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.


***  IMMUNE SYSTEM 03-JUL-23 8JYQ  ***

elNémo ID: 2602022316101172576

Job options:

ID        	=	 2602022316101172576
JOBID     	=	 IMMUNE SYSTEM 03-JUL-23 8JYQ
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    IMMUNE SYSTEM                           03-JUL-23   8JYQ              
TITLE     CRYSTAL STRUCTURE OF CANCER-SPECIFIC ANTI-HER2 ANTIBODY H2MAB-214 IN  
TITLE    2 COMPLEX WITH EPITOPE PEPTIDE                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: H2CASMAB-1 VH(S112C),SARAH;                                
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: H2CASMAB-1 VL,SARAH(S37C);                                 
COMPND   7 CHAIN: B, E;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: H2CASMAB-1 EPITOPE PEPTIDE;                                
COMPND  11 CHAIN: C, F;                                                         
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE   3 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE   4 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: MUS MUSCULUS, HOMO SAPIENS;                     
SOURCE   8 ORGANISM_TAXID: 10090, 9606;                                         
SOURCE   9 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  10 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    HER2, ANTIBODY, IMMUNE SYSTEM                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.ARIMORI,J.TAKAGI                                                    
REVDAT   4   13-NOV-24 8JYQ    1       REMARK                                   
REVDAT   3   15-MAY-24 8JYQ    1       JRNL                                     
REVDAT   2   27-MAR-24 8JYQ    1       JRNL                                     
REVDAT   1   13-MAR-24 8JYQ    0                                                
JRNL        AUTH   T.ARIMORI,E.MIHARA,H.SUZUKI,T.OHISHI,T.TANAKA,M.K.KANEKO,    
JRNL        AUTH 2 J.TAKAGI,Y.KATO                                              
JRNL        TITL   LOCALLY MISFOLDED HER2 EXPRESSED ON CANCER CELLS IS A        
JRNL        TITL 2 PROMISING TARGET FOR DEVELOPMENT OF CANCER-SPECIFIC          
JRNL        TITL 3 ANTIBODIES.                                                  
JRNL        REF    STRUCTURE                     V.  32   536 2024              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   38460519                                                     
JRNL        DOI    10.1016/J.STR.2024.02.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.19.2_4158                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.46                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 70773                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.198                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3540                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 36.4600 -  5.1000    0.99     2801   148  0.1568 0.1785        
REMARK   3     2  5.1000 -  4.0500    0.98     2725   143  0.1382 0.1807        
REMARK   3     3  4.0500 -  3.5400    0.99     2719   144  0.1625 0.1982        
REMARK   3     4  3.5400 -  3.2200    0.99     2726   143  0.1871 0.2291        
REMARK   3     5  3.2100 -  2.9800    0.99     2720   143  0.2092 0.2288        
REMARK   3     6  2.9800 -  2.8100    0.99     2713   143  0.2134 0.2690        
REMARK   3     7  2.8100 -  2.6700    0.99     2709   142  0.2176 0.2452        
REMARK   3     8  2.6700 -  2.5500    0.99     2682   142  0.2175 0.2878        
REMARK   3     9  2.5500 -  2.4500    0.99     2677   141  0.2242 0.2672        
REMARK   3    10  2.4500 -  2.3700    0.99     2717   143  0.2216 0.2717        
REMARK   3    11  2.3700 -  2.3000    0.99     2699   142  0.2248 0.2598        
REMARK   3    12  2.3000 -  2.2300    0.99     2677   141  0.2198 0.2573        
REMARK   3    13  2.2300 -  2.1700    0.99     2692   142  0.2196 0.2682        
REMARK   3    14  2.1700 -  2.1200    0.99     2727   143  0.2183 0.2512        
REMARK   3    15  2.1200 -  2.0700    0.99     2680   141  0.2266 0.2716        
REMARK   3    16  2.0700 -  2.0300    0.99     2664   140  0.2625 0.2943        
REMARK   3    17  2.0300 -  1.9900    0.99     2726   143  0.2689 0.3283        
REMARK   3    18  1.9900 -  1.9500    0.98     2682   141  0.2713 0.3084        
REMARK   3    19  1.9500 -  1.9100    0.98     2647   140  0.2877 0.3006        
REMARK   3    20  1.9100 -  1.8800    0.99     2700   142  0.2882 0.3256        
REMARK   3    21  1.8800 -  1.8500    0.98     2628   138  0.3198 0.4073        
REMARK   3    22  1.8500 -  1.8200    0.99     2664   140  0.3544 0.3772        
REMARK   3    23  1.8200 -  1.7900    0.98     2701   143  0.3899 0.4001        
REMARK   3    24  1.7900 -  1.7700    0.98     2669   140  0.4402 0.4682        
REMARK   3    25  1.7700 -  1.7500    0.93     2488   132  0.4946 0.5228        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.286            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.108           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 36.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.94                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           5519                                  
REMARK   3   ANGLE     :  0.881           7479                                  
REMARK   3   CHIRALITY :  0.056            827                                  
REMARK   3   PLANARITY :  0.007            952                                  
REMARK   3   DIHEDRAL  :  5.705            739                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 21                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 40:52 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):    4.028    4.157  -11.813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3323 T22:   0.3183                                     
REMARK   3      T33:   0.3254 T12:  -0.0355                                     
REMARK   3      T13:   0.0955 T23:   0.0223                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5278 L22:   8.1520                                     
REMARK   3      L33:   3.5961 L12:  -1.7703                                     
REMARK   3      L13:  -0.6464 L23:  -1.1450                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3267 S12:   0.5051 S13:   0.7760                       
REMARK   3      S21:  -0.2192 S22:  -0.1004 S23:  -0.1009                       
REMARK   3      S31:  -0.4871 S32:   0.0752 S33:  -0.0156                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 53:60 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):    6.981   -3.512   -0.308              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4586 T22:   0.4370                                     
REMARK   3      T33:   0.3238 T12:  -0.0941                                     
REMARK   3      T13:   0.0493 T23:  -0.0415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9303 L22:   3.5962                                     
REMARK   3      L33:   4.8497 L12:  -2.4842                                     
REMARK   3      L13:   2.8076 L23:  -4.0543                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1587 S12:  -0.2771 S13:  -0.0682                       
REMARK   3      S21:   1.2942 S22:   0.1570 S23:  -0.0072                       
REMARK   3      S31:  -0.6689 S32:  -0.0850 S33:   0.0826                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 61:75 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -0.628    0.029   -1.424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2914 T22:   0.3174                                     
REMARK   3      T33:   0.3167 T12:   0.0211                                     
REMARK   3      T13:   0.0304 T23:  -0.0226                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3197 L22:   2.6865                                     
REMARK   3      L33:   7.9445 L12:   1.7989                                     
REMARK   3      L13:  -1.8164 L23:  -1.8843                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1782 S12:  -0.1313 S13:   0.0794                       
REMARK   3      S21:   1.0594 S22:   0.0460 S23:   0.2407                       
REMARK   3      S31:  -0.3154 S32:  -0.1399 S33:  -0.2503                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 76:82 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   -5.432    0.882   -4.091              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3430 T22:   0.3486                                     
REMARK   3      T33:   0.2885 T12:  -0.0453                                     
REMARK   3      T13:   0.0291 T23:   0.0117                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.2232 L22:   2.2566                                     
REMARK   3      L33:   4.8214 L12:   0.8829                                     
REMARK   3      L13:   0.2427 L23:   1.3254                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0282 S12:  -0.1883 S13:  -0.2662                       
REMARK   3      S21:   0.6445 S22:   0.5136 S23:   0.3856                       
REMARK   3      S31:   0.4761 S32:  -0.3466 S33:  -0.2454                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 83:100 )                           
REMARK   3    ORIGIN FOR THE GROUP (A):    4.762   -1.025  -13.011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3285 T22:   0.2970                                     
REMARK   3      T33:   0.2119 T12:  -0.0452                                     
REMARK   3      T13:   0.0332 T23:  -0.0082                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7166 L22:   4.8642                                     
REMARK   3      L33:   1.3215 L12:  -4.1648                                     
REMARK   3      L13:   0.4809 L23:  -0.9102                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1780 S12:   0.1019 S13:   0.0778                       
REMARK   3      S21:   0.0485 S22:  -0.1135 S23:   0.0517                       
REMARK   3      S31:  -0.1529 S32:   0.0293 S33:  -0.0557                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 101:113 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.225    1.558  -15.826              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3467 T22:   0.3086                                     
REMARK   3      T33:   0.3043 T12:  -0.0649                                     
REMARK   3      T13:  -0.0007 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1529 L22:   8.1084                                     
REMARK   3      L33:   5.3012 L12:  -5.6583                                     
REMARK   3      L13:  -0.3446 L23:   1.0515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5377 S12:   0.4181 S13:   0.3313                       
REMARK   3      S21:  -0.5991 S22:  -0.4567 S23:   0.0437                       
REMARK   3      S31:  -0.1064 S32:  -0.2219 S33:  -0.1442                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 114:124 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -27.107   22.796   -9.791              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7797 T22:   0.7184                                     
REMARK   3      T33:   1.1366 T12:   0.0848                                     
REMARK   3      T13:   0.0742 T23:  -0.1884                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2145 L22:   7.1742                                     
REMARK   3      L33:   2.1450 L12:   1.8045                                     
REMARK   3      L13:   1.9448 L23:  -2.3690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0066 S12:  -0.6102 S13:   1.0598                       
REMARK   3      S21:   1.2471 S22:  -0.4229 S23:   0.4952                       
REMARK   3      S31:  -0.6531 S32:   0.4052 S33:   0.3484                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN D AND RESID 125:163 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -19.080    7.280  -31.902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5841 T22:   0.6189                                     
REMARK   3      T33:   0.5238 T12:   0.1350                                     
REMARK   3      T13:  -0.1579 T23:   0.0606                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.0985 L22:   6.2597                                     
REMARK   3      L33:   8.6207 L12:  -6.4266                                     
REMARK   3      L13:  -9.2980 L23:   6.8075                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8877 S12:   1.4210 S13:   0.0288                       
REMARK   3      S21:  -1.0257 S22:  -0.9849 S23:   0.4243                       
REMARK   3      S31:  -0.8696 S32:  -1.3368 S33:   0.0842                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN E AND RESID 0:112 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   14.039    2.592  -25.400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2804 T22:   0.3822                                     
REMARK   3      T33:   0.2847 T12:  -0.0021                                     
REMARK   3      T13:   0.0541 T23:   0.0266                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6000 L22:   3.2226                                     
REMARK   3      L33:   8.7983 L12:   0.0160                                     
REMARK   3      L13:   0.1776 L23:   0.4866                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0390 S12:   0.3095 S13:   0.1091                       
REMARK   3      S21:  -0.3011 S22:  -0.3252 S23:   0.0231                       
REMARK   3      S31:  -0.0519 S32:   0.0650 S33:   0.3197                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN E AND RESID 113:162 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.871    3.147  -26.211              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4728 T22:   0.3825                                     
REMARK   3      T33:   0.4198 T12:   0.0523                                     
REMARK   3      T13:   0.0046 T23:   0.0651                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6459 L22:   2.5498                                     
REMARK   3      L33:   3.4125 L12:  -0.9513                                     
REMARK   3      L13:  -1.4138 L23:   2.1039                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0733 S12:  -0.0004 S13:  -0.0559                       
REMARK   3      S21:  -0.1102 S22:   0.2424 S23:  -0.2291                       
REMARK   3      S31:   0.2813 S32:   0.3806 S33:  -0.1713                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN F AND RESID 612:618 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   17.120   -7.332   -4.837              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4706 T22:   0.6444                                     
REMARK   3      T33:   0.3130 T12:  -0.0506                                     
REMARK   3      T13:  -0.0072 T23:  -0.0119                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8510 L22:   2.8255                                     
REMARK   3      L33:   3.6989 L12:  -3.3969                                     
REMARK   3      L13:  -4.1311 L23:   2.5990                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1534 S12:  -0.9410 S13:   0.5511                       
REMARK   3      S21:   0.9236 S22:   0.3610 S23:  -0.4106                       
REMARK   3      S31:   0.3105 S32:   1.2187 S33:  -0.3457                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 1:109 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -31.574   -6.383  -20.444              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4673 T22:   0.2942                                     
REMARK   3      T33:   0.3267 T12:  -0.0620                                     
REMARK   3      T13:   0.0400 T23:  -0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6024 L22:   1.9494                                     
REMARK   3      L33:   3.6916 L12:  -0.0456                                     
REMARK   3      L13:   0.5147 L23:  -0.4860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1094 S12:   0.1274 S13:   0.1435                       
REMARK   3      S21:  -0.3944 S22:  -0.0119 S23:  -0.0442                       
REMARK   3      S31:  -0.2840 S32:   0.1893 S33:  -0.0781                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 110:124 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -43.627   -7.563  -48.857              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8519 T22:   0.9650                                     
REMARK   3      T33:   0.6542 T12:  -0.0464                                     
REMARK   3      T13:   0.0226 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8695 L22:   0.1177                                     
REMARK   3      L33:   5.1640 L12:   0.1261                                     
REMARK   3      L13:   0.4100 L23:   0.8101                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0806 S12:   1.4556 S13:  -0.0741                       
REMARK   3      S21:  -0.0081 S22:   0.0478 S23:  -0.6149                       
REMARK   3      S31:   0.6403 S32:  -0.3006 S33:  -0.1390                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN A AND RESID 125:161 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -59.433  -18.682  -32.460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5402 T22:   0.6968                                     
REMARK   3      T33:   0.5842 T12:  -0.1160                                     
REMARK   3      T13:   0.0046 T23:  -0.1121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3213 L22:   3.5487                                     
REMARK   3      L33:   7.2688 L12:   0.7596                                     
REMARK   3      L13:  -1.3140 L23:  -3.2631                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1084 S12:   0.6949 S13:  -0.4230                       
REMARK   3      S21:  -0.6985 S22:   0.6918 S23:   0.4209                       
REMARK   3      S31:   1.0743 S32:  -1.2396 S33:  -0.1189                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 0:7 )                              
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.556  -25.358  -18.945              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4665 T22:   0.3719                                     
REMARK   3      T33:   0.5400 T12:   0.0295                                     
REMARK   3      T13:   0.1451 T23:   0.0101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0742 L22:   2.0325                                     
REMARK   3      L33:   6.6363 L12:   1.4373                                     
REMARK   3      L13:   0.0983 L23:   1.8406                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0416 S12:   0.0778 S13:  -0.5597                       
REMARK   3      S21:  -0.8786 S22:   0.0375 S23:  -0.7747                       
REMARK   3      S31:  -0.2952 S32:   0.7018 S33:  -0.0158                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 8:101 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -32.948  -24.071   -8.424              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2288 T22:   0.2384                                     
REMARK   3      T33:   0.2854 T12:   0.0030                                     
REMARK   3      T13:  -0.0264 T23:   0.0477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5601 L22:   3.7053                                     
REMARK   3      L33:   3.4978 L12:   0.4694                                     
REMARK   3      L13:  -1.6655 L23:   0.4022                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0279 S12:  -0.2947 S13:  -0.2184                       
REMARK   3      S21:   0.1545 S22:  -0.0808 S23:  -0.1036                       
REMARK   3      S31:   0.0582 S32:   0.3214 S33:   0.0369                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 102:119 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -48.671  -31.140  -11.309              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5636 T22:   0.7067                                     
REMARK   3      T33:   0.7684 T12:  -0.1076                                     
REMARK   3      T13:   0.0455 T23:   0.0578                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7908 L22:   1.9247                                     
REMARK   3      L33:   6.6264 L12:   1.0222                                     
REMARK   3      L13:  -0.1237 L23:   2.7805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2772 S12:   0.3783 S13:  -1.6212                       
REMARK   3      S21:   0.6750 S22:   0.0039 S23:   0.3324                       
REMARK   3      S31:   0.9721 S32:  -1.7982 S33:   0.2304                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN B AND RESID 120:159 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -52.196  -13.982  -28.133              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4873 T22:   0.5855                                     
REMARK   3      T33:   0.5979 T12:   0.0489                                     
REMARK   3      T13:   0.0146 T23:  -0.1417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4167 L22:   7.5903                                     
REMARK   3      L33:   4.9897 L12:   2.2650                                     
REMARK   3      L13:  -2.7369 L23:  -6.4697                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4674 S12:   0.0539 S13:  -0.4182                       
REMARK   3      S21:   0.4348 S22:  -0.0633 S23:  -0.6588                       
REMARK   3      S31:  -0.7970 S32:  -0.3837 S33:   0.5237                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 611:618 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -17.472   -8.274   -6.888              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4189 T22:   0.5477                                     
REMARK   3      T33:   0.5128 T12:  -0.1019                                     
REMARK   3      T13:  -0.0332 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5228 L22:   2.0879                                     
REMARK   3      L33:   7.5686 L12:  -0.0399                                     
REMARK   3      L13:   0.9968 L23:  -0.4636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3007 S12:  -0.4047 S13:  -0.2217                       
REMARK   3      S21:  -0.1225 S22:  -0.1995 S23:  -0.8053                       
REMARK   3      S31:  -0.0768 S32:   1.3777 S33:   0.3044                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 1:7 )                              
REMARK   3    ORIGIN FOR THE GROUP (A):   -4.269   -9.298  -15.644              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4975 T22:   0.4306                                     
REMARK   3      T33:   0.4607 T12:  -0.0071                                     
REMARK   3      T13:  -0.0095 T23:  -0.0605                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8965 L22:   2.8490                                     
REMARK   3      L33:   4.8662 L12:   0.4321                                     
REMARK   3      L13:  -4.6006 L23:   0.7732                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4104 S12:   1.1097 S13:  -0.4405                       
REMARK   3      S21:  -0.8420 S22:  -0.7036 S23:   1.2586                       
REMARK   3      S31:   0.1603 S32:  -0.9791 S33:   0.4749                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 8:39 )                             
REMARK   3    ORIGIN FOR THE GROUP (A):   -3.768   -1.833   -8.589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3829 T22:   0.3870                                     
REMARK   3      T33:   0.2756 T12:  -0.0333                                     
REMARK   3      T13:   0.0055 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.9697 L22:   6.2431                                     
REMARK   3      L33:   0.9892 L12:  -2.8501                                     
REMARK   3      L13:  -0.6305 L23:  -0.2758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0082 S12:   0.0318 S13:  -0.0811                       
REMARK   3      S21:   0.1349 S22:   0.0034 S23:   0.2049                       
REMARK   3      S31:   0.0927 S32:  -0.0709 S33:  -0.0036                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 8JYQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JUL-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300039109.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-OCT-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL44XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 16M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 70833                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.750                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.580                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY                : 3.860                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05200                            
REMARK 200   FOR THE DATA SET  : 10.9500                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.75                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.83                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.96100                            
REMARK 200   FOR SHELL         : 1.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.35                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M CHES PH 9.5, 20% W/V PEG 8000,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       31.39650            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5860 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 15990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -50.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16660 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
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    -1                                                      
REMARK 465     ARG A     0                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     LYS A   164                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     ARG B   108                                                      
REMARK 465     GLY B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     TYR B   112                                                      
REMARK 465     GLU B   113                                                      
REMARK 465     PHE B   114                                                      
REMARK 465     LEU B   115                                                      
REMARK 465     LYS B   116                                                      
REMARK 465     SER B   117                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     THR B   161                                                      
REMARK 465     LEU B   162                                                      
REMARK 465     LEU B   163                                                      
REMARK 465     GLY B   164                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     ARG D     0                                                      
REMARK 465     LYS D   164                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     GLY E   109                                                      
REMARK 465     SER E   110                                                      
REMARK 465     ASP E   111                                                      
REMARK 465     LEU E   163                                                      
REMARK 465     GLY E   164                                                      
REMARK 465     MET F   611                                                      
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    SER A  15       -9.28     80.88                                   
REMARK 500    SER A 113      -77.03    -86.87                                   
REMARK 500    SER A 115       81.30   -164.37                                   
REMARK 500    ALA B  51      -41.51     75.45                                   
REMARK 500    LYS C 615     -112.52   -109.30                                   
REMARK 500    SER D  15       -5.32     75.86                                   
REMARK 500    LYS D  43     -160.44   -128.28                                   
REMARK 500    SER D  82B      73.21     36.86                                   
REMARK 500    LEU E  32       61.79   -102.50                                   
REMARK 500    ALA E  51      -41.06     73.77                                   
REMARK 500    LYS F 615     -111.27   -116.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  8JYQ A   -1   113  PDB    8JYQ     8JYQ            -1    113             
DBREF  8JYQ A  114   164  PDB    8JYQ     8JYQ           114    164             
DBREF  8JYQ B   -1   108  PDB    8JYQ     8JYQ            -1    108             
DBREF  8JYQ B  109   164  PDB    8JYQ     8JYQ           109    164             
DBREF  8JYQ C  611   618  PDB    8JYQ     8JYQ           611    618             
DBREF  8JYQ D   -1   113  PDB    8JYQ     8JYQ            -1    113             
DBREF  8JYQ D  114   164  PDB    8JYQ     8JYQ           114    164             
DBREF  8JYQ E   -1   108  PDB    8JYQ     8JYQ            -1    108             
DBREF  8JYQ E  109   164  PDB    8JYQ     8JYQ           109    164             
DBREF  8JYQ F  611   618  PDB    8JYQ     8JYQ           611    618             
SEQRES   1 A  174  GLY ARG GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE          
SEQRES   2 A  174  LEU GLN PRO SER GLN THR LEU SER LEU THR CYS SER PHE          
SEQRES   3 A  174  SER GLY PHE SER LEU SER THR SER GLY MET GLY VAL SER          
SEQRES   4 A  174  TRP ILE ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU          
SEQRES   5 A  174  ALA HIS ILE PHE TRP ASP ASP ASP LYS ARG TYR ASN PRO          
SEQRES   6 A  174  SER LEU LYS SER ARG LEU THR ILE SER LYS ASP THR SER          
SEQRES   7 A  174  ARG ASN LYS VAL PHE LEU LYS ILE THR SER VAL ASP THR          
SEQRES   8 A  174  ALA ASP THR ALA THR TYR TYR CYS ALA ARG ARG VAL VAL          
SEQRES   9 A  174  ALA THR ASP TRP TYR PHE ASP VAL TRP GLY ALA GLY THR          
SEQRES  10 A  174  THR VAL THR VAL CYS SER GLY SER ASP TYR GLU PHE LEU          
SEQRES  11 A  174  LYS SER TRP THR VAL GLU ASP LEU GLN LYS ARG LEU LEU          
SEQRES  12 A  174  ALA LEU ASP PRO MET MET GLU GLN GLU ILE GLU GLU ILE          
SEQRES  13 A  174  ARG GLN LYS TYR GLN SER LYS ARG GLN PRO ILE LEU ASP          
SEQRES  14 A  174  ALA ILE GLU ALA LYS                                          
SEQRES   1 B  170  GLY ARG ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU          
SEQRES   2 B  170  ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG          
SEQRES   3 B  170  ALA SER GLU SER VAL GLU TYR TYR GLY THR THR LEU MET          
SEQRES   4 B  170  GLN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU          
SEQRES   5 B  170  LEU ILE TYR ALA ALA SER LYS VAL GLU SER GLY VAL PRO          
SEQRES   6 B  170  ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE SER          
SEQRES   7 B  170  LEU ASN ILE HIS PRO VAL GLU GLU ASP ASP VAL ALA MET          
SEQRES   8 B  170  TYR PHE CYS GLN GLN SER ARG LYS VAL PRO LEU THR PHE          
SEQRES   9 B  170  GLY ALA GLY THR LYS LEU GLU LEU LYS ARG GLY SER ASP          
SEQRES  10 B  170  TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP LEU GLN          
SEQRES  11 B  170  LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU GLN GLU          
SEQRES  12 B  170  ILE GLU GLU ILE ARG GLN LYS TYR GLN CYS LYS ARG GLN          
SEQRES  13 B  170  PRO ILE LEU ASP ALA ILE GLU ALA LYS GLY THR LEU LEU          
SEQRES  14 B  170  GLY                                                          
SEQRES   1 C    8  MET PRO ILE TRP LYS PHE PRO ASP                              
SEQRES   1 D  174  GLY ARG GLN VAL THR LEU LYS GLU SER GLY PRO GLY ILE          
SEQRES   2 D  174  LEU GLN PRO SER GLN THR LEU SER LEU THR CYS SER PHE          
SEQRES   3 D  174  SER GLY PHE SER LEU SER THR SER GLY MET GLY VAL SER          
SEQRES   4 D  174  TRP ILE ARG GLN PRO SER GLY LYS GLY LEU GLU TRP LEU          
SEQRES   5 D  174  ALA HIS ILE PHE TRP ASP ASP ASP LYS ARG TYR ASN PRO          
SEQRES   6 D  174  SER LEU LYS SER ARG LEU THR ILE SER LYS ASP THR SER          
SEQRES   7 D  174  ARG ASN LYS VAL PHE LEU LYS ILE THR SER VAL ASP THR          
SEQRES   8 D  174  ALA ASP THR ALA THR TYR TYR CYS ALA ARG ARG VAL VAL          
SEQRES   9 D  174  ALA THR ASP TRP TYR PHE ASP VAL TRP GLY ALA GLY THR          
SEQRES  10 D  174  THR VAL THR VAL CYS SER GLY SER ASP TYR GLU PHE LEU          
SEQRES  11 D  174  LYS SER TRP THR VAL GLU ASP LEU GLN LYS ARG LEU LEU          
SEQRES  12 D  174  ALA LEU ASP PRO MET MET GLU GLN GLU ILE GLU GLU ILE          
SEQRES  13 D  174  ARG GLN LYS TYR GLN SER LYS ARG GLN PRO ILE LEU ASP          
SEQRES  14 D  174  ALA ILE GLU ALA LYS                                          
SEQRES   1 E  170  GLY ARG ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU          
SEQRES   2 E  170  ALA VAL SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG          
SEQRES   3 E  170  ALA SER GLU SER VAL GLU TYR TYR GLY THR THR LEU MET          
SEQRES   4 E  170  GLN TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU          
SEQRES   5 E  170  LEU ILE TYR ALA ALA SER LYS VAL GLU SER GLY VAL PRO          
SEQRES   6 E  170  ALA ARG PHE SER GLY SER GLY SER GLY THR ASP PHE SER          
SEQRES   7 E  170  LEU ASN ILE HIS PRO VAL GLU GLU ASP ASP VAL ALA MET          
SEQRES   8 E  170  TYR PHE CYS GLN GLN SER ARG LYS VAL PRO LEU THR PHE          
SEQRES   9 E  170  GLY ALA GLY THR LYS LEU GLU LEU LYS ARG GLY SER ASP          
SEQRES  10 E  170  TYR GLU PHE LEU LYS SER TRP THR VAL GLU ASP LEU GLN          
SEQRES  11 E  170  LYS ARG LEU LEU ALA LEU ASP PRO MET MET GLU GLN GLU          
SEQRES  12 E  170  ILE GLU GLU ILE ARG GLN LYS TYR GLN CYS LYS ARG GLN          
SEQRES  13 E  170  PRO ILE LEU ASP ALA ILE GLU ALA LYS GLY THR LEU LEU          
SEQRES  14 E  170  GLY                                                          
SEQRES   1 F    8  MET PRO ILE TRP LYS PHE PRO ASP                              
FORMUL   7  HOH   *193(H2 O)                                                    
HELIX    1 AA1 LEU A   63  SER A   65  5                                   3    
HELIX    2 AA2 ASP A   83  ASP A   86  5                                   4    
HELIX    3 AA3 ASP A  116  TRP A  123  1                                   8    
HELIX    4 AA4 THR A  124  ILE A  161  1                                  38    
HELIX    5 AA5 GLU B   79  VAL B   83  5                                   5    
HELIX    6 AA6 THR B  119  LYS B  159  1                                  41    
HELIX    7 AA7 PRO D   61  SER D   65  5                                   5    
HELIX    8 AA8 THR D   73  ARG D   75  5                                   3    
HELIX    9 AA9 ASP D   83  THR D   87  5                                   5    
HELIX   10 AB1 ASP D  116  LYS D  121  1                                   6    
HELIX   11 AB2 THR D  124  ALA D  163  1                                  40    
HELIX   12 AB3 GLU E   79  VAL E   83  5                                   5    
HELIX   13 AB4 TYR E  112  TRP E  118  5                                   7    
HELIX   14 AB5 THR E  119  ALA E  158  1                                  40    
SHEET    1 AA1 4 THR A   3  SER A   7  0                                        
SHEET    2 AA1 4 LEU A  18  SER A  25 -1  O  SER A  23   N  LYS A   5           
SHEET    3 AA1 4 LYS A  77  ILE A  82 -1  O  ILE A  82   N  LEU A  18           
SHEET    4 AA1 4 LEU A  67  ASP A  72 -1  N  SER A  70   O  PHE A  79           
SHEET    1 AA2 6 ILE A  11  LEU A  12  0                                        
SHEET    2 AA2 6 THR A 107  VAL A 111  1  O  THR A 110   N  LEU A  12           
SHEET    3 AA2 6 ALA A  88  VAL A  96 -1  N  TYR A  90   O  THR A 107           
SHEET    4 AA2 6 MET A  32  PRO A  40 -1  N  ILE A  37   O  TYR A  91           
SHEET    5 AA2 6 GLU A  46  PHE A  52 -1  O  GLU A  46   N  ARG A  38           
SHEET    6 AA2 6 LYS A  57  TYR A  59 -1  O  ARG A  58   N  HIS A  50           
SHEET    1 AA3 4 ILE A  11  LEU A  12  0                                        
SHEET    2 AA3 4 THR A 107  VAL A 111  1  O  THR A 110   N  LEU A  12           
SHEET    3 AA3 4 ALA A  88  VAL A  96 -1  N  TYR A  90   O  THR A 107           
SHEET    4 AA3 4 PHE A 100C TRP A 103 -1  O  VAL A 102   N  ARG A  94           
SHEET    1 AA4 4 LEU B   4  SER B   7  0                                        
SHEET    2 AA4 4 ALA B  19  ALA B  25 -1  O  SER B  22   N  SER B   7           
SHEET    3 AA4 4 ASP B  70  ILE B  75 -1  O  PHE B  71   N  CYS B  23           
SHEET    4 AA4 4 PHE B  62  SER B  67 -1  N  SER B  63   O  ASN B  74           
SHEET    1 AA5 6 SER B  10  VAL B  13  0                                        
SHEET    2 AA5 6 THR B 102  LEU B 106  1  O  LYS B 103   N  LEU B  11           
SHEET    3 AA5 6 ALA B  84  GLN B  90 -1  N  ALA B  84   O  LEU B 104           
SHEET    4 AA5 6 MET B  33  GLN B  38 -1  N  GLN B  38   O  MET B  85           
SHEET    5 AA5 6 LYS B  45  TYR B  49 -1  O  LYS B  45   N  GLN B  37           
SHEET    6 AA5 6 LYS B  53  VAL B  54 -1  O  LYS B  53   N  TYR B  49           
SHEET    1 AA6 4 SER B  10  VAL B  13  0                                        
SHEET    2 AA6 4 THR B 102  LEU B 106  1  O  LYS B 103   N  LEU B  11           
SHEET    3 AA6 4 ALA B  84  GLN B  90 -1  N  ALA B  84   O  LEU B 104           
SHEET    4 AA6 4 THR B  97  PHE B  98 -1  O  THR B  97   N  GLN B  90           
SHEET    1 AA7 4 THR D   3  SER D   7  0                                        
SHEET    2 AA7 4 LEU D  18  SER D  25 -1  O  SER D  23   N  LYS D   5           
SHEET    3 AA7 4 LYS D  77  ILE D  82 -1  O  VAL D  78   N  CYS D  22           
SHEET    4 AA7 4 LEU D  67  ASP D  72 -1  N  SER D  70   O  PHE D  79           
SHEET    1 AA8 6 ILE D  11  LEU D  12  0                                        
SHEET    2 AA8 6 THR D 107  VAL D 111  1  O  THR D 110   N  LEU D  12           
SHEET    3 AA8 6 ALA D  88  VAL D  96 -1  N  TYR D  90   O  THR D 107           
SHEET    4 AA8 6 MET D  32  GLN D  39 -1  N  ILE D  37   O  TYR D  91           
SHEET    5 AA8 6 GLU D  46  PHE D  52 -1  O  LEU D  48   N  TRP D  36           
SHEET    6 AA8 6 LYS D  57  TYR D  59 -1  O  ARG D  58   N  HIS D  50           
SHEET    1 AA9 4 ILE D  11  LEU D  12  0                                        
SHEET    2 AA9 4 THR D 107  VAL D 111  1  O  THR D 110   N  LEU D  12           
SHEET    3 AA9 4 ALA D  88  VAL D  96 -1  N  TYR D  90   O  THR D 107           
SHEET    4 AA9 4 PHE D 100C TRP D 103 -1  O  ASP D 101   N  ARG D  94           
SHEET    1 AB1 4 LEU E   4  SER E   7  0                                        
SHEET    2 AB1 4 ALA E  19  ALA E  25 -1  O  ARG E  24   N  THR E   5           
SHEET    3 AB1 4 ASP E  70  ILE E  75 -1  O  PHE E  71   N  CYS E  23           
SHEET    4 AB1 4 PHE E  62  SER E  67 -1  N  SER E  63   O  ASN E  74           
SHEET    1 AB2 6 SER E  10  VAL E  13  0                                        
SHEET    2 AB2 6 THR E 102  LEU E 106  1  O  LYS E 103   N  LEU E  11           
SHEET    3 AB2 6 MET E  85  GLN E  90 -1  N  TYR E  86   O  THR E 102           
SHEET    4 AB2 6 MET E  33  GLN E  38 -1  N  TYR E  36   O  PHE E  87           
SHEET    5 AB2 6 LYS E  45  TYR E  49 -1  O  LEU E  47   N  TRP E  35           
SHEET    6 AB2 6 LYS E  53  VAL E  54 -1  O  LYS E  53   N  TYR E  49           
SHEET    1 AB3 4 SER E  10  VAL E  13  0                                        
SHEET    2 AB3 4 THR E 102  LEU E 106  1  O  LYS E 103   N  LEU E  11           
SHEET    3 AB3 4 MET E  85  GLN E  90 -1  N  TYR E  86   O  THR E 102           
SHEET    4 AB3 4 THR E  97  PHE E  98 -1  O  THR E  97   N  GLN E  90           
SHEET    1 AB4 2 GLU E  30  TYR E  30A 0                                        
SHEET    2 AB4 2 THR E  30D THR E  31 -1  O  THR E  30D  N  TYR E  30A          
SSBOND   1 CYS A   22    CYS A   92                          1555   1555  2.06  
SSBOND   2 CYS A  112    CYS B  147                          1555   1555  2.04  
SSBOND   3 CYS B   23    CYS B   88                          1555   1555  2.09  
SSBOND   4 CYS D   22    CYS D   92                          1555   1555  2.07  
SSBOND   5 CYS D  112    CYS E  147                          1555   1555  2.05  
SSBOND   6 CYS E   23    CYS E   88                          1555   1555  2.08  
CISPEP   1 SER B    7    PRO B    8          0        -3.49                     
CISPEP   2 HIS B   76    PRO B   77          0        -7.29                     
CISPEP   3 VAL B   94    PRO B   95          0         5.82                     
CISPEP   4 SER E    7    PRO E    8          0        -6.17                     
CISPEP   5 HIS E   76    PRO E   77          0         0.11                     
CISPEP   6 VAL E   94    PRO E   95          0         2.70                     
CRYST1   73.143   62.793   78.122  90.00  94.42  90.00 P 1 21 1      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      0.013672  0.000000  0.001057        0.00000                         
SCALE2      0.000000  0.015925  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012839        0.00000                         
ATOM      1  N   GLN A   1     -42.308  -2.005  -3.374  1.00 57.74           N  
ANISOU    1  N   GLN A   1     7645   7486   6806    363    805   -452       N  
ATOM      2  CA  GLN A   1     -41.690  -3.142  -4.041  1.00 55.52           C  
ANISOU    2  CA  GLN A   1     7288   7206   6601    162    704   -364       C  
ATOM      3  C   GLN A   1     -40.928  -2.681  -5.276  1.00 39.99           C  
ANISOU    3  C   GLN A   1     5462   5023   4708    119    638   -377       C  
ATOM      4  O   GLN A   1     -41.016  -1.523  -5.707  1.00 42.69           O  
ANISOU    4  O   GLN A   1     5950   5218   5054    240    659   -430       O  
ATOM      5  CB  GLN A   1     -42.739  -4.186  -4.434  1.00 51.37           C  
ANISOU    5  CB  GLN A   1     6528   6866   6123    153    673   -226       C  
ATOM      6  CG  GLN A   1     -43.707  -3.675  -5.490  1.00 63.43           C  
ANISOU    6  CG  GLN A   1     8007   8384   7710    308    656   -179       C  
ATOM      7  CD  GLN A   1     -44.806  -4.659  -5.830  1.00 76.32           C  
ANISOU    7  CD  GLN A   1     9394  10221   9383    281    613    -43       C  
ATOM      8  OE1 GLN A   1     -44.763  -5.830  -5.432  1.00 77.46           O  
ANISOU    8  OE1 GLN A   1     9428  10480   9524    117    582     26       O  
ATOM      9  NE2 GLN A   1     -45.822  -4.178  -6.553  1.00 68.41           N  
ANISOU    9  NE2 GLN A   1     8310   9266   8417    440    602      3       N  
ATOM     10  N   VAL A   2     -40.179  -3.611  -5.841  1.00 38.44           N  
ANISOU   10  N   VAL A   2     5230   4811   4564    -47    559   -323       N  
ATOM     11  CA  VAL A   2     -39.354  -3.351  -7.013  1.00 37.50           C  
ANISOU   11  CA  VAL A   2     5224   4523   4501   -110    506   -324       C  
ATOM     12  C   VAL A   2     -40.016  -4.023  -8.204  1.00 39.10           C  
ANISOU   12  C   VAL A   2     5327   4763   4767    -96    440   -220       C  
ATOM     13  O   VAL A   2     -40.332  -5.219  -8.153  1.00 43.86           O  
ANISOU   13  O   VAL A   2     5788   5491   5387   -167    395   -148       O  
ATOM     14  CB  VAL A   2     -37.918  -3.849  -6.790  1.00 43.92           C  
ANISOU   14  CB  VAL A   2     6076   5298   5312   -289    473   -353       C  
ATOM     15  CG1 VAL A   2     -37.129  -3.819  -8.094  1.00 39.89           C  
ANISOU   15  CG1 VAL A   2     5635   4666   4855   -358    429   -331       C  
ATOM     16  CG2 VAL A   2     -37.241  -2.979  -5.725  1.00 44.74           C  
ANISOU   16  CG2 VAL A   2     6304   5347   5347   -314    518   -464       C  
ATOM     17  N   THR A   3     -40.273  -3.249  -9.254  1.00 36.03           N  
ANISOU   17  N   THR A   3     5026   4260   4404     -6    426   -209       N  
ATOM     18  CA  THR A   3     -40.865  -3.770 -10.475  1.00 38.92           C  
ANISOU   18  CA  THR A   3     5324   4650   4814      8    350   -117       C  
ATOM     19  C   THR A   3     -39.960  -3.446 -11.653  1.00 42.71           C  
ANISOU   19  C   THR A   3     5955   4964   5307    -50    318   -120       C  
ATOM     20  O   THR A   3     -39.317  -2.394 -11.687  1.00 39.81           O  
ANISOU   20  O   THR A   3     5752   4452   4924    -40    362   -176       O  
ATOM     21  CB  THR A   3     -42.262  -3.192 -10.726  1.00 39.30           C  
ANISOU   21  CB  THR A   3     5305   4760   4867    197    352    -74       C  
ATOM     22  OG1 THR A   3     -42.161  -1.795 -11.007  1.00 52.60           O  
ANISOU   22  OG1 THR A   3     7170   6278   6536    328    390   -124       O  
ATOM     23  CG2 THR A   3     -43.145  -3.375  -9.495  1.00 45.63           C  
ANISOU   23  CG2 THR A   3     5947   5750   5641    269    413    -74       C  
ATOM     24  N   LEU A   4     -39.902  -4.374 -12.594  1.00 40.30           N  
ANISOU   24  N   LEU A   4     5606   4684   5023   -122    244    -59       N  
ATOM     25  CA  LEU A   4     -39.188  -4.219 -13.852  1.00 39.65           C  
ANISOU   25  CA  LEU A   4     5648   4481   4936   -166    216    -46       C  
ATOM     26  C   LEU A   4     -40.189  -4.592 -14.932  1.00 47.62           C  
ANISOU   26  C   LEU A   4     6611   5532   5950   -105    128     35       C  
ATOM     27  O   LEU A   4     -40.947  -5.556 -14.760  1.00 40.41           O  
ANISOU   27  O   LEU A   4     5553   4749   5054   -125     67     79       O  
ATOM     28  CB  LEU A   4     -37.971  -5.149 -13.895  1.00 35.87           C  
ANISOU   28  CB  LEU A   4     5167   4005   4456   -313    211    -66       C  
ATOM     29  CG  LEU A   4     -36.876  -4.936 -12.852  1.00 46.35           C  
ANISOU   29  CG  LEU A   4     6513   5320   5776   -395    274   -137       C  
ATOM     30  CD1 LEU A   4     -36.185  -6.264 -12.650  1.00 53.27           C  
ANISOU   30  CD1 LEU A   4     7309   6272   6662   -491    241   -132       C  
ATOM     31  CD2 LEU A   4     -35.882  -3.928 -13.322  1.00 62.02           C  
ANISOU   31  CD2 LEU A   4     8642   7178   7746   -440    323   -169       C  
ATOM     32  N   LYS A   5     -40.223  -3.825 -16.021  1.00 40.83           N  
ANISOU   32  N   LYS A   5     5878   4566   5069    -44    111     62       N  
ATOM     33  CA  LYS A   5     -41.132  -4.103 -17.125  1.00 45.20           C  
ANISOU   33  CA  LYS A   5     6405   5159   5612     13     10    139       C  
ATOM     34  C   LYS A   5     -40.391  -3.939 -18.448  1.00 39.76           C  
ANISOU   34  C   LYS A   5     5881   4354   4873    -29     -7    156       C  
ATOM     35  O   LYS A   5     -39.872  -2.859 -18.739  1.00 44.08           O  
ANISOU   35  O   LYS A   5     6582   4769   5396     -2     50    149       O  
ATOM     36  CB  LYS A   5     -42.357  -3.173 -17.128  1.00 48.18           C  
ANISOU   36  CB  LYS A   5     6751   5558   5996    198     -6    180       C  
ATOM     37  CG  LYS A   5     -43.552  -3.907 -17.698  1.00 63.61           C  
ANISOU   37  CG  LYS A   5     8552   7659   7958    228   -127    263       C  
ATOM     38  CD  LYS A   5     -44.769  -3.108 -18.011  1.00 71.31           C  
ANISOU   38  CD  LYS A   5     9476   8682   8936    421   -172    325       C  
ATOM     39  CE  LYS A   5     -44.859  -3.059 -19.517  1.00 71.82           C  
ANISOU   39  CE  LYS A   5     9649   8685   8954    429   -281    388       C  
ATOM     40  NZ  LYS A   5     -45.681  -4.113 -20.176  1.00 75.71           N  
ANISOU   40  NZ  LYS A   5    10001   9326   9440    365   -429    457       N  
ATOM     41  N   GLU A   6     -40.387  -4.993 -19.257  1.00 37.65           N  
ANISOU   41  N   GLU A   6     5595   4132   4580    -98    -88    182       N  
ATOM     42  CA  GLU A   6     -39.814  -4.954 -20.596  1.00 41.54           C  
ANISOU   42  CA  GLU A   6     6238   4544   5002   -125   -107    202       C  
ATOM     43  C   GLU A   6     -40.857  -4.492 -21.609  1.00 49.36           C  
ANISOU   43  C   GLU A   6     7272   5531   5953    -20   -205    279       C  
ATOM     44  O   GLU A   6     -42.033  -4.858 -21.525  1.00 43.96           O  
ANISOU   44  O   GLU A   6     6456   4954   5294     31   -303    321       O  
ATOM     45  CB  GLU A   6     -39.293  -6.340 -20.972  1.00 42.54           C  
ANISOU   45  CB  GLU A   6     6350   4711   5102   -230   -149    177       C  
ATOM     46  CG  GLU A   6     -38.350  -6.941 -19.932  1.00 42.76           C  
ANISOU   46  CG  GLU A   6     6313   4761   5172   -314    -76    112       C  
ATOM     47  CD  GLU A   6     -39.036  -7.792 -18.872  1.00 44.47           C  
ANISOU   47  CD  GLU A   6     6371   5077   5448   -341   -125    112       C  
ATOM     48  OE1 GLU A   6     -40.271  -7.693 -18.698  1.00 39.94           O  
ANISOU   48  OE1 GLU A   6     5704   4572   4899   -292   -188    160       O  
ATOM     49  OE2 GLU A   6     -38.320  -8.539 -18.172  1.00 37.55           O1-
ANISOU   49  OE2 GLU A   6     5455   4219   4592   -410    -97     72       O1-
ATOM     50  N   SER A   7     -40.420  -3.686 -22.574  1.00 42.46           N  
ANISOU   50  N   SER A   7     6577   4546   5011      6   -182    310       N  
ATOM     51  CA  SER A   7     -41.282  -3.308 -23.683  1.00 48.99           C  
ANISOU   51  CA  SER A   7     7471   5365   5777    103   -288    392       C  
ATOM     52  C   SER A   7     -40.484  -3.395 -24.975  1.00 46.40           C  
ANISOU   52  C   SER A   7     7324   4970   5336     40   -283    410       C  
ATOM     53  O   SER A   7     -39.261  -3.245 -24.982  1.00 48.59           O  
ANISOU   53  O   SER A   7     7691   5182   5590    -46   -166    373       O  
ATOM     54  CB  SER A   7     -41.876  -1.901 -23.505  1.00 47.50           C  
ANISOU   54  CB  SER A   7     7341   5098   5609    260   -272    438       C  
ATOM     55  OG  SER A   7     -40.925  -1.013 -22.946  1.00 59.60           O  
ANISOU   55  OG  SER A   7     8992   6496   7158    229   -138    395       O  
ATOM     56  N   GLY A   8     -41.185  -3.668 -26.064  1.00 51.83           N  
ANISOU   56  N   GLY A   8     8055   5693   5946     80   -412    468       N  
ATOM     57  CA  GLY A   8     -40.547  -3.860 -27.338  1.00 49.55           C  
ANISOU   57  CA  GLY A   8     7940   5364   5524     30   -414    483       C  
ATOM     58  C   GLY A   8     -41.524  -3.633 -28.463  1.00 53.23           C  
ANISOU   58  C   GLY A   8     8481   5847   5898    116   -566    571       C  
ATOM     59  O   GLY A   8     -42.674  -3.241 -28.249  1.00 51.08           O  
ANISOU   59  O   GLY A   8     8112   5619   5676    226   -665    627       O  
ATOM     60  N   PRO A   9     -41.080  -3.883 -29.696  1.00 53.28           N  
ANISOU   60  N   PRO A   9     8654   5833   5756     77   -586    587       N  
ATOM     61  CA  PRO A   9     -41.939  -3.628 -30.858  1.00 54.89           C  
ANISOU   61  CA  PRO A   9     8957   6052   5845    155   -740    676       C  
ATOM     62  C   PRO A   9     -42.937  -4.739 -31.132  1.00 58.17           C  
ANISOU   62  C   PRO A   9     9262   6593   6247    134   -935    665       C  
ATOM     63  O   PRO A   9     -43.813  -4.559 -31.991  1.00 52.98           O  
ANISOU   63  O   PRO A   9     8647   5975   5506    198  -1096    743       O  
ATOM     64  CB  PRO A   9     -40.925  -3.514 -31.998  1.00 54.32           C  
ANISOU   64  CB  PRO A   9     9120   5918   5603    102   -661    687       C  
ATOM     65  CG  PRO A   9     -39.878  -4.517 -31.598  1.00 52.34           C  
ANISOU   65  CG  PRO A   9     8824   5695   5369    -12   -548    572       C  
ATOM     66  CD  PRO A   9     -39.746  -4.364 -30.102  1.00 52.25           C  
ANISOU   66  CD  PRO A   9     8633   5678   5542    -26   -463    526       C  
ATOM     67  N   GLY A  10     -42.824  -5.877 -30.451  1.00 48.96           N  
ANISOU   67  N   GLY A  10     7966   5484   5153     36   -938    578       N  
ATOM     68  CA  GLY A  10     -43.717  -6.994 -30.683  1.00 52.06           C  
ANISOU   68  CA  GLY A  10     8271   5978   5532    -24  -1129    567       C  
ATOM     69  C   GLY A  10     -43.298  -7.831 -31.876  1.00 52.69           C  
ANISOU   69  C   GLY A  10     8547   6033   5440    -94  -1198    520       C  
ATOM     70  O   GLY A  10     -43.008  -9.024 -31.736  1.00 51.95           O  
ANISOU   70  O   GLY A  10     8456   5942   5343   -193  -1222    433       O  
ATOM     71  N   ILE A  11     -43.281  -7.222 -33.061  1.00 51.87           N  
ANISOU   71  N   ILE A  11     8627   5900   5180    -35  -1233    579       N  
ATOM     72  CA  ILE A  11     -42.808  -7.889 -34.265  1.00 46.68           C  
ANISOU   72  CA  ILE A  11     8189   5220   4325    -82  -1274    531       C  
ATOM     73  C   ILE A  11     -41.720  -7.026 -34.888  1.00 52.88           C  
ANISOU   73  C   ILE A  11     9169   5930   4994    -37  -1092    556       C  
ATOM     74  O   ILE A  11     -41.608  -5.827 -34.616  1.00 52.14           O  
ANISOU   74  O   ILE A  11     9068   5791   4954     27   -997    636       O  
ATOM     75  CB  ILE A  11     -43.932  -8.156 -35.293  1.00 53.34           C  
ANISOU   75  CB  ILE A  11     9092   6131   5044    -80  -1531    584       C  
ATOM     76  CG1 ILE A  11     -44.746  -6.887 -35.557  1.00 52.68           C  
ANISOU   76  CG1 ILE A  11     8977   6076   4964     44  -1601    727       C  
ATOM     77  CG2 ILE A  11     -44.849  -9.259 -34.802  1.00 48.43           C  
ANISOU   77  CG2 ILE A  11     8300   5589   4512   -181  -1714    547       C  
ATOM     78  CD1 ILE A  11     -45.042  -6.667 -37.022  1.00 58.02           C  
ANISOU   78  CD1 ILE A  11     9867   6762   5416     80  -1741    791       C  
ATOM     79  N   LEU A  12     -40.925  -7.650 -35.753  1.00 56.48           N  
ANISOU   79  N   LEU A  12     9811   6371   5278    -73  -1044    489       N  
ATOM     80  CA  LEU A  12     -39.803  -6.970 -36.387  1.00 57.46           C  
ANISOU   80  CA  LEU A  12    10107   6454   5272    -54   -853    513       C  
ATOM     81  C   LEU A  12     -39.405  -7.731 -37.642  1.00 56.30           C  
ANISOU   81  C   LEU A  12    10181   6328   4883    -64   -876    454       C  
ATOM     82  O   LEU A  12     -39.324  -8.962 -37.625  1.00 61.27           O  
ANISOU   82  O   LEU A  12    10819   6970   5491    -98   -931    335       O  
ATOM     83  CB  LEU A  12     -38.612  -6.873 -35.425  1.00 68.84           C  
ANISOU   83  CB  LEU A  12    11450   7870   6836    -90   -619    458       C  
ATOM     84  CG  LEU A  12     -37.621  -5.729 -35.622  1.00 53.99           C  
ANISOU   84  CG  LEU A  12     9655   5949   4909    -95   -414    529       C  
ATOM     85  CD1 LEU A  12     -38.284  -4.363 -35.470  1.00 70.64           C  
ANISOU   85  CD1 LEU A  12    11770   7990   7080    -49   -454    661       C  
ATOM     86  CD2 LEU A  12     -36.464  -5.886 -34.660  1.00 52.07           C  
ANISOU   86  CD2 LEU A  12     9286   5713   4784   -152   -217    457       C  
ATOM     87  N   GLN A  13     -39.153  -6.996 -38.723  1.00 62.84           N  
ANISOU   87  N   GLN A  13    11206   7151   5520    -30   -834    536       N  
ATOM     88  CA  GLN A  13     -38.728  -7.655 -39.946  1.00 58.64           C  
ANISOU   88  CA  GLN A  13    10902   6651   4728    -27   -836    477       C  
ATOM     89  C   GLN A  13     -37.242  -8.001 -39.870  1.00 59.62           C  
ANISOU   89  C   GLN A  13    11054   6792   4808    -38   -574    389       C  
ATOM     90  O   GLN A  13     -36.481  -7.326 -39.176  1.00 60.04           O  
ANISOU   90  O   GLN A  13    10994   6835   4983    -60   -384    426       O  
ATOM     91  CB  GLN A  13     -39.002  -6.762 -41.155  1.00 67.35           C  
ANISOU   91  CB  GLN A  13    12214   7758   5618     12   -884    608       C  
ATOM     92  CG  GLN A  13     -40.484  -6.482 -41.364  1.00 70.66           C  
ANISOU   92  CG  GLN A  13    12607   8186   6055     46  -1164    698       C  
ATOM     93  CD  GLN A  13     -41.214  -7.638 -42.033  1.00 73.56           C  
ANISOU   93  CD  GLN A  13    13056   8602   6289     20  -1402    613       C  
ATOM     94  OE1 GLN A  13     -40.646  -8.352 -42.860  1.00 77.13           O  
ANISOU   94  OE1 GLN A  13    13710   9067   6529      7  -1369    520       O  
ATOM     95  NE2 GLN A  13     -42.470  -7.848 -41.646  1.00 74.12           N  
ANISOU   95  NE2 GLN A  13    12971   8708   6484      7  -1642    639       N  
ATOM     96  N   PRO A  14     -36.809  -9.063 -40.557  1.00 58.20           N  
ANISOU   96  N   PRO A  14    11018   6642   4453    -19   -566    268       N  
ATOM     97  CA  PRO A  14     -35.392  -9.440 -40.500  1.00 63.88           C  
ANISOU   97  CA  PRO A  14    11742   7404   5126      2   -313    182       C  
ATOM     98  C   PRO A  14     -34.528  -8.319 -41.050  1.00 58.89           C  
ANISOU   98  C   PRO A  14    11178   6821   4375     -6    -95    296       C  
ATOM     99  O   PRO A  14     -34.957  -7.559 -41.920  1.00 60.87           O  
ANISOU   99  O   PRO A  14    11585   7068   4475     -7   -152    412       O  
ATOM    100  CB  PRO A  14     -35.313 -10.681 -41.395  1.00 62.90           C  
ANISOU  100  CB  PRO A  14    11824   7292   4784     57   -381     41       C  
ATOM    101  CG  PRO A  14     -36.691 -11.213 -41.439  1.00 70.41           C  
ANISOU  101  CG  PRO A  14    12804   8186   5762     21   -690     23       C  
ATOM    102  CD  PRO A  14     -37.589 -10.006 -41.377  1.00 64.87           C  
ANISOU  102  CD  PRO A  14    12028   7484   5136    -10   -794    194       C  
ATOM    103  N   SER A  15     -33.301  -8.230 -40.523  1.00 56.94           N  
ANISOU  103  N   SER A  15    10810   6627   4197    -21    148    272       N  
ATOM    104  CA  SER A  15     -32.257  -7.248 -40.801  1.00 59.06           C  
ANISOU  104  CA  SER A  15    11085   6960   4394    -68    392    375       C  
ATOM    105  C   SER A  15     -32.469  -5.936 -40.041  1.00 58.45           C  
ANISOU  105  C   SER A  15    10896   6806   4506   -157    403    516       C  
ATOM    106  O   SER A  15     -31.569  -5.091 -40.044  1.00 63.57           O  
ANISOU  106  O   SER A  15    11524   7489   5140   -234    600    604       O  
ATOM    107  CB  SER A  15     -32.094  -6.928 -42.302  1.00 61.65           C  
ANISOU  107  CB  SER A  15    11672   7347   4404    -48    443    445       C  
ATOM    108  OG  SER A  15     -31.481  -5.664 -42.451  1.00 73.20           O  
ANISOU  108  OG  SER A  15    13142   8830   5841   -137    616    604       O  
ATOM    109  N   GLN A  16     -33.612  -5.732 -39.387  1.00 58.21           N  
ANISOU  109  N   GLN A  16    10795   6677   4645   -151    203    539       N  
ATOM    110  CA  GLN A  16     -33.869  -4.513 -38.640  1.00 57.77           C  
