   LEU A 342      39.740  33.387  15.610  1.00 40.60           O  
ATOM    903  CB  LEU A 342      42.840  34.162  15.393  1.00 39.27           C  
ATOM    904  CG  LEU A 342      43.501  33.675  16.687  1.00 40.88           C  
ATOM    905  CD1 LEU A 342      44.289  32.407  16.427  1.00 41.47           C  
ATOM    906  CD2 LEU A 342      44.408  34.748  17.226  1.00 42.05           C  
ATOM    907  N   ASP A 343      40.241  33.844  13.483  1.00 40.01           N  
ATOM    908  CA  ASP A 343      38.894  34.295  13.201  1.00 42.07           C  
ATOM    909  C   ASP A 343      37.940  33.106  13.209  1.00 41.09           C  
ATOM    910  O   ASP A 343      36.825  33.181  13.725  1.00 41.32           O  
ATOM    911  CB  ASP A 343      38.846  35.001  11.846  1.00 47.15           C  
ATOM    912  CG  ASP A 343      37.464  35.525  11.515  1.00 52.15           C  
ATOM    913  OD1 ASP A 343      36.840  36.160  12.397  1.00 53.08           O  
ATOM    914  OD2 ASP A 343      36.999  35.296  10.375  1.00 56.30           O  
ATOM    915  N   MET A 344      38.389  31.996  12.637  1.00 38.72           N  
ATOM    916  CA  MET A 344      37.592  30.780  12.627  1.00 37.83           C  
ATOM    917  C   MET A 344      37.356  30.294  14.047  1.00 36.92           C  
ATOM    918  O   MET A 344      36.258  29.867  14.396  1.00 38.24           O  
ATOM    919  CB  MET A 344      38.299  29.691  11.824  1.00 39.39           C  
ATOM    920  CG  MET A 344      38.502  30.087  10.376  1.00 42.36           C  
ATOM    921  SD  MET A 344      39.545  28.913   9.507  1.00 45.24           S  
ATOM    922  CE  MET A 344      38.341  27.768   8.881  1.00 47.50           C  
ATOM    923  N   ALA A 345      38.399  30.359  14.866  1.00 36.08           N  
ATOM    924  CA  ALA A 345      38.288  30.011  16.275  1.00 34.94           C  
ATOM    925  C   ALA A 345      37.223  30.885  16.925  1.00 36.68           C  
ATOM    926  O   ALA A 345      36.405  30.421  17.720  1.00 37.00           O  
ATOM    927  CB  ALA A 345      39.623  30.222  16.967  1.00 32.96           C  
ATOM    928  N   ALA A 346      37.235  32.165  16.569  1.00 37.15           N  
ATOM    929  CA  ALA A 346      36.288  33.122  17.125  1.00 37.04           C  
ATOM    930  C   ALA A 346      34.860  32.737  16.757  1.00 37.30           C  
ATOM    931  O   ALA A 346      33.938  32.871  17.561  1.00 38.51           O  
ATOM    932  CB  ALA A 346      36.602  34.520  16.610  1.00 36.23           C  
ATOM    933  N   GLN A 347      34.679  32.256  15.532  1.00 36.39           N  
ATOM    934  CA  GLN A 347      33.356  31.871  15.064  1.00 36.44           C  
ATOM    935  C   GLN A 347      32.889  30.645  15.832  1.00 36.63           C  
ATOM    936  O   GLN A 347      31.734  30.548  16.250  1.00 36.23           O  
ATOM    937  CB  GLN A 347      33.386  31.565  13.563  1.00 37.17           C  
ATOM    938  CG  GLN A 347      33.769  32.775  12.723  1.00 40.94           C  
ATOM    939  CD  GLN A 347      33.945  32.369  11.270  1.00 42.72           C  
ATOM    940  OE1 GLN A 347      33.828  33.191  10.364  1.00 44.13           O  
ATOM    941  NE2 GLN A 347      34.229  31.093  11.044  1.00 46.29           N  
ATOM    942  N   ILE A 348      33.807  29.702  16.023  1.00 35.52           N  
ATOM    943  CA  ILE A 348      33.493  28.476  16.740  1.00 34.46           C  
ATOM    944  C   ILE A 348      33.090  28.822  18.166  1.00 35.04           C  
ATOM    945  O   ILE A 348      32.111  28.295  18.695  1.00 37.09           O  
ATOM    946  CB  ILE A 348      34.703  27.517  16.757  1.00 34.31           C  
ATOM    947  CG1 ILE A 348      35.080  27.134  15.325  1.00 33.51           C  
ATOM    948  CG2 ILE A 348      34.372  26.266  17.551  1.00 32.50           C  
ATOM    949  CD1 ILE A 348      36.211  26.148  15.244  1.00 30.96           C  
ATOM    950  N   ALA A 349      33.845  29.725  18.781  1.00 33.50           N  
ATOM    951  CA  ALA A 349      33.515  30.211  20.113  1.00 33.82           C  
ATOM    952  C   ALA A 349      32.158  30.909  20.092  1.00 34.68           C  
ATOM    953  O   ALA A 349      31.363  30.808  21.026  1.00 32.50           O  
ATOM    954  CB  ALA A 349      34.590  31.176  20.597  1.00 32.82           C  
ATOM    955  N   GLU A 350      31.891  31.621  19.006  1.00 36.38           N  
ATOM    956  CA  GLU A 350      30.662  32.389  18.907  1.00 39.02           C  
ATOM    957  C   GLU A 350      29.451  31.457  18.951  1.00 39.63           C  
ATOM    958  O   GLU A 350      28.505  31.680  19.714  1.00 38.87           O  
ATOM    959  CB  GLU A 350      30.656  33.199  17.611  1.00 40.22           C  
ATOM    960  CG  GLU A 350      29.445  34.102  17.516  1.00 44.89           C  
ATOM    961  CD  GLU A 350      29.383  34.796  16.173  1.00 49.72           C  
ATOM    962  OE1 GLU A 350      30.454  35.058  15.577  1.00 52.65           O  
ATOM    963  OE2 GLU A 350      28.256  35.079  15.713  1.00 52.55           O  
ATOM    964  N   GLY A 351      29.495  30.404  18.137  1.00 38.95           N  
ATOM    965  CA  GLY A 351      28.399  29.454  18.089  1.00 37.41           C  
ATOM    966  C   GLY A 351      28.271  28.672  19.382  1.00 37.91           C  
ATOM    967  O   GLY A 351      27.167  28.382  19.839  1.00 39.95           O  
ATOM    968  N   MET A 352      29.404  28.333  19.982  1.00 37.07           N  
ATOM    969  CA  MET A 352      29.389  27.682  21.281  1.00 35.98           C  
ATOM    970  C   MET A 352      28.755  28.589  22.328  1.00 36.37           C  
ATOM    971  O   MET A 352      28.100  28.118  23.257  1.00 36.09           O  
ATOM    972  CB  MET A 352      30.809  27.313  21.703  1.00 33.78           C  
ATOM    973  CG  MET A 352      31.299  26.047  21.022  1.00 34.62           C  
ATOM    974  SD  MET A 352      30.155  24.658  21.216  1.00 33.94           S  
ATOM    975  CE  MET A 352      29.794  24.744  22.957  1.00 34.06           C  
ATOM    976  N   ALA A 353      28.947  29.895  22.172  1.00 37.21           N  
ATOM    977  CA  ALA A 353      28.387  30.859  23.114  1.00 36.19           C  
ATOM    978  C   ALA A 353      26.872  30.851  22.980  1.00 37.26           C  
ATOM    979  O   ALA A 353      26.140  31.030  23.956  1.00 36.07           O  
ATOM    980  CB  ALA A 353      28.930  32.250  22.829  1.00 33.76           C  
ATOM    981  N   PHE A 354      26.409  30.633  21.752  1.00 37.38           N  
ATOM    982  CA  PHE A 354      24.985  30.561  21.463  1.00 37.58           C  
ATOM    983  C   PHE A 354      24.395  29.296  22.076  1.00 38.86           C  
ATOM    984  O   PHE A 354      23.325  29.319  22.694  1.00 38.05           O  
ATOM    985  CB  PHE A 354      24.757  30.560  19.949  1.00 37.02           C  
ATOM    986  CG  PHE A 354      23.344  30.237  19.549  1.00 38.60           C  
ATOM    987  CD1 PHE A 354      22.294  31.063  19.927  1.00 37.64           C  
ATOM    988  CD2 PHE A 354      23.064  29.103  18.802  1.00 37.60           C  
ATOM    989  CE1 PHE A 354      20.991  30.763  19.567  1.00 37.71           C  
ATOM    990  CE2 PHE A 354      21.762  28.797  18.439  1.00 39.45           C  
ATOM    991  CZ  PHE A 354      20.723  29.629  18.823  1.00 38.71           C  
ATOM    992  N   ILE A 355      25.108  28.187  21.899  1.00 39.00           N  
ATOM    993  CA  ILE A 355      24.715  26.915  22.493  1.00 40.07           C  
ATOM    994  C   ILE A 355      24.653  27.010  24.012  1.00 40.59           C  
ATOM    995  O   ILE A 355      23.775  26.427  24.644  1.00 40.40           O  
ATOM    996  CB  ILE A 355      25.704  25.797  22.101  1.00 39.97           C  
ATOM    997  CG1 ILE A 355      25.507  25.436  20.628  1.00 38.54           C  
ATOM    998  CG2 ILE A 355      25.528  24.591  23.012  1.00 37.52           C  
ATOM    999  CD1 ILE A 355      26.423  24.345  20.140  1.00 41.00           C  
ATOM   1000  N   GLU A 356      25.591  27.753  24.589  1.00 41.88           N  
ATOM   1001  CA  GLU A 356      25.600  28.019  26.023  1.00 44.65           C  
ATOM   1002  C   GLU A 356      24.361  28.846  26.383  1.00 45.55           C  
ATOM   1003  O   GLU A 356      23.625  28.545  27.325  1.00 44.67           O  
ATOM   1004  CB  GLU A 356      26.881  28.781  26.395  1.00 45.13           C  
ATOM   1005  CG  GLU A 356      27.144  28.862  27.893  1.00 47.28           C  
ATOM   1006  CD  GLU A 356      28.555  29.382  28.157  1.00 50.32           C  
ATOM   1007  OE1 GLU A 356      29.082  29.171  29.274  1.00 53.84           O  
ATOM   1008  OE2 GLU A 356      29.144  30.005  27.248  1.00 49.93           O  
ATOM   1009  N   GLU A 357      24.128  29.892  25.597  1.00 46.20           N  
ATOM   1010  CA  GLU A 357      23.022  30.809  25.831  1.00 47.17           C  
ATOM   1011  C   GLU A 357      21.682  30.093  25.736  1.00 47.11           C  
ATOM   1012  O   GLU A 357      20.747  30.405  26.472  1.00 47.31           O  
ATOM   1013  CB  GLU A 357      23.073  31.950  24.814  1.00 50.13           C  
ATOM   1014  CG  GLU A 357      21.977  32.983  25.012  1.00 54.37           C  
ATOM   1015  CD  GLU A 357      21.945  33.895  23.792  1.00 58.22           C  
ATOM   1016  OE1 GLU A 357      22.255  35.097  23.936  1.00 61.57           O  
ATOM   1017  OE2 GLU A 357      21.609  33.411  22.688  1.00 59.04           O  
ATOM   1018  N   ARG A 358      21.589  29.130  24.825  1.00 47.32           N  
ATOM   1019  CA  ARG A 358      20.368  28.348  24.681  1.00 46.64           C  
ATOM   1020  C   ARG A 358      20.305  27.195  25.673  1.00 45.33           C  
ATOM   1021  O   ARG A 358      19.347  26.422  25.697  1.00 45.61           O  
ATOM   1022  CB  ARG A 358      20.234  27.826  23.245  1.00 48.46           C  
ATOM   1023  CG  ARG A 358      19.605  28.868  22.324  1.00 48.51           C  
ATOM   1024  CD  ARG A 358      18.890  29.807  23.294  1.00 53.94           C  
ATOM   1025  NE  ARG A 358      17.541  30.184  22.875  1.00 54.96           N  
ATOM   1026  CZ  ARG A 358      16.478  29.390  22.960  1.00 56.92           C  
ATOM   1027  NH1 ARG A 358      16.594  28.157  23.444  1.00 56.93           N  
ATOM   1028  NH2 ARG A 358      15.293  29.836  22.571  1.00 58.99           N  
ATOM   1029  N   ASN A 359      21.339  27.091  26.501  1.00 43.82           N  
ATOM   1030  CA  ASN A 359      21.346  26.158  27.623  1.00 43.74           C  
ATOM   1031  C   ASN A 359      21.458  24.699  27.178  1.00 42.47           C  
ATOM   1032  O   ASN A 359      20.775  23.803  27.674  1.00 41.42           O  
ATOM   1033  CB  ASN A 359      20.089  26.351  28.475  1.00 45.17           C  
ATOM   1034  CG  ASN A 359      20.287  25.903  29.912  1.00 47.63           C  
ATOM   1035  OD1 ASN A 359      19.371  25.986  30.733  1.00 49.56           O  
ATOM   1036  ND2 ASN A 359      21.490  25.425  30.224  1.00 46.53           N  
ATOM   1037  N   TYR A 360      22.341  24.471  26.213  1.00 41.42           N  
ATOM   1038  CA  TYR A 360      22.705  23.128  25.793  1.00 38.86           C  
ATOM   1039  C   TYR A 360      24.208  22.977  25.968  1.00 38.07           C  
ATOM   1040  O   TYR A 360      24.893  23.938  26.316  1.00 36.94           O  
ATOM   1041  CB  TYR A 360      22.328  22.911  24.325  1.00 39.89           C  
ATOM   1042  CG  TYR A 360      20.838  22.838  24.080  1.00 41.29           C  
ATOM   1043  CD1 TYR A 360      20.091  23.990  23.870  1.00 40.79           C  
ATOM   1044  CD2 TYR A 360      20.174  21.616  24.083  1.00 42.63           C  
ATOM   1045  CE1 TYR A 360      18.726  23.929  23.673  1.00 41.94           C  
ATOM   1046  CE2 TYR A 360      18.809  21.546  23.888  1.00 43.23           C  
ATOM   1047  CZ  TYR A 360      18.091  22.704  23.685  1.00 43.27           C  
ATOM   1048  OH  TYR A 360      16.732  22.637  23.496  1.00 46.29           O  
ATOM   1049  N   ILE A 361      24.717  21.772  25.744  1.00 36.77           N  
ATOM   1050  CA  ILE A 361      26.154  21.574  25.632  1.00 38.43           C  
ATOM   1051  C   ILE A 361      26.430  20.801  24.354  1.00 39.47           C  
ATOM   1052  O   ILE A 361      25.489  20.419  23.659  1.00 40.26           O  
ATOM   1053  CB  ILE A 361      26.735  20.774  26.823  1.00 37.94           C  
ATOM   1054  CG1 ILE A 361      26.196  19.346  26.811  1.00 36.57           C  
ATOM   1055  CG2 ILE A 361      26.395  21.463  28.133  1.00 35.38           C  
ATOM   1056  CD1 ILE A 361      26.826  18.464  27.860  1.00 37.14           C  
ATOM   1057  N   HIS A 362      27.705  20.577  24.046  1.00 40.45           N  
ATOM   1058  CA  HIS A 362      28.074  19.857  22.834  1.00 40.23           C  
ATOM   1059  C   HIS A 362      28.492  18.421  23.124  1.00 40.89           C  
ATOM   1060  O   HIS A 362      27.933  17.480  22.554  1.00 40.02           O  
ATOM   1061  CB  HIS A 362      29.209  20.577  22.107  1.00 39.00           C  
ATOM   1062  CG  HIS A 362      29.416  20.092  20.709  1.00 38.62           C  
ATOM   1063  ND1 HIS A 362      30.050  18.903  20.422  1.00 39.11           N  
ATOM   1064  CD2 HIS A 362      29.020  20.604  19.520  1.00 39.41           C  
ATOM   1065  CE1 HIS A 362      30.034  18.702  19.116  1.00 37.93           C  
ATOM   1066  NE2 HIS A 362      29.414  19.719  18.546  1.00 38.64           N  
ATOM   1067  N   ARG A 363      29.481  18.270  24.002  1.00 41.97           N  
ATOM   1068  CA  ARG A 363      29.981  16.963  24.431  1.00 44.85           C  
ATOM   1069  C   ARG A 363      31.101  16.411  23.559  1.00 43.37           C  
ATOM   1070  O   ARG A 363      31.889  15.597  24.036  1.00 44.92           O  
ATOM   1071  CB  ARG A 363      28.849  15.930  24.500  1.00 48.05           C  
ATOM   1072  CG  ARG A 363      28.297  15.754  25.901  1.00 53.46           C  
ATOM   1073  CD  ARG A 363      27.267  14.635  26.004  1.00 59.42           C  
ATOM   1074  NE  ARG A 363      26.553  14.668  27.281  1.00 64.84           N  
ATOM   1075  CZ  ARG A 363      26.863  13.920  28.338  1.00 66.18           C  
ATOM   1076  NH1 ARG A 363      27.881  13.069  28.275  1.00 65.65           N  
ATOM   1077  NH2 ARG A 363      26.160  14.030  29.461  1.00 66.19           N  
ATOM   1078  N   ASP A 364      31.175  16.831  22.301  1.00 41.14           N  
ATOM   1079  CA  ASP A 364      32.237  16.353  21.423  1.00 41.66           C  
ATOM   1080  C   ASP A 364      32.809  17.483  20.564  1.00 40.69           C  
ATOM   1081  O   ASP A 364      32.973  17.364  19.349  1.00 40.38           O  
ATOM   1082  CB  ASP A 364      31.712  15.220  20.532  1.00 42.79           C  
ATOM   1083  CG  ASP A 364      32.828  14.346  19.975  1.00 44.14           C  