ANISOU  110  CA  GLN A  16    10656   6532   4761   -204    208    653       C  
ATOM    111  C   GLN A  16     -33.218  -4.581 -37.264  1.00 51.90           C  
ANISOU  111  C   GLN A  16     9680   5791   4249   -258    321    590       C  
ATOM    112  O   GLN A  16     -32.729  -5.623 -36.825  1.00 54.86           O  
ANISOU  112  O   GLN A  16     9940   6232   4671   -241    364    464       O  
ATOM    113  CB  GLN A  16     -35.370  -4.276 -38.508  1.00 55.60           C  
ANISOU  113  CB  GLN A  16    10386   6176   4562   -145    -43    701       C  
ATOM    114  CG  GLN A  16     -36.039  -3.994 -39.839  1.00 61.40           C  
ANISOU  114  CG  GLN A  16    11351   6908   5072    -95   -172    793       C  
ATOM    115  CD  GLN A  16     -37.471  -3.533 -39.695  1.00 72.44           C  
ANISOU  115  CD  GLN A  16    12727   8243   6552    -28   -409    871       C  
ATOM    116  OE1 GLN A  16     -38.196  -3.966 -38.795  1.00 69.79           O  
ANISOU  116  OE1 GLN A  16    12205   7908   6403     -6   -528    812       O  
ATOM    117  NE2 GLN A  16     -37.888  -2.641 -40.584  1.00 77.10           N  
ANISOU  117  NE2 GLN A  16    13502   8792   6999     12   -476   1014       N  
ATOM    118  N   THR A  17     -33.205  -3.444 -36.584  1.00 49.85           N  
ANISOU  118  N   THR A  17     9369   5449   4125   -318    362    679       N  
ATOM    119  CA  THR A  17     -32.604  -3.329 -35.263  1.00 49.92           C  
ANISOU  119  CA  THR A  17     9175   5453   4340   -384    460    630       C  
ATOM    120  C   THR A  17     -33.687  -3.475 -34.203  1.00 49.57           C  
ANISOU  120  C   THR A  17     9001   5341   4491   -330    295    589       C  
ATOM    121  O   THR A  17     -34.741  -2.837 -34.290  1.00 52.61           O  
ANISOU  121  O   THR A  17     9448   5642   4897   -276    160    664       O  
ATOM    122  CB  THR A  17     -31.875  -1.993 -35.102  1.00 50.67           C  
ANISOU  122  CB  THR A  17     9308   5489   4457   -502    606    741       C  
ATOM    123  OG1 THR A  17     -30.733  -1.976 -35.969  1.00 54.54           O  
ANISOU  123  OG1 THR A  17     9866   6084   4772   -575    788    777       O  
ATOM    124  CG2 THR A  17     -31.413  -1.802 -33.666  1.00 47.62           C  
ANISOU  124  CG2 THR A  17     8725   5083   4285   -575    666    688       C  
ATOM    125  N   LEU A  18     -33.428  -4.324 -33.216  1.00 43.26           N  
ANISOU  125  N   LEU A  18     8018   4592   3826   -336    307    478       N  
ATOM    126  CA  LEU A  18     -34.342  -4.527 -32.100  1.00 45.38           C  
ANISOU  126  CA  LEU A  18     8142   4823   4277   -302    180    439       C  
ATOM    127  C   LEU A  18     -33.989  -3.528 -31.005  1.00 49.90           C  
ANISOU  127  C   LEU A  18     8627   5334   4998   -363    269    466       C  
ATOM    128  O   LEU A  18     -32.836  -3.473 -30.566  1.00 55.77           O  
ANISOU  128  O   LEU A  18     9300   6115   5772   -449    417    436       O  
ATOM    129  CB  LEU A  18     -34.253  -5.964 -31.584  1.00 47.25           C  
ANISOU  129  CB  LEU A  18     8252   5132   4569   -287    142    316       C  
ATOM    130  CG  LEU A  18     -35.144  -6.322 -30.379  1.00 48.99           C  
ANISOU  130  CG  LEU A  18     8308   5338   4968   -272     23    280       C  
ATOM    131  CD1 LEU A  18     -36.614  -6.036 -30.667  1.00 48.84           C  
ANISOU  131  CD1 LEU A  18     8318   5289   4950   -213   -158    344       C  
ATOM    132  CD2 LEU A  18     -34.944  -7.767 -29.942  1.00 42.06           C  
ANISOU  132  CD2 LEU A  18     7342   4511   4126   -273    -10    173       C  
ATOM    133  N   SER A  19     -34.968  -2.716 -30.591  1.00 44.04           N  
ANISOU  133  N   SER A  19     7894   4501   4338   -313    175    521       N  
ATOM    134  CA  SER A  19     -34.798  -1.752 -29.502  1.00 45.96           C  
ANISOU  134  CA  SER A  19     8086   4660   4715   -351    236    531       C  
ATOM    135  C   SER A  19     -35.746  -2.135 -28.374  1.00 45.64           C  
ANISOU  135  C   SER A  19     7882   4637   4822   -279    134    474       C  
ATOM    136  O   SER A  19     -36.968  -2.052 -28.527  1.00 46.63           O  
ANISOU  136  O   SER A  19     8009   4752   4957   -172     -1    511       O  
ATOM    137  CB  SER A  19     -35.060  -0.318 -29.961  1.00 49.14           C  
ANISOU  137  CB  SER A  19     8676   4920   5074   -335    237    648       C  
ATOM    138  OG  SER A  19     -34.298  -0.008 -31.107  1.00 55.86           O  
ANISOU  138  OG  SER A  19     9688   5768   5767   -408    324    721       O  
ATOM    139  N   LEU A  20     -35.176  -2.560 -27.257  1.00 42.64           N  
ANISOU  139  N   LEU A  20     7353   4302   4548   -339    198    391       N  
ATOM    140  CA  LEU A  20     -35.914  -2.998 -26.085  1.00 38.14           C  
ANISOU  140  CA  LEU A  20     6618   3767   4105   -294    128    336       C  
ATOM    141  C   LEU A  20     -35.723  -1.978 -24.973  1.00 38.31           C  
ANISOU  141  C   LEU A  20     6622   3712   4224   -315    196    325       C  
ATOM    142  O   LEU A  20     -34.700  -1.297 -24.911  1.00 38.75           O  
ANISOU  142  O   LEU A  20     6747   3710   4266   -413    306    330       O  
ATOM    143  CB  LEU A  20     -35.409  -4.362 -25.632  1.00 41.28           C  
ANISOU  143  CB  LEU A  20     6880   4271   4532   -342    138    250       C  
ATOM    144  CG  LEU A  20     -35.654  -5.509 -26.625  1.00 41.72           C  
ANISOU  144  CG  LEU A  20     6974   4385   4494   -316     54    237       C  
ATOM    145  CD1 LEU A  20     -34.675  -6.657 -26.352  1.00 39.04           C  
ANISOU  145  CD1 LEU A  20     6564   4112   4155   -361    112    154       C  
ATOM    146  CD2 LEU A  20     -37.094  -6.008 -26.550  1.00 51.89           C  
ANISOU  146  CD2 LEU A  20     8200   5700   5815   -254   -116    252       C  
ATOM    147  N   THR A  21     -36.714  -1.880 -24.087  1.00 42.08           N  
ANISOU  147  N   THR A  21     7006   4194   4790   -228    131    309       N  
ATOM    148  CA  THR A  21     -36.685  -0.934 -22.976  1.00 38.13           C  
ANISOU  148  CA  THR A  21     6506   3614   4367   -220    184    282       C  
ATOM    149  C   THR A  21     -37.150  -1.671 -21.733  1.00 42.36           C  
ANISOU  149  C   THR A  21     6848   4254   4992   -196    159    214       C  
ATOM    150  O   THR A  21     -38.125  -2.427 -21.793  1.00 38.16           O  
ANISOU  150  O   THR A  21     6208   3818   4474   -127     65    228       O  
ATOM    151  CB  THR A  21     -37.562   0.300 -23.249  1.00 45.50           C  
ANISOU  151  CB  THR A  21     7577   4421   5291    -88    143    348       C  
ATOM    152  OG1 THR A  21     -37.106   0.982 -24.433  1.00 44.24           O  
ANISOU  152  OG1 THR A  21     7618   4154   5035   -123    164    428       O  
ATOM    153  CG2 THR A  21     -37.523   1.273 -22.080  1.00 45.79           C  
ANISOU  153  CG2 THR A  21     7648   4355   5396    -65    199    301       C  
ATOM    154  N   CYS A  22     -36.392  -1.516 -20.645  1.00 36.39           N  
ANISOU  154  N   CYS A  22     6049   3493   4286   -277    238    148       N  
ATOM    155  CA  CYS A  22     -36.723  -2.036 -19.320  1.00 37.26           C  
ANISOU  155  CA  CYS A  22     6001   3690   4466   -264    231     87       C  
ATOM    156  C   CYS A  22     -37.053  -0.833 -18.451  1.00 42.93           C  
ANISOU  156  C   CYS A  22     6784   4314   5214   -198    268     60       C  
ATOM    157  O   CYS A  22     -36.175  -0.017 -18.146  1.00 43.93           O  
ANISOU  157  O   CYS A  22     7022   4336   5334   -282    336     28       O  
ATOM    158  CB  CYS A  22     -35.554  -2.831 -18.738  1.00 35.21           C  
ANISOU  158  CB  CYS A  22     5654   3503   4222   -397    282     29       C  
ATOM    159  SG  CYS A  22     -35.780  -3.467 -17.075  1.00 45.13           S  
ANISOU  159  SG  CYS A  22     6741   4863   5542   -403    278    -36       S  
ATOM    160  N   SER A  23     -38.314  -0.708 -18.065  1.00 43.44           N  
ANISOU  160  N   SER A  23     6783   4418   5303    -48    222     71       N  
ATOM    161  CA  SER A  23     -38.747   0.381 -17.207  1.00 41.26           C  
ANISOU  161  CA  SER A  23     6573   4060   5045     59    261     33       C  
ATOM    162  C   SER A  23     -38.868  -0.179 -15.799  1.00 46.44           C  
ANISOU  162  C   SER A  23     7072   4840   5734     45    290    -37       C  
ATOM    163  O   SER A  23     -39.489  -1.225 -15.605  1.00 44.97           O  
ANISOU  163  O   SER A  23     6704   4816   5568     58    247    -16       O  
ATOM    164  CB  SER A  23     -40.082   0.944 -17.688  1.00 45.26           C  
ANISOU  164  CB  SER A  23     7098   4550   5547    270    202     95       C  
ATOM    165  OG  SER A  23     -39.984   1.393 -19.026  1.00 53.15           O  
ANISOU  165  OG  SER A  23     8250   5442   6501    280    162    173       O  
ATOM    166  N   PHE A  24     -38.237   0.475 -14.827  1.00 39.45           N  
ANISOU  166  N   PHE A  24     6266   3878   4844     -1    357   -117       N  
ATOM    167  CA  PHE A  24     -38.200  -0.091 -13.488  1.00 41.04           C  
ANISOU  167  CA  PHE A  24     6335   4202   5056    -34    385   -183       C  
ATOM    168  C   PHE A  24     -38.671   0.936 -12.471  1.00 39.89           C  
ANISOU  168  C   PHE A  24     6273   3992   4890     89    435   -255       C  
ATOM    169  O   PHE A  24     -38.662   2.145 -12.714  1.00 40.22           O  
ANISOU  169  O   PHE A  24     6515   3851   4915    158    452   -272       O  
ATOM    170  CB  PHE A  24     -36.808  -0.619 -13.102  1.00 41.71           C  
ANISOU  170  CB  PHE A  24     6401   4309   5140   -237    406   -225       C  
ATOM    171  CG  PHE A  24     -35.699   0.388 -13.223  1.00 42.80           C  
ANISOU  171  CG  PHE A  24     6718   4285   5258   -350    445   -262       C  
ATOM    172  CD1 PHE A  24     -35.417   1.255 -12.182  1.00 40.66           C  
ANISOU  172  CD1 PHE A  24     6552   3930   4966   -371    480   -347       C  
ATOM    173  CD2 PHE A  24     -34.895   0.428 -14.360  1.00 48.22           C  
ANISOU  173  CD2 PHE A  24     7469   4914   5937   -455    446   -210       C  
ATOM    174  CE1 PHE A  24     -34.390   2.193 -12.285  1.00 44.71           C  
ANISOU  174  CE1 PHE A  24     7239   4288   5462   -512    500   -376       C  
ATOM    175  CE2 PHE A  24     -33.860   1.338 -14.459  1.00 42.58           C  
ANISOU  175  CE2 PHE A  24     6903   4069   5204   -592    483   -227       C  
ATOM    176  CZ  PHE A  24     -33.613   2.237 -13.424  1.00 45.71           C  
ANISOU  176  CZ  PHE A  24     7410   4368   5591   -632    503   -308       C  
ATOM    177  N   SER A  25     -39.116   0.431 -11.323  1.00 40.46           N  
ANISOU  177  N   SER A  25     6206   4211   4955    124    460   -294       N  
ATOM    178  CA  SER A  25     -39.495   1.306 -10.226  1.00 40.32           C  
ANISOU  178  CA  SER A  25     6268   4154   4897    244    521   -381       C  
ATOM    179  C   SER A  25     -39.077   0.662  -8.913  1.00 39.42           C  
ANISOU  179  C   SER A  25     6056   4170   4750    143    552   -444       C  
ATOM    180  O   SER A  25     -38.804  -0.536  -8.843  1.00 37.28           O  
ANISOU  180  O   SER A  25     5625   4040   4499     24    522   -401       O  
ATOM    181  CB  SER A  25     -41.006   1.598 -10.221  1.00 51.15           C  
ANISOU  181  CB  SER A  25     7564   5605   6268    499    533   -349       C  
ATOM    182  OG  SER A  25     -41.741   0.400 -10.042  1.00 54.65           O  
ANISOU  182  OG  SER A  25     7744   6291   6731    497    513   -282       O  
ATOM    183  N   GLY A  26     -39.022   1.481  -7.862  1.00 39.08           N  
ANISOU  183  N   GLY A  26     6135   4065   4647    197    607   -549       N  
ATOM    184  CA  GLY A  26     -38.712   0.993  -6.537  1.00 45.13           C  
ANISOU  184  CA  GLY A  26     6832   4957   5358    122    636   -612       C  
ATOM    185  C   GLY A  26     -37.255   1.090  -6.146  1.00 49.71           C  
ANISOU  185  C   GLY A  26     7515   5456   5917    -95    612   -676       C  
ATOM    186  O   GLY A  26     -36.921   0.793  -4.996  1.00 43.58           O  
ANISOU  186  O   GLY A  26     6707   4771   5080   -159    623   -735       O  
ATOM    187  N   PHE A  27     -36.382   1.491  -7.065  1.00 42.70           N  
ANISOU  187  N   PHE A  27     6737   4417   5070   -214    577   -658       N  
ATOM    188  CA  PHE A  27     -34.968   1.680  -6.773  1.00 42.48           C  
ANISOU  188  CA  PHE A  27     6787   4326   5027   -433    551   -710       C  
ATOM    189  C   PHE A  27     -34.392   2.604  -7.840  1.00 47.16           C  
ANISOU  189  C   PHE A  27     7557   4712   5650   -507    540   -690       C  
ATOM    190  O   PHE A  27     -35.049   2.912  -8.836  1.00 38.56           O  
ANISOU  190  O   PHE A  27     6516   3544   4592   -390    544   -626       O  
ATOM    191  CB  PHE A  27     -34.221   0.337  -6.707  1.00 38.28           C  
ANISOU  191  CB  PHE A  27     6052   3972   4522   -577    513   -658       C  
ATOM    192  CG  PHE A  27     -33.967  -0.278  -8.046  1.00 39.62           C  
ANISOU  192  CG  PHE A  27     6140   4152   4761   -618    489   -559       C  
ATOM    193  CD1 PHE A  27     -34.978  -0.963  -8.700  1.00 36.32           C  
ANISOU  193  CD1 PHE A  27     5615   3807   4377   -494    481   -480       C  
ATOM    194  CD2 PHE A  27     -32.734  -0.126  -8.689  1.00 36.36           C  
ANISOU  194  CD2 PHE A  27     5763   3684   4369   -782    476   -544       C  
ATOM    195  CE1 PHE A  27     -34.769  -1.522  -9.940  1.00 40.58           C  
ANISOU  195  CE1 PHE A  27     6108   4349   4960   -525    453   -401       C  
ATOM    196  CE2 PHE A  27     -32.526  -0.683  -9.911  1.00 42.14           C  
ANISOU  196  CE2 PHE A  27     6433   4436   5143   -799    468   -461       C  
ATOM    197  CZ  PHE A  27     -33.536  -1.378 -10.547  1.00 42.39           C  
ANISOU  197  CZ  PHE A  27     6385   4522   5198   -667    453   -396       C  
ATOM    198  N   SER A  28     -33.169   3.068  -7.610  1.00 42.99           N  
ANISOU  198  N   SER A  28     7126   4103   5104   -712    520   -736       N  
ATOM    199  CA  SER A  28     -32.450   3.859  -8.602  1.00 41.62           C  
ANISOU  199  CA  SER A  28     7104   3756   4955   -840    512   -699       C  
ATOM    200  C   SER A  28     -31.248   3.070  -9.101  1.00 44.49           C  
ANISOU  200  C   SER A  28     7304   4245   5353  -1043    495   -638       C  
ATOM    201  O   SER A  28     -30.474   2.533  -8.302  1.00 40.97           O  
ANISOU  201  O   SER A  28     6741   3931   4894  -1166    471   -675       O  
ATOM    202  CB  SER A  28     -31.998   5.203  -8.025  1.00 42.95           C  
ANISOU  202  CB  SER A  28     7540   3708   5072   -935    502   -796       C  
ATOM    203  OG  SER A  28     -31.153   5.889  -8.940  1.00 49.60           O  
ANISOU  203  OG  SER A  28     8512   4399   5935  -1116    491   -743       O  
ATOM    204  N   LEU A  29     -31.088   3.006 -10.421  1.00 42.49           N  
ANISOU  204  N   LEU A  29     7047   3962   5135  -1064    508   -542       N  
ATOM    205  CA  LEU A  29     -29.882   2.405 -10.970  1.00 49.71           C  
ANISOU  205  CA  LEU A  29     7827   4990   6070  -1243    511   -488       C  
ATOM    206  C   LEU A  29     -28.629   3.225 -10.690  1.00 53.16           C  
ANISOU  206  C   LEU A  29     8349   5360   6490  -1490    504   -519       C  
ATOM    207  O   LEU A  29     -27.530   2.707 -10.888  1.00 57.06           O  
ANISOU  207  O   LEU A  29     8690   5994   6998  -1645    508   -485       O  
ATOM    208  CB  LEU A  29     -30.050   2.177 -12.473  1.00 50.48           C  
ANISOU  208  CB  LEU A  29     7919   5077   6186  -1196    537   -383       C  
ATOM    209  CG  LEU A  29     -29.057   1.232 -13.148  1.00 50.98           C  
ANISOU  209  CG  LEU A  29     7804   5305   6262  -1299    556   -325       C  
ATOM    210  CD1 LEU A  29     -28.837  -0.045 -12.374  1.00 40.12           C  
ANISOU  210  CD1 LEU A  29     6212   4128   4904  -1274    528   -356       C  
ATOM    211  CD2 LEU A  29     -29.569   0.909 -14.535  1.00 47.11           C  
ANISOU  211  CD2 LEU A  29     7330   4804   5766  -1195    575   -239       C  
ATOM    212  N   SER A  30     -28.755   4.469 -10.222  1.00 47.70           N  
ANISOU  212  N   SER A  30     7895   4462   5765  -1533    491   -582       N  
ATOM    213  CA  SER A  30     -27.592   5.229  -9.792  1.00 50.39           C  
ANISOU  213  CA  SER A  30     8323   4739   6085  -1800    462   -622       C  
ATOM    214  C   SER A  30     -27.092   4.831  -8.404  1.00 51.37           C  
ANISOU  214  C   SER A  30     8336   5001   6180  -1881    410   -717       C  
ATOM    215  O   SER A  30     -25.999   5.257  -8.016  1.00 49.02           O  
ANISOU  215  O   SER A  30     8051   4709   5866  -2128    368   -744       O  
ATOM    216  CB  SER A  30     -27.899   6.733  -9.819  1.00 55.04           C  
ANISOU  216  CB  SER A  30     9254   5018   6641  -1826    452   -659       C  
ATOM    217  OG  SER A  30     -28.713   7.124  -8.718  1.00 62.03           O  
ANISOU  217  OG  SER A  30    10278   5810   7482  -1673    430   -781       O  
ATOM    218  N   THR A  31     -27.854   4.049  -7.637  1.00 48.94           N  
ANISOU  218  N   THR A  31     7924   4811   5858  -1695    405   -762       N  
ATOM    219  CA  THR A  31     -27.382   3.618  -6.325  1.00 48.57           C  
ANISOU  219  CA  THR A  31     7779   4907   5768  -1767    351   -839       C  
ATOM    220  C   THR A  31     -26.208   2.653  -6.439  1.00 40.34           C  
ANISOU  220  C   THR A  31     6474   4094   4761  -1912    324   -779       C  
ATOM    221  O   THR A  31     -26.215   1.730  -7.249  1.00 38.54           O  
ANISOU  221  O   THR A  31     6076   3984   4584  -1835    358   -692       O  
ATOM    222  CB  THR A  31     -28.523   2.983  -5.514  1.00 44.42           C  
ANISOU  222  CB  THR A  31     7205   4463   5209  -1536    363   -881       C  
ATOM    223  OG1 THR A  31     -29.598   3.928  -5.367  1.00 43.98           O  
ANISOU  223  OG1 THR A  31     7380   4216   5117  -1376    397   -943       O  
ATOM    224  CG2 THR A  31     -28.025   2.500  -4.163  1.00 49.69           C  
ANISOU  224  CG2 THR A  31     7780   5284   5814  -1611    306   -949       C  
ATOM    225  N   SER A  31A    -25.189   2.896  -5.621  1.00 46.74           N  
ANISOU  225  N   SER A  31A    7259   4965   5536  -2117    256   -831       N  
ATOM    226  CA  SER A  31A    -23.985   2.079  -5.620  1.00 45.59           C  
ANISOU  226  CA  SER A  31A    6853   5051   5418  -2251    221   -778       C  
ATOM    227  C   SER A  31A    -24.319   0.597  -5.458  1.00 45.31           C  
ANISOU  227  C   SER A  31A    6603   5211   5403  -2063    224   -737       C  
ATOM    228  O   SER A  31A    -25.031   0.198  -4.527  1.00 41.72           O  
ANISOU  228  O   SER A  31A    6163   4785   4903  -1938    201   -785       O  
ATOM    229  CB  SER A  31A    -23.057   2.564  -4.498  1.00 55.94           C  
ANISOU  229  CB  SER A  31A    8178   6406   6670  -2474    122   -856       C  
ATOM    230  OG  SER A  31A    -21.819   1.878  -4.480  1.00 68.98           O  
ANISOU  230  OG  SER A  31A    9562   8298   8348  -2609     77   -800       O  
ATOM    231  N   GLY A  31B    -23.829  -0.214  -6.396  1.00 49.13           N  
ANISOU  231  N   GLY A  31B    6902   5820   5946  -2040    259   -644       N  
ATOM    232  CA  GLY A  31B    -23.998  -1.652  -6.368  1.00 42.52           C  
ANISOU  232  CA  GLY A  31B    5880   5144   5131  -1879    253   -599       C  
ATOM    233  C   GLY A  31B    -25.179  -2.188  -7.147  1.00 39.12           C  
ANISOU  233  C   GLY A  31B    5488   4645   4729  -1673    309   -556       C  
ATOM    234  O   GLY A  31B    -25.362  -3.412  -7.193  1.00 40.01           O  
ANISOU  234  O   GLY A  31B    5474   4868   4862  -1550    297   -516       O  
ATOM    235  N   MET A  32     -25.995  -1.323  -7.748  1.00 36.81           N  
ANISOU  235  N   MET A  32     5376   4174   4438  -1632    357   -562       N  
ATOM    236  CA  MET A  32     -27.127  -1.795  -8.533  1.00 35.58           C  
ANISOU  236  CA  MET A  32     5244   3968   4306  -1447    395   -515       C  
ATOM    237  C   MET A  32     -26.664  -2.129  -9.953  1.00 37.89           C  
ANISOU  237  C   MET A  32     5478   4284   4632  -1452    439   -438       C  
ATOM    238  O   MET A  32     -25.720  -1.523 -10.477  1.00 38.96           O  
ANISOU  238  O   MET A  32     5622   4412   4768  -1598    469   -418       O  
ATOM    239  CB  MET A  32     -28.216  -0.725  -8.600  1.00 40.23           C  
ANISOU  239  CB  MET A  32     6041   4369   4877  -1372    420   -547       C  
ATOM    240  CG  MET A  32     -28.882  -0.416  -7.280  1.00 37.19           C  
ANISOU  240  CG  MET A  32     5727   3963   4442  -1315    398   -629       C  
ATOM    241  SD  MET A  32     -29.939  -1.764  -6.764  1.00 41.71           S  
ANISOU  241  SD  MET A  32     6153   4682   5014  -1136    388   -600       S  
ATOM    242  CE  MET A  32     -30.446  -1.226  -5.107  1.00 41.12           C  
ANISOU  242  CE  MET A  32     6169   4607   4847  -1106    382   -704       C  
ATOM    243  N   GLY A  33     -27.353  -3.077 -10.582  1.00 34.85           N  
ANISOU  243  N   GLY A  33     5046   3931   4266  -1301    445   -393       N  
ATOM    244  CA  GLY A  33     -27.124  -3.379 -11.986  1.00 36.94           C  
ANISOU  244  CA  GLY A  33     5296   4200   4539  -1275    489   -330       C  
ATOM    245  C   GLY A  33     -28.318  -4.104 -12.555  1.00 37.16           C  
ANISOU  245  C   GLY A  33     5345   4199   4573  -1108    472   -299       C  
ATOM    246  O   GLY A  33     -29.146  -4.648 -11.814  1.00 37.00           O  
ANISOU  246  O   GLY A  33     5296   4200   4561  -1025    426   -314       O  
ATOM    247  N   VAL A  34     -28.406  -4.114 -13.885  1.00 34.72           N  
ANISOU  247  N   VAL A  34     5089   3853   4253  -1073    505   -250       N  
ATOM    248  CA  VAL A  34     -29.529  -4.737 -14.585  1.00 30.09           C  
ANISOU  248  CA  VAL A  34     4535   3236   3663   -936    474   -218       C  
ATOM    249  C   VAL A  34     -28.999  -5.509 -15.782  1.00 37.78           C  
ANISOU  249  C   VAL A  34     5483   4263   4610   -909    497   -184       C  
ATOM    250  O   VAL A  34     -28.168  -4.989 -16.541  1.00 33.96           O  
ANISOU  250  O   VAL A  34     5027   3781   4094   -980    565   -161       O  
ATOM    251  CB  VAL A  34     -30.569  -3.689 -15.046  1.00 37.63           C  
ANISOU  251  CB  VAL A  34     5641   4051   4606   -885    475   -196       C  
ATOM    252  CG1 VAL A  34     -31.651  -4.357 -15.913  1.00 39.77           C  
ANISOU  252  CG1 VAL A  34     5926   4317   4868   -760    428   -152       C  
ATOM    253  CG2 VAL A  34     -31.195  -2.970 -13.853  1.00 40.67           C  
ANISOU  253  CG2 VAL A  34     6064   4384   5007   -868    461   -242       C  
ATOM    254  N   SER A  35     -29.501  -6.737 -15.965  1.00 37.07           N  
ANISOU  254  N   SER A  35     5351   4210   4522   -811    442   -179       N  
ATOM    255  CA  SER A  35     -29.137  -7.602 -17.074  1.00 36.08           C  
ANISOU  255  CA  SER A  35     5232   4120   4357   -756    452   -165       C  
ATOM    256  C   SER A  35     -30.296  -7.719 -18.048  1.00 40.32           C  
ANISOU  256  C   SER A  35     5879   4579   4861   -680    403   -134       C  
ATOM    257  O   SER A  35     -31.463  -7.630 -17.670  1.00 37.35           O  
ANISOU  257  O   SER A  35     5518   4160   4512   -646    338   -122       O  
ATOM    258  CB  SER A  35     -28.790  -9.005 -16.599  1.00 34.65           C  
ANISOU  258  CB  SER A  35     4956   4017   4194   -700    405   -188       C  
ATOM    259  OG  SER A  35     -27.414  -9.163 -16.373  1.00 38.87           O  
ANISOU  259  OG  SER A  35     5387   4655   4727   -731    461   -205       O  
ATOM    260  N   TRP A  36     -29.959  -7.957 -19.308  1.00 36.76           N  
ANISOU  260  N   TRP A  36     5494   4130   4343   -649    435   -119       N  
ATOM    261  CA  TRP A  36     -30.920  -8.408 -20.297  1.00 33.63           C  
ANISOU  261  CA  TRP A  36     5197   3682   3898   -574    366    -98       C  
ATOM    262  C   TRP A  36     -30.665  -9.889 -20.571  1.00 36.63           C  
ANISOU  262  C   TRP A  36     5566   4100   4252   -510    323   -134       C  
ATOM    263  O   TRP A  36     -29.511 -10.317 -20.697  1.00 37.62           O  
ANISOU  263  O   TRP A  36     5648   4291   4353   -493    393   -163       O  
ATOM    264  CB  TRP A  36     -30.765  -7.606 -21.596  1.00 39.30           C  
ANISOU  264  CB  TRP A  36     6039   4363   4529   -580    425    -57       C  
ATOM    265  CG  TRP A  36     -31.495  -6.310 -21.589  1.00 36.87           C  
ANISOU  265  CG  TRP A  36     5808   3966   4234   -602    418    -10       C  
ATOM    266  CD1 TRP A  36     -30.951  -5.069 -21.381  1.00 41.23           C  
ANISOU  266  CD1 TRP A  36     6395   4476   4795   -685    497     12       C  
ATOM    267  CD2 TRP A  36     -32.898  -6.107 -21.777  1.00 36.40           C  
ANISOU  267  CD2 TRP A  36     5804   3845   4181   -534    319     23       C  
ATOM    268  NE1 TRP A  36     -31.930  -4.108 -21.447  1.00 39.57           N  
ANISOU  268  NE1 TRP A  36     6284   4158   4592   -651    457     51       N  
ATOM    269  CE2 TRP A  36     -33.135  -4.715 -21.685  1.00 38.99           C  
ANISOU  269  CE2 TRP A  36     6208   4087   4519   -548    351     61       C  
ATOM    270  CE3 TRP A  36     -33.979  -6.962 -22.011  1.00 41.65           C  
ANISOU  270  CE3 TRP A  36     6459   4524   4844   -468    201     28       C  
ATOM    271  CZ2 TRP A  36     -34.406  -4.161 -21.838  1.00 39.02           C  
ANISOU  271  CZ2 TRP A  36     6268   4029   4530   -463    275    104       C  
ATOM    272  CZ3 TRP A  36     -35.240  -6.414 -22.163  1.00 37.94           C  
ANISOU  272  CZ3 TRP A  36     6018   4015   4383   -411    122     76       C  
ATOM    273  CH2 TRP A  36     -35.446  -5.032 -22.068  1.00 35.97           C  
ANISOU  273  CH2 TRP A  36     5832   3691   4143   -392    163    113       C  
ATOM    274  N   ILE A  37     -31.749 -10.655 -20.682  1.00 34.35           N  
ANISOU  274  N   ILE A  37     5317   3767   3966   -472    206   -130       N  
ATOM    275  CA  ILE A  37     -31.749 -12.107 -20.842  1.00 35.80           C  
ANISOU  275  CA  ILE A  37     5530   3942   4132   -422    131   -164       C  
ATOM    276  C   ILE A  37     -32.829 -12.446 -21.856  1.00 34.06           C  
ANISOU  276  C   ILE A  37     5433   3659   3851   -402     25   -148       C  
ATOM    277  O   ILE A  37     -33.801 -11.705 -22.015  1.00 37.64           O  
ANISOU  277  O   ILE A  37     5894   4095   4311   -426    -17   -101       O  
ATOM    278  CB  ILE A  37     -32.010 -12.837 -19.485  1.00 33.63           C  
ANISOU  278  CB  ILE A  37     5157   3678   3943   -446     64   -166       C  
ATOM    279  CG1 ILE A  37     -30.958 -12.474 -18.441  1.00 36.15           C  
ANISOU  279  CG1 ILE A  37     5356   4070   4311   -470    149   -180       C  
ATOM    280  CG2 ILE A  37     -32.161 -14.351 -19.626  1.00 36.54           C  
ANISOU  280  CG2 ILE A  37     5592   3997   4294   -407    -37   -189       C  
ATOM    281  CD1 ILE A  37     -31.563 -12.204 -17.040  1.00 37.91           C  
ANISOU  281  CD1 ILE A  37     5484   4313   4607   -529    114   -158       C  
ATOM    282  N   ARG A  38     -32.673 -13.568 -22.553  1.00 36.76           N  
ANISOU  282  N   ARG A  38     5877   3965   4126   -351    -27   -190       N  
ATOM    283  CA  ARG A  38     -33.718 -13.964 -23.477  1.00 34.53           C  
ANISOU  283  CA  ARG A  38     5720   3623   3779   -354   -154   -181       C  
ATOM    284  C   ARG A  38     -33.864 -15.483 -23.498  1.00 37.85           C  
ANISOU  284  C   ARG A  38     6226   3974   4183   -341   -269   -228       C  
ATOM    285  O   ARG A  38     -32.926 -16.232 -23.205  1.00 37.69           O  
ANISOU  285  O   ARG A  38     6215   3943   4163   -281   -225   -279       O  
ATOM    286  CB  ARG A  38     -33.439 -13.432 -24.894  1.00 38.16           C  
ANISOU  286  CB  ARG A  38     6312   4081   4107   -309   -100   -186       C  
ATOM    287  CG  ARG A  38     -32.283 -14.130 -25.624  1.00 40.05           C  
ANISOU  287  CG  ARG A  38     6648   4326   4242   -220    -18   -259       C  
ATOM    288  CD  ARG A  38     -32.163 -13.609 -27.054  1.00 40.15           C  
ANISOU  288  CD  ARG A  38     6803   4350   4103   -185     32   -253       C  
ATOM    289  NE  ARG A  38     -31.100 -14.285 -27.792  1.00 41.57           N  
ANISOU  289  NE  ARG A  38     7075   4556   4163    -81    124   -327       N  
ATOM    290  CZ  ARG A  38     -30.752 -13.983 -29.034  1.00 47.76           C  
ANISOU  290  CZ  ARG A  38     7988   5372   4788    -34    200   -332       C  
ATOM    291  NH1 ARG A  38     -31.361 -13.018 -29.703  1.00 47.18           N  
ANISOU  291  NH1 ARG A  38     7977   5294   4654    -88    183   -260       N  
ATOM    292  NH2 ARG A  38     -29.787 -14.684 -29.626  1.00 49.80           N  
ANISOU  292  NH2 ARG A  38     8319   5670   4933     82    295   -409       N  
ATOM    293  N   GLN A  39     -35.062 -15.926 -23.859  1.00 37.67           N  
ANISOU  293  N   GLN A  39     6269   3901   4143   -399   -426   -205       N  
ATOM    294  CA  GLN A  39     -35.348 -17.343 -24.075  1.00 37.46           C  
ANISOU  294  CA  GLN A  39     6374   3776   4083   -415   -564   -246       C  
ATOM    295  C   GLN A  39     -35.824 -17.538 -25.502  1.00 48.71           C  
ANISOU  295  C   GLN A  39     7985   5149   5374   -407   -657   -275       C  
ATOM    296  O   GLN A  39     -37.006 -17.286 -25.804  1.00 45.57           O  
ANISOU  296  O   GLN A  39     7575   4766   4974   -491   -781   -220       O  
ATOM    297  CB  GLN A  39     -36.394 -17.853 -23.091  1.00 40.80           C  
ANISOU  297  CB  GLN A  39     6706   4190   4608   -538   -693   -185       C  
ATOM    298  CG  GLN A  39     -36.668 -19.335 -23.257  1.00 39.11           C  
ANISOU  298  CG  GLN A  39     6650   3848   4363   -585   -847   -219       C  
ATOM    299  CD  GLN A  39     -37.082 -19.980 -21.970  1.00 41.34           C  
ANISOU  299  CD  GLN A  39     6838   4119   4752   -687   -912   -162       C  
ATOM    300  OE1 GLN A  39     -37.705 -19.345 -21.125  1.00 45.62           O  
ANISOU  300  OE1 GLN A  39     7189   4767   5377   -759   -892    -83       O  
ATOM    301  NE2 GLN A  39     -36.719 -21.244 -21.799  1.00 43.13           N  
ANISOU  301  NE2 GLN A  39     7207   4213   4966   -684   -984   -200       N  
ATOM    302  N   PRO A  40     -34.949 -17.956 -26.418  1.00 42.94           N  
ANISOU  302  N   PRO A  40     7422   4374   4518   -300   -601   -359       N  
ATOM    303  CA  PRO A  40     -35.384 -18.185 -27.796  1.00 55.77           C  
ANISOU  303  CA  PRO A  40     9253   5949   5989   -289   -695   -396       C  
ATOM    304  C   PRO A  40     -36.421 -19.293 -27.853  1.00 59.15           C  
ANISOU  304  C   PRO A  40     9794   6267   6413   -396   -923   -408       C  
ATOM    305  O   PRO A  40     -36.535 -20.126 -26.951  1.00 58.85           O  
ANISOU  305  O   PRO A  40     9726   6165   6468   -451   -988   -406       O  
ATOM    306  CB  PRO A  40     -34.089 -18.580 -28.525  1.00 52.47           C  
ANISOU  306  CB  PRO A  40     8981   5512   5441   -133   -564   -497       C  
ATOM    307  CG  PRO A  40     -32.981 -18.018 -27.654  1.00 53.26           C  
ANISOU  307  CG  PRO A  40     8889   5710   5637    -73   -369   -479       C  
ATOM    308  CD  PRO A  40     -33.503 -18.172 -26.249  1.00 49.26           C  
ANISOU  308  CD  PRO A  40     8219   5193   5304   -172   -441   -422       C  
ATOM    309  N   SER A  41     -37.197 -19.279 -28.933  1.00 56.50           N  
ANISOU  309  N   SER A  41     9594   5913   5962   -440  -1054   -410       N  
ATOM    310  CA  SER A  41     -38.271 -20.251 -29.092  1.00 64.65           C  
ANISOU  310  CA  SER A  41    10732   6852   6981   -578  -1294   -413       C  
ATOM    311  C   SER A  41     -37.709 -21.668 -29.038  1.00 62.96           C  
ANISOU  311  C   SER A  41    10727   6468   6728   -545  -1344   -518       C  
ATOM    312  O   SER A  41     -36.754 -21.998 -29.749  1.00 60.27           O  
ANISOU  312  O   SER A  41    10574   6068   6259   -391  -1257   -626       O  
ATOM    313  CB  SER A  41     -39.002 -20.003 -30.412  1.00 66.33           C  
ANISOU  313  CB  SER A  41    11083   7077   7041   -611  -1425   -415       C  
ATOM    314  OG  SER A  41     -39.699 -18.761 -30.375  1.00 62.89           O  
ANISOU  314  OG  SER A  41    10454   6784   6657   -642  -1415   -301       O  
ATOM    315  N   GLY A  42     -38.280 -22.492 -28.160  1.00 56.09           N  
ANISOU  315  N   GLY A  42     9824   5521   5966   -680  -1475   -482       N  
ATOM    316  CA  GLY A  42     -37.851 -23.869 -28.041  1.00 65.62           C  
ANISOU  316  CA  GLY A  42    11254   6534   7145   -659  -1548   -569       C  
ATOM    317  C   GLY A  42     -36.459 -24.081 -27.486  1.00 66.74           C  
ANISOU  317  C   GLY A  42    11390   6651   7316   -465  -1362   -626       C  
ATOM    318  O   GLY A  42     -35.914 -25.180 -27.621  1.00 63.51           O  
ANISOU  318  O   GLY A  42    11209   6072   6850   -377  -1400   -720       O  
ATOM    319  N   LYS A  43     -35.861 -23.066 -26.867  1.00 51.77           N  
ANISOU  319  N   LYS A  43     9248   4918   5505   -392  -1168   -573       N  
ATOM    320  CA  LYS A  43     -34.533 -23.191 -26.285  1.00 52.35           C  
ANISOU  320  CA  LYS A  43     9270   5005   5613   -220   -998   -614       C  
ATOM    321  C   LYS A  43     -34.539 -22.679 -24.850  1.00 55.10           C  
ANISOU  321  C   LYS A  43     9344   5459   6132   -289   -934   -511       C  
ATOM    322  O   LYS A  43     -35.535 -22.142 -24.357  1.00 54.15           O  
ANISOU  322  O   LYS A  43     9070   5410   6093   -446   -994   -415       O  
ATOM    323  CB  LYS A  43     -33.478 -22.451 -27.123  1.00 55.88           C  
ANISOU  323  CB  LYS A  43     9716   5561   5953    -42   -800   -673       C  
ATOM    324  CG  LYS A  43     -33.409 -22.937 -28.572  1.00 66.65           C  
ANISOU  324  CG  LYS A  43    11367   6838   7119     47   -843   -783       C  
ATOM    325  CD  LYS A  43     -32.199 -22.374 -29.300  1.00 74.28           C  
ANISOU  325  CD  LYS A  43    12329   7925   7971    239   -620   -840       C  
ATOM    326  CE  LYS A  43     -32.458 -22.259 -30.797  1.00 80.75           C  
ANISOU  326  CE  LYS A  43    13367   8731   8581    269   -647   -900       C  
ATOM    327  NZ  LYS A  43     -32.043 -20.931 -31.332  1.00 71.74           N  
ANISOU  327  NZ  LYS A  43    12099   7776   7384    295   -468   -846       N  
ATOM    328  N   GLY A  44     -33.402 -22.876 -24.172  1.00 44.32           N  
ANISOU  328  N   GLY A  44     7917   4112   4810   -156   -813   -535       N  
ATOM    329  CA  GLY A  44     -33.238 -22.394 -22.817  1.00 37.73           C  
ANISOU  329  CA  GLY A  44     6841   3382   4114   -203   -744   -452       C  
ATOM    330  C   GLY A  44     -32.855 -20.928 -22.763  1.00 46.44           C  
ANISOU  330  C   GLY A  44     7736   4670   5241   -187   -577   -419       C  
ATOM    331  O   GLY A  44     -32.548 -20.287 -23.771  1.00 40.74           O  
ANISOU  331  O   GLY A  44     7050   4000   4429   -125   -492   -455       O  
ATOM    332  N   LEU A  45     -32.875 -20.390 -21.547  1.00 36.06           N  
ANISOU  332  N   LEU A  45     6216   3445   4038   -252   -532   -349       N  
ATOM    333  CA  LEU A  45     -32.570 -18.987 -21.343  1.00 35.03           C  
ANISOU  333  CA  LEU A  45     5907   3462   3940   -260   -391   -317       C  
ATOM    334  C   LEU A  45     -31.111 -18.693 -21.680  1.00 41.72           C  
ANISOU  334  C   LEU A  45     6726   4384   4742   -121   -231   -372       C  
ATOM    335  O   LEU A  45     -30.230 -19.542 -21.504  1.00 35.36           O  
ANISOU  335  O   LEU A  45     5956   3554   3926     -6   -213   -419       O  
ATOM    336  CB  LEU A  45     -32.841 -18.593 -19.893  1.00 37.85           C  
ANISOU  336  CB  LEU A  45     6080   3890   4412   -349   -384   -247       C  
ATOM    337  CG  LEU A  45     -34.314 -18.383 -19.571  1.00 37.71           C  
ANISOU  337  CG  LEU A  45     6015   3876   4439   -489   -487   -173       C  
ATOM    338  CD1 LEU A  45     -34.592 -18.828 -18.124  1.00 41.16           C  
ANISOU  338  CD1 LEU A  45     6350   4331   4959   -565   -528   -115       C  
ATOM    339  CD2 LEU A  45     -34.708 -16.953 -19.793  1.00 35.56           C  
ANISOU  339  CD2 LEU A  45     5644   3694   4172   -510   -413   -144       C  
ATOM    340  N   GLU A  46     -30.861 -17.452 -22.110  1.00 36.83           N  
ANISOU  340  N   GLU A  46     6031   3862   4099   -134   -114   -356       N  
ATOM    341  CA  GLU A  46     -29.539 -17.007 -22.547  1.00 38.37           C  
ANISOU  341  CA  GLU A  46     6178   4158   4243    -40     50   -390       C  
ATOM    342  C   GLU A  46     -29.293 -15.577 -22.074  1.00 35.79           C  
ANISOU  342  C   GLU A  46     5688   3939   3971   -130    156   -335       C  
ATOM    343  O   GLU A  46     -30.088 -14.676 -22.366  1.00 39.84           O  
ANISOU  343  O   GLU A  46     6219   4438   4481   -211    143   -292       O  
ATOM    344  CB  GLU A  46     -29.426 -17.100 -24.078  1.00 39.48           C  
ANISOU  344  CB  GLU A  46     6487   4277   4236     38     84   -437       C  
ATOM    345  CG  GLU A  46     -28.116 -16.629 -24.660  1.00 48.09           C  
ANISOU  345  CG  GLU A  46     7524   5496   5253    127    269   -460       C  
ATOM    346  CD  GLU A  46     -28.103 -16.737 -26.176  1.00 64.38           C  
ANISOU  346  CD  GLU A  46     9772   7544   7147    203    304   -504       C  
ATOM    347  OE1 GLU A  46     -29.187 -16.602 -26.784  1.00 62.70           O  
ANISOU  347  OE1 GLU A  46     9694   7245   6885    138    198   -488       O  
ATOM    348  OE2 GLU A  46     -27.022 -16.996 -26.757  1.00 68.46           O1-
ANISOU  348  OE2 GLU A  46    10296   8145   7569    335    435   -554       O1-
ATOM    349  N   TRP A  47     -28.187 -15.365 -21.358  1.00 35.56           N  
ANISOU  349  N   TRP A  47     5510   4014   3988   -112    252   -337       N  
ATOM    350  CA  TRP A  47     -27.819 -14.038 -20.874  1.00 36.39           C  
ANISOU  350  CA  TRP A  47     5479   4209   4139   -213    345   -295       C  
ATOM    351  C   TRP A  47     -27.211 -13.199 -22.001  1.00 39.61           C  
ANISOU  351  C   TRP A  47     5913   4679   4458   -217    476   -287       C  
ATOM    352  O   TRP A  47     -26.382 -13.685 -22.772  1.00 37.69           O  
ANISOU  352  O   TRP A  47     5693   4496   4132   -115    554   -322       O  
ATOM    353  CB  TRP A  47     -26.825 -14.158 -19.713  1.00 37.66           C  
ANISOU  353  CB  TRP A  47     5469   4469   4370   -213    381   -299       C  
ATOM    354  CG  TRP A  47     -26.295 -12.839 -19.205  1.00 35.21           C  
ANISOU  354  CG  TRP A  47     5031   4249   4098   -333    468   -267       C  
ATOM    355  CD1 TRP A  47     -26.939 -11.941 -18.385  1.00 39.81           C  
ANISOU  355  CD1 TRP A  47     5587   4798   4741   -452    437   -238       C  
ATOM    356  CD2 TRP A  47     -25.011 -12.270 -19.489  1.00 39.34           C  
ANISOU  356  CD2 TRP A  47     5443   4908   4594   -354    598   -263       C  
ATOM    357  NE1 TRP A  47     -26.127 -10.855 -18.148  1.00 39.59           N  
ANISOU  357  NE1 TRP A  47     5470   4850   4724   -551    528   -224       N  
ATOM    358  CE2 TRP A  47     -24.940 -11.034 -18.810  1.00 38.16           C  
ANISOU  358  CE2 TRP A  47     5224   4781   4495   -510    625   -231       C  
ATOM    359  CE3 TRP A  47     -23.912 -12.685 -20.258  1.00 44.56           C  
ANISOU  359  CE3 TRP A  47     6057   5686   5190   -256    700   -282       C  
ATOM    360  CZ2 TRP A  47     -23.812 -10.203 -18.882  1.00 36.86           C  
ANISOU  360  CZ2 TRP A  47     4944   4740   4320   -605    734   -210       C  
ATOM    361  CZ3 TRP A  47     -22.789 -11.857 -20.325  1.00 39.29           C  
ANISOU  361  CZ3 TRP A  47     5242   5174   4513   -339    824   -254       C  
ATOM    362  CH2 TRP A  47     -22.755 -10.629 -19.637  1.00 36.81           C  
ANISOU  362  CH2 TRP A  47     4862   4868   4255   -529    833   -214       C  
ATOM    363  N   LEU A  48     -27.611 -11.927 -22.084  1.00 36.22           N  
ANISOU  363  N   LEU A  48     5488   4236   4038   -327    507   -236       N  
ATOM    364  CA  LEU A  48     -27.151 -11.050 -23.162  1.00 40.01           C  
ANISOU  364  CA  LEU A  48     6019   4756   4426   -357    623   -205       C  
ATOM    365  C   LEU A  48     -26.126 -10.025 -22.703  1.00 39.64           C  
ANISOU  365  C   LEU A  48     5837   4809   4414   -467    742   -171       C  
ATOM    366  O   LEU A  48     -25.037  -9.927 -23.291  1.00 37.98           O  
ANISOU  366  O   LEU A  48     5572   4718   4139   -462    868   -164       O  
ATOM    367  CB  LEU A  48     -28.351 -10.339 -23.822  1.00 33.90           C  
ANISOU  367  CB  LEU A  48     5391   3873   3615   -395    562   -160       C  
ATOM    368  CG  LEU A  48     -29.377 -11.335 -24.399  1.00 34.22           C  
ANISOU  368  CG  LEU A  48     5563   3830   3608   -313    430   -188       C  
ATOM    369  CD1 LEU A  48     -30.625 -10.599 -24.873  1.00 41.50           C  
ANISOU  369  CD1 LEU A  48     6587   4671   4512   -351    348   -132       C  
ATOM    370  CD2 LEU A  48     -28.751 -12.156 -25.527  1.00 44.01           C  
ANISOU  370  CD2 LEU A  48     6904   5103   4715   -207    478   -238       C  
ATOM    371  N   ALA A  49     -26.443  -9.248 -21.672  1.00 35.52           N  
ANISOU  371  N   ALA A  49     5261   4249   3986   -573    705   -150       N  
ATOM    372  CA  ALA A  49     -25.594  -8.131 -21.274  1.00 33.18           C  
ANISOU  372  CA  ALA A  49     4876   4014   3716   -714    795   -117       C  
ATOM    373  C   ALA A  49     -26.019  -7.671 -19.892  1.00 35.23           C  
ANISOU  373  C   ALA A  49     5087   4222   4076   -790    722   -128       C  
ATOM    374  O   ALA A  49     -27.125  -7.972 -19.442  1.00 35.26           O  
ANISOU  374  O   ALA A  49     5141   4138   4118   -739    622   -141       O  
ATOM    375  CB  ALA A  49     -25.686  -6.979 -22.271  1.00 35.64           C  
ANISOU  375  CB  ALA A  49     5314   4273   3956   -796    866    -53       C  
ATOM    376  N   HIS A  50     -25.127  -6.934 -19.226  1.00 35.01           N  
ANISOU  376  N   HIS A  50     4959   4261   4084   -920    773   -121       N  
ATOM    377  CA  HIS A  50     -25.409  -6.382 -17.901  1.00 36.87           C  
ANISOU  377  CA  HIS A  50     5166   4450   4393  -1002    712   -141       C  
ATOM    378  C   HIS A  50     -24.814  -4.986 -17.815  1.00 37.05           C  
ANISOU  378  C   HIS A  50     5212   4451   4413  -1183    773   -113       C  
ATOM    379  O   HIS A  50     -23.714  -4.744 -18.325  1.00 37.59           O  
ANISOU  379  O   HIS A  50     5207   4626   4450  -1272    861    -81       O  
ATOM    380  CB  HIS A  50     -24.824  -7.282 -16.808  1.00 41.33           C  
ANISOU  380  CB  HIS A  50     5567   5131   5004   -973    667   -181       C  
ATOM    381  CG  HIS A  50     -25.207  -6.893 -15.411  1.00 37.57           C  
ANISOU  381  CG  HIS A  50     5076   4618   4582  -1037    596   -209       C  
ATOM    382  ND1 HIS A  50     -26.369  -7.331 -14.814  1.00 34.05           N  
ANISOU  382  ND1 HIS A  50     4682   4098   4159   -958    513   -225       N  
ATOM    383  CD2 HIS A  50     -24.570  -6.134 -14.486  1.00 34.65           C  
ANISOU  383  CD2 HIS A  50     4646   4286   4232  -1176    595   -226       C  
ATOM    384  CE1 HIS A  50     -26.435  -6.862 -13.579  1.00 33.51           C  
ANISOU  384  CE1 HIS A  50     4589   4028   4116  -1028    478   -253       C  
ATOM    385  NE2 HIS A  50     -25.353  -6.139 -13.351  1.00 36.75           N  
ANISOU  385  NE2 HIS A  50     4942   4496   4523  -1159    518   -260       N  
ATOM    386  N   ILE A  51     -25.537  -4.056 -17.193  1.00 35.10           N  
ANISOU  386  N   ILE A  51     5074   4067   4195  -1239    728   -123       N  
ATOM    387  CA  ILE A  51     -25.024  -2.702 -17.004  1.00 35.73           C  
ANISOU  387  CA  ILE A  51     5218   4084   4274  -1422    765   -105       C  
ATOM    388  C   ILE A  51     -25.100  -2.339 -15.525  1.00 33.31           C  
ANISOU  388  C   ILE A  51     4893   3750   4016  -1486    698   -168       C  
ATOM    389  O   ILE A  51     -26.145  -2.512 -14.886  1.00 38.25           O  
ANISOU  389  O   ILE A  51     5570   4303   4662  -1378    634   -207       O  
ATOM    390  CB  ILE A  51     -25.768  -1.662 -17.873  1.00 42.26           C  
ANISOU  390  CB  ILE A  51     6265   4728   5062  -1429    785    -54       C  
ATOM    391  CG1 ILE A  51     -25.082  -0.294 -17.765  1.00 38.80           C  
ANISOU  391  CG1 ILE A  51     5917   4207   4616  -1643    824    -26       C  
ATOM    392  CG2 ILE A  51     -27.255  -1.572 -17.520  1.00 41.01           C  
ANISOU  392  CG2 ILE A  51     6223   4431   4927  -1284    705    -81       C  
ATOM    393  CD1 ILE A  51     -25.353   0.631 -18.935  1.00 41.17           C  
ANISOU  393  CD1 ILE A  51     6421   4364   4859  -1680    871     58       C  
ATOM    394  N   PHE A  52     -23.992  -1.831 -14.990  1.00 40.77           N  
ANISOU  394  N   PHE A  52     5760   4765   4968  -1668    712   -176       N  
ATOM    395  CA  PHE A  52     -23.851  -1.458 -13.590  1.00 40.13           C  
ANISOU  395  CA  PHE A  52     5662   4674   4909  -1757    643   -241       C  
ATOM    396  C   PHE A  52     -24.166   0.020 -13.358  1.00 41.30           C  
ANISOU  396  C   PHE A  52     6030   4617   5045  -1882    634   -259       C  
ATOM    397  O   PHE A  52     -24.242   0.826 -14.287  1.00 42.37           O  
ANISOU  397  O   PHE A  52     6310   4629   5158  -1938    684   -204       O  
ATOM    398  CB  PHE A  52     -22.436  -1.763 -13.098  1.00 40.15           C  
ANISOU  398  CB  PHE A  52     5452   4881   4922  -1895    640   -243       C  
ATOM    399  CG  PHE A  52     -22.118  -3.227 -13.062  1.00 39.65           C  
ANISOU  399  CG  PHE A  52     5188   5004   4872  -1744    630   -240       C  
ATOM    400  CD1 PHE A  52     -22.550  -4.012 -12.002  1.00 43.73           C  
ANISOU  400  CD1 PHE A  52     5657   5552   5407  -1636    546   -287       C  
ATOM    401  CD2 PHE A  52     -21.371  -3.818 -14.081  1.00 39.11           C  
ANISOU  401  CD2 PHE A  52     4994   5077   4790  -1704    709   -188       C  
ATOM    402  CE1 PHE A  52     -22.264  -5.364 -11.960  1.00 39.09           C  
ANISOU  402  CE1 PHE A  52     4917   5104   4830  -1495    526   -279       C  
ATOM    403  CE2 PHE A  52     -21.078  -5.183 -14.042  1.00 37.72           C  
ANISOU  403  CE2 PHE A  52     4662   5047   4623  -1539    696   -194       C  
ATOM    404  CZ  PHE A  52     -21.526  -5.950 -12.981  1.00 38.17           C  
ANISOU  404  CZ  PHE A  52     4691   5106   4706  -1438    597   -237       C  
ATOM    405  N   TRP A  53     -24.331   0.367 -12.071  1.00 39.14           N  
ANISOU  405  N   TRP A  53     5796   4299   4775  -1921    566   -338       N  
ATOM    406  CA  TRP A  53     -24.681   1.734 -11.680  1.00 41.52           C  
ANISOU  406  CA  TRP A  53     6336   4384   5057  -2012    545   -379       C  
ATOM    407  C   TRP A  53     -23.694   2.769 -12.215  1.00 48.53           C  
ANISOU  407  C   TRP A  53     7301   5208   5931  -2267    576   -332       C  
ATOM    408  O   TRP A  53     -24.056   3.945 -12.385  1.00 44.28           O  
ANISOU  408  O   TRP A  53     7014   4437   5373  -2328    575   -334       O  
ATOM    409  CB  TRP A  53     -24.738   1.846 -10.149  1.00 42.28           C  
ANISOU  409  CB  TRP A  53     6442   4486   5137  -2038    469   -483       C  
ATOM    410  CG  TRP A  53     -23.378   1.889  -9.503  1.00 40.34           C  
ANISOU  410  CG  TRP A  53     6061   4381   4886  -2268    426   -501       C  
ATOM    411  CD1 TRP A  53     -22.713   2.992  -9.075  1.00 45.69           C  
ANISOU  411  CD1 TRP A  53     6856   4966   5539  -2508    387   -536       C  
ATOM    412  CD2 TRP A  53     -22.517   0.771  -9.235  1.00 41.21           C  
ANISOU  412  CD2 TRP A  53     5891   4752   5013  -2278    405   -479       C  
ATOM    413  NE1 TRP A  53     -21.495   2.639  -8.545  1.00 48.19           N  
ANISOU  413  NE1 TRP A  53     6960   5493   5858  -2682    339   -535       N  
ATOM    414  CE2 TRP A  53     -21.353   1.280  -8.626  1.00 45.61           C  
ANISOU  414  CE2 TRP A  53     6383   5388   5557  -2528    351   -499       C  
ATOM    415  CE3 TRP A  53     -22.631  -0.610  -9.423  1.00 40.12           C  
ANISOU  415  CE3 TRP A  53     5565   4778   4899  -2097    416   -446       C  
ATOM    416  CZ2 TRP A  53     -20.298   0.459  -8.228  1.00 57.23           C  
ANISOU  416  CZ2 TRP A  53     7582   7122   7042  -2584    312   -480       C  
ATOM    417  CZ3 TRP A  53     -21.585  -1.424  -9.024  1.00 44.14           C  
ANISOU  417  CZ3 TRP A  53     5834   5518   5419  -2140    382   -432       C  
ATOM    418  CH2 TRP A  53     -20.433  -0.887  -8.438  1.00 49.01           C  
ANISOU  418  CH2 TRP A  53     6365   6232   6025  -2371    331   -446       C  
ATOM    419  N   ASP A  54     -22.440   2.376 -12.448  1.00 45.60           N  
ANISOU  419  N   ASP A  54     6719   5039   5567  -2421    601   -285       N  
ATOM    420  CA  ASP A  54     -21.425   3.317 -12.902  1.00 44.49           C  
ANISOU  420  CA  ASP A  54     6614   4878   5413  -2701    633   -225       C  
ATOM    421  C   ASP A  54     -21.198   3.243 -14.404  1.00 47.81           C  
ANISOU  421  C   ASP A  54     7013   5337   5815  -2700    742   -108       C  
ATOM    422  O   ASP A  54     -20.138   3.670 -14.876  1.00 51.39           O  
ANISOU  422  O   ASP A  54     7395   5877   6254  -2932    793    -35       O  
ATOM    423  CB  ASP A  54     -20.100   3.084 -12.171  1.00 49.38           C  
ANISOU  423  CB  ASP A  54     6994   5724   6043  -2906    592   -238       C  
ATOM    424  CG  ASP A  54     -19.565   1.667 -12.364  1.00 45.93           C  
ANISOU  424  CG  ASP A  54     6240   5584   5627  -2772    625   -208       C  
ATOM    425  OD1 ASP A  54     -20.283   0.838 -12.961  1.00 46.76           O  
ANISOU  425  OD1 ASP A  54     6336   5695   5736  -2526    669   -194       O  
ATOM    426  OD2 ASP A  54     -18.431   1.392 -11.913  1.00 49.58           O1-
ANISOU  426  OD2 ASP A  54     6469   6268   6100  -2910    599   -200       O1-
ATOM    427  N   ASP A  55     -22.159   2.702 -15.158  1.00 44.13           N  
ANISOU  427  N   ASP A  55     6602   4825   5340  -2455    777    -87       N  
ATOM    428  CA  ASP A  55     -22.123   2.632 -16.622  1.00 47.53           C  
ANISOU  428  CA  ASP A  55     7057   5272   5730  -2423    874     16       C  
ATOM    429  C   ASP A  55     -21.107   1.615 -17.143  1.00 48.43           C  
ANISOU  429  C   ASP A  55     6891   5680   5832  -2423    951     59       C  
ATOM    430  O   ASP A  55     -20.835   1.573 -18.355  1.00 47.38           O  
ANISOU  430  O   ASP A  55     6756   5601   5644  -2427   1049    145       O  
ATOM    431  CB  ASP A  55     -21.863   4.017 -17.235  1.00 46.69           C  
ANISOU  431  CB  ASP A  55     7170   4985   5586  -2641    911     97       C  
ATOM    432  CG  ASP A  55     -22.671   4.271 -18.494  1.00 58.25           C  
ANISOU  432  CG  ASP A  55     8829   6306   6997  -2514    958    178       C  
ATOM    433  OD1 ASP A  55     -23.783   3.725 -18.632  1.00 57.22           O  
ANISOU  433  OD1 ASP A  55     8745   6126   6871  -2256    924    145       O  
ATOM    434  OD2 ASP A  55     -22.178   5.018 -19.363  1.00 62.60           O1-
ANISOU  434  OD2 ASP A  55     9484   6806   7497  -2686   1026    284       O1-
ATOM    435  N   ASP A  56     -20.530   0.800 -16.264  1.00 47.87           N  
ANISOU  435  N   ASP A  56     6587   5802   5801  -2404    911      2       N  
ATOM    436  CA  ASP A  56     -19.743  -0.351 -16.683  1.00 52.92           C  
ANISOU  436  CA  ASP A  56     6964   6710   6431  -2316    973     26       C  
ATOM    437  C   ASP A  56     -20.651  -1.393 -17.342  1.00 48.30           C  
ANISOU  437  C   ASP A  56     6420   6104   5828  -2030    985     12       C  
ATOM    438  O   ASP A  56     -21.679  -1.780 -16.777  1.00 46.54           O  
ANISOU  438  O   ASP A  56     6279   5771   5634  -1878    901    -48       O  
ATOM    439  CB  ASP A  56     -19.033  -0.938 -15.463  1.00 57.90           C  
ANISOU  439  CB  ASP A  56     7368   7522   7111  -2341    899    -32       C  
ATOM    440  CG  ASP A  56     -18.089  -2.083 -15.801  1.00 62.75           C  
ANISOU  440  CG  ASP A  56     7698   8423   7720  -2239    958     -8       C  
ATOM    441  OD1 ASP A  56     -18.068  -2.566 -16.955  1.00 58.94           O  
ANISOU  441  OD1 ASP A  56     7204   7998   7192  -2116   1060     36       O  
ATOM    442  OD2 ASP A  56     -17.366  -2.508 -14.875  1.00 56.56           O1-
ANISOU  442  OD2 ASP A  56     6710   7809   6971  -2268    897    -36       O1-
ATOM    443  N   LYS A  57     -20.261  -1.853 -18.536  1.00 43.70           N  
ANISOU  443  N   LYS A  57     5780   5636   5186  -1965   1090     69       N  
ATOM    444  CA  LYS A  57     -21.084  -2.716 -19.382  1.00 45.14           C  
ANISOU  444  CA  LYS A  57     6044   5780   5327  -1726   1102     61       C  
ATOM    445  C   LYS A  57     -20.337  -4.010 -19.687  1.00 48.23           C  
ANISOU  445  C   LYS A  57     6229   6399   5697  -1581   1154     45       C  
ATOM    446  O   LYS A  57     -19.157  -3.974 -20.068  1.00 45.63           O  
ANISOU  446  O   LYS A  57     5732   6268   5335  -1665   1258     89       O  
ATOM    447  CB  LYS A  57     -21.444  -2.016 -20.708  1.00 49.51           C  
ANISOU  447  CB  LYS A  57     6792   6224   5796  -1756   1178    140       C  
ATOM    448  CG  LYS A  57     -22.102  -0.632 -20.589  1.00 47.12           C  
ANISOU  448  CG  LYS A  57     6724   5678   5502  -1888   1137    173       C  
ATOM    449  CD  LYS A  57     -22.227   0.033 -21.971  1.00 44.01           C  
ANISOU  449  CD  LYS A  57     6508   5206   5010  -1931   1220    275       C  
ATOM    450  CE  LYS A  57     -22.396   1.545 -21.850  1.00 52.45           C  
ANISOU  450  CE  LYS A  57     7788   6058   6084  -2123   1201    330       C  
ATOM    451  NZ  LYS A  57     -21.205   2.205 -21.246  1.00 53.03           N  
ANISOU  451  NZ  LYS A  57     7754   6207   6188  -2400   1233    350       N  
ATOM    452  N   ARG A  58     -21.038  -5.145 -19.571  1.00 43.74           N  
ANISOU  452  N   ARG A  58     5679   5800   5140  -1360   1087    -13       N  
ATOM    453  CA  ARG A  58     -20.500  -6.468 -19.881  1.00 39.17           C  
ANISOU  453  CA  ARG A  58     4964   5384   4537  -1177   1119    -42       C  
ATOM    454  C   ARG A  58     -21.430  -7.190 -20.845  1.00 44.64           C  
ANISOU  454  C   ARG A  58     5826   5969   5164   -989   1108    -61       C  
ATOM    455  O   ARG A  58     -22.655  -7.123 -20.708  1.00 40.22           O  
ANISOU  455  O   ARG A  58     5427   5229   4625   -954   1012    -76       O  
ATOM    456  CB  ARG A  58     -20.322  -7.326 -18.615  1.00 40.56           C  
ANISOU  456  CB  ARG A  58     4997   5623   4791  -1099   1019    -98       C  
ATOM    457  CG  ARG A  58     -19.602  -6.618 -17.493  1.00 52.72           C  
ANISOU  457  CG  ARG A  58     6395   7246   6392  -1289    987    -91       C  
ATOM    458  CD  ARG A  58     -18.132  -6.405 -17.799  1.00 57.30           C  
ANISOU  458  CD  ARG A  58     6752   8071   6950  -1390   1094    -45       C  
ATOM    459  NE  ARG A  58     -17.496  -5.667 -16.715  1.00 62.98           N  
ANISOU  459  NE  ARG A  58     7347   8858   7723  -1606   1038    -38       N  
ATOM    460  CZ  ARG A  58     -16.907  -6.223 -15.665  1.00 51.24           C  
ANISOU  460  CZ  ARG A  58     5673   7512   6283  -1579    959    -66       C  
ATOM    461  NH1 ARG A  58     -16.820  -7.536 -15.537  1.00 55.13           N  
ANISOU  461  NH1 ARG A  58     6076   8088   6783  -1338    930    -95       N  
ATOM    462  NH2 ARG A  58     -16.386  -5.440 -14.724  1.00 62.75           N  
ANISOU  462  NH2 ARG A  58     7048   9020   7775  -1802    896    -63       N  
ATOM    463  N   TYR A  59     -20.850  -7.925 -21.792  1.00 38.56           N  
ANISOU  463  N   TYR A  59     5016   5324   4312   -861   1199    -64       N  
ATOM    464  CA  TYR A  59     -21.617  -8.517 -22.874  1.00 40.62           C  
ANISOU  464  CA  TYR A  59     5461   5490   4482   -708   1194    -83       C  
ATOM    465  C   TYR A  59     -21.329 -10.006 -22.985  1.00 44.06           C  
ANISOU  465  C   TYR A  59     5850   5997   4893   -483   1182   -154       C  
ATOM    466  O   TYR A  59     -20.228 -10.475 -22.674  1.00 45.16           O  
ANISOU  466  O   TYR A  59     5795   6318   5046   -425   1242   -167       O  
ATOM    467  CB  TYR A  59     -21.291  -7.875 -24.240  1.00 42.24           C  
ANISOU  467  CB  TYR A  59     5747   5744   4558   -759   1334    -21       C  
ATOM    468  CG  TYR A  59     -21.757  -6.445 -24.339  1.00 41.14           C  
ANISOU  468  CG  TYR A  59     5730   5477   4423   -956   1332     56       C  
ATOM    469  CD1 TYR A  59     -23.051  -6.147 -24.761  1.00 43.46           C  
ANISOU  469  CD1 TYR A  59     6250   5570   4693   -926   1244     67       C  
ATOM    470  CD2 TYR A  59     -20.890  -5.400 -24.085  1.00 40.18           C  
ANISOU  470  CD2 TYR A  59     5507   5436   4323  -1169   1414    122       C  
ATOM    471  CE1 TYR A  59     -23.489  -4.843 -24.861  1.00 43.67           C  
ANISOU  471  CE1 TYR A  59     6407   5465   4723  -1073   1237    139       C  
ATOM    472  CE2 TYR A  59     -21.311  -4.087 -24.191  1.00 49.65           C  
ANISOU  472  CE2 TYR A  59     6858   6485   5523  -1345   1405    192       C  
ATOM    473  CZ  TYR A  59     -22.611  -3.816 -24.590  1.00 43.07           C  
ANISOU  473  CZ  TYR A  59     6260   5439   4667  -1279   1320    200       C  
ATOM    474  OH  TYR A  59     -23.055  -2.517 -24.713  1.00 42.95           O  
ANISOU  474  OH  TYR A  59     6414   5256   4648  -1419   1305    271       O  
ATOM    475  N   ASN A  60     -22.318 -10.734 -23.480  1.00 42.48           N  
ANISOU  475  N   ASN A  60     5836   5654   4651   -354   1098   -195       N  
ATOM    476  CA  ASN A  60     -22.090 -12.110 -23.897  1.00 38.81           C  
ANISOU  476  CA  ASN A  60     5401   5216   4128   -136   1094   -266       C  
ATOM    477  C   ASN A  60     -21.109 -12.102 -25.060  1.00 41.01           C  
ANISOU  477  C   ASN A  60     5651   5662   4272    -63   1270   -261       C  
ATOM    478  O   ASN A  60     -21.427 -11.532 -26.112  1.00 48.83           O  
ANISOU  478  O   ASN A  60     6780   6621   5154   -110   1330   -228       O  
ATOM    479  CB  ASN A  60     -23.397 -12.772 -24.320  1.00 44.23           C  
ANISOU  479  CB  ASN A  60     6320   5704   4780    -57    960   -306       C  
ATOM    480  CG  ASN A  60     -23.262 -14.267 -24.462  1.00 49.07           C  
ANISOU  480  CG  ASN A  60     6995   6291   5357    152    912   -389       C  
ATOM    481  OD1 ASN A  60     -22.231 -14.759 -24.902  1.00 52.15           O  
ANISOU  481  OD1 ASN A  60     7322   6814   5678    291   1023   -424       O  
ATOM    482  ND2 ASN A  60     -24.297 -15.001 -24.072  1.00 39.28           N  
ANISOU  482  ND2 ASN A  60     5880   4882   4163    176    747   -418       N  
ATOM    483  N   PRO A  61     -19.929 -12.719 -24.926  1.00 49.49           N  
ANISOU  483  N   PRO A  61     6544   6924   5337     61   1360   -288       N  
ATOM    484  CA  PRO A  61     -18.929 -12.630 -26.007  1.00 51.28           C  
ANISOU  484  CA  PRO A  61     6705   7353   5427    129   1556   -275       C  
ATOM    485  C   PRO A  61     -19.416 -13.174 -27.335  1.00 52.78           C  
ANISOU  485  C   PRO A  61     7142   7462   5448    280   1586   -327       C  
ATOM    486  O   PRO A  61     -18.932 -12.732 -28.385  1.00 56.61           O  
ANISOU  486  O   PRO A  61     7640   8076   5794    270   1747   -292       O  
ATOM    487  CB  PRO A  61     -17.747 -13.448 -25.459  1.00 49.46           C  
ANISOU  487  CB  PRO A  61     6234   7323   5234    295   1609   -311       C  
ATOM    488  CG  PRO A  61     -18.316 -14.257 -24.314  1.00 60.54           C  
ANISOU  488  CG  PRO A  61     7670   8568   6763    365   1416   -361       C  
ATOM    489  CD  PRO A  61     -19.402 -13.413 -23.738  1.00 49.43           C  
ANISOU  489  CD  PRO A  61     6360   6979   5442    138   1294   -318       C  
ATOM    490  N   SER A  62     -20.362 -14.113 -27.325  1.00 55.55           N  
ANISOU  490  N   SER A  62     7698   7608   5800    404   1431   -405       N  
ATOM    491  CA  SER A  62     -20.865 -14.697 -28.563  1.00 56.69           C  
ANISOU  491  CA  SER A  62     8103   7661   5777    541   1430   -468       C  
ATOM    492  C   SER A  62     -21.765 -13.745 -29.332  1.00 58.11           C  
ANISOU  492  C   SER A  62     8456   7742   5882    380   1409   -405       C  
ATOM    493  O   SER A  62     -22.003 -13.964 -30.522  1.00 52.01           O  
ANISOU  493  O   SER A  62     7881   6946   4935    462   1442   -436       O  
ATOM    494  CB  SER A  62     -21.633 -15.983 -28.262  1.00 60.92           C  
ANISOU  494  CB  SER A  62     8812   7992   6343    684   1246   -565       C  
ATOM    495  OG  SER A  62     -20.847 -16.869 -27.488  1.00 73.57           O  
ANISOU  495  OG  SER A  62    10276   9659   8019    844   1247   -613       O  
ATOM    496  N   LEU A  63     -22.282 -12.712 -28.674  1.00 46.37           N  
ANISOU  496  N   LEU A  63     6914   6190   4513    169   1346   -321       N  
ATOM    497  CA  LEU A  63     -23.191 -11.759 -29.289  1.00 52.57           C  
ANISOU  497  CA  LEU A  63     7861   6866   5246     32   1306   -251       C  
ATOM    498  C   LEU A  63     -22.697 -10.327 -29.193  1.00 49.60           C  
ANISOU  498  C   LEU A  63     7374   6576   4896   -171   1420   -137       C  
ATOM    499  O   LEU A  63     -23.402  -9.425 -29.655  1.00 49.67           O  
ANISOU  499  O   LEU A  63     7522   6483   4867   -283   1389    -65       O  
ATOM    500  CB  LEU A  63     -24.588 -11.847 -28.643  1.00 49.47           C  
ANISOU  500  CB  LEU A  63     7567   6263   4965    -18   1091   -258       C  
ATOM    501  CG  LEU A  63     -25.219 -13.231 -28.748  1.00 61.08           C  
ANISOU  501  CG  LEU A  63     9175   7619   6411    134    951   -357       C  
ATOM    502  CD1 LEU A  63     -26.173 -13.495 -27.595  1.00 55.24           C  
ANISOU  502  CD1 LEU A  63     8407   6746   5835     75    770   -359       C  
ATOM    503  CD2 LEU A  63     -25.900 -13.393 -30.112  1.00 63.84           C  
ANISOU  503  CD2 LEU A  63     9777   7896   6583    183    910   -376       C  
ATOM    504  N   LYS A  64     -21.515 -10.100 -28.604  1.00 51.05           N  
ANISOU  504  N   LYS A  64     7316   6937   5142   -224   1538   -114       N  
ATOM    505  CA  LYS A  64     -21.044  -8.750 -28.291  1.00 57.94           C  
ANISOU  505  CA  LYS A  64     8078   7869   6066   -457   1616     -7       C  
ATOM    506  C   LYS A  64     -21.145  -7.811 -29.488  1.00 53.07           C  
ANISOU  506  C   LYS A  64     7618   7245   5302   -559   1713     87       C  
ATOM    507  O   LYS A  64     -21.648  -6.687 -29.368  1.00 55.13           O  
ANISOU  507  O   LYS A  64     7965   7381   5602   -732   1671    169       O  
ATOM    508  CB  LYS A  64     -19.600  -8.807 -27.784  1.00 54.57           C  
ANISOU  508  CB  LYS A  64     7362   7690   5683   -486   1747      4       C  
ATOM    509  CG  LYS A  64     -18.937  -7.437 -27.643  1.00 66.87           C  
ANISOU  509  CG  LYS A  64     8808   9336   7265   -756   1845    120       C  
ATOM    510  CD  LYS A  64     -17.854  -7.424 -26.571  1.00 70.33           C  
ANISOU  510  CD  LYS A  64     8943   9959   7821   -836   1872    123       C  
ATOM    511  CE  LYS A  64     -17.487  -5.995 -26.158  1.00 76.42           C  
ANISOU  511  CE  LYS A  64     9652  10735   8650  -1151   1898    226       C  
ATOM    512  NZ  LYS A  64     -18.272  -4.942 -26.879  1.00 68.44           N  
ANISOU  512  NZ  LYS A  64     8905   9528   7572  -1288   1895    304       N  
ATOM    513  N   SER A  65     -20.691  -8.267 -30.656  1.00 50.42           N  
ANISOU  513  N   SER A  65     7338   7034   4786   -441   1842     76       N  
ATOM    514  CA  SER A  65     -20.632  -7.408 -31.839  1.00 46.73           C  
ANISOU  514  CA  SER A  65     7011   6595   4151   -540   1958    180       C  
ATOM    515  C   SER A  65     -22.009  -6.971 -32.328  1.00 51.91           C  
ANISOU  515  C   SER A  65     7948   7011   4763   -561   1811    210       C  
ATOM    516  O   SER A  65     -22.087  -6.068 -33.171  1.00 59.58           O  
ANISOU  516  O   SER A  65     9057   7965   5615   -670   1876    319       O  
ATOM    517  CB  SER A  65     -19.882  -8.121 -32.962  1.00 57.71           C  
ANISOU  517  CB  SER A  65     8406   8185   5335   -376   2130    145       C  
ATOM    518  OG  SER A  65     -20.629  -9.218 -33.452  1.00 59.42           O  
ANISOU  518  OG  SER A  65     8818   8293   5467   -152   2025     28       O  
ATOM    519  N   ARG A  66     -23.088  -7.575 -31.814  1.00 49.17           N  
ANISOU  519  N   ARG A  66     7683   6490   4509   -464   1613    130       N  
ATOM    520  CA  ARG A  66     -24.451  -7.228 -32.190  1.00 45.22           C  
ANISOU  520  CA  ARG A  66     7410   5788   3985   -470   1454    158       C  
ATOM    521  C   ARG A  66     -25.203  -6.452 -31.116  1.00 46.67           C  
ANISOU  521  C   ARG A  66     7565   5814   4354   -585   1323    196       C  
ATOM    522  O   ARG A  66     -26.314  -5.987 -31.390  1.00 49.91           O  
ANISOU  522  O   ARG A  66     8139   6072   4753   -590   1200    238       O  
ATOM    523  CB  ARG A  66     -25.274  -8.493 -32.507  1.00 50.85           C  
ANISOU  523  CB  ARG A  66     8250   6424   4648   -285   1311     46       C  
ATOM    524  CG  ARG A  66     -24.617  -9.488 -33.460  1.00 64.44           C  
ANISOU  524  CG  ARG A  66    10027   8271   6184   -123   1416    -33       C  
ATOM    525  CD  ARG A  66     -25.514 -10.706 -33.677  1.00 67.46           C  
ANISOU  525  CD  ARG A  66    10569   8533   6530     30   1241   -150       C  
ATOM    526  NE  ARG A  66     -26.816 -10.348 -34.233  1.00 60.24           N  
ANISOU  526  NE  ARG A  66     9859   7470   5561    -11   1076   -107       N  
ATOM    527  CZ  ARG A  66     -27.972 -10.875 -33.850  1.00 57.38           C  
ANISOU  527  CZ  ARG A  66     9558   6963   5281      7    860   -151       C  
ATOM    528  NH1 ARG A  66     -28.033 -11.796 -32.900  1.00 58.40           N  
ANISOU  528  NH1 ARG A  66     9588   7052   5549     55    780   -235       N  
ATOM    529  NH2 ARG A  66     -29.095 -10.464 -34.429  1.00 56.98           N  
ANISOU  529  NH2 ARG A  66     9665   6813   5170    -30    718    -98       N  
ATOM    530  N   LEU A  67     -24.654  -6.317 -29.910  1.00 45.73           N  
ANISOU  530  N   LEU A  67     7247   5735   4396   -661   1340    179       N  
ATOM    531  CA  LEU A  67     -25.418  -5.820 -28.771  1.00 39.86           C  
ANISOU  531  CA  LEU A  67     6479   4846   3821   -728   1208    181       C  
ATOM    532  C   LEU A  67     -24.906  -4.470 -28.288  1.00 43.64           C  
ANISOU  532  C   LEU A  67     6914   5305   4361   -929   1277    266       C  
ATOM    533  O   LEU A  67     -23.708  -4.177 -28.353  1.00 44.85           O  
ANISOU  533  O   LEU A  67     6949   5603   4489  -1037   1421    303       O  
ATOM    534  CB  LEU A  67     -25.358  -6.803 -27.600  1.00 42.48           C  
ANISOU  534  CB  LEU A  67     6646   5209   4286   -656   1135     82       C  
ATOM    535  CG  LEU A  67     -25.864  -8.231 -27.816  1.00 46.22           C  
ANISOU  535  CG  LEU A  67     7164   5669   4728   -476   1042    -10       C  
ATOM    536  CD1 LEU A  67     -25.547  -9.062 -26.576  1.00 39.94           C  
ANISOU  536  CD1 LEU A  67     6197   4913   4065   -433    996    -82       C  
ATOM    537  CD2 LEU A  67     -27.349  -8.248 -28.110  1.00 52.71           C  
ANISOU  537  CD2 LEU A  67     8155   6331   5540   -438    879     -3       C  
ATOM    538  N   THR A  68     -25.826  -3.651 -27.771  1.00 39.37           N  
ANISOU  538  N   THR A  68     6470   4586   3903   -978   1169    296       N  
ATOM    539  CA  THR A  68     -25.473  -2.379 -27.141  1.00 38.52           C  
ANISOU  539  CA  THR A  68     6359   4408   3868  -1163   1201    356       C  
ATOM    540  C   THR A  68     -26.417  -2.184 -25.964  1.00 39.77           C  
ANISOU  540  C   THR A  68     6520   4425   4167  -1131   1062    305       C  
ATOM    541  O   THR A  68     -27.627  -2.054 -26.168  1.00 41.79           O  
ANISOU  541  O   THR A  68     6908   4549   4420  -1030    955    315       O  
ATOM    542  CB  THR A  68     -25.594  -1.207 -28.106  1.00 50.39           C  
ANISOU  542  CB  THR A  68     8071   5808   5269  -1259   1248    480       C  
ATOM    543  OG1 THR A  68     -24.729  -1.426 -29.220  1.00 54.63           O  
ANISOU  543  OG1 THR A  68     8603   6500   5654  -1287   1392    532       O  
ATOM    544  CG2 THR A  68     -25.195   0.096 -27.411  1.00 51.55           C  
ANISOU  544  CG2 THR A  68     8244   5850   5492  -1466   1270    535       C  
ATOM    545  N   ILE A  69     -25.879  -2.187 -24.751  1.00 40.25           N  
ANISOU  545  N   ILE A  69     6424   4529   4338  -1208   1062    254       N  
ATOM    546  CA  ILE A  69     -26.677  -1.910 -23.556  1.00 35.18           C  
ANISOU  546  CA  ILE A  69     5786   3768   3813  -1189    951    204       C  
ATOM    547  C   ILE A  69     -26.381  -0.486 -23.092  1.00 43.96           C  
ANISOU  547  C   ILE A  69     6986   4760   4958  -1364    975    246       C  
ATOM    548  O   ILE A  69     -25.300   0.069 -23.348  1.00 41.26           O  
ANISOU  548  O   ILE A  69     6622   4473   4582  -1539   1073    299       O  
ATOM    549  CB  ILE A  69     -26.418  -2.967 -22.450  1.00 34.42           C  
ANISOU  549  CB  ILE A  69     5487   3787   3802  -1139    912    111       C  
ATOM    550  CG1 ILE A  69     -27.527  -2.919 -21.380  1.00 34.13           C  
ANISOU  550  CG1 ILE A  69     5469   3644   3856  -1072    794     63       C  
ATOM    551  CG2 ILE A  69     -25.025  -2.797 -21.839  1.00 43.24           C  
ANISOU  551  CG2 ILE A  69     6442   5036   4952  -1292    991    103       C  
ATOM    552  CD1 ILE A  69     -27.587  -4.160 -20.490  1.00 39.85           C  
ANISOU  552  CD1 ILE A  69     6035   4466   4641   -990    735    -11       C  
ATOM    553  N   SER A  70     -27.377   0.145 -22.469  1.00 41.53           N  
ANISOU  553  N   SER A  70     6791   4282   4707  -1316    885    228       N  
ATOM    554  CA  SER A  70     -27.296   1.549 -22.080  1.00 37.01           C  
ANISOU  554  CA  SER A  70     6370   3538   4156  -1451    888    258       C  
ATOM    555  C   SER A  70     -28.403   1.835 -21.071  1.00 39.58           C  
ANISOU  555  C   SER A  70     6751   3731   4555  -1334    788    193       C  
ATOM    556  O   SER A  70     -29.299   1.019 -20.857  1.00 42.42           O  
ANISOU  556  O   SER A  70     7038   4138   4942  -1161    722    150       O  
ATOM    557  CB  SER A  70     -27.403   2.487 -23.294  1.00 41.16           C  
ANISOU  557  CB  SER A  70     7118   3931   4589  -1496    926    376       C  
ATOM    558  OG  SER A  70     -28.683   2.382 -23.895  1.00 45.73           O  
ANISOU  558  OG  SER A  70     7816   4424   5137  -1296    848    400       O  
ATOM    559  N   LYS A  71     -28.329   3.008 -20.450  1.00 44.77           N  
ANISOU  559  N   LYS A  71     7547   4225   5240  -1434    779    184       N  
ATOM    560  CA  LYS A  71     -29.291   3.341 -19.414  1.00 43.34           C  
ANISOU  560  CA  LYS A  71     7421   3930   5115  -1314    704    110       C  
ATOM    561  C   LYS A  71     -29.569   4.838 -19.436  1.00 46.16           C  
ANISOU  561  C   LYS A  71     8055   4026   5458  -1350    691    140       C  
ATOM    562  O   LYS A  71     -28.779   5.641 -19.948  1.00 44.60           O  
ANISOU  562  O   LYS A  71     7988   3735   5221  -1537    737    208       O  
ATOM    563  CB  LYS A  71     -28.784   2.897 -18.037  1.00 43.64           C  
ANISOU  563  CB  LYS A  71     7294   4076   5212  -1381    692      7       C  
ATOM    564  CG  LYS A  71     -27.603   3.690 -17.528  1.00 46.96           C  
ANISOU  564  CG  LYS A  71     7750   4458   5635  -1631    724     -7       C  
ATOM    565  CD  LYS A  71     -27.393   3.398 -16.063  1.00 52.72           C  
ANISOU  565  CD  LYS A  71     8362   5261   6409  -1660    682   -116       C  
ATOM    566  CE  LYS A  71     -25.935   3.425 -15.673  1.00 54.33           C  
ANISOU  566  CE  LYS A  71     8441   5584   6617  -1910    707   -124       C  
ATOM    567  NZ  LYS A  71     -25.262   4.571 -16.295  1.00 62.00           N  
ANISOU  567  NZ  LYS A  71     9575   6425   7556  -2125    746    -52       N  
ATOM    568  N   ASP A  72     -30.730   5.201 -18.886  1.00 40.64           N  
ANISOU  568  N   ASP A  72     7447   3207   4786  -1161    629     94       N  
ATOM    569  CA  ASP A  72     -31.116   6.596 -18.631  1.00 50.01           C  
ANISOU  569  CA  ASP A  72     8911   4124   5967  -1141    605     91       C  
ATOM    570  C   ASP A  72     -31.717   6.604 -17.234  1.00 52.03           C  
ANISOU  570  C   ASP A  72     9129   4370   6268  -1022    570    -36       C  
ATOM    571  O   ASP A  72     -32.919   6.379 -17.071  1.00 47.34           O  
ANISOU  571  O   ASP A  72     8503   3795   5690   -778    534    -54       O  
ATOM    572  CB  ASP A  72     -32.097   7.135 -19.660  1.00 51.08           C  
ANISOU  572  CB  ASP A  72     9230   4115   6063   -961    571    187       C  
ATOM    573  CG  ASP A  72     -32.428   8.604 -19.443  1.00 62.66           C  
ANISOU  573  CG  ASP A  72    11014   5274   7520   -925    545    189       C  
ATOM    574  OD1 ASP A  72     -31.892   9.235 -18.498  1.00 62.36           O  
ANISOU  574  OD1 ASP A  72    11074   5120   7500  -1057    552    108       O  
ATOM    575  OD2 ASP A  72     -33.237   9.135 -20.238  1.00 74.41           O1-
ANISOU  575  OD2 ASP A  72    12672   6626   8975   -759    507    273       O1-
ATOM    576  N   THR A  73     -30.870   6.856 -16.235  1.00 49.26           N  
ANISOU  576  N   THR A  73     8775   4011   5930  -1201    580   -118       N  
ATOM    577  CA  THR A  73     -31.331   6.794 -14.859  1.00 53.49           C  
ANISOU  577  CA  THR A  73     9272   4564   6486  -1104    554   -245       C  
ATOM    578  C   THR A  73     -32.293   7.923 -14.517  1.00 57.14           C  
ANISOU  578  C   THR A  73     9997   4781   6932   -923    530   -288       C  
ATOM    579  O   THR A  73     -33.017   7.812 -13.524  1.00 54.55           O  
ANISOU  579  O   THR A  73     9631   4489   6609   -758    520   -383       O  
ATOM    580  CB  THR A  73     -30.134   6.773 -13.900  1.00 51.50           C  
ANISOU  580  CB  THR A  73     8957   4373   6236  -1351    557   -321       C  
ATOM    581  OG1 THR A  73     -29.325   7.942 -14.088  1.00 53.39           O  
ANISOU  581  OG1 THR A  73     9426   4408   6452  -1574    556   -302       O  
ATOM    582  CG2 THR A  73     -29.299   5.525 -14.114  1.00 51.07           C  
ANISOU  582  CG2 THR A  73     8611   4592   6202  -1462    580   -287       C  
ATOM    583  N   SER A  74     -32.346   8.986 -15.324  1.00 56.66           N  
ANISOU  583  N   SER A  74    10204   4477   6846   -932    522   -216       N  
ATOM    584  CA  SER A  74     -33.316  10.043 -15.067  1.00 57.56           C  
ANISOU  584  CA  SER A  74    10582   4345   6944   -712    495   -253       C  
ATOM    585  C   SER A  74     -34.740   9.603 -15.384  1.00 62.59           C  
ANISOU  585  C   SER A  74    11109   5077   7594   -375    479   -221       C  
ATOM    586  O   SER A  74     -35.688  10.191 -14.854  1.00 63.80           O  
ANISOU  586  O   SER A  74    11379   5120   7741   -132    466   -281       O  
ATOM    587  CB  SER A  74     -32.950  11.306 -15.856  1.00 51.73           C  
ANISOU  587  CB  SER A  74    10186   3297   6171   -820    480   -171       C  
ATOM    588  OG  SER A  74     -33.307  11.203 -17.225  1.00 59.04           O  
ANISOU  588  OG  SER A  74    11122   4228   7083   -742    477    -22       O  
ATOM    589  N   ARG A  75     -34.911   8.575 -16.217  1.00 55.40           N  
ANISOU  589  N   ARG A  75     9972   4379   6699   -354    476   -132       N  
ATOM    590  CA  ARG A  75     -36.227   8.044 -16.551  1.00 50.98           C  
ANISOU  590  CA  ARG A  75     9273   3943   6153    -77    444    -92       C  
ATOM    591  C   ARG A  75     -36.428   6.617 -16.058  1.00 50.71           C  
ANISOU  591  C   ARG A  75     8903   4213   6153    -69    449   -127       C  
ATOM    592  O   ARG A  75     -37.432   5.989 -16.408  1.00 51.75           O  
ANISOU  592  O   ARG A  75     8880   4485   6298    107    413    -82       O  
ATOM    593  CB  ARG A  75     -36.465   8.111 -18.062  1.00 60.95           C  
ANISOU  593  CB  ARG A  75    10603   5168   7389    -38    409     53       C  
ATOM    594  CG  ARG A  75     -36.132   9.457 -18.705  1.00 65.41           C  
ANISOU  594  CG  ARG A  75    11516   5427   7909    -87    402    121       C  
ATOM    595  CD  ARG A  75     -37.134   9.785 -19.808  1.00 68.47           C  
ANISOU  595  CD  ARG A  75    12002   5747   8267    140    339    242       C  
ATOM    596  NE  ARG A  75     -36.844  11.047 -20.484  1.00 83.43           N  
ANISOU  596  NE  ARG A  75    14251   7337  10112     98    326    328       N  
ATOM    597  CZ  ARG A  75     -37.310  12.227 -20.096  1.00 85.54           C  
ANISOU  597  CZ  ARG A  75    14794   7333  10376    256    301    301       C  
ATOM    598  NH1 ARG A  75     -38.002  12.362 -18.974  1.00 83.28           N  
ANISOU  598  NH1 ARG A  75    14467   7048  10126    460    303    175       N  
ATOM    599  NH2 ARG A  75     -37.065  13.302 -20.843  1.00 90.92           N  
ANISOU  599  NH2 ARG A  75    15812   7726  11006    210    277    403       N  
ATOM    600  N   ASN A  76     -35.501   6.099 -15.254  1.00 45.89           N  
ANISOU  600  N   ASN A  76     8181   3701   5552   -261    481   -201       N  
ATOM    601  CA  ASN A  76     -35.519   4.730 -14.752  1.00 43.80           C  
ANISOU  601  CA  ASN A  76     7628   3699   5314   -282    482   -228       C  
ATOM    602  C   ASN A  76     -35.723   3.735 -15.890  1.00 42.15           C  
ANISOU  602  C   ASN A  76     7272   3631   5113   -270    452   -130       C  
ATOM    603  O   ASN A  76     -36.669   2.952 -15.903  1.00 41.82           O  
ANISOU  603  O   ASN A  76     7067   3734   5089   -134    417   -110       O  
ATOM    604  CB  ASN A  76     -36.589   4.546 -13.671  1.00 48.06           C  
ANISOU  604  CB  ASN A  76     8068   4330   5863    -87    483   -297       C  
ATOM    605  CG  ASN A  76     -36.181   5.152 -12.351  1.00 55.40           C  
ANISOU  605  CG  ASN A  76     9097   5186   6768   -136    516   -420       C  
ATOM    606  OD1 ASN A  76     -35.041   5.590 -12.182  1.00 48.07           O  
ANISOU  606  OD1 ASN A  76     8284   4154   5824   -345    523   -455       O  
ATOM    607  ND2 ASN A  76     -37.101   5.174 -11.406  1.00 57.53           N  
ANISOU  607  ND2 ASN A  76     9317   5519   7023     48    535   -484       N  
ATOM    608  N   LYS A  77     -34.812   3.789 -16.863  1.00 42.62           N  
ANISOU  608  N   LYS A  77     7398   3647   5148   -425    467    -67       N  
ATOM    609  CA  LYS A  77     -34.889   2.947 -18.045  1.00 40.06           C  
ANISOU  609  CA  LYS A  77     6985   3431   4804   -419    444     17       C  
ATOM    610  C   LYS A  77     -33.523   2.343 -18.349  1.00 39.06           C  
ANISOU  610  C   LYS A  77     6784   3395   4662   -630    492     21       C  
ATOM    611  O   LYS A  77     -32.488   2.989 -18.153  1.00 43.46           O  
ANISOU  611  O   LYS A  77     7426   3877   5211   -799    542      8       O  
ATOM    612  CB  LYS A  77     -35.407   3.756 -19.253  1.00 52.84           C  
ANISOU  612  CB  LYS A  77     8797   4904   6377   -327    415    116       C  
ATOM    613  CG  LYS A  77     -36.848   4.252 -19.077  1.00 53.09           C  
ANISOU  613  CG  LYS A  77     8869   4880   6424    -75    357    124       C  
ATOM    614  CD  LYS A  77     -37.561   4.469 -20.404  1.00 58.88           C  
ANISOU  614  CD  LYS A  77     9691   5569   7110     49    293    239       C  
ATOM    615  CE  LYS A  77     -38.887   5.194 -20.214  1.00 59.01           C  
ANISOU  615  CE  LYS A  77     9764   5515   7143    314    238    255       C  
ATOM    616  NZ  LYS A  77     -39.875   4.361 -19.481  1.00 58.21           N  
ANISOU  616  NZ  LYS A  77     9406   5621   7092    447    207    212       N  
ATOM    617  N   VAL A  78     -33.536   1.089 -18.794  1.00 38.70           N  
ANISOU  617  N   VAL A  78     6577   3515   4612   -615    474     37       N  
ATOM    618  CA  VAL A  78     -32.377   0.394 -19.342  1.00 41.39           C  
ANISOU  618  CA  VAL A  78     6843   3959   4925   -753    521     52       C  
ATOM    619  C   VAL A  78     -32.746  -0.018 -20.755  1.00 46.78           C  
ANISOU  619  C   VAL A  78     7568   4664   5543   -685    497    127       C  
ATOM    620  O   VAL A  78     -33.876  -0.449 -20.999  1.00 43.11           O  
ANISOU  620  O   VAL A  78     7077   4222   5080   -544    418    143       O  
ATOM    621  CB  VAL A  78     -31.985  -0.841 -18.499  1.00 42.89           C  
ANISOU  621  CB  VAL A  78     6822   4318   5157   -780    516    -15       C  
ATOM    622  CG1 VAL A  78     -30.902  -1.673 -19.195  1.00 40.65           C  
ANISOU  622  CG1 VAL A  78     6456   4152   4837   -863    562      0       C  
ATOM    623  CG2 VAL A  78     -31.504  -0.414 -17.139  1.00 46.51           C  
ANISOU  623  CG2 VAL A  78     7248   4766   5656   -863    534    -86       C  
ATOM    624  N   PHE A  79     -31.809   0.112 -21.689  1.00 42.98           N  
ANISOU  624  N   PHE A  79     7148   4188   4995   -792    564    176       N  
ATOM    625  CA  PHE A  79     -32.103  -0.185 -23.079  1.00 39.33           C  
ANISOU  625  CA  PHE A  79     6760   3742   4443   -733    546    247       C  
ATOM    626  C   PHE A  79     -31.192  -1.285 -23.607  1.00 42.71           C  
ANISOU  626  C   PHE A  79     7081   4325   4820   -784    601    229       C  
ATOM    627  O   PHE A  79     -30.058  -1.463 -23.148  1.00 38.20           O  
ANISOU  627  O   PHE A  79     6409   3836   4270   -898    680    195       O  
ATOM    628  CB  PHE A  79     -31.950   1.057 -23.967  1.00 41.41           C  
ANISOU  628  CB  PHE A  79     7242   3859   4632   -782    583    343       C  
ATOM    629  CG  PHE A  79     -32.634   2.290 -23.441  1.00 50.10           C  
ANISOU  629  CG  PHE A  79     8488   4771   5777   -731    544    358       C  
ATOM    630  CD1 PHE A  79     -33.991   2.482 -23.642  1.00 42.70           C  
ANISOU  630  CD1 PHE A  79     7609   3772   4843   -539    445    386       C  
ATOM    631  CD2 PHE A  79     -31.903   3.296 -22.821  1.00 44.20           C  
ANISOU  631  CD2 PHE A  79     7831   3904   5057   -874    602    347       C  
ATOM    632  CE1 PHE A  79     -34.622   3.632 -23.182  1.00 46.84           C  
ANISOU  632  CE1 PHE A  79     8277   4120   5402   -453    415    396       C  
ATOM    633  CE2 PHE A  79     -32.522   4.458 -22.366  1.00 56.45           C  
ANISOU  633  CE2 PHE A  79     9560   5252   6638   -810    564    350       C  
ATOM    634  CZ  PHE A  79     -33.881   4.627 -22.546  1.00 52.78           C  
ANISOU  634  CZ  PHE A  79     9151   4725   6176   -582    477    372       C  
ATOM    635  N   LEU A  80     -31.707  -2.034 -24.568  1.00 37.11           N  
ANISOU  635  N   LEU A  80     6397   3662   4040   -690    550    249       N  
ATOM    636  CA  LEU A  80     -30.886  -2.967 -25.331  1.00 41.72           C  
ANISOU  636  CA  LEU A  80     6941   4370   4543   -708    609    235       C  
ATOM    637  C   LEU A  80     -31.173  -2.777 -26.808  1.00 44.06           C  
ANISOU  637  C   LEU A  80     7404   4637   4698   -667    603    309       C  
ATOM    638  O   LEU A  80     -32.332  -2.658 -27.213  1.00 45.05           O  
ANISOU  638  O   LEU A  80     7618   4697   4803   -571    490    343       O  
ATOM    639  CB  LEU A  80     -31.152  -4.425 -24.926  1.00 41.00           C  
ANISOU  639  CB  LEU A  80     6717   4371   4488   -628    540    154       C  
ATOM    640  CG  LEU A  80     -30.220  -5.425 -25.604  1.00 41.18           C  
ANISOU  640  CG  LEU A  80     6709   4510   4429   -618    607    120       C  
ATOM    641  CD1 LEU A  80     -28.787  -5.213 -25.100  1.00 44.01           C  
ANISOU  641  CD1 LEU A  80     6949   4958   4814   -721    741    106       C  
ATOM    642  CD2 LEU A  80     -30.675  -6.848 -25.409  1.00 39.71           C  
ANISOU  642  CD2 LEU A  80     6464   4363   4262   -526    510     51       C  
ATOM    643  N   LYS A  81     -30.109  -2.738 -27.609  1.00 45.16           N  
ANISOU  643  N   LYS A  81     7579   4846   4733   -740    725    340       N  
ATOM    644  CA  LYS A  81     -30.204  -2.700 -29.058  1.00 42.39           C  
ANISOU  644  CA  LYS A  81     7389   4501   4218   -706    740    405       C  
ATOM    645  C   LYS A  81     -29.559  -3.970 -29.591  1.00 47.54           C  
ANISOU  645  C   LYS A  81     7978   5303   4783   -656    793    337       C  
ATOM    646  O   LYS A  81     -28.432  -4.292 -29.201  1.00 43.17           O  
ANISOU  646  O   LYS A  81     7288   4862   4254   -710    909    297       O  
ATOM    647  CB  LYS A  81     -29.474  -1.477 -29.618  1.00 45.14           C  
ANISOU  647  CB  LYS A  81     7856   4806   4489   -838    860    513       C  
ATOM    648  CG  LYS A  81     -30.080  -0.164 -29.193  1.00 57.43           C  
ANISOU  648  CG  LYS A  81     9530   6177   6115   -874    806    581       C  
ATOM    649  CD  LYS A  81     -31.387   0.148 -29.892  1.00 75.79           C  
ANISOU  649  CD  LYS A  81    12024   8392   8382   -740    672    643       C  
ATOM    650  CE  LYS A  81     -31.824   1.590 -29.609  1.00 70.92           C  
ANISOU  650  CE  LYS A  81    11561   7575   7812   -761    642    724       C  
ATOM    651  NZ  LYS A  81     -31.788   2.459 -30.817  1.00 79.99           N  
ANISOU  651  NZ  LYS A  81    12949   8632   8813   -793    665    864       N  
ATOM    652  N   ILE A  82     -30.274  -4.693 -30.455  1.00 43.97           N  
ANISOU  652  N   ILE A  82     7627   4853   4228   -546    700    320       N  
ATOM    653  CA  ILE A  82     -29.723  -5.833 -31.190  1.00 45.00           C  
ANISOU  653  CA  ILE A  82     7768   5095   4235   -478    747    252       C  
ATOM    654  C   ILE A  82     -29.824  -5.542 -32.683  1.00 46.03           C  
ANISOU  654  C   ILE A  82     8104   5230   4154   -455    771    320       C  
ATOM    655  O   ILE A  82     -30.930  -5.381 -33.215  1.00 50.62           O  
ANISOU  655  O   ILE A  82     8822   5728   4684   -407    627    358       O  
ATOM    656  CB  ILE A  82     -30.447  -7.146 -30.857  1.00 49.78           C  
ANISOU  656  CB  ILE A  82     8336   5691   4888   -376    600    151       C  
ATOM    657  CG1 ILE A  82     -30.613  -7.336 -29.347  1.00 43.72           C  
ANISOU  657  CG1 ILE A  82     7387   4902   4321   -400    550    107       C  
ATOM    658  CG2 ILE A  82     -29.696  -8.340 -31.471  1.00 50.45           C  
ANISOU  658  CG2 ILE A  82     8444   5871   4854   -292    663     62       C  
ATOM    659  CD1 ILE A  82     -31.111  -8.733 -28.984  1.00 43.15           C  
ANISOU  659  CD1 ILE A  82     7276   4828   4290   -325    427     16       C  
ATOM    660  N   THR A  82A    -28.681  -5.509 -33.369  1.00 51.61           N  
ANISOU  660  N   THR A  82A    8826   6054   4729   -486    949    337       N  
ATOM    661  CA  THR A  82A    -28.660  -5.204 -34.793  1.00 52.37           C  
ANISOU  661  CA  THR A  82A    9124   6174   4600   -474    997    409       C  
ATOM    662  C   THR A  82A    -28.854  -6.463 -35.634  1.00 57.75           C  
ANISOU  662  C   THR A  82A    9906   6911   5125   -333    947    309       C  
ATOM    663  O   THR A  82A    -28.527  -7.576 -35.210  1.00 52.06           O  
ANISOU  663  O   THR A  82A    9086   6244   4451   -253    949    186       O  
ATOM    664  CB  THR A  82A    -27.347  -4.520 -35.183  1.00 52.61           C  
ANISOU  664  CB  THR A  82A    9124   6323   4541   -588   1229    489       C  
ATOM    665  OG1 THR A  82A    -26.243  -5.273 -34.665  1.00 48.34           O  
ANISOU  665  OG1 THR A  82A    8377   5939   4050   -571   1359    401       O  
ATOM    666  CG2 THR A  82A    -27.296  -3.098 -34.638  1.00 58.95           C  
ANISOU  666  CG2 THR A  82A    9922   7024   5452   -753   1252    610       C  
ATOM    667  N   SER A  82B    -29.429  -6.265 -36.824  1.00 54.13           N  
ANISOU  667  N   SER A  82B    9668   6424   4474   -300    887    363       N  
ATOM    668  CA  SER A  82B    -29.507  -7.271 -37.891  1.00 53.95           C  
ANISOU  668  CA  SER A  82B    9804   6456   4238   -183    858    280       C  
ATOM    669  C   SER A  82B    -30.174  -8.566 -37.424  1.00 55.28           C  
ANISOU  669  C   SER A  82B    9946   6569   4490    -90    682    137       C  
ATOM    670  O   SER A  82B    -29.584  -9.646 -37.476  1.00 61.97           O  
ANISOU  670  O   SER A  82B   10782   7478   5288      1    737     14       O  
ATOM    671  CB  SER A  82B    -28.118  -7.575 -38.456  1.00 65.57           C  
ANISOU  671  CB  SER A  82B   11258   8102   5555   -153   1104    248       C  
ATOM    672  OG  SER A  82B    -27.457  -6.399 -38.850  1.00 60.99           O  
ANISOU  672  OG  SER A  82B   10688   7584   4901   -273   1275    394       O  
ATOM    673  N   VAL A  82C    -31.433  -8.450 -36.992  1.00 57.57           N  
ANISOU  673  N   VAL A  82C   10233   6742   4898   -110    466    160       N  
ATOM    674  CA  VAL A  82C    -32.109  -9.592 -36.389  1.00 50.50           C  
ANISOU  674  CA  VAL A  82C    9286   5791   4109    -66    294     49       C  
ATOM    675  C   VAL A  82C    -32.504 -10.608 -37.458  1.00 53.94           C  
ANISOU  675  C   VAL A  82C    9936   6217   4342     11    177    -39       C  
ATOM    676  O   VAL A  82C    -32.646 -10.283 -38.648  1.00 60.44           O  
ANISOU  676  O   VAL A  82C   10953   7061   4949     29    170      5       O  
ATOM    677  CB  VAL A  82C    -33.337  -9.130 -35.584  1.00 52.76           C  
ANISOU  677  CB  VAL A  82C    9476   5990   4580   -118    113    110       C  
ATOM    678  CG1 VAL A  82C    -32.907  -8.190 -34.482  1.00 54.54           C  
ANISOU  678  CG1 VAL A  82C    9518   6211   4993   -184    228    172       C  
ATOM    679  CG2 VAL A  82C    -34.359  -8.467 -36.492  1.00 59.28           C  
ANISOU  679  CG2 VAL A  82C   10455   6777   5291   -116    -28    209       C  
ATOM    680  N   ASP A  83     -32.657 -11.861 -37.032  1.00 57.59           N  
ANISOU  680  N   ASP A  83    10383   6637   4860     54     81   -165       N  
ATOM    681  CA  ASP A  83     -33.213 -12.913 -37.871  1.00 53.11           C  
ANISOU  681  CA  ASP A  83    10032   6019   4130    104    -82   -262       C  
ATOM    682  C   ASP A  83     -34.119 -13.770 -36.995  1.00 58.00           C  
ANISOU  682  C   ASP A  83    10575   6540   4921     57   -294   -315       C  
ATOM    683  O   ASP A  83     -34.422 -13.415 -35.851  1.00 52.81           O  
ANISOU  683  O   ASP A  83     9706   5873   4488     -7   -314   -259       O  
ATOM    684  CB  ASP A  83     -32.101 -13.720 -38.563  1.00 54.99           C  
ANISOU  684  CB  ASP A  83    10408   6308   4177    229     74   -385       C  
ATOM    685  CG  ASP A  83     -31.147 -14.401 -37.586  1.00 65.87           C  
ANISOU  685  CG  ASP A  83    11625   7704   5698    292    201   -470       C  
ATOM    686  OD1 ASP A  83     -31.431 -14.458 -36.371  1.00 70.19           O  
ANISOU  686  OD1 ASP A  83    11984   8203   6481    230    136   -452       O  
ATOM    687  OD2 ASP A  83     -30.096 -14.898 -38.048  1.00 74.60           O1-
ANISOU  687  OD2 ASP A  83    12794   8883   6669    419    369   -555       O1-
ATOM    688  N   THR A  84     -34.539 -14.923 -37.526  1.00 59.10           N  
ANISOU  688  N   THR A  84    10901   6608   4947     80   -453   -424       N  
ATOM    689  CA  THR A  84     -35.478 -15.772 -36.801  1.00 56.23           C  
ANISOU  689  CA  THR A  84    10489   6148   4728      1   -674   -459       C  
ATOM    690  C   THR A  84     -34.899 -16.292 -35.492  1.00 53.94           C  
ANISOU  690  C   THR A  84    10021   5832   4642     12   -591   -500       C  
ATOM    691  O   THR A  84     -35.662 -16.598 -34.569  1.00 56.05           O  
ANISOU  691  O   THR A  84    10162   6051   5084    -82   -729   -474       O  
ATOM    692  CB  THR A  84     -35.914 -16.942 -37.680  1.00 66.56           C  
ANISOU  692  CB  THR A  84    12072   7364   5856     10   -859   -577       C  
ATOM    693  OG1 THR A  84     -34.752 -17.607 -38.192  1.00 65.25           O  
ANISOU  693  OG1 THR A  84    12073   7187   5533    156   -700   -706       O  
ATOM    694  CG2 THR A  84     -36.756 -16.435 -38.855  1.00 65.22           C  
ANISOU  694  CG2 THR A  84    12057   7224   5500    -31  -1005   -520       C  
ATOM    695  N   ALA A  85     -33.573 -16.384 -35.379  1.00 50.75           N  
ANISOU  695  N   ALA A  85     9591   5475   4215    122   -368   -554       N  
ATOM    696  CA  ALA A  85     -32.956 -16.814 -34.131  1.00 58.34           C  
ANISOU  696  CA  ALA A  85    10375   6428   5362    143   -290   -582       C  
ATOM    697  C   ALA A  85     -33.126 -15.804 -33.003  1.00 49.46           C  
ANISOU  697  C   ALA A  85     8981   5361   4451     48   -243   -465       C  
ATOM    698  O   ALA A  85     -32.806 -16.126 -31.851  1.00 56.64           O  
ANISOU  698  O   ALA A  85     9735   6264   5524     41   -214   -476       O  
ATOM    699  CB  ALA A  85     -31.469 -17.102 -34.349  1.00 55.31           C  
ANISOU  699  CB  ALA A  85    10007   6116   4893    299    -63   -660       C  
ATOM    700  N   ASP A  86     -33.622 -14.604 -33.293  1.00 46.08           N  
ANISOU  700  N   ASP A  86     8512   4980   4015    -14   -240   -357       N  
ATOM    701  CA  ASP A  86     -33.843 -13.586 -32.274  1.00 49.20           C  
ANISOU  701  CA  ASP A  86     8690   5410   4595    -89   -202   -256       C  
ATOM    702  C   ASP A  86     -35.292 -13.528 -31.800  1.00 45.41           C  
ANISOU  702  C   ASP A  86     8142   4887   4224   -175   -408   -198       C  
ATOM    703  O   ASP A  86     -35.609 -12.729 -30.911  1.00 45.12           O  
ANISOU  703  O   ASP A  86     7933   4874   4336   -220   -387   -124       O  
ATOM    704  CB  ASP A  86     -33.395 -12.214 -32.793  1.00 49.73           C  
ANISOU  704  CB  ASP A  86     8757   5542   4596    -94    -53   -166       C  
ATOM    705  CG  ASP A  86     -31.916 -12.180 -33.149  1.00 55.02           C  
ANISOU  705  CG  ASP A  86     9438   6296   5173    -33    174   -202       C  
ATOM    706  OD1 ASP A  86     -31.081 -12.483 -32.263  1.00 49.73           O  
ANISOU  706  OD1 ASP A  86     8618   5664   4613    -18    276   -242       O  
ATOM    707  OD2 ASP A  86     -31.584 -11.847 -34.309  1.00 51.39           O1-
ANISOU  707  OD2 ASP A  86     9124   5878   4522     -1    251   -183       O1-
ATOM    708  N   THR A  87     -36.173 -14.347 -32.380  1.00 44.14           N  
ANISOU  708  N   THR A  87     8111   4673   3986   -200   -605   -232       N  
ATOM    709  CA  THR A  87     -37.509 -14.557 -31.834  1.00 53.75           C  
ANISOU  709  CA  THR A  87     9230   5875   5316   -296   -807   -183       C  
ATOM    710  C   THR A  87     -37.405 -15.179 -30.451  1.00 45.78           C  
ANISOU  710  C   THR A  87     8061   4846   4488   -340   -798   -204       C  
ATOM    711  O   THR A  87     -36.848 -16.269 -30.297  1.00 43.96           O  
ANISOU  711  O   THR A  87     7910   4551   4243   -320   -796   -294       O  
ATOM    712  CB  THR A  87     -38.317 -15.460 -32.769  1.00 49.29           C  
ANISOU  712  CB  THR A  87     8852   5258   4620   -340  -1026   -226       C  
ATOM    713  OG1 THR A  87     -38.519 -14.792 -34.022  1.00 53.10           O  
ANISOU  713  OG1 THR A  87     9477   5773   4926   -302  -1050   -190       O  
ATOM    714  CG2 THR A  87     -39.666 -15.819 -32.156  1.00 51.29           C  
ANISOU  714  CG2 THR A  87     8974   5517   4995   -466  -1238   -171       C  
ATOM    715  N   ALA A  88     -37.925 -14.481 -29.441  1.00 45.95           N  
ANISOU  715  N   ALA A  88     7872   4920   4666   -384   -788   -123       N  
ATOM    716  CA  ALA A  88     -37.723 -14.891 -28.056  1.00 46.52           C  
ANISOU  716  CA  ALA A  88     7786   4993   4897   -421   -750   -131       C  
ATOM    717  C   ALA A  88     -38.571 -14.011 -27.148  1.00 35.79           C  
ANISOU  717  C   ALA A  88     6218   3706   3672   -462   -761    -37       C  
ATOM    718  O   ALA A  88     -39.097 -12.976 -27.564  1.00 39.73           O  
ANISOU  718  O   ALA A  88     6698   4246   4152   -435   -767     29       O  
ATOM    719  CB  ALA A  88     -36.249 -14.798 -27.647  1.00 45.01           C  
ANISOU  719  CB  ALA A  88     7575   4806   4720   -348   -548   -183       C  
ATOM    720  N   THR A  89     -38.707 -14.453 -25.900  1.00 38.46           N  
ANISOU  720  N   THR A  89     6414   4058   4139   -516   -765    -31       N  
ATOM    721  CA  THR A  89     -39.174 -13.596 -24.822  1.00 37.95           C  
ANISOU  721  CA  THR A  89     6150   4070   4198   -526   -714     36       C  
ATOM    722  C   THR A  89     -37.947 -12.965 -24.186  1.00 40.81           C  
ANISOU  722  C   THR A  89     6475   4433   4599   -474   -522      5       C  
ATOM    723  O   THR A  89     -36.990 -13.672 -23.848  1.00 39.03           O  
ANISOU  723  O   THR A  89     6273   4178   4377   -469   -464    -54       O  
ATOM    724  CB  THR A  89     -39.981 -14.390 -23.792  1.00 39.22           C  
ANISOU  724  CB  THR A  89     6177   4266   4457   -623   -813     67       C  
ATOM    725  OG1 THR A  89     -41.067 -15.051 -24.451  1.00 46.33           O  
ANISOU  725  OG1 THR A  89     7115   5171   5317   -703  -1006     97       O  
ATOM    726  CG2 THR A  89     -40.538 -13.479 -22.710  1.00 43.23           C  
ANISOU  726  CG2 THR A  89     6482   4871   5070   -613   -752    130       C  
ATOM    727  N   TYR A  90     -37.957 -11.640 -24.068  1.00 35.89           N  
ANISOU  727  N   TYR A  90     5802   3837   3998   -433   -434     46       N  
ATOM    728  CA  TYR A  90     -36.832 -10.884 -23.533  1.00 36.58           C  
ANISOU  728  CA  TYR A  90     5863   3922   4115   -412   -266     24       C  
ATOM    729  C   TYR A  90     -37.168 -10.447 -22.118  1.00 38.88           C  
ANISOU  729  C   TYR A  90     5995   4254   4522   -432   -235     43       C  
ATOM    730  O   TYR A  90     -38.281  -9.984 -21.864  1.00 43.52           O  
ANISOU  730  O   TYR A  90     6512   4875   5148   -416   -294     94       O  
ATOM    731  CB  TYR A  90     -36.512  -9.670 -24.417  1.00 40.65           C  
ANISOU  731  CB  TYR A  90     6477   4410   4557   -371   -187     56       C  
ATOM    732  CG  TYR A  90     -35.839 -10.099 -25.701  1.00 40.44           C  
ANISOU  732  CG  TYR A  90     6606   4363   4396   -351   -168     26       C  
ATOM    733  CD1 TYR A  90     -36.590 -10.571 -26.770  1.00 43.16           C  
ANISOU  733  CD1 TYR A  90     7064   4692   4643   -335   -298     37       C  
ATOM    734  CD2 TYR A  90     -34.458 -10.057 -25.836  1.00 37.06           C  
ANISOU  734  CD2 TYR A  90     6206   3948   3928   -348    -21    -13       C  
ATOM    735  CE1 TYR A  90     -35.993 -10.991 -27.926  1.00 42.42           C  
ANISOU  735  CE1 TYR A  90     7130   4582   4404   -306   -277     -1       C  
ATOM    736  CE2 TYR A  90     -33.844 -10.478 -27.004  1.00 38.82           C  
ANISOU  736  CE2 TYR A  90     6564   4174   4012   -312     14    -44       C  
ATOM    737  CZ  TYR A  90     -34.621 -10.937 -28.049  1.00 41.08           C  
ANISOU  737  CZ  TYR A  90     6987   4431   4191   -285   -111    -42       C  
ATOM    738  OH  TYR A  90     -34.041 -11.372 -29.218  1.00 43.92           O  
ANISOU  738  OH  TYR A  90     7503   4795   4390   -238    -74    -82       O  
ATOM    739  N   TYR A  91     -36.210 -10.622 -21.205  1.00 35.58           N  
ANISOU  739  N   TYR A  91     5519   3849   4151   -455   -145      1       N  
ATOM    740  CA  TYR A  91     -36.386 -10.336 -19.789  1.00 34.92           C  
ANISOU  740  CA  TYR A  91     5303   3808   4155   -478   -112      5       C  
ATOM    741  C   TYR A  91     -35.289  -9.389 -19.339  1.00 35.58           C  
ANISOU  741  C   TYR A  91     5385   3883   4251   -484     22    -24       C  
ATOM    742  O   TYR A  91     -34.151  -9.465 -19.817  1.00 34.40           O  
ANISOU  742  O   TYR A  91     5284   3725   4061   -494     90    -54       O  
ATOM    743  CB  TYR A  91     -36.265 -11.601 -18.912  1.00 34.75           C  
ANISOU  743  CB  TYR A  91     5212   3815   4174   -524   -158    -13       C  
ATOM    744  CG  TYR A  91     -37.271 -12.682 -19.182  1.00 36.37           C  
ANISOU  744  CG  TYR A  91     5423   4020   4376   -561   -301     18       C  
ATOM    745  CD1 TYR A  91     -36.996 -13.673 -20.121  1.00 37.24           C  
ANISOU  745  CD1 TYR A  91     5658   4066   4424   -563   -370    -12       C  
ATOM    746  CD2 TYR A  91     -38.474 -12.751 -18.483  1.00 39.24           C  
ANISOU  746  CD2 TYR A  91     5669   4450   4790   -602   -366     75       C  
ATOM    747  CE1 TYR A  91     -37.895 -14.691 -20.366  1.00 40.32           C  
ANISOU  747  CE1 TYR A  91     6078   4436   4807   -625   -518     13       C  
ATOM    748  CE2 TYR A  91     -39.385 -13.770 -18.731  1.00 37.70           C  
ANISOU  748  CE2 TYR A  91     5470   4262   4592   -674   -507    114       C  
ATOM    749  CZ  TYR A  91     -39.086 -14.734 -19.680  1.00 42.48           C  
ANISOU  749  CZ  TYR A  91     6223   4780   5139   -695   -592     81       C  
ATOM    750  OH  TYR A  91     -39.971 -15.754 -19.940  1.00 44.75           O  
ANISOU  750  OH  TYR A  91     6531   5052   5418   -791   -748    116       O  
ATOM    751  N   CYS A  92     -35.610  -8.538 -18.379  1.00 35.01           N  
ANISOU  751  N   CYS A  92     5250   3823   4229   -484     59    -18       N  
ATOM    752  CA  CYS A  92     -34.584  -7.806 -17.654  1.00 36.97           C  
ANISOU  752  CA  CYS A  92     5486   4066   4496   -524    161    -56       C  
ATOM    753  C   CYS A  92     -34.653  -8.214 -16.188  1.00 37.43           C  
ANISOU  753  C   CYS A  92     5430   4187   4604   -551    155    -78       C  
ATOM    754  O   CYS A  92     -35.695  -8.662 -15.708  1.00 38.56           O  
ANISOU  754  O   CYS A  92     5508   4373   4771   -531     93    -52       O  
ATOM    755  CB  CYS A  92     -34.716  -6.267 -17.839  1.00 43.21           C  
ANISOU  755  CB  CYS A  92     6361   4781   5277   -506    217    -42       C  
ATOM    756  SG  CYS A  92     -36.257  -5.457 -17.322  1.00 45.40           S  
ANISOU  756  SG  CYS A  92     6622   5044   5586   -408    179    -14       S  
ATOM    757  N   ALA A  93     -33.522  -8.120 -15.494  1.00 34.12           N  
ANISOU  757  N   ALA A  93     4979   3791   4194   -605    214   -119       N  
ATOM    758  CA  ALA A  93     -33.468  -8.571 -14.112  1.00 34.82           C  
ANISOU  758  CA  ALA A  93     4973   3946   4312   -633    202   -138       C  
ATOM    759  C   ALA A  93     -32.425  -7.761 -13.367  1.00 40.29           C  
ANISOU  759  C   ALA A  93     5658   4647   5004   -695    270   -184       C  
ATOM    760  O   ALA A  93     -31.401  -7.378 -13.939  1.00 34.74           O  
ANISOU  760  O   ALA A  93     4984   3928   4287   -738    319   -196       O  
ATOM    761  CB  ALA A  93     -33.152 -10.069 -13.998  1.00 30.94           C  
ANISOU  761  CB  ALA A  93     4434   3497   3825   -638    143   -129       C  
ATOM    762  N   ARG A  94     -32.697  -7.501 -12.089  1.00 31.79           N  
ANISOU  762  N   ARG A  94     4539   3606   3934   -710    271   -206       N  
ATOM    763  CA  ARG A  94     -31.809  -6.702 -11.259  1.00 32.57           C  
ANISOU  763  CA  ARG A  94     4644   3710   4022   -783    315   -259       C  
ATOM    764  C   ARG A  94     -30.885  -7.596 -10.445  1.00 34.20           C  
ANISOU  764  C   ARG A  94     4751   4014   4227   -832    286   -270       C  
ATOM    765  O   ARG A  94     -31.304  -8.645  -9.946  1.00 31.99           O  
ANISOU  765  O   ARG A  94     4414   3791   3952   -800    235   -242       O  
ATOM    766  CB  ARG A  94     -32.609  -5.811 -10.307  1.00 32.90           C  
ANISOU  766  CB  ARG A  94     4724   3728   4047   -757    333   -292       C  
ATOM    767  CG  ARG A  94     -31.730  -4.954  -9.418  1.00 34.79           C  
ANISOU  767  CG  ARG A  94     5004   3955   4262   -846    361   -359       C  
ATOM    768  CD  ARG A  94     -32.548  -4.139  -8.428  1.00 28.23           C  
ANISOU  768  CD  ARG A  94     4236   3095   3394   -796    383   -408       C  
ATOM    769  NE  ARG A  94     -33.026  -4.906  -7.291  1.00 35.29           N  
ANISOU  769  NE  ARG A  94     5039   4109   4262   -769    363   -407       N  
ATOM    770  CZ  ARG A  94     -33.567  -4.331  -6.229  1.00 43.97           C  
ANISOU  770  CZ  ARG A  94     6178   5222   5307   -728    391   -460       C  
ATOM    771  NH1 ARG A  94     -33.721  -3.018  -6.166  1.00 40.47           N  
ANISOU  771  NH1 ARG A  94     5876   4662   4838   -697    432   -525       N  
ATOM    772  NH2 ARG A  94     -33.951  -5.085  -5.202  1.00 34.57           N  
ANISOU  772  NH2 ARG A  94     4901   4158   4077   -716    380   -445       N  
ATOM    773  N   ARG A  95     -29.641  -7.154 -10.275  1.00 32.47           N  
ANISOU  773  N   ARG A  95     4514   3821   4002   -916    313   -302       N  
ATOM    774  CA  ARG A  95     -28.749  -7.721  -9.274  1.00 35.05           C  
ANISOU  774  CA  ARG A  95     4742   4254   4321   -963    278   -317       C  
ATOM    775  C   ARG A  95     -28.218  -6.615  -8.368  1.00 36.65           C  
ANISOU  775  C   ARG A  95     4969   4460   4497  -1070    290   -374       C  
ATOM    776  O   ARG A  95     -27.779  -5.562  -8.850  1.00 33.73           O  
ANISOU  776  O   ARG A  95     4662   4026   4126  -1147    333   -395       O  
ATOM    777  CB  ARG A  95     -27.582  -8.466  -9.930  1.00 33.20           C  
ANISOU  777  CB  ARG A  95     4423   4088   4101   -959    278   -297       C  
ATOM    778  CG  ARG A  95     -26.637  -9.128  -8.929  1.00 32.57           C  
ANISOU  778  CG  ARG A  95     4227   4131   4016   -981    227   -302       C  
ATOM    779  CD  ARG A  95     -25.408  -8.293  -8.587  1.00 30.87           C  
ANISOU  779  CD  ARG A  95     3946   3992   3793  -1106    245   -333       C  
ATOM    780  NE  ARG A  95     -24.675  -8.943  -7.504  1.00 37.56           N  
ANISOU  780  NE  ARG A  95     4680   4966   4627  -1114    173   -332       N  
ATOM    781  CZ  ARG A  95     -23.467  -8.592  -7.087  1.00 39.95           C  
ANISOU  781  CZ  ARG A  95     4873   5384   4922  -1212    155   -346       C  
ATOM    782  NH1 ARG A  95     -22.817  -7.573  -7.625  1.00 36.69           N  
ANISOU  782  NH1 ARG A  95     4451   4976   4516  -1336    210   -362       N  
ATOM    783  NH2 ARG A  95     -22.884  -9.297  -6.120  1.00 38.04           N  
ANISOU  783  NH2 ARG A  95     4528   5264   4663  -1194     73   -335       N  
ATOM    784  N   VAL A  96     -28.219  -6.878  -7.055  1.00 31.34           N  
ANISOU  784  N   VAL A  96     4258   3857   3791  -1087    246   -396       N  
ATOM    785  CA  VAL A  96     -27.758  -5.924  -6.051  1.00 31.74           C  
ANISOU  785  CA  VAL A  96     4349   3916   3796  -1191    238   -463       C  
ATOM    786  C   VAL A  96     -26.485  -6.485  -5.442  1.00 35.29           C  
ANISOU  786  C   VAL A  96     4671   4502   4235  -1265    179   -459       C  
ATOM    787  O   VAL A  96     -26.382  -7.696  -5.228  1.00 36.73           O  
ANISOU  787  O   VAL A  96     4760   4770   4425  -1196    134   -412       O  
ATOM    788  CB  VAL A  96     -28.816  -5.712  -4.946  1.00 37.04           C  
ANISOU  788  CB  VAL A  96     5087   4577   4410  -1142    236   -497       C  
ATOM    789  CG1 VAL A  96     -28.366  -4.605  -3.995  1.00 36.57           C  
ANISOU  789  CG1 VAL A  96     5116   4495   4286  -1245    228   -586       C  
ATOM    790  CG2 VAL A  96     -30.178  -5.430  -5.553  1.00 38.34           C  
ANISOU  790  CG2 VAL A  96     5326   4649   4592  -1029    287   -480       C  
ATOM    791  N   VAL A  97     -25.525  -5.607  -5.139  1.00 36.62           N  
ANISOU  791  N   VAL A  97     4840   4688   4384  -1408    167   -506       N  
ATOM    792  CA  VAL A  97     -24.254  -6.059  -4.583  1.00 38.66           C  
ANISOU  792  CA  VAL A  97     4951   5105   4634  -1485    100   -497       C  
ATOM    793  C   VAL A  97     -24.499  -6.907  -3.335  1.00 40.67           C  
ANISOU  793  C   VAL A  97     5169   5448   4835  -1427     24   -490       C  
ATOM    794  O   VAL A  97     -25.330  -6.569  -2.482  1.00 37.45           O  
ANISOU  794  O   VAL A  97     4868   4996   4365  -1417     21   -530       O  
ATOM    795  CB  VAL A  97     -23.350  -4.855  -4.262  1.00 42.09           C  
ANISOU  795  CB  VAL A  97     5407   5542   5042  -1684     81   -553       C  
ATOM    796  CG1 VAL A  97     -24.105  -3.848  -3.402  1.00 42.77           C  
ANISOU  796  CG1 VAL A  97     5686   5505   5060  -1728     74   -638       C  
ATOM    797  CG2 VAL A  97     -22.057  -5.305  -3.581  1.00 42.45           C  
ANISOU  797  CG2 VAL A  97     5273   5782   5073  -1769     -8   -541       C  
ATOM    798  N   ALA A  98     -23.772  -8.021  -3.246  1.00 43.20           N  
ANISOU  798  N   ALA A  98     5344   5896   5174  -1375    -33   -435       N  
ATOM    799  CA  ALA A  98     -23.808  -8.935  -2.113  1.00 42.24           C  
ANISOU  799  CA  ALA A  98     5182   5867   4999  -1324   -119   -405       C  
ATOM    800  C   ALA A  98     -22.530  -9.765  -2.155  1.00 44.53           C  
ANISOU  800  C   ALA A  98     5298   6306   5317  -1295   -187   -356       C  
ATOM    801  O   ALA A  98     -21.706  -9.618  -3.063  1.00 42.92           O  
ANISOU  801  O   ALA A  98     4996   6143   5168  -1312   -151   -350       O  
ATOM    802  CB  ALA A  98     -25.058  -9.822  -2.153  1.00 45.90           C  
ANISOU  802  CB  ALA A  98     5714   6261   5465  -1193   -101   -354       C  
ATOM    803  N   THR A  99     -22.369 -10.658  -1.170  1.00 43.99           N  
ANISOU  803  N   THR A  99     5188   6327   5201  -1241   -282   -314       N  
ATOM    804  CA  THR A  99     -21.258 -11.607  -1.231  1.00 42.59           C  
ANISOU  804  CA  THR A  99     4849   6283   5052  -1159   -353   -256       C  
ATOM    805  C   THR A  99     -21.514 -12.736  -2.226  1.00 41.92           C  
ANISOU  805  C   THR A  99     4766   6128   5033   -983   -318   -198       C  
ATOM    806  O   THR A  99     -20.564 -13.401  -2.648  1.00 41.87           O  
ANISOU  806  O   THR A  99     4632   6212   5064   -884   -342   -165       O  
ATOM    807  CB  THR A  99     -20.974 -12.204   0.148  1.00 43.77           C  
ANISOU  807  CB  THR A  99     4971   6540   5120  -1148   -481   -219       C  
ATOM    808  OG1 THR A  99     -22.182 -12.751   0.680  1.00 48.15           O  
ANISOU  808  OG1 THR A  99     5669   6998   5626  -1093   -481   -185       O  
ATOM    809  CG2 THR A  99     -20.429 -11.141   1.090  1.00 45.27           C  
ANISOU  809  CG2 THR A  99     5141   6827   5233  -1326   -539   -284       C  
ATOM    810  N   ASP A 100     -22.767 -12.973  -2.589  1.00 41.39           N  
ANISOU  810  N   ASP A 100     4841   5910   4975   -937   -269   -189       N  
ATOM    811  CA  ASP A 100     -23.151 -13.868  -3.672  1.00 36.57           C  
ANISOU  811  CA  ASP A 100     4272   5201   4420   -803   -236   -153       C  
ATOM    812  C   ASP A 100     -23.555 -13.035  -4.881  1.00 41.09           C  
ANISOU  812  C   ASP A 100     4893   5685   5033   -841   -125   -198       C  
ATOM    813  O   ASP A 100     -23.557 -11.800  -4.841  1.00 45.22           O  
ANISOU  813  O   ASP A 100     5427   6210   5546   -964    -77   -248       O  
ATOM    814  CB  ASP A 100     -24.282 -14.792  -3.209  1.00 49.37           C  
ANISOU  814  CB  ASP A 100     6013   6726   6018   -751   -281    -95       C  
ATOM    815  CG  ASP A 100     -23.920 -15.569  -1.954  1.00 50.24           C  
ANISOU  815  CG  ASP A 100     6101   6916   6073   -725   -392    -36       C  
ATOM    816  OD1 ASP A 100     -22.904 -16.293  -1.986  1.00 47.96           O  
ANISOU  816  OD1 ASP A 100     5729   6693   5799   -624   -455     -5       O  
ATOM    817  OD2 ASP A 100     -24.608 -15.427  -0.924  1.00 50.89           O  
ANISOU  817  OD2 ASP A 100     6244   7007   6086   -797   -415    -18       O  
ATOM    818  N   TRP A 100A    -23.884 -13.708  -5.982  1.00 37.45           N  
ANISOU  818  N   TRP A 100A    4482   5138   4610   -734    -93   -179       N  
ATOM    819  CA  TRP A 100A    -24.257 -13.016  -7.215  1.00 38.11           C  
ANISOU  819  CA  TRP A 100A    4620   5141   4718   -754      2   -210       C  
ATOM    820  C   TRP A 100A    -25.525 -13.659  -7.757  1.00 35.49           C  
ANISOU  820  C   TRP A 100A    4419   4670   4396   -689     -5   -185       C  
ATOM    821  O   TRP A 100A    -25.474 -14.767  -8.295  1.00 37.85           O  
ANISOU  821  O   TRP A 100A    4750   4925   4706   -576    -37   -160       O  
ATOM    822  CB  TRP A 100A    -23.125 -13.057  -8.254  1.00 37.50           C  
ANISOU  822  CB  TRP A 100A    4449   5136   4662   -702     60   -220       C  
ATOM    823  CG  TRP A 100A    -23.141 -11.873  -9.185  1.00 36.24           C  
ANISOU  823  CG  TRP A 100A    4316   4946   4507   -794    162   -249       C  
ATOM    824  CD1 TRP A 100A    -22.232 -10.849  -9.216  1.00 38.32           C  
ANISOU  824  CD1 TRP A 100A    4487   5305   4769   -921    210   -266       C  
ATOM    825  CD2 TRP A 100A    -24.100 -11.586 -10.219  1.00 34.01           C  
ANISOU  825  CD2 TRP A 100A    4167   4529   4225   -780    216   -252       C  
ATOM    826  NE1 TRP A 100A    -22.577  -9.939 -10.182  1.00 36.18           N  
ANISOU  826  NE1 TRP A 100A    4302   4948   4495   -985    296   -275       N  
ATOM    827  CE2 TRP A 100A    -23.717 -10.362 -10.812  1.00 32.72           C  
ANISOU  827  CE2 TRP A 100A    4000   4374   4056   -890    300   -268       C  
ATOM    828  CE3 TRP A 100A    -25.253 -12.235 -10.687  1.00 35.78           C  
ANISOU  828  CE3 TRP A 100A    4515   4630   4450   -698    191   -237       C  
ATOM    829  CZ2 TRP A 100A    -24.442  -9.767 -11.844  1.00 35.21           C  
ANISOU  829  CZ2 TRP A 100A    4439   4574   4363   -899    360   -266       C  
ATOM    830  CZ3 TRP A 100A    -25.972 -11.649 -11.719  1.00 34.65           C  
ANISOU  830  CZ3 TRP A 100A    4475   4392   4300   -711    245   -241       C  
ATOM    831  CH2 TRP A 100A    -25.553 -10.424 -12.297  1.00 33.51           C  
ANISOU  831  CH2 TRP A 100A    4331   4254   4145   -799    330   -254       C  
ATOM    832  N   TYR A 100B    -26.656 -12.957  -7.642  1.00 35.08           N  
ANISOU  832  N   TYR A 100B    4446   4548   4336   -757     20   -193       N  
ATOM    833  CA  TYR A 100B    -27.927 -13.504  -8.090  1.00 32.56           C  
ANISOU  833  CA  TYR A 100B    4221   4125   4024   -719      2   -160       C  
ATOM    834  C   TYR A 100B    -28.879 -12.381  -8.476  1.00 36.62           C  
ANISOU  834  C   TYR A 100B    4791   4584   4540   -768     63   -182       C  
ATOM    835  O   TYR A 100B    -28.834 -11.288  -7.913  1.00 35.06           O  
ANISOU  835  O   TYR A 100B    4586   4411   4325   -833    102   -218       O  
ATOM    836  CB  TYR A 100B    -28.543 -14.386  -6.987  1.00 33.76           C  
ANISOU  836  CB  TYR A 100B    4386   4285   4156   -722    -76   -104       C  
ATOM    837  CG  TYR A 100B    -28.757 -13.657  -5.675  1.00 35.02           C  
ANISOU  837  CG  TYR A 100B    4517   4520   4271   -801    -67   -115       C  
ATOM    838  CD1 TYR A 100B    -27.767 -13.652  -4.695  1.00 38.15           C  
ANISOU  838  CD1 TYR A 100B    4848   5014   4634   -825   -104   -124       C  
ATOM    839  CD2 TYR A 100B    -29.950 -12.991  -5.409  1.00 36.08           C  
ANISOU  839  CD2 TYR A 100B    4687   4636   4386   -840    -26   -119       C  
ATOM    840  CE1 TYR A 100B    -27.954 -12.989  -3.489  1.00 39.63           C  
ANISOU  840  CE1 TYR A 100B    5032   5266   4758   -898   -102   -145       C  
ATOM    841  CE2 TYR A 100B    -30.151 -12.332  -4.195  1.00 38.81           C  
ANISOU  841  CE2 TYR A 100B    5024   5050   4672   -892     -9   -142       C  
ATOM    842  CZ  TYR A 100B    -29.148 -12.333  -3.248  1.00 42.25           C  
ANISOU  842  CZ  TYR A 100B    5421   5569   5064   -927    -48   -159       C  
ATOM    843  OH  TYR A 100B    -29.350 -11.670  -2.056  1.00 40.33           O  
ANISOU  843  OH  TYR A 100B    5194   5390   4741   -979    -35   -194       O  
ATOM    844  N   PHE A 100C    -29.753 -12.665  -9.439  1.00 32.49           N  
ANISOU  844  N   PHE A 100C    4334   3978   4030   -728     60   -161       N  
ATOM    845  CA  PHE A 100C    -30.848 -11.749  -9.759  1.00 34.76           C  
ANISOU  845  CA  PHE A 100C    4669   4220   4319   -747     96   -164       C  