ATOM   1084  OD1 ASP A 364      32.524  13.264  19.430  1.00 44.29           O  
ATOM   1085  OD2 ASP A 364      34.009  14.741  20.082  1.00 46.36           O  
ATOM   1086  N   LEU A 365      33.122  18.597  21.212  1.00 39.69           N  
ATOM   1087  CA  LEU A 365      33.595  19.770  20.496  1.00 39.90           C  
ATOM   1088  C   LEU A 365      35.058  19.603  20.090  1.00 39.95           C  
ATOM   1089  O   LEU A 365      35.963  19.667  20.922  1.00 40.16           O  
ATOM   1090  CB  LEU A 365      33.429  21.015  21.370  1.00 41.34           C  
ATOM   1091  CG  LEU A 365      33.949  22.309  20.734  1.00 41.79           C  
ATOM   1092  CD1 LEU A 365      33.082  22.679  19.541  1.00 39.35           C  
ATOM   1093  CD2 LEU A 365      33.944  23.426  21.771  1.00 41.84           C  
ATOM   1094  N   ARG A 366      35.281  19.387  18.797  1.00 38.66           N  
ATOM   1095  CA  ARG A 366      36.626  19.221  18.255  1.00 37.84           C  
ATOM   1096  C   ARG A 366      36.599  19.427  16.745  1.00 37.30           C  
ATOM   1097  O   ARG A 366      35.530  19.397  16.136  1.00 37.41           O  
ATOM   1098  CB  ARG A 366      37.163  17.823  18.584  1.00 38.90           C  
ATOM   1099  CG  ARG A 366      36.286  16.710  18.037  1.00 41.13           C  
ATOM   1100  CD  ARG A 366      36.624  15.382  18.685  1.00 42.25           C  
ATOM   1101  NE  ARG A 366      37.126  14.405  17.721  1.00 45.24           N  
ATOM   1102  CZ  ARG A 366      36.527  13.250  17.443  1.00 45.38           C  
ATOM   1103  NH1 ARG A 366      35.399  12.919  18.054  1.00 46.72           N  
ATOM   1104  NH2 ARG A 366      37.057  12.423  16.553  1.00 44.33           N  
ATOM   1105  N   ALA A 367      37.769  19.628  16.145  1.00 35.52           N  
ATOM   1106  CA  ALA A 367      37.851  20.014  14.738  1.00 33.43           C  
ATOM   1107  C   ALA A 367      37.089  19.077  13.803  1.00 33.62           C  
ATOM   1108  O   ALA A 367      36.769  19.440  12.673  1.00 32.44           O  
ATOM   1109  CB  ALA A 367      39.300  20.091  14.313  1.00 33.26           C  
ATOM   1110  N   ALA A 368      36.799  17.869  14.272  1.00 33.99           N  
ATOM   1111  CA  ALA A 368      36.169  16.870  13.418  1.00 35.40           C  
ATOM   1112  C   ALA A 368      34.668  17.114  13.285  1.00 36.32           C  
ATOM   1113  O   ALA A 368      34.019  16.640  12.351  1.00 35.74           O  
ATOM   1114  CB  ALA A 368      36.427  15.475  13.970  1.00 33.24           C  
ATOM   1115  N   ASN A 369      34.115  17.857  14.234  1.00 36.61           N  
ATOM   1116  CA  ASN A 369      32.698  18.185  14.198  1.00 38.60           C  
ATOM   1117  C   ASN A 369      32.464  19.625  13.763  1.00 39.09           C  
ATOM   1118  O   ASN A 369      31.383  20.178  13.962  1.00 40.14           O  
ATOM   1119  CB  ASN A 369      32.061  17.946  15.569  1.00 38.97           C  
ATOM   1120  CG  ASN A 369      31.471  16.558  15.701  1.00 38.71           C  
ATOM   1121  OD1 ASN A 369      30.765  16.088  14.812  1.00 40.77           O  
ATOM   1122  ND2 ASN A 369      31.757  15.896  16.813  1.00 40.23           N  
ATOM   1123  N   ILE A 370      33.487  20.232  13.171  1.00 38.62           N  
ATOM   1124  CA  ILE A 370      33.346  21.564  12.598  1.00 38.28           C  
ATOM   1125  C   ILE A 370      33.367  21.492  11.075  1.00 39.06           C  
ATOM   1126  O   ILE A 370      34.283  20.919  10.489  1.00 38.99           O  
ATOM   1127  CB  ILE A 370      34.489  22.493  13.043  1.00 37.70           C  
ATOM   1128  CG1 ILE A 370      34.540  22.555  14.572  1.00 37.21           C  
ATOM   1129  CG2 ILE A 370      34.302  23.876  12.435  1.00 34.53           C  
ATOM   1130  CD1 ILE A 370      33.205  22.843  15.224  1.00 37.05           C  
ATOM   1131  N   LEU A 371      32.354  22.069  10.436  1.00 39.80           N  
ATOM   1132  CA  LEU A 371      32.334  22.156   8.980  1.00 40.60           C  
ATOM   1133  C   LEU A 371      32.813  23.518   8.484  1.00 40.38           C  
ATOM   1134  O   LEU A 371      32.546  24.559   9.089  1.00 39.73           O  
ATOM   1135  CB  LEU A 371      30.925  21.876   8.453  1.00 41.56           C  
ATOM   1136  CG  LEU A 371      30.644  20.374   8.574  1.00 42.84           C  
ATOM   1137  CD1 LEU A 371      29.194  20.081   8.202  1.00 41.34           C  
ATOM   1138  CD2 LEU A 371      31.601  19.609   7.669  1.00 41.98           C  
ATOM   1139  N   VAL A 372      33.541  23.494   7.372  1.00 40.17           N  
ATOM   1140  CA  VAL A 372      34.047  24.706   6.742  1.00 40.45           C  
ATOM   1141  C   VAL A 372      33.180  25.079   5.536  1.00 41.90           C  
ATOM   1142  O   VAL A 372      32.958  24.280   4.625  1.00 40.48           O  
ATOM   1143  CB  VAL A 372      35.516  24.509   6.299  1.00 39.13           C  
ATOM   1144  CG1 VAL A 372      36.034  25.766   5.613  1.00 36.64           C  
ATOM   1145  CG2 VAL A 372      36.374  24.160   7.511  1.00 37.93           C  
ATOM   1146  N   SER A 373      32.684  26.311   5.538  1.00 44.58           N  
ATOM   1147  CA  SER A 373      31.776  26.769   4.493  1.00 46.86           C  
ATOM   1148  C   SER A 373      32.552  27.256   3.279  1.00 49.52           C  
ATOM   1149  O   SER A 373      33.781  27.339   3.291  1.00 49.11           O  
ATOM   1150  CB  SER A 373      30.895  27.906   5.010  1.00 45.21           C  
ATOM   1151  OG  SER A 373      31.611  29.126   5.012  1.00 43.09           O  
ATOM   1152  N   ASP A 374      31.810  27.589   2.227  1.00 53.29           N  
ATOM   1153  CA  ASP A 374      32.399  28.005   0.961  1.00 55.75           C  
ATOM   1154  C   ASP A 374      33.175  29.303   1.115  1.00 55.12           C  
ATOM   1155  O   ASP A 374      34.111  29.560   0.362  1.00 57.13           O  
ATOM   1156  CB  ASP A 374      31.306  28.180  -0.098  1.00 60.65           C  
ATOM   1157  CG  ASP A 374      30.542  26.889  -0.372  1.00 67.44           C  
ATOM   1158  OD1 ASP A 374      30.926  25.831   0.184  1.00 70.12           O  
ATOM   1159  OD2 ASP A 374      29.557  26.933  -1.144  1.00 69.09           O  
ATOM   1160  N   THR A 375      32.791  30.118   2.093  1.00 53.73           N  
ATOM   1161  CA  THR A 375      33.494  31.373   2.352  1.00 51.22           C  
ATOM   1162  C   THR A 375      34.563  31.208   3.427  1.00 50.93           C  
ATOM   1163  O   THR A 375      35.135  32.188   3.907  1.00 51.20           O  
ATOM   1164  CB  THR A 375      32.528  32.475   2.810  1.00 49.17           C  
ATOM   1165  OG1 THR A 375      31.923  32.098   4.050  1.00 50.17           O  
ATOM   1166  CG2 THR A 375      31.445  32.690   1.770  1.00 48.69           C  
ATOM   1167  N   LEU A 376      34.820  29.958   3.804  1.00 50.26           N  
ATOM   1168  CA  LEU A 376      35.849  29.637   4.788  1.00 49.41           C  
ATOM   1169  C   LEU A 376      35.468  30.060   6.200  1.00 48.50           C  
ATOM   1170  O   LEU A 376      36.337  30.313   7.035  1.00 48.32           O  
ATOM   1171  CB  LEU A 376      37.183  30.282   4.399  1.00 48.64           C  
ATOM   1172  CG  LEU A 376      38.062  29.188   3.795  1.00 46.54           C  
ATOM   1173  CD1 LEU A 376      37.297  28.488   2.685  1.00 46.68           C  
ATOM   1174  CD2 LEU A 376      39.352  29.788   3.273  1.00 46.34           C  
ATOM   1175  N   SER A 377      34.167  30.138   6.460  1.00 47.87           N  
ATOM   1176  CA  SER A 377      33.673  30.308   7.820  1.00 47.51           C  
ATOM   1177  C   SER A 377      33.377  28.933   8.417  1.00 45.87           C  
ATOM   1178  O   SER A 377      33.324  27.941   7.690  1.00 44.86           O  
ATOM   1179  CB  SER A 377      32.410  31.178   7.826  1.00 49.45           C  
ATOM   1180  OG  SER A 377      31.367  30.585   7.072  1.00 54.33           O  
ATOM   1181  N   CYS A 378      33.197  28.876   9.734  1.00 45.54           N  
ATOM   1182  CA  CYS A 378      33.051  27.600  10.431  1.00 44.46           C  
ATOM   1183  C   CYS A 378      31.641  27.368  10.961  1.00 43.68           C  
ATOM   1184  O   CYS A 378      31.054  28.243  11.596  1.00 42.18           O  
ATOM   1185  CB  CYS A 378      34.054  27.517  11.585  1.00 44.47           C  
ATOM   1186  SG  CYS A 378      35.784  27.350  11.057  1.00 46.09           S  
ATOM   1187  N   LYS A 379      31.106  26.178  10.689  1.00 43.79           N  
ATOM   1188  CA  LYS A 379      29.789  25.776  11.185  1.00 43.53           C  
ATOM   1189  C   LYS A 379      29.959  24.644  12.187  1.00 42.25           C  
ATOM   1190  O   LYS A 379      30.587  23.632  11.883  1.00 43.39           O  
ATOM   1191  CB  LYS A 379      28.900  25.284  10.039  1.00 44.85           C  
ATOM   1192  CG  LYS A 379      28.851  26.237   8.855  1.00 49.31           C  
ATOM   1193  CD  LYS A 379      28.021  27.491   9.041  1.00 52.63           C  
ATOM   1194  CE  LYS A 379      27.490  27.946   7.689  1.00 56.64           C  
ATOM   1195  NZ  LYS A 379      26.730  26.862   6.993  1.00 60.17           N  
ATOM   1196  N   ILE A 380      29.394  24.814  13.375  1.00 40.20           N  
ATOM   1197  CA  ILE A 380      29.454  23.785  14.401  1.00 38.98           C  
ATOM   1198  C   ILE A 380      28.491  22.658  14.071  1.00 38.91           C  
ATOM   1199  O   ILE A 380      27.303  22.886  13.856  1.00 40.40           O  
ATOM   1200  CB  ILE A 380      29.060  24.341  15.781  1.00 38.94           C  
ATOM   1201  CG1 ILE A 380      30.089  25.374  16.236  1.00 36.30           C  
ATOM   1202  CG2 ILE A 380      28.936  23.208  16.779  1.00 37.07           C  
ATOM   1203  CD1 ILE A 380      29.720  26.072  17.513  1.00 36.84           C  
ATOM   1204  N   ALA A 381      29.007  21.437  14.027  1.00 37.96           N  
ATOM   1205  CA  ALA A 381      28.170  20.279  13.765  1.00 37.84           C  
ATOM   1206  C   ALA A 381      28.316  19.272  14.889  1.00 38.41           C  
ATOM   1207  O   ALA A 381      29.257  19.330  15.671  1.00 38.95           O  
ATOM   1208  CB  ALA A 381      28.559  19.644  12.449  1.00 36.52           C  
ATOM   1209  N   ASP A 382      27.365  18.353  14.974  1.00 39.89           N  
ATOM   1210  CA  ASP A 382      27.530  17.162  15.792  1.00 41.34           C  
ATOM   1211  C   ASP A 382      27.167  15.941  14.952  1.00 41.98           C  
ATOM   1212  O   ASP A 382      25.991  15.651  14.720  1.00 42.73           O  
ATOM   1213  CB  ASP A 382      26.638  17.233  17.032  1.00 40.55           C  
ATOM   1214  CG  ASP A 382      26.806  16.027  17.932  1.00 42.95           C  
ATOM   1215  OD1 ASP A 382      27.782  15.270  17.739  1.00 40.50           O  
ATOM   1216  OD2 ASP A 382      25.962  15.833  18.832  1.00 47.23           O  
ATOM   1217  N   PHE A 383      28.193  15.231  14.492  1.00 41.25           N  
ATOM   1218  CA  PHE A 383      28.006  14.116  13.576  1.00 41.08           C  
ATOM   1219  C   PHE A 383      27.700  12.820  14.310  1.00 41.56           C  
ATOM   1220  O   PHE A 383      27.492  11.786  13.681  1.00 42.17           O  
ATOM   1221  CB  PHE A 383      29.254  13.923  12.719  1.00 40.15           C  
ATOM   1222  CG  PHE A 383      29.598  15.110  11.876  1.00 42.92           C  
ATOM   1223  CD1 PHE A 383      30.916  15.504  11.715  1.00 43.98           C  
ATOM   1224  CD2 PHE A 383      28.606  15.832  11.235  1.00 44.32           C  
ATOM   1225  CE1 PHE A 383      31.239  16.597  10.925  1.00 45.46           C  
ATOM   1226  CE2 PHE A 383      28.922  16.925  10.444  1.00 44.90           C  
ATOM   1227  CZ  PHE A 383      30.242  17.309  10.289  1.00 44.06           C  
ATOM   1228  N   GLY A 384      27.675  12.873  15.636  1.00 42.64           N  
ATOM   1229  CA  GLY A 384      27.534  11.654  16.409  1.00 43.93           C  
ATOM   1230  C   GLY A 384      28.688  10.711  16.130  1.00 44.48           C  
ATOM   1231  O   GLY A 384      28.485   9.532  15.851  1.00 45.67           O  
ATOM   1232  N   LEU A 385      29.905  11.234  16.200  1.00 44.79           N  
ATOM   1233  CA  LEU A 385      31.083  10.476  15.811  1.00 47.71           C  
ATOM   1234  C   LEU A 385      31.255   9.195  16.627  1.00 51.79           C  
ATOM   1235  O   LEU A 385      31.711   8.178  16.108  1.00 53.00           O  
ATOM   1236  CB  LEU A 385      32.332  11.351  15.953  1.00 45.13           C  
ATOM   1237  CG  LEU A 385      32.838  12.113  14.724  1.00 43.29           C  
ATOM   1238  CD1 LEU A 385      31.740  12.210  13.695  1.00 42.87           C  
ATOM   1239  CD2 LEU A 385      33.326  13.495  15.132  1.00 40.32           C  
ATOM   1240  N   ALA A 386      30.887   9.243  17.903  1.00 55.00           N  
ATOM   1241  CA  ALA A 386      31.172   8.140  18.813  1.00 58.49           C  
ATOM   1242  C   ALA A 386      30.303   6.920  18.523  1.00 62.69           C  
ATOM   1243  O   ALA A 386      30.800   5.801  18.384  1.00 63.08           O  
ATOM   1244  CB  ALA A 386      30.972   8.592  20.251  1.00 56.46           C  
ATOM   1245  N   ARG A 387      28.996   7.145  18.431  1.00 67.86           N  
ATOM   1246  CA  ARG A 387      28.041   6.065  18.212  1.00 71.47           C  
ATOM   1247  C   ARG A 387      28.113   5.593  16.768  1.00 73.32           C  
ATOM   1248  O   ARG A 387      27.320   4.773  16.309  1.00 74.24           O  
ATOM   1249  CB  ARG A 387      26.622   6.543  18.531  1.00 72.66           C  
ATOM   1250  CG  ARG A 387      26.149   7.648  17.596  1.00 76.42           C  
ATOM   1251  CD  ARG A 387      24.831   8.249  18.066  1.00 80.01           C  
ATOM   1252  NE  ARG A 387      23.945   7.234  18.633  1.00 84.22           N  
ATOM   1253  CZ  ARG A 387      22.659   7.429  18.916  1.00 85.33           C  
ATOM   1254  NH1 ARG A 387      22.096   8.609  18.685  1.00 85.53           N  
ATOM   1255  NH2 ARG A 387      21.936   6.442  19.432  1.00 84.78           N  
ATOM   1256  N   LEU A 388      29.089   6.128  16.046  1.00 76.00           N  
ATOM   1257  CA  LEU A 388      29.249   5.830  14.633  1.00 79.57           C  
ATOM   1258  C   LEU A 388      30.263   4.703  14.438  1.00 82.25           C  
ATOM   1259  O   LEU A 388      30.317   4.070  13.384  1.00 83.09           O  
ATOM   1260  CB  LEU A 388      29.706   7.088  13.892  1.00 79.02           C  
ATOM   1261  CG  LEU A 388      29.591   7.106  12.370  1.00 78.20           C  
ATOM   1262  CD1 LEU A 388      28.145   6.890  11.950  1.00 77.88           C  
ATOM   1263  CD2 LEU A 388      30.104   8.439  11.856  1.00 78.62           C  
ATOM   1264  N   ILE A 389      31.069   4.458  15.468  1.00 85.47           N  