ATOM    846  C   PHE A 100C    -31.924 -11.818  -8.676  1.00 33.56           C  
ANISOU  846  C   PHE A 100C    4497   4102   4152   -769     73   -134       C  
ATOM    847  O   PHE A 100C    -32.495 -12.889  -8.452  1.00 36.71           O  
ANISOU  847  O   PHE A 100C    4889   4506   4553   -767     11    -78       O  
ATOM    848  CB  PHE A 100C    -31.441 -12.134 -11.106  1.00 34.18           C  
ANISOU  848  CB  PHE A 100C    4661   4070   4255   -700     79   -143       C  
ATOM    849  CG  PHE A 100C    -30.466 -11.990 -12.233  1.00 34.77           C  
ANISOU  849  CG  PHE A 100C    4765   4124   4322   -670    123   -171       C  
ATOM    850  CD1 PHE A 100C    -29.946 -10.744 -12.558  1.00 35.50           C  
ANISOU  850  CD1 PHE A 100C    4864   4218   4408   -708    203   -200       C  
ATOM    851  CD2 PHE A 100C    -30.044 -13.099 -12.935  1.00 36.56           C  
ANISOU  851  CD2 PHE A 100C    5021   4329   4540   -606     88   -168       C  
ATOM    852  CE1 PHE A 100C    -29.029 -10.606 -13.600  1.00 36.44           C  
ANISOU  852  CE1 PHE A 100C    4996   4342   4508   -695    259   -212       C  
ATOM    853  CE2 PHE A 100C    -29.122 -12.971 -13.977  1.00 35.60           C  
ANISOU  853  CE2 PHE A 100C    4918   4215   4395   -564    149   -196       C  
ATOM    854  CZ  PHE A 100C    -28.620 -11.730 -14.303  1.00 34.78           C  
ANISOU  854  CZ  PHE A 100C    4795   4138   4281   -615    238   -211       C  
ATOM    855  N   ASP A 101     -32.221 -10.687  -8.006  1.00 30.25           N  
ANISOU  855  N   ASP A 101     4078   3705   3710   -791    126   -170       N  
ATOM    856  CA  ASP A 101     -33.222 -10.766  -6.950  1.00 32.36           C  
ANISOU  856  CA  ASP A 101     4315   4033   3946   -795    124   -144       C  
ATOM    857  C   ASP A 101     -34.634 -10.469  -7.442  1.00 37.90           C  
ANISOU  857  C   ASP A 101     5018   4722   4662   -750    141   -112       C  
ATOM    858  O   ASP A 101     -35.603 -10.876  -6.785  1.00 35.86           O  
ANISOU  858  O   ASP A 101     4704   4537   4383   -754    132    -62       O  
ATOM    859  CB  ASP A 101     -32.862  -9.844  -5.763  1.00 33.77           C  
ANISOU  859  CB  ASP A 101     4500   4260   4070   -825    167   -205       C  
ATOM    860  CG  ASP A 101     -32.928  -8.340  -6.075  1.00 39.72           C  
ANISOU  860  CG  ASP A 101     5328   4944   4820   -809    235   -276       C  
ATOM    861  OD1 ASP A 101     -32.808  -7.891  -7.231  1.00 39.88           O  
ANISOU  861  OD1 ASP A 101     5394   4879   4879   -793    252   -281       O  
ATOM    862  OD2 ASP A 101     -33.125  -7.580  -5.093  1.00 39.81           O1-
ANISOU  862  OD2 ASP A 101     5372   4978   4775   -810    271   -328       O1-
ATOM    863  N   VAL A 102     -34.780  -9.771  -8.564  1.00 31.55           N  
ANISOU  863  N   VAL A 102     4265   3840   3883   -710    163   -131       N  
ATOM    864  CA  VAL A 102     -36.075  -9.385  -9.117  1.00 33.09           C  
ANISOU  864  CA  VAL A 102     4454   4029   4091   -650    168    -99       C  
ATOM    865  C   VAL A 102     -35.987  -9.442 -10.634  1.00 35.26           C  
ANISOU  865  C   VAL A 102     4787   4218   4391   -629    137    -85       C  
ATOM    866  O   VAL A 102     -35.010  -8.961 -11.222  1.00 33.43           O  
ANISOU  866  O   VAL A 102     4625   3918   4157   -638    167   -125       O  
ATOM    867  CB  VAL A 102     -36.501  -7.960  -8.677  1.00 41.43           C  
ANISOU  867  CB  VAL A 102     5544   5075   5123   -584    245   -149       C  
ATOM    868  CG1 VAL A 102     -37.878  -7.619  -9.238  1.00 39.41           C  
ANISOU  868  CG1 VAL A 102     5257   4835   4881   -491    243   -105       C  
ATOM    869  CG2 VAL A 102     -36.513  -7.820  -7.144  1.00 42.02           C  
ANISOU  869  CG2 VAL A 102     5586   5236   5145   -597    285   -182       C  
ATOM    870  N   TRP A 103     -37.035  -9.968 -11.270  1.00 35.36           N  
ANISOU  870  N   TRP A 103     4772   4246   4419   -611     77    -25       N  
ATOM    871  CA  TRP A 103     -37.119 -10.068 -12.719  1.00 32.89           C  
ANISOU  871  CA  TRP A 103     4525   3860   4109   -590     33    -10       C  
ATOM    872  C   TRP A 103     -38.353  -9.315 -13.189  1.00 33.92           C  
ANISOU  872  C   TRP A 103     4638   4007   4244   -518     24     24       C  
ATOM    873  O   TRP A 103     -39.305  -9.117 -12.428  1.00 33.41           O  
ANISOU  873  O   TRP A 103     4477   4031   4186   -488     36     51       O  
ATOM    874  CB  TRP A 103     -37.305 -11.517 -13.193  1.00 34.17           C  
ANISOU  874  CB  TRP A 103     4688   4020   4277   -640    -69     32       C  
ATOM    875  CG  TRP A 103     -36.142 -12.430 -13.104  1.00 34.44           C  
ANISOU  875  CG  TRP A 103     4764   4016   4304   -672    -82      6       C  
ATOM    876  CD1 TRP A 103     -35.515 -12.851 -11.962  1.00 34.97           C  
ANISOU  876  CD1 TRP A 103     4788   4123   4374   -704    -67     -2       C  
ATOM    877  CD2 TRP A 103     -35.508 -13.111 -14.186  1.00 34.75           C  
ANISOU  877  CD2 TRP A 103     4897   3980   4325   -657   -120    -14       C  
ATOM    878  NE1 TRP A 103     -34.514 -13.737 -12.273  1.00 37.89           N  
ANISOU  878  NE1 TRP A 103     5211   4447   4740   -697    -96    -21       N  
ATOM    879  CE2 TRP A 103     -34.489 -13.918 -13.632  1.00 38.83           C  
ANISOU  879  CE2 TRP A 103     5416   4495   4843   -662   -122    -34       C  
ATOM    880  CE3 TRP A 103     -35.702 -13.121 -15.572  1.00 31.30           C  
ANISOU  880  CE3 TRP A 103     4550   3484   3858   -627   -153    -18       C  
ATOM    881  CZ2 TRP A 103     -33.658 -14.724 -14.422  1.00 41.04           C  
ANISOU  881  CZ2 TRP A 103     5779   4714   5100   -619   -144    -64       C  
ATOM    882  CZ3 TRP A 103     -34.878 -13.923 -16.351  1.00 39.89           C  
ANISOU  882  CZ3 TRP A 103     5734   4512   4912   -600   -173    -53       C  
ATOM    883  CH2 TRP A 103     -33.872 -14.716 -15.771  1.00 39.05           C  
ANISOU  883  CH2 TRP A 103     5621   4403   4812   -587   -163    -78       C  
ATOM    884  N   GLY A 104     -38.351  -8.946 -14.462  1.00 34.36           N  
ANISOU  884  N   GLY A 104     4780   3989   4287   -480      2     30       N  
ATOM    885  CA  GLY A 104     -39.598  -8.616 -15.122  1.00 38.11           C  
ANISOU  885  CA  GLY A 104     5228   4490   4763   -414    -53     84       C  
ATOM    886  C   GLY A 104     -40.322  -9.875 -15.599  1.00 37.22           C  
ANISOU  886  C   GLY A 104     5059   4428   4652   -478   -176    142       C  
ATOM    887  O   GLY A 104     -39.769 -10.975 -15.566  1.00 35.86           O  
ANISOU  887  O   GLY A 104     4914   4235   4478   -561   -216    132       O  
ATOM    888  N   ALA A 105     -41.560  -9.689 -16.078  1.00 38.10           N  
ANISOU  888  N   ALA A 105     5104   4605   4769   -435   -245    202       N  
ATOM    889  CA  ALA A 105     -42.353 -10.800 -16.606  1.00 38.34           C  
ANISOU  889  CA  ALA A 105     5083   4686   4797   -520   -384    262       C  
ATOM    890  C   ALA A 105     -41.995 -11.173 -18.037  1.00 41.44           C  
ANISOU  890  C   ALA A 105     5629   4977   5141   -538   -468    248       C  
ATOM    891  O   ALA A 105     -42.417 -12.237 -18.502  1.00 44.11           O  
ANISOU  891  O   ALA A 105     5975   5320   5465   -630   -594    275       O  
ATOM    892  CB  ALA A 105     -43.844 -10.474 -16.564  1.00 36.29           C  
ANISOU  892  CB  ALA A 105     4661   4570   4559   -476   -438    341       C  
ATOM    893  N   GLY A 106     -41.277 -10.319 -18.745  1.00 39.92           N  
ANISOU  893  N   GLY A 106     5564   4693   4909   -460   -405    209       N  
ATOM    894  CA  GLY A 106     -40.816 -10.604 -20.091  1.00 39.05           C  
ANISOU  894  CA  GLY A 106     5613   4496   4728   -466   -457    191       C  
ATOM    895  C   GLY A 106     -41.685  -9.953 -21.153  1.00 47.27           C  
ANISOU  895  C   GLY A 106     6685   5549   5726   -398   -536    244       C  
ATOM    896  O   GLY A 106     -42.863  -9.645 -20.936  1.00 48.22           O  
ANISOU  896  O   GLY A 106     6676   5766   5881   -362   -595    306       O  
ATOM    897  N   THR A 107     -41.085  -9.719 -22.324  1.00 40.88           N  
ANISOU  897  N   THR A 107     6045   4654   4833   -372   -532    226       N  
ATOM    898  CA  THR A 107     -41.811  -9.270 -23.501  1.00 45.54           C  
ANISOU  898  CA  THR A 107     6703   5246   5356   -316   -629    280       C  
ATOM    899  C   THR A 107     -41.432 -10.171 -24.668  1.00 43.84           C  
ANISOU  899  C   THR A 107     6645   4978   5034   -371   -710    248       C  
ATOM    900  O   THR A 107     -40.252 -10.491 -24.861  1.00 41.66           O  
ANISOU  900  O   THR A 107     6480   4633   4714   -387   -621    183       O  
ATOM    901  CB  THR A 107     -41.522  -7.774 -23.842  1.00 54.87           C  
ANISOU  901  CB  THR A 107     7973   6364   6511   -206   -533    303       C  
ATOM    902  OG1 THR A 107     -42.369  -7.350 -24.917  1.00 52.33           O  
ANISOU  902  OG1 THR A 107     7706   6054   6122   -138   -648    373       O  
ATOM    903  CG2 THR A 107     -40.057  -7.534 -24.238  1.00 44.43           C  
ANISOU  903  CG2 THR A 107     6809   4943   5130   -230   -404    253       C  
ATOM    904  N  ATHR A 108     -42.436 -10.589 -25.434  0.54 42.68           N  
ANISOU  904  N  ATHR A 108     6502   4874   4839   -395   -881    290       N  
ATOM    905  N  BTHR A 108     -42.438 -10.598 -25.432  0.46 42.72           N  
ANISOU  905  N  BTHR A 108     6508   4880   4845   -395   -882    290       N  
ATOM    906  CA ATHR A 108     -42.221 -11.498 -26.552  0.54 45.37           C  
ANISOU  906  CA ATHR A 108     7014   5162   5062   -448   -982    250       C  
ATOM    907  CA BTHR A 108     -42.207 -11.500 -26.553  0.46 45.36           C  
ANISOU  907  CA BTHR A 108     7014   5159   5060   -448   -981    249       C  
ATOM    908  C  ATHR A 108     -42.017 -10.708 -27.840  0.54 48.60           C  
ANISOU  908  C  ATHR A 108     7593   5532   5342   -367   -977    271       C  
ATOM    909  C  BTHR A 108     -41.995 -10.690 -27.825  0.46 48.58           C  
ANISOU  909  C  BTHR A 108     7590   5528   5340   -366   -972    270       C  
ATOM    910  O  ATHR A 108     -42.797  -9.800 -28.150  0.54 47.56           O  
ANISOU  910  O  ATHR A 108     7422   5443   5204   -297  -1028    351       O  
ATOM    911  O  BTHR A 108     -42.749  -9.752 -28.109  0.46 47.50           O  
ANISOU  911  O  BTHR A 108     7414   5433   5200   -294  -1017    350       O  
ATOM    912  CB ATHR A 108     -43.403 -12.457 -26.696  0.54 45.06           C  
ANISOU  912  CB ATHR A 108     6907   5186   5027   -553  -1194    283       C  
ATOM    913  CB BTHR A 108     -43.375 -12.469 -26.744  0.46 45.07           C  
ANISOU  913  CB BTHR A 108     6918   5184   5023   -553  -1194    280       C  
ATOM    914  OG1ATHR A 108     -43.507 -13.267 -25.517  0.54 45.95           O  
ANISOU  914  OG1ATHR A 108     6888   5325   5247   -649  -1191    273       O  
ATOM    915  OG1BTHR A 108     -44.581 -11.735 -26.987  0.46 47.86           O  
ANISOU  915  OG1BTHR A 108     7150   5644   5389   -508  -1296    376       O  
ATOM    916  CG2ATHR A 108     -43.223 -13.353 -27.909  0.54 45.38           C  
ANISOU  916  CG2ATHR A 108     7164   5151   4926   -607  -1316    228       C  
ATOM    917  CG2BTHR A 108     -43.561 -13.324 -25.500  0.46 45.88           C  
ANISOU  917  CG2BTHR A 108     6872   5318   5240   -656  -1200    275       C  
ATOM    918  N   VAL A 109     -40.963 -11.051 -28.582  1.00 43.87           N  
ANISOU  918  N   VAL A 109     7180   4857   4630   -365   -910    204       N  
ATOM    919  CA  VAL A 109     -40.658 -10.443 -29.873  1.00 47.36           C  
ANISOU  919  CA  VAL A 109     7809   5267   4918   -305   -893    223       C  
ATOM    920  C   VAL A 109     -40.652 -11.551 -30.905  1.00 51.34           C  
ANISOU  920  C   VAL A 109     8486   5744   5275   -346  -1013    162       C  
ATOM    921  O   VAL A 109     -39.987 -12.572 -30.710  1.00 43.79           O  
ANISOU  921  O   VAL A 109     7581   4745   4313   -380   -982     70       O  
ATOM    922  CB  VAL A 109     -39.298  -9.721 -29.871  1.00 53.66           C  
ANISOU  922  CB  VAL A 109     8679   6020   5690   -263   -672    203       C  
ATOM    923  CG1 VAL A 109     -38.970  -9.187 -31.271  1.00 49.60           C  
ANISOU  923  CG1 VAL A 109     8372   5482   4993   -219   -649    234       C  
ATOM    924  CG2 VAL A 109     -39.284  -8.600 -28.857  1.00 47.04           C  
ANISOU  924  CG2 VAL A 109     7707   5182   4984   -236   -566    252       C  
ATOM    925  N   THR A 110     -41.392 -11.363 -31.991  1.00 58.85           N  
ANISOU  925  N   THR A 110     9966   5050   7343      1  -1582    102       N  
ATOM    926  CA  THR A 110     -41.376 -12.300 -33.109  1.00 60.31           C  
ANISOU  926  CA  THR A 110    10343   5082   7491    -42  -1463      2       C  
ATOM    927  C   THR A 110     -40.700 -11.622 -34.290  1.00 59.64           C  
ANISOU  927  C   THR A 110    10012   5117   7532    113  -1340    -80       C  
ATOM    928  O   THR A 110     -41.135 -10.547 -34.718  1.00 58.01           O  
ANISOU  928  O   THR A 110     9566   5180   7294     49  -1287    -54       O  
ATOM    929  CB  THR A 110     -42.785 -12.757 -33.490  1.00 60.63           C  
ANISOU  929  CB  THR A 110    10539   5235   7261   -388  -1399    -28       C  
ATOM    930  OG1 THR A 110     -43.394 -13.422 -32.376  1.00 61.64           O  
ANISOU  930  OG1 THR A 110    10896   5272   7254   -570  -1511     69       O  
ATOM    931  CG2 THR A 110     -42.726 -13.728 -34.655  1.00 62.47           C  
ANISOU  931  CG2 THR A 110    10959   5312   7463   -436  -1274   -177       C  
ATOM    932  N   VAL A 111     -39.628 -12.233 -34.788  1.00 61.20           N  
ANISOU  932  N   VAL A 111    10261   5129   7865    327  -1304   -168       N  
ATOM    933  CA  VAL A 111     -39.016 -11.798 -36.040  1.00 62.23           C  
ANISOU  933  CA  VAL A 111    10171   5410   8063    438  -1172   -258       C  
ATOM    934  C   VAL A 111     -39.781 -12.447 -37.187  1.00 62.13           C  
ANISOU  934  C   VAL A 111    10283   5458   7867    254  -1038   -384       C  
ATOM    935  O   VAL A 111     -39.926 -13.672 -37.241  1.00 64.16           O  
ANISOU  935  O   VAL A 111    10837   5469   8070    210  -1039   -491       O  
ATOM    936  CB  VAL A 111     -37.525 -12.157 -36.098  1.00 63.38           C  
ANISOU  936  CB  VAL A 111    10270   5413   8399    760  -1189   -332       C  
ATOM    937  CG1 VAL A 111     -36.949 -11.732 -37.435  1.00 63.02           C  
ANISOU  937  CG1 VAL A 111     9974   5592   8379    836  -1044   -425       C  
ATOM    938  CG2 VAL A 111     -36.773 -11.475 -34.979  1.00 61.98           C  
ANISOU  938  CG2 VAL A 111     9932   5238   8379    922  -1316   -227       C  
ATOM    939  N   CYS A 112     -40.272 -11.620 -38.100  1.00 60.99           N  
ANISOU  939  N   CYS A 112     9911   5636   7626    143   -927   -371       N  
ATOM    940  CA  CYS A 112     -41.193 -12.061 -39.129  1.00 61.71           C  
ANISOU  940  CA  CYS A 112    10065   5890   7492    -70   -803   -480       C  
ATOM    941  C   CYS A 112     -40.445 -12.905 -40.152  1.00 63.97           C  
ANISOU  941  C   CYS A 112    10394   6107   7803     55   -703   -685       C  
ATOM    942  O   CYS A 112     -39.235 -12.760 -40.335  1.00 64.53           O  
ANISOU  942  O   CYS A 112    10326   6146   8044    313   -700   -713       O  
ATOM    943  CB  CYS A 112     -41.822 -10.849 -39.812  1.00 60.12           C  
ANISOU  943  CB  CYS A 112     9574   6089   7180   -167   -722   -378       C  
ATOM    944  SG  CYS A 112     -43.016  -9.923 -38.780  1.00 71.02           S  
ANISOU  944  SG  CYS A 112    10908   7611   8467   -325   -829   -205       S  
ATOM    945  N   SER A 113     -41.176 -13.795 -40.821  1.00 66.77           N  
ANISOU  945  N   SER A 113    10926   6468   7975   -136   -622   -856       N  
ATOM    946  CA  SER A 113     -40.561 -14.694 -41.808  1.00 76.42           C  
ANISOU  946  CA  SER A 113    12206   7625   9206    -22   -529  -1112       C  
ATOM    947  C   SER A 113     -40.492 -14.046 -43.188  1.00 82.88           C  
ANISOU  947  C   SER A 113    12683   8905   9903    -22   -372  -1166       C  
ATOM    948  O   SER A 113     -39.425 -13.597 -43.616  1.00 95.53           O  
ANISOU  948  O   SER A 113    14046  10631  11621    209   -339  -1161       O  
ATOM    949  CB  SER A 113     -41.310 -16.028 -41.859  1.00 75.79           C  
ANISOU  949  CB  SER A 113    12498   7292   9008   -237   -520  -1306       C  
ATOM    950  OG  SER A 113     -41.050 -16.797 -40.697  1.00 85.24           O  
ANISOU  950  OG  SER A 113    14030   8006  10353   -171   -665  -1254       O  
ATOM    951  N   GLY A 114     -41.619 -13.999 -43.897  1.00 82.63           N  
ANISOU  951  N   GLY A 114    12610   9171   9614   -288   -275  -1212       N  
ATOM    952  CA  GLY A 114     -41.582 -13.601 -45.293  1.00 89.82           C  
ANISOU  952  CA  GLY A 114    13222  10540  10368   -292   -121  -1284       C  
ATOM    953  C   GLY A 114     -42.540 -12.505 -45.716  1.00 81.05           C  
ANISOU  953  C   GLY A 114    11863   9880   9054   -462    -62  -1082       C  
ATOM    954  O   GLY A 114     -43.760 -12.704 -45.720  1.00 86.66           O  
ANISOU  954  O   GLY A 114    12663  10722   9543   -714    -46  -1112       O  
ATOM    955  N   SER A 115     -41.993 -11.351 -46.103  1.00 84.89           N  
ANISOU  955  N   SER A 115    12033  10618   9604   -326    -31   -876       N  
ATOM    956  CA  SER A 115     -42.801 -10.257 -46.629  1.00 80.17           C  
ANISOU  956  CA  SER A 115    11191  10442   8829   -433     24   -659       C  
ATOM    957  C   SER A 115     -41.937  -9.226 -47.344  1.00 85.70           C  
ANISOU  957  C   SER A 115    11560  11393   9609   -282     87   -466       C  
ATOM    958  O   SER A 115     -41.604  -8.184 -46.768  1.00 95.15           O  
ANISOU  958  O   SER A 115    12663  12492  10998   -197     12   -214       O  
ATOM    959  CB  SER A 115     -43.588  -9.595 -45.501  1.00 76.81           C  
ANISOU  959  CB  SER A 115    10849   9890   8447   -503   -102   -458       C  
ATOM    960  OG  SER A 115     -44.817 -10.268 -45.292  1.00 78.20           O  
ANISOU  960  OG  SER A 115    11208  10112   8391   -737   -108   -583       O  
ATOM    961  N   ASP A 116     -41.581  -9.495 -48.599  1.00 79.91           N  
ANISOU  961  N   ASP A 116    10642  11000   8722   -268    225   -587       N  
ATOM    962  CA  ASP A 116     -40.703  -8.591 -49.328  1.00 90.15           C  
ANISOU  962  CA  ASP A 116    11614  12573  10066   -158    293   -394       C  
ATOM    963  C   ASP A 116     -41.425  -7.282 -49.626  1.00 85.39           C  
ANISOU  963  C   ASP A 116    10819  12257   9368   -235    308    -40       C  
ATOM    964  O   ASP A 116     -42.514  -7.262 -50.209  1.00 80.96           O  
ANISOU  964  O   ASP A 116    10212  12023   8527   -365    368    -28       O  
ATOM    965  CB  ASP A 116     -40.195  -9.243 -50.615  1.00 82.27           C  
ANISOU  965  CB  ASP A 116    10440  11939   8882   -130    439   -628       C  
ATOM    966  CG  ASP A 116     -39.345  -8.298 -51.461  1.00 89.71           C  
ANISOU  966  CG  ASP A 116    11010  13259   9815    -61    523   -400       C  
ATOM    967  OD1 ASP A 116     -39.914  -7.443 -52.175  1.00 88.97           O  
ANISOU  967  OD1 ASP A 116    10708  13557   9541   -160    591   -141       O  
ATOM    968  OD2 ASP A 116     -38.100  -8.403 -51.406  1.00 89.67           O  
ANISOU  968  OD2 ASP A 116    10917  13177   9975     91    518   -466       O  
ATOM    969  N   TYR A 117     -40.787  -6.191 -49.215  1.00 83.49           N  
ANISOU  969  N   TYR A 117    10468  11888   9367   -147    249    242       N  
ATOM    970  CA  TYR A 117     -41.370  -4.858 -49.282  1.00 83.15           C  
ANISOU  970  CA  TYR A 117    10297  11975   9323   -180    228    601       C  
ATOM    971  C   TYR A 117     -41.607  -4.434 -50.729  1.00 85.14           C  
ANISOU  971  C   TYR A 117    10272  12778   9299   -234    371    762       C  
ATOM    972  O   TYR A 117     -42.713  -4.014 -51.092  1.00 76.75           O  
ANISOU  972  O   TYR A 117     9163  11974   8023   -294    387    903       O  
ATOM    973  CB  TYR A 117     -40.413  -3.928 -48.531  1.00 92.17           C  
ANISOU  973  CB  TYR A 117    11400  12801  10821    -87    136    805       C  
ATOM    974  CG  TYR A 117     -40.467  -2.443 -48.762  1.00 97.45           C  
ANISOU  974  CG  TYR A 117    11900  13542  11584    -94    127   1196       C  
ATOM    975  CD1 TYR A 117     -41.418  -1.653 -48.136  1.00 89.72           C  
ANISOU  975  CD1 TYR A 117    11011  12418  10659    -87     25   1360       C  
ATOM    976  CD2 TYR A 117     -39.518  -1.823 -49.564  1.00 96.17           C  
ANISOU  976  CD2 TYR A 117    11495  13576  11470   -103    211   1399       C  
ATOM    977  CE1 TYR A 117     -41.437  -0.280 -48.322  1.00 98.29           C  
ANISOU  977  CE1 TYR A 117    11977  13497  11872    -69      2   1715       C  
ATOM    978  CE2 TYR A 117     -39.531  -0.460 -49.769  1.00 99.29           C  
ANISOU  978  CE2 TYR A 117    11769  13979  11979   -130    197   1785       C  
ATOM    979  CZ  TYR A 117     -40.487   0.306 -49.139  1.00103.23           C  
ANISOU  979  CZ  TYR A 117    12392  14268  12561   -100     88   1940       C  
ATOM    980  OH  TYR A 117     -40.506   1.672 -49.349  1.00107.01           O  
ANISOU  980  OH  TYR A 117    12783  14695  13182   -105     64   2324       O  
ATOM    981  N   GLU A 118     -40.583  -4.582 -51.579  1.00 84.79           N  
ANISOU  981  N   GLU A 118    10022  12969   9226   -205    475    733       N  
ATOM    982  CA  GLU A 118     -40.723  -4.261 -52.997  1.00 83.25           C  
ANISOU  982  CA  GLU A 118     9535  13363   8734   -263    619    880       C  
ATOM    983  C   GLU A 118     -41.727  -5.181 -53.681  1.00 81.60           C  
ANISOU  983  C   GLU A 118     9338  13510   8154   -352    703    615       C  
ATOM    984  O   GLU A 118     -42.457  -4.753 -54.584  1.00 82.84           O  
ANISOU  984  O   GLU A 118     9308  14147   8021   -415    782    787       O  
ATOM    985  CB  GLU A 118     -39.363  -4.351 -53.696  1.00 86.37           C  
ANISOU  985  CB  GLU A 118     9691  13975   9152   -222    711    850       C  
ATOM    986  CG  GLU A 118     -38.363  -3.291 -53.273  1.00 86.15           C  
ANISOU  986  CG  GLU A 118     9570  13731   9431   -193    657   1158       C  
ATOM    987  CD  GLU A 118     -38.695  -1.917 -53.832  1.00 98.90           C  
ANISOU  987  CD  GLU A 118    11010  15561  11005   -272    683   1652       C  
ATOM    988  OE1 GLU A 118     -39.414  -1.835 -54.854  1.00 86.02           O  
ANISOU  988  OE1 GLU A 118     9229  14406   9048   -326    777   1766       O  
ATOM    989  OE2 GLU A 118     -38.241  -0.915 -53.240  1.00103.68           O  
ANISOU  989  OE2 GLU A 118    11634  15854  11906   -277    603   1928       O  
ATOM    990  N   PHE A 119     -41.769  -6.454 -53.275  1.00 78.96           N  
ANISOU  990  N   PHE A 119     9225  12955   7820   -364    686    197       N  
ATOM    991  CA  PHE A 119     -42.737  -7.383 -53.851  1.00 77.36           C  
ANISOU  991  CA  PHE A 119     9063  13044   7286   -491    762    -98       C  
ATOM    992  C   PHE A 119     -44.154  -6.923 -53.534  1.00 75.20           C  
ANISOU  992  C   PHE A 119     8863  12848   6863   -595    712     61       C  
ATOM    993  O   PHE A 119     -45.006  -6.832 -54.425  1.00 73.17           O  
ANISOU  993  O   PHE A 119     8431  13115   6257   -687    800     88       O  
ATOM    994  CB  PHE A 119     -42.490  -8.796 -53.311  1.00 81.37           C  
ANISOU  994  CB  PHE A 119     9858  13168   7889   -493    729   -549       C  
ATOM    995  CG  PHE A 119     -43.496  -9.826 -53.766  1.00 88.00           C  
ANISOU  995  CG  PHE A 119    10796  14213   8427   -671    796   -891       C  
ATOM    996  CD1 PHE A 119     -43.938 -10.810 -52.892  1.00 89.27           C  
ANISOU  996  CD1 PHE A 119    11319  13929   8671   -762    717  -1156       C  
ATOM    997  CD2 PHE A 119     -43.923  -9.873 -55.089  1.00 86.59           C  
ANISOU  997  CD2 PHE A 119    10341  14681   7878   -761    940   -965       C  
ATOM    998  CE1 PHE A 119     -44.845 -11.777 -53.306  1.00 91.10           C  
ANISOU  998  CE1 PHE A 119    11652  14326   8634   -973    781  -1485       C  
ATOM    999  CE2 PHE A 119     -44.823 -10.844 -55.513  1.00 87.00           C  
ANISOU  999  CE2 PHE A 119    10470  14938   7648   -951   1006  -1323       C  
ATOM   1000  CZ  PHE A 119     -45.282 -11.799 -54.619  1.00 82.64           C  
ANISOU 1000  CZ  PHE A 119    10297  13905   7199  -1070    927  -1589       C  
ATOM   1001  N   LEU A 120     -44.409  -6.581 -52.265  1.00 79.11           N  
ANISOU 1001  N   LEU A 120     9582  12875   7601   -566    566    169       N  
ATOM   1002  CA  LEU A 120     -45.751  -6.178 -51.856  1.00 69.09           C  
ANISOU 1002  CA  LEU A 120     8376  11689   6186   -643    504    281       C  
ATOM   1003  C   LEU A 120     -46.159  -4.826 -52.435  1.00 68.79           C  
ANISOU 1003  C   LEU A 120     8088  12002   6047   -570    519    693       C  
ATOM   1004  O   LEU A 120     -47.335  -4.626 -52.754  1.00 76.59           O  
ANISOU 1004  O   LEU A 120     9002  13356   6742   -625    534    747       O  
ATOM   1005  CB  LEU A 120     -45.874  -6.177 -50.332  1.00 73.87           C  
ANISOU 1005  CB  LEU A 120     9261  11745   7063   -622    342    268       C  
ATOM   1006  CG  LEU A 120     -45.857  -7.586 -49.749  1.00 67.73           C  
ANISOU 1006  CG  LEU A 120     8767  10662   6305   -731    319   -110       C  
ATOM   1007  CD1 LEU A 120     -45.838  -7.566 -48.236  1.00 71.54           C  
ANISOU 1007  CD1 LEU A 120     9499  10633   7050   -701    157    -86       C  
ATOM   1008  CD2 LEU A 120     -47.085  -8.292 -50.257  1.00 75.41           C  
ANISOU 1008  CD2 LEU A 120     9758  11998   6897   -947    390   -320       C  
ATOM   1009  N   LYS A 121     -45.228  -3.874 -52.579  1.00 73.11           N  
ANISOU 1009  N   LYS A 121     8504  12452   6822   -448    512    999       N  
ATOM   1010  CA  LYS A 121     -45.599  -2.660 -53.311  1.00 79.76           C  
ANISOU 1010  CA  LYS A 121     9118  13642   7546   -388    539   1412       C  
ATOM   1011  C   LYS A 121     -46.028  -2.955 -54.738  1.00 74.65           C  
ANISOU 1011  C   LYS A 121     8215  13687   6462   -461    694   1393       C  
ATOM   1012  O   LYS A 121     -46.899  -2.265 -55.278  1.00 80.94           O  
ANISOU 1012  O   LYS A 121     8863  14869   7022   -430    708   1649       O  
ATOM   1013  CB  LYS A 121     -44.494  -1.608 -53.336  1.00 87.17           C  
ANISOU 1013  CB  LYS A 121     9956  14374   8790   -299    519   1759       C  
ATOM   1014  CG  LYS A 121     -44.514  -0.710 -52.138  1.00 97.77           C  
ANISOU 1014  CG  LYS A 121    11466  15190  10491   -207    358   1939       C  
ATOM   1015  CD  LYS A 121     -43.265   0.100 -52.010  1.00101.04           C  
ANISOU 1015  CD  LYS A 121    11819  15324  11248   -173    338   2180       C  
ATOM   1016  CE  LYS A 121     -43.368   0.956 -50.768  1.00102.90           C  
ANISOU 1016  CE  LYS A 121    12228  15034  11836    -89    172   2296       C  
ATOM   1017  NZ  LYS A 121     -42.311   1.990 -50.767  1.00107.09           N  
ANISOU 1017  NZ  LYS A 121    12676  15330  12682    -87    155   2593       N  
ATOM   1018  N   SER A 122     -45.428  -3.960 -55.374  1.00 83.86           N  
ANISOU 1018  N   SER A 122     9311  15046   7504   -537    807   1086       N  
ATOM   1019  CA  SER A 122     -45.845  -4.295 -56.728  1.00 76.62           C  
ANISOU 1019  CA  SER A 122     8128  14835   6147   -616    956   1015       C  
ATOM   1020  C   SER A 122     -47.270  -4.837 -56.766  1.00 84.09           C  
ANISOU 1020  C   SER A 122     9126  16063   6760   -729    964    799       C  
ATOM   1021  O   SER A 122     -47.903  -4.803 -57.826  1.00 86.12           O  
ANISOU 1021  O   SER A 122     9132  16974   6615   -780   1066    832       O  
ATOM   1022  CB  SER A 122     -44.869  -5.296 -57.348  1.00 82.06           C  
ANISOU 1022  CB  SER A 122     8732  15656   6790   -656   1067    665       C  
ATOM   1023  OG  SER A 122     -45.283  -6.628 -57.113  1.00 84.02           O  
ANISOU 1023  OG  SER A 122     9175  15804   6943   -763   1079    160       O  
ATOM   1024  N   TRP A 123     -47.787  -5.317 -55.636  1.00 78.15           N  
ANISOU 1024  N   TRP A 123     8671  14878   6143   -783    858    590       N  
ATOM   1025  CA  TRP A 123     -49.166  -5.776 -55.562  1.00 86.38           C  
ANISOU 1025  CA  TRP A 123     9761  16191   6869   -925    856    399       C  
ATOM   1026  C   TRP A 123     -50.134  -4.622 -55.794  1.00 88.98           C  
ANISOU 1026  C   TRP A 123     9909  16898   7001   -824    822    780       C  
ATOM   1027  O   TRP A 123     -49.848  -3.465 -55.474  1.00 84.96           O  
ANISOU 1027  O   TRP A 123     9383  16168   6731   -641    738   1176       O  
ATOM   1028  CB  TRP A 123     -49.439  -6.412 -54.199  1.00 73.73           C  
ANISOU 1028  CB  TRP A 123     8513  14025   5476  -1010    737    163       C  
ATOM   1029  CG  TRP A 123     -48.803  -7.753 -54.005  1.00 82.02           C  
ANISOU 1029  CG  TRP A 123     9774  14750   6638  -1127    769   -257       C  
ATOM   1030  CD1 TRP A 123     -47.624  -8.181 -54.532  1.00 78.30           C  
ANISOU 1030  CD1 TRP A 123     9254  14206   6290  -1061    841   -386       C  
ATOM   1031  CD2 TRP A 123     -49.280  -8.821 -53.172  1.00 77.66           C  
ANISOU 1031  CD2 TRP A 123     9533  13869   6106  -1311    715   -588       C  
ATOM   1032  NE1 TRP A 123     -47.352  -9.461 -54.115  1.00 82.32           N  
ANISOU 1032  NE1 TRP A 123    10031  14348   6900  -1159    833   -793       N  
ATOM   1033  CE2 TRP A 123     -48.351  -9.876 -53.275  1.00 86.60           C  
ANISOU 1033  CE2 TRP A 123    10812  14701   7389  -1328    756   -904       C  
ATOM   1034  CE3 TRP A 123     -50.410  -8.994 -52.364  1.00 83.85           C  
ANISOU 1034  CE3 TRP A 123    10475  14605   6777  -1468    636   -644       C  
ATOM   1035  CZ2 TRP A 123     -48.514 -11.088 -52.600  1.00 84.88           C  
ANISOU 1035  CZ2 TRP A 123    10930  14080   7242  -1494    716  -1244       C  
ATOM   1036  CZ3 TRP A 123     -50.570 -10.199 -51.692  1.00 75.54           C  
ANISOU 1036  CZ3 TRP A 123     9738  13194   5772  -1675    605   -974       C  
ATOM   1037  CH2 TRP A 123     -49.627 -11.229 -51.816  1.00 85.96           C  
ANISOU 1037  CH2 TRP A 123    11232  14160   7269  -1685    643  -1256       C  
ATOM   1038  N   THR A 124     -51.289  -4.949 -56.363  1.00 94.99           N  
ANISOU 1038  N   THR A 124    10534  18236   7321   -941    883    644       N  
ATOM   1039  CA  THR A 124     -52.375  -3.997 -56.516  1.00 92.25           C  
ANISOU 1039  CA  THR A 124    10024  18291   6737   -827    838    946       C  
ATOM   1040  C   THR A 124     -53.114  -3.821 -55.192  1.00 90.11           C  
ANISOU 1040  C   THR A 124     9981  17654   6604   -808    683    915       C  
ATOM   1041  O   THR A 124     -52.993  -4.635 -54.272  1.00 87.68           O  
ANISOU 1041  O   THR A 124     9938  16906   6470   -953    634    616       O  
ATOM   1042  CB  THR A 124     -53.342  -4.466 -57.600  1.00 94.44           C  
ANISOU 1042  CB  THR A 124    10046  19273   6565   -949    933    761       C  
ATOM   1043  OG1 THR A 124     -53.863  -5.753 -57.247  1.00 96.67           O  
ANISOU 1043  OG1 THR A 124    10491  19444   6793  -1214    939    257       O  
ATOM   1044  CG2 THR A 124     -52.624  -4.564 -58.938  1.00 89.96           C  
ANISOU 1044  CG2 THR A 124     9219  19039   5923   -941   1051    789       C  
ATOM   1045  N   VAL A 125     -53.890  -2.737 -55.102  1.00 93.73           N  
ANISOU 1045  N   VAL A 125    10353  17901   7359   -284   1041   2321       N  
ATOM   1046  CA  VAL A 125     -54.610  -2.452 -53.862  1.00 91.60           C  
ANISOU 1046  CA  VAL A 125     9915  17292   7596   -110    996   2445       C  
ATOM   1047  C   VAL A 125     -55.640  -3.541 -53.572  1.00 92.83           C  
ANISOU 1047  C   VAL A 125    10048  17629   7594   -349    686   2248       C  
ATOM   1048  O   VAL A 125     -55.781  -3.986 -52.429  1.00 88.08           O  
ANISOU 1048  O   VAL A 125     9479  16652   7335   -296    683   1986       O  
ATOM   1049  CB  VAL A 125     -55.235  -1.040 -53.907  1.00 96.82           C  
ANISOU 1049  CB  VAL A 125    10287  18007   8495    154   1052   3152       C  
ATOM   1050  CG1 VAL A 125     -56.601  -1.032 -54.584  1.00100.13           C  
ANISOU 1050  CG1 VAL A 125    10416  19040   8588     46    754   3631       C  
ATOM   1051  CG2 VAL A 125     -55.360  -0.481 -52.497  1.00 86.22           C  
ANISOU 1051  CG2 VAL A 125     8906  16083   7771    443   1207   3180       C  
ATOM   1052  N   GLU A 126     -56.333  -4.027 -54.606  1.00 97.63           N  
ANISOU 1052  N   GLU A 126    10619  18824   7650   -660    412   2358       N  
ATOM   1053  CA  GLU A 126     -57.350  -5.055 -54.402  1.00 94.04           C  
ANISOU 1053  CA  GLU A 126    10140  18582   7010   -977     82   2207       C  
ATOM   1054  C   GLU A 126     -56.722  -6.346 -53.897  1.00 91.12           C  
ANISOU 1054  C   GLU A 126    10166  17824   6633  -1144    118   1474       C  
ATOM   1055  O   GLU A 126     -57.262  -6.999 -52.997  1.00 91.81           O  
ANISOU 1055  O   GLU A 126    10243  17712   6931  -1228     -8   1297       O  
ATOM   1056  CB  GLU A 126     -58.113  -5.308 -55.703  1.00 92.84           C  
ANISOU 1056  CB  GLU A 126     9907  19171   6198  -1357   -239   2459       C  
ATOM   1057  CG  GLU A 126     -58.306  -4.065 -56.565  1.00107.48           C  
ANISOU 1057  CG  GLU A 126    11464  21445   7927  -1182   -205   3143       C  
ATOM   1058  CD  GLU A 126     -57.115  -3.800 -57.477  1.00114.86           C  
ANISOU 1058  CD  GLU A 126    12658  22395   8587  -1145     34   3003       C  
ATOM   1059  OE1 GLU A 126     -57.064  -4.371 -58.588  1.00119.36           O  
ANISOU 1059  OE1 GLU A 126    13417  23425   8510  -1487   -111   2857       O  
ATOM   1060  OE2 GLU A 126     -56.221  -3.024 -57.071  1.00115.00           O1-
ANISOU 1060  OE2 GLU A 126    12703  21972   9020   -794    372   3037       O1-
ATOM   1061  N   ASP A 127     -55.576  -6.727 -54.466  1.00 85.54           N  
ANISOU 1061  N   ASP A 127     9804  17011   5688  -1169    314   1076       N  
ATOM   1062  CA  ASP A 127     -54.865  -7.913 -53.999  1.00 90.16           C  
ANISOU 1062  CA  ASP A 127    10777  17187   6295  -1238    416    414       C  
ATOM   1063  C   ASP A 127     -54.452  -7.761 -52.541  1.00 87.31           C  
ANISOU 1063  C   ASP A 127    10345  16242   6586   -933    594    296       C  
ATOM   1064  O   ASP A 127     -54.659  -8.667 -51.725  1.00 73.79           O  
ANISOU 1064  O   ASP A 127     8760  14248   5026  -1020    517    -29       O  
ATOM   1065  CB  ASP A 127     -53.646  -8.166 -54.887  1.00 87.53           C  
ANISOU 1065  CB  ASP A 127    10767  16870   5618  -1209    671    104       C  
ATOM   1066  CG  ASP A 127     -53.870  -9.297 -55.873  1.00107.51           C  
ANISOU 1066  CG  ASP A 127    13686  19685   7478  -1606    516   -260       C  
ATOM   1067  OD1 ASP A 127     -55.040  -9.528 -56.250  1.00106.18           O  
ANISOU 1067  OD1 ASP A 127    13441  19905   6998  -1968    155    -89       O  
ATOM   1068  OD2 ASP A 127     -52.876  -9.933 -56.293  1.00103.85           O1-
ANISOU 1068  OD2 ASP A 127    13607  19074   6778  -1563    763   -698       O1-
ATOM   1069  N   LEU A 128     -53.869  -6.612 -52.195  1.00 78.85           N  
ANISOU 1069  N   LEU A 128     9091  14983   5887   -605    827    568       N  
ATOM   1070  CA  LEU A 128     -53.490  -6.362 -50.809  1.00 80.94           C  
ANISOU 1070  CA  LEU A 128     9300  14725   6728   -354    980    477       C  
ATOM   1071  C   LEU A 128     -54.712  -6.389 -49.897  1.00 80.94           C  
ANISOU 1071  C   LEU A 128     9099  14675   6979   -363    782    652       C  
ATOM   1072  O   LEU A 128     -54.710  -7.068 -48.863  1.00 72.11           O  
ANISOU 1072  O   LEU A 128     8064  13228   6106   -357    771    356       O  
ATOM   1073  CB  LEU A 128     -52.756  -5.023 -50.704  1.00 74.40           C  
ANISOU 1073  CB  LEU A 128     8339  13733   6196    -82   1233    779       C  
ATOM   1074  CG  LEU A 128     -51.360  -4.970 -51.332  1.00 77.02           C  
ANISOU 1074  CG  LEU A 128     8821  14054   6389    -40   1482    610       C  
ATOM   1075  CD1 LEU A 128     -50.924  -3.533 -51.555  1.00 75.16           C  
ANISOU 1075  CD1 LEU A 128     8424  13795   6337    121   1661   1048       C  
ATOM   1076  CD2 LEU A 128     -50.349  -5.708 -50.468  1.00 74.18           C  
ANISOU 1076  CD2 LEU A 128     8624  13300   6263     36   1636    147       C  
ATOM   1077  N   GLN A 129     -55.777  -5.675 -50.281  1.00 87.02           N  
ANISOU 1077  N   GLN A 129     9581  15804   7677   -362    634   1170       N  
ATOM   1078  CA  GLN A 129     -56.983  -5.625 -49.455  1.00 85.33           C  
ANISOU 1078  CA  GLN A 129     9115  15611   7695   -324    480   1419       C  
ATOM   1079  C   GLN A 129     -57.620  -7.001 -49.316  1.00 84.68           C  
ANISOU 1079  C   GLN A 129     9123  15653   7397   -682    208   1116       C  
ATOM   1080  O   GLN A 129     -58.118  -7.356 -48.243  1.00 81.74           O  
ANISOU 1080  O   GLN A 129     8677  15072   7309   -652    162   1057       O  
ATOM   1081  CB  GLN A 129     -57.991  -4.638 -50.046  1.00 88.82           C  
ANISOU 1081  CB  GLN A 129     9197  16497   8055   -231    385   2095       C  
ATOM   1082  CG  GLN A 129     -57.528  -3.188 -50.089  1.00 91.55           C  
ANISOU 1082  CG  GLN A 129     9465  16652   8667    142    667   2468       C  
ATOM   1083  CD  GLN A 129     -57.943  -2.383 -48.879  1.00 93.08           C  
ANISOU 1083  CD  GLN A 129     9525  16462   9380    505    840   2703       C  
ATOM   1084  OE1 GLN A 129     -58.093  -2.915 -47.778  1.00 94.17           O  
ANISOU 1084  OE1 GLN A 129     9710  16314   9757    523    840   2427       O  
ATOM   1085  NE2 GLN A 129     -58.133  -1.081 -49.079  1.00 92.57           N  
ANISOU 1085  NE2 GLN A 129     9320  16373   9479    810   1012   3223       N  
ATOM   1086  N   LYS A 130     -57.622  -7.789 -50.394  1.00 86.71           N  
ANISOU 1086  N   LYS A 130     9571  16241   7134  -1045     31    923       N  
ATOM   1087  CA  LYS A 130     -58.219  -9.121 -50.333  1.00 85.69           C  
ANISOU 1087  CA  LYS A 130     9603  16190   6766  -1457   -236    616       C  
ATOM   1088  C   LYS A 130     -57.440 -10.034 -49.394  1.00 78.18           C  
ANISOU 1088  C   LYS A 130     8982  14655   6069  -1404    -84     54       C  
ATOM   1089  O   LYS A 130     -58.034 -10.747 -48.576  1.00 71.79           O  
ANISOU 1089  O   LYS A 130     8164  13702   5412  -1542   -220    -54       O  
ATOM   1090  CB  LYS A 130     -58.300  -9.720 -51.739  1.00 86.96           C  
ANISOU 1090  CB  LYS A 130     9991  16787   6264  -1877   -432    486       C  
ATOM   1091  CG  LYS A 130     -58.824 -11.144 -51.794  1.00 88.60           C  
ANISOU 1091  CG  LYS A 130    10483  17020   6162  -2381   -703    107       C  
ATOM   1092  CD  LYS A 130     -58.290 -11.860 -53.020  1.00 95.29           C  
ANISOU 1092  CD  LYS A 130    11807  18003   6395  -2697   -721   -292       C  
ATOM   1093  CE  LYS A 130     -57.264 -12.928 -52.663  1.00 95.90           C  
ANISOU 1093  CE  LYS A 130    12429  17480   6527  -2650   -483   -972       C  
ATOM   1094  NZ  LYS A 130     -57.229 -14.018 -53.690  1.00 93.48           N  
ANISOU 1094  NZ  LYS A 130    12666  17281   5572  -3112   -596  -1411       N  
ATOM   1095  N   ARG A 131     -56.109 -10.017 -49.492  1.00 69.72           N  
ANISOU 1095  N   ARG A 131     8170  13271   5049  -1197    203   -261       N  
ATOM   1096  CA  ARG A 131     -55.284 -10.805 -48.581  1.00 68.31           C  
ANISOU 1096  CA  ARG A 131     8253  12565   5137  -1081    374   -722       C  
ATOM   1097  C   ARG A 131     -55.476 -10.377 -47.129  1.00 71.29           C  
ANISOU 1097  C   ARG A 131     8398  12630   6061   -831    435   -584       C  
ATOM   1098  O   ARG A 131     -55.573 -11.229 -46.237  1.00 61.01           O  
ANISOU 1098  O   ARG A 131     7206  11042   4933   -885    396   -832       O  
ATOM   1099  CB  ARG A 131     -53.820 -10.699 -49.006  1.00 72.63           C  
ANISOU 1099  CB  ARG A 131     9017  12939   5640   -865    685   -966       C  
ATOM   1100  CG  ARG A 131     -52.819 -11.377 -48.092  1.00 69.27           C  
ANISOU 1100  CG  ARG A 131     8792  12020   5508   -673    897  -1356       C  
ATOM   1101  CD  ARG A 131     -52.983 -12.857 -47.908  1.00 69.18           C  
ANISOU 1101  CD  ARG A 131     9131  11793   5361   -882    812  -1774       C  
ATOM   1102  NE  ARG A 131     -51.856 -13.358 -47.131  1.00 69.89           N  
ANISOU 1102  NE  ARG A 131     9370  11448   5736   -610   1067  -2065       N  
ATOM   1103  CZ  ARG A 131     -51.861 -14.482 -46.430  1.00 72.90           C  
ANISOU 1103  CZ  ARG A 131     9982  11487   6229   -652   1054  -2358       C  
ATOM   1104  NH1 ARG A 131     -52.941 -15.242 -46.352  1.00 67.25           N  
ANISOU 1104  NH1 ARG A 131     9393  10775   5384   -992    792  -2424       N  
ATOM   1105  NH2 ARG A 131     -50.757 -14.846 -45.783  1.00 71.23           N  
ANISOU 1105  NH2 ARG A 131     9855  10938   6269   -358   1303  -2550       N  
ATOM   1106  N   LEU A 132     -55.555  -9.065 -46.877  1.00 71.49           N  
ANISOU 1106  N   LEU A 132     8132  12691   6342   -562    540   -186       N  
ATOM   1107  CA  LEU A 132     -55.720  -8.564 -45.511  1.00 70.78           C  
ANISOU 1107  CA  LEU A 132     7875  12289   6728   -313    634    -71       C  
ATOM   1108  C   LEU A 132     -57.031  -9.037 -44.898  1.00 67.15           C  
ANISOU 1108  C   LEU A 132     7243  11948   6322   -454    413     70       C  
ATOM   1109  O   LEU A 132     -57.048  -9.589 -43.792  1.00 74.35           O  
ANISOU 1109  O   LEU A 132     8206  12565   7479   -425    428   -122       O  
ATOM   1110  CB  LEU A 132     -55.658  -7.037 -45.496  1.00 63.02           C  
ANISOU 1110  CB  LEU A 132     6686  11306   5954    -23    801    339       C  
ATOM   1111  CG  LEU A 132     -55.900  -6.353 -44.149  1.00 73.64           C  
ANISOU 1111  CG  LEU A 132     7913  12325   7743    244    929    476       C  
ATOM   1112  CD1 LEU A 132     -54.676  -6.506 -43.264  1.00 62.26           C  
ANISOU 1112  CD1 LEU A 132     6675  10432   6549    342   1111    105       C  
ATOM   1113  CD2 LEU A 132     -56.261  -4.885 -44.349  1.00 73.92           C  
ANISOU 1113  CD2 LEU A 132     7764  12415   7906    494   1058    965       C  
ATOM   1114  N   LEU A 133     -58.146  -8.806 -45.596  1.00 67.92           N  
ANISOU 1114  N   LEU A 133     7098  12521   6189   -610    204    455       N  
ATOM   1115  CA  LEU A 133     -59.448  -9.192 -45.060  1.00 72.55           C  
ANISOU 1115  CA  LEU A 133     7437  13310   6818   -757    -11    678       C  
ATOM   1116  C   LEU A 133     -59.567 -10.700 -44.902  1.00 72.45           C  
ANISOU 1116  C   LEU A 133     7670  13213   6645  -1150   -205    274       C  
ATOM   1117  O   LEU A 133     -60.295 -11.175 -44.024  1.00 71.84           O  
ANISOU 1117  O   LEU A 133     7467  13095   6733  -1230   -305    326       O  
ATOM   1118  CB  LEU A 133     -60.566  -8.660 -45.955  1.00 74.49           C  
ANISOU 1118  CB  LEU A 133     7328  14169   6807   -870   -216   1224       C  
ATOM   1119  CG  LEU A 133     -61.297  -7.417 -45.440  1.00 82.85           C  
ANISOU 1119  CG  LEU A 133     7981  15326   8172   -466    -84   1801       C  
ATOM   1120  CD1 LEU A 133     -62.284  -7.782 -44.335  1.00 81.67           C  
ANISOU 1120  CD1 LEU A 133     7593  15190   8248   -452   -151   1946       C  
ATOM   1121  CD2 LEU A 133     -60.312  -6.360 -44.952  1.00 79.11           C  
ANISOU 1121  CD2 LEU A 133     7648  14370   8041    -18    284   1749       C  
ATOM   1122  N   ALA A 134     -58.861 -11.467 -45.736  1.00 64.89           N  
ANISOU 1122  N   ALA A 134     7087  12207   5362  -1386   -233   -124       N  
ATOM   1123  CA  ALA A 134     -58.859 -12.918 -45.602  1.00 65.80           C  
ANISOU 1123  CA  ALA A 134     7541  12127   5332  -1736   -365   -550       C  
ATOM   1124  C   ALA A 134     -58.108 -13.388 -44.364  1.00 68.12           C  
ANISOU 1124  C   ALA A 134     8013  11853   6015  -1503   -160   -870       C  
ATOM   1125  O   ALA A 134     -58.386 -14.483 -43.865  1.00 71.05           O  
ANISOU 1125  O   ALA A 134     8562  12031   6401  -1736   -271  -1091       O  
ATOM   1126  CB  ALA A 134     -58.250 -13.560 -46.851  1.00 68.84           C  
ANISOU 1126  CB  ALA A 134     8344  12567   5244  -1989   -384   -905       C  
ATOM   1127  N   LEU A 135     -57.171 -12.585 -43.851  1.00 64.62           N  
ANISOU 1127  N   LEU A 135     7524  11153   5876  -1079    120   -876       N  
ATOM   1128  CA  LEU A 135     -56.360 -13.031 -42.723  1.00 66.06           C  
ANISOU 1128  CA  LEU A 135     7863  10855   6383   -877    298  -1163       C  
ATOM   1129  C   LEU A 135     -57.166 -13.072 -41.433  1.00 65.68           C  
ANISOU 1129  C   LEU A 135     7598  10720   6637   -839    232   -992       C  
ATOM   1130  O   LEU A 135     -56.825 -13.831 -40.518  1.00 62.18           O  
ANISOU 1130  O   LEU A 135     7304   9942   6378   -812    280  -1225       O  
ATOM   1131  CB  LEU A 135     -55.147 -12.119 -42.545  1.00 64.89           C  
ANISOU 1131  CB  LEU A 135     7697  10519   6438   -509    579  -1182       C  
ATOM   1132  CG  LEU A 135     -53.970 -12.309 -43.506  1.00 65.42           C  
ANISOU 1132  CG  LEU A 135     8015  10558   6285   -471    735  -1435       C  
ATOM   1133  CD1 LEU A 135     -53.032 -11.120 -43.382  1.00 63.66           C  
ANISOU 1133  CD1 LEU A 135     7650  10272   6264   -172    964  -1296       C  
ATOM   1134  CD2 LEU A 135     -53.230 -13.624 -43.286  1.00 53.81           C  
ANISOU 1134  CD2 LEU A 135     6889   8766   4791   -494    816  -1865       C  
ATOM   1135  N   ASP A 136     -58.228 -12.270 -41.337  1.00 66.54           N  
ANISOU 1135  N   ASP A 136     7348  11138   6794   -806    144   -559       N  
ATOM   1136  CA  ASP A 136     -59.015 -12.238 -40.104  1.00 70.51           C  
ANISOU 1136  CA  ASP A 136     7627  11594   7571   -721    130   -365       C  
ATOM   1137  C   ASP A 136     -59.714 -13.563 -39.825  1.00 65.86           C  
ANISOU 1137  C   ASP A 136     7108  11021   6893  -1097    -95   -474       C  
ATOM   1138  O   ASP A 136     -59.540 -14.099 -38.716  1.00 61.70           O  
ANISOU 1138  O   ASP A 136     6662  10187   6595  -1034    -31   -622       O  
ATOM   1139  CB  ASP A 136     -60.014 -11.073 -40.149  1.00 66.46           C  
ANISOU 1139  CB  ASP A 136     6707  11431   7116   -546    134    165       C  
ATOM   1140  CG  ASP A 136     -59.336  -9.714 -40.218  1.00 81.18           C  
ANISOU 1140  CG  ASP A 136     8550  13165   9130   -158    392    283       C  
ATOM   1141  OD1 ASP A 136     -58.086  -9.656 -40.268  1.00 84.20           O  
ANISOU 1141  OD1 ASP A 136     9192  13246   9556    -69    541    -30       O  
ATOM   1142  OD2 ASP A 136     -60.065  -8.699 -40.237  1.00 87.44           O1-
ANISOU 1142  OD2 ASP A 136     9063  14163   9998     57    454    718       O1-
ATOM   1143  N   PRO A 137     -60.496 -14.150 -40.747  1.00 66.40           N  
ANISOU 1143  N   PRO A 137     7168  11432   6629  -1526   -368   -402       N  
ATOM   1144  CA  PRO A 137     -61.177 -15.411 -40.407  1.00 67.19           C  
ANISOU 1144  CA  PRO A 137     7363  11506   6662  -1943   -589   -496       C  
ATOM   1145  C   PRO A 137     -60.220 -16.519 -40.010  1.00 66.19           C  
ANISOU 1145  C   PRO A 137     7712  10837   6600  -1982   -491   -999       C  
ATOM   1146  O   PRO A 137     -60.558 -17.343 -39.155  1.00 59.19           O  
ANISOU 1146  O   PRO A 137     6878   9757   5854  -2126   -552  -1049       O  
ATOM   1147  CB  PRO A 137     -61.925 -15.762 -41.698  1.00 67.60           C  
ANISOU 1147  CB  PRO A 137     7410  12008   6266  -2443   -899   -396       C  
ATOM   1148  CG  PRO A 137     -62.164 -14.459 -42.349  1.00 71.35           C  
ANISOU 1148  CG  PRO A 137     7536  12901   6673  -2212   -866      1       C  
ATOM   1149  CD  PRO A 137     -60.919 -13.662 -42.074  1.00 65.31           C  
ANISOU 1149  CD  PRO A 137     6902  11763   6149  -1693   -516   -171       C  
ATOM   1150  N   MET A 138     -59.026 -16.557 -40.604  1.00 65.71           N  
ANISOU 1150  N   MET A 138     7984  10537   6446  -1832   -321  -1337       N  
ATOM   1151  CA  MET A 138     -58.080 -17.625 -40.297  1.00 65.83           C  
ANISOU 1151  CA  MET A 138     8444  10051   6518  -1808   -191  -1776       C  
ATOM   1152  C   MET A 138     -57.524 -17.487 -38.886  1.00 61.06           C  
ANISOU 1152  C   MET A 138     7744   9125   6331  -1434      4  -1776       C  
ATOM   1153  O   MET A 138     -57.427 -18.475 -38.149  1.00 58.10           O  
ANISOU 1153  O   MET A 138     7564   8428   6084  -1500      7  -1935       O  
ATOM   1154  CB  MET A 138     -56.948 -17.637 -41.324  1.00 63.88           C  
ANISOU 1154  CB  MET A 138     8521   9698   6053  -1689    -20  -2080       C  
ATOM   1155  CG  MET A 138     -57.407 -17.804 -42.758  1.00 78.14           C  
ANISOU 1155  CG  MET A 138    10485  11827   7379  -2070   -200  -2122       C  
ATOM   1156  SD  MET A 138     -56.288 -16.995 -43.921  1.00 91.36           S  
ANISOU 1156  SD  MET A 138    12246  13630   8834  -1792     31  -2215       S  
ATOM   1157  CE  MET A 138     -54.711 -17.525 -43.254  1.00 60.57           C  
ANISOU 1157  CE  MET A 138     8640   9162   5211  -1366    398  -2582       C  
ATOM   1158  N   MET A 139     -57.142 -16.266 -38.494  1.00 51.35           N  
ANISOU 1158  N   MET A 139     6244   7968   5300  -1062    167  -1594       N  
ATOM   1159  CA  MET A 139     -56.667 -16.047 -37.133  1.00 55.31           C  
ANISOU 1159  CA  MET A 139     6656   8215   6144   -758    325  -1583       C  
ATOM   1160  C   MET A 139     -57.742 -16.399 -36.115  1.00 57.04           C  
ANISOU 1160  C   MET A 139     6694   8475   6502   -881    203  -1382       C  
ATOM   1161  O   MET A 139     -57.446 -16.938 -35.040  1.00 51.56           O  
ANISOU 1161  O   MET A 139     6072   7513   6004   -794    266  -1470       O  
ATOM   1162  CB  MET A 139     -56.259 -14.592 -36.935  1.00 52.24           C  
ANISOU 1162  CB  MET A 139     6039   7910   5898   -424    493  -1406       C  
ATOM   1163  CG  MET A 139     -55.707 -14.338 -35.544  1.00 52.24           C  
ANISOU 1163  CG  MET A 139     5995   7660   6192   -165    642  -1428       C  
ATOM   1164  SD  MET A 139     -55.089 -12.668 -35.305  1.00 55.16           S  
ANISOU 1164  SD  MET A 139     6218   8034   6705    152    844  -1289       S  
ATOM   1165  CE  MET A 139     -56.568 -11.911 -34.634  1.00 58.97           C  
ANISOU 1165  CE  MET A 139     6422   8705   7279    218    821   -915       C  
ATOM   1166  N   GLU A 140     -58.993 -16.062 -36.420  1.00 53.01           N  
ANISOU 1166  N   GLU A 140     5910   8344   5887  -1067     37  -1064       N  
ATOM   1167  CA  GLU A 140     -60.065 -16.305 -35.464  1.00 59.53           C  
ANISOU 1167  CA  GLU A 140     6494   9283   6840  -1162    -54   -806       C  
ATOM   1168  C   GLU A 140     -60.272 -17.795 -35.247  1.00 66.25           C  
ANISOU 1168  C   GLU A 140     7592   9934   7647  -1530   -208   -985       C  
ATOM   1169  O   GLU A 140     -60.524 -18.232 -34.120  1.00 54.27           O  
ANISOU 1169  O   GLU A 140     6020   8282   6317  -1510   -187   -919       O  
ATOM   1170  CB  GLU A 140     -61.355 -15.635 -35.934  1.00 66.24           C  
ANISOU 1170  CB  GLU A 140     6944  10648   7576  -1269   -192   -366       C  
ATOM   1171  CG  GLU A 140     -62.556 -15.874 -35.011  1.00 73.74           C  
ANISOU 1171  CG  GLU A 140     7575  11805   8638  -1366   -273    -29       C  
ATOM   1172  CD  GLU A 140     -63.673 -16.651 -35.693  1.00 85.17           C  
ANISOU 1172  CD  GLU A 140     8894  13623   9845  -1911   -601    161       C  
ATOM   1173  OE1 GLU A 140     -63.570 -16.878 -36.922  1.00 87.88           O  
ANISOU 1173  OE1 GLU A 140     9399  14088   9904  -2201   -767     38       O  
ATOM   1174  OE2 GLU A 140     -64.652 -17.029 -35.006  1.00 84.59           O1-
ANISOU 1174  OE2 GLU A 140     8556  13745   9841  -2076   -697    444       O1-
ATOM   1175  N   GLN A 141     -60.141 -18.598 -36.306  1.00 65.27           N  
ANISOU 1175  N   GLN A 141     7783   9756   7260  -1871   -345  -1222       N  
ATOM   1176  CA  GLN A 141     -60.335 -20.032 -36.134  1.00 59.05           C  
ANISOU 1176  CA  GLN A 141     7313   8696   6426  -2245   -474  -1410       C  
ATOM   1177  C   GLN A 141     -59.197 -20.623 -35.305  1.00 63.70           C  
ANISOU 1177  C   GLN A 141     8203   8757   7245  -1957   -255  -1691       C  
ATOM   1178  O   GLN A 141     -59.421 -21.515 -34.482  1.00 65.17           O  
ANISOU 1178  O   GLN A 141     8493   8706   7564  -2085   -290  -1692       O  
ATOM   1179  CB  GLN A 141     -60.434 -20.724 -37.494  1.00 70.27           C  
ANISOU 1179  CB  GLN A 141     9089  10141   7470  -2688   -649  -1640       C  
ATOM   1180  CG  GLN A 141     -60.958 -22.164 -37.436  1.00 79.05           C  
ANISOU 1180  CG  GLN A 141    10542  11013   8481  -3214   -840  -1780       C  
ATOM   1181  CD  GLN A 141     -62.058 -22.368 -36.383  1.00 87.58           C  
ANISOU 1181  CD  GLN A 141    11265  12262   9750  -3408   -987  -1411       C  
ATOM   1182  OE1 GLN A 141     -62.035 -23.326 -35.618  1.00 86.02           O  
ANISOU 1182  OE1 GLN A 141    11283  11699   9703  -3525   -977  -1494       O  
ATOM   1183  NE2 GLN A 141     -63.063 -21.497 -36.400  1.00 85.51           N  
ANISOU 1183  NE2 GLN A 141    10453  12576   9461  -3449  -1118   -969       N  
ATOM   1184  N   GLU A 142     -57.972 -20.113 -35.486  1.00 65.50           N  
ANISOU 1184  N   GLU A 142     8534   8829   7525  -1567    -30  -1881       N  
ATOM   1185  CA  GLU A 142     -56.842 -20.581 -34.684  1.00 67.05           C  
ANISOU 1185  CA  GLU A 142     8928   8608   7939  -1258    177  -2075       C  
ATOM   1186  C   GLU A 142     -57.019 -20.221 -33.216  1.00 58.69           C  
ANISOU 1186  C   GLU A 142     7578   7562   7159  -1052    226  -1848       C  
ATOM   1187  O   GLU A 142     -56.734 -21.038 -32.332  1.00 59.15           O  
ANISOU 1187  O   GLU A 142     7770   7332   7373  -1008    270  -1896       O  
ATOM   1188  CB  GLU A 142     -55.530 -20.008 -35.229  1.00 54.95           C  
ANISOU 1188  CB  GLU A 142     7479   7012   6386   -912    393  -2256       C  
ATOM   1189  CG  GLU A 142     -55.228 -20.423 -36.656  1.00 67.14           C  
ANISOU 1189  CG  GLU A 142     9359   8526   7625  -1067    399  -2510       C  
ATOM   1190  CD  GLU A 142     -53.766 -20.237 -37.044  1.00 70.24           C  
ANISOU 1190  CD  GLU A 142     9891   8773   8025   -698    666  -2709       C  
ATOM   1191  OE1 GLU A 142     -52.882 -20.256 -36.155  1.00 67.59           O  
ANISOU 1191  OE1 GLU A 142     9494   8248   7939   -374    830  -2708       O  
ATOM   1192  OE2 GLU A 142     -53.506 -20.077 -38.253  1.00 68.00           O1-
ANISOU 1192  OE2 GLU A 142     9757   8606   7474   -745    707  -2841       O1-
ATOM   1193  N   ILE A 143     -57.496 -19.003 -32.938  1.00 59.26           N  
ANISOU 1193  N   ILE A 143     7278   7956   7281   -911    238  -1591       N  
ATOM   1194  CA  ILE A 143     -57.758 -18.585 -31.561  1.00 57.55           C  
ANISOU 1194  CA  ILE A 143     6820   7772   7274   -721    307  -1386       C  
ATOM   1195  C   ILE A 143     -58.893 -19.398 -30.942  1.00 58.96           C  
ANISOU 1195  C   ILE A 143     6914   8009   7480  -1002    159  -1196       C  
ATOM   1196  O   ILE A 143     -58.832 -19.770 -29.763  1.00 56.77           O  
ANISOU 1196  O   ILE A 143     6620   7592   7358   -913    214  -1139       O  
ATOM   1197  CB  ILE A 143     -58.047 -17.074 -31.517  1.00 45.75           C  
ANISOU 1197  CB  ILE A 143     5022   6560   5802   -491    395  -1172       C  
ATOM   1198  CG1 ILE A 143     -56.828 -16.293 -32.011  1.00 47.30           C  
ANISOU 1198  CG1 ILE A 143     5314   6662   5994   -246    546  -1347       C  
ATOM   1199  CG2 ILE A 143     -58.462 -16.634 -30.117  1.00 45.39           C  
ANISOU 1199  CG2 ILE A 143     4774   6554   5917   -306    490   -972       C  
ATOM   1200  CD1 ILE A 143     -57.043 -14.805 -32.107  1.00 46.50           C  
ANISOU 1200  CD1 ILE A 143     4999   6758   5910    -44    647  -1153       C  
ATOM   1201  N   GLU A 144     -59.945 -19.684 -31.717  1.00 59.86           N  
ANISOU 1201  N   GLU A 144     6955   8364   7424  -1375    -43  -1065       N  
ATOM   1202  CA  GLU A 144     -61.076 -20.442 -31.179  1.00 62.99           C  
ANISOU 1202  CA  GLU A 144     7227   8869   7836  -1708   -205   -834       C  
ATOM   1203  C   GLU A 144     -60.672 -21.856 -30.774  1.00 64.35           C  
ANISOU 1203  C   GLU A 144     7778   8599   8073  -1895   -233  -1041       C  
ATOM   1204  O   GLU A 144     -61.148 -22.371 -29.756  1.00 66.47           O  
ANISOU 1204  O   GLU A 144     7957   8828   8470  -1973   -251   -863       O  
ATOM   1205  CB  GLU A 144     -62.223 -20.477 -32.191  1.00 67.35           C  
ANISOU 1205  CB  GLU A 144     7612   9817   8160  -2136   -453   -636       C  
ATOM   1206  CG  GLU A 144     -63.462 -21.268 -31.750  1.00 74.78           C  
ANISOU 1206  CG  GLU A 144     8378  10944   9093  -2572   -657   -349       C  
ATOM   1207  CD  GLU A 144     -64.111 -20.754 -30.466  1.00 79.69           C  
ANISOU 1207  CD  GLU A 144     8574  11796   9909  -2322   -537     27       C  
ATOM   1208  OE1 GLU A 144     -64.039 -19.537 -30.186  1.00 78.34           O  
ANISOU 1208  OE1 GLU A 144     8146  11807   9810  -1879   -347    164       O  
ATOM   1209  OE2 GLU A 144     -64.721 -21.579 -29.751  1.00 73.89           O1-
ANISOU 1209  OE2 GLU A 144     7786  11049   9238  -2582   -622    191       O1-
ATOM   1210  N   GLU A 145     -59.801 -22.505 -31.559  1.00 65.81           N  
ANISOU 1210  N   GLU A 145     8399   8439   8167  -1946   -209  -1396       N  
ATOM   1211  CA  GLU A 145     -59.282 -23.808 -31.145  1.00 67.08           C  
ANISOU 1211  CA  GLU A 145     8964   8102   8420  -2019   -169  -1587       C  
ATOM   1212  C   GLU A 145     -58.622 -23.729 -29.778  1.00 65.22           C  
ANISOU 1212  C   GLU A 145     8628   7708   8444  -1619     12  -1510       C  
ATOM   1213  O   GLU A 145     -58.812 -24.615 -28.938  1.00 60.99           O  
ANISOU 1213  O   GLU A 145     8187   6955   8032  -1721     -6  -1420       O  