ATOM   1265  CA  ILE A 389      32.018   3.346  15.460  1.00 88.32           C  
ATOM   1266  C   ILE A 389      31.382   2.059  15.983  1.00 90.21           C  
ATOM   1267  O   ILE A 389      30.742   2.041  17.037  1.00 89.97           O  
ATOM   1268  CB  ILE A 389      33.260   3.642  16.340  1.00 88.62           C  
ATOM   1269  CG1 ILE A 389      34.166   4.671  15.655  1.00 88.15           C  
ATOM   1270  CG2 ILE A 389      34.028   2.355  16.602  1.00 87.95           C  
ATOM   1271  CD1 ILE A 389      33.560   6.049  15.518  1.00 87.08           C  
ATOM   1272  N   GLU A 390      31.570   0.975  15.236  1.00 92.23           N  
ATOM   1273  CA  GLU A 390      31.014  -0.320  15.614  1.00 94.25           C  
ATOM   1274  C   GLU A 390      31.884  -1.045  16.636  1.00 93.84           C  
ATOM   1275  O   GLU A 390      33.101  -1.163  16.472  1.00 93.58           O  
ATOM   1276  CB  GLU A 390      30.833  -1.200  14.371  1.00 96.26           C  
ATOM   1277  CG  GLU A 390      29.461  -1.033  13.729  1.00 98.64           C  
ATOM   1278  CD  GLU A 390      28.421  -1.714  14.607  1.00101.02           C  
ATOM   1279  OE1 GLU A 390      27.652  -2.549  14.082  1.00101.18           O  
ATOM   1280  OE2 GLU A 390      28.372  -1.415  15.821  1.00101.97           O  
ATOM   1281  N   ASP A 391      31.242  -1.537  17.693  1.00 92.99           N  
ATOM   1282  CA  ASP A 391      31.934  -2.242  18.771  1.00 92.29           C  
ATOM   1283  C   ASP A 391      32.500  -3.571  18.257  1.00 89.72           C  
ATOM   1284  O   ASP A 391      31.864  -4.249  17.449  1.00 89.48           O  
ATOM   1285  CB  ASP A 391      30.956  -2.495  19.926  1.00 94.77           C  
ATOM   1286  CG  ASP A 391      31.648  -2.585  21.279  1.00 96.54           C  
ATOM   1287  OD1 ASP A 391      32.561  -3.425  21.437  1.00 95.89           O  
ATOM   1288  OD2 ASP A 391      31.272  -1.810  22.186  1.00 97.72           O  
ATOM   1289  N   ASN A 392      33.693  -3.937  18.721  1.00 86.21           N  
ATOM   1290  CA  ASN A 392      34.349  -5.157  18.258  1.00 82.87           C  
ATOM   1291  C   ASN A 392      34.479  -6.201  19.365  1.00 81.21           C  
ATOM   1292  O   ASN A 392      34.110  -5.965  20.516  1.00 80.66           O  
ATOM   1293  CB  ASN A 392      35.735  -4.834  17.690  1.00 82.50           C  
ATOM   1294  CG  ASN A 392      36.736  -4.456  18.765  1.00 82.83           C  
ATOM   1295  OD1 ASN A 392      36.363  -4.015  19.851  1.00 83.90           O  
ATOM   1296  ND2 ASN A 392      38.019  -4.631  18.467  1.00 82.06           N  
ATOM   1297  N   GLU A 393      35.013  -7.364  19.005  1.00 79.57           N  
ATOM   1298  CA  GLU A 393      35.108  -8.490  19.929  1.00 79.21           C  
ATOM   1299  C   GLU A 393      35.978  -8.143  21.130  1.00 78.81           C  
ATOM   1300  O   GLU A 393      35.871  -8.760  22.188  1.00 78.51           O  
ATOM   1301  CB  GLU A 393      35.706  -9.713  19.226  1.00 79.11           C  
ATOM   1302  CG  GLU A 393      35.377  -9.782  17.744  1.00 80.60           C  
ATOM   1303  CD  GLU A 393      36.475  -9.080  16.961  1.00 81.54           C  
ATOM   1304  OE1 GLU A 393      37.422  -9.764  16.516  1.00 82.90           O  
ATOM   1305  OE2 GLU A 393      36.392  -7.846  16.787  1.00 81.96           O  
ATOM   1306  N   TYR A 394      36.844  -7.151  20.956  1.00 78.82           N  
ATOM   1307  CA  TYR A 394      37.894  -6.876  21.926  1.00 78.95           C  
ATOM   1308  C   TYR A 394      37.525  -5.802  22.942  1.00 80.90           C  
ATOM   1309  O   TYR A 394      38.198  -5.640  23.959  1.00 80.51           O  
ATOM   1310  CB  TYR A 394      39.177  -6.488  21.192  1.00 75.57           C  
ATOM   1311  CG  TYR A 394      39.774  -7.643  20.427  1.00 73.30           C  
ATOM   1312  CD1 TYR A 394      39.592  -7.767  19.055  1.00 72.03           C  
ATOM   1313  CD2 TYR A 394      40.482  -8.639  21.087  1.00 72.93           C  
ATOM   1314  CE1 TYR A 394      40.097  -8.857  18.364  1.00 71.16           C  
ATOM   1315  CE2 TYR A 394      40.990  -9.728  20.407  1.00 72.44           C  
ATOM   1316  CZ  TYR A 394      40.794  -9.834  19.049  1.00 72.27           C  
ATOM   1317  OH  TYR A 394      41.291 -10.931  18.386  1.00 71.73           O  
ATOM   1318  N   THR A 395      36.449  -5.075  22.664  1.00 83.69           N  
ATOM   1319  CA  THR A 395      35.994  -4.016  23.553  1.00 86.85           C  
ATOM   1320  C   THR A 395      34.615  -4.329  24.118  1.00 87.90           C  
ATOM   1321  O   THR A 395      33.745  -4.846  23.420  1.00 87.30           O  
ATOM   1322  CB  THR A 395      35.910  -2.667  22.816  1.00 88.77           C  
ATOM   1323  OG1 THR A 395      34.974  -2.772  21.735  1.00 90.64           O  
ATOM   1324  CG2 THR A 395      37.275  -2.275  22.264  1.00 88.50           C  
ATOM   1325  N   ALA A 396      34.421  -4.004  25.392  1.00 90.89           N  
ATOM   1326  CA  ALA A 396      33.149  -4.253  26.059  1.00 94.17           C  
ATOM   1327  C   ALA A 396      32.819  -3.175  27.090  1.00 96.16           C  
ATOM   1328  O   ALA A 396      32.170  -3.455  28.101  1.00 95.95           O  
ATOM   1329  CB  ALA A 396      33.174  -5.619  26.727  1.00 95.20           C  
ATOM   1330  N   ARG A 397      33.265  -1.948  26.835  1.00 98.68           N  
ATOM   1331  CA  ARG A 397      33.015  -0.840  27.751  1.00100.11           C  
ATOM   1332  C   ARG A 397      31.528  -0.501  27.807  1.00100.73           C  
ATOM   1333  O   ARG A 397      30.858  -0.335  26.785  1.00100.32           O  
ATOM   1334  CB  ARG A 397      33.809   0.402  27.321  1.00101.10           C  
ATOM   1335  CG  ARG A 397      33.290   1.030  26.029  1.00102.72           C  
ATOM   1336  CD  ARG A 397      33.878   2.396  25.685  1.00103.33           C  
ATOM   1337  NE  ARG A 397      33.844   3.309  26.825  1.00104.49           N  
ATOM   1338  CZ  ARG A 397      34.926   3.758  27.456  1.00105.28           C  
ATOM   1339  NH1 ARG A 397      34.802   4.584  28.488  1.00104.59           N  
ATOM   1340  NH2 ARG A 397      36.135   3.387  27.051  1.00104.80           N  
ATOM   1341  N   GLU A 398      31.007  -0.406  29.025  1.00101.42           N  
ATOM   1342  CA  GLU A 398      29.641   0.050  29.226  1.00102.25           C  
ATOM   1343  C   GLU A 398      29.668   1.405  29.929  1.00102.16           C  
ATOM   1344  O   GLU A 398      28.649   1.894  30.420  1.00102.91           O  
ATOM   1345  CB  GLU A 398      28.853  -0.967  30.060  1.00103.44           C  
ATOM   1346  CG  GLU A 398      27.348  -0.726  29.997  1.00105.07           C  
ATOM   1347  CD  GLU A 398      26.533  -1.841  30.633  1.00105.89           C  
ATOM   1348  OE1 GLU A 398      26.373  -1.831  31.873  1.00106.35           O  
ATOM   1349  OE2 GLU A 398      26.050  -2.725  29.891  1.00105.37           O  
ATOM   1350  N   GLY A 399      30.855   2.006  29.974  1.00100.75           N  
ATOM   1351  CA  GLY A 399      30.989   3.353  30.503  1.00 98.40           C  
ATOM   1352  C   GLY A 399      30.397   4.384  29.559  1.00 96.52           C  
ATOM   1353  O   GLY A 399      29.346   4.150  28.958  1.00 97.61           O  
ATOM   1354  N   ALA A 400      31.060   5.529  29.430  1.00 93.57           N  
ATOM   1355  CA  ALA A 400      30.665   6.533  28.445  1.00 89.55           C  
ATOM   1356  C   ALA A 400      31.582   6.445  27.227  1.00 86.20           C  
ATOM   1357  O   ALA A 400      32.628   5.795  27.264  1.00 86.69           O  
ATOM   1358  CB  ALA A 400      30.735   7.934  29.059  1.00 89.15           C  
ATOM   1359  N   LYS A 401      31.186   7.094  26.141  1.00 81.05           N  
ATOM   1360  CA  LYS A 401      32.054   7.182  24.977  1.00 76.11           C  
ATOM   1361  C   LYS A 401      32.456   8.634  24.755  1.00 72.32           C  
ATOM   1362  O   LYS A 401      31.609   9.525  24.685  1.00 71.46           O  
ATOM   1363  CB  LYS A 401      31.338   6.645  23.740  1.00 76.90           C  
ATOM   1364  CG  LYS A 401      32.309   6.273  22.641  1.00 78.02           C  
ATOM   1365  CD  LYS A 401      33.007   4.985  23.030  1.00 79.65           C  
ATOM   1366  CE  LYS A 401      31.993   3.853  23.096  1.00 81.90           C  
ATOM   1367  NZ  LYS A 401      31.290   3.649  21.793  1.00 82.26           N  
ATOM   1368  N   PHE A 402      33.758   8.872  24.651  1.00 67.95           N  
ATOM   1369  CA  PHE A 402      34.264  10.227  24.472  1.00 63.22           C  
ATOM   1370  C   PHE A 402      35.696  10.233  23.953  1.00 59.34           C  
ATOM   1371  O   PHE A 402      36.475   9.319  24.227  1.00 58.44           O  
ATOM   1372  CB  PHE A 402      34.186  10.993  25.795  1.00 63.05           C  
ATOM   1373  CG  PHE A 402      34.758  10.244  26.965  1.00 65.05           C  
ATOM   1374  CD1 PHE A 402      36.129  10.083  27.101  1.00 65.72           C  
ATOM   1375  CD2 PHE A 402      33.926   9.706  27.934  1.00 65.42           C  
ATOM   1376  CE1 PHE A 402      36.657   9.399  28.181  1.00 65.81           C  
ATOM   1377  CE2 PHE A 402      34.449   9.020  29.017  1.00 64.50           C  
ATOM   1378  CZ  PHE A 402      35.815   8.867  29.140  1.00 64.98           C  
ATOM   1379  N   PRO A 403      36.057  11.272  23.182  1.00 55.94           N  
ATOM   1380  CA  PRO A 403      37.418  11.467  22.670  1.00 53.24           C  
ATOM   1381  C   PRO A 403      38.363  11.774  23.820  1.00 51.22           C  
ATOM   1382  O   PRO A 403      38.290  12.846  24.419  1.00 51.40           O  
ATOM   1383  CB  PRO A 403      37.284  12.656  21.721  1.00 54.04           C  
ATOM   1384  CG  PRO A 403      35.825  12.747  21.419  1.00 54.64           C  
ATOM   1385  CD  PRO A 403      35.135  12.294  22.666  1.00 55.06           C  
ATOM   1386  N   ILE A 404      39.248  10.832  24.122  1.00 48.95           N  
ATOM   1387  CA  ILE A 404      40.069  10.920  25.321  1.00 48.42           C  
ATOM   1388  C   ILE A 404      40.808  12.252  25.363  1.00 48.08           C  
ATOM   1389  O   ILE A 404      40.820  12.952  26.379  1.00 48.24           O  
ATOM   1390  CB  ILE A 404      41.113   9.771  25.376  1.00 48.67           C  
ATOM   1391  CG1 ILE A 404      40.411   8.413  25.235  1.00 47.92           C  
ATOM   1392  CG2 ILE A 404      41.894   9.834  26.681  1.00 46.11           C  
ATOM   1393  CD1 ILE A 404      39.177   8.251  26.108  1.00 45.89           C  
ATOM   1394  N   LYS A 405      41.408  12.611  24.235  1.00 46.49           N  
ATOM   1395  CA  LYS A 405      42.323  13.740  24.186  1.00 45.59           C  
ATOM   1396  C   LYS A 405      41.633  15.100  24.169  1.00 44.26           C  
ATOM   1397  O   LYS A 405      42.303  16.129  24.218  1.00 42.45           O  
ATOM   1398  CB  LYS A 405      43.239  13.599  22.969  1.00 46.56           C  
ATOM   1399  CG  LYS A 405      44.202  12.430  23.123  1.00 44.83           C  
ATOM   1400  CD  LYS A 405      45.042  12.245  21.877  1.00 45.98           C  
ATOM   1401  CE  LYS A 405      46.395  11.625  22.172  1.00 45.26           C  
ATOM   1402  NZ  LYS A 405      47.241  11.574  20.950  1.00 45.71           N  
ATOM   1403  N   TRP A 406      40.305  15.103  24.101  1.00 44.55           N  
ATOM   1404  CA  TRP A 406      39.542  16.350  24.092  1.00 43.80           C  
ATOM   1405  C   TRP A 406      38.690  16.525  25.341  1.00 44.20           C  
ATOM   1406  O   TRP A 406      38.119  17.589  25.573  1.00 44.96           O  
ATOM   1407  CB  TRP A 406      38.629  16.408  22.872  1.00 42.40           C  
ATOM   1408  CG  TRP A 406      39.325  16.771  21.607  1.00 41.64           C  
ATOM   1409  CD1 TRP A 406      39.453  18.017  21.070  1.00 38.07           C  
ATOM   1410  CD2 TRP A 406      39.947  15.869  20.685  1.00 42.57           C  
ATOM   1411  NE1 TRP A 406      40.112  17.949  19.867  1.00 38.03           N  
ATOM   1412  CE2 TRP A 406      40.427  16.642  19.607  1.00 41.80           C  
ATOM   1413  CE3 TRP A 406      40.145  14.484  20.666  1.00 42.47           C  
ATOM   1414  CZ2 TRP A 406      41.092  16.076  18.519  1.00 43.52           C  
ATOM   1415  CZ3 TRP A 406      40.806  13.922  19.586  1.00 44.59           C  
ATOM   1416  CH2 TRP A 406      41.272  14.719  18.526  1.00 44.20           C  
ATOM   1417  N   THR A 407      38.598  15.475  26.144  1.00 44.08           N  
ATOM   1418  CA  THR A 407      37.653  15.460  27.247  1.00 44.16           C  
ATOM   1419  C   THR A 407      38.283  15.940  28.555  1.00 44.90           C  
ATOM   1420  O   THR A 407      39.333  15.453  28.983  1.00 44.71           O  
ATOM   1421  CB  THR A 407      37.066  14.044  27.420  1.00 44.36           C  
ATOM   1422  OG1 THR A 407      36.429  13.644  26.200  1.00 43.66           O  
ATOM   1423  CG2 THR A 407      36.047  14.018  28.545  1.00 43.81           C  
ATOM   1424  N   ALA A 408      37.625  16.908  29.189  1.00 45.01           N  
ATOM   1425  CA  ALA A 408      38.046  17.405  30.493  1.00 44.84           C  
ATOM   1426  C   ALA A 408      38.092  16.261  31.499  1.00 46.12           C  
ATOM   1427  O   ALA A 408      37.306  15.313  31.433  1.00 44.59           O  
ATOM   1428  CB  ALA A 408      37.088  18.484  30.977  1.00 42.90           C  
ATOM   1429  N   PRO A 409      39.023  16.345  32.463  1.00 47.71           N  
ATOM   1430  CA  PRO A 409      39.251  15.263  33.428  1.00 47.76           C  
ATOM   1431  C   PRO A 409      38.040  14.944  34.314  1.00 47.77           C  
ATOM   1432  O   PRO A 409      37.839  13.792  34.703  1.00 47.63           O  
ATOM   1433  CB  PRO A 409      40.453  15.749  34.237  1.00 46.31           C  
ATOM   1434  CG  PRO A 409      40.428  17.229  34.095  1.00 47.14           C  
ATOM   1435  CD  PRO A 409      39.884  17.511  32.725  1.00 45.94           C  
ATOM   1436  N   GLU A 410      37.234  15.955  34.628  1.00 46.53           N  
ATOM   1437  CA  GLU A 410      36.054  15.726  35.452  1.00 46.27           C  
ATOM   1438  C   GLU A 410      35.036  14.894  34.680  1.00 47.28           C  
ATOM   1439  O   GLU A 410      34.228  14.169  35.258  1.00 46.49           O  
ATOM   1440  CB  GLU A 410      35.421  17.054  35.879  1.00 45.44           C  
ATOM   1441  CG  GLU A 410      34.656  17.740  34.762  1.00 45.65           C  
ATOM   1442  CD  GLU A 410      35.503  18.837  34.151  1.00 45.92           C  
ATOM   1443  OE1 GLU A 410      36.683  18.962  34.542  1.00 45.77           O  
ATOM   1444  OE2 GLU A 410      34.987  19.574  33.283  1.00 43.10           O  
ATOM   1445  N   ALA A 411      35.082  14.999  33.356  1.00 48.28           N  
ATOM   1446  CA  ALA A 411      34.225  14.183  32.510  1.00 49.82           C  
ATOM   1447  C   ALA A 411      34.778  12.760  32.439  1.00 51.92           C  
ATOM   1448  O   ALA A 411      34.033  11.779  32.476  1.00 52.28           O  
ATOM   1449  CB  ALA A 411      34.143  14.787  31.124  1.00 47.15           C  
ATOM   1450  N   ILE A 412      36.102  12.657  32.347  1.00 53.21           N  
ATOM   1451  CA  ILE A 412      36.782  11.364  32.321  1.00 53.38           C  
ATOM   1452  C   ILE A 412      36.588  10.595  33.624  1.00 54.92           C  
ATOM   1453  O   ILE A 412      36.311   9.394  33.618  1.00 55.88           O  
ATOM   1454  CB  ILE A 412      38.301  11.533  32.115  1.00 52.77           C  
ATOM   1455  CG1 ILE A 412      38.579  12.102  30.723  1.00 51.15           C  
ATOM   1456  CG2 ILE A 412      39.003  10.201  32.303  1.00 53.11           C  
ATOM   1457  CD1 ILE A 412      39.994  12.594  30.544  1.00 48.62           C  
ATOM   1458  N   ASN A 413      36.732  11.299  34.744  1.00 55.22           N  
ATOM   1459  CA  ASN A 413      36.674  10.671  36.060  1.00 55.75           C  
ATOM   1460  C   ASN A 413      35.245  10.415  36.523  1.00 55.99           C  
ATOM   1461  O   ASN A 413      34.898   9.315  36.948  1.00 56.52           O  
ATOM   1462  CB  ASN A 413      37.382  11.548  37.094  1.00 54.87           C  
ATOM   1463  CG  ASN A 413      38.823  11.828  36.728  1.00 56.02           C  
ATOM   1464  OD1 ASN A 413      39.517  10.968  36.180  1.00 54.47           O  
ATOM   1465  ND2 ASN A 413      39.283  13.040  37.029  1.00 54.97           N  
ATOM   1466  N   TYR A 414      34.413  11.444  36.441  1.00 56.61           N  
ATOM   1467  CA  TYR A 414      33.105  11.402  37.075  1.00 56.96           C  
ATOM   1468  C   TYR A 414      31.962  11.423  36.070  1.00 56.72           C  
ATOM   1469  O   TYR A 414      30.793  11.452  36.457  1.00 56.82           O  
ATOM   1470  CB  TYR A 414      32.978  12.571  38.045  1.00 58.33           C  
ATOM   1471  CG  TYR A 414      34.151  12.659  38.988  1.00 62.06           C  
ATOM   1472  CD1 TYR A 414      34.403  11.645  39.905  1.00 63.16           C  
ATOM   1473  CD2 TYR A 414      35.021  13.743  38.949  1.00 63.00           C  
ATOM   1474  CE1 TYR A 414      35.491  11.705  40.758  1.00 65.30           C  
ATOM   1475  CE2 TYR A 414      36.114  13.815  39.799  1.00 64.33           C  
ATOM   1476  CZ  TYR A 414      36.344  12.791  40.702  1.00 65.79           C  
ATOM   1477  OH  TYR A 414      37.429  12.849  41.551  1.00 66.09           O  
ATOM   1478  N   GLY A 415      32.304  11.409  34.785  1.00 55.93           N  
ATOM   1479  CA  GLY A 415      31.289  11.407  33.748  1.00 53.59           C  
ATOM   1480  C   GLY A 415      30.458  12.675  33.726  1.00 53.29           C  
ATOM   1481  O   GLY A 415      29.354  12.687  33.180  1.00 53.50           O  
ATOM   1482  N   THR A 416      30.977  13.746  34.318  1.00 52.58           N  
ATOM   1483  CA  THR A 416      30.226  14.993  34.398  1.00 54.04           C  
ATOM   1484  C   THR A 416      30.561  15.924  33.236  1.00 53.31           C  
ATOM   1485  O   THR A 416      31.591  16.598  33.210  1.00 52.58           O  
ATOM   1486  CB  THR A 416      30.498  15.728  35.732  1.00 55.65           C  
ATOM   1487  OG1 THR A 416      31.889  16.055  35.828  1.00 59.70           O  
ATOM   1488  CG2 THR A 416      30.108  14.847  36.914  1.00 55.91           C  
ATOM   1489  N   PHE A 417      29.664  15.955  32.258  1.00 52.74           N  
ATOM   1490  CA  PHE A 417      29.844  16.798  31.085  1.00 51.78           C  
ATOM   1491  C   PHE A 417      29.004  18.060  31.199  1.00 50.80           C  
ATOM   1492  O   PHE A 417      27.799  17.993  31.418  1.00 51.36           O  
ATOM   1493  CB  PHE A 417      29.446  16.035  29.823  1.00 51.72           C  
ATOM   1494  CG  PHE A 417      30.364  14.894  29.487  1.00 51.91           C  
ATOM   1495  CD1 PHE A 417      30.230  13.668  30.119  1.00 52.28           C  
ATOM   1496  CD2 PHE A 417      31.348  15.042  28.522  1.00 52.06           C  
ATOM   1497  CE1 PHE A 417      31.061  12.610  29.793  1.00 52.86           C  
ATOM   1498  CE2 PHE A 417      32.182  13.989  28.191  1.00 51.29           C  
ATOM   1499  CZ  PHE A 417      32.038  12.772  28.827  1.00 52.44           C  
ATOM   1500  N   THR A 418      29.651  19.210  31.050  1.00 49.46           N  
ATOM   1501  CA  THR A 418      28.964  20.492  31.122  1.00 47.04           C  
ATOM   1502  C   THR A 418      29.467  21.391  30.004  1.00 46.13           C  
ATOM   1503  O   THR A 418      30.243  20.958  29.152  1.00 44.73           O  
ATOM   1504  CB  THR A 418      29.235  21.198  32.458  1.00 47.95           C  
ATOM   1505  OG1 THR A 418      30.633  21.493  32.565  1.00 50.26           O  
ATOM   1506  CG2 THR A 418      28.824  20.311  33.620  1.00 45.59           C  
ATOM   1507  N   ILE A 419      29.027  22.645  30.009  1.00 44.58           N  
ATOM   1508  CA  ILE A 419      29.477  23.603  29.011  1.00 42.48           C  
ATOM   1509  C   ILE A 419      30.938  23.940  29.299  1.00 42.25           C  
ATOM   1510  O   ILE A 419      31.728  24.241  28.407  1.00 43.08           O  
ATOM   1511  CB  ILE A 419      28.619  24.894  29.050  1.00 40.54           C  
ATOM   1512  CG1 ILE A 419      28.931  25.776  27.838  1.00 38.69           C  
ATOM   1513  CG2 ILE A 419      28.903  25.666  30.320  1.00 38.49           C  
ATOM   1514  CD1 ILE A 419      28.507  25.181  26.514  1.00 36.05           C  
ATOM   1515  N   LYS A 420      31.301  23.877  30.574  1.00 42.87           N  
ATOM   1516  CA  LYS A 420      32.673  24.154  30.980  1.00 42.44           C  
ATOM   1517  C   LYS A 420      33.572  23.012  30.534  1.00 41.55           C  
ATOM   1518  O   LYS A 420      34.771  23.161  30.319  1.00 41.98           O  
ATOM   1519  CB  LYS A 420      32.747  24.324  32.500  1.00 41.92           C  
ATOM   1520  CG  LYS A 420      32.174  25.666  32.960  1.00 39.47           C  
ATOM   1521  CD  LYS A 420      33.037  26.830  32.497  1.00 38.96           C  
ATOM   1522  CE  LYS A 420      32.699  28.198  33.074  1.00 38.99           C  
ATOM   1523  NZ  LYS A 420      31.866  29.023  32.149  1.00 40.64           N  
ATOM   1524  N   SER A 421      32.955  21.848  30.390  1.00 41.34           N  
ATOM   1525  CA  SER A 421      33.621  20.675  29.852  1.00 41.30           C  
ATOM   1526  C   SER A 421      33.924  20.875  28.357  1.00 41.86           C  
ATOM   1527  O   SER A 421      34.910  20.359  27.821  1.00 41.29           O  
ATOM   1528  CB  SER A 421      32.719  19.455  30.059  1.00 41.54           C  
ATOM   1529  OG  SER A 421      33.370  18.256  29.689  1.00 46.36           O  
ATOM   1530  N   ASP A 422      33.065  21.642  27.689  1.00 42.12           N  
ATOM   1531  CA  ASP A 422      33.237  21.953  26.270  1.00 41.77           C  
ATOM   1532  C   ASP A 422      34.312  23.014  26.078  1.00 40.32           C  
ATOM   1533  O   ASP A 422      35.016  23.055  25.068  1.00 39.83           O  
ATOM   1534  CB  ASP A 422      31.922  22.464  25.665  1.00 41.34           C  
ATOM   1535  CG  ASP A 422      30.874  21.373  25.520  1.00 43.27           C  
ATOM   1536  OD1 ASP A 422      31.247  20.183  25.386  1.00 41.98           O  
ATOM   1537  OD2 ASP A 422      29.669  21.713  25.539  1.00 43.64           O  
ATOM   1538  N   VAL A 423      34.423  23.893  27.065  1.00 39.43           N  
ATOM   1539  CA  VAL A 423      35.439  24.925  27.038  1.00 39.27           C  
ATOM   1540  C   VAL A 423      36.805  24.265  27.026  1.00 38.98           C  
ATOM   1541  O   VAL A 423      37.704  24.692  26.305  1.00 39.29           O  
ATOM   1542  CB  VAL A 423      35.323  25.841  28.263  1.00 39.90           C  
ATOM   1543  CG1 VAL A 423      36.483  26.821  28.291  1.00 40.76           C  
ATOM   1544  CG2 VAL A 423      34.003  26.592  28.218  1.00 39.73           C  
ATOM   1545  N   TRP A 424      36.953  23.211  27.821  1.00 38.17           N  
ATOM   1546  CA  TRP A 424      38.181  22.429  27.813  1.00 38.63           C  
ATOM   1547  C   TRP A 424      38.452  21.922  26.398  1.00 39.19           C  
ATOM   1548  O   TRP A 424      39.529  22.139  25.836  1.00 38.08           O  
ATOM   1549  CB  TRP A 424      38.056  21.248  28.780  1.00 39.45           C  
ATOM   1550  CG  TRP A 424      39.276  20.357  28.835  1.00 38.89           C  
ATOM   1551  CD1 TRP A 424      39.647  19.419  27.915  1.00 37.95           C  
ATOM   1552  CD2 TRP A 424      40.262  20.308  29.876  1.00 38.17           C  
ATOM   1553  NE1 TRP A 424      40.800  18.790  28.316  1.00 37.55           N  
ATOM   1554  CE2 TRP A 424      41.199  19.315  29.516  1.00 39.47           C  
ATOM   1555  CE3 TRP A 424      40.445  21.006  31.076  1.00 38.47           C  
ATOM   1556  CZ2 TRP A 424      42.306  18.999  30.317  1.00 37.80           C  
ATOM   1557  CZ3 TRP A 424      41.546  20.691  31.871  1.00 39.61           C  
ATOM   1558  CH2 TRP A 424      42.460  19.695  31.485  1.00 36.45           C  
ATOM   1559  N   SER A 425      37.455  21.254  25.822  1.00 39.57           N  
ATOM   1560  CA  SER A 425      37.553  20.739  24.457  1.00 38.65           C  
ATOM   1561  C   SER A 425      37.950  21.837  23.482  1.00 36.24           C  
ATOM   1562  O   SER A 425      38.734  21.614  22.561  1.00 36.34           O  
ATOM   1563  CB  SER A 425      36.216  20.140  24.013  1.00 39.77           C  
ATOM   1564  OG  SER A 425      35.816  19.084  24.865  1.00 44.93           O  
ATOM   1565  N   PHE A 426      37.398  23.027  23.686  1.00 34.03           N  
ATOM   1566  CA  PHE A 426      37.702  24.153  22.817  1.00 33.43           C  
ATOM   1567  C   PHE A 426      39.190  24.511  22.852  1.00 33.51           C  
ATOM   1568  O   PHE A 426      39.776  24.880  21.833  1.00 31.79           O  
ATOM   1569  CB  PHE A 426      36.873  25.373  23.219  1.00 31.44           C  
ATOM   1570  CG  PHE A 426      37.094  26.558  22.332  1.00 31.73           C  
ATOM   1571  CD1 PHE A 426      36.494  26.626  21.083  1.00 32.45           C  
ATOM   1572  CD2 PHE A 426      37.932  27.588  22.725  1.00 32.57           C  
ATOM   1573  CE1 PHE A 426      36.733  27.694  20.240  1.00 30.22           C  
ATOM   1574  CE2 PHE A 426      38.175  28.660  21.885  1.00 33.19           C  
ATOM   1575  CZ  PHE A 426      37.572  28.712  20.641  1.00 32.34           C  
ATOM   1576  N   GLY A 427      39.796  24.401  24.031  1.00 33.70           N  
ATOM   1577  CA  GLY A 427      41.215  24.666  24.149  1.00 33.76           C  
ATOM   1578  C   GLY A 427      42.015  23.658  23.347  1.00 34.81           C  
ATOM   1579  O   GLY A 427      42.980  24.011  22.667  1.00 35.36           O  
ATOM   1580  N   ILE A 428      41.609  22.395  23.413  1.00 33.98           N  
ATOM   1581  CA  ILE A 428      42.287  21.356  22.654  1.00 34.38           C  
ATOM   1582  C   ILE A 428      42.031  21.573  21.165  1.00 35.12           C  
ATOM   1583  O   ILE A 428      42.917  21.419  20.321  1.00 34.18           O  
ATOM   1584  CB  ILE A 428      41.791  19.951  23.055  1.00 34.42           C  
ATOM   1585  CG1 ILE A 428      41.949  19.743  24.565  1.00 34.09           C  
ATOM   1586  CG2 ILE A 428      42.601  18.890  22.317  1.00 35.47           C  
ATOM   1587  CD1 ILE A 428      43.393  19.591  25.024  1.00 30.92           C  
ATOM   1588  N   LEU A 429      40.795  21.946  20.846  1.00 36.62           N  
ATOM   1589  CA  LEU A 429      40.433  22.284  19.476  1.00 37.18           C  
ATOM   1590  C   LEU A 429      41.354  23.391  18.951  1.00 37.54           C  
ATOM   1591  O   LEU A 429      41.799  23.338  17.803  1.00 37.98           O  
ATOM   1592  CB  LEU A 429      38.967  22.734  19.423  1.00 37.73           C  
ATOM   1593  CG  LEU A 429      38.295  22.890  18.052  1.00 37.37           C  
ATOM   1594  CD1 LEU A 429      36.791  22.901  18.219  1.00 36.73           C  
ATOM   1595  CD2 LEU A 429      38.757  24.167  17.389  1.00 37.37           C  
ATOM   1596  N   LEU A 430      41.642  24.379  19.798  1.00 35.96           N  
ATOM   1597  CA  LEU A 430      42.549  25.466  19.444  1.00 35.10           C  
ATOM   1598  C   LEU A 430      43.912  24.966  18.983  1.00 35.58           C  
ATOM   1599  O   LEU A 430      44.495  25.504  18.045  1.00 36.01           O  
ATOM   1600  CB  LEU A 430      42.741  26.413  20.632  1.00 34.81           C  
ATOM   1601  CG  LEU A 430      41.598  27.397  20.897  1.00 36.55           C  
ATOM   1602  CD1 LEU A 430      41.948  28.285  22.088  1.00 34.69           C  
ATOM   1603  CD2 LEU A 430      41.359  28.244  19.658  1.00 35.31           C  
ATOM   1604  N   THR A 431      44.431  23.938  19.640  1.00 37.25           N  
ATOM   1605  CA  THR A 431      45.738  23.422  19.260  1.00 38.45           C  
ATOM   1606  C   THR A 431      45.653  22.738  17.900  1.00 38.65           C  
ATOM   1607  O   THR A 431      46.603  22.794  17.123  1.00 38.39           O  
ATOM   1608  CB  THR A 431      46.275  22.430  20.307  1.00 39.32           C  
ATOM   1609  OG1 THR A 431      45.489  21.231  20.291  1.00 39.74           O  
ATOM   1610  CG2 THR A 431      46.213  23.054  21.694  1.00 37.76           C  
ATOM   1611  N   GLU A 432      44.517  22.109  17.609  1.00 38.91           N  
ATOM   1612  CA  GLU A 432      44.295  21.526  16.288  1.00 38.81           C  
ATOM   1613  C   GLU A 432      44.322  22.612  15.213  1.00 40.39           C  
ATOM   1614  O   GLU A 432      44.966  22.467  14.175  1.00 40.53           O  
ATOM   1615  CB  GLU A 432      42.946  20.811  16.232  1.00 37.81           C  
ATOM   1616  CG  GLU A 432      42.836  19.647  17.190  1.00 39.76           C  
ATOM   1617  CD  GLU A 432      41.500  18.996  16.864  1.00 41.46           C  
ATOM   1618  OE1 GLU A 432      40.449  19.518  17.305  1.00 42.32           O  
ATOM   1619  OE2 GLU A 432      41.499  17.962  16.162  1.00 42.70           O  
ATOM   1620  N   ILE A 433      43.609  23.706  15.471  1.00 41.67           N  
ATOM   1621  CA  ILE A 433      43.512  24.813  14.521  1.00 42.40           C  
ATOM   1622  C   ILE A 433      44.885  25.384  14.183  1.00 42.82           C  
ATOM   1623  O   ILE A 433      45.206  25.746  13.046  1.00 42.54           O  
ATOM   1624  CB  ILE A 433      42.658  25.971  15.091  1.00 42.37           C  
ATOM   1625  CG1 ILE A 433      41.190  25.555  15.159  1.00 42.61           C  
ATOM   1626  CG2 ILE A 433      42.815  27.215  14.233  1.00 42.25           C  
ATOM   1627  CD1 ILE A 433      40.269  26.650  15.665  1.00 43.19           C  