ATOM   1214  CB  GLU A 145     -58.288 -24.360 -32.170  1.00 63.81           C  
ANISOU 1214  CB  GLU A 145     9038   7331   7877  -1986    -77  -1982       C  
ATOM   1215  CG  GLU A 145     -58.717 -24.291 -33.619  1.00 70.04           C  
ANISOU 1215  CG  GLU A 145     9968   8301   8343  -2333   -227  -2113       C  
ATOM   1216  CD  GLU A 145     -59.677 -25.396 -33.997  1.00 85.61           C  
ANISOU 1216  CD  GLU A 145    12212  10170  10144  -2960   -469  -2136       C  
ATOM   1217  OE1 GLU A 145     -59.436 -26.552 -33.589  1.00 98.35           O  
ANISOU 1217  OE1 GLU A 145    14223  11292  11852  -3060   -421  -2276       O  
ATOM   1218  OE2 GLU A 145     -60.660 -25.119 -34.712  1.00 88.73           O1-
ANISOU 1218  OE2 GLU A 145    12432  10974  10305  -3369   -711  -1996       O1-
ATOM   1219  N   ILE A 146     -57.832 -22.680 -29.542  1.00 56.78           N  
ANISOU 1219  N   ILE A 146     7381   6751   7442  -1195    174  -1532       N  
ATOM   1220  CA  ILE A 146     -57.209 -22.499 -28.235  1.00 60.72           C  
ANISOU 1220  CA  ILE A 146     7768   7170   8134   -861    315  -1450       C  
ATOM   1221  C   ILE A 146     -58.269 -22.342 -27.157  1.00 63.68           C  
ANISOU 1221  C   ILE A 146     7846   7778   8573   -948    259  -1132       C  
ATOM   1222  O   ILE A 146     -58.184 -22.948 -26.083  1.00 58.03           O  
ANISOU 1222  O   ILE A 146     7154   6919   7974   -905    290  -1032       O  
ATOM   1223  CB  ILE A 146     -56.251 -21.298 -28.263  1.00 57.03           C  
ANISOU 1223  CB  ILE A 146     7167   6820   7683   -489    466  -1527       C  
ATOM   1224  CG1 ILE A 146     -55.217 -21.507 -29.374  1.00 57.08           C  
ANISOU 1224  CG1 ILE A 146     7436   6639   7613   -403    542  -1805       C  
ATOM   1225  CG2 ILE A 146     -55.643 -21.057 -26.890  1.00 53.10           C  
ANISOU 1225  CG2 ILE A 146     6553   6293   7328   -215    574  -1440       C  
ATOM   1226  CD1 ILE A 146     -54.288 -22.662 -29.116  1.00 66.04           C  
ANISOU 1226  CD1 ILE A 146     8866   7382   8843   -280    639  -1942       C  
ATOM   1227  N   ARG A 147     -59.281 -21.516 -27.426  1.00 59.90           N  
ANISOU 1227  N   ARG A 147     7068   7684   8009  -1042    195   -936       N  
ATOM   1228  CA  ARG A 147     -60.314 -21.264 -26.430  1.00 64.02           C  
ANISOU 1228  CA  ARG A 147     7269   8478   8577  -1061    193   -602       C  
ATOM   1229  C   ARG A 147     -61.101 -22.531 -26.107  1.00 65.87           C  
ANISOU 1229  C   ARG A 147     7556   8638   8832  -1451     44   -448       C  
ATOM   1230  O   ARG A 147     -61.423 -22.786 -24.942  1.00 63.29           O  
ANISOU 1230  O   ARG A 147     7106   8345   8595  -1411     92   -243       O  
ATOM   1231  CB  ARG A 147     -61.230 -20.142 -26.917  1.00 57.02           C  
ANISOU 1231  CB  ARG A 147     6042   8023   7598  -1037    185   -384       C  
ATOM   1232  CG  ARG A 147     -60.493 -18.820 -27.108  1.00 65.71           C  
ANISOU 1232  CG  ARG A 147     7114   9154   8700   -652    357   -500       C  
ATOM   1233  CD  ARG A 147     -61.443 -17.628 -27.088  1.00 74.19           C  
ANISOU 1233  CD  ARG A 147     7838  10610   9742   -494    438   -200       C  
ATOM   1234  NE  ARG A 147     -62.417 -17.702 -28.172  1.00 81.12           N  
ANISOU 1234  NE  ARG A 147     8530  11793  10496   -776    260     -6       N  
ATOM   1235  CZ  ARG A 147     -62.423 -16.902 -29.231  1.00 73.97           C  
ANISOU 1235  CZ  ARG A 147     7559  11051   9496   -718    250     11       C  
ATOM   1236  NH1 ARG A 147     -61.580 -15.887 -29.338  1.00 68.48           N  
ANISOU 1236  NH1 ARG A 147     6956  10228   8837   -380    429   -134       N  
ATOM   1237  NH2 ARG A 147     -63.306 -17.120 -30.203  1.00 76.31           N  
ANISOU 1237  NH2 ARG A 147     7685  11665   9643  -1038     42    203       N  
ATOM   1238  N   GLN A 148     -61.403 -23.349 -27.121  1.00 69.38           N  
ANISOU 1238  N   GLN A 148     8215   8971   9176  -1859   -137   -549       N  
ATOM   1239  CA  GLN A 148     -62.091 -24.611 -26.863  1.00 72.73           C  
ANISOU 1239  CA  GLN A 148     8762   9254   9618  -2301   -290   -426       C  
ATOM   1240  C   GLN A 148     -61.193 -25.579 -26.103  1.00 74.12           C  
ANISOU 1240  C   GLN A 148     9285   8927   9950  -2170   -184   -563       C  
ATOM   1241  O   GLN A 148     -61.641 -26.238 -25.156  1.00 61.19           O  
ANISOU 1241  O   GLN A 148     7601   7236   8412  -2301   -204   -336       O  
ATOM   1242  CB  GLN A 148     -62.566 -25.232 -28.177  1.00 63.62           C  
ANISOU 1242  CB  GLN A 148     7834   8065   8275  -2818   -516   -549       C  
ATOM   1243  CG  GLN A 148     -63.943 -25.870 -28.110  1.00 78.52           C  
ANISOU 1243  CG  GLN A 148     9546  10189  10098  -3395   -756   -230       C  
ATOM   1244  CD  GLN A 148     -65.004 -24.943 -27.535  1.00 90.34           C  
ANISOU 1244  CD  GLN A 148    10404  12308  11613  -3304   -755    234       C  
ATOM   1245  OE1 GLN A 148     -65.554 -25.192 -26.456  1.00 86.83           O  
ANISOU 1245  OE1 GLN A 148     9734  11973  11284  -3322   -718    537       O  
ATOM   1246  NE2 GLN A 148     -65.296 -23.865 -28.257  1.00 83.45           N  
ANISOU 1246  NE2 GLN A 148     9240  11848  10620  -3175   -768    315       N  
ATOM   1247  N   LYS A 149     -59.919 -25.660 -26.499  1.00 67.12           N  
ANISOU 1247  N   LYS A 149     8716   7698   9088  -1891    -57   -890       N  
ATOM   1248  CA  LYS A 149     -58.956 -26.512 -25.807  1.00 71.72           C  
ANISOU 1248  CA  LYS A 149     9590   7834   9828  -1678     72   -976       C  
ATOM   1249  C   LYS A 149     -58.876 -26.177 -24.322  1.00 71.67           C  
ANISOU 1249  C   LYS A 149     9295   7987   9948  -1403    167   -720       C  
ATOM   1250  O   LYS A 149     -58.764 -27.078 -23.481  1.00 70.45           O  
ANISOU 1250  O   LYS A 149     9266   7590   9913  -1417    190   -592       O  
ATOM   1251  CB  LYS A 149     -57.585 -26.373 -26.473  1.00 68.44           C  
ANISOU 1251  CB  LYS A 149     9427   7171   9406  -1335    226  -1301       C  
ATOM   1252  CG  LYS A 149     -56.379 -26.597 -25.566  1.00 76.94           C  
ANISOU 1252  CG  LYS A 149    10557   8026  10651   -903    406  -1296       C  
ATOM   1253  CD  LYS A 149     -55.081 -26.591 -26.377  1.00 69.46           C  
ANISOU 1253  CD  LYS A 149     9844   6858   9688   -600    563  -1579       C  
ATOM   1254  CE  LYS A 149     -53.888 -26.177 -25.522  1.00 72.01           C  
ANISOU 1254  CE  LYS A 149     9985   7242  10132   -139    712  -1507       C  
ATOM   1255  NZ  LYS A 149     -53.070 -27.340 -25.076  1.00 89.51           N  
ANISOU 1255  NZ  LYS A 149    12461   9048  12499     73    838  -1469       N  
ATOM   1256  N   TYR A 150     -58.948 -24.892 -23.975  1.00 66.04           N  
ANISOU 1256  N   TYR A 150     8229   7668   9195  -1158    232   -639       N  
ATOM   1257  CA  TYR A 150     -58.844 -24.502 -22.576  1.00 67.82           C  
ANISOU 1257  CA  TYR A 150     8236   8055   9479   -906    335   -441       C  
ATOM   1258  C   TYR A 150     -60.184 -24.527 -21.845  1.00 64.42           C  
ANISOU 1258  C   TYR A 150     7523   7926   9027  -1114    286    -93       C  
ATOM   1259  O   TYR A 150     -60.194 -24.657 -20.617  1.00 62.74           O  
ANISOU 1259  O   TYR A 150     7215   7771   8851   -994    360     96       O  
ATOM   1260  CB  TYR A 150     -58.192 -23.116 -22.458  1.00 64.73           C  
ANISOU 1260  CB  TYR A 150     7682   7876   9036   -546    461   -547       C  
ATOM   1261  CG  TYR A 150     -56.675 -23.190 -22.474  1.00 54.76           C  
ANISOU 1261  CG  TYR A 150     6608   6372   7828   -273    545   -763       C  
ATOM   1262  CD1 TYR A 150     -55.955 -23.451 -21.312  1.00 58.59           C  
ANISOU 1262  CD1 TYR A 150     7091   6802   8371    -76    608   -674       C  
ATOM   1263  CD2 TYR A 150     -55.965 -23.009 -23.654  1.00 63.97           C  
ANISOU 1263  CD2 TYR A 150     7924   7413   8968   -214    563  -1016       C  
ATOM   1264  CE1 TYR A 150     -54.572 -23.537 -21.326  1.00 66.05           C  
ANISOU 1264  CE1 TYR A 150     8138   7595   9363    170    673   -804       C  
ATOM   1265  CE2 TYR A 150     -54.586 -23.085 -23.678  1.00 58.78           C  
ANISOU 1265  CE2 TYR A 150     7381   6591   8363     48    657  -1159       C  
ATOM   1266  CZ  TYR A 150     -53.891 -23.351 -22.515  1.00 67.15           C  
ANISOU 1266  CZ  TYR A 150     8397   7621   9497    240    707  -1039       C  
ATOM   1267  OH  TYR A 150     -52.513 -23.431 -22.541  1.00 56.38           O  
ANISOU 1267  OH  TYR A 150     7079   6160   8181    501    791  -1119       O  
ATOM   1268  N   GLN A 151     -61.313 -24.431 -22.557  1.00 67.54           N  
ANISOU 1268  N   GLN A 151     7760   8556   9347  -1427    162     29       N  
ATOM   1269  CA  GLN A 151     -62.604 -24.604 -21.891  1.00 74.43           C  
ANISOU 1269  CA  GLN A 151     8329   9744  10209  -1651    116    418       C  
ATOM   1270  C   GLN A 151     -62.801 -26.040 -21.428  1.00 79.64           C  
ANISOU 1270  C   GLN A 151     9185  10118  10957  -1979     20    546       C  
ATOM   1271  O   GLN A 151     -63.387 -26.279 -20.366  1.00 81.65           O  
ANISOU 1271  O   GLN A 151     9242  10541  11242  -2017     60    864       O  
ATOM   1272  CB  GLN A 151     -63.757 -24.196 -22.802  1.00 80.57           C  
ANISOU 1272  CB  GLN A 151     8834  10900  10880  -1931    -16    580       C  
ATOM   1273  CG  GLN A 151     -64.335 -22.834 -22.484  1.00 90.59           C  
ANISOU 1273  CG  GLN A 151     9685  12644  12092  -1613    137    792       C  
ATOM   1274  CD  GLN A 151     -65.321 -22.365 -23.531  1.00105.05           C  
ANISOU 1274  CD  GLN A 151    11231  14863  13821  -1824     10    971       C  
ATOM   1275  OE1 GLN A 151     -66.071 -23.167 -24.095  1.00103.10           O  
ANISOU 1275  OE1 GLN A 151    10942  14706  13525  -2326   -222   1114       O  
ATOM   1276  NE2 GLN A 151     -65.331 -21.063 -23.796  1.00107.48           N  
ANISOU 1276  NE2 GLN A 151    11347  15406  14084  -1465    154    985       N  
ATOM   1277  N   SER A 152     -62.338 -27.008 -22.217  1.00 72.97           N  
ANISOU 1277  N   SER A 152     8756   8825  10145  -2217    -84    312       N  
ATOM   1278  CA  SER A 152     -62.421 -28.397 -21.790  1.00 75.97           C  
ANISOU 1278  CA  SER A 152     9412   8823  10629  -2506   -146    416       C  
ATOM   1279  C   SER A 152     -61.463 -28.699 -20.644  1.00 76.75           C  
ANISOU 1279  C   SER A 152     9622   8684  10857  -2119     21    450       C  
ATOM   1280  O   SER A 152     -61.684 -29.665 -19.908  1.00 80.04           O  
ANISOU 1280  O   SER A 152    10139   8903  11368  -2284      7    675       O  
ATOM   1281  CB  SER A 152     -62.155 -29.331 -22.974  1.00 75.61           C  
ANISOU 1281  CB  SER A 152     9869   8298  10564  -2838   -260    121       C  
ATOM   1282  OG  SER A 152     -60.777 -29.358 -23.304  1.00 79.56           O  
ANISOU 1282  OG  SER A 152    10702   8416  11111  -2441   -110   -222       O  
ATOM   1283  N   LYS A 153     -60.410 -27.895 -20.473  1.00 72.50           N  
ANISOU 1283  N   LYS A 153     9052   8183  10313  -1636    165    264       N  
ATOM   1284  CA  LYS A 153     -59.509 -28.074 -19.339  1.00 74.37           C  
ANISOU 1284  CA  LYS A 153     9320   8308  10630  -1285    294    342       C  
ATOM   1285  C   LYS A 153     -60.099 -27.509 -18.054  1.00 78.40           C  
ANISOU 1285  C   LYS A 153     9466   9252  11072  -1189    354    653       C  
ATOM   1286  O   LYS A 153     -59.769 -27.987 -16.962  1.00 71.39           O  
ANISOU 1286  O   LYS A 153     8592   8309  10224  -1068    411    844       O  
ATOM   1287  CB  LYS A 153     -58.155 -27.418 -19.624  1.00 74.94           C  
ANISOU 1287  CB  LYS A 153     9466   8314  10694   -866    400     57       C  
ATOM   1288  CG  LYS A 153     -57.226 -28.225 -20.525  1.00 73.67           C  
ANISOU 1288  CG  LYS A 153     9710   7659  10623   -814    426   -196       C  
ATOM   1289  CD  LYS A 153     -55.764 -27.882 -20.249  1.00 74.94           C  
ANISOU 1289  CD  LYS A 153     9871   7782  10821   -350    558   -301       C  
ATOM   1290  CE  LYS A 153     -54.888 -28.086 -21.479  1.00 70.98           C  
ANISOU 1290  CE  LYS A 153     9653   6975  10341   -224    628   -611       C  
ATOM   1291  NZ  LYS A 153     -54.589 -29.533 -21.708  1.00 76.18           N  
ANISOU 1291  NZ  LYS A 153    10738   7074  11131   -252    688   -622       N  
ATOM   1292  N   ARG A 154     -60.972 -26.504 -18.167  1.00 72.57           N  
ANISOU 1292  N   ARG A 154     8408   8950  10216  -1218    365    724       N  
ATOM   1293  CA  ARG A 154     -61.587 -25.886 -16.999  1.00 73.44           C  
ANISOU 1293  CA  ARG A 154     8198   9478  10229  -1083    478    999       C  
ATOM   1294  C   ARG A 154     -62.714 -26.741 -16.441  1.00 72.90           C  
ANISOU 1294  C   ARG A 154     7988   9522  10188  -1422    421   1393       C  
ATOM   1295  O   ARG A 154     -62.997 -26.676 -15.240  1.00 79.24           O  
ANISOU 1295  O   ARG A 154     8619  10560  10927  -1309    532   1656       O  
ATOM   1296  CB  ARG A 154     -62.142 -24.509 -17.368  1.00 62.27           C  
ANISOU 1296  CB  ARG A 154     6513   8453   8694   -939    559    962       C  
ATOM   1297  CG  ARG A 154     -61.085 -23.506 -17.759  1.00 74.81           C  
ANISOU 1297  CG  ARG A 154     8213   9972  10241   -612    637    619       C  
ATOM   1298  CD  ARG A 154     -61.692 -22.188 -18.192  1.00 65.80           C  
ANISOU 1298  CD  ARG A 154     6848   9151   9004   -476    731    613       C  
ATOM   1299  NE  ARG A 154     -60.687 -21.135 -18.217  1.00 70.11           N  
ANISOU 1299  NE  ARG A 154     7504   9641   9494   -157    842    334       N  
ATOM   1300  CZ  ARG A 154     -60.250 -20.569 -19.333  1.00 72.62           C  
ANISOU 1300  CZ  ARG A 154     7895   9872   9825   -116    812    102       C  
ATOM   1301  NH1 ARG A 154     -60.741 -20.906 -20.515  1.00 72.36           N  
ANISOU 1301  NH1 ARG A 154     7842   9823   9828   -351    678    101       N  
ATOM   1302  NH2 ARG A 154     -59.286 -19.656 -19.267  1.00 75.11           N  
ANISOU 1302  NH2 ARG A 154     8315  10129  10096    132    907   -124       N  
ATOM   1303  N   GLN A 155     -63.365 -27.534 -17.297  1.00 71.90           N  
ANISOU 1303  N   GLN A 155     7941   9248  10129  -1868    248   1443       N  
ATOM   1304  CA  GLN A 155     -64.559 -28.266 -16.880  1.00 79.27           C  
ANISOU 1304  CA  GLN A 155     8691  10349  11081  -2277    168   1853       C  
ATOM   1305  C   GLN A 155     -64.285 -29.247 -15.750  1.00 80.61           C  
ANISOU 1305  C   GLN A 155     9002  10293  11333  -2290    212   2076       C  
ATOM   1306  O   GLN A 155     -65.005 -29.192 -14.739  1.00 86.66           O  
ANISOU 1306  O   GLN A 155     9468  11420  12040  -2300    294   2450       O  
ATOM   1307  CB  GLN A 155     -65.197 -28.962 -18.090  1.00 83.08           C  
ANISOU 1307  CB  GLN A 155     9298  10676  11592  -2833    -66   1822       C  
ATOM   1308  CG  GLN A 155     -66.163 -28.097 -18.883  1.00 88.47           C  
ANISOU 1308  CG  GLN A 155     9607  11855  12155  -2972   -140   1905       C  
ATOM   1309  CD  GLN A 155     -67.311 -27.578 -18.038  1.00 84.16           C  
ANISOU 1309  CD  GLN A 155     8512  11921  11542  -2938    -41   2380       C  
ATOM   1310  OE1 GLN A 155     -67.642 -26.395 -18.085  1.00 93.67           O  
ANISOU 1310  OE1 GLN A 155     9386  13550  12655  -2624     90   2434       O  
ATOM   1311  NE2 GLN A 155     -67.920 -28.461 -17.260  1.00 90.91           N  
ANISOU 1311  NE2 GLN A 155     9282  12816  12445  -3240    -74   2746       N  
ATOM   1312  N   PRO A 156     -63.292 -30.152 -15.831  1.00 86.34           N  
ANISOU 1312  N   PRO A 156    10157  10458  12189  -2261    186   1907       N  
ATOM   1313  CA  PRO A 156     -63.060 -31.056 -14.689  1.00 88.36           C  
ANISOU 1313  CA  PRO A 156    10515  10532  12525  -2239    238   2194       C  
ATOM   1314  C   PRO A 156     -62.784 -30.315 -13.391  1.00 84.31           C  
ANISOU 1314  C   PRO A 156     9735  10420  11878  -1823    406   2349       C  
ATOM   1315  O   PRO A 156     -63.212 -30.763 -12.320  1.00 77.47           O  
ANISOU 1315  O   PRO A 156     8743   9706  10987  -1889    454   2727       O  
ATOM   1316  CB  PRO A 156     -61.847 -31.881 -15.141  1.00 77.56           C  
ANISOU 1316  CB  PRO A 156     9643   8512  11313  -2118    234   1936       C  
ATOM   1317  CG  PRO A 156     -61.956 -31.916 -16.614  1.00 79.54           C  
ANISOU 1317  CG  PRO A 156    10114   8532  11577  -2367    122   1603       C  
ATOM   1318  CD  PRO A 156     -62.456 -30.535 -16.988  1.00 83.17           C  
ANISOU 1318  CD  PRO A 156    10178   9553  11869  -2279    119   1509       C  
ATOM   1319  N   ILE A 157     -62.081 -29.181 -13.462  1.00 74.59           N  
ANISOU 1319  N   ILE A 157     8440   9366  10536  -1427    496   2065       N  
ATOM   1320  CA  ILE A 157     -61.813 -28.392 -12.264  1.00 74.40           C  
ANISOU 1320  CA  ILE A 157     8224   9715  10328  -1079    648   2156       C  
ATOM   1321  C   ILE A 157     -63.098 -27.765 -11.736  1.00 88.46           C  
ANISOU 1321  C   ILE A 157     9635  12022  11952  -1140    754   2425       C  
ATOM   1322  O   ILE A 157     -63.413 -27.864 -10.542  1.00 78.89           O  
ANISOU 1322  O   ILE A 157     8284  11074  10618  -1080    861   2727       O  
ATOM   1323  CB  ILE A 157     -60.743 -27.326 -12.555  1.00 71.58           C  
ANISOU 1323  CB  ILE A 157     7933   9377   9887   -716    702   1768       C  
ATOM   1324  CG1 ILE A 157     -59.523 -27.965 -13.226  1.00 62.00           C  
ANISOU 1324  CG1 ILE A 157     7035   7682   8841   -642    621   1536       C  
ATOM   1325  CG2 ILE A 157     -60.359 -26.599 -11.284  1.00 72.26           C  
ANISOU 1325  CG2 ILE A 157     7910   9797   9747   -423    835   1829       C  
ATOM   1326  CD1 ILE A 157     -58.426 -26.988 -13.564  1.00 61.53           C  
ANISOU 1326  CD1 ILE A 157     7010   7657   8712   -331    659   1196       C  
ATOM   1327  N   LEU A 158     -63.865 -27.122 -12.621  1.00 84.60           N  
ANISOU 1327  N   LEU A 158     8969  11722  11453  -1241    740   2352       N  
ATOM   1328  CA  LEU A 158     -65.066 -26.416 -12.191  1.00 86.12           C  
ANISOU 1328  CA  LEU A 158     8772  12448  11503  -1212    885   2631       C  
ATOM   1329  C   LEU A 158     -66.099 -27.369 -11.594  1.00 86.44           C  
ANISOU 1329  C   LEU A 158     8610  12657  11574  -1557    857   3123       C  
ATOM   1330  O   LEU A 158     -66.873 -26.971 -10.715  1.00 83.91           O  
ANISOU 1330  O   LEU A 158     7984  12794  11103  -1442   1043   3436       O  
ATOM   1331  CB  LEU A 158     -65.648 -25.636 -13.372  1.00 82.73           C  
ANISOU 1331  CB  LEU A 158     8173  12176  11083  -1254    853   2512       C  
ATOM   1332  CG  LEU A 158     -65.185 -24.179 -13.475  1.00 77.28           C  
ANISOU 1332  CG  LEU A 158     7483  11613  10266   -808   1030   2217       C  
ATOM   1333  CD1 LEU A 158     -65.975 -23.426 -14.532  1.00 78.58           C  
ANISOU 1333  CD1 LEU A 158     7410  12008  10437   -834   1025   2232       C  
ATOM   1334  CD2 LEU A 158     -65.289 -23.476 -12.128  1.00 82.38           C  
ANISOU 1334  CD2 LEU A 158     8032  12567  10703   -460   1303   2338       C  
ATOM   1335  N   ASP A 159     -66.118 -28.630 -12.040  1.00 91.99           N  
ANISOU 1335  N   ASP A 159     9505  12984  12462  -1981    647   3203       N  
ATOM   1336  CA  ASP A 159     -67.039 -29.603 -11.455  1.00 93.40           C  
ANISOU 1336  CA  ASP A 159     9528  13276  12685  -2370    604   3690       C  
ATOM   1337  C   ASP A 159     -66.648 -29.948 -10.024  1.00 92.81           C  
ANISOU 1337  C   ASP A 159     9492  13240  12532  -2161    746   3919       C  
ATOM   1338  O   ASP A 159     -67.514 -30.043  -9.145  1.00 82.71           O  
ANISOU 1338  O   ASP A 159     7909  12366  11150  -2235    860   4353       O  
ATOM   1339  CB  ASP A 159     -67.094 -30.879 -12.299  1.00 90.80           C  
ANISOU 1339  CB  ASP A 159     9495  12442  12565  -2910    349   3682       C  
ATOM   1340  CG  ASP A 159     -67.425 -30.613 -13.756  1.00 95.56           C  
ANISOU 1340  CG  ASP A 159    10107  13006  13195  -3170    178   3436       C  
ATOM   1341  OD1 ASP A 159     -67.838 -29.480 -14.089  1.00 97.63           O  
ANISOU 1341  OD1 ASP A 159    10047  13708  13338  -2968    251   3389       O  
ATOM   1342  OD2 ASP A 159     -67.281 -31.552 -14.569  1.00 90.05           O1-
ANISOU 1342  OD2 ASP A 159     9765  11826  12623  -3577    -19   3299       O1-
ATOM   1343  N   ALA A 160     -65.351 -30.148  -9.771  1.00 88.24           N  
ANISOU 1343  N   ALA A 160     9257  12286  11984  -1899    742   3670       N  
ATOM   1344  CA  ALA A 160     -64.907 -30.535  -8.435  1.00 92.39           C  
ANISOU 1344  CA  ALA A 160     9824  12864  12416  -1721    841   3916       C  
ATOM   1345  C   ALA A 160     -65.112 -29.415  -7.423  1.00 93.28           C  
ANISOU 1345  C   ALA A 160     9677  13550  12214  -1362   1074   3974       C  
ATOM   1346  O   ALA A 160     -65.271 -29.685  -6.227  1.00 81.54           O  
ANISOU 1346  O   ALA A 160     8100  12305  10576  -1309   1183   4307       O  
ATOM   1347  CB  ALA A 160     -63.438 -30.955  -8.471  1.00 85.10           C  
ANISOU 1347  CB  ALA A 160     9279  11464  11592  -1502    774   3668       C  
ATOM   1348  N   ILE A 161     -65.105 -28.164  -7.873  1.00 92.13           N  
ANISOU 1348  N   ILE A 161     9448  13606  11952  -1112   1168   3657       N  
ATOM   1349  CA  ILE A 161     -65.321 -27.031  -6.982  1.00 91.46           C  
ANISOU 1349  CA  ILE A 161     9201  13996  11554   -760   1428   3658       C  
ATOM   1350  C   ILE A 161     -66.775 -26.996  -6.525  1.00 76.37           C  
ANISOU 1350  C   ILE A 161     6901  12567   9548   -866   1596   4108       C  
ATOM   1351  O   ILE A 161     -67.074 -27.271  -5.362  1.00 82.96           O  
ANISOU 1351  O   ILE A 161     7635  13677  10207   -829   1736   4440       O  
ATOM   1352  CB  ILE A 161     -64.918 -25.707  -7.660  1.00 87.27           C  
ANISOU 1352  CB  ILE A 161     8738  13469  10952   -472   1499   3202       C  
ATOM   1353  CG1 ILE A 161     -63.406 -25.683  -7.902  1.00 82.68           C  
ANISOU 1353  CG1 ILE A 161     8494  12505  10415   -343   1362   2810       C  
ATOM   1354  CG2 ILE A 161     -65.354 -24.516  -6.812  1.00 86.53           C  
ANISOU 1354  CG2 ILE A 161     8521  13823  10535   -129   1813   3211       C  
ATOM   1355  CD1 ILE A 161     -62.898 -24.443  -8.613  1.00 76.40           C  
ANISOU 1355  CD1 ILE A 161     7793  11667   9570   -113   1408   2368       C  
TER    1356      ILE A 161                                                      
ATOM   1357  N   ARG B   0     -14.642 -23.175 -22.192  1.00 65.74           N  
ANISOU 1357  N   ARG B   0     7272   8826   8880  -1080   3496   -761       N  
ATOM   1358  CA  ARG B   0     -14.732 -21.733 -21.997  1.00 74.97           C  
ANISOU 1358  CA  ARG B   0     8785   9976   9726  -1487   3482   -675       C  
ATOM   1359  C   ARG B   0     -15.988 -21.358 -21.204  1.00 65.44           C  
ANISOU 1359  C   ARG B   0     7875   8484   8505  -1349   3116   -440       C  
ATOM   1360  O   ARG B   0     -15.921 -21.199 -19.983  1.00 72.88           O  
ANISOU 1360  O   ARG B   0     8558   9548   9585  -1314   2932   -314       O  
ATOM   1361  CB  ARG B   0     -14.705 -21.009 -23.342  1.00 85.90           C  
ANISOU 1361  CB  ARG B   0    10682  11240  10715  -1841   3736   -799       C  
ATOM   1362  CG  ARG B   0     -14.329 -19.539 -23.244  1.00 80.63           C  
ANISOU 1362  CG  ARG B   0    10325  10620   9691  -2348   3828   -771       C  
ATOM   1363  CD  ARG B   0     -14.752 -18.772 -24.492  1.00 89.50           C  
ANISOU 1363  CD  ARG B   0    12164  11460  10383  -2633   3953   -804       C  
ATOM   1364  NE  ARG B   0     -14.192 -19.338 -25.716  1.00116.61           N  
ANISOU 1364  NE  ARG B   0    15545  15001  13761  -2699   4224  -1024       N  
ATOM   1365  CZ  ARG B   0     -14.887 -19.992 -26.639  1.00109.05           C  
ANISOU 1365  CZ  ARG B   0    14830  13826  12776  -2501   4262  -1068       C  
ATOM   1366  NH1 ARG B   0     -16.182 -20.225 -26.497  1.00 97.35           N  
ANISOU 1366  NH1 ARG B   0    13621  12014  11353  -2156   3941   -903       N  
ATOM   1367  NH2 ARG B   0     -14.265 -20.423 -27.733  1.00101.04           N  
ANISOU 1367  NH2 ARG B   0    13754  12936  11699  -2604   4503  -1286       N  
ATOM   1368  N   ASP B   1     -17.126 -21.217 -21.888  1.00 60.54           N  
ANISOU 1368  N   ASP B   1     7776   7520   7705  -1270   3010   -398       N  
ATOM   1369  CA  ASP B   1     -18.385 -20.954 -21.192  1.00 61.43           C  
ANISOU 1369  CA  ASP B   1     8124   7408   7808  -1092   2663   -221       C  
ATOM   1370  C   ASP B   1     -18.746 -22.124 -20.287  1.00 56.05           C  
ANISOU 1370  C   ASP B   1     7033   6769   7494   -727   2450   -141       C  
ATOM   1371  O   ASP B   1     -18.497 -23.280 -20.623  1.00 50.00           O  
ANISOU 1371  O   ASP B   1     6025   6031   6943   -517   2532   -220       O  
ATOM   1372  CB  ASP B   1     -19.520 -20.728 -22.194  1.00 59.49           C  
ANISOU 1372  CB  ASP B   1     8453   6846   7306  -1027   2586   -226       C  
ATOM   1373  CG  ASP B   1     -19.364 -19.448 -22.979  1.00 64.53           C  
ANISOU 1373  CG  ASP B   1     9626   7363   7531  -1374   2721   -252       C  
ATOM   1374  OD1 ASP B   1     -18.280 -18.824 -22.909  1.00 78.84           O  
ANISOU 1374  OD1 ASP B   1    11360   9349   9246  -1722   2941   -302       O  
ATOM   1375  OD2 ASP B   1     -20.329 -19.070 -23.680  1.00 68.16           O  
ANISOU 1375  OD2 ASP B   1    10598   7560   7741  -1310   2602   -227       O  
ATOM   1376  N   ILE B   2     -19.344 -21.825 -19.136  1.00 46.06           N  
ANISOU 1376  N   ILE B   2     5724   5492   6283   -663   2177     11       N  
ATOM   1377  CA  ILE B   2     -19.843 -22.878 -18.255  1.00 47.69           C  
ANISOU 1377  CA  ILE B   2     5634   5707   6780   -364   1949    106       C  
ATOM   1378  C   ILE B   2     -21.196 -23.339 -18.784  1.00 45.84           C  
ANISOU 1378  C   ILE B   2     5718   5221   6478   -166   1800    100       C  
ATOM   1379  O   ILE B   2     -22.145 -22.553 -18.856  1.00 49.68           O  
ANISOU 1379  O   ILE B   2     6559   5578   6737   -199   1653    128       O  
ATOM   1380  CB  ILE B   2     -19.966 -22.385 -16.806  1.00 42.47           C  
ANISOU 1380  CB  ILE B   2     4793   5167   6174   -415   1726    253       C  
ATOM   1381  CG1 ILE B   2     -18.646 -21.769 -16.327  1.00 50.14           C  
ANISOU 1381  CG1 ILE B   2     5478   6422   7152   -673   1878    243       C  
ATOM   1382  CG2 ILE B   2     -20.435 -23.553 -15.896  1.00 41.45           C  
ANISOU 1382  CG2 ILE B   2     4377   5050   6322   -144   1499    359       C  
ATOM   1383  CD1 ILE B   2     -18.599 -21.510 -14.829  1.00 46.90           C  
ANISOU 1383  CD1 ILE B   2     4796   6184   6838   -715   1670    383       C  
ATOM   1384  N   VAL B   3     -21.289 -24.604 -19.162  1.00 43.23           N  
ANISOU 1384  N   VAL B   3     5267   4829   6330     46   1834     47       N  
ATOM   1385  CA  VAL B   3     -22.546 -25.155 -19.650  1.00 42.25           C  
ANISOU 1385  CA  VAL B   3     5407   4509   6137    198   1705     21       C  
ATOM   1386  C   VAL B   3     -23.271 -25.815 -18.490  1.00 40.80           C  
ANISOU 1386  C   VAL B   3     5042   4335   6125    345   1434    139       C  
ATOM   1387  O   VAL B   3     -22.680 -26.600 -17.741  1.00 40.81           O  
ANISOU 1387  O   VAL B   3     4709   4409   6388    440   1413    206       O  
ATOM   1388  CB  VAL B   3     -22.312 -26.148 -20.797  1.00 48.60           C  
ANISOU 1388  CB  VAL B   3     6254   5214   6998    295   1914   -127       C  
ATOM   1389  CG1 VAL B   3     -23.631 -26.812 -21.186  1.00 49.80           C  
ANISOU 1389  CG1 VAL B   3     6644   5197   7080    424   1767   -158       C  
ATOM   1390  CG2 VAL B   3     -21.700 -25.435 -22.002  1.00 49.18           C  
ANISOU 1390  CG2 VAL B   3     6552   5292   6842     97   2185   -256       C  
ATOM   1391  N   LEU B   4     -24.545 -25.484 -18.325  1.00 44.46           N  
ANISOU 1391  N   LEU B   4     5726   4743   6423    362   1221    158       N  
ATOM   1392  CA  LEU B   4     -25.366 -26.085 -17.285  1.00 37.16           C  
ANISOU 1392  CA  LEU B   4     4661   3854   5603    445    976    240       C  
ATOM   1393  C   LEU B   4     -26.288 -27.118 -17.920  1.00 35.59           C  
ANISOU 1393  C   LEU B   4     4610   3533   5380    548    943    152       C  
ATOM   1394  O   LEU B   4     -27.142 -26.769 -18.742  1.00 42.34           O  
ANISOU 1394  O   LEU B   4     5746   4341   5999    549    916     50       O  
ATOM   1395  CB  LEU B   4     -26.182 -25.027 -16.545  1.00 33.98           C  
ANISOU 1395  CB  LEU B   4     4343   3541   5027    380    759    283       C  
ATOM   1396  CG  LEU B   4     -25.342 -23.958 -15.844  1.00 41.35           C  
ANISOU 1396  CG  LEU B   4     5168   4585   5957    237    786    363       C  
ATOM   1397  CD1 LEU B   4     -26.226 -23.093 -14.954  1.00 34.95           C  
ANISOU 1397  CD1 LEU B   4     4420   3852   5009    206    554    391       C  
ATOM   1398  CD2 LEU B   4     -24.164 -24.553 -15.074  1.00 37.37           C  
ANISOU 1398  CD2 LEU B   4     4268   4205   5726    213    853    461       C  
ATOM   1399  N   THR B   5     -26.143 -28.368 -17.510  1.00 37.38           N  
ANISOU 1399  N   THR B   5     4668   3706   5828    628    929    191       N  
ATOM   1400  CA  THR B   5     -26.999 -29.453 -17.980  1.00 33.58           C  
ANISOU 1400  CA  THR B   5     4336   3097   5325    679    902    107       C  
ATOM   1401  C   THR B   5     -28.026 -29.772 -16.898  1.00 37.63           C  
ANISOU 1401  C   THR B   5     4790   3691   5815    623    646    178       C  
ATOM   1402  O   THR B   5     -27.689 -30.379 -15.876  1.00 36.08           O  
ANISOU 1402  O   THR B   5     4407   3496   5807    629    562    309       O  
ATOM   1403  CB  THR B   5     -26.189 -30.685 -18.325  1.00 40.50           C  
ANISOU 1403  CB  THR B   5     5145   3807   6435    796   1072     83       C  
ATOM   1404  OG1 THR B   5     -25.222 -30.348 -19.339  1.00 45.53           O  
ANISOU 1404  OG1 THR B   5     5801   4426   7074    822   1332    -19       O  
ATOM   1405  CG2 THR B   5     -27.116 -31.798 -18.822  1.00 42.77           C  
ANISOU 1405  CG2 THR B   5     5645   3934   6670    803   1055    -15       C  
ATOM   1406  N   GLN B   6     -29.274 -29.417 -17.164  1.00 36.51           N  
ANISOU 1406  N   GLN B   6     4811   3633   5426    569    522     78       N  
ATOM   1407  CA  GLN B   6     -30.373 -29.545 -16.215  1.00 37.12           C  
ANISOU 1407  CA  GLN B   6     4820   3867   5418    480    290     89       C  
ATOM   1408  C   GLN B   6     -31.264 -30.716 -16.617  1.00 39.60           C  
ANISOU 1408  C   GLN B   6     5262   4123   5660    418    276    -20       C  
ATOM   1409  O   GLN B   6     -31.646 -30.830 -17.787  1.00 40.14           O  
ANISOU 1409  O   GLN B   6     5527   4140   5585    443    367   -168       O  
ATOM   1410  CB  GLN B   6     -31.187 -28.252 -16.177  1.00 32.34           C  
ANISOU 1410  CB  GLN B   6     4267   3455   4564    480    147     14       C  
ATOM   1411  CG  GLN B   6     -32.311 -28.282 -15.117  1.00 36.56           C  
ANISOU 1411  CG  GLN B   6     4669   4223   4999    384    -86    -12       C  
ATOM   1412  CD  GLN B   6     -33.088 -27.000 -15.039  1.00 37.44           C  
ANISOU 1412  CD  GLN B   6     4815   4530   4882    448   -236   -112       C  
ATOM   1413  OE1 GLN B   6     -32.657 -25.962 -15.535  1.00 34.92           O  
ANISOU 1413  OE1 GLN B   6     4633   4137   4498    549   -187   -107       O  
ATOM   1414  NE2 GLN B   6     -34.280 -27.074 -14.454  1.00 33.72           N  
ANISOU 1414  NE2 GLN B   6     4240   4309   4263    387   -420   -223       N  
ATOM   1415  N   SER B   7     -31.608 -31.574 -15.655  1.00 35.15           N  
ANISOU 1415  N   SER B   7     4615   3574   5166    303    165     49       N  
ATOM   1416  CA  SER B   7     -32.503 -32.690 -15.930  1.00 33.64           C  
ANISOU 1416  CA  SER B   7     4574   3336   4873    172    152    -60       C  
ATOM   1417  C   SER B   7     -33.486 -32.872 -14.779  1.00 40.74           C  
ANISOU 1417  C   SER B   7     5369   4457   5653    -41    -54    -50       C  
ATOM   1418  O   SER B   7     -33.154 -32.588 -13.619  1.00 39.60           O  
ANISOU 1418  O   SER B   7     5048   4392   5607    -76   -162    102       O  
ATOM   1419  CB  SER B   7     -31.737 -34.010 -16.131  1.00 47.69           C  
ANISOU 1419  CB  SER B   7     6470   4780   6870    214    295      5       C  
ATOM   1420  OG  SER B   7     -30.656 -34.103 -15.222  1.00 57.51           O  
ANISOU 1420  OG  SER B   7     7550   5932   8371    310    275    213       O  
ATOM   1421  N   PRO B   8     -34.700 -33.361 -15.065  1.00 45.95           N  
ANISOU 1421  N   PRO B   8     6022   4637   6798    124    359    110       N  
ATOM   1422  CA  PRO B   8     -35.225 -33.683 -16.392  1.00 42.95           C  
ANISOU 1422  CA  PRO B   8     5729   4206   6383      7    384    -74       C  
ATOM   1423  C   PRO B   8     -35.777 -32.457 -17.111  1.00 40.67           C  
ANISOU 1423  C   PRO B   8     5406   4091   5956    -64    219   -152       C  
ATOM   1424  O   PRO B   8     -36.030 -31.448 -16.469  1.00 39.72           O  
ANISOU 1424  O   PRO B   8     5196   4096   5799    -40    106    -76       O  
ATOM   1425  CB  PRO B   8     -36.342 -34.668 -16.080  1.00 45.53           C  
ANISOU 1425  CB  PRO B   8     6099   4409   6791   -112    449   -141       C  
ATOM   1426  CG  PRO B   8     -36.885 -34.177 -14.788  1.00 41.78           C  
ANISOU 1426  CG  PRO B   8     5529   4014   6331   -100    378    -24       C  
ATOM   1427  CD  PRO B   8     -35.709 -33.611 -14.016  1.00 43.75           C  
ANISOU 1427  CD  PRO B   8     5727   4337   6557     66    350    153       C  
ATOM   1428  N   ALA B   9     -35.957 -32.557 -18.431  1.00 38.59           N  
ANISOU 1428  N   ALA B   9     5234   3824   5606   -144    214   -298       N  
ATOM   1429  CA  ALA B   9     -36.655 -31.501 -19.156  1.00 46.00           C  
ANISOU 1429  CA  ALA B   9     6160   4920   6400   -201     42   -358       C  
ATOM   1430  C   ALA B   9     -38.108 -31.398 -18.697  1.00 46.79           C  
ANISOU 1430  C   ALA B   9     6156   5088   6532   -287    -79   -394       C  
ATOM   1431  O   ALA B   9     -38.673 -30.299 -18.628  1.00 45.18           O  
ANISOU 1431  O   ALA B   9     5874   5023   6269   -265   -226   -358       O  
ATOM   1432  CB  ALA B   9     -36.569 -31.762 -20.663  1.00 46.17           C  
ANISOU 1432  CB  ALA B   9     6325   4927   6289   -278     58   -506       C  
ATOM   1433  N   SER B  10     -38.721 -32.530 -18.363  1.00 47.55           N  
ANISOU 1433  N   SER B  10     6250   5077   6740   -384      4   -464       N  
ATOM   1434  CA  SER B  10     -40.118 -32.568 -17.959  1.00 47.26           C  
ANISOU 1434  CA  SER B  10     6094   5101   6763   -492    -76   -523       C  
ATOM   1435  C   SER B  10     -40.278 -33.537 -16.799  1.00 46.90           C  
ANISOU 1435  C   SER B  10     6040   4902   6877   -521     87   -475       C  
ATOM   1436  O   SER B  10     -39.748 -34.652 -16.834  1.00 46.91           O  
ANISOU 1436  O   SER B  10     6162   4720   6943   -535    256   -492       O  
ATOM   1437  CB  SER B  10     -41.013 -32.986 -19.131  1.00 56.03           C  
ANISOU 1437  CB  SER B  10     7218   6261   7810   -657   -160   -726       C  
ATOM   1438  OG  SER B  10     -42.367 -33.089 -18.728  1.00 72.22           O  
ANISOU 1438  OG  SER B  10     9109   8382   9950   -774   -230   -797       O  
ATOM   1439  N   LEU B  11     -41.038 -33.122 -15.791  1.00 39.87           N  
ANISOU 1439  N   LEU B  11     5026   4074   6050   -528     55   -413       N  
ATOM   1440  CA  LEU B  11     -41.225 -33.897 -14.570  1.00 48.20           C  
ANISOU 1440  CA  LEU B  11     6093   4994   7227   -551    215   -340       C  
ATOM   1441  C   LEU B  11     -42.715 -33.981 -14.282  1.00 46.68           C  
ANISOU 1441  C   LEU B  11     5765   4851   7122   -707    203   -443       C  
ATOM   1442  O   LEU B  11     -43.333 -32.976 -13.920  1.00 46.04           O  
ANISOU 1442  O   LEU B  11     5541   4920   7031   -679     96   -418       O  
ATOM   1443  CB  LEU B  11     -40.480 -33.253 -13.401  1.00 45.15           C  
ANISOU 1443  CB  LEU B  11     5704   4637   6813   -395    224   -139       C  
ATOM   1444  CG  LEU B  11     -40.414 -34.079 -12.122  1.00 48.43           C  
ANISOU 1444  CG  LEU B  11     6185   4910   7306   -384    389    -20       C  
ATOM   1445  CD1 LEU B  11     -40.081 -35.515 -12.460  1.00 54.18           C  
ANISOU 1445  CD1 LEU B  11     7054   5416   8116   -416    557    -50       C  
ATOM   1446  CD2 LEU B  11     -39.379 -33.477 -11.176  1.00 54.94           C  
ANISOU 1446  CD2 LEU B  11     7028   5792   8055   -221    361    172       C  
ATOM   1447  N   ALA B  12     -43.296 -35.161 -14.472  1.00 44.51           N  
ANISOU 1447  N   ALA B  12     5525   4442   6944   -877    327   -572       N  
ATOM   1448  CA  ALA B  12     -44.687 -35.417 -14.113  1.00 52.81           C  
ANISOU 1448  CA  ALA B  12     6431   5521   8114  -1056    360   -683       C  
ATOM   1449  C   ALA B  12     -44.693 -36.096 -12.749  1.00 60.12           C  
ANISOU 1449  C   ALA B  12     7436   6266   9140  -1066    592   -562       C  
ATOM   1450  O   ALA B  12     -44.206 -37.223 -12.605  1.00 60.18           O  
ANISOU 1450  O   ALA B  12     7625   6045   9195  -1091    779   -537       O  
ATOM   1451  CB  ALA B  12     -45.381 -36.287 -15.161  1.00 54.62           C  
ANISOU 1451  CB  ALA B  12     6647   5721   8384  -1281    362   -923       C  
ATOM   1452  N   VAL B  13     -45.258 -35.427 -11.751  1.00 52.80           N  
ANISOU 1452  N   VAL B  13     6395   5427   8240  -1042    595   -484       N  
ATOM   1453  CA  VAL B  13     -45.179 -35.908 -10.383  1.00 54.89           C  
ANISOU 1453  CA  VAL B  13     6766   5542   8546  -1030    804   -339       C  
ATOM   1454  C   VAL B  13     -46.593 -35.999  -9.822  1.00 69.78           C  
ANISOU 1454  C   VAL B  13     8499   7450  10563  -1211    912   -438       C  
ATOM   1455  O   VAL B  13     -47.535 -35.380 -10.327  1.00 54.48           O  
ANISOU 1455  O   VAL B  13     6329   5692   8679  -1286    782   -580       O  
ATOM   1456  CB  VAL B  13     -44.286 -34.992  -9.511  1.00 63.27           C  
ANISOU 1456  CB  VAL B  13     7881   6679   9478   -818    744   -128       C  
ATOM   1457  CG1 VAL B  13     -44.838 -33.570  -9.497  1.00 56.57           C  
ANISOU 1457  CG1 VAL B  13     6843   6055   8595   -779    585   -160       C  
ATOM   1458  CG2 VAL B  13     -44.066 -35.566  -8.098  1.00 69.15           C  
ANISOU 1458  CG2 VAL B  13     8783   7278  10214   -792    943     46       C  
ATOM   1459  N   SER B  14     -46.739 -36.819  -8.787  1.00 64.27           N  
ANISOU 1459  N   SER B  14     7934   6563   9923  -1279   1161   -357       N  
ATOM   1460  CA  SER B  14     -47.986 -36.929  -8.051  1.00 70.20           C  
ANISOU 1460  CA  SER B  14     8564   7309  10799  -1452   1324   -427       C  
ATOM   1461  C   SER B  14     -47.974 -35.939  -6.896  1.00 57.26           C  
ANISOU 1461  C   SER B  14     6908   5772   9077  -1326   1332   -278       C  
ATOM   1462  O   SER B  14     -46.923 -35.673  -6.308  1.00 67.48           O  
ANISOU 1462  O   SER B  14     8377   7044  10218  -1147   1306    -84       O  
ATOM   1463  CB  SER B  14     -48.169 -38.350  -7.522  1.00 62.10           C  
ANISOU 1463  CB  SER B  14     7731   5996   9867  -1609   1630   -415       C  
ATOM   1464  OG  SER B  14     -48.161 -39.289  -8.578  1.00 76.54           O  
ANISOU 1464  OG  SER B  14     9604   7720  11758  -1730   1640   -571       O  
ATOM   1465  N   LEU B  15     -49.143 -35.387  -6.580  1.00 66.97           N  
ANISOU 1465  N   LEU B  15     7916   7120  10411  -1423   1371   -380       N  
ATOM   1466  CA  LEU B  15     -49.238 -34.469  -5.453  1.00 65.70           C  
ANISOU 1466  CA  LEU B  15     7753   7034  10178  -1329   1426   -268       C  
ATOM   1467  C   LEU B  15     -48.843 -35.216  -4.183  1.00 48.34           C  
ANISOU 1467  C   LEU B  15     5836   4636   7893  -1343   1678    -95       C  
ATOM   1468  O   LEU B  15     -49.264 -36.350  -3.965  1.00 48.32           O  
ANISOU 1468  O   LEU B  15     5924   4447   7989  -1506   1903   -122       O  
ATOM   1469  CB  LEU B  15     -50.660 -33.910  -5.348  1.00 61.30           C  
ANISOU 1469  CB  LEU B  15     6894   6606   9790  -1440   1478   -423       C  
ATOM   1470  CG  LEU B  15     -51.011 -32.666  -4.513  1.00 63.71           C  
ANISOU 1470  CG  LEU B  15     7109   7032  10064  -1338   1505   -379       C  
ATOM   1471  CD1 LEU B  15     -52.521 -32.483  -4.512  1.00 82.64           C  
ANISOU 1471  CD1 LEU B  15     9181   9519  12697  -1474   1608   -555       C  
ATOM   1472  CD2 LEU B  15     -50.477 -32.646  -3.076  1.00 76.04           C  
ANISOU 1472  CD2 LEU B  15     8943   8488  11460  -1293   1700   -202       C  
ATOM   1473  N   GLY B  16     -47.995 -34.594  -3.367  1.00 51.53           N  
ANISOU 1473  N   GLY B  16     6397   5080   8102  -1175   1635     86       N  
ATOM   1474  CA  GLY B  16     -47.512 -35.199  -2.146  1.00 61.02           C  
ANISOU 1474  CA  GLY B  16     7884   6132   9168  -1154   1823    281       C  
ATOM   1475  C   GLY B  16     -46.160 -35.873  -2.254  1.00 60.13           C  
ANISOU 1475  C   GLY B  16     7999   5913   8933  -1006   1746    457       C  
ATOM   1476  O   GLY B  16     -45.567 -36.197  -1.217  1.00 53.10           O  
ANISOU 1476  O   GLY B  16     7345   4944   7884   -927   1834    661       O  
ATOM   1477  N   GLN B  17     -45.656 -36.102  -3.467  1.00 53.76           N  
ANISOU 1477  N   GLN B  17     7130   5107   8191   -957   1589    390       N  
ATOM   1478  CA  GLN B  17     -44.399 -36.814  -3.625  1.00 52.43           C  
ANISOU 1478  CA  GLN B  17     7153   4820   7948   -807   1550    546       C  
ATOM   1479  C   GLN B  17     -43.219 -35.856  -3.545  1.00 44.96           C  
ANISOU 1479  C   GLN B  17     6199   4054   6828   -599   1313    663       C  
ATOM   1480  O   GLN B  17     -43.367 -34.633  -3.445  1.00 44.09           O  
ANISOU 1480  O   GLN B  17     5958   4141   6653   -582   1185    612       O  
ATOM   1481  CB  GLN B  17     -44.380 -37.594  -4.941  1.00 53.34           C  
ANISOU 1481  CB  GLN B  17     7232   4824   8212   -868   1540    405       C  
ATOM   1482  CG  GLN B  17     -45.441 -38.670  -4.997  1.00 62.07           C  
ANISOU 1482  CG  GLN B  17     8367   5727   9489  -1102   1792    280       C  
ATOM   1483  CD  GLN B  17     -45.411 -39.580  -3.770  1.00 76.24           C  
ANISOU 1483  CD  GLN B  17    10417   7319  11231  -1095   2041    463       C  
ATOM   1484  OE1 GLN B  17     -46.408 -39.712  -3.060  1.00 66.98           O  
ANISOU 1484  OE1 GLN B  17     9224   6153  10072  -1228   2193    412       O  
ATOM   1485  NE2 GLN B  17     -44.277 -40.246  -3.546  1.00 71.87           N  
ANISOU 1485  NE2 GLN B  17    10080   6644  10582   -899   2042    662       N  
ATOM   1486  N   ARG B  18     -42.021 -36.425  -3.594  1.00 47.07           N  
ANISOU 1486  N   ARG B  18     6603   4246   7034   -439   1269    818       N  
ATOM   1487  CA  ARG B  18     -40.800 -35.640  -3.711  1.00 47.06           C  
ANISOU 1487  CA  ARG B  18     6561   4416   6905   -259   1044    904       C  
ATOM   1488  C   ARG B  18     -40.458 -35.428  -5.182  1.00 46.95           C  
ANISOU 1488  C   ARG B  18     6411   4446   6981   -238    911    760       C  
ATOM   1489  O   ARG B  18     -40.509 -36.369  -5.978  1.00 48.12           O  
ANISOU 1489  O   ARG B  18     6599   4432   7253   -273    997    693       O  
ATOM   1490  CB  ARG B  18     -39.651 -36.348  -2.989  1.00 52.16           C  
ANISOU 1490  CB  ARG B  18     7386   4984   7448    -78   1054   1155       C  
ATOM   1491  CG  ARG B  18     -38.319 -35.638  -3.061  1.00 50.91           C  
ANISOU 1491  CG  ARG B  18     7155   5014   7174     99    826   1243       C  
ATOM   1492  CD  ARG B  18     -37.257 -36.487  -2.419  1.00 49.35           C  
ANISOU 1492  CD  ARG B  18     7101   4740   6909    294    831   1494       C  
ATOM   1493  NE  ARG B  18     -37.784 -37.052  -1.182  1.00 64.93           N  
ANISOU 1493  NE  ARG B  18     9278   6608   8786    262    985   1644       N  
ATOM   1494  CZ  ARG B  18     -37.548 -36.565   0.029  1.00 63.74           C  
ANISOU 1494  CZ  ARG B  18     9204   6604   8410    298    912   1785       C  
ATOM   1495  NH1 ARG B  18     -36.811 -35.478   0.202  1.00 59.67           N  
ANISOU 1495  NH1 ARG B  18     8566   6353   7755    350    684   1781       N  
ATOM   1496  NH2 ARG B  18     -38.074 -37.179   1.091  1.00 67.97           N  
ANISOU 1496  NH2 ARG B  18     9962   7015   8848    260   1086   1924       N  
ATOM   1497  N   ALA B  19     -40.133 -34.192  -5.542  1.00 42.01           N  
ANISOU 1497  N   ALA B  19     5652   4026   6286   -194    723    706       N  
ATOM   1498  CA  ALA B  19     -39.571 -33.881  -6.848  1.00 45.23           C  
ANISOU 1498  CA  ALA B  19     5968   4489   6727   -147    593    610       C  
ATOM   1499  C   ALA B  19     -38.133 -33.422  -6.670  1.00 47.14           C  
ANISOU 1499  C   ALA B  19     6214   4837   6862     20    468    740       C  
ATOM   1500  O   ALA B  19     -37.833 -32.628  -5.771  1.00 40.94           O  
ANISOU 1500  O   ALA B  19     5419   4186   5950     54    394    822       O  
ATOM   1501  CB  ALA B  19     -40.383 -32.801  -7.568  1.00 41.29           C  
ANISOU 1501  CB  ALA B  19     5312   4131   6246   -235    487    438       C  
ATOM   1502  N   THR B  20     -37.251 -33.912  -7.534  1.00 38.53           N  
ANISOU 1502  N   THR B  20     5129   3689   5823    109    453    742       N  
ATOM   1503  CA  THR B  20     -35.851 -33.513  -7.521  1.00 40.74           C  
ANISOU 1503  CA  THR B  20     5365   4078   6037    260    343    843       C  
ATOM   1504  C   THR B  20     -35.428 -33.098  -8.920  1.00 42.50           C  
ANISOU 1504  C   THR B  20     5509   4340   6298    260    285    710       C  
ATOM   1505  O   THR B  20     -35.715 -33.797  -9.896  1.00 41.12           O  
ANISOU 1505  O   THR B  20     5375   4034   6215    218    368    605       O  
ATOM   1506  CB  THR B  20     -34.938 -34.643  -7.029  1.00 52.57           C  
ANISOU 1506  CB  THR B  20     6950   5457   7567    421    414   1027       C  
ATOM   1507  OG1 THR B  20     -35.415 -35.120  -5.766  1.00 50.05           O  
ANISOU 1507  OG1 THR B  20     6749   5075   7191    415    488   1163       O  
ATOM   1508  CG2 THR B  20     -33.518 -34.125  -6.855  1.00 48.41           C  
ANISOU 1508  CG2 THR B  20     6321   5096   6976    573    275   1133       C  
ATOM   1509  N   ILE B  21     -34.736 -31.974  -9.008  1.00 34.99           N  
ANISOU 1509  N   ILE B  21     4466   3563   5266    293    159    710       N  
ATOM   1510  CA  ILE B  21     -34.253 -31.433 -10.274  1.00 36.91           C  
ANISOU 1510  CA  ILE B  21     4656   3852   5518    291    116    601       C  
ATOM   1511  C   ILE B  21     -32.747 -31.293 -10.168  1.00 39.66           C  
ANISOU 1511  C   ILE B  21     4932   4281   5856    417     79    695       C  
ATOM   1512  O   ILE B  21     -32.234 -30.839  -9.142  1.00 40.19           O  
ANISOU 1512  O   ILE B  21     4947   4474   5851    456     -1    800       O  
ATOM   1513  CB  ILE B  21     -34.912 -30.077 -10.591  1.00 40.27           C  
ANISOU 1513  CB  ILE B  21     5035   4399   5868    195     23    498       C  
ATOM   1514  CG1 ILE B  21     -36.434 -30.224 -10.561  1.00 38.62           C  
ANISOU 1514  CG1 ILE B  21     4844   4138   5692     88     49    415       C  
ATOM   1515  CG2 ILE B  21     -34.417 -29.554 -11.938  1.00 38.70           C  
ANISOU 1515  CG2 ILE B  21     4822   4229   5654    194     -5    405       C  
ATOM   1516  CD1 ILE B  21     -37.188 -28.913 -10.612  1.00 38.65           C  
ANISOU 1516  CD1 ILE B  21     4791   4252   5642     32    -34    348       C  
ATOM   1517  N   SER B  22     -32.033 -31.662 -11.234  1.00 39.86           N  
ANISOU 1517  N   SER B  22     4947   4249   5950    470    139    646       N  
ATOM   1518  CA  SER B  22     -30.590 -31.781 -11.173  1.00 41.17           C  
ANISOU 1518  CA  SER B  22     5014   4470   6157    606    139    735       C  
ATOM   1519  C   SER B  22     -29.958 -30.811 -12.158  1.00 40.16           C  
ANISOU 1519  C   SER B  22     4816   4440   6002    563    120    630       C  
ATOM   1520  O   SER B  22     -30.516 -30.539 -13.223  1.00 37.30           O  
ANISOU 1520  O   SER B  22     4530   4028   5613    471    155    498       O  
ATOM   1521  CB  SER B  22     -30.130 -33.204 -11.492  1.00 45.18           C  
ANISOU 1521  CB  SER B  22     5571   4792   6802    737    285    786       C  
ATOM   1522  OG  SER B  22     -30.805 -34.139 -10.665  1.00 62.71           O  
ANISOU 1522  OG  SER B  22     7898   6879   9048    761    337    881       O  
ATOM   1523  N   CYS B  23     -28.811 -30.272 -11.768  1.00 36.16           N  
ANISOU 1523  N   CYS B  23     4167   4082   5491    618     62    693       N  
ATOM   1524  CA  CYS B  23     -28.027 -29.371 -12.607  1.00 36.35           C  
ANISOU 1524  CA  CYS B  23     4114   4194   5504    572     77    606       C  
ATOM   1525  C   CYS B  23     -26.578 -29.802 -12.480  1.00 43.09           C  
ANISOU 1525  C   CYS B  23     4793   5109   6468    709    110    683       C  
ATOM   1526  O   CYS B  23     -26.060 -29.901 -11.364  1.00 46.89           O  
ANISOU 1526  O   CYS B  23     5154   5711   6951    786      6    809       O  
ATOM   1527  CB  CYS B  23     -28.218 -27.906 -12.173  1.00 46.79           C  
ANISOU 1527  CB  CYS B  23     5410   5664   6703    443    -34    569       C  
ATOM   1528  SG  CYS B  23     -27.769 -26.673 -13.418  1.00 56.65           S  
ANISOU 1528  SG  CYS B  23     6669   6946   7910    334     27    439       S  
ATOM   1529  N   ARG B  24     -25.937 -30.100 -13.608  1.00 41.50           N  
ANISOU 1529  N   ARG B  24     4576   4834   6357    746    255    612       N  
ATOM   1530  CA  ARG B  24     -24.521 -30.423 -13.625  1.00 40.60           C  
ANISOU 1530  CA  ARG B  24     4260   4787   6381    881    312    667       C  
ATOM   1531  C   ARG B  24     -23.810 -29.369 -14.459  1.00 51.27           C  
ANISOU 1531  C   ARG B  24     5531   6232   7717    768    373    548       C  
ATOM   1532  O   ARG B  24     -24.219 -29.097 -15.592  1.00 43.76           O  
ANISOU 1532  O   ARG B  24     4738   5178   6709    671    485    425       O  
ATOM   1533  CB  ARG B  24     -24.274 -31.823 -14.185  1.00 46.12           C  
ANISOU 1533  CB  ARG B  24     5005   5283   7234   1043    491    688       C  
ATOM   1534  CG  ARG B  24     -22.808 -32.194 -14.246  1.00 51.98           C  
ANISOU 1534  CG  ARG B  24     5511   6086   8153   1216    571    748       C  
ATOM   1535  CD  ARG B  24     -22.633 -33.667 -14.544  1.00 60.10           C  
ANISOU 1535  CD  ARG B  24     6600   6885   9348   1415    753    802       C  
ATOM   1536  NE  ARG B  24     -22.008 -34.345 -13.418  1.00 59.68           N  
ANISOU 1536  NE  ARG B  24     6384   6889   9404   1647    664   1016       N  
ATOM   1537  CZ  ARG B  24     -21.890 -35.660 -13.306  1.00 73.39           C  
ANISOU 1537  CZ  ARG B  24     8177   8419  11287   1863    792   1127       C  
ATOM   1538  NH1 ARG B  24     -22.328 -36.478 -14.250  1.00 72.00           N  
ANISOU 1538  NH1 ARG B  24     8217   7960  11179   1857   1031   1019       N  
ATOM   1539  NH2 ARG B  24     -21.324 -36.169 -12.216  1.00 75.55           N  
ANISOU 1539  NH2 ARG B  24     8320   8779  11607   2065    669   1337       N  
ATOM   1540  N   ALA B  25     -22.773 -28.763 -13.890  1.00 45.22           N  
ANISOU 1540  N   ALA B  25     4528   5667   6987    768    299    584       N  
ATOM   1541  CA  ALA B  25     -22.014 -27.713 -14.555  1.00 46.94           C  
ANISOU 1541  CA  ALA B  25     4653   5979   7205    637    375    472       C  
ATOM   1542  C   ALA B  25     -20.777 -28.298 -15.224  1.00 41.63           C  
ANISOU 1542  C   ALA B  25     3797   5298   6723    755    552    457       C  
ATOM   1543  O   ALA B  25     -20.196 -29.276 -14.746  1.00 44.10           O  
ANISOU 1543  O   ALA B  25     3947   5626   7183    956    542    567       O  
ATOM   1544  CB  ALA B  25     -21.598 -26.623 -13.564  1.00 43.91           C  
ANISOU 1544  CB  ALA B  25     4106   5824   6754    519    209    481       C  
ATOM   1545  N   SER B  26     -20.369 -27.689 -16.339  1.00 41.90           N  
ANISOU 1545  N   SER B  26     3864   5299   6756    639    731    326       N  
ATOM   1546  CA  SER B  26     -19.213 -28.222 -17.056  1.00 50.03           C  
ANISOU 1546  CA  SER B  26     4726   6308   7976    740    947    291       C  
ATOM   1547  C   SER B  26     -17.901 -27.932 -16.334  1.00 52.82           C  
ANISOU 1547  C   SER B  26     4682   6904   8482    778    882    334       C  
ATOM   1548  O   SER B  26     -16.883 -28.552 -16.655  1.00 52.24           O  
ANISOU 1548  O   SER B  26     4388   6842   8617    922   1030    341       O  
ATOM   1549  CB  SER B  26     -19.175 -27.664 -18.480  1.00 42.73           C  
ANISOU 1549  CB  SER B  26     3981   5272   6982    592   1182    139       C  
ATOM   1550  OG  SER B  26     -19.117 -26.252 -18.464  1.00 44.94           O  
ANISOU 1550  OG  SER B  26     4268   5662   7145    379   1140     79       O  
ATOM   1551  N   GLU B  27     -17.899 -26.992 -15.386  1.00 49.01           N  
ANISOU 1551  N   GLU B  27     4095   6620   7904    646    670    350       N  
ATOM   1552  CA  GLU B  27     -16.754 -26.749 -14.516  1.00 50.77           C  
ANISOU 1552  CA  GLU B  27     3930   7118   8244    666    542    391       C  
ATOM   1553  C   GLU B  27     -17.280 -26.187 -13.203  1.00 44.23           C  
ANISOU 1553  C   GLU B  27     3115   6446   7243    576    251    451       C  
ATOM   1554  O   GLU B  27     -18.450 -25.826 -13.093  1.00 42.36           O  
ANISOU 1554  O   GLU B  27     3174   6097   6824    480    198    439       O  
ATOM   1555  CB  GLU B  27     -15.746 -25.787 -15.153  1.00 52.13           C  
ANISOU 1555  CB  GLU B  27     3916   7396   8496    478    703    242       C  
ATOM   1556  CG  GLU B  27     -16.402 -24.674 -15.940  1.00 58.37           C  
ANISOU 1556  CG  GLU B  27     5015   8054   9109    225    828    110       C  
ATOM   1557  CD  GLU B  27     -15.398 -23.715 -16.536  1.00 59.93           C  
ANISOU 1557  CD  GLU B  27     5057   8332   9383     22   1019    -31       C  
ATOM   1558  OE1 GLU B  27     -14.545 -23.199 -15.783  1.00 62.80           O  
ANISOU 1558  OE1 GLU B  27     5098   8938   9825    -74    912    -59       O  
ATOM   1559  OE2 GLU B  27     -15.452 -23.493 -17.762  1.00 69.83           O1-
ANISOU 1559  OE2 GLU B  27     6512   9410  10610    -53   1281   -118       O1-
ATOM   1560  N   SER B  28     -16.393 -26.102 -12.212  1.00 45.18           N  
ANISOU 1560  N   SER B  28     2905   6841   7422    606     66    509       N  
ATOM   1561  CA  SER B  28     -16.795 -25.687 -10.872  1.00 52.65           C  
ANISOU 1561  CA  SER B  28     3861   7957   8188    532   -215    570       C  
ATOM   1562  C   SER B  28     -17.371 -24.275 -10.879  1.00 50.97           C  
ANISOU 1562  C   SER B  28     3838   7736   7792    222   -210    418       C  
ATOM   1563  O   SER B  28     -16.876 -23.389 -11.583  1.00 44.28           O  
ANISOU 1563  O   SER B  28     2943   6894   6987     33    -57    269       O  
ATOM   1564  CB  SER B  28     -15.594 -25.754  -9.926  1.00 53.02           C  
ANISOU 1564  CB  SER B  28     3491   8340   8315    592   -421    634       C  
ATOM   1565  OG  SER B  28     -15.972 -25.363  -8.619  1.00 57.37           O  
ANISOU 1565  OG  SER B  28     4080   9065   8653    507   -693    684       O  
ATOM   1566  N   VAL B  29     -18.424 -24.066 -10.091  1.00 45.93           N  
ANISOU 1566  N   VAL B  29     3428   7065   6958    175   -352    459       N  
ATOM   1567  CA  VAL B  29     -18.985 -22.736  -9.897  1.00 47.73           C  
ANISOU 1567  CA  VAL B  29     3830   7286   7018    -92   -358    331       C  
ATOM   1568  C   VAL B  29     -18.637 -22.179  -8.515  1.00 45.52           C  
ANISOU 1568  C   VAL B  29     3408   7275   6614   -218   -591    322       C  
ATOM   1569  O   VAL B  29     -19.234 -21.201  -8.078  1.00 48.29           O  
ANISOU 1569  O   VAL B  29     3934   7611   6804   -417   -615    232       O  
ATOM   1570  CB  VAL B  29     -20.504 -22.711 -10.147  1.00 44.34           C  
ANISOU 1570  CB  VAL B  29     3775   6608   6463    -86   -305    344       C  
ATOM   1571  CG1 VAL B  29     -20.819 -23.043 -11.597  1.00 43.87           C  
ANISOU 1571  CG1 VAL B  29     3868   6314   6486    -22    -88    313       C  
ATOM   1572  CG2 VAL B  29     -21.228 -23.667  -9.210  1.00 41.93           C  
ANISOU 1572  CG2 VAL B  29     3549   6296   6087     80   -457    497       C  
ATOM   1573  N   GLU B  30     -17.657 -22.773  -7.837  1.00 46.40           N  
ANISOU 1573  N   GLU B  30     3202   7635   6792   -104   -760    409       N  
ATOM   1574  CA  GLU B  30     -17.220 -22.301  -6.530  1.00 47.94           C  
ANISOU 1574  CA  GLU B  30     3240   8130   6845   -228  -1011    398       C  
ATOM   1575  C   GLU B  30     -16.360 -21.045  -6.661  1.00 55.86           C  
ANISOU 1575  C   GLU B  30     4056   9296   7872   -535   -971    184       C  
ATOM   1576  O   GLU B  30     -15.637 -20.860  -7.648  1.00 58.77           O  
ANISOU 1576  O   GLU B  30     4267   9632   8430   -578   -786     96       O  
ATOM   1577  CB  GLU B  30     -16.425 -23.392  -5.812  1.00 53.73           C  
ANISOU 1577  CB  GLU B  30     3680   9094   7639     25  -1228    584       C  
ATOM   1578  CG  GLU B  30     -17.256 -24.602  -5.429  1.00 61.13           C  
ANISOU 1578  CG  GLU B  30     4825   9880   8523    304  -1280    805       C  
ATOM   1579  CD  GLU B  30     -18.091 -24.390  -4.174  1.00 75.42           C  
ANISOU 1579  CD  GLU B  30     6858  11749  10048    227  -1460    857       C  
ATOM   1580  OE1 GLU B  30     -17.890 -23.371  -3.473  1.00 80.26           O  
ANISOU 1580  OE1 GLU B  30     7433  12566  10497    -24  -1584    730       O  
ATOM   1581  OE2 GLU B  30     -18.969 -25.240  -3.905  1.00 72.11           O1-
ANISOU 1581  OE2 GLU B  30     6671  11158   9569    401  -1451   1011       O1-
ATOM   1582  N   TYR B  30A    -16.415 -20.189  -5.634  1.00 52.28           N  