ATOM   1628  N   VAL A 434      45.718  25.462  15.208  1.00 43.39           N  
ATOM   1629  CA  VAL A 434      46.973  26.165  15.079  1.00 44.12           C  
ATOM   1630  C   VAL A 434      48.087  25.203  14.648  1.00 44.72           C  
ATOM   1631  O   VAL A 434      49.230  25.612  14.453  1.00 45.12           O  
ATOM   1632  CB  VAL A 434      47.304  26.884  16.408  1.00 42.74           C  
ATOM   1633  CG1 VAL A 434      47.952  25.921  17.383  1.00 41.99           C  
ATOM   1634  CG2 VAL A 434      48.179  28.082  16.142  1.00 46.91           C  
ATOM   1635  N   THR A 435      47.752  23.925  14.486  1.00 44.87           N  
ATOM   1636  CA  THR A 435      48.744  22.939  14.058  1.00 45.45           C  
ATOM   1637  C   THR A 435      48.321  22.105  12.847  1.00 46.74           C  
ATOM   1638  O   THR A 435      48.646  20.921  12.783  1.00 47.36           O  
ATOM   1639  CB  THR A 435      49.081  21.931  15.180  1.00 44.95           C  
ATOM   1640  OG1 THR A 435      47.911  21.176  15.520  1.00 43.49           O  
ATOM   1641  CG2 THR A 435      49.592  22.657  16.413  1.00 44.38           C  
ATOM   1642  N   HIS A 436      47.607  22.714  11.904  1.00 47.75           N  
ATOM   1643  CA  HIS A 436      47.221  22.032  10.671  1.00 48.18           C  
ATOM   1644  C   HIS A 436      46.388  20.784  10.944  1.00 47.18           C  
ATOM   1645  O   HIS A 436      46.409  19.835  10.165  1.00 47.39           O  
ATOM   1646  CB  HIS A 436      48.463  21.635   9.867  1.00 51.54           C  
ATOM   1647  CG  HIS A 436      49.387  22.776   9.573  1.00 57.72           C  
ATOM   1648  ND1 HIS A 436      48.967  24.089   9.546  1.00 60.15           N  
ATOM   1649  CD2 HIS A 436      50.711  22.798   9.284  1.00 58.08           C  
ATOM   1650  CE1 HIS A 436      49.991  24.871   9.252  1.00 59.36           C  
ATOM   1651  NE2 HIS A 436      51.061  24.113   9.089  1.00 59.66           N  
ATOM   1652  N   GLY A 437      45.664  20.777  12.055  1.00 46.54           N  
ATOM   1653  CA  GLY A 437      44.783  19.658  12.337  1.00 47.20           C  
ATOM   1654  C   GLY A 437      45.506  18.479  12.954  1.00 46.73           C  
ATOM   1655  O   GLY A 437      45.012  17.353  12.927  1.00 47.10           O  
ATOM   1656  N   ARG A 438      46.679  18.741  13.515  1.00 47.41           N  
ATOM   1657  CA  ARG A 438      47.481  17.703  14.144  1.00 48.61           C  
ATOM   1658  C   ARG A 438      46.760  17.151  15.372  1.00 48.73           C  
ATOM   1659  O   ARG A 438      46.066  17.883  16.081  1.00 48.44           O  
ATOM   1660  CB  ARG A 438      48.837  18.281  14.546  1.00 51.98           C  
ATOM   1661  CG  ARG A 438      49.818  17.235  15.041  1.00 58.39           C  
ATOM   1662  CD  ARG A 438      51.051  17.998  15.507  1.00 64.74           C  
ATOM   1663  NE  ARG A 438      52.169  17.111  15.824  1.00 72.06           N  
ATOM   1664  CZ  ARG A 438      53.318  17.514  16.363  1.00 75.09           C  
ATOM   1665  NH1 ARG A 438      53.509  18.797  16.652  1.00 76.40           N  
ATOM   1666  NH2 ARG A 438      54.280  16.633  16.615  1.00 75.01           N  
ATOM   1667  N   ILE A 439      46.923  15.854  15.617  1.00 48.14           N  
ATOM   1668  CA  ILE A 439      46.319  15.211  16.780  1.00 47.38           C  
ATOM   1669  C   ILE A 439      46.902  15.782  18.068  1.00 48.05           C  
ATOM   1670  O   ILE A 439      48.111  15.986  18.194  1.00 47.44           O  
ATOM   1671  CB  ILE A 439      46.563  13.686  16.767  1.00 47.54           C  
ATOM   1672  CG1 ILE A 439      45.942  13.078  15.509  1.00 47.15           C  
ATOM   1673  CG2 ILE A 439      45.971  13.039  18.016  1.00 43.19           C  
ATOM   1674  CD1 ILE A 439      46.115  11.581  15.423  1.00 50.61           C  
ATOM   1675  N   PRO A 440      46.034  16.055  19.051  1.00 48.42           N  
ATOM   1676  CA  PRO A 440      46.478  16.634  20.322  1.00 47.80           C  
ATOM   1677  C   PRO A 440      47.442  15.706  21.047  1.00 48.04           C  
ATOM   1678  O   PRO A 440      47.540  14.526  20.717  1.00 47.04           O  
ATOM   1679  CB  PRO A 440      45.178  16.833  21.099  1.00 47.70           C  
ATOM   1680  CG  PRO A 440      44.121  16.901  20.048  1.00 47.61           C  
ATOM   1681  CD  PRO A 440      44.567  15.948  18.982  1.00 47.47           C  
ATOM   1682  N   TYR A 441      48.150  16.251  22.032  1.00 49.35           N  
ATOM   1683  CA  TYR A 441      49.082  15.470  22.836  1.00 50.83           C  
ATOM   1684  C   TYR A 441      49.949  14.598  21.943  1.00 53.95           C  
ATOM   1685  O   TYR A 441      49.892  13.367  21.993  1.00 53.98           O  
ATOM   1686  CB  TYR A 441      48.320  14.587  23.829  1.00 48.08           C  
ATOM   1687  CG  TYR A 441      47.453  15.362  24.798  1.00 45.85           C  
ATOM   1688  CD1 TYR A 441      48.011  16.006  25.898  1.00 41.96           C  
ATOM   1689  CD2 TYR A 441      46.078  15.453  24.609  1.00 43.32           C  
ATOM   1690  CE1 TYR A 441      47.224  16.719  26.779  1.00 39.34           C  
ATOM   1691  CE2 TYR A 441      45.283  16.163  25.485  1.00 40.55           C  
ATOM   1692  CZ  TYR A 441      45.860  16.795  26.568  1.00 39.15           C  
ATOM   1693  OH  TYR A 441      45.065  17.503  27.441  1.00 35.70           O  
ATOM   1694  N   PRO A 442      50.771  15.233  21.099  1.00 56.06           N  
ATOM   1695  CA  PRO A 442      51.658  14.468  20.222  1.00 57.99           C  
ATOM   1696  C   PRO A 442      52.654  13.646  21.039  1.00 60.48           C  
ATOM   1697  O   PRO A 442      53.314  14.169  21.943  1.00 60.10           O  
ATOM   1698  CB  PRO A 442      52.340  15.542  19.380  1.00 57.23           C  
ATOM   1699  CG  PRO A 442      52.278  16.773  20.221  1.00 55.44           C  
ATOM   1700  CD  PRO A 442      50.994  16.685  20.988  1.00 55.35           C  
ATOM   1701  N   GLY A 443      52.745  12.356  20.722  1.00 61.21           N  
ATOM   1702  CA  GLY A 443      53.682  11.487  21.411  1.00 61.95           C  
ATOM   1703  C   GLY A 443      53.115  10.838  22.660  1.00 62.74           C  
ATOM   1704  O   GLY A 443      53.860  10.304  23.484  1.00 63.80           O  
ATOM   1705  N   MET A 444      51.796  10.886  22.812  1.00 61.98           N  
ATOM   1706  CA  MET A 444      51.150  10.259  23.956  1.00 61.30           C  
ATOM   1707  C   MET A 444      49.991   9.380  23.514  1.00 60.96           C  
ATOM   1708  O   MET A 444      49.214   9.759  22.638  1.00 62.27           O  
ATOM   1709  CB  MET A 444      50.650  11.327  24.932  1.00 61.05           C  
ATOM   1710  CG  MET A 444      51.783  12.181  25.483  1.00 61.58           C  
ATOM   1711  SD  MET A 444      51.244  13.352  26.749  1.00 60.38           S  
ATOM   1712  CE  MET A 444      50.389  12.263  27.861  1.00 62.33           C  
ATOM   1713  N   THR A 445      49.880   8.200  24.118  1.00 59.36           N  
ATOM   1714  CA  THR A 445      48.733   7.335  23.879  1.00 57.32           C  
ATOM   1715  C   THR A 445      47.599   7.821  24.771  1.00 57.13           C  
ATOM   1716  O   THR A 445      47.853   8.467  25.788  1.00 56.32           O  
ATOM   1717  CB  THR A 445      49.044   5.867  24.233  1.00 55.70           C  
ATOM   1718  OG1 THR A 445      49.135   5.720  25.654  1.00 56.01           O  
ATOM   1719  CG2 THR A 445      50.360   5.446  23.610  1.00 53.67           C  
ATOM   1720  N   ASN A 446      46.362   7.521  24.391  1.00 56.93           N  
ATOM   1721  CA  ASN A 446      45.205   7.934  25.177  1.00 56.74           C  
ATOM   1722  C   ASN A 446      45.352   7.531  26.647  1.00 57.08           C  
ATOM   1723  O   ASN A 446      45.002   8.295  27.551  1.00 55.93           O  
ATOM   1724  CB  ASN A 446      43.923   7.329  24.593  1.00 56.52           C  
ATOM   1725  CG  ASN A 446      43.629   7.824  23.188  1.00 56.04           C  
ATOM   1726  OD1 ASN A 446      44.280   8.741  22.692  1.00 56.82           O  
ATOM   1727  ND2 ASN A 446      42.642   7.217  22.541  1.00 56.91           N  
ATOM   1728  N   PRO A 447      45.875   6.319  26.905  1.00 57.75           N  
ATOM   1729  CA  PRO A 447      46.159   5.914  28.286  1.00 57.52           C  
ATOM   1730  C   PRO A 447      47.200   6.809  28.949  1.00 57.20           C  
ATOM   1731  O   PRO A 447      47.027   7.235  30.089  1.00 57.00           O  
ATOM   1732  CB  PRO A 447      46.644   4.472  28.145  1.00 57.55           C  
ATOM   1733  CG  PRO A 447      46.033   4.001  26.869  1.00 55.81           C  
ATOM   1734  CD  PRO A 447      46.047   5.196  25.966  1.00 56.88           C  
ATOM   1735  N   GLU A 448      48.278   7.096  28.225  1.00 57.72           N  
ATOM   1736  CA  GLU A 448      49.326   7.978  28.729  1.00 58.37           C  
ATOM   1737  C   GLU A 448      48.739   9.344  29.071  1.00 57.16           C  
ATOM   1738  O   GLU A 448      48.982   9.906  30.137  1.00 56.50           O  
ATOM   1739  CB  GLU A 448      50.437   8.139  27.681  1.00 60.94           C  
ATOM   1740  CG  GLU A 448      51.204   6.844  27.425  1.00 63.70           C  
ATOM   1741  CD  GLU A 448      52.251   6.971  26.328  1.00 65.45           C  
ATOM   1742  OE1 GLU A 448      52.140   7.896  25.498  1.00 66.47           O  
ATOM   1743  OE2 GLU A 448      53.188   6.142  26.293  1.00 66.55           O  
ATOM   1744  N   VAL A 449      47.946   9.872  28.146  1.00 56.47           N  
ATOM   1745  CA  VAL A 449      47.288  11.157  28.334  1.00 54.94           C  
ATOM   1746  C   VAL A 449      46.528  11.210  29.653  1.00 55.63           C  
ATOM   1747  O   VAL A 449      46.673  12.153  30.428  1.00 56.68           O  
ATOM   1748  CB  VAL A 449      46.303  11.441  27.184  1.00 53.88           C  
ATOM   1749  CG1 VAL A 449      45.515  12.706  27.470  1.00 52.53           C  
ATOM   1750  CG2 VAL A 449      47.067  11.570  25.871  1.00 53.90           C  
ATOM   1751  N   ILE A 450      45.721  10.190  29.916  1.00 55.30           N  
ATOM   1752  CA  ILE A 450      44.924  10.178  31.132  1.00 55.76           C  
ATOM   1753  C   ILE A 450      45.813  10.115  32.371  1.00 56.53           C  
ATOM   1754  O   ILE A 450      45.536  10.777  33.374  1.00 55.86           O  
ATOM   1755  CB  ILE A 450      43.943   8.993  31.134  1.00 55.79           C  
ATOM   1756  CG1 ILE A 450      43.005   9.106  29.933  1.00 55.13           C  
ATOM   1757  CG2 ILE A 450      43.133   8.986  32.423  1.00 55.31           C  
ATOM   1758  CD1 ILE A 450      41.924   8.066  29.913  1.00 54.05           C  
ATOM   1759  N   GLN A 451      46.885   9.329  32.291  1.00 57.15           N  
ATOM   1760  CA  GLN A 451      47.830   9.204  33.398  1.00 58.55           C  
ATOM   1761  C   GLN A 451      48.440  10.555  33.746  1.00 57.25           C  
ATOM   1762  O   GLN A 451      48.531  10.934  34.915  1.00 57.35           O  
ATOM   1763  CB  GLN A 451      48.954   8.231  33.036  1.00 62.11           C  
ATOM   1764  CG  GLN A 451      48.463   6.816  32.770  1.00 67.39           C  
ATOM   1765  CD  GLN A 451      49.627   6.006  32.217  1.00 70.70           C  
ATOM   1766  OE1 GLN A 451      50.702   6.546  31.944  1.00 71.37           O  
ATOM   1767  NE2 GLN A 451      49.415   4.703  32.049  1.00 71.92           N  
ATOM   1768  N   ASN A 452      48.861  11.281  32.716  1.00 56.38           N  
ATOM   1769  CA  ASN A 452      49.519  12.568  32.903  1.00 55.22           C  
ATOM   1770  C   ASN A 452      48.542  13.635  33.361  1.00 53.74           C  
ATOM   1771  O   ASN A 452      48.924  14.551  34.089  1.00 52.14           O  
ATOM   1772  CB  ASN A 452      50.199  13.011  31.606  1.00 55.32           C  
ATOM   1773  CG  ASN A 452      51.469  12.233  31.325  1.00 57.16           C  
ATOM   1774  OD1 ASN A 452      51.490  11.342  30.475  1.00 58.32           O  
ATOM   1775  ND2 ASN A 452      52.537  12.563  32.046  1.00 57.05           N  
ATOM   1776  N   LEU A 453      47.286  13.516  32.941  1.00 52.89           N  
ATOM   1777  CA  LEU A 453      46.256  14.439  33.399  1.00 53.56           C  
ATOM   1778  C   LEU A 453      46.131  14.352  34.913  1.00 55.11           C  
ATOM   1779  O   LEU A 453      45.948  15.362  35.595  1.00 54.03           O  
ATOM   1780  CB  LEU A 453      44.907  14.118  32.745  1.00 51.45           C  
ATOM   1781  CG  LEU A 453      44.769  14.662  31.319  1.00 49.15           C  
ATOM   1782  CD1 LEU A 453      43.329  14.527  30.855  1.00 46.61           C  
ATOM   1783  CD2 LEU A 453      45.198  16.123  31.286  1.00 48.24           C  
ATOM   1784  N   GLU A 454      46.243  13.133  35.432  1.00 57.71           N  
ATOM   1785  CA  GLU A 454      46.207  12.898  36.869  1.00 59.99           C  
ATOM   1786  C   GLU A 454      47.328  13.661  37.565  1.00 60.16           C  
ATOM   1787  O   GLU A 454      47.218  14.027  38.735  1.00 59.95           O  
ATOM   1788  CB  GLU A 454      46.349  11.404  37.160  1.00 62.60           C  
ATOM   1789  CG  GLU A 454      45.215  10.582  36.564  1.00 68.25           C  
ATOM   1790  CD  GLU A 454      45.510   9.099  36.735  1.00 70.65           C  
ATOM   1791  OE1 GLU A 454      44.608   8.275  36.463  1.00 71.66           O  
ATOM   1792  OE2 GLU A 454      46.643   8.757  37.140  1.00 71.06           O  
ATOM   1793  N   ARG A 455      48.410  13.901  36.832  1.00 61.01           N  
ATOM   1794  CA  ARG A 455      49.576  14.586  37.383  1.00 61.07           C  
ATOM   1795  C   ARG A 455      49.538  16.094  37.156  1.00 58.95           C  
ATOM   1796  O   ARG A 455      50.482  16.797  37.516  1.00 59.85           O  
ATOM   1797  CB  ARG A 455      50.860  14.017  36.774  1.00 63.32           C  
ATOM   1798  CG  ARG A 455      51.079  12.560  37.141  1.00 65.83           C  
ATOM   1799  CD  ARG A 455      52.471  12.112  36.733  1.00 69.73           C  
ATOM   1800  NE  ARG A 455      52.445  11.253  35.553  1.00 73.29           N  
ATOM   1801  CZ  ARG A 455      51.993  10.002  35.557  1.00 75.36           C  
ATOM   1802  NH1 ARG A 455      51.528   9.470  36.681  1.00 75.74           N  
ATOM   1803  NH2 ARG A 455      52.012   9.282  34.440  1.00 75.71           N  
ATOM   1804  N   GLY A 456      48.457  16.583  36.557  1.00 56.19           N  
ATOM   1805  CA  GLY A 456      48.331  18.009  36.307  1.00 52.99           C  
ATOM   1806  C   GLY A 456      48.978  18.452  35.004  1.00 50.66           C  
ATOM   1807  O   GLY A 456      49.082  19.650  34.724  1.00 48.49           O  
ATOM   1808  N   TYR A 457      49.410  17.483  34.201  1.00 49.07           N  
ATOM   1809  CA  TYR A 457      50.109  17.777  32.956  1.00 46.85           C  
ATOM   1810  C   TYR A 457      49.216  18.480  31.940  1.00 45.76           C  
ATOM   1811  O   TYR A 457      48.028  18.188  31.796  1.00 44.07           O  
ATOM   1812  CB  TYR A 457      50.671  16.492  32.342  1.00 45.49           C  
ATOM   1813  CG  TYR A 457      51.240  16.687  30.956  1.00 45.38           C  
ATOM   1814  CD1 TYR A 457      52.537  17.151  30.770  1.00 45.68           C  
ATOM   1815  CD2 TYR A 457      50.473  16.422  29.828  1.00 46.50           C  
ATOM   1816  CE1 TYR A 457      53.053  17.348  29.493  1.00 47.01           C  
ATOM   1817  CE2 TYR A 457      50.976  16.614  28.550  1.00 45.65           C  
ATOM   1818  CZ  TYR A 457      52.263  17.076  28.387  1.00 46.13           C  
ATOM   1819  OH  TYR A 457      52.752  17.268  27.117  1.00 44.97           O  
ATOM   1820  N   ARG A 458      49.817  19.431  31.232  1.00 45.27           N  
ATOM   1821  CA  ARG A 458      49.140  20.161  30.174  1.00 43.81           C  
ATOM   1822  C   ARG A 458      49.960  20.096  28.894  1.00 43.71           C  
ATOM   1823  O   ARG A 458      51.184  19.988  28.932  1.00 43.81           O  
ATOM   1824  CB  ARG A 458      48.939  21.618  30.589  1.00 43.18           C  
ATOM   1825  CG  ARG A 458      47.975  21.751  31.746  1.00 41.49           C  
ATOM   1826  CD  ARG A 458      46.647  21.113  31.376  1.00 41.41           C  
ATOM   1827  NE  ARG A 458      45.619  21.398  32.373  1.00 43.16           N  
ATOM   1828  CZ  ARG A 458      45.293  20.578  33.368  1.00 43.12           C  
ATOM   1829  NH1 ARG A 458      45.917  19.413  33.502  1.00 43.82           N  
ATOM   1830  NH2 ARG A 458      44.347  20.924  34.232  1.00 41.15           N  
ATOM   1831  N   MET A 459      49.276  20.161  27.757  1.00 43.88           N  
ATOM   1832  CA  MET A 459      49.936  20.028  26.463  1.00 44.79           C  
ATOM   1833  C   MET A 459      50.934  21.168  26.272  1.00 45.06           C  
ATOM   1834  O   MET A 459      50.712  22.284  26.746  1.00 47.16           O  
ATOM   1835  CB  MET A 459      48.891  20.046  25.344  1.00 43.64           C  
ATOM   1836  CG  MET A 459      49.412  19.460  24.044  1.00 45.34           C  
ATOM   1837  SD  MET A 459      48.168  19.434  22.730  1.00 46.08           S  
ATOM   1838  CE  MET A 459      46.735  18.831  23.626  1.00 47.63           C  
ATOM   1839  N   VAL A 460      52.041  20.890  25.590  1.00 43.71           N  
ATOM   1840  CA  VAL A 460      53.047  21.922  25.358  1.00 41.43           C  
ATOM   1841  C   VAL A 460      52.579  22.887  24.275  1.00 40.83           C  
ATOM   1842  O   VAL A 460      51.921  22.489  23.311  1.00 39.31           O  
ATOM   1843  CB  VAL A 460      54.406  21.312  24.931  1.00 38.68           C  
ATOM   1844  CG1 VAL A 460      55.394  22.421  24.594  1.00 34.73           C  
ATOM   1845  CG2 VAL A 460      54.958  20.450  26.050  1.00 38.13           C  
ATOM   1846  N   ARG A 461      52.918  24.162  24.441  1.00 39.68           N  
ATOM   1847  CA  ARG A 461      52.552  25.165  23.457  1.00 40.34           C  
ATOM   1848  C   ARG A 461      53.049  24.755  22.080  1.00 41.85           C  
ATOM   1849  O   ARG A 461      54.247  24.577  21.857  1.00 42.28           O  
ATOM   1850  CB  ARG A 461      53.152  26.517  23.826  1.00 39.94           C  
ATOM   1851  CG  ARG A 461      52.827  27.571  22.794  1.00 39.88           C  
ATOM   1852  CD  ARG A 461      53.574  28.850  23.081  1.00 41.90           C  
ATOM   1853  NE  ARG A 461      54.436  29.230  21.965  1.00 45.65           N  
ATOM   1854  CZ  ARG A 461      55.754  29.059  21.945  1.00 46.95           C  
ATOM   1855  NH1 ARG A 461      56.458  29.435  20.886  1.00 48.21           N  
ATOM   1856  NH2 ARG A 461      56.369  28.513  22.984  1.00 49.27           N  
ATOM   1857  N   PRO A 462      52.123  24.601  21.126  1.00 42.97           N  
ATOM   1858  CA  PRO A 462      52.507  24.224  19.765  1.00 44.17           C  
ATOM   1859  C   PRO A 462      53.493  25.231  19.185  1.00 46.79           C  
ATOM   1860  O   PRO A 462      53.470  26.411  19.542  1.00 47.92           O  
ATOM   1861  CB  PRO A 462      51.180  24.214  19.007  1.00 43.23           C  
ATOM   1862  CG  PRO A 462      50.147  24.010  20.065  1.00 42.39           C  
ATOM   1863  CD  PRO A 462      50.665  24.742  21.266  1.00 42.35           C  
ATOM   1864  N   ASP A 463      54.361  24.767  18.296  1.00 48.96           N  
ATOM   1865  CA  ASP A 463      55.351  25.648  17.704  1.00 52.38           C  
ATOM   1866  C   ASP A 463      54.663  26.795  16.994  1.00 53.73           C  
ATOM   1867  O   ASP A 463      53.610  26.625  16.381  1.00 53.65           O  
ATOM   1868  CB  ASP A 463      56.235  24.882  16.715  1.00 54.44           C  
ATOM   1869  CG  ASP A 463      57.304  24.050  17.406  1.00 56.77           C  
ATOM   1870  OD1 ASP A 463      57.276  23.952  18.653  1.00 59.20           O  
ATOM   1871  OD2 ASP A 463      58.175  23.495  16.701  1.00 56.80           O  
ATOM   1872  N   ASN A 464      55.263  27.975  17.100  1.00 57.68           N  
ATOM   1873  CA  ASN A 464      54.794  29.154  16.381  1.00 60.93           C  
ATOM   1874  C   ASN A 464      53.492  29.711  16.948  1.00 59.90           C  
ATOM   1875  O   ASN A 464      53.202  30.893  16.754  1.00 61.11           O  
ATOM   1876  CB  ASN A 464      54.624  28.828  14.892  1.00 65.74           C  
ATOM   1877  CG  ASN A 464      55.939  28.451  14.225  1.00 69.99           C  
ATOM   1878  OD1 ASN A 464      56.993  28.999  14.554  1.00 72.22           O  
ATOM   1879  ND2 ASN A 464      55.882  27.510  13.285  1.00 71.81           N  
ATOM   1880  N   CYS A 465      52.720  28.870  17.636  1.00 56.89           N  
ATOM   1881  CA  CYS A 465      51.537  29.329  18.358  1.00 52.31           C  
ATOM   1882  C   CYS A 465      51.914  30.410  19.368  1.00 50.40           C  
ATOM   1883  O   CYS A 465      52.744  30.194  20.250  1.00 49.65           O  
ATOM   1884  CB  CYS A 465      50.878  28.166  19.095  1.00 51.54           C  
ATOM   1885  SG  CYS A 465      49.753  28.694  20.413  1.00 51.11           S  
ATOM   1886  N   PRO A 466      51.295  31.593  19.252  1.00 48.34           N  
ATOM   1887  CA  PRO A 466      51.586  32.752  20.104  1.00 46.82           C  
ATOM   1888  C   PRO A 466      51.361  32.459  21.584  1.00 46.11           C  
ATOM   1889  O   PRO A 466      50.305  31.962  21.974  1.00 47.55           O  
ATOM   1890  CB  PRO A 466      50.630  33.825  19.587  1.00 46.89           C  
ATOM   1891  CG  PRO A 466      50.323  33.408  18.190  1.00 47.46           C  
ATOM   1892  CD  PRO A 466      50.295  31.914  18.221  1.00 48.05           C  
ATOM   1893  N   GLU A 467      52.356  32.781  22.404  1.00 43.56           N  
ATOM   1894  CA  GLU A 467      52.298  32.494  23.831  1.00 42.06           C  
ATOM   1895  C   GLU A 467      50.987  32.971  24.453  1.00 41.71           C  
ATOM   1896  O   GLU A 467      50.484  32.369  25.407  1.00 39.96           O  
ATOM   1897  CB  GLU A 467      53.481  33.154  24.546  1.00 39.28           C  
ATOM   1898  CG  GLU A 467      53.366  33.066  26.061  1.00 38.52           C  
ATOM   1899  CD  GLU A 467      53.654  31.667  26.578  1.00 40.12           C  
ATOM   1900  OE1 GLU A 467      54.095  30.808  25.782  1.00 39.80           O  
ATOM   1901  OE2 GLU A 467      53.442  31.428  27.786  1.00 41.87           O  
ATOM   1902  N   GLU A 468      50.437  34.051  23.905  1.00 41.80           N  
ATOM   1903  CA  GLU A 468      49.198  34.632  24.417  1.00 43.43           C  
ATOM   1904  C   GLU A 468      48.033  33.694  24.150  1.00 40.18           C  
ATOM   1905  O   GLU A 468      47.191  33.456  25.012  1.00 39.99           O  
ATOM   1906  CB  GLU A 468      48.917  35.984  23.752  1.00 48.33           C  
ATOM   1907  CG  GLU A 468      50.057  36.974  23.918  1.00 55.84           C  
ATOM   1908  CD  GLU A 468      51.211  36.557  23.019  1.00 60.97           C  
ATOM   1909  OE1 GLU A 468      52.379  36.791  23.401  1.00 64.72           O  
ATOM   1910  OE2 GLU A 468      50.950  35.995  21.933  1.00 62.74           O  
ATOM   1911  N   LEU A 469      47.993  33.157  22.938  1.00 37.30           N  
ATOM   1912  CA  LEU A 469      46.960  32.207  22.569  1.00 36.02           C  
ATOM   1913  C   LEU A 469      47.077  30.953  23.425  1.00 36.15           C  
ATOM   1914  O   LEU A 469      46.079  30.415  23.901  1.00 37.60           O  
ATOM   1915  CB  LEU A 469      47.090  31.848  21.091  1.00 34.55           C  
ATOM   1916  CG  LEU A 469      46.005  30.841  20.720  1.00 34.38           C  
ATOM   1917  CD1 LEU A 469      44.635  31.422  21.034  1.00 33.90           C  
ATOM   1918  CD2 LEU A 469      46.128  30.490  19.244  1.00 34.12           C  
ATOM   1919  N   TYR A 470      48.308  30.494  23.626  1.00 35.45           N  
ATOM   1920  CA  TYR A 470      48.566  29.336  24.473  1.00 35.81           C  
ATOM   1921  C   TYR A 470      48.022  29.578  25.878  1.00 37.23           C  
ATOM   1922  O   TYR A 470      47.396  28.724  26.507  1.00 37.95           O  
ATOM   1923  CB  TYR A 470      50.072  29.065  24.546  1.00 35.11           C  
ATOM   1924  CG  TYR A 470      50.435  27.896  25.432  1.00 35.34           C  
ATOM   1925  CD1 TYR A 470      49.987  26.611  25.134  1.00 36.21           C  
ATOM   1926  CD2 TYR A 470      51.215  28.072  26.571  1.00 34.76           C  
ATOM   1927  CE1 TYR A 470      50.304  25.532  25.947  1.00 35.97           C  
ATOM   1928  CE2 TYR A 470      51.540  26.998  27.391  1.00 35.46           C  
ATOM   1929  CZ  TYR A 470      51.079  25.728  27.073  1.00 36.61           C  
ATOM   1930  OH  TYR A 470      51.388  24.649  27.876  1.00 35.49           O  
ATOM   1931  N   GLN A 471      48.274  30.780  26.375  1.00 38.18           N  
ATOM   1932  CA  GLN A 471      47.850  31.154  27.712  1.00 39.51           C  
ATOM   1933  C   GLN A 471      46.324  31.132  27.777  1.00 40.71           C  
ATOM   1934  O   GLN A 471      45.718  30.840  28.810  1.00 40.08           O  
ATOM   1935  CB  GLN A 471      48.381  32.549  28.039  1.00 40.59           C  
ATOM   1936  CG  GLN A 471      48.955  32.648  29.435  1.00 43.85           C  
ATOM   1937  CD  GLN A 471      49.855  31.466  29.723  1.00 46.26           C  
ATOM   1938  OE1 GLN A 471      50.830  31.216  29.012  1.00 47.79           O  
ATOM   1939  NE2 GLN A 471      49.529  30.728  30.775  1.00 48.65           N  
ATOM   1940  N   LEU A 472      45.703  31.445  26.644  1.00 42.13           N  
ATOM   1941  CA  LEU A 472      44.254  31.384  26.516  1.00 41.03           C  
ATOM   1942  C   LEU A 472      43.831  29.921  26.630  1.00 40.78           C  
ATOM   1943  O   LEU A 472      42.833  29.589  27.273  1.00 41.20           O  
ATOM   1944  CB  LEU A 472      43.820  31.941  25.156  1.00 42.21           C  
ATOM   1945  CG  LEU A 472      42.486  32.696  25.056  1.00 45.94           C  
ATOM   1946  CD1 LEU A 472      41.839  32.401  23.711  1.00 42.95           C  
ATOM   1947  CD2 LEU A 472      41.555  32.287  26.187  1.00 45.64           C  
ATOM   1948  N   MET A 473      44.610  29.045  25.998  1.00 38.55           N  
ATOM   1949  CA  MET A 473      44.367  27.611  26.074  1.00 37.09           C  
ATOM   1950  C   MET A 473      44.467  27.150  27.513  1.00 37.08           C  
ATOM   1951  O   MET A 473      43.662  26.352  27.989  1.00 37.12           O  
ATOM   1952  CB  MET A 473      45.398  26.850  25.249  1.00 37.97           C  
ATOM   1953  CG  MET A 473      45.381  27.232  23.796  1.00 39.85           C  
ATOM   1954  SD  MET A 473      46.720  26.421  22.925  1.00 42.68           S  
ATOM   1955  CE  MET A 473      46.299  26.825  21.210  1.00 41.86           C  
ATOM   1956  N   ARG A 474      45.478  27.660  28.208  1.00 37.15           N  
ATOM   1957  CA  ARG A 474      45.719  27.274  29.587  1.00 36.42           C  
ATOM   1958  C   ARG A 474      44.546  27.676  30.472  1.00 37.70           C  
ATOM   1959  O   ARG A 474      44.295  27.030  31.488  1.00 39.37           O  
ATOM   1960  CB  ARG A 474      47.015  27.912  30.088  1.00 34.74           C  
ATOM   1961  CG  ARG A 474      48.226  27.401  29.321  1.00 34.91           C  
ATOM   1962  CD  ARG A 474      48.389  25.888  29.459  1.00 35.47           C  
ATOM   1963  NE  ARG A 474      48.544  25.485  30.857  1.00 35.48           N  
ATOM   1964  CZ  ARG A 474      49.652  24.957  31.372  1.00 33.90           C  
ATOM   1965  NH1 ARG A 474      50.716  24.755  30.607  1.00 32.94           N  
ATOM   1966  NH2 ARG A 474      49.700  24.646  32.661  1.00 31.11           N  
ATOM   1967  N   LEU A 475      43.826  28.726  30.084  1.00 38.47           N  
ATOM   1968  CA  LEU A 475      42.593  29.096  30.775  1.00 38.48           C  
ATOM   1969  C   LEU A 475      41.495  28.067  30.528  1.00 39.47           C  
ATOM   1970  O   LEU A 475      40.679  27.800  31.413  1.00 39.35           O  
ATOM   1971  CB  LEU A 475      42.106  30.477  30.323  1.00 38.43           C  
ATOM   1972  CG  LEU A 475      43.024  31.619  30.775  1.00 39.40           C  
ATOM   1973  CD1 LEU A 475      42.315  32.949  30.600  1.00 37.20           C  
ATOM   1974  CD2 LEU A 475      43.403  31.426  32.230  1.00 38.65           C  
ATOM   1975  N   CYS A 476      41.475  27.488  29.330  1.00 39.10           N  
ATOM   1976  CA  CYS A 476      40.484  26.470  29.002  1.00 40.46           C  
ATOM   1977  C   CYS A 476      40.769  25.167  29.738  1.00 41.14           C  
ATOM   1978  O   CYS A 476      39.903  24.297  29.846  1.00 40.94           O  
ATOM   1979  CB  CYS A 476      40.462  26.205  27.494  1.00 41.32           C  
ATOM   1980  SG  CYS A 476      39.940  27.613  26.483  1.00 46.15           S  
ATOM   1981  N   TRP A 477      41.992  25.033  30.242  1.00 42.30           N  
ATOM   1982  CA  TRP A 477      42.409  23.800  30.896  1.00 43.94           C  
ATOM   1983  C   TRP A 477      42.638  23.977  32.390  1.00 46.79           C  
ATOM   1984  O   TRP A 477      43.424  23.239  32.982  1.00 47.76           O  
ATOM   1985  CB  TRP A 477      43.685  23.262  30.250  1.00 41.98           C  
ATOM   1986  CG  TRP A 477      43.559  23.043  28.777  1.00 41.19           C  
ATOM   1987  CD1 TRP A 477      42.427  22.721  28.090  1.00 40.44           C  
ATOM   1988  CD2 TRP A 477      44.609  23.130  27.806  1.00 41.23           C  
ATOM   1989  NE1 TRP A 477      42.704  22.601  26.750  1.00 40.33           N  
ATOM   1990  CE2 TRP A 477      44.036  22.846  26.548  1.00 40.05           C  
ATOM   1991  CE3 TRP A 477      45.977  23.420  27.878  1.00 40.66           C  