ANISOU 1582  N   TYR B  30A    3628   9014   7221   -766  -1127     91       N  
ATOM   1583  CA  TYR B  30A    -15.666 -18.928  -5.665  1.00 64.50           C  
ANISOU 1583  CA  TYR B  30A    5032  10700   8777  -1107  -1077   -138       C  
ATOM   1584  C   TYR B  30A    -15.364 -18.492  -4.231  1.00 59.76           C  
ANISOU 1584  C   TYR B  30A    4406  10324   7974  -1245  -1330   -191       C  
ATOM   1585  O   TYR B  30A    -16.200 -17.847  -3.593  1.00 67.10           O  
ANISOU 1585  O   TYR B  30A    5599  11214   8684  -1410  -1355   -256       O  
ATOM   1586  CB  TYR B  30A    -16.447 -17.860  -6.424  1.00 56.32           C  
ANISOU 1586  CB  TYR B  30A    4341   9355   7704  -1309   -806   -284       C  
ATOM   1587  CG  TYR B  30A    -15.759 -16.515  -6.502  1.00 61.72           C  
ANISOU 1587  CG  TYR B  30A    4942  10112   8397  -1678   -698   -524       C  
ATOM   1588  CD1 TYR B  30A    -14.685 -16.315  -7.362  1.00 55.19           C  
ANISOU 1588  CD1 TYR B  30A    3876   9312   7783  -1754   -535   -612       C  
ATOM   1589  CD2 TYR B  30A    -16.201 -15.432  -5.745  1.00 55.64           C  
ANISOU 1589  CD2 TYR B  30A    4373   9336   7431  -1950   -719   -668       C  
ATOM   1590  CE1 TYR B  30A    -14.055 -15.093  -7.452  1.00 61.54           C  
ANISOU 1590  CE1 TYR B  30A    4704  10078   8601  -2048   -401   -804       C  
ATOM   1591  CE2 TYR B  30A    -15.573 -14.194  -5.835  1.00 55.19           C  
ANISOU 1591  CE2 TYR B  30A    4346   9231   7392  -2236   -575   -871       C  
ATOM   1592  CZ  TYR B  30A    -14.502 -14.035  -6.691  1.00 60.61           C  
ANISOU 1592  CZ  TYR B  30A    4826   9917   8288  -2285   -422   -931       C  
ATOM   1593  OH  TYR B  30A    -13.864 -12.815  -6.792  1.00 66.49           O  
ANISOU 1593  OH  TYR B  30A    5610  10607   9047  -2568   -267  -1120       O  
ATOM   1594  N   TYR B  30B    -14.170 -18.836  -3.745  1.00 69.33           N  
ANISOU 1594  N   TYR B  30B    5332  11743   9268  -1170  -1497   -169       N  
ATOM   1595  CA  TYR B  30B    -13.648 -18.362  -2.458  1.00 60.63           C  
ANISOU 1595  CA  TYR B  30B    4185  10861   7990  -1316  -1729   -242       C  
ATOM   1596  C   TYR B  30B    -14.683 -18.473  -1.334  1.00 75.63           C  
ANISOU 1596  C   TYR B  30B    6377  12778   9582  -1299  -1882   -166       C  
ATOM   1597  O   TYR B  30B    -15.035 -17.493  -0.673  1.00 77.65           O  
ANISOU 1597  O   TYR B  30B    6822  13049   9632  -1562  -1886   -317       O  
ATOM   1598  CB  TYR B  30B    -13.131 -16.924  -2.576  1.00 69.96           C  
ANISOU 1598  CB  TYR B  30B    5356  12051   9175  -1694  -1602   -507       C  
ATOM   1599  CG  TYR B  30B    -12.010 -16.709  -3.578  1.00 62.72           C  
ANISOU 1599  CG  TYR B  30B    4153  11130   8546  -1754  -1440   -593       C  
ATOM   1600  CD1 TYR B  30B    -10.843 -17.461  -3.519  1.00 61.92           C  
ANISOU 1600  CD1 TYR B  30B    3676  11213   8637  -1577  -1581   -509       C  
ATOM   1601  CD2 TYR B  30B    -12.121 -15.751  -4.580  1.00 61.79           C  
ANISOU 1601  CD2 TYR B  30B    4157  10809   8512  -1981  -1128   -752       C  
ATOM   1602  CE1 TYR B  30B     -9.815 -17.258  -4.427  1.00 64.88           C  
ANISOU 1602  CE1 TYR B  30B    3781  11583   9286  -1641  -1410   -587       C  
ATOM   1603  CE2 TYR B  30B    -11.104 -15.546  -5.495  1.00 62.75           C  
ANISOU 1603  CE2 TYR B  30B    4044  10917   8881  -2045   -951   -824       C  
ATOM   1604  CZ  TYR B  30B     -9.953 -16.300  -5.415  1.00 63.07           C  
ANISOU 1604  CZ  TYR B  30B    3691  11157   9116  -1882  -1088   -743       C  
ATOM   1605  OH  TYR B  30B     -8.939 -16.092  -6.326  1.00 71.79           O  
ANISOU 1605  OH  TYR B  30B    4555  12248  10473  -1955   -889   -812       O  
ATOM   1606  N   GLY B  30C    -15.164 -19.693  -1.116  1.00 66.81           N  
ANISOU 1606  N   GLY B  30C    5312  11636   8438   -984  -1983     73       N  
ATOM   1607  CA  GLY B  30C    -16.050 -19.954   0.000  1.00 77.24           C  
ANISOU 1607  CA  GLY B  30C    6895  12978   9474   -940  -2126    176       C  
ATOM   1608  C   GLY B  30C    -17.515 -19.690  -0.252  1.00 72.82           C  
ANISOU 1608  C   GLY B  30C    6664  12204   8803  -1009  -1968    174       C  
ATOM   1609  O   GLY B  30C    -18.290 -19.626   0.710  1.00 76.27           O  
ANISOU 1609  O   GLY B  30C    7343  12651   8985  -1053  -2047    205       O  
ATOM   1610  N   THR B  30D    -17.915 -19.511  -1.507  1.00 67.93           N  
ANISOU 1610  N   THR B  30D    6059  11392   8362  -1029  -1744    134       N  
ATOM   1611  CA  THR B  30D    -19.317 -19.458  -1.880  1.00 64.90           C  
ANISOU 1611  CA  THR B  30D    6048  10670   7942   -989  -1548    153       C  
ATOM   1612  C   THR B  30D    -19.474 -20.131  -3.237  1.00 56.04           C  
ANISOU 1612  C   THR B  30D    4921   9298   7073   -775  -1354    236       C  
ATOM   1613  O   THR B  30D    -18.523 -20.214  -4.019  1.00 58.25           O  
ANISOU 1613  O   THR B  30D    4948   9634   7551   -752  -1298    205       O  
ATOM   1614  CB  THR B  30D    -19.859 -18.014  -1.899  1.00 64.86           C  
ANISOU 1614  CB  THR B  30D    6273  10530   7840  -1302  -1386    -78       C  
ATOM   1615  OG1 THR B  30D    -21.291 -18.042  -1.924  1.00 60.14           O  
ANISOU 1615  OG1 THR B  30D    6026   9650   7174  -1228  -1251    -33       O  
ATOM   1616  CG2 THR B  30D    -19.347 -17.234  -3.106  1.00 57.02           C  
ANISOU 1616  CG2 THR B  30D    5200   9419   7046  -1443  -1170   -233       C  
ATOM   1617  N   THR B  31     -20.673 -20.643  -3.490  1.00 53.59           N  
ANISOU 1617  N   THR B  31     4887   8723   6752   -626  -1247    332       N  
ATOM   1618  CA  THR B  31     -20.980 -21.409  -4.694  1.00 53.24           C  
ANISOU 1618  CA  THR B  31     4884   8439   6905   -424  -1080    411       C  
ATOM   1619  C   THR B  31     -22.049 -20.663  -5.473  1.00 54.66           C  
ANISOU 1619  C   THR B  31     5345   8341   7083   -526   -870    302       C  
ATOM   1620  O   THR B  31     -23.188 -20.565  -5.022  1.00 51.52           O  
ANISOU 1620  O   THR B  31     5186   7825   6566   -533   -857    319       O  
ATOM   1621  CB  THR B  31     -21.445 -22.816  -4.339  1.00 51.63           C  
ANISOU 1621  CB  THR B  31     4739   8176   6702   -147  -1151    629       C  
ATOM   1622  OG1 THR B  31     -20.738 -23.266  -3.178  1.00 57.13           O  
ANISOU 1622  OG1 THR B  31     5264   9149   7295    -78  -1393    747       O  
ATOM   1623  CG2 THR B  31     -21.190 -23.768  -5.491  1.00 54.11           C  
ANISOU 1623  CG2 THR B  31     4976   8336   7247     64  -1018    703       C  
ATOM   1624  N   LEU B  32     -21.696 -20.173  -6.654  1.00 41.02           N  
ANISOU 1624  N   LEU B  32     3588   6508   5489   -590   -700    204       N  
ATOM   1625  CA  LEU B  32     -22.540 -19.204  -7.353  1.00 42.84           C  
ANISOU 1625  CA  LEU B  32     4072   6512   5695   -712   -521     96       C  
ATOM   1626  C   LEU B  32     -23.578 -19.894  -8.245  1.00 44.39           C  
ANISOU 1626  C   LEU B  32     4454   6464   5946   -531   -420    178       C  
ATOM   1627  O   LEU B  32     -23.626 -19.693  -9.455  1.00 44.90           O  
ANISOU 1627  O   LEU B  32     4589   6380   6089   -527   -266    138       O  
ATOM   1628  CB  LEU B  32     -21.666 -18.247  -8.153  1.00 43.31           C  
ANISOU 1628  CB  LEU B  32     4048   6571   5836   -892   -378    -46       C  
ATOM   1629  CG  LEU B  32     -20.622 -17.550  -7.283  1.00 48.63           C  
ANISOU 1629  CG  LEU B  32     4511   7502   6464  -1111   -479   -159       C  
ATOM   1630  CD1 LEU B  32     -19.641 -16.746  -8.131  1.00 44.99           C  
ANISOU 1630  CD1 LEU B  32     3929   7042   6122  -1296   -309   -300       C  
ATOM   1631  CD2 LEU B  32     -21.307 -16.668  -6.245  1.00 42.34           C  
ANISOU 1631  CD2 LEU B  32     3906   6706   5474  -1284   -529   -242       C  
ATOM   1632  N   MET B  33     -24.450 -20.685  -7.613  1.00 37.20           N  
ANISOU 1632  N   MET B  33     3638   5518   4978   -402   -503    286       N  
ATOM   1633  CA  MET B  33     -25.492 -21.439  -8.300  1.00 36.49           C  
ANISOU 1633  CA  MET B  33     3703   5224   4936   -254   -429    352       C  
ATOM   1634  C   MET B  33     -26.852 -21.072  -7.710  1.00 40.07           C  
ANISOU 1634  C   MET B  33     4360   5584   5281   -291   -432    344       C  
ATOM   1635  O   MET B  33     -27.042 -21.186  -6.495  1.00 36.03           O  
ANISOU 1635  O   MET B  33     3858   5169   4665   -310   -528    384       O  
ATOM   1636  CB  MET B  33     -25.253 -22.943  -8.145  1.00 36.10           C  
ANISOU 1636  CB  MET B  33     3559   5195   4964    -52   -488    494       C  
ATOM   1637  CG  MET B  33     -26.285 -23.852  -8.809  1.00 40.52           C  
ANISOU 1637  CG  MET B  33     4270   5545   5580     74   -407    542       C  
ATOM   1638  SD  MET B  33     -26.361 -23.590 -10.590  1.00 50.96           S  
ANISOU 1638  SD  MET B  33     5670   6706   6988     58   -240    442       S  
ATOM   1639  CE  MET B  33     -24.852 -24.402 -11.114  1.00 48.33           C  
ANISOU 1639  CE  MET B  33     5118   6438   6808    169   -188    476       C  
ATOM   1640  N   GLN B  34     -27.800 -20.682  -8.574  1.00 31.53           N  
ANISOU 1640  N   GLN B  34     3436   4323   4222   -289   -327    299       N  
ATOM   1641  CA  GLN B  34     -29.132 -20.205  -8.198  1.00 33.14           C  
ANISOU 1641  CA  GLN B  34     3805   4426   4361   -313   -302    278       C  
ATOM   1642  C   GLN B  34     -30.215 -21.093  -8.792  1.00 37.34           C  
ANISOU 1642  C   GLN B  34     4406   4824   4956   -185   -279    331       C  
ATOM   1643  O   GLN B  34     -30.006 -21.752  -9.809  1.00 31.25           O  
ANISOU 1643  O   GLN B  34     3613   3998   4264   -108   -251    348       O  
ATOM   1644  CB  GLN B  34     -29.342 -18.749  -8.667  1.00 33.62           C  
ANISOU 1644  CB  GLN B  34     3978   4400   4397   -426   -205    174       C  
ATOM   1645  CG  GLN B  34     -28.667 -17.765  -7.760  1.00 34.61           C  
ANISOU 1645  CG  GLN B  34     4083   4630   4436   -599   -210     90       C  
ATOM   1646  CD  GLN B  34     -27.160 -17.820  -7.796  1.00 35.58           C  
ANISOU 1646  CD  GLN B  34     4024   4913   4583   -675   -251     65       C  
ATOM   1647  OE1 GLN B  34     -26.533 -17.876  -6.737  1.00 40.53           O  
ANISOU 1647  OE1 GLN B  34     4542   5722   5137   -752   -358     55       O  
ATOM   1648  NE2 GLN B  34     -26.558 -17.755  -8.994  1.00 33.56           N  
ANISOU 1648  NE2 GLN B  34     3726   4604   4420   -665   -166     48       N  
ATOM   1649  N   TRP B  35     -31.379 -21.138  -8.133  1.00 27.72           N  
ANISOU 1649  N   TRP B  35     3270   3557   3704   -177   -279    342       N  
ATOM   1650  CA  TRP B  35     -32.540 -21.817  -8.687  1.00 31.43           C  
ANISOU 1650  CA  TRP B  35     3791   3911   4242    -94   -253    360       C  
ATOM   1651  C   TRP B  35     -33.686 -20.817  -8.746  1.00 33.83           C  
ANISOU 1651  C   TRP B  35     4181   4138   4535   -123   -206    300       C  
ATOM   1652  O   TRP B  35     -33.908 -20.077  -7.790  1.00 32.96           O  
ANISOU 1652  O   TRP B  35     4111   4051   4362   -189   -180    271       O  
ATOM   1653  CB  TRP B  35     -32.956 -23.027  -7.811  1.00 33.92           C  
ANISOU 1653  CB  TRP B  35     4095   4231   4564    -44   -273    442       C  
ATOM   1654  CG  TRP B  35     -32.040 -24.236  -7.923  1.00 29.47           C  
ANISOU 1654  CG  TRP B  35     3459   3691   4047     41   -302    527       C  
ATOM   1655  CD1 TRP B  35     -31.074 -24.604  -7.032  1.00 32.55           C  
ANISOU 1655  CD1 TRP B  35     3781   4198   4388     67   -367    612       C  
ATOM   1656  CD2 TRP B  35     -32.024 -25.233  -8.963  1.00 32.72           C  
ANISOU 1656  CD2 TRP B  35     3864   4005   4564    122   -262    537       C  
ATOM   1657  NE1 TRP B  35     -30.458 -25.760  -7.450  1.00 31.83           N  
ANISOU 1657  NE1 TRP B  35     3631   4074   4388    186   -362    689       N  
ATOM   1658  CE2 TRP B  35     -31.027 -26.171  -8.627  1.00 35.32           C  
ANISOU 1658  CE2 TRP B  35     4122   4371   4927    211   -280    634       C  
ATOM   1659  CE3 TRP B  35     -32.761 -25.423 -10.136  1.00 31.20           C  
ANISOU 1659  CE3 TRP B  35     3722   3702   4432    126   -216    469       C  
ATOM   1660  CZ2 TRP B  35     -30.739 -27.290  -9.428  1.00 37.28           C  
ANISOU 1660  CZ2 TRP B  35     4363   4517   5286    307   -218    658       C  
ATOM   1661  CZ3 TRP B  35     -32.477 -26.526 -10.932  1.00 32.29           C  
ANISOU 1661  CZ3 TRP B  35     3861   3758   4650    191   -169    475       C  
ATOM   1662  CH2 TRP B  35     -31.473 -27.446 -10.573  1.00 40.70           C  
ANISOU 1662  CH2 TRP B  35     4869   4829   5765    281   -152    565       C  
ATOM   1663  N   TYR B  36     -34.407 -20.788  -9.860  1.00 29.39           N  
ANISOU 1663  N   TYR B  36     3650   3490   4029    -67   -194    281       N  
ATOM   1664  CA  TYR B  36     -35.549 -19.901 -10.036  1.00 31.09           C  
ANISOU 1664  CA  TYR B  36     3920   3635   4258    -49   -165    246       C  
ATOM   1665  C   TYR B  36     -36.793 -20.702 -10.385  1.00 33.62           C  
ANISOU 1665  C   TYR B  36     4198   3920   4655     14   -192    249       C  
ATOM   1666  O   TYR B  36     -36.717 -21.771 -10.989  1.00 29.79           O  
ANISOU 1666  O   TYR B  36     3682   3433   4203     36   -227    260       O  
ATOM   1667  CB  TYR B  36     -35.306 -18.831 -11.137  1.00 34.96           C  
ANISOU 1667  CB  TYR B  36     4491   4068   4726    -36   -142    225       C  
ATOM   1668  CG  TYR B  36     -34.168 -17.886 -10.826  1.00 32.54           C  
ANISOU 1668  CG  TYR B  36     4227   3777   4360   -133    -84    196       C  
ATOM   1669  CD1 TYR B  36     -32.858 -18.224 -11.152  1.00 36.04           C  
ANISOU 1669  CD1 TYR B  36     4622   4282   4789   -181    -88    196       C  
ATOM   1670  CD2 TYR B  36     -34.401 -16.660 -10.196  1.00 30.48           C  
ANISOU 1670  CD2 TYR B  36     4046   3464   4071   -187     -7    153       C  
ATOM   1671  CE1 TYR B  36     -31.806 -17.359 -10.869  1.00 35.42           C  
ANISOU 1671  CE1 TYR B  36     4551   4237   4671   -299    -34    149       C  
ATOM   1672  CE2 TYR B  36     -33.356 -15.793  -9.902  1.00 36.18           C  
ANISOU 1672  CE2 TYR B  36     4810   4197   4739   -315     57     99       C  
ATOM   1673  CZ  TYR B  36     -32.058 -16.155 -10.248  1.00 40.43           C  
ANISOU 1673  CZ  TYR B  36     5275   4820   5265   -379     35     95       C  
ATOM   1674  OH  TYR B  36     -30.992 -15.337  -9.964  1.00 40.72           O  
ANISOU 1674  OH  TYR B  36     5316   4891   5264   -532     96     24       O  
ATOM   1675  N   GLN B  37     -37.944 -20.169  -9.998  1.00 36.22           N  
ANISOU 1675  N   GLN B  37     4520   4218   5023     35   -162    227       N  
ATOM   1676  CA  GLN B  37     -39.235 -20.729 -10.360  1.00 34.30           C  
ANISOU 1676  CA  GLN B  37     4200   3961   4872     81   -190    211       C  
ATOM   1677  C   GLN B  37     -39.928 -19.756 -11.301  1.00 34.71           C  
ANISOU 1677  C   GLN B  37     4258   3984   4945    168   -229    201       C  
ATOM   1678  O   GLN B  37     -39.868 -18.541 -11.090  1.00 37.76           O  
ANISOU 1678  O   GLN B  37     4713   4326   5310    195   -174    207       O  
ATOM   1679  CB  GLN B  37     -40.094 -20.928  -9.109  1.00 32.80           C  
ANISOU 1679  CB  GLN B  37     3962   3769   4733     50   -108    198       C  
ATOM   1680  CG  GLN B  37     -41.499 -21.427  -9.373  1.00 34.33           C  
ANISOU 1680  CG  GLN B  37     4036   3959   5050     75   -115    162       C  
ATOM   1681  CD  GLN B  37     -42.325 -21.406  -8.103  1.00 38.96           C  
ANISOU 1681  CD  GLN B  37     4584   4531   5689     37     12    142       C  
ATOM   1682  OE1 GLN B  37     -42.683 -20.332  -7.626  1.00 35.86           O  
ANISOU 1682  OE1 GLN B  37     4208   4114   5304     68     86    122       O  
ATOM   1683  NE2 GLN B  37     -42.622 -22.577  -7.544  1.00 38.16           N  
ANISOU 1683  NE2 GLN B  37     4452   4424   5623    -33     66    144       N  
ATOM   1684  N   GLN B  38     -40.595 -20.268 -12.335  1.00 31.76           N  
ANISOU 1684  N   GLN B  38     3826   3634   4607    213   -324    189       N  
ATOM   1685  CA  GLN B  38     -41.317 -19.368 -13.225  1.00 32.46           C  
ANISOU 1685  CA  GLN B  38     3916   3717   4700    322   -394    204       C  
ATOM   1686  C   GLN B  38     -42.692 -19.917 -13.556  1.00 36.40           C  
ANISOU 1686  C   GLN B  38     4252   4280   5299    358   -483    167       C  
ATOM   1687  O   GLN B  38     -42.806 -21.001 -14.133  1.00 35.88           O  
ANISOU 1687  O   GLN B  38     4140   4263   5231    300   -558    123       O  
ATOM   1688  CB  GLN B  38     -40.554 -19.119 -14.518  1.00 33.01           C  
ANISOU 1688  CB  GLN B  38     4111   3779   4651    348   -458    234       C  
ATOM   1689  CG  GLN B  38     -41.267 -18.095 -15.371  1.00 35.89           C  
ANISOU 1689  CG  GLN B  38     4513   4131   4993    484   -531    285       C  
ATOM   1690  CD  GLN B  38     -40.548 -17.843 -16.671  1.00 44.21           C  
ANISOU 1690  CD  GLN B  38     5729   5171   5900    504   -579    325       C  
ATOM   1691  OE1 GLN B  38     -39.613 -18.558 -17.008  1.00 44.38           O  
ANISOU 1691  OE1 GLN B  38     5804   5202   5856    412   -557    294       O  
ATOM   1692  NE2 GLN B  38     -40.974 -16.816 -17.403  1.00 45.09           N  
ANISOU 1692  NE2 GLN B  38     5928   5249   5956    636   -628    402       N  
ATOM   1693  N   LYS B  39     -43.759 -19.127 -13.211  1.00 37.92           N  
ANISOU 1693  N   LYS B  39     4348   4470   5591    454   -467    175       N  
ATOM   1694  CA  LYS B  39     -45.137 -19.391 -13.584  1.00 39.51           C  
ANISOU 1694  CA  LYS B  39     4349   4756   5908    511   -565    141       C  
ATOM   1695  C   LYS B  39     -45.490 -18.631 -14.855  1.00 44.35           C  
ANISOU 1695  C   LYS B  39     4976   5411   6465    663   -727    201       C  
ATOM   1696  O   LYS B  39     -44.926 -17.562 -15.115  1.00 41.58           O  
ANISOU 1696  O   LYS B  39     4792   4977   6031    756   -696    282       O  
ATOM   1697  CB  LYS B  39     -46.092 -18.972 -12.459  1.00 46.04           C  
ANISOU 1697  CB  LYS B  39     5038   5561   6894    547   -437    119       C  
ATOM   1698  CG  LYS B  39     -45.668 -19.513 -11.114  1.00 48.87           C  
ANISOU 1698  CG  LYS B  39     5442   5868   7260    408   -261     84       C  
ATOM   1699  CD  LYS B  39     -46.256 -20.862 -10.866  1.00 46.15           C  
ANISOU 1699  CD  LYS B  39     4958   5574   7000    287   -253     16       C  
ATOM   1700  CE  LYS B  39     -46.187 -21.244  -9.393  1.00 52.62           C  
ANISOU 1700  CE  LYS B  39     5814   6338   7841    182    -56      1       C  
ATOM   1701  NZ  LYS B  39     -47.137 -20.525  -8.512  1.00 50.84           N  
ANISOU 1701  NZ  LYS B  39     5494   6090   7733    228     93    -27       N  
ATOM   1702  N   PRO B  40     -46.420 -19.163 -15.649  1.00 39.28           N  
ANISOU 1702  N   PRO B  40     4170   4898   5857    684   -899    164       N  
ATOM   1703  CA  PRO B  40     -46.806 -18.499 -16.902  1.00 44.93           C  
ANISOU 1703  CA  PRO B  40     4903   5684   6486    841  -1092    237       C  
ATOM   1704  C   PRO B  40     -47.216 -17.046 -16.701  1.00 50.52           C  
ANISOU 1704  C   PRO B  40     5623   6317   7255   1058  -1048    349       C  
ATOM   1705  O   PRO B  40     -48.071 -16.729 -15.873  1.00 46.65           O  
ANISOU 1705  O   PRO B  40     4956   5819   6951   1125   -966    333       O  
ATOM   1706  CB  PRO B  40     -47.981 -19.350 -17.393  1.00 45.13           C  
ANISOU 1706  CB  PRO B  40     4669   5890   6590    804  -1273    148       C  
ATOM   1707  CG  PRO B  40     -47.684 -20.706 -16.840  1.00 47.68           C  
ANISOU 1707  CG  PRO B  40     4963   6198   6954    574  -1172     23       C  
ATOM   1708  CD  PRO B  40     -47.141 -20.435 -15.464  1.00 45.42           C  
ANISOU 1708  CD  PRO B  40     4750   5767   6740    546   -930     48       C  
ATOM   1709  N   GLY B  41     -46.603 -16.160 -17.487  1.00 46.43           N  
ANISOU 1709  N   GLY B  41     5331   5726   6582   1168  -1080    462       N  
ATOM   1710  CA  GLY B  41     -46.910 -14.743 -17.456  1.00 45.53           C  
ANISOU 1710  CA  GLY B  41     5286   5502   6510   1389  -1027    586       C  
ATOM   1711  C   GLY B  41     -46.398 -13.997 -16.247  1.00 46.76           C  
ANISOU 1711  C   GLY B  41     5552   5469   6746   1361   -755    578       C  
ATOM   1712  O   GLY B  41     -46.690 -12.802 -16.110  1.00 49.28           O  
ANISOU 1712  O   GLY B  41     5939   5660   7126   1538   -665    665       O  
ATOM   1713  N  AGLN B  42     -45.648 -14.653 -15.363  0.47 44.32           N  
ANISOU 1713  N  AGLN B  42     5272   5135   6432   1149   -622    477       N  
ATOM   1714  N  BGLN B  42     -45.638 -14.649 -15.376  0.53 44.30           N  
ANISOU 1714  N  BGLN B  42     5272   5132   6427   1149   -622    478       N  
ATOM   1715  CA AGLN B  42     -45.160 -14.055 -14.133  0.47 45.09           C  
ANISOU 1715  CA AGLN B  42     5465   5090   6576   1084   -385    443       C  
ATOM   1716  CA BGLN B  42     -45.164 -14.005 -14.169  0.53 45.13           C  
ANISOU 1716  CA BGLN B  42     5476   5091   6580   1092   -386    448       C  
ATOM   1717  C  AGLN B  42     -43.647 -13.874 -14.194  0.47 45.56           C  
ANISOU 1717  C  AGLN B  42     5768   5067   6475    948   -303    444       C  
ATOM   1718  C  BGLN B  42     -43.648 -13.863 -14.204  0.53 45.52           C  
ANISOU 1718  C  BGLN B  42     5765   5062   6470    949   -303    445       C  
ATOM   1719  O  AGLN B  42     -42.959 -14.603 -14.915  0.47 43.69           O  
ANISOU 1719  O  AGLN B  42     5577   4900   6122    861   -400    439       O  
ATOM   1720  O  BGLN B  42     -42.962 -14.613 -14.904  0.53 43.61           O  
ANISOU 1720  O  BGLN B  42     5566   4892   6114    860   -400    438       O  
ATOM   1721  CB AGLN B  42     -45.513 -14.922 -12.915  0.47 45.24           C  
ANISOU 1721  CB AGLN B  42     5319   5164   6705    948   -296    333       C  
ATOM   1722  CB BGLN B  42     -45.553 -14.794 -12.913  0.53 45.23           C  
ANISOU 1722  CB BGLN B  42     5324   5153   6710    964   -288    339       C  
ATOM   1723  CG AGLN B  42     -47.020 -15.061 -12.634  0.47 48.27           C  
ANISOU 1723  CG AGLN B  42     5434   5620   7287   1052   -314    306       C  
ATOM   1724  CG BGLN B  42     -47.002 -14.604 -12.466  0.53 47.85           C  
ANISOU 1724  CG BGLN B  42     5423   5513   7245   1091   -257    321       C  
ATOM   1725  CD AGLN B  42     -47.322 -15.755 -11.307  0.47 47.75           C  
ANISOU 1725  CD AGLN B  42     5258   5567   7318    906   -158    204       C  
ATOM   1726  CD BGLN B  42     -47.344 -13.159 -12.152  0.53 47.05           C  
ANISOU 1726  CD BGLN B  42     5397   5254   7225   1268   -108    375       C  
ATOM   1727  OE1AGLN B  42     -46.473 -15.818 -10.414  0.47 46.25           O  
ANISOU 1727  OE1AGLN B  42     5218   5310   7045    767    -18    170       O  
ATOM   1728  OE1BGLN B  42     -46.676 -12.506 -11.353  0.53 50.29           O  
ANISOU 1728  OE1BGLN B  42     5994   5520   7594   1198     91    347       O  
ATOM   1729  NE2AGLN B  42     -48.530 -16.296 -11.182  0.47 42.62           N  
ANISOU 1729  NE2AGLN B  42     4344   5015   6836    929   -185    154       N  
ATOM   1730  NE2BGLN B  42     -48.415 -12.665 -12.758  0.53 45.47           N  
ANISOU 1730  NE2BGLN B  42     5046   5083   7148   1501   -202    448       N  
ATOM   1731  N   PRO B  43     -43.097 -12.897 -13.481  1.00 38.47           N  
ANISOU 1731  N   PRO B  43     5022   4020   5572    917   -113    436       N  
ATOM   1732  CA  PRO B  43     -41.646 -12.805 -13.357  1.00 38.61           C  
ANISOU 1732  CA  PRO B  43     5215   3992   5463    747    -29    406       C  
ATOM   1733  C   PRO B  43     -41.082 -14.063 -12.723  1.00 39.05           C  
ANISOU 1733  C   PRO B  43     5171   4171   5495    569    -58    326       C  
ATOM   1734  O   PRO B  43     -41.655 -14.593 -11.757  1.00 39.58           O  
ANISOU 1734  O   PRO B  43     5109   4288   5642    532    -28    273       O  
ATOM   1735  CB  PRO B  43     -41.446 -11.582 -12.439  1.00 43.25           C  
ANISOU 1735  CB  PRO B  43     5938   4413   6083    723    188    373       C  
ATOM   1736  CG  PRO B  43     -42.845 -11.137 -12.054  1.00 54.42           C  
ANISOU 1736  CG  PRO B  43     7244   5780   7654    900    231    390       C  
ATOM   1737  CD  PRO B  43     -43.736 -11.625 -13.122  1.00 51.03           C  
ANISOU 1737  CD  PRO B  43     6667   5460   7263   1069     23    473       C  
ATOM   1738  N   PRO B  44     -39.984 -14.592 -13.249  1.00 35.27           N  
ANISOU 1738  N   PRO B  44     4752   3738   4912    469   -103    324       N  
ATOM   1739  CA  PRO B  44     -39.231 -15.599 -12.506  1.00 33.85           C  
ANISOU 1739  CA  PRO B  44     4507   3644   4712    318    -98    267       C  
ATOM   1740  C   PRO B  44     -38.995 -15.137 -11.075  1.00 37.36           C  
ANISOU 1740  C   PRO B  44     4971   4060   5163    223     32    212       C  
ATOM   1741  O   PRO B  44     -38.753 -13.957 -10.814  1.00 35.07           O  
ANISOU 1741  O   PRO B  44     4802   3667   4854    206    148    195       O  
ATOM   1742  CB  PRO B  44     -37.920 -15.695 -13.289  1.00 36.96           C  
ANISOU 1742  CB  PRO B  44     4994   4044   5005    248   -105    278       C  
ATOM   1743  CG  PRO B  44     -38.341 -15.406 -14.685  1.00 31.48           C  
ANISOU 1743  CG  PRO B  44     4374   3318   4270    366   -178    340       C  
ATOM   1744  CD  PRO B  44     -39.382 -14.326 -14.570  1.00 30.91           C  
ANISOU 1744  CD  PRO B  44     4333   3157   4255    501   -149    382       C  
ATOM   1745  N   LYS B  45     -39.064 -16.083 -10.148  1.00 33.82           N  
ANISOU 1745  N   LYS B  45     4425   3695   4729    151     23    182       N  
ATOM   1746  CA  LYS B  45     -38.895 -15.828  -8.727  1.00 40.67           C  
ANISOU 1746  CA  LYS B  45     5320   4567   5565     50    127    130       C  
ATOM   1747  C   LYS B  45     -37.670 -16.590  -8.243  1.00 33.71           C  
ANISOU 1747  C   LYS B  45     4428   3791   4591    -73     80    129       C  
ATOM   1748  O   LYS B  45     -37.565 -17.797  -8.471  1.00 33.71           O  
ANISOU 1748  O   LYS B  45     4345   3858   4606    -58     -4    168       O  
ATOM   1749  CB  LYS B  45     -40.155 -16.268  -7.954  1.00 34.90           C  
ANISOU 1749  CB  LYS B  45     4497   3845   4920     86    172    114       C  
ATOM   1750  CG  LYS B  45     -39.997 -16.287  -6.442  1.00 50.10           C  
ANISOU 1750  CG  LYS B  45     6467   5795   6774    -32    276     65       C  
ATOM   1751  CD  LYS B  45     -41.183 -16.968  -5.762  1.00 54.72           C  
ANISOU 1751  CD  LYS B  45     6960   6391   7442    -12    338     56       C  
ATOM   1752  CE  LYS B  45     -41.400 -16.411  -4.353  1.00 64.84           C  
ANISOU 1752  CE  LYS B  45     8334   7643   8660    -97    508    -10       C  
ATOM   1753  NZ  LYS B  45     -42.334 -17.253  -3.561  1.00 67.16           N  
ANISOU 1753  NZ  LYS B  45     8559   7958   9001   -116    592    -14       N  
ATOM   1754  N   LEU B  46     -36.765 -15.896  -7.554  1.00 31.12           N  
ANISOU 1754  N   LEU B  46     4176   3478   4172   -193    136     81       N  
ATOM   1755  CA  LEU B  46     -35.627 -16.562  -6.928  1.00 29.51           C  
ANISOU 1755  CA  LEU B  46     3930   3406   3878   -298     71     86       C  
ATOM   1756  C   LEU B  46     -36.068 -17.487  -5.802  1.00 37.26           C  
ANISOU 1756  C   LEU B  46     4873   4459   4826   -309     56    112       C  
ATOM   1757  O   LEU B  46     -36.786 -17.071  -4.885  1.00 35.07           O  
ANISOU 1757  O   LEU B  46     4654   4150   4522   -343    150     68       O  
ATOM   1758  CB  LEU B  46     -34.647 -15.525  -6.384  1.00 34.89           C  
ANISOU 1758  CB  LEU B  46     4684   4110   4462   -449    125      5       C  
ATOM   1759  CG  LEU B  46     -33.429 -16.046  -5.616  1.00 35.13           C  
ANISOU 1759  CG  LEU B  46     4644   4318   4388   -565     33      2       C  
ATOM   1760  CD1 LEU B  46     -32.429 -16.712  -6.549  1.00 38.13           C  
ANISOU 1760  CD1 LEU B  46     4910   4764   4814   -528    -56     56       C  
ATOM   1761  CD2 LEU B  46     -32.780 -14.863  -4.912  1.00 38.30           C  
ANISOU 1761  CD2 LEU B  46     5125   4739   4687   -749    100   -118       C  
ATOM   1762  N   LEU B  47     -35.602 -18.739  -5.848  1.00 34.76           N  
ANISOU 1762  N   LEU B  47     4476   4223   4507   -282    -38    186       N  
ATOM   1763  CA  LEU B  47     -35.871 -19.706  -4.787  1.00 34.80           C  
ANISOU 1763  CA  LEU B  47     4475   4284   4464   -290    -46    238       C  
ATOM   1764  C   LEU B  47     -34.651 -19.931  -3.914  1.00 34.49           C  
ANISOU 1764  C   LEU B  47     4433   4389   4283   -363   -126    272       C  
ATOM   1765  O   LEU B  47     -34.726 -19.820  -2.692  1.00 37.51           O  
ANISOU 1765  O   LEU B  47     4885   4832   4534   -438   -106    266       O  
ATOM   1766  CB  LEU B  47     -36.303 -21.049  -5.389  1.00 34.08           C  
ANISOU 1766  CB  LEU B  47     4316   4156   4477   -195    -79    311       C  
ATOM   1767  CG  LEU B  47     -37.577 -21.047  -6.214  1.00 42.01           C  
ANISOU 1767  CG  LEU B  47     5288   5061   5615   -133    -38    276       C  
ATOM   1768  CD1 LEU B  47     -37.692 -22.407  -6.928  1.00 41.52           C  
ANISOU 1768  CD1 LEU B  47     5165   4973   5635    -80    -82    321       C  
ATOM   1769  CD2 LEU B  47     -38.789 -20.742  -5.323  1.00 37.75           C  
ANISOU 1769  CD2 LEU B  47     4767   4482   5094   -156     75    238       C  
ATOM   1770  N   ILE B  48     -33.508 -20.216  -4.543  1.00 32.36           N  
ANISOU 1770  N   ILE B  48     4077   4186   4031   -343   -217    305       N  
ATOM   1771  CA  ILE B  48     -32.292 -20.633  -3.865  1.00 32.51           C  
ANISOU 1771  CA  ILE B  48     4032   4370   3952   -372   -328    360       C  
ATOM   1772  C   ILE B  48     -31.135 -19.855  -4.474  1.00 33.11           C  
ANISOU 1772  C   ILE B  48     4028   4511   4039   -442   -360    291       C  
ATOM   1773  O   ILE B  48     -31.023 -19.753  -5.700  1.00 33.40           O  
ANISOU 1773  O   ILE B  48     4034   4465   4191   -397   -321    273       O  
ATOM   1774  CB  ILE B  48     -32.044 -22.152  -4.030  1.00 38.63           C  
ANISOU 1774  CB  ILE B  48     4737   5152   4788   -236   -388    497       C  
ATOM   1775  CG1 ILE B  48     -33.253 -22.988  -3.567  1.00 36.23           C  
ANISOU 1775  CG1 ILE B  48     4520   4746   4498   -185   -318    558       C  
ATOM   1776  CG2 ILE B  48     -30.759 -22.571  -3.322  1.00 38.94           C  
ANISOU 1776  CG2 ILE B  48     4685   5376   4734   -226   -521    579       C  
ATOM   1777  CD1 ILE B  48     -33.401 -23.107  -2.059  1.00 38.66           C  
ANISOU 1777  CD1 ILE B  48     4922   5135   4633   -237   -325    610       C  
ATOM   1778  N   TYR B  49     -30.247 -19.353  -3.632  1.00 33.39           N  
ANISOU 1778  N   TYR B  49     4030   4707   3949   -566   -429    249       N  
ATOM   1779  CA  TYR B  49     -29.019 -18.750  -4.118  1.00 39.02           C  
ANISOU 1779  CA  TYR B  49     4629   5511   4687   -655   -460    180       C  
ATOM   1780  C   TYR B  49     -27.855 -19.334  -3.344  1.00 39.15           C  
ANISOU 1780  C   TYR B  49     4486   5767   4624   -665   -628    241       C  
ATOM   1781  O   TYR B  49     -28.036 -19.972  -2.303  1.00 37.97           O  
ANISOU 1781  O   TYR B  49     4364   5708   4354   -625   -718    330       O  
ATOM   1782  CB  TYR B  49     -29.056 -17.208  -4.033  1.00 32.41           C  
ANISOU 1782  CB  TYR B  49     3895   4623   3797   -843   -356     18       C  
ATOM   1783  CG  TYR B  49     -29.193 -16.652  -2.634  1.00 38.53           C  
ANISOU 1783  CG  TYR B  49     4764   5489   4388   -994   -373    -58       C  
ATOM   1784  CD1 TYR B  49     -30.449 -16.474  -2.066  1.00 39.10           C  
ANISOU 1784  CD1 TYR B  49     5007   5439   4408   -977   -274    -71       C  
ATOM   1785  CD2 TYR B  49     -28.082 -16.281  -1.896  1.00 42.18           C  
ANISOU 1785  CD2 TYR B  49     5139   6164   4722  -1165   -479   -133       C  
ATOM   1786  CE1 TYR B  49     -30.588 -15.960  -0.790  1.00 42.52           C  
ANISOU 1786  CE1 TYR B  49     5555   5945   4656  -1125   -258   -155       C  
ATOM   1787  CE2 TYR B  49     -28.214 -15.760  -0.620  1.00 40.95           C  
ANISOU 1787  CE2 TYR B  49     5096   6099   4362  -1326   -494   -222       C  
ATOM   1788  CZ  TYR B  49     -29.468 -15.603  -0.078  1.00 47.32           C  
ANISOU 1788  CZ  TYR B  49     6106   6764   5109  -1305   -372   -233       C  
ATOM   1789  OH  TYR B  49     -29.604 -15.085   1.190  1.00 47.58           O  
ANISOU 1789  OH  TYR B  49     6278   6877   4922  -1474   -360   -334       O  
ATOM   1790  N   ALA B  50     -26.654 -19.144  -3.899  1.00 39.25           N  
ANISOU 1790  N   ALA B  50     4322   5882   4708   -706   -665    204       N  
ATOM   1791  CA  ALA B  50     -25.432 -19.734  -3.352  1.00 42.93           C  
ANISOU 1791  CA  ALA B  50     4569   6598   5145   -682   -841    271       C  
ATOM   1792  C   ALA B  50     -25.632 -21.216  -2.994  1.00 37.89           C  
ANISOU 1792  C   ALA B  50     3910   5972   4514   -454   -931    472       C  
ATOM   1793  O   ALA B  50     -25.209 -21.683  -1.934  1.00 39.12           O  
ANISOU 1793  O   ALA B  50     4008   6317   4539   -423  -1093    566       O  
ATOM   1794  CB  ALA B  50     -24.933 -18.927  -2.153  1.00 38.14           C  
ANISOU 1794  CB  ALA B  50     3945   6206   4341   -894   -952    171       C  
ATOM   1795  N   ALA B  51     -26.327 -21.939  -3.885  1.00 35.01           N  
ANISOU 1795  N   ALA B  51     3616   5396   4289   -301   -819    537       N  
ATOM   1796  CA  ALA B  51     -26.534 -23.389  -3.869  1.00 34.17           C  
ANISOU 1796  CA  ALA B  51     3509   5227   4247    -86   -840    710       C  
ATOM   1797  C   ALA B  51     -27.553 -23.871  -2.833  1.00 40.51           C  
ANISOU 1797  C   ALA B  51     4493   5982   4916    -58   -849    799       C  
ATOM   1798  O   ALA B  51     -28.363 -24.756  -3.133  1.00 38.17           O  
ANISOU 1798  O   ALA B  51     4295   5510   4700     56   -761    874       O  
ATOM   1799  CB  ALA B  51     -25.212 -24.127  -3.658  1.00 36.24           C  
ANISOU 1799  CB  ALA B  51     3543   5671   4554     40   -975    826       C  
ATOM   1800  N   SER B  52     -27.530 -23.311  -1.617  1.00 40.08           N  
ANISOU 1800  N   SER B  52     4495   6080   4655   -178   -937    780       N  
ATOM   1801  CA  SER B  52     -28.357 -23.846  -0.534  1.00 38.02           C  
ANISOU 1801  CA  SER B  52     4412   5793   4242   -150   -936    881       C  
ATOM   1802  C   SER B  52     -29.087 -22.801   0.307  1.00 44.02           C  
ANISOU 1802  C   SER B  52     5339   6567   4819   -344   -882    754       C  
ATOM   1803  O   SER B  52     -29.821 -23.176   1.234  1.00 39.62           O  
ANISOU 1803  O   SER B  52     4947   5983   4123   -342   -848    822       O  
ATOM   1804  CB  SER B  52     -27.495 -24.711   0.394  1.00 36.88           C  
ANISOU 1804  CB  SER B  52     4198   5841   3974    -32  -1120   1068       C  
ATOM   1805  OG  SER B  52     -26.425 -23.956   0.932  1.00 43.00           O  
ANISOU 1805  OG  SER B  52     4832   6891   4616   -151  -1296   1003       O  
ATOM   1806  N   LYS B  53     -28.925 -21.519   0.026  1.00 38.73           N  
ANISOU 1806  N   LYS B  53     4652   5917   4147   -512   -843    570       N  
ATOM   1807  CA  LYS B  53     -29.567 -20.477   0.813  1.00 41.78           C  
ANISOU 1807  CA  LYS B  53     5208   6294   4373   -694   -762    434       C  
ATOM   1808  C   LYS B  53     -30.960 -20.210   0.258  1.00 44.59           C  
ANISOU 1808  C   LYS B  53     5692   6393   4857   -670   -553    376       C  
ATOM   1809  O   LYS B  53     -31.129 -20.031  -0.949  1.00 39.59           O  
ANISOU 1809  O   LYS B  53     5000   5627   4416   -615   -484    340       O  
ATOM   1810  CB  LYS B  53     -28.724 -19.200   0.804  1.00 44.60           C  
ANISOU 1810  CB  LYS B  53     5502   6770   4674   -897   -796    256       C  
ATOM   1811  CG  LYS B  53     -27.307 -19.416   1.303  1.00 45.95           C  
ANISOU 1811  CG  LYS B  53     5487   7233   4737   -936  -1025    294       C  
ATOM   1812  CD  LYS B  53     -26.501 -18.123   1.314  1.00 54.26           C  
ANISOU 1812  CD  LYS B  53     6471   8402   5742  -1184  -1039     86       C  
ATOM   1813  CE  LYS B  53     -25.068 -18.371   1.767  1.00 60.15           C  
ANISOU 1813  CE  LYS B  53     6972   9477   6404  -1226  -1289    114       C  
ATOM   1814  NZ  LYS B  53     -24.146 -17.268   1.369  1.00 55.80           N  
ANISOU 1814  NZ  LYS B  53     6279   9016   5906  -1456  -1278    -89       N  
ATOM   1815  N   VAL B  54     -31.954 -20.208   1.136  1.00 35.73           N  
ANISOU 1815  N   VAL B  54     4738   5212   3625   -705   -454    371       N  
ATOM   1816  CA  VAL B  54     -33.339 -19.991   0.736  1.00 41.23           C  
ANISOU 1816  CA  VAL B  54     5521   5692   4454   -674   -260    319       C  
ATOM   1817  C   VAL B  54     -33.663 -18.504   0.815  1.00 42.86           C  
ANISOU 1817  C   VAL B  54     5815   5833   4637   -814   -135    136       C  
ATOM   1818  O   VAL B  54     -33.390 -17.847   1.825  1.00 42.63           O  
ANISOU 1818  O   VAL B  54     5890   5898   4409   -968   -129     47       O  
ATOM   1819  CB  VAL B  54     -34.302 -20.810   1.613  1.00 43.26           C  
ANISOU 1819  CB  VAL B  54     5899   5898   4638   -637   -174    406       C  
ATOM   1820  CG1 VAL B  54     -35.724 -20.607   1.143  1.00 43.59           C  
ANISOU 1820  CG1 VAL B  54     5969   5740   4853   -603     19    342       C  
ATOM   1821  CG2 VAL B  54     -33.931 -22.294   1.556  1.00 42.19           C  
ANISOU 1821  CG2 VAL B  54     5710   5794   4528   -495   -275    599       C  
ATOM   1822  N   GLU B  55     -34.263 -17.979  -0.247  1.00 36.09           N  
ANISOU 1822  N   GLU B  55     4932   4808   3973   -756    -32     80       N  
ATOM   1823  CA  GLU B  55     -34.640 -16.575  -0.306  1.00 35.84           C  
ANISOU 1823  CA  GLU B  55     4996   4664   3958   -846    114    -72       C  
ATOM   1824  C   GLU B  55     -35.874 -16.326   0.556  1.00 41.07           C  
ANISOU 1824  C   GLU B  55     5791   5231   4584   -864    292   -123       C  
ATOM   1825  O   GLU B  55     -36.661 -17.236   0.829  1.00 39.60           O  
ANISOU 1825  O   GLU B  55     5595   5023   4428   -782    323    -39       O  
ATOM   1826  CB  GLU B  55     -34.874 -16.168  -1.767  1.00 40.33           C  
ANISOU 1826  CB  GLU B  55     5502   5087   4733   -743    151    -76       C  
ATOM   1827  CG  GLU B  55     -35.464 -14.763  -1.968  1.00 42.86           C  
ANISOU 1827  CG  GLU B  55     5937   5238   5111   -775    327   -195       C  
ATOM   1828  CD  GLU B  55     -34.465 -13.651  -1.696  1.00 44.27           C  
ANISOU 1828  CD  GLU B  55     6196   5441   5183   -962    357   -322       C  
ATOM   1829  OE1 GLU B  55     -34.203 -12.841  -2.610  1.00 54.83           O  
ANISOU 1829  OE1 GLU B  55     7557   6666   6612   -962    414   -358       O  
ATOM   1830  OE2 GLU B  55     -33.987 -13.541  -0.543  1.00 54.17           O1-
ANISOU 1830  OE2 GLU B  55     7508   6822   6252  -1124    336   -393       O1-
ATOM   1831  N   SER B  56     -36.025 -15.085   1.023  1.00 39.58           N  
ANISOU 1831  N   SER B  56     5734   4973   4333   -984    434   -272       N  
ATOM   1832  CA  SER B  56     -37.197 -14.768   1.838  1.00 43.28           C  
ANISOU 1832  CA  SER B  56     6328   5334   4782   -997    644   -338       C  
ATOM   1833  C   SER B  56     -38.472 -14.980   1.030  1.00 40.90           C  
ANISOU 1833  C   SER B  56     5933   4871   4735   -808    745   -286       C  
ATOM   1834  O   SER B  56     -38.497 -14.818  -0.194  1.00 46.87           O  
ANISOU 1834  O   SER B  56     6588   5556   5664   -694    692   -251       O  
ATOM   1835  CB  SER B  56     -37.129 -13.330   2.358  1.00 51.93           C  
ANISOU 1835  CB  SER B  56     7593   6344   5793  -1150    812   -523       C  
ATOM   1836  OG  SER B  56     -37.237 -12.408   1.290  1.00 57.71           O  
ANISOU 1836  OG  SER B  56     8306   6906   6715  -1080    886   -564       O  
ATOM   1837  N   GLY B  57     -39.527 -15.404   1.720  1.00 42.45           N  
ANISOU 1837  N   GLY B  57     6157   5028   4944   -783    883   -280       N  
ATOM   1838  CA  GLY B  57     -40.801 -15.663   1.082  1.00 47.62           C  
ANISOU 1838  CA  GLY B  57     6685   5564   5843   -624    974   -247       C  
ATOM   1839  C   GLY B  57     -40.881 -16.940   0.272  1.00 58.82           C  
ANISOU 1839  C   GLY B  57     7940   7034   7376   -520    818   -116       C  
ATOM   1840  O   GLY B  57     -41.797 -17.074  -0.549  1.00 57.82           O  
ANISOU 1840  O   GLY B  57     7676   6831   7462   -396    840   -100       O  
ATOM   1841  N   VAL B  58     -39.953 -17.869   0.450  1.00 41.18           N  
ANISOU 1841  N   VAL B  58     5710   4924   5012   -563    660    -25       N  
ATOM   1842  CA  VAL B  58     -39.965 -19.142  -0.263  1.00 34.45           C  
ANISOU 1842  CA  VAL B  58     4734   4094   4262   -474    541     91       C  
ATOM   1843  C   VAL B  58     -40.435 -20.218   0.709  1.00 40.62           C  
ANISOU 1843  C   VAL B  58     5569   4892   4974   -510    618    158       C  
ATOM   1844  O   VAL B  58     -39.923 -20.277   1.833  1.00 39.66           O  
ANISOU 1844  O   VAL B  58     5589   4850   4629   -602    626    179       O  
ATOM   1845  CB  VAL B  58     -38.580 -19.489  -0.829  1.00 39.86           C  
ANISOU 1845  CB  VAL B  58     5383   4877   4885   -465    338    159       C  
ATOM   1846  CG1 VAL B  58     -38.588 -20.893  -1.453  1.00 39.87           C  
ANISOU 1846  CG1 VAL B  58     5289   4875   4984   -377    253    271       C  
ATOM   1847  CG2 VAL B  58     -38.163 -18.428  -1.840  1.00 39.08           C  
ANISOU 1847  CG2 VAL B  58     5250   4740   4858   -443    299     94       C  
ATOM   1848  N   PRO B  59     -41.389 -21.063   0.328  1.00 44.70           N  
ANISOU 1848  N   PRO B  59     5987   5337   5659   -454    679    190       N  
ATOM   1849  CA  PRO B  59     -41.864 -22.116   1.238  1.00 45.23           C  
ANISOU 1849  CA  PRO B  59     6127   5389   5669   -503    791    258       C  
ATOM   1850  C   PRO B  59     -40.747 -23.042   1.704  1.00 40.22           C  
ANISOU 1850  C   PRO B  59     5596   4837   4850   -510    661    400       C  
ATOM   1851  O   PRO B  59     -39.782 -23.302   0.984  1.00 39.86           O  
ANISOU 1851  O   PRO B  59     5488   4842   4816   -447    480    458       O  
ATOM   1852  CB  PRO B  59     -42.887 -22.871   0.382  1.00 43.07           C  
ANISOU 1852  CB  PRO B  59     5688   5029   5648   -450    836    251       C  
ATOM   1853  CG  PRO B  59     -43.425 -21.815  -0.533  1.00 49.62           C  
ANISOU 1853  CG  PRO B  59     6376   5832   6644   -382    822    146       C  
ATOM   1854  CD  PRO B  59     -42.194 -21.009  -0.907  1.00 42.28           C  
ANISOU 1854  CD  PRO B  59     5506   4960   5598   -359    667    150       C  
ATOM   1855  N   ALA B  60     -40.914 -23.581   2.921  1.00 42.42           N  
ANISOU 1855  N   ALA B  60     6034   5123   4960   -575    768    468       N  
ATOM   1856  CA  ALA B  60     -39.913 -24.488   3.473  1.00 42.19           C  
ANISOU 1856  CA  ALA B  60     6116   5173   4740   -553    644    636       C  
ATOM   1857  C   ALA B  60     -39.836 -25.817   2.725  1.00 46.04           C  
ANISOU 1857  C   ALA B  60     6531   5577   5386   -455    597    754       C  
ATOM   1858  O   ALA B  60     -38.941 -26.617   3.013  1.00 50.64           O  
ANISOU 1858  O   ALA B  60     7183   6205   5853   -391    486    912       O  
ATOM   1859  CB  ALA B  60     -40.203 -24.753   4.955  1.00 52.61           C  
ANISOU 1859  CB  ALA B  60     7662   6509   5818   -640    784    696       C  
ATOM   1860  N   ARG B  61     -40.740 -26.067   1.776  1.00 41.10           N  
ANISOU 1860  N   ARG B  61     5766   4832   5017   -439    678    679       N  
ATOM   1861  CA  ARG B  61     -40.703 -27.290   0.980  1.00 40.54           C  
ANISOU 1861  CA  ARG B  61     5637   4666   5101   -375    653    752       C  
ATOM   1862  C   ARG B  61     -39.551 -27.310  -0.007  1.00 39.18           C  
ANISOU 1862  C   ARG B  61     5374   4551   4963   -274    444    782       C  
ATOM   1863  O   ARG B  61     -39.258 -28.371  -0.568  1.00 37.68           O  
ANISOU 1863  O   ARG B  61     5171   4282   4865   -209    422    857       O  
ATOM   1864  CB  ARG B  61     -42.013 -27.460   0.218  1.00 41.99           C  
ANISOU 1864  CB  ARG B  61     5681   4740   5535   -417    778    629       C  
ATOM   1865  CG  ARG B  61     -43.257 -27.297   1.087  1.00 47.29           C  
ANISOU 1865  CG  ARG B  61     6384   5360   6223   -522   1013    565       C  
ATOM   1866  CD  ARG B  61     -44.494 -27.595   0.278  1.00 48.03           C  
ANISOU 1866  CD  ARG B  61     6289   5374   6588   -564   1109    446       C  
ATOM   1867  NE  ARG B  61     -44.588 -26.725  -0.893  1.00 47.57           N  
ANISOU 1867  NE  ARG B  61     6040   5377   6659   -498    960    337       N  
ATOM   1868  CZ  ARG B  61     -45.221 -25.559  -0.920  1.00 57.78           C  
ANISOU 1868  CZ  ARG B  61     7231   6711   8011   -485    995    232       C  
ATOM   1869  NH1 ARG B  61     -45.774 -25.042   0.170  1.00 55.92           N  
ANISOU 1869  NH1 ARG B  61     7061   6466   7718   -540   1183    198       N  
ATOM   1870  NH2 ARG B  61     -45.312 -24.899  -2.071  1.00 54.39           N  
ANISOU 1870  NH2 ARG B  61     6648   6322   7697   -406    854    163       N  
ATOM   1871  N   PHE B  62     -38.905 -26.172  -0.230  1.00 36.86           N  
ANISOU 1871  N   PHE B  62     5027   4373   4605   -270    322    716       N  
ATOM   1872  CA  PHE B  62     -37.821 -26.057  -1.196  1.00 38.07           C  
ANISOU 1872  CA  PHE B  62     5083   4582   4798   -193    155    725       C  
ATOM   1873  C   PHE B  62     -36.488 -26.084  -0.462  1.00 43.41           C  
ANISOU 1873  C   PHE B  62     5809   5401   5284   -164     21    835       C  
ATOM   1874  O   PHE B  62     -36.320 -25.425   0.567  1.00 42.43           O  
ANISOU 1874  O   PHE B  62     5769   5382   4971   -238     10    825       O  
ATOM   1875  CB  PHE B  62     -37.941 -24.755  -1.994  1.00 39.54           C  
ANISOU 1875  CB  PHE B  62     5179   4796   5049   -217    120    582       C  
ATOM   1876  CG  PHE B  62     -39.126 -24.719  -2.903  1.00 39.50           C  
ANISOU 1876  CG  PHE B  62     5087   4688   5233   -211    193    489       C  
ATOM   1877  CD1 PHE B  62     -39.039 -25.173  -4.205  1.00 35.60           C  
ANISOU 1877  CD1 PHE B  62     4506   4151   4869   -155    127    473       C  
ATOM   1878  CD2 PHE B  62     -40.327 -24.215  -2.457  1.00 40.08           C  
ANISOU 1878  CD2 PHE B  62     5157   4721   5349   -262    325    412       C  
ATOM   1879  CE1 PHE B  62     -40.139 -25.140  -5.030  1.00 40.33           C  
ANISOU 1879  CE1 PHE B  62     5015   4691   5617   -157    159    385       C  
ATOM   1880  CE2 PHE B  62     -41.430 -24.174  -3.284  1.00 38.15           C  
ANISOU 1880  CE2 PHE B  62     4791   4416   5289   -246    365    330       C  
ATOM   1881  CZ  PHE B  62     -41.340 -24.642  -4.562  1.00 37.92           C  
ANISOU 1881  CZ  PHE B  62     4674   4367   5367   -197    266    318       C  
ATOM   1882  N   SER B  63     -35.540 -26.845  -0.995  1.00 38.88           N  
ANISOU 1882  N   SER B  63     5174   4839   4761    -56    -80    931       N  
ATOM   1883  CA  SER B  63     -34.185 -26.844  -0.476  1.00 39.76           C  
ANISOU 1883  CA  SER B  63     5263   5114   4729     -5   -239   1033       C  
ATOM   1884  C   SER B  63     -33.224 -27.019  -1.642  1.00 45.08           C  
ANISOU 1884  C   SER B  63     5784   5801   5545     89   -328   1030       C  
ATOM   1885  O   SER B  63     -33.573 -27.623  -2.658  1.00 41.42           O  
ANISOU 1885  O   SER B  63     5289   5192   5256    142   -258   1008       O  
ATOM   1886  CB  SER B  63     -33.994 -27.951   0.573  1.00 42.94           C  
ANISOU 1886  CB  SER B  63     5789   5518   5008     73   -244   1232       C  
ATOM   1887  OG  SER B  63     -34.118 -29.236  -0.004  1.00 47.06           O  
ANISOU 1887  OG  SER B  63     6319   5868   5693    191   -170   1329       O  
ATOM   1888  N   GLY B  64     -32.024 -26.468  -1.498  1.00 38.54           N  
ANISOU 1888  N   GLY B  64     4857   5152   4634     90   -473   1035       N  
ATOM   1889  CA  GLY B  64     -30.973 -26.642  -2.479  1.00 39.57           C  
ANISOU 1889  CA  GLY B  64     4828   5314   4892    177   -540   1039       C  
ATOM   1890  C   GLY B  64     -29.756 -27.304  -1.862  1.00 43.20           C  
ANISOU 1890  C   GLY B  64     5204   5921   5289    301   -681   1204       C  
ATOM   1891  O   GLY B  64     -29.438 -27.085  -0.694  1.00 41.15           O  
ANISOU 1891  O   GLY B  64     4975   5827   4832    267   -791   1268       O  
ATOM   1892  N   SER B  65     -29.063 -28.111  -2.667  1.00 42.71           N  
ANISOU 1892  N   SER B  65     5031   5805   5390    452   -677   1270       N  
ATOM   1893  CA  SER B  65     -27.841 -28.755  -2.214  1.00 41.52           C  
ANISOU 1893  CA  SER B  65     4755   5794   5226    613   -811   1436       C  
ATOM   1894  C   SER B  65     -26.904 -28.958  -3.400  1.00 40.46           C  
ANISOU 1894  C   SER B  65     4429   5645   5299    711   -789   1401       C  
ATOM   1895  O   SER B  65     -27.289 -28.836  -4.562  1.00 40.77           O  
ANISOU 1895  O   SER B  65     4485   5533   5474    668   -656   1274       O  
ATOM   1896  CB  SER B  65     -28.143 -30.081  -1.509  1.00 50.42           C  
ANISOU 1896  CB  SER B  65     6025   6807   6326    776   -779   1652       C  
ATOM   1897  OG  SER B  65     -28.616 -31.049  -2.427  1.00 57.39           O  
ANISOU 1897  OG  SER B  65     6971   7422   7411    866   -602   1660       O  
ATOM   1898  N   GLY B  66     -25.661 -29.278  -3.084  1.00 44.66           N  
ANISOU 1898  N   GLY B  66     4774   6348   5847    847   -922   1519       N  
ATOM   1899  CA  GLY B  66     -24.681 -29.527  -4.113  1.00 52.28           C  
ANISOU 1899  CA  GLY B  66     5535   7309   7020    955   -881   1495       C  
ATOM   1900  C   GLY B  66     -23.391 -28.792  -3.846  1.00 52.01           C  
ANISOU 1900  C   GLY B  66     5225   7576   6961    919  -1050   1466       C  
ATOM   1901  O   GLY B  66     -23.345 -27.874  -3.023  1.00 48.45           O  
ANISOU 1901  O   GLY B  66     4762   7326   6321    754  -1190   1410       O  
ATOM   1902  N   SER B  67     -22.336 -29.195  -4.545  1.00 56.64           N  
ANISOU 1902  N   SER B  67     5583   8193   7743   1061  -1024   1488       N  
ATOM   1903  CA  SER B  67     -21.023 -28.580  -4.443  1.00 56.83           C  
ANISOU 1903  CA  SER B  67     5287   8506   7800   1028  -1162   1446       C  
ATOM   1904  C   SER B  67     -20.308 -28.776  -5.772  1.00 56.94           C  
ANISOU 1904  C   SER B  67     5130   8431   8073   1100   -989   1367       C  
ATOM   1905  O   SER B  67     -20.629 -29.694  -6.530  1.00 48.86           O  
ANISOU 1905  O   SER B  67     4217   7153   7195   1250   -809   1408       O  
ATOM   1906  CB  SER B  67     -20.207 -29.193  -3.299  1.00 53.28           C  
ANISOU 1906  CB  SER B  67     4677   8286   7283   1215  -1393   1653       C  
ATOM   1907  OG  SER B  67     -20.049 -30.587  -3.485  1.00 66.27           O  
ANISOU 1907  OG  SER B  67     6384   9723   9070   1493  -1293   1796       O  
ATOM   1908  N   GLY B  68     -19.346 -27.900  -6.053  1.00 57.82           N  
ANISOU 1908  N   GLY B  68     4985   8747   8239    970  -1023   1237       N  
ATOM   1909  CA  GLY B  68     -18.539 -28.042  -7.250  1.00 52.29           C  
ANISOU 1909  CA  GLY B  68     4099   7988   7779   1029   -844   1159       C  
ATOM   1910  C   GLY B  68     -19.340 -27.943  -8.532  1.00 48.43           C  
ANISOU 1910  C   GLY B  68     3862   7201   7341    945   -583   1025       C  
ATOM   1911  O   GLY B  68     -19.654 -26.837  -8.980  1.00 48.95           O  
ANISOU 1911  O   GLY B  68     4018   7252   7328    705   -521    856       O  
ATOM   1912  N   THR B  69     -19.695 -29.093  -9.123  1.00 49.76           N  
ANISOU 1912  N   THR B  69     4159   7122   7627   1139   -431   1100       N  
ATOM   1913  CA  THR B  69     -20.415 -29.133 -10.393  1.00 46.55           C  
ANISOU 1913  CA  THR B  69     3984   6449   7254   1068   -199    972       C  
ATOM   1914  C   THR B  69     -21.828 -29.702 -10.313  1.00 43.06           C  
ANISOU 1914  C   THR B  69     3863   5781   6718   1077   -168   1008       C  
ATOM   1915  O   THR B  69     -22.619 -29.454 -11.229  1.00 47.46           O  
ANISOU 1915  O   THR B  69     4620   6172   7240    959    -40    880       O  
ATOM   1916  CB  THR B  69     -19.636 -29.963 -11.429  1.00 49.96           C  
ANISOU 1916  CB  THR B  69     4309   6757   7915   1237     14    962       C  
ATOM   1917  OG1 THR B  69     -19.551 -31.321 -10.985  1.00 51.78           O  
ANISOU 1917  OG1 THR B  69     4534   6888   8253   1511     14   1144       O  
ATOM   1918  CG2 THR B  69     -18.227 -29.418 -11.621  1.00 49.55           C  
ANISOU 1918  CG2 THR B  69     3909   6925   7994   1220     25    907       C  
ATOM   1919  N   ASP B  70     -22.168 -30.458  -9.265  1.00 44.77           N  
ANISOU 1919  N   ASP B  70     4132   5990   6888   1208   -279   1177       N  
ATOM   1920  CA  ASP B  70     -23.446 -31.165  -9.175  1.00 43.06           C  
ANISOU 1920  CA  ASP B  70     4197   5544   6619   1220   -214   1215       C  
ATOM   1921  C   ASP B  70     -24.348 -30.468  -8.163  1.00 48.24           C  
ANISOU 1921  C   ASP B  70     4974   6289   7065   1069   -360   1222       C  
ATOM   1922  O   ASP B  70     -23.975 -30.320  -6.995  1.00 41.27           O  
ANISOU 1922  O   ASP B  70     4006   5595   6081   1100   -532   1336       O  
ATOM   1923  CB  ASP B  70     -23.251 -32.628  -8.764  1.00 46.01           C  
ANISOU 1923  CB  ASP B  70     4594   5783   7103   1480   -170   1409       C  
ATOM   1924  CG  ASP B  70     -22.393 -33.418  -9.747  1.00 57.39           C  
ANISOU 1924  CG  ASP B  70     5933   7098   8776   1656     14   1402       C  
ATOM   1925  OD1 ASP B  70     -22.051 -32.887 -10.821  1.00 61.21           O  
ANISOU 1925  OD1 ASP B  70     6355   7582   9318   1557    126   1233       O  
ATOM   1926  OD2 ASP B  70     -22.051 -34.575  -9.426  1.00 64.73           O1-
ANISOU 1926  OD2 ASP B  70     6856   7914   9825   1900     64   1571       O1-
ATOM   1927  N   PHE B  71     -25.537 -30.071  -8.601  1.00 39.22           N  
ANISOU 1927  N   PHE B  71     4029   5017   5854    912   -290   1100       N  
ATOM   1928  CA  PHE B  71     -26.488 -29.383  -7.735  1.00 41.24           C  
ANISOU 1928  CA  PHE B  71     4403   5329   5937    770   -382   1085       C  
ATOM   1929  C   PHE B  71     -27.863 -29.997  -7.914  1.00 42.01           C  
ANISOU 1929  C   PHE B  71     4716   5207   6038    744   -276   1069       C  
ATOM   1930  O   PHE B  71     -28.166 -30.578  -8.958  1.00 42.35           O  
ANISOU 1930  O   PHE B  71     4826   5075   6189    764   -144   1002       O  
ATOM   1931  CB  PHE B  71     -26.512 -27.874  -8.050  1.00 35.95           C  
ANISOU 1931  CB  PHE B  71     3704   4771   5186    572   -413    925       C  
ATOM   1932  CG  PHE B  71     -25.177 -27.231  -7.849  1.00 41.72           C  
ANISOU 1932  CG  PHE B  71     4211   5721   5919    551   -502    914       C  
ATOM   1933  CD1 PHE B  71     -24.791 -26.786  -6.597  1.00 39.97           C  
ANISOU 1933  CD1 PHE B  71     3908   5712   5566    505   -670    968       C  
ATOM   1934  CD2 PHE B  71     -24.264 -27.161  -8.898  1.00 41.08           C  
ANISOU 1934  CD2 PHE B  71     3994   5642   5974    574   -412    847       C  
ATOM   1935  CE1 PHE B  71     -23.548 -26.240  -6.401  1.00 39.67           C  
ANISOU 1935  CE1 PHE B  71     3634   5900   5538    466   -766    942       C  
ATOM   1936  CE2 PHE B  71     -23.015 -26.617  -8.706  1.00 40.74           C  
ANISOU 1936  CE2 PHE B  71     3709   5810   5960    541   -481    827       C  
ATOM   1937  CZ  PHE B  71     -22.654 -26.160  -7.465  1.00 43.89           C  
ANISOU 1937  CZ  PHE B  71     4005   6436   6238    484   -668    870       C  
ATOM   1938  N   SER B  72     -28.698 -29.882  -6.883  1.00 37.63           N  
ANISOU 1938  N   SER B  72     4269   4669   5360    683   -326   1116       N  
ATOM   1939  CA  SER B  72     -30.057 -30.383  -6.996  1.00 38.52           C  
ANISOU 1939  CA  SER B  72     4554   4594   5488    629   -220   1082       C  
ATOM   1940  C   SER B  72     -31.008 -29.464  -6.243  1.00 45.18           C  
ANISOU 1940  C   SER B  72     5467   5506   6194    480   -262   1029       C  
ATOM   1941  O   SER B  72     -30.646 -28.869  -5.226  1.00 39.16           O  
ANISOU 1941  O   SER B  72     4678   4905   5296    452   -364   1079       O  
ATOM   1942  CB  SER B  72     -30.172 -31.832  -6.490  1.00 48.06           C  
ANISOU 1942  CB  SER B  72     5860   5649   6753    764   -142   1240       C  
ATOM   1943  OG  SER B  72     -29.914 -31.910  -5.102  1.00 52.56           O  
ANISOU 1943  OG  SER B  72     6448   6332   7191    820   -240   1405       O  
ATOM   1944  N   LEU B  73     -32.216 -29.331  -6.783  1.00 39.58           N  
ANISOU 1944  N   LEU B  73     4836   4681   5521    384   -180    915       N  
ATOM   1945  CA  LEU B  73     -33.323 -28.654  -6.123  1.00 38.56           C  
ANISOU 1945  CA  LEU B  73     4772   4570   5307    266   -172    864       C  
ATOM   1946  C   LEU B  73     -34.294 -29.733  -5.663  1.00 38.07           C  
ANISOU 1946  C   LEU B  73     4819   4360   5287    264    -61    918       C  
ATOM   1947  O   LEU B  73     -34.611 -30.653  -6.425  1.00 37.07           O  
ANISOU 1947  O   LEU B  73     4719   4081   5284    285     26    892       O  
ATOM   1948  CB  LEU B  73     -34.018 -27.680  -7.073  1.00 31.92           C  
ANISOU 1948  CB  LEU B  73     3910   3720   4499    175   -163    704       C  
ATOM   1949  CG  LEU B  73     -35.255 -26.919  -6.564  1.00 35.77           C  
ANISOU 1949  CG  LEU B  73     4436   4209   4944     78   -133    636       C  
ATOM   1950  CD1 LEU B  73     -34.838 -25.937  -5.465  1.00 34.31           C  
ANISOU 1950  CD1 LEU B  73     4265   4157   4616     30   -181    655       C  
ATOM   1951  CD2 LEU B  73     -35.966 -26.188  -7.673  1.00 35.01           C  
ANISOU 1951  CD2 LEU B  73     4311   4083   4907     40   -133    510       C  
ATOM   1952  N   ASN B  74     -34.731 -29.658  -4.408  1.00 40.19           N  
ANISOU 1952  N   ASN B  74     5165   4662   5443    225    -44    986       N  
ATOM   1953  CA  ASN B  74     -35.638 -30.657  -3.858  1.00 44.55           C  
ANISOU 1953  CA  ASN B  74     5837   5065   6025    204     92   1046       C  
ATOM   1954  C   ASN B  74     -36.918 -29.977  -3.400  1.00 43.29           C  
ANISOU 1954  C   ASN B  74     5701   4911   5836     66    167    945       C  
ATOM   1955  O   ASN B  74     -36.868 -28.966  -2.698  1.00 39.69           O  
ANISOU 1955  O   ASN B  74     5248   4584   5249     20    118    926       O  
ATOM   1956  CB  ASN B  74     -35.000 -31.417  -2.690  1.00 46.58           C  
ANISOU 1956  CB  ASN B  74     6199   5330   6169    304     85   1256       C  
ATOM   1957  CG  ASN B  74     -34.158 -32.595  -3.150  1.00 57.06           C  
ANISOU 1957  CG  ASN B  74     7531   6547   7601    466    100   1376       C  
ATOM   1958  OD1 ASN B  74     -34.678 -33.685  -3.405  1.00 66.33           O  
ANISOU 1958  OD1 ASN B  74     8802   7508   8893    478    253   1398       O  
ATOM   1959  ND2 ASN B  74     -32.852 -32.378  -3.269  1.00 63.95           N  
ANISOU 1959  ND2 ASN B  74     8293   7556   8449    588    -41   1442       N  
ATOM   1960  N   ILE B  75     -38.054 -30.518  -3.824  1.00 38.19           N  
ANISOU 1960  N   ILE B  75     5060   4128   5324     -7    293    864       N  
ATOM   1961  CA  ILE B  75     -39.364 -30.029  -3.418  1.00 39.26           C  
ANISOU 1961  CA  ILE B  75     5183   4257   5478   -127    392    767       C  
ATOM   1962  C   ILE B  75     -40.117 -31.175  -2.763  1.00 37.73           C  
ANISOU 1962  C   ILE B  75     5098   3910   5326   -186    577    825       C  
ATOM   1963  O   ILE B  75     -40.371 -32.209  -3.393  1.00 37.25           O  
ANISOU 1963  O   ILE B  75     5046   3704   5401   -202    654    806       O  
ATOM   1964  CB  ILE B  75     -40.160 -29.422  -4.586  1.00 38.09           C  
ANISOU 1964  CB  ILE B  75     4888   4121   5464   -178    360    592       C  
ATOM   1965  CG1 ILE B  75     -39.226 -28.689  -5.560  1.00 40.65           C  
ANISOU 1965  CG1 ILE B  75     5146   4534   5765   -105    202    560       C  
ATOM   1966  CG2 ILE B  75     -41.311 -28.555  -4.086  1.00 44.65           C  
ANISOU 1966  CG2 ILE B  75     5664   4993   6309   -258    433    502       C  
ATOM   1967  CD1 ILE B  75     -39.905 -28.249  -6.823  1.00 42.46           C  
ANISOU 1967  CD1 ILE B  75     5267   4768   6097   -130    154    420       C  
ATOM   1968  N   HIS B  76     -40.471 -30.989  -1.495  1.00 37.65           N  
ANISOU 1968  N   HIS B  76     5191   3921   5192   -234    671    888       N  
ATOM   1969  CA  HIS B  76     -41.143 -32.043  -0.758  1.00 38.27           C  
ANISOU 1969  CA  HIS B  76     5409   3845   5287   -298    878    961       C  
ATOM   1970  C   HIS B  76     -41.925 -31.445   0.402  1.00 40.99           C  
ANISOU 1970  C   HIS B  76     5818   4233   5522   -398   1009    943       C  
ATOM   1971  O   HIS B  76     -41.358 -30.696   1.208  1.00 40.85           O  
ANISOU 1971  O   HIS B  76     5875   4349   5298   -368    932   1001       O  
ATOM   1972  CB  HIS B  76     -40.133 -33.063  -0.236  1.00 42.07           C  
ANISOU 1972  CB  HIS B  76     6067   4252   5664   -177    870   1183       C  
ATOM   1973  CG  HIS B  76     -40.744 -34.180   0.550  1.00 39.16           C  
ANISOU 1973  CG  HIS B  76     5892   3693   5295   -233   1104   1290       C  
ATOM   1974  ND1 HIS B  76     -41.637 -35.078   0.005  1.00 47.23           N  
ANISOU 1974  ND1 HIS B  76     6908   4513   6524   -340   1292   1203       N  
ATOM   1975  CD2 HIS B  76     -40.531 -34.591   1.820  1.00 35.74           C  
ANISOU 1975  CD2 HIS B  76     5682   3230   4666   -200   1184   1486       C  
ATOM   1976  CE1 HIS B  76     -41.967 -35.975   0.912  1.00 41.47           C  
ANISOU 1976  CE1 HIS B  76     6393   3619   5746   -379   1505   1337       C  
ATOM   1977  NE2 HIS B  76     -41.319 -35.696   2.029  1.00 43.78           N  
ANISOU 1977  NE2 HIS B  76     6839   4011   5784   -285   1443   1521       N  
ATOM   1978  N   PRO B  77     -43.228 -31.731   0.508  1.00 42.58           N  
ANISOU 1978  N   PRO B  77     5986   4334   5859   -533   1218    845       N  
ATOM   1979  CA  PRO B  77     -44.003 -32.459  -0.499  1.00 41.90           C  
ANISOU 1979  CA  PRO B  77     5772   4127   6022   -610   1292    726       C  
ATOM   1980  C   PRO B  77     -44.454 -31.520  -1.622  1.00 43.75           C  
ANISOU 1980  C   PRO B  77     5750   4477   6394   -616   1154    537       C  
ATOM   1981  O   PRO B  77     -44.579 -30.317  -1.404  1.00 43.36           O  
ANISOU 1981  O   PRO B  77     5630   4556   6290   -593   1096    486       O  
ATOM   1982  CB  PRO B  77     -45.195 -32.995   0.305  1.00 45.82           C  
ANISOU 1982  CB  PRO B  77     6326   4502   6580   -768   1581    700       C  
ATOM   1983  CG  PRO B  77     -45.381 -31.997   1.346  1.00 54.68           C  
ANISOU 1983  CG  PRO B  77     7496   5736   7545   -779   1630    708       C  
ATOM   1984  CD  PRO B  77     -44.018 -31.499   1.727  1.00 42.48           C  
ANISOU 1984  CD  PRO B  77     6076   4310   5753   -637   1425    848       C  
ATOM   1985  N   VAL B  78     -44.682 -32.051  -2.816  1.00 42.72           N  
ANISOU 1985  N   VAL B  78     5504   4298   6430   -644   1103    439       N  
ATOM   1986  CA  VAL B  78     -45.127 -31.210  -3.919  1.00 44.52           C  
ANISOU 1986  CA  VAL B  78     5508   4644   6762   -638    953    281       C  
ATOM   1987  C   VAL B  78     -46.590 -30.840  -3.716  1.00 51.42           C  
ANISOU 1987  C   VAL B  78     6205   5552   7780   -751   1074    147       C  
ATOM   1988  O   VAL B  78     -47.426 -31.690  -3.379  1.00 45.14           O  
ANISOU 1988  O   VAL B  78     5398   4653   7098   -892   1268    102       O  
ATOM   1989  CB  VAL B  78     -44.895 -31.904  -5.267  1.00 46.44           C  
ANISOU 1989  CB  VAL B  78     5703   4844   7100   -644    852    211       C  
ATOM   1990  CG1 VAL B  78     -45.664 -31.187  -6.368  1.00 50.59           C  
ANISOU 1990  CG1 VAL B  78     5999   5493   7731   -667    715     44       C  
ATOM   1991  CG2 VAL B  78     -43.414 -31.881  -5.577  1.00 42.19           C  
ANISOU 1991  CG2 VAL B  78     5280   4315   6434   -498    715    325       C  
ATOM   1992  N   GLU B  79     -46.890 -29.560  -3.900  1.00 43.28           N  
ANISOU 1992  N   GLU B  79     5034   4654   6756   -686    978     84       N  
ATOM   1993  CA  GLU B  79     -48.217 -28.988  -3.768  1.00 47.02           C  
ANISOU 1993  CA  GLU B  79     5298   5183   7383   -740   1070    -38       C  
ATOM   1994  C   GLU B  79     -48.610 -28.318  -5.080  1.00 52.73           C  
ANISOU 1994  C   GLU B  79     5793   6026   8216   -671    861   -144       C  
ATOM   1995  O   GLU B  79     -47.775 -28.097  -5.963  1.00 42.52           O  
ANISOU 1995  O   GLU B  79     4545   4771   6839   -581    662   -115       O  
ATOM   1996  CB  GLU B  79     -48.250 -27.991  -2.601  1.00 49.26           C  
ANISOU 1996  CB  GLU B  79     5657   5495   7564   -697   1186      3       C  
ATOM   1997  CG  GLU B  79     -47.960 -28.638  -1.238  1.00 51.63           C  
ANISOU 1997  CG  GLU B  79     6202   5697   7718   -773   1392    113       C  
ATOM   1998  CD  GLU B  79     -48.098 -27.662  -0.068  1.00 65.42           C  
ANISOU 1998  CD  GLU B  79     8038   7477   9343   -763   1528    123       C  
ATOM   1999  OE1 GLU B  79     -48.548 -26.521  -0.300  1.00 67.92           O  
ANISOU 1999  OE1 GLU B  79     8207   7865   9734   -701   1500     31       O  
ATOM   2000  OE2 GLU B  79     -47.810 -28.052   1.093  1.00 62.17           O1-
ANISOU 2000  OE2 GLU B  79     7855   7009   8756   -819   1678    220       O1-
ATOM   2001  N   GLU B  80     -49.901 -27.989  -5.198  1.00 46.13           N  
ANISOU 2001  N   GLU B  80     4706   5255   7566   -709    911   -263       N  
ATOM   2002  CA  GLU B  80     -50.410 -27.366  -6.420  1.00 55.33           C  
ANISOU 2002  CA  GLU B  80     5637   6554   8833   -629    697   -348       C  
ATOM   2003  C   GLU B  80     -49.636 -26.109  -6.797  1.00 47.29           C  
ANISOU 2003  C   GLU B  80     4697   5590   7682   -439    530   -272       C  
ATOM   2004  O   GLU B  80     -49.434 -25.830  -7.984  1.00 48.48           O  
ANISOU 2004  O   GLU B  80     4794   5814   7811   -362    313   -285       O  
ATOM   2005  CB  GLU B  80     -51.888 -27.018  -6.262  1.00 60.35           C  
ANISOU 2005  CB  GLU B  80     5968   7268   9694   -658    786   -462       C  
ATOM   2006  CG  GLU B  80     -52.543 -26.597  -7.564  1.00 71.39           C  
ANISOU 2006  CG  GLU B  80     7093   8826  11205   -582    540   -546       C  
ATOM   2007  CD  GLU B  80     -52.581 -27.722  -8.585  1.00 81.58           C  
ANISOU 2007  CD  GLU B  80     8337  10147  12514   -725    405   -635       C  
ATOM   2008  OE1 GLU B  80     -52.226 -27.479  -9.759  1.00 75.37           O  
ANISOU 2008  OE1 GLU B  80     7546   9448  11643   -644    151   -636       O  
ATOM   2009  OE2 GLU B  80     -52.995 -28.845  -8.213  1.00 87.35           O1-
ANISOU 2009  OE2 GLU B  80     9048  10803  13339   -930    573   -713       O1-
ATOM   2010  N   ASP B  81     -49.209 -25.325  -5.803  1.00 39.53           N  
ANISOU 2010  N   ASP B  81     3855   4566   6598   -377    642   -201       N  
ATOM   2011  CA  ASP B  81     -48.540 -24.062  -6.080  1.00 45.44           C  
ANISOU 2011  CA  ASP B  81     4682   5344   7240   -225    527   -147       C  
ATOM   2012  C   ASP B  81     -47.160 -24.265  -6.697  1.00 44.67           C  
ANISOU 2012  C   ASP B  81     4764   5238   6971   -198    369    -73       C  
ATOM   2013  O   ASP B  81     -46.569 -23.297  -7.180  1.00 43.86           O  
ANISOU 2013  O   ASP B  81     4718   5158   6788    -91    260    -39       O  
ATOM   2014  CB  ASP B  81     -48.412 -23.232  -4.796  1.00 50.89           C  
ANISOU 2014  CB  ASP B  81     5496   5985   7854   -208    709   -120       C  
ATOM   2015  CG  ASP B  81     -47.898 -21.817  -5.057  1.00 68.25           C  
ANISOU 2015  CG  ASP B  81     7764   8190   9977    -70    632    -93       C  
ATOM   2016  OD1 ASP B  81     -48.394 -21.168  -6.009  1.00 62.53           O  
ANISOU 2016  OD1 ASP B  81     6895   7506   9358     52    515   -113       O  
ATOM   2017  OD2 ASP B  81     -46.961 -21.375  -4.352  1.00 62.17           O1-
ANISOU 2017  OD2 ASP B  81     7202   7386   9035    -88    679    -49       O1-
ATOM   2018  N   ASP B  82     -46.641 -25.489  -6.687  1.00 40.38           N  
ANISOU 2018  N   ASP B  82     4312   4647   6384   -290    379    -46       N  
ATOM   2019  CA  ASP B  82     -45.313 -25.795  -7.199  1.00 42.72           C  
ANISOU 2019  CA  ASP B  82     4761   4928   6544   -259    264     23       C  
ATOM   2020  C   ASP B  82     -45.302 -26.173  -8.672  1.00 38.96           C  
ANISOU 2020  C   ASP B  82     4217   4484   6103   -249    104    -31       C  
ATOM   2021  O   ASP B  82     -44.218 -26.330  -9.241  1.00 42.07           O  
ANISOU 2021  O   ASP B  82     4723   4864   6395   -213     21     13       O  
ATOM   2022  CB  ASP B  82     -44.694 -26.926  -6.369  1.00 49.50           C  
ANISOU 2022  CB  ASP B  82     5770   5701   7337   -331    375    100       C  
ATOM   2023  CG  ASP B  82     -44.652 -26.597  -4.891  1.00 47.42           C  
ANISOU 2023  CG  ASP B  82     5611   5422   6985   -352    522    161       C  
ATOM   2024  OD1 ASP B  82     -44.604 -25.393  -4.575  1.00 44.82           O  
ANISOU 2024  OD1 ASP B  82     5285   5145   6601   -302    514    151       O  
ATOM   2025  OD2 ASP B  82     -44.722 -27.525  -4.048  1.00 52.04           O1-
ANISOU 2025  OD2 ASP B  82     6290   5933   7549   -426    660    215       O1-
ATOM   2026  N   VAL B  83     -46.467 -26.351  -9.294  1.00 40.62           N  
ANISOU 2026  N   VAL B  83     4240   4745   6448   -288     61   -133       N  
ATOM   2027  CA  VAL B  83     -46.554 -26.551 -10.740  1.00 41.59           C  
ANISOU 2027  CA  VAL B  83     4302   4931   6569   -283   -119   -199       C  
ATOM   2028  C   VAL B  83     -45.981 -25.329 -11.447  1.00 41.75           C  
ANISOU 2028  C   VAL B  83     4377   5008   6477   -133   -263   -142       C  
ATOM   2029  O   VAL B  83     -46.569 -24.241 -11.391  1.00 39.38           O  
ANISOU 2029  O   VAL B  83     3985   4762   6217    -33   -294   -130       O  
ATOM   2030  CB  VAL B  83     -48.012 -26.808 -11.160  1.00 47.41           C  
ANISOU 2030  CB  VAL B  83     4790   5755   7468   -355   -162   -325       C  
ATOM   2031  CG1 VAL B  83     -48.148 -26.822 -12.678  1.00 46.12           C  
ANISOU 2031  CG1 VAL B  83     4567   5697   7258   -341   -388   -392       C  
ATOM   2032  CG2 VAL B  83     -48.497 -28.119 -10.562  1.00 47.92           C  
ANISOU 2032  CG2 VAL B  83     4827   5737   7645   -541     10   -394       C  
ATOM   2033  N   ALA B  84     -44.837 -25.488 -12.117  1.00 36.33           N  
ANISOU 2033  N   ALA B  84     3846   4295   5661   -113   -327   -105       N  
ATOM   2034  CA  ALA B  84     -44.106 -24.334 -12.637  1.00 34.75           C  
ANISOU 2034  CA  ALA B  84     3741   4118   5345      6   -411    -39       C  
ATOM   2035  C   ALA B  84     -42.933 -24.812 -13.495  1.00 38.63           C  
ANISOU 2035  C   ALA B  84     4378   4581   5720     -6   -454    -28       C  
ATOM   2036  O   ALA B  84     -42.642 -26.009 -13.586  1.00 36.90           O  
ANISOU 2036  O   ALA B  84     4193   4311   5516    -90   -409    -63       O  
ATOM   2037  CB  ALA B  84     -43.605 -23.448 -11.497  1.00 38.51           C  
ANISOU 2037  CB  ALA B  84     4290   4554   5790     52   -302     36       C  
ATOM   2038  N   MET B  85     -42.280 -23.848 -14.139  1.00 35.77           N  
ANISOU 2038  N   MET B  85     4107   4233   5249     78   -516     20       N  
ATOM   2039  CA  MET B  85     -40.986 -24.021 -14.785  1.00 32.56           C  
ANISOU 2039  CA  MET B  85     3844   3794   4733     77   -510     43       C  
ATOM   2040  C   MET B  85     -39.897 -23.691 -13.765  1.00 37.65           C  
ANISOU 2040  C   MET B  85     4550   4399   5357     82   -406    115       C  
ATOM   2041  O   MET B  85     -40.035 -22.741 -12.991  1.00 38.01           O  
ANISOU 2041  O   MET B  85     4586   4448   5406    111   -372    149       O  
ATOM   2042  CB  MET B  85     -40.924 -23.090 -16.005  1.00 35.58           C  
ANISOU 2042  CB  MET B  85     4302   4215   5004    151   -614     58       C  
ATOM   2043  CG  MET B  85     -39.573 -22.830 -16.603  1.00 46.07           C  
ANISOU 2043  CG  MET B  85     5783   5505   6216    158   -571     92       C  
ATOM   2044  SD  MET B  85     -38.864 -24.313 -17.339  1.00 50.58           S  
ANISOU 2044  SD  MET B  85     6415   6042   6760     77   -532     20       S  
ATOM   2045  CE  MET B  85     -40.113 -24.705 -18.561  1.00 47.72           C  
ANISOU 2045  CE  MET B  85     6033   5754   6343     46   -688    -76       C  
ATOM   2046  N   TYR B  86     -38.832 -24.491 -13.735  1.00 32.03           N  
ANISOU 2046  N   TYR B  86     3892   3652   4626     55   -353    131       N  
ATOM   2047  CA  TYR B  86     -37.706 -24.251 -12.838  1.00 28.84           C  
ANISOU 2047  CA  TYR B  86     3516   3248   4194     60   -290    199       C  
ATOM   2048  C   TYR B  86     -36.422 -24.222 -13.651  1.00 35.00           C  
ANISOU 2048  C   TYR B  86     4357   4024   4916     76   -278    207       C  
ATOM   2049  O   TYR B  86     -36.278 -24.987 -14.604  1.00 36.30           O  
ANISOU 2049  O   TYR B  86     4555   4156   5082     74   -274    167       O  
ATOM   2050  CB  TYR B  86     -37.579 -25.345 -11.779  1.00 29.58           C  
ANISOU 2050  CB  TYR B  86     3586   3314   4341     36   -226    239       C  
ATOM   2051  CG  TYR B  86     -38.755 -25.361 -10.833  1.00 31.31           C  
ANISOU 2051  CG  TYR B  86     3757   3529   4612      2   -194    233       C  
ATOM   2052  CD1 TYR B  86     -39.909 -26.070 -11.149  1.00 35.32           C  
ANISOU 2052  CD1 TYR B  86     4208   4004   5207    -40   -187    168       C  
ATOM   2053  CD2 TYR B  86     -38.732 -24.618  -9.664  1.00 32.06           C  
ANISOU 2053  CD2 TYR B  86     3859   3658   4666     -5   -158    271       C  
ATOM   2054  CE1 TYR B  86     -41.016 -26.074 -10.287  1.00 33.47           C  
ANISOU 2054  CE1 TYR B  86     3908   3768   5042    -82   -128    152       C  
ATOM   2055  CE2 TYR B  86     -39.821 -24.608  -8.815  1.00 37.75           C  
ANISOU 2055  CE2 TYR B  86     4544   4366   5433    -40    -93    255       C  
ATOM   2056  CZ  TYR B  86     -40.956 -25.336  -9.129  1.00 37.72           C  
ANISOU 2056  CZ  TYR B  86     4466   4328   5539    -73    -71    200       C  
ATOM   2057  OH  TYR B  86     -42.037 -25.306  -8.265  1.00 35.67           O  
ANISOU 2057  OH  TYR B  86     4150   4059   5344   -117     22    176       O  
ATOM   2058  N   PHE B  87     -35.471 -23.380 -13.253  1.00 31.83           N  
ANISOU 2058  N   PHE B  87     3968   3657   4469     74   -253    243       N  
ATOM   2059  CA  PHE B  87     -34.185 -23.389 -13.952  1.00 31.68           C  
ANISOU 2059  CA  PHE B  87     3975   3641   4420     77   -215    244       C  
ATOM   2060  C   PHE B  87     -33.056 -23.009 -13.003  1.00 35.07           C  
ANISOU 2060  C   PHE B  87     4346   4136   4844     53   -190    285       C  
ATOM   2061  O   PHE B  87     -33.255 -22.247 -12.046  1.00 32.05           O  
ANISOU 2061  O   PHE B  87     3955   3792   4432     15   -204    294       O  
ATOM   2062  CB  PHE B  87     -34.179 -22.473 -15.202  1.00 33.93           C  
ANISOU 2062  CB  PHE B  87     4360   3906   4628     77   -214    212       C  
ATOM   2063  CG  PHE B  87     -34.570 -21.029 -14.950  1.00 37.42           C  
ANISOU 2063  CG  PHE B  87     4848   4344   5025     72   -222    226       C  
ATOM   2064  CD1 PHE B  87     -33.623 -20.085 -14.589  1.00 31.74           C  
ANISOU 2064  CD1 PHE B  87     4148   3633   4277     20   -156    232       C  
ATOM   2065  CD2 PHE B  87     -35.869 -20.595 -15.185  1.00 35.70           C  
ANISOU 2065  CD2 PHE B  87     4654   4108   4802    120   -286    225       C  
ATOM   2066  CE1 PHE B  87     -33.979 -18.747 -14.384  1.00 31.65           C  
ANISOU 2066  CE1 PHE B  87     4213   3581   4234     10   -129    235       C  
ATOM   2067  CE2 PHE B  87     -36.229 -19.252 -15.001  1.00 36.23           C  
ANISOU 2067  CE2 PHE B  87     4778   4141   4845    145   -268    247       C  
ATOM   2068  CZ  PHE B  87     -35.278 -18.332 -14.608  1.00 34.78           C  
ANISOU 2068  CZ  PHE B  87     4650   3932   4631     87   -177    250       C  
ATOM   2069  N   CYS B  88     -31.862 -23.562 -13.276  1.00 29.37           N  
ANISOU 2069  N   CYS B  88     3574   3434   4152     71   -150    299       N  
ATOM   2070  CA  CYS B  88     -30.665 -23.194 -12.537  1.00 31.28           C  
ANISOU 2070  CA  CYS B  88     3719   3773   4392     43   -148    327       C  
ATOM   2071  C   CYS B  88     -29.932 -22.095 -13.295  1.00 32.69           C  
ANISOU 2071  C   CYS B  88     3925   3961   4535    -24    -86    273       C  
ATOM   2072  O   CYS B  88     -30.184 -21.841 -14.477  1.00 37.18           O  
ANISOU 2072  O   CYS B  88     4599   4453   5075    -22    -36    237       O  
ATOM   2073  CB  CYS B  88     -29.697 -24.373 -12.331  1.00 31.77           C  
ANISOU 2073  CB  CYS B  88     3670   3867   4534    121   -135    384       C  
ATOM   2074  SG  CYS B  88     -29.391 -25.415 -13.809  1.00 39.57           S  
ANISOU 2074  SG  CYS B  88     4697   4740   5599    193    -27    349       S  
ATOM   2075  N   GLN B  89     -28.976 -21.473 -12.612  1.00 31.55           N  
ANISOU 2075  N   GLN B  89     3688   3917   4382    -96    -88    266       N  
ATOM   2076  CA  GLN B  89     -28.245 -20.333 -13.152  1.00 32.39           C  
ANISOU 2076  CA  GLN B  89     3817   4026   4463   -199     -3    204       C  
ATOM   2077  C   GLN B  89     -26.914 -20.222 -12.417  1.00 37.92           C  
ANISOU 2077  C   GLN B  89     4330   4879   5199   -271    -18    191       C  
ATOM   2078  O   GLN B  89     -26.886 -20.289 -11.184  1.00 35.50           O  
ANISOU 2078  O   GLN B  89     3944   4680   4863   -291   -119    215       O  
ATOM   2079  CB  GLN B  89     -29.076 -19.055 -12.973  1.00 33.58           C  
ANISOU 2079  CB  GLN B  89     4113   4109   4536   -268     10    172       C  
ATOM   2080  CG  GLN B  89     -28.532 -17.798 -13.598  1.00 40.35           C  
ANISOU 2080  CG  GLN B  89     5060   4910   5360   -376    128    116       C  
ATOM   2081  CD  GLN B  89     -27.751 -16.967 -12.595  1.00 43.20           C  
ANISOU 2081  CD  GLN B  89     5342   5360   5710   -531    144     54       C  
ATOM   2082  OE1 GLN B  89     -26.594 -16.612 -12.837  1.00 49.43           O  
ANISOU 2082  OE1 GLN B  89     6051   6201   6529   -640    222      0       O  
ATOM   2083  NE2 GLN B  89     -28.343 -16.734 -11.416  1.00 35.58           N  
ANISOU 2083  NE2 GLN B  89     4385   4429   4703   -556     73     47       N  
ATOM   2084  N   GLN B  90     -25.811 -20.085 -13.158  1.00 33.62           N  
ANISOU 2084  N   GLN B  90     3705   4358   4711   -312     82    150       N  
ATOM   2085  CA  GLN B  90     -24.507 -19.917 -12.536  1.00 36.58           C  
ANISOU 2085  CA  GLN B  90     3855   4905   5138   -393     63    122       C  
ATOM   2086  C   GLN B  90     -24.018 -18.486 -12.715  1.00 38.56           C  
ANISOU 2086  C   GLN B  90     4144   5152   5354   -594    166     16       C  
ATOM   2087  O   GLN B  90     -24.261 -17.844 -13.744  1.00 36.24           O  
ANISOU 2087  O   GLN B  90     4029   4708   5033   -636    308    -18       O  
ATOM   2088  CB  GLN B  90     -23.468 -20.905 -13.100  1.00 36.86           C  
ANISOU 2088  CB  GLN B  90     3707   4992   5308   -293    118    147       C  
ATOM   2089  CG  GLN B  90     -23.118 -20.677 -14.574  1.00 39.68           C  
ANISOU 2089  CG  GLN B  90     4150   5229   5698   -322    319     86       C  
ATOM   2090  CD  GLN B  90     -21.993 -19.679 -14.789  1.00 39.94           C  
ANISOU 2090  CD  GLN B  90     4074   5333   5769   -499    440     -8       C  
ATOM   2091  OE1 GLN B  90     -21.213 -19.388 -13.878  1.00 37.06           O  
ANISOU 2091  OE1 GLN B  90     3488   5147   5446   -587    362    -38       O  
ATOM   2092  NE2 GLN B  90     -21.918 -19.126 -16.007  1.00 42.41           N  
ANISOU 2092  NE2 GLN B  90     4551   5509   6054   -567    636    -62       N  
ATOM   2093  N   SER B  91     -23.302 -18.002 -11.700  1.00 40.13           N  
ANISOU 2093  N   SER B  91     4185   5519   5545   -727     96    -36       N  
ATOM   2094  CA  SER B  91     -22.759 -16.653 -11.691  1.00 36.57           C  
ANISOU 2094  CA  SER B  91     3755   5072   5070   -959    201   -160       C  
ATOM   2095  C   SER B  91     -21.250 -16.655 -11.527  1.00 39.20           C  
ANISOU 2095  C   SER B  91     3786   5608   5502  -1074    207   -230       C  
ATOM   2096  O   SER B  91     -20.660 -15.599 -11.254  1.00 39.31           O  
ANISOU 2096  O   SER B  91     3760   5674   5501  -1309    269   -356       O  
ATOM   2097  CB  SER B  91     -23.399 -15.843 -10.560  1.00 38.08           C  
ANISOU 2097  CB  SER B  91     4057   5272   5140  -1074    126   -207       C  
ATOM   2098  OG  SER B  91     -24.773 -15.666 -10.828  1.00 44.09           O  
ANISOU 2098  OG  SER B  91     5078   5835   5840   -975    158   -157       O  
ATOM   2099  N   ARG B  92     -20.614 -17.822 -11.678  1.00 39.39           N  
ANISOU 2099  N   ARG B  92     3584   5743   5638   -916    152   -157       N  
ATOM   2100  CA  ARG B  92     -19.173 -17.934 -11.465  1.00 41.88           C  
ANISOU 2100  CA  ARG B  92     3549   6285   6076   -987    134   -209       C  
ATOM   2101  C   ARG B  92     -18.381 -17.231 -12.564  1.00 40.25           C  
ANISOU 2101  C   ARG B  92     3319   6008   5966  -1144    388   -323       C  
ATOM   2102  O   ARG B  92     -17.343 -16.607 -12.294  1.00 40.49           O  
ANISOU 2102  O   ARG B  92     3124   6199   6061  -1347    418   -440       O  
ATOM   2103  CB  ARG B  92     -18.793 -19.414 -11.390  1.00 43.73           C  
ANISOU 2103  CB  ARG B  92     3570   6618   6426   -728     33    -77       C  
ATOM   2104  CG  ARG B  92     -17.303 -19.668 -11.299  1.00 42.11           C  
ANISOU 2104  CG  ARG B  92     2962   6649   6389   -740     19   -109       C  
ATOM   2105  CD  ARG B  92     -16.715 -18.988 -10.084  1.00 44.35           C  
ANISOU 2105  CD  ARG B  92     3037   7206   6608   -932   -170   -183       C  
ATOM   2106  NE  ARG B  92     -15.268 -19.139 -10.033  1.00 51.00           N  
ANISOU 2106  NE  ARG B  92     3448   8304   7625   -964   -193   -229       N  
ATOM   2107  CZ  ARG B  92     -14.409 -18.316 -10.622  1.00 56.91           C  
ANISOU 2107  CZ  ARG B  92     4054   9089   8482  -1192     -9   -392       C  
ATOM   2108  NH1 ARG B  92     -14.820 -17.267 -11.317  1.00 51.85           N  
ANISOU 2108  NH1 ARG B  92     3698   8225   7777  -1403    220   -510       N  
ATOM   2109  NH2 ARG B  92     -13.105 -18.547 -10.505  1.00 55.37           N  
ANISOU 2109  NH2 ARG B  92     3414   9156   8467  -1205    -47   -431       N  
ATOM   2110  N   LYS B  93     -18.826 -17.346 -13.813  1.00 41.05           N  
ANISOU 2110  N   LYS B  93     3645   5880   6070  -1064    576   -297       N  
ATOM   2111  CA  LYS B  93     -18.089 -16.779 -14.934  1.00 43.47           C  
ANISOU 2111  CA  LYS B  93     3967   6101   6450  -1198    848   -388       C  
ATOM   2112  C   LYS B  93     -19.043 -16.109 -15.909  1.00 37.31           C  
ANISOU 2112  C   LYS B  93     3601   5040   5534  -1218   1008   -376       C  
ATOM   2113  O   LYS B  93     -20.181 -16.542 -16.088  1.00 41.91           O  
ANISOU 2113  O   LYS B  93     4401   5502   6020  -1053    925   -282       O  
ATOM   2114  CB  LYS B  93     -17.258 -17.834 -15.691  1.00 46.18           C  
ANISOU 2114  CB  LYS B  93     4102   6486   6958  -1051    956   -362       C  
ATOM   2115  CG  LYS B  93     -16.241 -18.584 -14.847  1.00 51.35           C  
ANISOU 2115  CG  LYS B  93     4316   7418   7776   -975    804   -346       C  
ATOM   2116  CD  LYS B  93     -14.989 -18.913 -15.665  1.00 62.34           C  
ANISOU 2116  CD  LYS B  93     5444   8865   9378   -972   1023   -405       C  
ATOM   2117  CE  LYS B  93     -14.297 -20.170 -15.156  1.00 71.36           C  
ANISOU 2117  CE  LYS B  93     6215  10202  10699   -732    884   -315       C  
ATOM   2118  NZ  LYS B  93     -13.018 -19.906 -14.427  1.00 75.04           N  
ANISOU 2118  NZ  LYS B  93     6211  10982  11317   -843    793   -384       N  
ATOM   2119  N   VAL B  94     -18.543 -15.064 -16.562  1.00 45.80           N  
ANISOU 2119  N   VAL B  94     4775   6019   6609  -1424   1244   -469       N  
ATOM   2120  CA  VAL B  94     -19.230 -14.400 -17.667  1.00 37.26           C  
ANISOU 2120  CA  VAL B  94     4086   4672   5400  -1436   1431   -440       C  
ATOM   2121  C   VAL B  94     -18.833 -15.159 -18.932  1.00 44.94           C  
ANISOU 2121  C   VAL B  94     5079   5584   6410  -1332   1604   -416       C  
ATOM   2122  O   VAL B  94     -17.638 -15.382 -19.155  1.00 45.96           O  
ANISOU 2122  O   VAL B  94     4956   5818   6690  -1409   1746   -491       O  
ATOM   2123  CB  VAL B  94     -18.847 -12.908 -17.730  1.00 46.42           C  
ANISOU 2123  CB  VAL B  94     5375   5729   6535  -1711   1633   -542       C  
ATOM   2124  CG1 VAL B  94     -19.286 -12.265 -19.038  1.00 49.55           C  
ANISOU 2124  CG1 VAL B  94     6168   5850   6809  -1714   1870   -493       C  
ATOM   2125  CG2 VAL B  94     -19.412 -12.154 -16.527  1.00 44.28           C  
ANISOU 2125  CG2 VAL B  94     5151   5473   6200  -1804   1484   -575       C  
ATOM   2126  N   PRO B  95     -19.775 -15.558 -19.796  1.00 45.20           N  
ANISOU 2126  N   PRO B  95     5400   5460   6314  -1170   1607   -328       N  
ATOM   2127  CA  PRO B  95     -21.207 -15.236 -19.722  1.00 42.19           C  
ANISOU 2127  CA  PRO B  95     5311   4953   5767  -1076   1463   -240       C  
ATOM   2128  C   PRO B  95     -21.967 -16.008 -18.659  1.00 45.14           C  
ANISOU 2128  C   PRO B  95     5558   5434   6159   -929   1179   -186       C  
ATOM   2129  O   PRO B  95     -21.678 -17.183 -18.434  1.00 43.28           O  
ANISOU 2129  O   PRO B  95     5115   5311   6019   -811   1094   -169       O  
ATOM   2130  CB  PRO B  95     -21.726 -15.635 -21.103  1.00 49.84           C  
ANISOU 2130  CB  PRO B  95     6553   5776   6607   -959   1556   -182       C  
ATOM   2131  CG  PRO B  95     -20.822 -16.758 -21.529  1.00 47.30           C  
ANISOU 2131  CG  PRO B  95     6025   5540   6407   -908   1651   -225       C  
ATOM   2132  CD  PRO B  95     -19.462 -16.446 -20.934  1.00 49.38           C  
ANISOU 2132  CD  PRO B  95     5963   5943   6858  -1066   1754   -319       C  
ATOM   2133  N   LEU B  96     -22.922 -15.341 -18.012  1.00 42.52           N  
ANISOU 2133  N   LEU B  96     5362   5049   5743   -933   1060   -155       N  
ATOM   2134  CA  LEU B  96     -23.871 -16.043 -17.166  1.00 40.98           C  
ANISOU 2134  CA  LEU B  96     5118   4916   5538   -789    826    -94       C  
ATOM   2135  C   LEU B  96     -24.605 -17.059 -18.028  1.00 42.04           C  
ANISOU 2135  C   LEU B  96     5361   4984   5626   -608    783    -26       C  
ATOM   2136  O   LEU B  96     -24.865 -16.808 -19.208  1.00 38.36           O  
ANISOU 2136  O   LEU B  96     5117   4392   5065   -592    893    -10       O  
ATOM   2137  CB  LEU B  96     -24.864 -15.052 -16.535  1.00 34.11           C  
ANISOU 2137  CB  LEU B  96     4416   3962   4582   -820    763    -80       C  
ATOM   2138  CG  LEU B  96     -24.237 -13.932 -15.704  1.00 43.19           C  
ANISOU 2138  CG  LEU B  96     5514   5142   5752  -1032    828   -175       C  
ATOM   2139  CD1 LEU B  96     -25.314 -12.997 -15.120  1.00 42.99           C  
ANISOU 2139  CD1 LEU B  96     5688   4997   5650  -1038    800   -165       C  
ATOM   2140  CD2 LEU B  96     -23.336 -14.484 -14.614  1.00 45.27           C  
ANISOU 2140  CD2 LEU B  96     5454   5643   6104  -1101    713   -230       C  
ATOM   2141  N   THR B  97     -24.892 -18.234 -17.458  1.00 35.26           N  
ANISOU 2141  N   THR B  97     4358   4211   4826   -484    633     10       N  
ATOM   2142  CA  THR B  97     -25.575 -19.270 -18.217  1.00 33.85           C  
ANISOU 2142  CA  THR B  97     4276   3970   4617   -343    602     46       C  
ATOM   2143  C   THR B  97     -26.665 -19.889 -17.350  1.00 38.89           C  
ANISOU 2143  C   THR B  97     4886   4632   5257   -245    410     98       C  
ATOM   2144  O   THR B  97     -26.643 -19.801 -16.117  1.00 35.75           O  
ANISOU 2144  O   THR B  97     4359   4323   4900   -264    313    113       O  
ATOM   2145  CB  THR B  97     -24.618 -20.358 -18.721  1.00 37.94           C  
ANISOU 2145  CB  THR B  97     4658   4519   5238   -291    703     22       C  
ATOM   2146  OG1 THR B  97     -23.847 -20.872 -17.632  1.00 36.64           O  
ANISOU 2146  OG1 THR B  97     4209   4496   5215   -267    635     35       O  
ATOM   2147  CG2 THR B  97     -23.656 -19.797 -19.798  1.00 40.85           C  
ANISOU 2147  CG2 THR B  97     5088   4840   5594   -391    937    -39       C  
ATOM   2148  N   PHE B  98     -27.622 -20.523 -18.024  1.00 32.49           N  
ANISOU 2148  N   PHE B  98     4207   3748   4391   -156    366    115       N  
ATOM   2149  CA  PHE B  98     -28.827 -21.054 -17.408  1.00 34.65           C  
ANISOU 2149  CA  PHE B  98     4480   4021   4663    -83    215    150       C  
ATOM   2150  C   PHE B  98     -28.988 -22.514 -17.795  1.00 38.19           C  
ANISOU 2150  C   PHE B  98     4907   4444   5160     -2    210    142       C  
ATOM   2151  O   PHE B  98     -28.594 -22.922 -18.887  1.00 37.16           O  
ANISOU 2151  O   PHE B  98     4852   4263   5006      4    313    101       O  
ATOM   2152  CB  PHE B  98     -30.066 -20.294 -17.872  1.00 33.23           C  
ANISOU 2152  CB  PHE B  98     4478   3774   4374    -70    155    164       C  
ATOM   2153  CG  PHE B  98     -30.067 -18.842 -17.487  1.00 35.11           C  
ANISOU 2153  CG  PHE B  98     4777   3990   4573   -132    184    176       C  
ATOM   2154  CD1 PHE B  98     -29.362 -17.904 -18.233  1.00 32.56           C  
ANISOU 2154  CD1 PHE B  98     4572   3607   4191   -203    320    163       C  
ATOM   2155  CD2 PHE B  98     -30.770 -18.416 -16.368  1.00 32.81           C  
ANISOU 2155  CD2 PHE B  98     4444   3716   4306   -129    105    192       C  
ATOM   2156  CE1 PHE B  98     -29.361 -16.574 -17.876  1.00 40.84           C  
ANISOU 2156  CE1 PHE B  98     5703   4601   5215   -271    377    167       C  
ATOM   2157  CE2 PHE B  98     -30.781 -17.065 -16.013  1.00 34.88           C  
ANISOU 2157  CE2 PHE B  98     4787   3927   4538   -192    162    186       C  
ATOM   2158  CZ  PHE B  98     -30.075 -16.151 -16.763  1.00 39.05           C  
ANISOU 2158  CZ  PHE B  98     5438   4383   5017   -263    297    174       C  
ATOM   2159  N   GLY B  99     -29.575 -23.305 -16.898  1.00 27.84           N  
ANISOU 2159  N   GLY B  99     3516   3151   3912     50    115    176       N  
ATOM   2160  CA  GLY B  99     -30.100 -24.590 -17.306  1.00 29.96           C  
ANISOU 2160  CA  GLY B  99     3819   3353   4212    105    114    157       C  
ATOM   2161  C   GLY B  99     -31.248 -24.420 -18.283  1.00 28.82           C  
ANISOU 2161  C   GLY B  99     3833   3160   3957     83     64    108       C  
ATOM   2162  O   GLY B  99     -31.878 -23.372 -18.357  1.00 32.95           O  
ANISOU 2162  O   GLY B  99     4419   3702   4400     63     -3    121       O  
ATOM   2163  N   ALA B 100     -31.507 -25.467 -19.076  1.00 35.79           N  
ANISOU 2163  N   ALA B 100     4785   3980   4835     90     98     46       N  
ATOM   2164  CA  ALA B 100     -32.525 -25.379 -20.117  1.00 37.64           C  
ANISOU 2164  CA  ALA B 100     5161   4200   4939     56     28    -15       C  
ATOM   2165  C   ALA B 100     -33.946 -25.506 -19.576  1.00 36.40           C  
ANISOU 2165  C   ALA B 100     4955   4072   4803     51   -120    -15       C  
ATOM   2166  O   ALA B 100     -34.898 -25.333 -20.344  1.00 39.54           O  
ANISOU 2166  O   ALA B 100     5426   4496   5100     30   -220    -59       O  
ATOM   2167  CB  ALA B 100     -32.287 -26.448 -21.192  1.00 42.28           C  
ANISOU 2167  CB  ALA B 100     5854   4717   5494     31    125   -113       C  
ATOM   2168  N   GLY B 101     -34.115 -25.809 -18.302  1.00 36.13           N  
ANISOU 2168  N   GLY B 101     4795   4043   4890     69   -134     33       N  
ATOM   2169  CA  GLY B 101     -35.436 -25.745 -17.702  1.00 34.08           C  
ANISOU 2169  CA  GLY B 101     4476   3813   4662     56   -241     35       C  
ATOM   2170  C   GLY B 101     -36.015 -27.124 -17.398  1.00 42.64           C  
ANISOU 2170  C   GLY B 101     5521   4839   5842     20   -218    -13       C  
ATOM   2171  O   GLY B 101     -35.730 -28.119 -18.078  1.00 39.59           O  
ANISOU 2171  O   GLY B 101     5199   4380   5463     -7   -147    -81       O  
ATOM   2172  N   THR B 102     -36.844 -27.176 -16.356  1.00 38.19           N  
ANISOU 2172  N   THR B 102     4638   4269   5604    404   -922  -1067       N  
ATOM   2173  CA  THR B 102     -37.649 -28.348 -16.017  1.00 40.13           C  
ANISOU 2173  CA  THR B 102     4789   4275   6183    315   -858  -1021       C  
ATOM   2174  C   THR B 102     -39.092 -27.903 -15.864  1.00 34.63           C  
ANISOU 2174  C   THR B 102     4047   3841   5270    288   -773   -711       C  
ATOM   2175  O   THR B 102     -39.397 -27.060 -15.012  1.00 38.35           O  
ANISOU 2175  O   THR B 102     4708   4345   5518    505   -764   -347       O  
ATOM   2176  CB  THR B 102     -37.183 -29.008 -14.721  1.00 35.22           C  
ANISOU 2176  CB  THR B 102     4391   3146   5846    515   -885   -827       C  
ATOM   2177  OG1 THR B 102     -35.847 -29.487 -14.881  1.00 44.14           O  
ANISOU 2177  OG1 THR B 102     5519   4055   7196    590   -991  -1159       O  
ATOM   2178  CG2 THR B 102     -38.132 -30.182 -14.326  1.00 39.02           C  
ANISOU 2178  CG2 THR B 102     4838   3347   6641    365   -791   -709       C  
ATOM   2179  N   LYS B 103     -39.969 -28.456 -16.687  1.00 36.63           N  
ANISOU 2179  N   LYS B 103     4017   4318   5580     27   -710   -898       N  
ATOM   2180  CA  LYS B 103     -41.403 -28.233 -16.560  1.00 40.08           C  
ANISOU 2180  CA  LYS B 103     4330   5050   5849    -18   -627   -679       C  
ATOM   2181  C   LYS B 103     -41.954 -29.265 -15.591  1.00 42.06           C  
ANISOU 2181  C   LYS B 103     4624   4948   6410   -110   -514   -528       C  
ATOM   2182  O   LYS B 103     -41.942 -30.472 -15.876  1.00 43.82           O  
ANISOU 2182  O   LYS B 103     4736   4925   6990   -363   -458   -780       O  
ATOM   2183  CB  LYS B 103     -42.091 -28.328 -17.919  1.00 48.21           C  
ANISOU 2183  CB  LYS B 103     4999   6566   6751   -272   -617   -978       C  
ATOM   2184  CG  LYS B 103     -43.535 -27.869 -17.906  1.00 54.49           C  
ANISOU 2184  CG  LYS B 103     5618   7800   7286   -255   -570   -785       C  
ATOM   2185  CD  LYS B 103     -44.074 -27.666 -19.312  1.00 59.76           C  
ANISOU 2185  CD  LYS B 103     5946   9052   7706   -421   -616  -1050       C  
ATOM   2186  CE  LYS B 103     -44.835 -26.347 -19.439  1.00 67.75           C  
ANISOU 2186  CE  LYS B 103     6959  10526   8257   -146   -704   -766       C  
ATOM   2187  NZ  LYS B 103     -45.223 -26.053 -20.857  1.00 80.37           N  
ANISOU 2187  NZ  LYS B 103     8269  12716   9551   -261   -794   -978       N  
ATOM   2188  N   LEU B 104     -42.414 -28.794 -14.439  1.00 41.65           N  
ANISOU 2188  N   LEU B 104     4750   4856   6220     79   -471   -126       N  
ATOM   2189  CA  LEU B 104     -42.999 -29.639 -13.407  1.00 43.54           C  
ANISOU 2189  CA  LEU B 104     5067   4813   6662    -30   -347     93       C  
ATOM   2190  C   LEU B 104     -44.512 -29.620 -13.571  1.00 52.22           C  
ANISOU 2190  C   LEU B 104     5885   6350   7607   -226   -214    117       C  
ATOM   2191  O   LEU B 104     -45.140 -28.566 -13.427  1.00 45.03           O  
ANISOU 2191  O   LEU B 104     4911   5851   6346    -32   -225    279       O  
ATOM   2192  CB  LEU B 104     -42.586 -29.152 -12.017  1.00 39.63           C  
ANISOU 2192  CB  LEU B 104     4901   4094   6064    264   -369    489       C  
ATOM   2193  CG  LEU B 104     -42.766 -30.039 -10.793  1.00 51.78           C  
ANISOU 2193  CG  LEU B 104     6637   5240   7798    190   -277    776       C  
ATOM   2194  CD1 LEU B 104     -41.833 -29.590  -9.694  1.00 53.11           C  
ANISOU 2194  CD1 LEU B 104     7126   5174   7878    521   -372   1050       C  
ATOM   2195  CD2 LEU B 104     -44.196 -29.958 -10.314  1.00 54.59           C  
ANISOU 2195  CD2 LEU B 104     6851   5920   7973     31   -106    970       C  
ATOM   2196  N   GLU B 105     -45.088 -30.782 -13.882  1.00 50.43           N  
ANISOU 2196  N   GLU B 105     5476   6038   7646   -606    -89    -79       N  
ATOM   2197  CA  GLU B 105     -46.520 -30.936 -14.088  1.00 50.48           C  
ANISOU 2197  CA  GLU B 105     5154   6496   7531   -866     58   -141       C  
ATOM   2198  C   GLU B 105     -47.052 -32.011 -13.150  1.00 52.47           C  
ANISOU 2198  C   GLU B 105     5505   6404   8026  -1173    252     17       C  
ATOM   2199  O   GLU B 105     -46.298 -32.841 -12.637  1.00 53.44           O  
ANISOU 2199  O   GLU B 105     5930   5895   8480  -1224    254    106       O  
ATOM   2200  CB  GLU B 105     -46.840 -31.318 -15.539  1.00 58.55           C  
ANISOU 2200  CB  GLU B 105     5794   7855   8596  -1144     56   -610       C  
ATOM   2201  CG  GLU B 105     -46.284 -30.353 -16.576  1.00 71.19           C  
ANISOU 2201  CG  GLU B 105     7313   9800   9934   -911   -131   -763       C  
ATOM   2202  CD  GLU B 105     -45.853 -31.059 -17.859  1.00 87.03           C  
ANISOU 2202  CD  GLU B 105     9098  11839  12129  -1188   -157  -1252       C  
ATOM   2203  OE1 GLU B 105     -45.265 -32.162 -17.760  1.00 83.75           O  
ANISOU 2203  OE1 GLU B 105     8782  10899  12141  -1383   -102  -1436       O  
ATOM   2204  OE2 GLU B 105     -46.087 -30.506 -18.960  1.00 84.64           O1-
ANISOU 2204  OE2 GLU B 105     8532  12088  11541  -1195   -240  -1456       O1-
ATOM   2205  N   LEU B 106     -48.363 -31.996 -12.931  1.00 54.83           N  
ANISOU 2205  N   LEU B 106     5550   7136   8147  -1379    412     50       N  
ATOM   2206  CA  LEU B 106     -49.003 -32.981 -12.070  1.00 62.74           C  
ANISOU 2206  CA  LEU B 106     6629   7888   9320  -1760    636    200       C  
ATOM   2207  C   LEU B 106     -49.590 -34.112 -12.911  1.00 65.94           C  
ANISOU 2207  C   LEU B 106     6760   8299   9996  -2295    788   -202       C  
ATOM   2208  O   LEU B 106     -49.950 -33.919 -14.074  1.00 67.16           O  
ANISOU 2208  O   LEU B 106     6526   8935  10057  -2369    748   -588       O  
ATOM   2209  CB  LEU B 106     -50.101 -32.336 -11.219  1.00 70.78           C  
ANISOU 2209  CB  LEU B 106     7511   9412   9971  -1725    759    441       C  
ATOM   2210  CG  LEU B 106     -49.618 -31.534 -10.001  1.00 66.03           C  
ANISOU 2210  CG  LEU B 106     7243   8680   9166  -1319    689    875       C  
ATOM   2211  CD1 LEU B 106     -50.793 -31.112  -9.119  1.00 62.61           C  
ANISOU 2211  CD1 LEU B 106     6635   8748   8407  -1373    856   1046       C  
ATOM   2212  CD2 LEU B 106     -48.564 -32.285  -9.189  1.00 70.38           C  
ANISOU 2212  CD2 LEU B 106     8278   8460  10003  -1322    666   1151       C  
ATOM   2213  N   LYS B 107     -49.671 -35.301 -12.317  1.00 66.85           N  
ANISOU 2213  N   LYS B 107     7094   7866  10439  -2681    963   -110       N  
ATOM   2214  CA  LYS B 107     -50.313 -36.428 -12.993  1.00 76.74           C  
ANISOU 2214  CA  LYS B 107     8112   9075  11970  -3261   1154   -499       C  
ATOM   2215  C   LYS B 107     -51.775 -36.577 -12.579  1.00 77.33           C  
ANISOU 2215  C   LYS B 107     7906   9646  11829  -3686   1422   -484       C  
ATOM   2216  O   LYS B 107     -52.192 -36.078 -11.535  1.00 81.15           O  
ANISOU 2216  O   LYS B 107     8485  10312  12035  -3579   1486   -106       O  
ATOM   2217  CB  LYS B 107     -49.562 -37.735 -12.721  1.00 75.51           C  
ANISOU 2217  CB  LYS B 107     8372   7965  12354  -3484   1199   -468       C  
ATOM   2218  CG  LYS B 107     -48.516 -38.067 -13.770  1.00 81.79           C  
ANISOU 2218  CG  LYS B 107     9159   8440  13477  -3351   1024   -870       C  
ATOM   2219  CD  LYS B 107     -47.714 -39.294 -13.382  1.00 92.72           C  
ANISOU 2219  CD  LYS B 107    10990   8829  15409  -3453   1028   -811       C  
ATOM   2220  CE  LYS B 107     -46.948 -39.080 -12.089  1.00 81.65           C  
ANISOU 2220  CE  LYS B 107    10103   6944  13977  -3053    905   -219       C  
ATOM   2221  NZ  LYS B 107     -46.517 -40.392 -11.520  1.00 92.60           N  
ANISOU 2221  NZ  LYS B 107    11952   7369  15862  -3227    950    -59       N  
ATOM   2222  N   TRP B 118     -59.233 -32.776  -2.986  1.00109.56           N  
ANISOU 2222  N   TRP B 118    10960  18122  12546  -4277   2959   1343       N  
ATOM   2223  CA  TRP B 118     -58.527 -31.546  -3.328  1.00105.06           C  
ANISOU 2223  CA  TRP B 118    10420  17560  11940  -3428   2603   1334       C  
ATOM   2224  C   TRP B 118     -59.319 -30.334  -2.845  1.00107.08           C  
ANISOU 2224  C   TRP B 118    10241  18685  11760  -3030   2600   1167       C  
ATOM   2225  O   TRP B 118     -60.538 -30.277  -3.005  1.00103.34           O  
ANISOU 2225  O   TRP B 118     9193  19000  11071  -3256   2765    804       O  
ATOM   2226  CB  TRP B 118     -58.293 -31.453  -4.838  1.00112.45           C  
ANISOU 2226  CB  TRP B 118    11169  18434  13124  -3207   2378    992       C  
ATOM   2227  CG  TRP B 118     -57.266 -32.414  -5.355  1.00117.18           C  
ANISOU 2227  CG  TRP B 118    12217  18132  14173  -3404   2305   1119       C  
ATOM   2228  CD1 TRP B 118     -57.063 -33.701  -4.940  1.00126.45           C  
ANISOU 2228  CD1 TRP B 118    13751  18691  15601  -3998   2506   1333       C  
ATOM   2229  CD2 TRP B 118     -56.302 -32.168  -6.386  1.00111.15           C  
ANISOU 2229  CD2 TRP B 118    11592  16980  13661  -3002   2009   1020       C  
ATOM   2230  NE1 TRP B 118     -56.033 -34.270  -5.651  1.00127.98           N  
ANISOU 2230  NE1 TRP B 118    14278  18131  16219  -3941   2339   1341       N  
ATOM   2231  CE2 TRP B 118     -55.548 -33.351  -6.544  1.00111.59           C  
ANISOU 2231  CE2 TRP B 118    12050  16216  14133  -3354   2044   1135       C  
ATOM   2232  CE3 TRP B 118     -56.002 -31.064  -7.190  1.00103.75           C  
ANISOU 2232  CE3 TRP B 118    10491  16303  12627  -2391   1723    849       C  
ATOM   2233  CZ2 TRP B 118     -54.515 -33.460  -7.473  1.00103.70           C  
ANISOU 2233  CZ2 TRP B 118    11233  14722  13446  -3113   1809   1028       C  
ATOM   2234  CZ3 TRP B 118     -54.976 -31.174  -8.112  1.00103.82           C  
ANISOU 2234  CZ3 TRP B 118    10711  15819  12916  -2206   1506    786       C  
ATOM   2235  CH2 TRP B 118     -54.245 -32.363  -8.246  1.00109.28           C  
ANISOU 2235  CH2 TRP B 118    11745  15764  14012  -2565   1553    849       C  
ATOM   2236  N   THR B 119     -58.624 -29.365  -2.259  1.00 97.20           N  
ANISOU 2236  N   THR B 119     9244  17303  10387  -2431   2411   1392       N  
ATOM   2237  CA  THR B 119     -59.292 -28.201  -1.697  1.00 96.56           C  
ANISOU 2237  CA  THR B 119     8805  17959   9926  -2017   2406   1232       C  
ATOM   2238  C   THR B 119     -59.803 -27.268  -2.795  1.00 96.98           C  
ANISOU 2238  C   THR B 119     8387  18529   9934  -1502   2187    809       C  
ATOM   2239  O   THR B 119     -59.339 -27.288  -3.940  1.00 84.91           O  
ANISOU 2239  O   THR B 119     6918  16702   8643  -1332   1976    722       O  
ATOM   2240  CB  THR B 119     -58.344 -27.449  -0.760  1.00102.63           C  
ANISOU 2240  CB  THR B 119    10006  18391  10599  -1546   2274   1568       C  
ATOM   2241  OG1 THR B 119     -57.517 -26.556  -1.522  1.00 91.64           O  
ANISOU 2241  OG1 THR B 119     8771  16691   9357   -888   1936   1526       O  
ATOM   2242  CG2 THR B 119     -57.469 -28.426   0.020  1.00 92.76           C  
ANISOU 2242  CG2 THR B 119     9343  16424   9480  -1935   2368   2050       C  
ATOM   2243  N   VAL B 120     -60.787 -26.441  -2.427  1.00 93.05           N  
ANISOU 2243  N   VAL B 120    13327  11831  10199   3499   2094    848       N  
ATOM   2244  CA  VAL B 120     -61.308 -25.434  -3.349  1.00 95.63           C  
ANISOU 2244  CA  VAL B 120    13874  12045  10418   3731   2283    637       C  
ATOM   2245  C   VAL B 120     -60.259 -24.365  -3.633  1.00 87.44           C  
ANISOU 2245  C   VAL B 120    13413  10807   9002   3244   1811    531       C  
ATOM   2246  O   VAL B 120     -60.225 -23.790  -4.729  1.00 83.88           O  
ANISOU 2246  O   VAL B 120    12793  10386   8694   3241   1784    374       O  
ATOM   2247  CB  VAL B 120     -62.600 -24.814  -2.782  1.00 83.78           C  
ANISOU 2247  CB  VAL B 120    13052  10276   8504   4340   2869    648       C  
ATOM   2248  CG1 VAL B 120     -63.099 -23.665  -3.669  1.00 77.87           C  
ANISOU 2248  CG1 VAL B 120    12578   9381   7628   4581   3082    513       C  
ATOM   2249  CG2 VAL B 120     -63.666 -25.878  -2.625  1.00 77.36           C  
ANISOU 2249  CG2 VAL B 120    11543   9697   8154   4814   3314    815       C  
ATOM   2250  N   GLU B 121     -59.399 -24.070  -2.653  1.00 93.11           N  
ANISOU 2250  N   GLU B 121    14836  11325   9218   2789   1407    644       N  
ATOM   2251  CA  GLU B 121     -58.337 -23.094  -2.867  1.00 88.41           C  
ANISOU 2251  CA  GLU B 121    14779  10546   8267   2238    883    606       C  
ATOM   2252  C   GLU B 121     -57.340 -23.592  -3.907  1.00 84.65           C  
ANISOU 2252  C   GLU B 121    13322  10382   8458   1866    496    691       C  
ATOM   2253  O   GLU B 121     -56.912 -22.831  -4.784  1.00 80.32           O  
ANISOU 2253  O   GLU B 121    12823   9779   7917   1697    312    567       O  
ATOM   2254  CB  GLU B 121     -57.628 -22.788  -1.546  1.00 88.41           C  
ANISOU 2254  CB  GLU B 121    15721  10295   7577   1724    463    787       C  
ATOM   2255  CG  GLU B 121     -58.335 -21.770  -0.649  1.00 90.05           C  
ANISOU 2255  CG  GLU B 121    17343   9995   6877   1932    797    635       C  
ATOM   2256  CD  GLU B 121     -59.601 -22.309  -0.001  1.00 86.50           C  
ANISOU 2256  CD  GLU B 121    16945   9503   6419   2607   1487    644       C  
ATOM   2257  OE1 GLU B 121     -60.686 -22.182  -0.607  1.00 93.70           O  
ANISOU 2257  OE1 GLU B 121    17584  10422   7596   3264   2088    524       O  
ATOM   2258  OE2 GLU B 121     -59.510 -22.842   1.122  1.00 89.36           O1-
ANISOU 2258  OE2 GLU B 121    17613   9830   6511   2465   1417    822       O1-
ATOM   2259  N   ASP B 122     -56.963 -24.872  -3.825  1.00 75.97           N  
ANISOU 2259  N   ASP B 122    11346   9582   7938   1762    428    925       N  
ATOM   2260  CA  ASP B 122     -56.060 -25.453  -4.814  1.00 83.36           C  
ANISOU 2260  CA  ASP B 122    11348  10759   9565   1484    218   1048       C  
ATOM   2261  C   ASP B 122     -56.730 -25.556  -6.177  1.00 80.61           C  
ANISOU 2261  C   ASP B 122    10439  10539   9652   1850    613    758       C  
ATOM   2262  O   ASP B 122     -56.086 -25.348  -7.213  1.00 71.87           O  
ANISOU 2262  O   ASP B 122     8996   9476   8834   1640    463    718       O  
ATOM   2263  CB  ASP B 122     -55.596 -26.833  -4.349  1.00 79.88           C  
ANISOU 2263  CB  ASP B 122    10148  10552   9651   1354    185   1401       C  
ATOM   2264  CG  ASP B 122     -54.232 -26.799  -3.691  1.00 85.88           C  
ANISOU 2264  CG  ASP B 122    10988  11308  10336    712   -432   1862       C  
ATOM   2265  OD1 ASP B 122     -53.669 -27.887  -3.441  1.00 91.93           O  
ANISOU 2265  OD1 ASP B 122    11026  12273  11631    566   -478   2250       O  
ATOM   2266  OD2 ASP B 122     -53.718 -25.689  -3.428  1.00 90.33           O1-
ANISOU 2266  OD2 ASP B 122    12331  11666  10326    330   -874   1885       O1-
ATOM   2267  N   LEU B 123     -58.021 -25.885  -6.196  1.00 76.30           N  
ANISOU 2267  N   LEU B 123     9783  10054   9152   2371   1108    599       N  
ATOM   2268  CA  LEU B 123     -58.717 -26.027  -7.467  1.00 75.61           C  
ANISOU 2268  CA  LEU B 123     9165  10121   9443   2638   1423    388       C  
ATOM   2269  C   LEU B 123     -58.929 -24.672  -8.133  1.00 75.53           C  
ANISOU 2269  C   LEU B 123     9675   9952   9070   2703   1393    182       C  
ATOM   2270  O   LEU B 123     -58.892 -24.576  -9.364  1.00 67.16           O  
ANISOU 2270  O   LEU B 123     8215   9005   8297   2661   1414     48       O  
ATOM   2271  CB  LEU B 123     -60.042 -26.753  -7.249  1.00 80.50           C  
ANISOU 2271  CB  LEU B 123     9487  10874  10227   3119   1899    384       C  
ATOM   2272  CG  LEU B 123     -59.945 -28.247  -6.909  1.00 72.48           C  
ANISOU 2272  CG  LEU B 123     7773  10053   9713   3086   2011    550       C  
ATOM   2273  CD1 LEU B 123     -61.262 -28.739  -6.323  1.00 84.10           C  
ANISOU 2273  CD1 LEU B 123     9263  11536  11156   3355   2284    566       C  
ATOM   2274  CD2 LEU B 123     -59.544 -29.100  -8.103  1.00 78.66           C  
ANISOU 2274  CD2 LEU B 123     7833  10968  11085   2757   1973    451       C  
ATOM   2275  N   GLN B 124     -59.124 -23.613  -7.343  1.00 70.79           N  
ANISOU 2275  N   GLN B 124    10017   9058   7820   2786   1367    161       N  
ATOM   2276  CA  GLN B 124     -59.216 -22.274  -7.919  1.00 73.22           C  
ANISOU 2276  CA  GLN B 124    10879   9165   7776   2826   1350     -7       C  
ATOM   2277  C   GLN B 124     -57.858 -21.787  -8.409  1.00 65.25           C  
ANISOU 2277  C   GLN B 124     9920   8103   6768   2274    825    -12       C  
ATOM   2278  O   GLN B 124     -57.770 -21.127  -9.452  1.00 68.57           O  
ANISOU 2278  O   GLN B 124    10274   8525   7255   2256    793   -154       O  
ATOM   2279  CB  GLN B 124     -59.794 -21.291  -6.899  1.00 81.28           C  
ANISOU 2279  CB  GLN B 124    13002   9800   8080   3073   1565    -20       C  
ATOM   2280  CG  GLN B 124     -60.327 -20.014  -7.526  1.00 82.06           C  
ANISOU 2280  CG  GLN B 124    13588   9687   7903   3333   1798   -160       C  
ATOM   2281  CD  GLN B 124     -60.819 -19.009  -6.499  1.00 88.17           C  
ANISOU 2281  CD  GLN B 124    15583   9974   7943   3573   2108   -162       C  
ATOM   2282  OE1 GLN B 124     -60.658 -19.198  -5.288  1.00 90.30           O  
ANISOU 2282  OE1 GLN B 124    16449  10043   7819   3460   2075    -89       O  
ATOM   2283  NE2 GLN B 124     -61.418 -17.927  -6.980  1.00 77.65           N  
ANISOU 2283  NE2 GLN B 124    14674   8421   6408   3900   2449   -225       N  
ATOM   2284  N   LYS B 125     -56.794 -22.077  -7.655  1.00 64.14           N  
ANISOU 2284  N   LYS B 125     9887   7924   6561   1810    397    202       N  
ATOM   2285  CA  LYS B 125     -55.448 -21.769  -8.125  1.00 72.79           C  
ANISOU 2285  CA  LYS B 125    10857   9013   7786   1266   -115    328       C  
ATOM   2286  C   LYS B 125     -55.181 -22.434  -9.468  1.00 60.17           C  
ANISOU 2286  C   LYS B 125     8277   7674   6910   1281     -3    298       C  
ATOM   2287  O   LYS B 125     -54.647 -21.803 -10.389  1.00 69.11           O  
ANISOU 2287  O   LYS B 125     9368   8772   8121   1109   -165    230       O  
ATOM   2288  CB  LYS B 125     -54.417 -22.210  -7.085  1.00 73.91           C  
ANISOU 2288  CB  LYS B 125    11063   9152   7868    763   -582    709       C  
ATOM   2289  CG  LYS B 125     -54.144 -21.185  -5.993  1.00 72.56           C  
ANISOU 2289  CG  LYS B 125    12065   8646   6858    424   -944    763       C  
ATOM   2290  CD  LYS B 125     -53.208 -21.733  -4.901  1.00 88.62           C  
ANISOU 2290  CD  LYS B 125    14120  10733   8819   -128  -1450   1219       C  
ATOM   2291  CE  LYS B 125     -51.965 -22.411  -5.473  1.00 83.33           C  
ANISOU 2291  CE  LYS B 125    12455  10330   8878   -533  -1816   1641       C  
ATOM   2292  NZ  LYS B 125     -51.163 -21.501  -6.356  1.00 75.03           N  
ANISOU 2292  NZ  LYS B 125    11456   9189   7862   -854  -2152   1655       N  
ATOM   2293  N   ARG B 126     -55.578 -23.702  -9.607  1.00 60.65           N  
ANISOU 2293  N   ARG B 126     7604   7964   7476   1484    312    338       N  
ATOM   2294  CA  ARG B 126     -55.403 -24.398 -10.878  1.00 67.56           C  
ANISOU 2294  CA  ARG B 126     7677   9019   8972   1482    506    277       C  
ATOM   2295  C   ARG B 126     -56.279 -23.788 -11.962  1.00 63.95           C  
ANISOU 2295  C   ARG B 126     7274   8593   8430   1752    750    -46       C  
ATOM   2296  O   ARG B 126     -55.832 -23.606 -13.101  1.00 57.25           O  
ANISOU 2296  O   ARG B 126     6167   7772   7812   1603    718   -131       O  
ATOM   2297  CB  ARG B 126     -55.705 -25.891 -10.711  1.00 62.61           C  
ANISOU 2297  CB  ARG B 126     6375   8575   8838   1614    825    379       C  
ATOM   2298  CG  ARG B 126     -55.258 -26.794 -11.880  1.00 75.07           C  
ANISOU 2298  CG  ARG B 126     7206  10252  11065   1502   1051    378       C  
ATOM   2299  CD  ARG B 126     -53.872 -26.477 -12.478  1.00 78.47           C  
ANISOU 2299  CD  ARG B 126     7494  10586  11735   1128    796    574       C  
ATOM   2300  NE  ARG B 126     -52.920 -25.900 -11.533  1.00 81.94           N  
ANISOU 2300  NE  ARG B 126     8262  10928  11944    816    296    919       N  
ATOM   2301  CZ  ARG B 126     -51.752 -25.365 -11.868  1.00 75.05           C  
ANISOU 2301  CZ  ARG B 126     7371   9967  11178    465    -39   1168       C  
ATOM   2302  NH1 ARG B 126     -51.367 -25.283 -13.131  1.00 68.76           N  
ANISOU 2302  NH1 ARG B 126     6273   9141  10710    433    120   1083       N  
ATOM   2303  NH2 ARG B 126     -50.955 -24.894 -10.912  1.00 73.63           N  
ANISOU 2303  NH2 ARG B 126     7505   9721  10750    106   -558   1540       N  
ATOM   2304  N   LEU B 127     -57.529 -23.463 -11.622  1.00 60.14           N  
ANISOU 2304  N   LEU B 127     7115   8104   7633   2152   1013   -170       N  
ATOM   2305  CA  LEU B 127     -58.413 -22.783 -12.565  1.00 69.21           C  
ANISOU 2305  CA  LEU B 127     8313   9297   8688   2408   1221   -362       C  
ATOM   2306  C   LEU B 127     -57.817 -21.452 -13.009  1.00 64.82           C  
ANISOU 2306  C   LEU B 127     8257   8552   7821   2239    959   -448       C  
ATOM   2307  O   LEU B 127     -57.740 -21.158 -14.208  1.00 63.02           O  
ANISOU 2307  O   LEU B 127     7782   8407   7757   2174    957   -566       O  
ATOM   2308  CB  LEU B 127     -59.786 -22.574 -11.921  1.00 71.86           C  
ANISOU 2308  CB  LEU B 127     8939   9613   8751   2895   1569   -333       C  
ATOM   2309  CG  LEU B 127     -60.881 -21.909 -12.756  1.00 74.29           C  
ANISOU 2309  CG  LEU B 127     9226   9996   9003   3221   1832   -381       C  
ATOM   2310  CD1 LEU B 127     -61.478 -22.886 -13.754  1.00 69.67           C  
ANISOU 2310  CD1 LEU B 127     7860   9706   8906   3081   1908   -382       C  
ATOM   2311  CD2 LEU B 127     -61.960 -21.338 -11.841  1.00 81.91           C  
ANISOU 2311  CD2 LEU B 127    10722  10794   9607   3715   2182   -244       C  
ATOM   2312  N   LEU B 128     -57.377 -20.639 -12.046  1.00 58.52           N  
ANISOU 2312  N   LEU B 128     8210   7481   6542   2124    727   -388       N  
ATOM   2313  CA  LEU B 128     -56.757 -19.359 -12.371  1.00 63.36           C  
ANISOU 2313  CA  LEU B 128     9371   7874   6829   1912    452   -457       C  
ATOM   2314  C   LEU B 128     -55.496 -19.545 -13.205  1.00 58.67           C  
ANISOU 2314  C   LEU B 128     8304   7364   6622   1475    112   -389       C  
ATOM   2315  O   LEU B 128     -55.234 -18.764 -14.126  1.00 56.38           O  
ANISOU 2315  O   LEU B 128     8071   7032   6318   1402     26   -494       O  
ATOM   2316  CB  LEU B 128     -56.441 -18.598 -11.083  1.00 61.61           C  
ANISOU 2316  CB  LEU B 128    10119   7310   5980   1752    234   -384       C  
ATOM   2317  CG  LEU B 128     -57.630 -17.877 -10.444  1.00 68.66           C  
ANISOU 2317  CG  LEU B 128    11778   7954   6354   2220    660   -476       C  
ATOM   2318  CD1 LEU B 128     -57.287 -17.435  -9.038  1.00 68.99           C  