ATOM   1992  CZ2 TRP A 477      44.782  22.843  25.372  1.00 40.09           C  
ATOM   1993  CZ3 TRP A 477      46.716  23.417  26.709  1.00 41.32           C  
ATOM   1994  CH2 TRP A 477      46.116  23.130  25.471  1.00 41.43           C  
ATOM   1995  N   LYS A 478      41.960  24.950  32.994  1.00 50.19           N  
ATOM   1996  CA  LYS A 478      41.927  25.058  34.449  1.00 53.23           C  
ATOM   1997  C   LYS A 478      41.351  23.766  35.013  1.00 54.97           C  
ATOM   1998  O   LYS A 478      40.418  23.196  34.443  1.00 55.54           O  
ATOM   1999  CB  LYS A 478      41.047  26.232  34.883  1.00 54.96           C  
ATOM   2000  CG  LYS A 478      41.639  27.590  34.539  1.00 58.05           C  
ATOM   2001  CD  LYS A 478      42.737  28.064  35.478  1.00 59.75           C  
ATOM   2002  CE  LYS A 478      42.942  29.571  35.393  1.00 60.99           C  
ATOM   2003  NZ  LYS A 478      41.668  30.325  35.604  1.00 61.63           N  
ATOM   2004  N   GLU A 479      41.904  23.307  36.131  1.00 56.04           N  
ATOM   2005  CA  GLU A 479      41.503  22.028  36.698  1.00 55.95           C  
ATOM   2006  C   GLU A 479      40.037  22.042  37.116  1.00 55.61           C  
ATOM   2007  O   GLU A 479      39.309  21.080  36.879  1.00 55.05           O  
ATOM   2008  CB  GLU A 479      42.384  21.687  37.902  1.00 58.14           C  
ATOM   2009  CG  GLU A 479      42.090  20.304  38.471  1.00 58.38           C  
ATOM   2010  CD  GLU A 479      42.279  19.204  37.439  1.00 60.27           C  
ATOM   2011  OE1 GLU A 479      41.615  18.153  37.566  1.00 62.26           O  
ATOM   2012  OE2 GLU A 479      43.088  19.385  36.502  1.00 61.27           O  
ATOM   2013  N   ARG A 480      39.606  23.135  37.736  1.00 56.49           N  
ATOM   2014  CA  ARG A 480      38.221  23.260  38.170  1.00 57.31           C  
ATOM   2015  C   ARG A 480      37.397  23.952  37.096  1.00 56.46           C  
ATOM   2016  O   ARG A 480      37.708  25.063  36.665  1.00 55.90           O  
ATOM   2017  CB  ARG A 480      38.135  24.052  39.478  1.00 61.22           C  
ATOM   2018  CG  ARG A 480      38.802  23.341  40.649  1.00 66.13           C  
ATOM   2019  CD  ARG A 480      38.173  23.658  42.007  1.00 73.09           C  
ATOM   2020  NE  ARG A 480      37.828  25.074  42.145  1.00 77.34           N  
ATOM   2021  CZ  ARG A 480      37.793  25.731  43.301  1.00 78.68           C  
ATOM   2022  NH1 ARG A 480      38.084  25.103  44.435  1.00 78.59           N  
ATOM   2023  NH2 ARG A 480      37.464  27.018  43.323  1.00 78.83           N  
ATOM   2024  N   PRO A 481      36.313  23.298  36.658  1.00 55.77           N  
ATOM   2025  CA  PRO A 481      35.534  23.723  35.491  1.00 55.58           C  
ATOM   2026  C   PRO A 481      35.024  25.156  35.604  1.00 55.91           C  
ATOM   2027  O   PRO A 481      34.888  25.855  34.602  1.00 56.11           O  
ATOM   2028  CB  PRO A 481      34.392  22.708  35.433  1.00 54.58           C  
ATOM   2029  CG  PRO A 481      34.918  21.513  36.155  1.00 54.26           C  
ATOM   2030  CD  PRO A 481      35.777  22.062  37.252  1.00 54.60           C  
ATOM   2031  N   GLU A 482      34.748  25.590  36.828  1.00 57.34           N  
ATOM   2032  CA  GLU A 482      34.192  26.919  37.053  1.00 58.13           C  
ATOM   2033  C   GLU A 482      35.247  28.007  36.861  1.00 57.09           C  
ATOM   2034  O   GLU A 482      34.927  29.174  36.639  1.00 57.06           O  
ATOM   2035  CB  GLU A 482      33.582  27.010  38.461  1.00 58.79           C  
ATOM   2036  CG  GLU A 482      34.587  26.748  39.576  1.00 62.39           C  
ATOM   2037  CD  GLU A 482      34.514  25.337  40.138  1.00 64.98           C  
ATOM   2038  OE1 GLU A 482      35.083  25.104  41.226  1.00 64.82           O  
ATOM   2039  OE2 GLU A 482      33.891  24.462  39.494  1.00 66.38           O  
ATOM   2040  N   ASP A 483      36.515  27.616  36.939  1.00 56.03           N  
ATOM   2041  CA  ASP A 483      37.608  28.561  36.755  1.00 55.46           C  
ATOM   2042  C   ASP A 483      37.895  28.821  35.280  1.00 53.54           C  
ATOM   2043  O   ASP A 483      38.672  29.714  34.934  1.00 55.21           O  
ATOM   2044  CB  ASP A 483      38.871  28.042  37.443  1.00 58.74           C  
ATOM   2045  CG  ASP A 483      38.749  28.035  38.955  1.00 62.35           C  
ATOM   2046  OD1 ASP A 483      38.047  28.913  39.502  1.00 63.23           O  
ATOM   2047  OD2 ASP A 483      39.356  27.151  39.596  1.00 65.68           O  
ATOM   2048  N   ARG A 484      37.265  28.036  34.411  1.00 50.01           N  
ATOM   2049  CA  ARG A 484      37.448  28.178  32.970  1.00 45.60           C  
ATOM   2050  C   ARG A 484      36.573  29.297  32.416  1.00 43.70           C  
ATOM   2051  O   ARG A 484      35.466  29.550  32.892  1.00 43.39           O  
ATOM   2052  CB  ARG A 484      37.102  26.864  32.267  1.00 44.00           C  
ATOM   2053  CG  ARG A 484      37.807  25.689  32.898  1.00 41.36           C  
ATOM   2054  CD  ARG A 484      37.784  24.425  32.069  1.00 39.67           C  
ATOM   2055  NE  ARG A 484      38.272  23.288  32.841  1.00 39.28           N  
ATOM   2056  CZ  ARG A 484      37.583  22.170  33.034  1.00 39.26           C  
ATOM   2057  NH1 ARG A 484      36.371  22.033  32.508  1.00 39.52           N  
ATOM   2058  NH2 ARG A 484      38.102  21.193  33.760  1.00 38.17           N  
ATOM   2059  N   PRO A 485      37.063  29.985  31.379  1.00 42.23           N  
ATOM   2060  CA  PRO A 485      36.334  31.112  30.793  1.00 41.79           C  
ATOM   2061  C   PRO A 485      34.951  30.702  30.294  1.00 42.56           C  
ATOM   2062  O   PRO A 485      34.575  29.528  30.358  1.00 42.34           O  
ATOM   2063  CB  PRO A 485      37.237  31.567  29.648  1.00 41.15           C  
ATOM   2064  CG  PRO A 485      38.594  31.064  30.014  1.00 42.07           C  
ATOM   2065  CD  PRO A 485      38.356  29.761  30.715  1.00 41.77           C  
ATOM   2066  N   THR A 486      34.191  31.675  29.805  1.00 42.77           N  
ATOM   2067  CA  THR A 486      32.967  31.376  29.073  1.00 44.57           C  
ATOM   2068  C   THR A 486      33.245  31.559  27.587  1.00 44.93           C  
ATOM   2069  O   THR A 486      34.219  32.218  27.216  1.00 45.90           O  
ATOM   2070  CB  THR A 486      31.819  32.323  29.461  1.00 44.00           C  
ATOM   2071  OG1 THR A 486      32.101  33.644  28.980  1.00 42.05           O  
ATOM   2072  CG2 THR A 486      31.659  32.359  30.969  1.00 43.41           C  
ATOM   2073  N   PHE A 487      32.398  30.981  26.743  1.00 43.49           N  
ATOM   2074  CA  PHE A 487      32.590  31.096  25.307  1.00 42.77           C  
ATOM   2075  C   PHE A 487      32.449  32.533  24.833  1.00 43.10           C  
ATOM   2076  O   PHE A 487      33.000  32.908  23.801  1.00 43.11           O  
ATOM   2077  CB  PHE A 487      31.609  30.185  24.566  1.00 40.58           C  
ATOM   2078  CG  PHE A 487      32.014  28.736  24.577  1.00 39.95           C  
ATOM   2079  CD1 PHE A 487      33.201  28.330  23.978  1.00 40.08           C  
ATOM   2080  CD2 PHE A 487      31.227  27.785  25.203  1.00 39.33           C  
ATOM   2081  CE1 PHE A 487      33.594  27.007  24.004  1.00 39.15           C  
ATOM   2082  CE2 PHE A 487      31.613  26.458  25.235  1.00 39.27           C  
ATOM   2083  CZ  PHE A 487      32.801  26.068  24.634  1.00 41.32           C  
ATOM   2084  N   ASP A 488      31.725  33.345  25.593  1.00 45.04           N  
ATOM   2085  CA  ASP A 488      31.629  34.767  25.287  1.00 47.16           C  
ATOM   2086  C   ASP A 488      32.982  35.442  25.445  1.00 46.88           C  
ATOM   2087  O   ASP A 488      33.446  36.182  24.576  1.00 46.29           O  
ATOM   2088  CB  ASP A 488      30.625  35.440  26.214  1.00 50.71           C  
ATOM   2089  CG  ASP A 488      29.423  35.962  25.473  1.00 56.51           C  
ATOM   2090  OD1 ASP A 488      29.566  36.270  24.267  1.00 58.69           O  
ATOM   2091  OD2 ASP A 488      28.339  36.062  26.095  1.00 60.78           O  
ATOM   2092  N   TYR A 489      33.615  35.176  26.582  1.00 46.60           N  
ATOM   2093  CA  TYR A 489      34.941  35.696  26.864  1.00 45.91           C  
ATOM   2094  C   TYR A 489      35.918  35.163  25.826  1.00 45.63           C  
ATOM   2095  O   TYR A 489      36.704  35.913  25.252  1.00 46.37           O  
ATOM   2096  CB  TYR A 489      35.376  35.269  28.265  1.00 46.53           C  
ATOM   2097  CG  TYR A 489      36.790  35.657  28.611  1.00 49.68           C  
ATOM   2098  CD1 TYR A 489      37.084  36.924  29.090  1.00 49.91           C  
ATOM   2099  CD2 TYR A 489      37.833  34.750  28.472  1.00 51.14           C  
ATOM   2100  CE1 TYR A 489      38.377  37.279  29.423  1.00 51.32           C  
ATOM   2101  CE2 TYR A 489      39.130  35.095  28.803  1.00 51.46           C  
ATOM   2102  CZ  TYR A 489      39.396  36.362  29.278  1.00 51.77           C  
ATOM   2103  OH  TYR A 489      40.684  36.717  29.606  1.00 51.93           O  
ATOM   2104  N   LEU A 490      35.855  33.859  25.579  1.00 45.22           N  
ATOM   2105  CA  LEU A 490      36.672  33.247  24.539  1.00 44.27           C  
ATOM   2106  C   LEU A 490      36.464  33.963  23.210  1.00 45.34           C  
ATOM   2107  O   LEU A 490      37.425  34.398  22.578  1.00 45.76           O  
ATOM   2108  CB  LEU A 490      36.313  31.771  24.384  1.00 41.24           C  
ATOM   2109  CG  LEU A 490      36.845  30.985  25.579  1.00 40.22           C  
ATOM   2110  CD1 LEU A 490      36.392  29.535  25.485  1.00 37.04           C  
ATOM   2111  CD2 LEU A 490      38.362  31.087  25.611  1.00 38.11           C  
ATOM   2112  N   ARG A 491      35.209  34.090  22.790  1.00 45.80           N  
ATOM   2113  CA  ARG A 491      34.911  34.761  21.536  1.00 46.28           C  
ATOM   2114  C   ARG A 491      35.562  36.132  21.533  1.00 46.46           C  
ATOM   2115  O   ARG A 491      36.244  36.519  20.587  1.00 47.53           O  
ATOM   2116  CB  ARG A 491      33.402  34.924  21.350  1.00 47.17           C  
ATOM   2117  CG  ARG A 491      33.085  35.688  20.075  1.00 48.45           C  
ATOM   2118  CD  ARG A 491      31.680  36.182  19.800  1.00 51.90           C  
ATOM   2119  NE  ARG A 491      31.597  36.821  18.488  1.00 58.07           N  
ATOM   2120  CZ  ARG A 491      30.571  37.556  18.066  1.00 60.47           C  
ATOM   2121  NH1 ARG A 491      29.519  37.759  18.851  1.00 62.97           N  
ATOM   2122  NH2 ARG A 491      30.597  38.094  16.852  1.00 60.86           N  
ATOM   2123  N   SER A 492      35.353  36.866  22.618  1.00 47.32           N  
ATOM   2124  CA  SER A 492      35.822  38.239  22.699  1.00 48.74           C  
ATOM   2125  C   SER A 492      37.340  38.315  22.534  1.00 47.40           C  
ATOM   2126  O   SER A 492      37.842  38.957  21.610  1.00 46.92           O  
ATOM   2127  CB  SER A 492      35.407  38.849  24.039  1.00 50.56           C  
ATOM   2128  OG  SER A 492      35.728  40.230  24.092  1.00 55.73           O  
ATOM   2129  N   VAL A 493      38.064  37.647  23.426  1.00 45.92           N  
ATOM   2130  CA  VAL A 493      39.523  37.626  23.377  1.00 45.79           C  
ATOM   2131  C   VAL A 493      40.034  37.267  21.984  1.00 47.70           C  
ATOM   2132  O   VAL A 493      40.997  37.849  21.478  1.00 48.51           O  
ATOM   2133  CB  VAL A 493      40.104  36.591  24.362  1.00 44.07           C  
ATOM   2134  CG1 VAL A 493      41.614  36.582  24.268  1.00 43.07           C  
ATOM   2135  CG2 VAL A 493      39.660  36.910  25.779  1.00 42.51           C  
ATOM   2136  N   LEU A 494      39.379  36.296  21.360  1.00 48.85           N  
ATOM   2137  CA  LEU A 494      39.812  35.819  20.059  1.00 51.28           C  
ATOM   2138  C   LEU A 494      39.648  36.908  19.015  1.00 53.72           C  
ATOM   2139  O   LEU A 494      40.555  37.133  18.213  1.00 53.75           O  
ATOM   2140  CB  LEU A 494      39.017  34.575  19.654  1.00 50.05           C  
ATOM   2141  CG  LEU A 494      39.569  33.369  20.423  1.00 49.03           C  
ATOM   2142  CD1 LEU A 494      38.774  32.112  20.087  1.00 48.14           C  
ATOM   2143  CD2 LEU A 494      41.038  33.185  20.070  1.00 48.38           C  
ATOM   2144  N   GLU A 495      38.505  37.590  19.043  1.00 57.07           N  
ATOM   2145  CA  GLU A 495      38.174  38.589  18.030  1.00 61.58           C  
ATOM   2146  C   GLU A 495      39.166  39.750  17.984  1.00 64.10           C  
ATOM   2147  O   GLU A 495      39.763  40.037  16.942  1.00 64.84           O  
ATOM   2148  CB  GLU A 495      36.766  39.134  18.270  1.00 62.86           C  
ATOM   2149  CG  GLU A 495      35.697  38.100  17.986  1.00 67.51           C  
ATOM   2150  CD  GLU A 495      34.319  38.704  18.176  1.00 70.68           C  
ATOM   2151  OE1 GLU A 495      34.139  39.497  19.127  1.00 71.17           O  
ATOM   2152  OE2 GLU A 495      33.418  38.382  17.371  1.00 73.36           O  
ATOM   2153  N   ASP A 496      39.341  40.432  19.107  1.00 66.17           N  
ATOM   2154  CA  ASP A 496      40.354  41.469  19.162  1.00 69.78           C  
ATOM   2155  C   ASP A 496      41.634  40.891  19.738  1.00 70.34           C  
ATOM   2156  O   ASP A 496      42.077  41.245  20.827  1.00 71.67           O  
ATOM   2157  CB  ASP A 496      39.872  42.672  19.990  1.00 72.17           C  
ATOM   2158  CG  ASP A 496      39.407  42.289  21.385  1.00 74.67           C  
ATOM   2159  OD1 ASP A 496      40.064  42.703  22.367  1.00 75.56           O  
ATOM   2160  OD2 ASP A 496      38.380  41.585  21.503  1.00 76.29           O  
ATOM   2161  N   PHE A 497      42.228  39.973  18.984  1.00 71.23           N  
ATOM   2162  CA  PHE A 497      43.495  39.379  19.376  1.00 72.17           C  
ATOM   2163  C   PHE A 497      44.657  40.109  18.713  1.00 73.45           C  
ATOM   2164  O   PHE A 497      45.712  40.289  19.322  1.00 74.14           O  
ATOM   2165  CB  PHE A 497      43.533  37.899  18.999  1.00 70.56           C  
ATOM   2166  CG  PHE A 497      44.728  37.174  19.544  1.00 71.04           C  
ATOM   2167  CD1 PHE A 497      45.933  37.182  18.860  1.00 71.76           C  
ATOM   2168  CD2 PHE A 497      44.651  36.493  20.748  1.00 71.66           C  
ATOM   2169  CE1 PHE A 497      47.042  36.527  19.368  1.00 72.54           C  
ATOM   2170  CE2 PHE A 497      45.754  35.836  21.262  1.00 72.23           C  
ATOM   2171  CZ  PHE A 497      46.953  35.852  20.569  1.00 72.74           C  
ATOM   2172  N   PHE A 498      44.462  40.527  17.466  1.00 74.89           N  
ATOM   2173  CA  PHE A 498      45.460  41.329  16.763  1.00 76.12           C  
ATOM   2174  C   PHE A 498      45.056  42.801  16.721  1.00 76.57           C  
ATOM   2175  O   PHE A 498      45.764  43.623  17.342  1.00 76.92           O  
ATOM   2176  CB  PHE A 498      45.650  40.808  15.336  1.00 77.15           C  
ATOM   2177  CG  PHE A 498      46.175  39.403  15.269  1.00 78.84           C  
ATOM   2178  CD1 PHE A 498      47.495  39.127  15.592  1.00 79.25           C  
ATOM   2179  CD2 PHE A 498      45.350  38.357  14.887  1.00 79.54           C  
ATOM   2180  CE1 PHE A 498      47.984  37.833  15.535  1.00 79.45           C  
ATOM   2181  CE2 PHE A 498      45.831  37.059  14.827  1.00 78.98           C  
ATOM   2182  CZ  PHE A 498      47.150  36.798  15.152  1.00 79.19           C  
TER    2183      PHE A 498                                                      
HETATM 2184  C1  STI A 200      29.553  18.318   4.059  1.00 39.54           C  
HETATM 2185  C6  STI A 200      28.670  17.770   5.005  1.00 38.55           C  
HETATM 2186  C5  STI A 200      29.087  16.642   5.780  1.00 41.65           C  
HETATM 2187  C4  STI A 200      30.395  16.120   5.555  1.00 42.52           C  
HETATM 2188  N3  STI A 200      31.199  16.685   4.636  1.00 41.88           N  
HETATM 2189  C2  STI A 200      30.825  17.746   3.898  1.00 41.68           C  
HETATM 2190  C7  STI A 200      28.159  16.047   6.796  1.00 39.49           C  
HETATM 2191  C12 STI A 200      28.395  14.767   7.377  1.00 39.30           C  
HETATM 2192  C11 STI A 200      27.462  14.300   8.322  1.00 39.92           C  
HETATM 2193  N10 STI A 200      26.397  15.063   8.644  1.00 39.54           N  
HETATM 2194  C9  STI A 200      26.206  16.269   8.072  1.00 38.05           C  
HETATM 2195  N8  STI A 200      27.067  16.745   7.175  1.00 39.71           N  
HETATM 2196  N13 STI A 200      25.103  17.050   8.397  1.00 34.55           N  
HETATM 2197  C14 STI A 200      24.130  16.666   9.336  1.00 35.34           C  
HETATM 2198  C19 STI A 200      23.111  15.705   9.018  1.00 34.81           C  
HETATM 2199  C18 STI A 200      22.155  15.359   9.992  1.00 35.98           C  
HETATM 2200  C17 STI A 200      22.193  15.950  11.273  1.00 38.19           C  
HETATM 2201  C16 STI A 200      23.195  16.904  11.602  1.00 37.61           C  
HETATM 2202  C15 STI A 200      24.162  17.254  10.620  1.00 36.09           C  
HETATM 2203  N21 STI A 200      23.175  17.489  12.910  1.00 38.80           N  
HETATM 2204  C22 STI A 200      24.168  18.231  13.510  1.00 37.44           C  
HETATM 2205  C23 STI A 200      23.936  18.771  14.879  1.00 38.17           C  
HETATM 2206  C25 STI A 200      23.074  18.089  15.790  1.00 39.45           C  
HETATM 2207  C26 STI A 200      22.858  18.609  17.085  1.00 40.72           C  
HETATM 2208  C27 STI A 200      23.498  19.808  17.486  1.00 42.23           C  
HETATM 2209  C28 STI A 200      24.353  20.490  16.585  1.00 41.57           C  
HETATM 2210  C29 STI A 200      24.575  19.981  15.293  1.00 39.77           C  
HETATM 2211  C46 STI A 200      23.276  20.377  18.880  1.00 41.69           C  
HETATM 2212  N48 STI A 200      23.491  19.356  19.929  1.00 42.82           N  
HETATM 2213  C53 STI A 200      24.935  19.094  20.182  1.00 43.57           C  
HETATM 2214  C52 STI A 200      25.066  17.933  21.192  1.00 42.97           C  
HETATM 2215  N51 STI A 200      24.333  18.269  22.441  1.00 42.15           N  
HETATM 2216  C54 STI A 200      24.467  17.193  23.434  1.00 41.96           C  
HETATM 2217  C50 STI A 200      22.900  18.590  22.203  1.00 43.35           C  
HETATM 2218  C49 STI A 200      22.787  19.740  21.178  1.00 44.36           C  
HETATM 2219  O29 STI A 200      25.228  18.467  12.947  1.00 36.93           O  
HETATM 2220  C20 STI A 200      23.036  15.057   7.652  1.00 34.71           C  
HETATM 2221  O   HOH A   1      24.112  12.118  17.261  1.00 37.50           O  
HETATM 2222  O   HOH A   2      32.272  19.344  33.498  1.00 49.84           O  
HETATM 2223  O   HOH A   3      39.134  16.335  15.614  1.00 23.71           O  
HETATM 2224  O   HOH A   4      16.165  24.842  22.091  1.00 29.49           O  
HETATM 2225  O   HOH A   5      42.478  16.988  26.683  1.00 28.23           O  
HETATM 2226  O   HOH A   6      26.563  23.407  31.368  1.00 30.24           O  
HETATM 2227  O   HOH A   7      46.865  35.285  27.226  1.00 48.70           O  
HETATM 2228  O   HOH A   8      26.418  33.083  25.949  1.00 39.14           O  
HETATM 2229  O   HOH A   9      46.461  19.921  27.511  1.00 33.47           O  
HETATM 2230  O   HOH A  10      52.117  17.184  24.462  1.00 35.99           O  
HETATM 2231  O   HOH A  11      19.747  32.913  15.794  1.00 45.55           O  
HETATM 2232  O   HOH A  12      33.185  36.065  14.891  1.00 42.21           O  
HETATM 2233  O   HOH A  13      26.661  15.543  32.905  1.00 42.51           O  
HETATM 2234  O   HOH A  14      35.383  17.566  27.378  1.00 35.80           O  
HETATM 2235  O   HOH A  15      23.081  33.927  13.834  1.00 52.16           O  
HETATM 2236  O   HOH A  16      46.809  19.618  18.409  1.00 42.68           O  
HETATM 2237  O   HOH A  18      35.038  34.020  31.643  1.00 42.35           O  
HETATM 2238  O   HOH A  19      45.916  24.896  31.994  1.00 33.60           O  
HETATM 2239  O   HOH A  20      36.036 -10.373  14.339  1.00 43.69           O  
HETATM 2240  O   HOH A  21      49.985  18.688  18.503  1.00 37.05           O  
HETATM 2241  O   HOH A  23      35.394  33.373   6.890  1.00 46.13           O  
HETATM 2242  O   HOH A  24      52.705  33.798  29.003  1.00 47.64           O  
HETATM 2243  O   HOH A  25      17.489  29.975  16.568  1.00 43.58           O  
HETATM 2244  O   HOH A  26      33.195  18.482  24.294  1.00 33.20           O  
HETATM 2245  O   HOH A  27      42.952  10.380  19.943  1.00 39.14           O  
HETATM 2246  O   HOH A  28      31.429  18.394  27.410  1.00 42.70           O  
HETATM 2247  O   HOH A  29      28.978  32.730  26.902  1.00 41.68           O  
HETATM 2248  O   HOH A  30      22.783  13.808  30.413  1.00 49.99           O  
HETATM 2249  O   HOH A  32      20.776   1.034   6.898  1.00 58.12           O  
HETATM 2250  O   HOH A  33      -0.663  26.602   2.563  1.00 46.74           O  
HETATM 2251  O   HOH A  34      55.127  28.346  25.703  1.00 37.33           O  
HETATM 2252  O   HOH A  35      24.659  13.890  13.242  1.00 29.94           O  
HETATM 2253  O   HOH A  36      41.514  44.083  17.218  1.00 45.16           O  
HETATM 2254  O   HOH A  37      32.068  38.601  21.322  1.00 37.47           O  
HETATM 2255  O   HOH A  38      25.493   9.164  14.482  1.00 54.09           O  
HETATM 2256  O   HOH A  39      44.162  44.809  19.326  1.00 51.08           O  
HETATM 2257  O   HOH A  40      35.251   6.771  25.476  1.00 40.55           O  
HETATM 2258  O   HOH A  41      29.115  35.352  20.827  1.00 51.67           O  
HETATM 2259  O   HOH A  42      45.101  33.423   4.773  1.00 39.38           O  
HETATM 2260  O   HOH A  43      43.318  36.220  28.509  1.00 47.28           O  
HETATM 2261  O   HOH A  44      43.398  16.177  15.248  1.00 38.72           O  
HETATM 2262  O   HOH A  45      30.211  11.403  19.330  1.00 53.08           O  
HETATM 2263  O   HOH A  46      51.609  34.249  31.930  1.00 46.71           O  
HETATM 2264  O   HOH A  47      30.170  13.468  17.673  1.00 42.00           O  
HETATM 2265  O   HOH A  48       9.615  19.124   9.327  1.00 36.68           O  
HETATM 2266  O   HOH A  49      50.023  30.167   9.556  1.00 45.71           O  
HETATM 2267  O   HOH A  50      21.877  26.906  11.529  1.00 48.48           O  
HETATM 2268  O   HOH A  51      45.115  34.184  28.778  1.00 53.43           O  
HETATM 2269  O   HOH A  53      49.151  19.961   1.944  1.00 62.90           O  
HETATM 2270  O   HOH A  54      31.780  35.278   9.030  1.00 44.91           O  
HETATM 2271  O   HOH A  55      42.598  39.740  23.420  1.00 51.03           O  
HETATM 2272  O   HOH A  56      29.593  11.638  26.403  1.00 47.23           O  
HETATM 2273  O   HOH A  58      14.484  25.481   4.752  1.00 51.71           O  
HETATM 2274  O   HOH A  60      42.658  11.953  35.122  1.00 47.11           O  
HETATM 2275  O   HOH A  61      15.389   8.521  -1.703  1.00 61.93           O  
HETATM 2276  O   HOH A  62      22.651  19.600  25.581  1.00 39.48           O  
HETATM 2277  O   HOH A  63      13.098  27.324   7.164  1.00 35.03           O  
HETATM 2278  O   HOH A  65      41.593  24.905  38.497  1.00 59.90           O  
HETATM 2279  O   HOH A  66      27.854   2.747  19.246  1.00 59.71           O  
HETATM 2280  O   HOH A  67      34.183  42.721  24.701  1.00 54.02           O  
HETATM 2281  O   HOH A  68      29.883  30.531   9.804  1.00 34.75           O  
HETATM 2282  O   HOH A  69      41.809  14.746  28.086  1.00 51.60           O  
HETATM 2283  O   HOH A  71      51.486  28.339  15.381  1.00 45.56           O  
HETATM 2284  O   HOH A  72      34.339  15.826  25.588  1.00 42.29           O  
HETATM 2285  O   HOH A  73      37.651  34.288  32.882  1.00 41.61           O  
HETATM 2286  O   HOH A  74      46.668  31.370  31.182  1.00 37.21           O  
HETATM 2287  O   HOH A  75      46.588  24.028  34.270  1.00 37.62           O  
HETATM 2288  O   HOH A  77      38.873  21.308   1.700  1.00 72.50           O  
HETATM 2289  O   HOH A  78      32.396  24.172   1.499  1.00 35.45           O  
HETATM 2290  O   HOH A  79      24.821  25.870  28.856  1.00 37.09           O  
HETATM 2291  O   HOH A  80      46.404  24.708   9.002  1.00 52.06           O  
HETATM 2292  O   HOH A  81      23.610  14.499  17.622  1.00 37.65           O  
HETATM 2293  O   HOH A  82      54.292  25.525  26.512  1.00 43.96           O  
HETATM 2294  O   HOH A  84      46.794  29.234  -2.932  1.00 41.92           O  
HETATM 2295  O   HOH A  85      41.070  10.887  22.050  1.00 40.18           O  
HETATM 2296  O   HOH A  86      25.224  13.581  10.819  1.00 36.63           O  
HETATM 2297  O   HOH A  87      52.103  20.368  32.457  1.00 30.14           O  
HETATM 2298  O   HOH A  88      42.570  39.456  15.847  1.00 51.59           O  
HETATM 2299  O   HOH A  89      14.488  28.802  19.466  1.00 28.58           O  
HETATM 2300  O   HOH A  90      43.624  22.623  -1.165  1.00 43.13           O  
HETATM 2301  O   HOH A  91      42.584  13.070  15.581  1.00 49.48           O  
HETATM 2302  O   HOH A  93      38.144  18.939  36.675  1.00 59.71           O  
HETATM 2303  O   HOH A  94      35.261  15.387  22.733  1.00 62.26           O  
HETATM 2304  O   HOH A  95      11.536  28.130   9.510  1.00 43.20           O  
HETATM 2305  O   HOH A  99      48.234  27.503   8.537  1.00 51.61           O  
HETATM 2306  O   HOH A 100      31.851  13.125  24.392  1.00 48.60           O  
HETATM 2307  O   HOH A 102      19.245  11.535  15.784  1.00 60.85           O  
HETATM 2308  O   HOH A 103      45.808   6.076  22.204  1.00 58.59           O  
HETATM 2309  O   HOH A 104      21.566   7.436  11.529  1.00 63.29           O  
HETATM 2310  O   HOH A 105      53.045  14.408  33.944  1.00 44.67           O  
HETATM 2311  O   HOH A 106      13.815   5.105   9.180  1.00 48.17           O  
HETATM 2312  O   HOH A 107      27.915   2.597  14.456  1.00 76.55           O  
HETATM 2313  O   HOH A 108      24.401  28.115   9.257  1.00 43.77           O  
CONECT 2184 2185 2189                                                           
CONECT 2185 2184 2186                                                           
CONECT 2186 2185 2187 2190                                                      
CONECT 2187 2186 2188                                                           
CONECT 2188 2187 2189                                                           
CONECT 2189 2184 2188                                                           
CONECT 2190 2186 2191 2195                                                      
CONECT 2191 2190 2192                                                           
CONECT 2192 2191 2193                                                           
CONECT 2193 2192 2194                                                           
CONECT 2194 2193 2195 2196                                                      
CONECT 2195 2190 2194                                                           
CONECT 2196 2194 2197                                                           
CONECT 2197 2196 2198 2202                                                      
CONECT 2198 2197 2199 2220                                                      
CONECT 2199 2198 2200                                                           
CONECT 2200 2199 2201                                                           
CONECT 2201 2200 2202 2203                                                      
CONECT 2202 2197 2201                                                           
CONECT 2203 2201 2204                                                           
CONECT 2204 2203 2205 2219                                                      
CONECT 2205 2204 2206 2210                                                      
CONECT 2206 2205 2207                                                           
CONECT 2207 2206 2208                                                           
CONECT 2208 2207 2209 2211                                                      
CONECT 2209 2208 2210                                                           
CONECT 2210 2205 2209                                                           
CONECT 2211 2208 2212                                                           
CONECT 2212 2211 2213 2218                                                      
CONECT 2213 2212 2214                                                           
CONECT 2214 2213 2215                                                           
CONECT 2215 2214 2216 2217                                                      
CONECT 2216 2215                                                                
CONECT 2217 2215 2218                                                           
CONECT 2218 2212 2217                                                           
CONECT 2219 2204                                                                
CONECT 2220 2198                                                                
MASTER      291    0    1   15    7    0    4    6 2312    1   37   23          
END                                                                             



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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: december 26th, 2025.