ANISOU 2318  CD1 LEU B 128    12823   7634   5757   1996    484   -405       C  
ATOM   2319  CD2 LEU B 128     -58.057 -16.686 -11.300  1.00 67.82           C  
ANISOU 2319  CD2 LEU B 128    11972   7714   6084   2439    842   -622       C  
ATOM   2320  N   ALA B 129     -54.708 -20.580 -12.908  1.00 57.93           N  
ANISOU 2320  N   ALA B 129     7720   7380   6912   1211    -37   -167       N  
ATOM   2321  CA  ALA B 129     -53.450 -20.791 -13.620  1.00 54.81           C  
ANISOU 2321  CA  ALA B 129     6861   7021   6944    831   -284     10       C  
ATOM   2322  C   ALA B 129     -53.650 -21.063 -15.107  1.00 58.71           C  
ANISOU 2322  C   ALA B 129     6815   7655   7839    951      9   -180       C  
ATOM   2323  O   ALA B 129     -52.707 -20.898 -15.888  1.00 51.43           O  
ANISOU 2323  O   ALA B 129     5663   6696   7180    702   -128    -86       O  
ATOM   2324  CB  ALA B 129     -52.677 -21.946 -12.988  1.00 57.35           C  
ANISOU 2324  CB  ALA B 129     6690   7426   7672    599   -382    374       C  
ATOM   2325  N   LEU B 130     -54.849 -21.479 -15.518  1.00 54.18           N  
ANISOU 2325  N   LEU B 130     6048   7233   7305   1294    401   -404       N  
ATOM   2326  CA  LEU B 130     -55.088 -21.769 -16.928  1.00 51.54           C  
ANISOU 2326  CA  LEU B 130     5282   7031   7269   1318    643   -576       C  
ATOM   2327  C   LEU B 130     -55.113 -20.501 -17.778  1.00 47.55           C  
ANISOU 2327  C   LEU B 130     5095   6466   6507   1318    525   -727       C  
ATOM   2328  O   LEU B 130     -54.761 -20.538 -18.967  1.00 53.82           O  
ANISOU 2328  O   LEU B 130     5616   7301   7531   1182    585   -806       O  
ATOM   2329  CB  LEU B 130     -56.402 -22.535 -17.076  1.00 60.89           C  
ANISOU 2329  CB  LEU B 130     6195   8416   8524   1596   1008   -702       C  
ATOM   2330  CG  LEU B 130     -56.382 -23.986 -16.578  1.00 67.00           C  
ANISOU 2330  CG  LEU B 130     6522   9267   9667   1576   1208   -588       C  
ATOM   2331  CD1 LEU B 130     -57.740 -24.616 -16.776  1.00 64.96           C  
ANISOU 2331  CD1 LEU B 130     6035   9206   9442   1811   1517   -694       C  
ATOM   2332  CD2 LEU B 130     -55.314 -24.790 -17.287  1.00 59.89           C  
ANISOU 2332  CD2 LEU B 130     5184   8315   9256   1284   1302   -510       C  
ATOM   2333  N   ASP B 131     -55.506 -19.373 -17.191  1.00 50.14           N  
ANISOU 2333  N   ASP B 131     6042   6659   6349   1469    400   -761       N  
ATOM   2334  CA  ASP B 131     -55.725 -18.176 -18.001  1.00 49.25           C  
ANISOU 2334  CA  ASP B 131     6218   6494   6002   1539    368   -895       C  
ATOM   2335  C   ASP B 131     -54.427 -17.619 -18.575  1.00 49.27           C  
ANISOU 2335  C   ASP B 131     6255   6367   6097   1187     54   -846       C  
ATOM   2336  O   ASP B 131     -54.399 -17.320 -19.779  1.00 49.60           O  
ANISOU 2336  O   ASP B 131     6104   6482   6260   1163    116   -954       O  
ATOM   2337  CB  ASP B 131     -56.503 -17.143 -17.190  1.00 51.53           C  
ANISOU 2337  CB  ASP B 131     7212   6604   5765   1832    432   -913       C  
ATOM   2338  CG  ASP B 131     -57.902 -17.633 -16.832  1.00 56.76           C  
ANISOU 2338  CG  ASP B 131     7746   7411   6408   2252    823   -891       C  
ATOM   2339  OD1 ASP B 131     -58.557 -17.028 -15.961  1.00 62.28           O1-
ANISOU 2339  OD1 ASP B 131     9010   7924   6729   2547    990   -842       O1-
ATOM   2340  OD2 ASP B 131     -58.338 -18.641 -17.434  1.00 69.23           O  
ANISOU 2340  OD2 ASP B 131     8684   9267   8354   2272    986   -898       O  
ATOM   2341  N   PRO B 132     -53.340 -17.451 -17.810  1.00 51.11           N  
ANISOU 2341  N   PRO B 132     6710   6421   6286    880   -301   -640       N  
ATOM   2342  CA  PRO B 132     -52.109 -16.924 -18.427  1.00 51.52           C  
ANISOU 2342  CA  PRO B 132     6712   6368   6496    540   -603   -509       C  
ATOM   2343  C   PRO B 132     -51.526 -17.847 -19.491  1.00 49.63           C  
ANISOU 2343  C   PRO B 132     5747   6256   6853    435   -414   -437       C  
ATOM   2344  O   PRO B 132     -50.887 -17.367 -20.438  1.00 49.32           O  
ANISOU 2344  O   PRO B 132     5616   6165   6959    301   -478   -420       O  
ATOM   2345  CB  PRO B 132     -51.158 -16.758 -17.230  1.00 59.40           C  
ANISOU 2345  CB  PRO B 132     8031   7193   7346    181  -1052   -194       C  
ATOM   2346  CG  PRO B 132     -51.745 -17.600 -16.142  1.00 55.15           C  
ANISOU 2346  CG  PRO B 132     7500   6720   6734    318   -919   -155       C  
ATOM   2347  CD  PRO B 132     -53.213 -17.519 -16.342  1.00 53.63           C  
ANISOU 2347  CD  PRO B 132     7440   6608   6328    796   -493   -480       C  
ATOM   2348  N   MET B 133     -51.747 -19.157 -19.376  1.00 48.67           N  
ANISOU 2348  N   MET B 133     5156   6263   7072    504   -127   -396       N  
ATOM   2349  CA  MET B 133     -51.283 -20.081 -20.407  1.00 47.49           C  
ANISOU 2349  CA  MET B 133     4437   6157   7449    425    183   -357       C  
ATOM   2350  C   MET B 133     -52.063 -19.889 -21.700  1.00 45.72           C  
ANISOU 2350  C   MET B 133     4196   6035   7140    555    450   -697       C  
ATOM   2351  O   MET B 133     -51.476 -19.872 -22.792  1.00 52.31           O  
ANISOU 2351  O   MET B 133     4863   6811   8201    425    570   -704       O  
ATOM   2352  CB  MET B 133     -51.419 -21.525 -19.923  1.00 56.34           C  
ANISOU 2352  CB  MET B 133     5144   7349   8913    470    473   -248       C  
ATOM   2353  CG  MET B 133     -50.734 -21.823 -18.600  1.00 65.56           C  
ANISOU 2353  CG  MET B 133     6278   8464  10170    329    206    141       C  
ATOM   2354  SD  MET B 133     -51.041 -23.520 -18.062  1.00 76.39           S  
ANISOU 2354  SD  MET B 133     7148   9929  11947    439    606    253       S  
ATOM   2355  CE  MET B 133     -50.535 -24.419 -19.533  1.00 71.06           C  
ANISOU 2355  CE  MET B 133     5974   9166  11860    386   1150    243       C  
ATOM   2356  N   MET B 134     -53.387 -19.758 -21.597  1.00 44.99           N  
ANISOU 2356  N   MET B 134     4265   6098   6732    798    554   -923       N  
ATOM   2357  CA  MET B 134     -54.198 -19.449 -22.770  1.00 47.85           C  
ANISOU 2357  CA  MET B 134     4615   6601   6964    871    714  -1155       C  
ATOM   2358  C   MET B 134     -53.763 -18.134 -23.397  1.00 44.97           C  
ANISOU 2358  C   MET B 134     4532   6144   6408    820    495  -1185       C  
ATOM   2359  O   MET B 134     -53.535 -18.059 -24.611  1.00 55.61           O  
ANISOU 2359  O   MET B 134     5754   7514   7862    695    594  -1274       O  
ATOM   2360  CB  MET B 134     -55.676 -19.376 -22.395  1.00 56.86           C  
ANISOU 2360  CB  MET B 134     5850   7930   7825   1156    811  -1238       C  
ATOM   2361  CG  MET B 134     -56.596 -19.181 -23.605  1.00 51.12           C  
ANISOU 2361  CG  MET B 134     5012   7413   6998   1172    938  -1365       C  
ATOM   2362  SD  MET B 134     -58.357 -19.164 -23.194  1.00 64.41           S  
ANISOU 2362  SD  MET B 134     6658   9349   8466   1507   1070  -1284       S  
ATOM   2363  CE  MET B 134     -58.417 -17.774 -22.068  1.00 61.79           C  
ANISOU 2363  CE  MET B 134     6900   8803   7776   1851    950  -1180       C  
ATOM   2364  N   GLU B 135     -53.634 -17.085 -22.573  1.00 45.43           N  
ANISOU 2364  N   GLU B 135     5035   6069   6158    894    215  -1114       N  
ATOM   2365  CA  GLU B 135     -53.280 -15.763 -23.085  1.00 48.62           C  
ANISOU 2365  CA  GLU B 135     5764   6357   6351    854     11  -1142       C  
ATOM   2366  C   GLU B 135     -51.945 -15.801 -23.825  1.00 45.85           C  
ANISOU 2366  C   GLU B 135     5192   5896   6334    559    -94  -1024       C  
ATOM   2367  O   GLU B 135     -51.772 -15.124 -24.846  1.00 55.97           O  
ANISOU 2367  O   GLU B 135     6504   7170   7592    522   -102  -1099       O  
ATOM   2368  CB  GLU B 135     -53.240 -14.741 -21.940  1.00 48.03           C  
ANISOU 2368  CB  GLU B 135     6312   6069   5868    910   -248  -1076       C  
ATOM   2369  CG  GLU B 135     -54.627 -14.248 -21.429  1.00 59.85           C  
ANISOU 2369  CG  GLU B 135     8174   7592   6976   1299    -41  -1170       C  
ATOM   2370  CD  GLU B 135     -54.629 -13.749 -19.966  1.00 70.60           C  
ANISOU 2370  CD  GLU B 135    10202   8684   7938   1343   -164  -1101       C  
ATOM   2371  OE1 GLU B 135     -55.731 -13.577 -19.382  1.00 61.17           O  
ANISOU 2371  OE1 GLU B 135     9292   7468   6483   1699    107  -1122       O  
ATOM   2372  OE2 GLU B 135     -53.534 -13.533 -19.391  1.00 67.72           O1-
ANISOU 2372  OE2 GLU B 135    10103   8118   7511   1002   -524   -983       O1-
ATOM   2373  N   GLN B 136     -50.996 -16.598 -23.330  1.00 46.51           N  
ANISOU 2373  N   GLN B 136     5016   5892   6764    366   -142   -780       N  
ATOM   2374  CA  GLN B 136     -49.692 -16.728 -23.978  1.00 49.85           C  
ANISOU 2374  CA  GLN B 136     5153   6186   7600    126   -164   -543       C  
ATOM   2375  C   GLN B 136     -49.808 -17.383 -25.351  1.00 56.19           C  
ANISOU 2375  C   GLN B 136     5641   7047   8664    143    276   -703       C  
ATOM   2376  O   GLN B 136     -49.154 -16.949 -26.312  1.00 57.93           O  
ANISOU 2376  O   GLN B 136     5823   7172   9016     46    309   -661       O  
ATOM   2377  CB  GLN B 136     -48.759 -17.531 -23.076  1.00 51.21           C  
ANISOU 2377  CB  GLN B 136     5046   6274   8139    -54   -258   -139       C  
ATOM   2378  CG  GLN B 136     -47.413 -17.863 -23.690  1.00 72.45           C  
ANISOU 2378  CG  GLN B 136     7319   8823  11387   -252   -170    246       C  
ATOM   2379  CD  GLN B 136     -46.574 -18.743 -22.783  1.00 88.51           C  
ANISOU 2379  CD  GLN B 136     8977  10807  13847   -405   -220    752       C  
ATOM   2380  OE1 GLN B 136     -46.674 -18.663 -21.554  1.00 85.64           O  
ANISOU 2380  OE1 GLN B 136     8794  10484  13260   -493   -574    885       O  
ATOM   2381  NE2 GLN B 136     -45.749 -19.599 -23.384  1.00 87.07           N  
ANISOU 2381  NE2 GLN B 136     8286  10516  14280   -435    174   1074       N  
ATOM   2382  N   GLU B 137     -50.625 -18.436 -25.458  1.00 51.54           N  
ANISOU 2382  N   GLU B 137     4871   6588   8124    234    620   -877       N  
ATOM   2383  CA  GLU B 137     -50.838 -19.111 -26.734  1.00 53.83           C  
ANISOU 2383  CA  GLU B 137     5000   6900   8551    170   1039  -1062       C  
ATOM   2384  C   GLU B 137     -51.567 -18.221 -27.736  1.00 53.92           C  
ANISOU 2384  C   GLU B 137     5241   7051   8197    194    976  -1318       C  
ATOM   2385  O   GLU B 137     -51.244 -18.233 -28.930  1.00 56.38           O  
ANISOU 2385  O   GLU B 137     5543   7298   8579     60   1178  -1395       O  
ATOM   2386  CB  GLU B 137     -51.624 -20.403 -26.518  1.00 53.42           C  
ANISOU 2386  CB  GLU B 137     4774   6951   8573    200   1359  -1180       C  
ATOM   2387  CG  GLU B 137     -50.905 -21.423 -25.656  1.00 65.62           C  
ANISOU 2387  CG  GLU B 137     6035   8358  10539    180   1510   -902       C  
ATOM   2388  CD  GLU B 137     -51.547 -22.794 -25.722  1.00 73.64           C  
ANISOU 2388  CD  GLU B 137     6878   9411  11688    172   1932  -1033       C  
ATOM   2389  OE1 GLU B 137     -52.346 -23.033 -26.650  1.00 77.83           O  
ANISOU 2389  OE1 GLU B 137     7519  10031  12022     89   2133  -1323       O  
ATOM   2390  OE2 GLU B 137     -51.265 -23.627 -24.834  1.00 79.86           O1-
ANISOU 2390  OE2 GLU B 137     7435  10145  12763    212   2039   -823       O1-
ATOM   2391  N   ILE B 138     -52.577 -17.474 -27.288  1.00 50.84           N  
ANISOU 2391  N   ILE B 138     5060   6837   7421    374    749  -1416       N  
ATOM   2392  CA  ILE B 138     -53.265 -16.575 -28.210  1.00 53.14           C  
ANISOU 2392  CA  ILE B 138     5508   7276   7406    413    689  -1559       C  
ATOM   2393  C   ILE B 138     -52.325 -15.473 -28.684  1.00 51.57           C  
ANISOU 2393  C   ILE B 138     5475   6913   7208    355    498  -1492       C  
ATOM   2394  O   ILE B 138     -52.299 -15.139 -29.873  1.00 59.23           O  
ANISOU 2394  O   ILE B 138     6453   7923   8128    260    574  -1580       O  
ATOM   2395  CB  ILE B 138     -54.546 -16.003 -27.573  1.00 59.40           C  
ANISOU 2395  CB  ILE B 138     6453   8256   7858    681    575  -1570       C  
ATOM   2396  CG1 ILE B 138     -55.317 -17.095 -26.835  1.00 55.83           C  
ANISOU 2396  CG1 ILE B 138     5818   7928   7465    761    731  -1562       C  
ATOM   2397  CG2 ILE B 138     -55.414 -15.332 -28.626  1.00 58.30           C  
ANISOU 2397  CG2 ILE B 138     6335   8334   7482    707    580  -1625       C  
ATOM   2398  CD1 ILE B 138     -56.783 -16.746 -26.581  1.00 61.74           C  
ANISOU 2398  CD1 ILE B 138     6596   8913   7949   1018    746  -1514       C  
ATOM   2399  N   GLU B 139     -51.526 -14.908 -27.772  1.00 46.64           N  
ANISOU 2399  N   GLU B 139     5001   6098   6621    366    227  -1312       N  
ATOM   2400  CA  GLU B 139     -50.605 -13.837 -28.150  1.00 53.35           C  
ANISOU 2400  CA  GLU B 139     6012   6781   7480    273     -1  -1204       C  
ATOM   2401  C   GLU B 139     -49.616 -14.291 -29.226  1.00 52.68           C  
ANISOU 2401  C   GLU B 139     5656   6585   7775     89    214  -1116       C  
ATOM   2402  O   GLU B 139     -49.294 -13.523 -30.141  1.00 53.52           O  
ANISOU 2402  O   GLU B 139     5842   6650   7843     49    181  -1137       O  
ATOM   2403  CB  GLU B 139     -49.874 -13.317 -26.910  1.00 49.50           C  
ANISOU 2403  CB  GLU B 139     5753   6097   6958    200   -373   -974       C  
ATOM   2404  CG  GLU B 139     -48.662 -12.430 -27.204  1.00 61.42           C  
ANISOU 2404  CG  GLU B 139     7348   7404   8585      1   -653   -756       C  
ATOM   2405  CD  GLU B 139     -49.020 -10.968 -27.358  1.00 75.91           C  
ANISOU 2405  CD  GLU B 139     9646   9186  10010     86   -862   -884       C  
ATOM   2406  OE1 GLU B 139     -50.109 -10.674 -27.903  1.00 77.21           O  
ANISOU 2406  OE1 GLU B 139     9894   9513   9930    316   -665  -1127       O  
ATOM   2407  OE2 GLU B 139     -48.215 -10.112 -26.924  1.00 80.42           O1-
ANISOU 2407  OE2 GLU B 139    10497   9548  10512    -98  -1227   -697       O1-
ATOM   2408  N  AGLU B 140     -49.124 -15.530 -29.128  0.43 54.08           N  
ANISOU 2408  N  AGLU B 140     5532   6683   8334      1    492   -993       N  
ATOM   2409  N  BGLU B 140     -49.123 -15.529 -29.135  0.57 54.07           N  
ANISOU 2409  N  BGLU B 140     5530   6680   8332      0    493   -993       N  
ATOM   2410  CA AGLU B 140     -48.295 -16.089 -30.193  0.43 55.07           C  
ANISOU 2410  CA AGLU B 140     5455   6644   8826   -122    869   -902       C  
ATOM   2411  CA BGLU B 140     -48.288 -16.065 -30.207  0.57 55.05           C  
ANISOU 2411  CA BGLU B 140     5456   6640   8820   -123    865   -902       C  
ATOM   2412  C  AGLU B 140     -49.028 -16.069 -31.527  0.43 53.75           C  
ANISOU 2412  C  AGLU B 140     5427   6590   8405   -157   1124  -1229       C  
ATOM   2413  C  BGLU B 140     -49.030 -16.063 -31.536  0.57 53.75           C  
ANISOU 2413  C  BGLU B 140     5429   6591   8404   -157   1124  -1231       C  
ATOM   2414  O  AGLU B 140     -48.442 -15.733 -32.565  0.43 50.29           O  
ANISOU 2414  O  AGLU B 140     5031   6028   8048   -236   1270  -1207       O  
ATOM   2415  O  BGLU B 140     -48.451 -15.735 -32.580  0.57 50.45           O  
ANISOU 2415  O  BGLU B 140     5053   6049   8065   -236   1273  -1211       O  
ATOM   2416  CB AGLU B 140     -47.888 -17.521 -29.850  0.43 60.56           C  
ANISOU 2416  CB AGLU B 140     5852   7216   9944   -162   1251   -732       C  
ATOM   2417  CB BGLU B 140     -47.828 -17.483 -29.879  0.57 60.59           C  
ANISOU 2417  CB BGLU B 140     5854   7210   9959   -165   1248   -719       C  
ATOM   2418  CG AGLU B 140     -47.079 -17.684 -28.579  0.43 65.28           C  
ANISOU 2418  CG AGLU B 140     6236   7721  10846   -184   1006   -308       C  
ATOM   2419  CG BGLU B 140     -46.904 -18.058 -30.946  0.57 54.19           C  
ANISOU 2419  CG BGLU B 140     4899   6134   9558   -247   1765   -567       C  
ATOM   2420  CD AGLU B 140     -46.844 -19.146 -28.242  0.43 68.82           C  
ANISOU 2420  CD AGLU B 140     6358   8076  11713   -182   1437   -132       C  
ATOM   2421  CD BGLU B 140     -46.407 -19.448 -30.618  0.57 66.35           C  
ANISOU 2421  CD BGLU B 140     6148   7482  11580   -249   2244   -325       C  
ATOM   2422  OE1AGLU B 140     -46.937 -19.987 -29.161  0.43 71.19           O  
ANISOU 2422  OE1AGLU B 140     6621   8266  12164   -189   2002   -278       O  
ATOM   2423  OE1BGLU B 140     -46.806 -19.996 -29.570  0.57 70.62           O  
ANISOU 2423  OE1BGLU B 140     6567   8135  12129   -206   2130   -294       O  
ATOM   2424  OE2AGLU B 140     -46.584 -19.455 -27.059  0.43 68.99           O1-
ANISOU 2424  OE2AGLU B 140     6210   8117  11887   -193   1226    153       O1-
ATOM   2425  OE2BGLU B 140     -45.621 -19.994 -31.420  0.57 68.25           O1-
ANISOU 2425  OE2BGLU B 140     6300   7432  12200   -273   2789   -145       O1-
ATOM   2426  N   ILE B 141     -50.307 -16.450 -31.519  1.00 51.94           N  
ANISOU 2426  N   ILE B 141     5264   6602   7870   -130   1171  -1488       N  
ATOM   2427  CA  ILE B 141     -51.114 -16.412 -32.733  1.00 50.61           C  
ANISOU 2427  CA  ILE B 141     5230   6599   7401   -250   1310  -1735       C  
ATOM   2428  C   ILE B 141     -51.250 -14.982 -33.233  1.00 49.46           C  
ANISOU 2428  C   ILE B 141     5245   6556   6990   -182   1009  -1746       C  
ATOM   2429  O   ILE B 141     -51.117 -14.712 -34.433  1.00 51.72           O  
ANISOU 2429  O   ILE B 141     5631   6836   7186   -321   1125  -1823       O  
ATOM   2430  CB  ILE B 141     -52.497 -17.038 -32.478  1.00 57.17           C  
ANISOU 2430  CB  ILE B 141     6033   7707   7982   -261   1322  -1889       C  
ATOM   2431  CG1 ILE B 141     -52.351 -18.488 -32.017  1.00 63.82           C  
ANISOU 2431  CG1 ILE B 141     6730   8423   9094   -338   1652  -1889       C  
ATOM   2432  CG2 ILE B 141     -53.358 -16.931 -33.733  1.00 57.25           C  
ANISOU 2432  CG2 ILE B 141     6170   7934   7649   -476   1361  -2052       C  
ATOM   2433  CD1 ILE B 141     -53.659 -19.115 -31.593  1.00 62.21           C  
ANISOU 2433  CD1 ILE B 141     6459   8483   8693   -340   1627  -1986       C  
ATOM   2434  N   ARG B 142     -51.532 -14.044 -32.321  1.00 46.89           N  
ANISOU 2434  N   ARG B 142     5001   6300   6517     29    656  -1666       N  
ATOM   2435  CA  ARG B 142     -51.734 -12.663 -32.751  1.00 52.10           C  
ANISOU 2435  CA  ARG B 142     5842   7028   6926    124    422  -1664       C  
ATOM   2436  C   ARG B 142     -50.464 -12.088 -33.365  1.00 47.95           C  
ANISOU 2436  C   ARG B 142     5352   6266   6600     28    393  -1559       C  
ATOM   2437  O   ARG B 142     -50.521 -11.397 -34.388  1.00 51.35           O  
ANISOU 2437  O   ARG B 142     5863   6755   6892     -6    389  -1610       O  
ATOM   2438  CB  ARG B 142     -52.212 -11.787 -31.588  1.00 45.11           C  
ANISOU 2438  CB  ARG B 142     5152   6153   5833    375    150  -1594       C  
ATOM   2439  CG  ARG B 142     -53.353 -12.395 -30.796  1.00 51.47           C  
ANISOU 2439  CG  ARG B 142     5903   7141   6513    522    221  -1622       C  
ATOM   2440  CD  ARG B 142     -54.011 -11.368 -29.876  1.00 58.18           C  
ANISOU 2440  CD  ARG B 142     7046   7972   7088    820     75  -1548       C  
ATOM   2441  NE  ARG B 142     -55.390 -11.752 -29.602  1.00 59.91           N  
ANISOU 2441  NE  ARG B 142     7149   8441   7172   1007    220  -1517       N  
ATOM   2442  CZ  ARG B 142     -56.447 -11.250 -30.225  1.00 66.95           C  
ANISOU 2442  CZ  ARG B 142     7965   9579   7896   1134    280  -1428       C  
ATOM   2443  NH1 ARG B 142     -56.320 -10.360 -31.200  1.00 60.44           N  
ANISOU 2443  NH1 ARG B 142     7184   8794   6988   1094    216  -1405       N  
ATOM   2444  NH2 ARG B 142     -57.661 -11.664 -29.874  1.00 69.10           N  
ANISOU 2444  NH2 ARG B 142     8068  10077   8111   1299    404  -1299       N  
ATOM   2445  N   GLN B 143     -49.305 -12.379 -32.771  1.00 44.83           N  
ANISOU 2445  N   GLN B 143     4859   5617   6558    -26    370  -1352       N  
ATOM   2446  CA  GLN B 143     -48.061 -11.825 -33.295  1.00 45.68           C  
ANISOU 2446  CA  GLN B 143     4938   5498   6922   -112    330  -1148       C  
ATOM   2447  C   GLN B 143     -47.698 -12.455 -34.634  1.00 46.37           C  
ANISOU 2447  C   GLN B 143     4933   5506   7181   -230    778  -1198       C  
ATOM   2448  O   GLN B 143     -47.157 -11.776 -35.516  1.00 51.66           O  
ANISOU 2448  O   GLN B 143     5658   6086   7885   -261    798  -1142       O  
ATOM   2449  CB  GLN B 143     -46.929 -12.020 -32.290  1.00 50.91           C  
ANISOU 2449  CB  GLN B 143     5450   5937   7956   -182    161   -786       C  
ATOM   2450  CG  GLN B 143     -46.982 -11.092 -31.096  1.00 55.79           C  
ANISOU 2450  CG  GLN B 143     6322   6535   8340   -165   -341   -699       C  
ATOM   2451  CD  GLN B 143     -45.668 -11.068 -30.345  1.00 57.89           C  
ANISOU 2451  CD  GLN B 143     6454   6582   8958   -364   -617   -245       C  
ATOM   2452  OE1 GLN B 143     -44.742 -11.815 -30.667  1.00 58.12           O  
ANISOU 2452  OE1 GLN B 143     6106   6492   9485   -453   -386     62       O  
ATOM   2453  NE2 GLN B 143     -45.570 -10.194 -29.353  1.00 55.15           N  
ANISOU 2453  NE2 GLN B 143     6440   6161   8352   -459  -1096   -150       N  
ATOM   2454  N   LYS B 144     -47.992 -13.746 -34.802  1.00 46.93           N  
ANISOU 2454  N   LYS B 144     4922   5574   7335   -307   1171  -1308       N  
ATOM   2455  CA  LYS B 144     -47.755 -14.405 -36.081  1.00 56.17           C  
ANISOU 2455  CA  LYS B 144     6168   6608   8567   -457   1675  -1405       C  
ATOM   2456  C   LYS B 144     -48.566 -13.748 -37.193  1.00 50.15           C  
ANISOU 2456  C   LYS B 144     5647   6064   7342   -553   1602  -1658       C  
ATOM   2457  O   LYS B 144     -48.063 -13.549 -38.307  1.00 53.41           O  
ANISOU 2457  O   LYS B 144     6196   6337   7761   -650   1835  -1663       O  
ATOM   2458  CB  LYS B 144     -48.087 -15.897 -35.973  1.00 58.82           C  
ANISOU 2458  CB  LYS B 144     6478   6882   8988   -559   2104  -1516       C  
ATOM   2459  CG  LYS B 144     -48.118 -16.606 -37.314  1.00 59.12           C  
ANISOU 2459  CG  LYS B 144     6786   6763   8915   -784   2650  -1708       C  
ATOM   2460  CD  LYS B 144     -48.304 -18.126 -37.174  1.00 62.68           C  
ANISOU 2460  CD  LYS B 144     7280   7053   9482   -905   3146  -1798       C  
ATOM   2461  CE  LYS B 144     -49.772 -18.521 -37.204  1.00 74.46           C  
ANISOU 2461  CE  LYS B 144     8924   8880  10489  -1103   2977  -2118       C  
ATOM   2462  NZ  LYS B 144     -50.029 -19.708 -36.345  1.00 62.22           N  
ANISOU 2462  NZ  LYS B 144     7236   7281   9124  -1093   3178  -2119       N  
ATOM   2463  N   TYR B 145     -49.815 -13.391 -36.905  1.00 46.97           N  
ANISOU 2463  N   TYR B 145     5287   6006   6555   -519   1294  -1811       N  
ATOM   2464  CA  TYR B 145     -50.652 -12.763 -37.917  1.00 49.50           C  
ANISOU 2464  CA  TYR B 145     5759   6587   6462   -626   1184  -1945       C  
ATOM   2465  C   TYR B 145     -50.343 -11.280 -38.098  1.00 52.51           C  
ANISOU 2465  C   TYR B 145     6175   6986   6792   -464    884  -1830       C  
ATOM   2466  O   TYR B 145     -50.573 -10.737 -39.184  1.00 51.85           O  
ANISOU 2466  O   TYR B 145     6204   7020   6479   -569    880  -1876       O  
ATOM   2467  CB  TYR B 145     -52.124 -12.944 -37.569  1.00 47.21           C  
ANISOU 2467  CB  TYR B 145     5419   6667   5851   -638   1001  -2022       C  
ATOM   2468  CG  TYR B 145     -52.676 -14.254 -38.078  1.00 57.33           C  
ANISOU 2468  CG  TYR B 145     6772   8007   7002   -965   1280  -2179       C  
ATOM   2469  CD1 TYR B 145     -52.532 -15.428 -37.343  1.00 56.51           C  
ANISOU 2469  CD1 TYR B 145     6593   7753   7126   -976   1511  -2216       C  
ATOM   2470  CD2 TYR B 145     -53.281 -14.332 -39.328  1.00 64.44           C  
ANISOU 2470  CD2 TYR B 145     7863   9086   7535  -1316   1317  -2275       C  
ATOM   2471  CE1 TYR B 145     -53.029 -16.636 -37.820  1.00 56.07           C  
ANISOU 2471  CE1 TYR B 145     6672   7702   6929  -1311   1792  -2374       C  
ATOM   2472  CE2 TYR B 145     -53.769 -15.529 -39.814  1.00 65.57           C  
ANISOU 2472  CE2 TYR B 145     8181   9242   7492  -1711   1550  -2425       C  
ATOM   2473  CZ  TYR B 145     -53.643 -16.677 -39.059  1.00 72.60           C  
ANISOU 2473  CZ  TYR B 145     9021   9953   8612  -1701   1804  -2489       C  
ATOM   2474  OH  TYR B 145     -54.137 -17.861 -39.561  1.00 72.86           O  
ANISOU 2474  OH  TYR B 145     9295   9958   8432  -2129   2053  -2650       O  
ATOM   2475  N   GLN B 146     -49.852 -10.596 -37.064  1.00 46.78           N  
ANISOU 2475  N   GLN B 146     5396   6141   6236   -247    620  -1674       N  
ATOM   2476  CA  GLN B 146     -49.457  -9.207 -37.281  1.00 45.84           C  
ANISOU 2476  CA  GLN B 146     5373   5972   6073   -136    369  -1568       C  
ATOM   2477  C   GLN B 146     -48.252  -9.143 -38.212  1.00 46.74           C  
ANISOU 2477  C   GLN B 146     5472   5838   6448   -248    565  -1466       C  
ATOM   2478  O   GLN B 146     -48.110  -8.188 -38.989  1.00 48.24           O  
ANISOU 2478  O   GLN B 146     5747   6048   6534   -232    480  -1442       O  
ATOM   2479  CB  GLN B 146     -49.162  -8.509 -35.954  1.00 46.93           C  
ANISOU 2479  CB  GLN B 146     5580   5979   6271     32     38  -1427       C  
ATOM   2480  CG  GLN B 146     -50.400  -8.285 -35.084  1.00 52.26           C  
ANISOU 2480  CG  GLN B 146     6362   6851   6642    218    -99  -1501       C  
ATOM   2481  CD  GLN B 146     -51.269  -7.112 -35.530  1.00 64.09           C  
ANISOU 2481  CD  GLN B 146     7997   8528   7825    383   -194  -1505       C  
ATOM   2482  OE1 GLN B 146     -51.247  -6.707 -36.694  1.00 59.03           O  
ANISOU 2482  OE1 GLN B 146     7319   7984   7128    309   -145  -1512       O  
ATOM   2483  NE2 GLN B 146     -52.046  -6.561 -34.591  1.00 63.65           N  
ANISOU 2483  NE2 GLN B 146     8118   8496   7569    624   -286  -1466       N  
ATOM   2484  N   CYS B 147     -47.407 -10.176 -38.163  1.00 47.51           N  
ANISOU 2484  N   CYS B 147     5451   5690   6910   -336    882  -1367       N  
ATOM   2485  CA  CYS B 147     -46.280 -10.304 -39.078  1.00 49.05           C  
ANISOU 2485  CA  CYS B 147     5624   5603   7411   -405   1219  -1210       C  
ATOM   2486  C   CYS B 147     -46.736 -10.319 -40.532  1.00 57.94           C  
ANISOU 2486  C   CYS B 147     6982   6816   8216   -552   1489  -1433       C  
ATOM   2487  O   CYS B 147     -46.022  -9.825 -41.415  1.00 58.43           O  
ANISOU 2487  O   CYS B 147     7108   6718   8376   -559   1634  -1329       O  
ATOM   2488  CB  CYS B 147     -45.517 -11.587 -38.760  1.00 50.34           C  
ANISOU 2488  CB  CYS B 147     5622   5486   8018   -441   1643  -1034       C  
ATOM   2489  SG  CYS B 147     -44.078 -11.325 -37.742  1.00 63.62           S  
ANISOU 2489  SG  CYS B 147     6963   6902  10308   -355   1434   -483       S  
ATOM   2490  N   LYS B 148     -47.906 -10.893 -40.801  1.00 50.07           N  
ANISOU 2490  N   LYS B 148     6123   6074   6828   -706   1544  -1702       N  
ATOM   2491  CA  LYS B 148     -48.455 -10.939 -42.149  1.00 52.80           C  
ANISOU 2491  CA  LYS B 148     6739   6547   6774   -956   1715  -1890       C  
ATOM   2492  C   LYS B 148     -49.300  -9.709 -42.474  1.00 57.08           C  
ANISOU 2492  C   LYS B 148     7277   7460   6953   -917   1277  -1897       C  
ATOM   2493  O   LYS B 148     -49.325  -9.275 -43.630  1.00 55.33           O  
ANISOU 2493  O   LYS B 148     7226   7294   6500  -1066   1334  -1926       O  
ATOM   2494  CB  LYS B 148     -49.299 -12.205 -42.319  1.00 55.71           C  
ANISOU 2494  CB  LYS B 148     7273   7009   6883  -1242   1949  -2111       C  
ATOM   2495  CG  LYS B 148     -48.761 -13.423 -41.565  1.00 66.28           C  
ANISOU 2495  CG  LYS B 148     8535   8050   8600  -1201   2312  -2082       C  
ATOM   2496  CD  LYS B 148     -49.760 -14.580 -41.594  1.00 73.49           C  
ANISOU 2496  CD  LYS B 148     9610   9093   9220  -1488   2459  -2309       C  
ATOM   2497  CE  LYS B 148     -49.288 -15.762 -40.750  1.00 68.17           C  
ANISOU 2497  CE  LYS B 148     8822   8136   8942  -1409   2818  -2262       C  
ATOM   2498  NZ  LYS B 148     -49.232 -17.055 -41.505  1.00 80.75           N  
ANISOU 2498  NZ  LYS B 148    10816   9428  10436  -1729   3452  -2442       N  
ATOM   2499  N   ARG B 149     -49.980  -9.122 -41.480  1.00 49.33           N  
ANISOU 2499  N   ARG B 149     6121   6702   5918   -704    887  -1835       N  
ATOM   2500  CA  ARG B 149     -50.861  -7.985 -41.743  1.00 49.26           C  
ANISOU 2500  CA  ARG B 149     6088   7020   5606   -616    564  -1772       C  
ATOM   2501  C   ARG B 149     -50.090  -6.689 -41.952  1.00 48.84           C  
ANISOU 2501  C   ARG B 149     6056   6821   5681   -428    423  -1638       C  
ATOM   2502  O   ARG B 149     -50.420  -5.904 -42.849  1.00 52.06           O  
ANISOU 2502  O   ARG B 149     6505   7405   5868   -461    342  -1594       O  
ATOM   2503  CB  ARG B 149     -51.850  -7.779 -40.596  1.00 49.22           C  
ANISOU 2503  CB  ARG B 149     5949   7230   5522   -398    317  -1708       C  
ATOM   2504  CG  ARG B 149     -52.885  -8.829 -40.434  1.00 48.98           C  
ANISOU 2504  CG  ARG B 149     5844   7441   5324   -566    373  -1774       C  
ATOM   2505  CD  ARG B 149     -53.819  -8.491 -39.253  1.00 48.34           C  
ANISOU 2505  CD  ARG B 149     5624   7533   5210   -266    180  -1645       C  
ATOM   2506  NE  ARG B 149     -54.771  -7.421 -39.549  1.00 49.42           N  
ANISOU 2506  NE  ARG B 149     5681   7965   5133   -116      7  -1430       N  
ATOM   2507  CZ  ARG B 149     -54.701  -6.170 -39.100  1.00 51.36           C  
ANISOU 2507  CZ  ARG B 149     5992   8115   5406    227    -95  -1296       C  
ATOM   2508  NH1 ARG B 149     -53.749  -5.779 -38.268  1.00 47.90           N  
ANISOU 2508  NH1 ARG B 149     5738   7309   5152    408   -125  -1366       N  
ATOM   2509  NH2 ARG B 149     -55.622  -5.289 -39.486  1.00 50.72           N  
ANISOU 2509  NH2 ARG B 149     5807   8304   5161    366   -166  -1044       N  
ATOM   2510  N   GLN B 150     -49.096  -6.422 -41.107  1.00 47.92           N  
ANISOU 2510  N   GLN B 150     5902   6399   5908   -258    354  -1533       N  
ATOM   2511  CA  GLN B 150     -48.468  -5.105 -41.129  1.00 47.79           C  
ANISOU 2511  CA  GLN B 150     5926   6247   5985   -103    140  -1383       C  
ATOM   2512  C   GLN B 150     -47.748  -4.800 -42.432  1.00 48.80           C  
ANISOU 2512  C   GLN B 150     6091   6274   6176   -207    316  -1336       C  
ATOM   2513  O   GLN B 150     -47.839  -3.647 -42.888  1.00 54.89           O  
ANISOU 2513  O   GLN B 150     6907   7120   6828   -114    149  -1267       O  
ATOM   2514  CB  GLN B 150     -47.529  -4.938 -39.928  1.00 55.60           C  
ANISOU 2514  CB  GLN B 150     6897   6932   7298    -14    -40  -1226       C  
ATOM   2515  CG  GLN B 150     -48.261  -4.755 -38.599  1.00 51.45           C  
ANISOU 2515  CG  GLN B 150     6464   6472   6613    130   -276  -1257       C  
ATOM   2516  CD  GLN B 150     -49.147  -3.514 -38.571  1.00 65.11           C  
ANISOU 2516  CD  GLN B 150     8369   8346   8023    331   -442  -1262       C  
ATOM   2517  OE1 GLN B 150     -48.801  -2.471 -39.126  1.00 59.46           O  
ANISOU 2517  OE1 GLN B 150     7738   7560   7293    375   -528  -1184       O  
ATOM   2518  NE2 GLN B 150     -50.294  -3.623 -37.903  1.00 69.27           N  
ANISOU 2518  NE2 GLN B 150     8941   9052   8326    481   -441  -1312       N  
ATOM   2519  N   PRO B 151     -47.043  -5.737 -43.078  1.00 56.13           N  
ANISOU 2519  N   PRO B 151     7036   7006   7285   -372    697  -1351       N  
ATOM   2520  CA  PRO B 151     -46.489  -5.422 -44.403  1.00 59.41           C  
ANISOU 2520  CA  PRO B 151     7561   7323   7691   -457    927  -1313       C  
ATOM   2521  C   PRO B 151     -47.556  -5.039 -45.405  1.00 60.83           C  
ANISOU 2521  C   PRO B 151     7881   7862   7371   -598    858  -1450       C  
ATOM   2522  O   PRO B 151     -47.317  -4.181 -46.266  1.00 59.96           O  
ANISOU 2522  O   PRO B 151     7825   7769   7187   -583    832  -1374       O  
ATOM   2523  CB  PRO B 151     -45.785  -6.726 -44.787  1.00 60.65           C  
ANISOU 2523  CB  PRO B 151     7796   7177   8071   -601   1468  -1325       C  
ATOM   2524  CG  PRO B 151     -45.323  -7.250 -43.477  1.00 58.96           C  
ANISOU 2524  CG  PRO B 151     7360   6798   8246   -487   1408  -1183       C  
ATOM   2525  CD  PRO B 151     -46.505  -7.013 -42.577  1.00 50.18           C  
ANISOU 2525  CD  PRO B 151     6214   6022   6830   -438    991  -1334       C  
ATOM   2526  N   ILE B 152     -48.743  -5.637 -45.296  1.00 53.97           N  
ANISOU 2526  N   ILE B 152     7037   7300   6169   -751    799  -1593       N  
ATOM   2527  CA  ILE B 152     -49.822  -5.334 -46.229  1.00 60.45           C  
ANISOU 2527  CA  ILE B 152     7932   8517   6519   -959    673  -1615       C  
ATOM   2528  C   ILE B 152     -50.392  -3.952 -45.953  1.00 62.53           C  
ANISOU 2528  C   ILE B 152     8011   9026   6722   -690    304  -1429       C  
ATOM   2529  O   ILE B 152     -50.631  -3.158 -46.873  1.00 55.50           O  
ANISOU 2529  O   ILE B 152     7134   8320   5633   -737    218  -1323       O  
ATOM   2530  CB  ILE B 152     -50.904  -6.417 -46.140  1.00 55.48           C  
ANISOU 2530  CB  ILE B 152     7341   8144   5595  -1246    683  -1732       C  
ATOM   2531  CG1 ILE B 152     -50.234  -7.785 -46.251  1.00 60.01           C  
ANISOU 2531  CG1 ILE B 152     8149   8369   6283  -1460   1129  -1922       C  
ATOM   2532  CG2 ILE B 152     -51.973  -6.191 -47.201  1.00 63.52           C  
ANISOU 2532  CG2 ILE B 152     8423   9592   6119  -1578    510  -1661       C  
ATOM   2533  CD1 ILE B 152     -51.136  -8.866 -46.665  1.00 64.82           C  
ANISOU 2533  CD1 ILE B 152     8966   9161   6501  -1898   1217  -2072       C  
ATOM   2534  N   LEU B 153     -50.620  -3.648 -44.678  1.00 57.33           N  
ANISOU 2534  N   LEU B 153     7219   8342   6220   -402    122  -1372       N  
ATOM   2535  CA  LEU B 153     -51.146  -2.344 -44.308  1.00 56.12           C  
ANISOU 2535  CA  LEU B 153     6986   8320   6018   -105   -119  -1190       C  
ATOM   2536  C   LEU B 153     -50.153  -1.246 -44.660  1.00 67.50           C  
ANISOU 2536  C   LEU B 153     8502   9514   7632     32   -159  -1110       C  
ATOM   2537  O   LEU B 153     -50.545  -0.148 -45.073  1.00 60.50           O  
ANISOU 2537  O   LEU B 153     7589   8772   6627    169   -266   -956       O  
ATOM   2538  CB  LEU B 153     -51.466  -2.336 -42.815  1.00 57.08           C  
ANISOU 2538  CB  LEU B 153     7093   8352   6242    152   -218  -1179       C  
ATOM   2539  CG  LEU B 153     -52.691  -3.160 -42.402  1.00 63.30           C  
ANISOU 2539  CG  LEU B 153     7751   9442   6859    101   -207  -1173       C  
ATOM   2540  CD1 LEU B 153     -52.605  -3.517 -40.925  1.00 54.51           C  
ANISOU 2540  CD1 LEU B 153     6690   8120   5902    293   -222  -1234       C  
ATOM   2541  CD2 LEU B 153     -53.994  -2.425 -42.711  1.00 57.73           C  
ANISOU 2541  CD2 LEU B 153     6883   9125   5928    222   -300   -900       C  
ATOM   2542  N   ASP B 154     -48.857  -1.535 -44.515  1.00 61.81           N  
ANISOU 2542  N   ASP B 154     7842   8418   7224     -3    -61  -1152       N  
ATOM   2543  CA  ASP B 154     -47.835  -0.559 -44.866  1.00 65.08           C  
ANISOU 2543  CA  ASP B 154     8293   8585   7847     90   -113  -1023       C  
ATOM   2544  C   ASP B 154     -47.755  -0.356 -46.372  1.00 64.92           C  
ANISOU 2544  C   ASP B 154     8298   8686   7683    -50     46  -1005       C  
ATOM   2545  O   ASP B 154     -47.405   0.736 -46.830  1.00 68.69           O  
ANISOU 2545  O   ASP B 154     8779   9115   8206     65    -42   -874       O  
ATOM   2546  CB  ASP B 154     -46.476  -0.998 -44.319  1.00 63.64           C  
ANISOU 2546  CB  ASP B 154     8087   7998   8094     62    -56   -949       C  
ATOM   2547  CG  ASP B 154     -46.422  -0.991 -42.801  1.00 71.45           C  
ANISOU 2547  CG  ASP B 154     9100   8847   9199    154   -296   -917       C  
ATOM   2548  OD1 ASP B 154     -47.429  -0.612 -42.160  1.00 72.30           O  
ANISOU 2548  OD1 ASP B 154     9300   9122   9048    287   -445   -985       O  
ATOM   2549  OD2 ASP B 154     -45.366  -1.363 -42.246  1.00 73.68           O  
ANISOU 2549  OD2 ASP B 154     9315   8841   9837     89   -318   -773       O  
ATOM   2550  N   ALA B 155     -48.072  -1.388 -47.156  1.00 64.61           N  
ANISOU 2550  N   ALA B 155     8329   8780   7438   -326    287  -1135       N  
ATOM   2551  CA  ALA B 155     -48.072  -1.226 -48.607  1.00 68.18           C  
ANISOU 2551  CA  ALA B 155     8907   9346   7652   -525    436  -1127       C  
ATOM   2552  C   ALA B 155     -49.232  -0.348 -49.058  1.00 75.09           C  
ANISOU 2552  C   ALA B 155     9687  10667   8177   -521    171  -1000       C  
ATOM   2553  O   ALA B 155     -49.076   0.485 -49.959  1.00 75.99           O  
ANISOU 2553  O   ALA B 155     9816  10849   8209   -514    150   -880       O  
ATOM   2554  CB  ALA B 155     -48.129  -2.591 -49.292  1.00 57.86           C  
ANISOU 2554  CB  ALA B 155     7841   8007   6136   -894    782  -1312       C  
ATOM   2555  N   ILE B 156     -50.400  -0.512 -48.434  1.00 59.20           N  
ANISOU 2555  N   ILE B 156     7539   8963   5993   -504    -10   -962       N  
ATOM   2556  CA  ILE B 156     -51.560   0.304 -48.783  1.00 66.75           C  
ANISOU 2556  CA  ILE B 156     8315  10353   6695   -461   -226   -710       C  
ATOM   2557  C   ILE B 156     -51.328   1.764 -48.408  1.00 73.85           C  
ANISOU 2557  C   ILE B 156     9131  11130   7799    -43   -329   -529       C  
ATOM   2558  O   ILE B 156     -51.635   2.675 -49.187  1.00 72.67           O  
ANISOU 2558  O   ILE B 156     8892  11184   7535     -2   -395   -310       O  
ATOM   2559  CB  ILE B 156     -52.824  -0.259 -48.108  1.00 65.85           C  
ANISOU 2559  CB  ILE B 156     8031  10556   6434   -498   -341   -626       C  
ATOM   2560  CG1 ILE B 156     -52.999  -1.742 -48.454  1.00 66.21           C  
ANISOU 2560  CG1 ILE B 156     8219  10671   6265   -961   -239   -830       C  
ATOM   2561  CG2 ILE B 156     -54.048   0.553 -48.502  1.00 70.80           C  
ANISOU 2561  CG2 ILE B 156     8387  11649   6864   -445   -526   -227       C  
ATOM   2562  CD1 ILE B 156     -54.328  -2.329 -48.022  1.00 70.05           C  
ANISOU 2562  CD1 ILE B 156     8507  11539   6571  -1092   -393   -684       C  
ATOM   2563  N   GLU B 157     -50.783   2.009 -47.213  1.00 64.97           N  
ANISOU 2563  N   GLU B 157     8074   9656   6957    237   -348   -601       N  
ATOM   2564  CA  GLU B 157     -50.563   3.380 -46.765  1.00 63.20           C  
ANISOU 2564  CA  GLU B 157     7898   9240   6874    581   -434   -456       C  
ATOM   2565  C   GLU B 157     -49.574   4.112 -47.672  1.00 78.26           C  
ANISOU 2565  C   GLU B 157     9856  10979   8902    560   -418   -412       C  
ATOM   2566  O   GLU B 157     -49.758   5.298 -47.971  1.00 77.31           O  
ANISOU 2566  O   GLU B 157     9714  10897   8765    754   -464   -223       O  
ATOM   2567  CB  GLU B 157     -50.078   3.378 -45.316  1.00 74.55           C  
ANISOU 2567  CB  GLU B 157     9513  10298   8515    753   -491   -561       C  
ATOM   2568  CG  GLU B 157     -50.255   4.702 -44.589  1.00 81.97           C  
ANISOU 2568  CG  GLU B 157    10637  11039   9470   1083   -551   -426       C  
ATOM   2569  CD  GLU B 157     -49.482   4.758 -43.283  1.00 88.81           C  
ANISOU 2569  CD  GLU B 157    11804  11456  10485   1119   -665   -537       C  
ATOM   2570  OE1 GLU B 157     -49.114   3.683 -42.759  1.00 83.45           O  
ANISOU 2570  OE1 GLU B 157    11098  10710   9900    951   -695   -674       O  
ATOM   2571  OE2 GLU B 157     -49.246   5.876 -42.777  1.00 96.98           O  
ANISOU 2571  OE2 GLU B 157    13132  12194  11522   1281   -727   -467       O  
ATOM   2572  N   ALA B 158     -48.526   3.419 -48.127  1.00 70.72           N  
ANISOU 2572  N   ALA B 158     8963   9815   8094    351   -302   -544       N  
ATOM   2573  CA  ALA B 158     -47.562   4.037 -49.035  1.00 80.70           C  
ANISOU 2573  CA  ALA B 158    10256  10907   9500    342   -238   -461       C  
ATOM   2574  C   ALA B 158     -48.224   4.461 -50.341  1.00 84.40           C  
ANISOU 2574  C   ALA B 158    10665  11744   9661    242   -209   -346       C  
ATOM   2575  O   ALA B 158     -47.933   5.540 -50.872  1.00 88.18           O  
ANISOU 2575  O   ALA B 158    11115  12189  10198    378   -248   -187       O  
ATOM   2576  CB  ALA B 158     -46.405   3.075 -49.310  1.00 76.72           C  
ANISOU 2576  CB  ALA B 158     9815  10102   9232    165     -7   -551       C  
ATOM   2577  N   LYS B 159     -49.115   3.629 -50.872  1.00 85.39           N  
ANISOU 2577  N   LYS B 159    10777  12224   9442    -37   -168   -392       N  
ATOM   2578  CA  LYS B 159     -49.859   3.967 -52.079  1.00 79.82           C  
ANISOU 2578  CA  LYS B 159    10013  11932   8383   -231   -217   -217       C  
ATOM   2579  C   LYS B 159     -50.745   5.191 -51.855  1.00 81.50           C  
ANISOU 2579  C   LYS B 159     9976  12406   8583     63   -402    103       C  
ATOM   2580  O   LYS B 159     -51.181   5.838 -52.807  1.00 79.90           O  
ANISOU 2580  O   LYS B 159     9654  12504   8198     -1   -463    354       O  
ATOM   2581  CB  LYS B 159     -50.707   2.779 -52.533  1.00 75.99           C  
ANISOU 2581  CB  LYS B 159     9598  11775   7499   -678   -212   -290       C  
ATOM   2582  CG  LYS B 159     -49.899   1.568 -52.961  1.00 73.38           C  
ANISOU 2582  CG  LYS B 159     9612  11152   7117   -994     85   -590       C  
ATOM   2583  CD  LYS B 159     -50.587   0.835 -54.100  1.00 82.68           C  
ANISOU 2583  CD  LYS B 159    11026  12645   7743  -1558    101   -609       C  
ATOM   2584  CE  LYS B 159     -50.246  -0.642 -54.102  1.00 81.70           C  
ANISOU 2584  CE  LYS B 159    11278  12252   7511  -1883    412   -926       C  
ATOM   2585  NZ  LYS B 159     -49.320  -0.998 -55.209  1.00 90.24           N  
ANISOU 2585  NZ  LYS B 159    12828  13000   8458  -2112    824  -1070       N  
TER    2586      LYS B 159                                                      
ATOM   2587  N   MET C 611     -16.622 -10.929   1.650  1.00 75.53           N  
ANISOU 2587  N   MET C 611     7781  11757   9161  -1155  -1761    755       N  
ATOM   2588  CA  MET C 611     -16.133 -10.005   0.635  1.00 62.98           C  
ANISOU 2588  CA  MET C 611     6180  10082   7666  -1271  -1550    497       C  
ATOM   2589  C   MET C 611     -17.181  -9.735  -0.441  1.00 60.30           C  
ANISOU 2589  C   MET C 611     6219   9275   7417  -1250  -1351    362       C  
ATOM   2590  O   MET C 611     -17.495 -10.618  -1.233  1.00 55.94           O  
ANISOU 2590  O   MET C 611     5804   8430   7022   -986  -1306    455       O  
ATOM   2591  CB  MET C 611     -14.859 -10.543  -0.007  1.00 65.48           C  
ANISOU 2591  CB  MET C 611     6194  10535   8151  -1039  -1522    571       C  
ATOM   2592  CG  MET C 611     -13.784  -9.496  -0.232  1.00 70.46           C  
ANISOU 2592  CG  MET C 611     6543  11479   8748  -1305  -1427    394       C  
ATOM   2593  SD  MET C 611     -13.102  -8.720   1.251  1.00 86.77           S  
ANISOU 2593  SD  MET C 611     8292  14114  10563  -1689  -1637    347       S  
ATOM   2594  CE  MET C 611     -13.179 -10.035   2.469  1.00 85.31           C  
ANISOU 2594  CE  MET C 611     7968  14161  10283  -1391  -1931    683       C  
ATOM   2595  N   PRO C 612     -17.715  -8.513  -0.470  1.00 53.80           N  
ANISOU 2595  N   PRO C 612     5576   8379   6488  -1517  -1246    135       N  
ATOM   2596  CA  PRO C 612     -18.735  -8.192  -1.470  1.00 48.94           C  
ANISOU 2596  CA  PRO C 612     5302   7362   5931  -1478  -1071     25       C  
ATOM   2597  C   PRO C 612     -18.161  -8.340  -2.867  1.00 51.74           C  
ANISOU 2597  C   PRO C 612     5646   7542   6471  -1340   -899      2       C  
ATOM   2598  O   PRO C 612     -16.969  -8.137  -3.094  1.00 54.85           O  
ANISOU 2598  O   PRO C 612     5779   8146   6916  -1390   -857    -15       O  
ATOM   2599  CB  PRO C 612     -19.097  -6.734  -1.169  1.00 54.01           C  
ANISOU 2599  CB  PRO C 612     6096   7994   6431  -1765  -1008   -219       C  
ATOM   2600  CG  PRO C 612     -18.605  -6.466   0.208  1.00 62.84           C  
ANISOU 2600  CG  PRO C 612     7006   9500   7372  -1954  -1184   -244       C  
ATOM   2601  CD  PRO C 612     -17.533  -7.449   0.534  1.00 61.91           C  
ANISOU 2601  CD  PRO C 612     6531   9679   7312  -1837  -1318    -28       C  
ATOM   2602  N   ILE C 613     -19.021  -8.721  -3.802  1.00 44.54           N  
ANISOU 2602  N   ILE C 613     4993   6299   5632  -1172   -801      1       N  
ATOM   2603  CA  ILE C 613     -18.689  -8.773  -5.219  1.00 43.74           C  
ANISOU 2603  CA  ILE C 613     4937   6032   5650  -1042   -616    -55       C  
ATOM   2604  C   ILE C 613     -19.397  -7.589  -5.867  1.00 44.61           C  
ANISOU 2604  C   ILE C 613     5313   5940   5695  -1211   -455   -205       C  
ATOM   2605  O   ILE C 613     -20.611  -7.634  -6.097  1.00 39.44           O  
ANISOU 2605  O   ILE C 613     4921   5066   4999  -1148   -448   -221       O  
ATOM   2606  CB  ILE C 613     -19.107 -10.105  -5.852  1.00 45.04           C  
ANISOU 2606  CB  ILE C 613     5217   5970   5927   -719   -644     34       C  
ATOM   2607  CG1 ILE C 613     -18.581 -11.280  -5.016  1.00 40.04           C  
ANISOU 2607  CG1 ILE C 613     4394   5459   5360   -535   -848    220       C  
ATOM   2608  CG2 ILE C 613     -18.649 -10.172  -7.307  1.00 40.89           C  
ANISOU 2608  CG2 ILE C 613     4708   5349   5479   -560   -448    -60       C  
ATOM   2609  CD1 ILE C 613     -19.065 -12.642  -5.485  1.00 45.70           C  
ANISOU 2609  CD1 ILE C 613     5295   5862   6205   -245   -922    311       C  
ATOM   2610  N   TRP C 614     -18.648  -6.511  -6.149  1.00 44.46           N  
ANISOU 2610  N   TRP C 614     5225   6004   5663  -1438   -338   -295       N  
ATOM   2611  CA  TRP C 614     -19.280  -5.283  -6.633  1.00 48.17           C  
ANISOU 2611  CA  TRP C 614     5985   6241   6076  -1608   -213   -410       C  
ATOM   2612  C   TRP C 614     -19.676  -5.372  -8.101  1.00 49.62           C  
ANISOU 2612  C   TRP C 614     6352   6206   6294  -1448    -38   -396       C  
ATOM   2613  O   TRP C 614     -20.727  -4.849  -8.490  1.00 40.72           O  
ANISOU 2613  O   TRP C 614     5520   4841   5110  -1426     12   -440       O  
ATOM   2614  CB  TRP C 614     -18.363  -4.084  -6.401  1.00 41.00           C  
ANISOU 2614  CB  TRP C 614     4990   5439   5150  -1964   -171   -489       C  
ATOM   2615  CG  TRP C 614     -18.346  -3.650  -4.972  1.00 51.16           C  
ANISOU 2615  CG  TRP C 614     6227   6871   6342  -2163   -345   -580       C  
ATOM   2616  CD1 TRP C 614     -17.435  -3.990  -4.014  1.00 53.61           C  
ANISOU 2616  CD1 TRP C 614     6200   7547   6624  -2266   -492   -550       C  
ATOM   2617  CD2 TRP C 614     -19.324  -2.823  -4.323  1.00 54.82           C  
ANISOU 2617  CD2 TRP C 614     6980   7156   6693  -2246   -397   -730       C  
ATOM   2618  NE1 TRP C 614     -17.770  -3.399  -2.814  1.00 55.77           N  
ANISOU 2618  NE1 TRP C 614     6545   7887   6756  -2445   -634   -683       N  
ATOM   2619  CE2 TRP C 614     -18.926  -2.681  -2.978  1.00 52.78           C  
ANISOU 2619  CE2 TRP C 614     6555   7173   6327  -2422   -570   -810       C  
ATOM   2620  CE3 TRP C 614     -20.488  -2.178  -4.755  1.00 50.78           C  
ANISOU 2620  CE3 TRP C 614     6841   6311   6144  -2157   -316   -813       C  
ATOM   2621  CZ2 TRP C 614     -19.653  -1.924  -2.062  1.00 59.40           C  
ANISOU 2621  CZ2 TRP C 614     7600   7958   7012  -2507   -651  -1001       C  
ATOM   2622  CZ3 TRP C 614     -21.208  -1.431  -3.847  1.00 49.64           C  
ANISOU 2622  CZ3 TRP C 614     6888   6105   5867  -2210   -395   -989       C  
ATOM   2623  CH2 TRP C 614     -20.787  -1.305  -2.515  1.00 56.76           C  
ANISOU 2623  CH2 TRP C 614     7632   7280   6654  -2384   -555  -1098       C  
ATOM   2624  N   LYS C 615     -18.847  -6.011  -8.925  1.00 41.48           N  
ANISOU 2624  N   LYS C 615     5136   5292   5331  -1312     56   -344       N  
ATOM   2625  CA  LYS C 615     -19.152  -6.213 -10.335  1.00 42.48           C  
ANISOU 2625  CA  LYS C 615     5411   5278   5450  -1140    217   -348       C  
ATOM   2626  C   LYS C 615     -19.448  -7.689 -10.556  1.00 41.19           C  
ANISOU 2626  C   LYS C 615     5237   5069   5346   -801    137   -332       C  
ATOM   2627  O   LYS C 615     -20.455  -8.199 -10.049  1.00 38.70           O  
ANISOU 2627  O   LYS C 615     5077   4599   5028   -728     -6   -317       O  
ATOM   2628  CB  LYS C 615     -17.993  -5.733 -11.228  1.00 39.45           C  
ANISOU 2628  CB  LYS C 615     4844   5087   5059  -1248    415   -327       C  
ATOM   2629  CG  LYS C 615     -17.618  -4.260 -11.059  1.00 47.74           C  
ANISOU 2629  CG  LYS C 615     5934   6132   6072  -1654    483   -320       C  
ATOM   2630  CD  LYS C 615     -18.785  -3.324 -11.338  1.00 48.60           C  
ANISOU 2630  CD  LYS C 615     6465   5879   6122  -1726    513   -344       C  
ATOM   2631  CE  LYS C 615     -18.385  -1.844 -11.180  1.00 47.65           C  
ANISOU 2631  CE  LYS C 615     6457   5657   5993  -2130    564   -341       C  
ATOM   2632  NZ  LYS C 615     -17.722  -1.246 -12.368  1.00 59.37           N  
ANISOU 2632  NZ  LYS C 615     7932   7180   7444  -2302    775   -223       N  
ATOM   2633  N   PHE C 616     -18.581  -8.391 -11.288  1.00 39.20           N  
ANISOU 2633  N   PHE C 616     4804   4951   5138   -598    223   -341       N  
ATOM   2634  CA  PHE C 616     -18.688  -9.835 -11.426  1.00 37.12           C  
ANISOU 2634  CA  PHE C 616     4548   4598   4958   -258    125   -351       C  
ATOM   2635  C   PHE C 616     -17.535 -10.493 -10.680  1.00 41.74           C  
ANISOU 2635  C   PHE C 616     4794   5425   5638   -130     27   -285       C  
ATOM   2636  O   PHE C 616     -16.546  -9.833 -10.343  1.00 44.19           O  
ANISOU 2636  O   PHE C 616     4815   6047   5928   -299     79   -254       O  
ATOM   2637  CB  PHE C 616     -18.665 -10.273 -12.902  1.00 41.89           C  
ANISOU 2637  CB  PHE C 616     5246   5148   5521    -22    285   -458       C  
ATOM   2638  CG  PHE C 616     -19.974 -10.066 -13.616  1.00 45.99           C  
ANISOU 2638  CG  PHE C 616     6113   5415   5946    -52    310   -512       C  
ATOM   2639  CD1 PHE C 616     -21.047 -10.923 -13.397  1.00 41.20           C  
ANISOU 2639  CD1 PHE C 616     5724   4552   5377     41    136   -525       C  
ATOM   2640  CD2 PHE C 616     -20.133  -9.015 -14.509  1.00 42.66           C  
ANISOU 2640  CD2 PHE C 616     5788   5033   5387   -190    496   -522       C  
ATOM   2641  CE1 PHE C 616     -22.256 -10.730 -14.051  1.00 36.02           C  
ANISOU 2641  CE1 PHE C 616     5335   3737   4613      1    146   -570       C  
ATOM   2642  CE2 PHE C 616     -21.338  -8.818 -15.166  1.00 50.29           C  
ANISOU 2642  CE2 PHE C 616     7047   5814   6247   -185    503   -553       C  
ATOM   2643  CZ  PHE C 616     -22.406  -9.684 -14.927  1.00 44.36           C  
ANISOU 2643  CZ  PHE C 616     6468   4860   5524    -86    324   -589       C  
ATOM   2644  N   PRO C 617     -17.641 -11.786 -10.369  1.00 40.88           N  
ANISOU 2644  N   PRO C 617     4716   5180   5636    156   -136   -246       N  
ATOM   2645  CA  PRO C 617     -16.539 -12.473  -9.686  1.00 46.87           C  
ANISOU 2645  CA  PRO C 617     5156   6168   6486    353   -246   -156       C  
ATOM   2646  C   PRO C 617     -15.224 -12.294 -10.418  1.00 53.72           C  
ANISOU 2646  C   PRO C 617     5685   7395   7334    490    -57   -225       C  
ATOM   2647  O   PRO C 617     -15.139 -12.569 -11.614  1.00 50.80           O  
ANISOU 2647  O   PRO C 617     5382   6980   6940    706    107   -355       O  
ATOM   2648  CB  PRO C 617     -16.992 -13.937  -9.700  1.00 49.93           C  
ANISOU 2648  CB  PRO C 617     5753   6217   7002    696   -410   -129       C  
ATOM   2649  CG  PRO C 617     -18.470 -13.818  -9.590  1.00 42.82           C  
ANISOU 2649  CG  PRO C 617     5210   5001   6058    479   -482   -117       C  
ATOM   2650  CD  PRO C 617     -18.833 -12.651 -10.465  1.00 41.93           C  
ANISOU 2650  CD  PRO C 617     5184   4937   5811    269   -264   -248       C  
ATOM   2651  N   ASP C 618     -14.208 -11.804  -9.717  1.00 57.65           N  
ANISOU 2651  N   ASP C 618     5797   8298   7808    343    -76   -144       N  
ATOM   2652  CA  ASP C 618     -12.911 -11.541 -10.326  1.00 63.51           C  
ANISOU 2652  CA  ASP C 618     6136   9492   8505    407    107   -180       C  
ATOM   2653  C   ASP C 618     -11.773 -12.078  -9.466  1.00 67.12           C  
ANISOU 2653  C   ASP C 618     6144  10347   9012    596    -35    -69       C  
ATOM   2654  O   ASP C 618     -12.003 -12.809  -8.503  1.00 74.87           O  
ANISOU 2654  O   ASP C 618     7177  11194  10075    746   -278     44       O  
ATOM   2655  CB  ASP C 618     -12.738 -10.032 -10.585  1.00 61.36           C  
ANISOU 2655  CB  ASP C 618     5799   9406   8110    -98    279   -191       C  
ATOM   2656  CG  ASP C 618     -12.315  -9.263  -9.345  1.00 70.71           C  
ANISOU 2656  CG  ASP C 618     6765  10831   9268   -492    139   -107       C  
ATOM   2657  OD1 ASP C 618     -12.826  -9.561  -8.240  1.00 73.86           O  
ANISOU 2657  OD1 ASP C 618     7271  11090   9701   -501    -89    -50       O  
ATOM   2658  OD2 ASP C 618     -11.448  -8.372  -9.470  1.00 81.77           O  
ANISOU 2658  OD2 ASP C 618     7879  12592  10599   -813    253    -95       O  
ATOM   2659  OXT ASP C 618     -10.600 -11.805  -9.721  1.00 74.61           O  
ANISOU 2659  OXT ASP C 618     6651  11792   9906    604     85    -68       O  
TER    2660      ASP C 618                                                      
ATOM   2661  N   GLN D   1      -0.464 -19.206 -18.348  1.00 60.02           N  
ANISOU 2661  N   GLN D   1     9333   5705   7765   -983   1079  -1989       N  
ATOM   2662  CA  GLN D   1      -0.263 -17.853 -18.864  1.00 59.12           C  
ANISOU 2662  CA  GLN D   1     9218   5988   7257   -717    704  -1798       C  
ATOM   2663  C   GLN D   1      -0.475 -16.810 -17.787  1.00 50.82           C  
ANISOU 2663  C   GLN D   1     7976   5044   6288   -660    653  -1450       C  
ATOM   2664  O   GLN D   1      -1.444 -16.879 -17.030  1.00 64.68           O  
ANISOU 2664  O   GLN D   1     9465   6754   8354   -860    663  -1569       O  
ATOM   2665  CB  GLN D   1      -1.204 -17.566 -20.029  1.00 65.96           C  
ANISOU 2665  CB  GLN D   1     9942   7213   7906   -735    286  -2236       C  
ATOM   2666  CG  GLN D   1      -0.693 -16.478 -20.954  1.00 73.36           C  
ANISOU 2666  CG  GLN D   1    11033   8485   8354   -402     -6  -2046       C  
ATOM   2667  CD  GLN D   1      -1.814 -15.659 -21.561  1.00 85.08           C  
ANISOU 2667  CD  GLN D   1    12250  10417   9658   -316   -458  -2241       C  
ATOM   2668  OE1 GLN D   1      -1.747 -14.428 -21.602  1.00 83.90           O  
ANISOU 2668  OE1 GLN D   1    12095  10483   9298    -38   -629  -1927       O  
ATOM   2669  NE2 GLN D   1      -2.849 -16.340 -22.047  1.00 87.03           N  
ANISOU 2669  NE2 GLN D   1    12262  10821   9983   -549   -628  -2763       N  
ATOM   2670  N   VAL D   2       0.402 -15.818 -17.719  1.00 44.31           N  
ANISOU 2670  N   VAL D   2     7284   4360   5192   -418    628  -1054       N  
ATOM   2671  CA  VAL D   2       0.298 -14.798 -16.682  1.00 51.50           C  
ANISOU 2671  CA  VAL D   2     8040   5361   6166   -402    649   -744       C  
ATOM   2672  C   VAL D   2      -0.526 -13.635 -17.217  1.00 50.89           C  
ANISOU 2672  C   VAL D   2     7813   5581   5940   -274    306   -830       C  
ATOM   2673  O   VAL D   2      -0.223 -13.074 -18.276  1.00 43.72           O  
ANISOU 2673  O   VAL D   2     7062   4868   4682    -39    113   -821       O  
ATOM   2674  CB  VAL D   2       1.680 -14.332 -16.208  1.00 45.73           C  
ANISOU 2674  CB  VAL D   2     7497   4636   5241   -260    870   -299       C  
ATOM   2675  CG1 VAL D   2       1.520 -13.178 -15.217  1.00 45.13           C  
ANISOU 2675  CG1 VAL D   2     7260   4692   5196   -294    904    -52       C  
ATOM   2676  CG2 VAL D   2       2.418 -15.502 -15.569  1.00 50.06           C  
ANISOU 2676  CG2 VAL D   2     8134   4930   5956   -336   1214   -154       C  
ATOM   2677  N   THR D   3      -1.584 -13.278 -16.492  1.00 42.44           N  
ANISOU 2677  N   THR D   3     6445   4543   5139   -407    253   -894       N  
ATOM   2678  CA  THR D   3      -2.443 -12.173 -16.883  1.00 46.60           C  
ANISOU 2678  CA  THR D   3     6787   5339   5581   -250    -30   -930       C  
ATOM   2679  C   THR D   3      -2.669 -11.257 -15.689  1.00 46.38           C  
ANISOU 2679  C   THR D   3     6608   5267   5747   -308    137   -673       C  
ATOM   2680  O   THR D   3      -2.716 -11.712 -14.545  1.00 42.78           O  
ANISOU 2680  O   THR D   3     6061   4616   5578   -559    380   -629       O  
ATOM   2681  CB  THR D   3      -3.795 -12.675 -17.447  1.00 48.09           C  
ANISOU 2681  CB  THR D   3     6678   5686   5909   -352   -319  -1385       C  
ATOM   2682  OG1 THR D   3      -4.724 -12.865 -16.376  1.00 64.58           O  
ANISOU 2682  OG1 THR D   3     8456   7652   8429   -612   -213  -1493       O  
ATOM   2683  CG2 THR D   3      -3.631 -13.969 -18.219  1.00 56.02           C  
ANISOU 2683  CG2 THR D   3     7798   6625   6862   -488   -334  -1737       C  
ATOM   2684  N   LEU D   4      -2.775  -9.955 -15.974  1.00 37.46           N  
ANISOU 2684  N   LEU D   4     5479   4308   4444    -67     46   -493       N  
ATOM   2685  CA  LEU D   4      -2.999  -8.907 -14.987  1.00 34.52           C  
ANISOU 2685  CA  LEU D   4     4990   3896   4229   -106    240   -271       C  
ATOM   2686  C   LEU D   4      -4.160  -8.051 -15.463  1.00 41.88           C  
ANISOU 2686  C   LEU D   4     5690   5016   5206    104      8   -336       C  
ATOM   2687  O   LEU D   4      -4.224  -7.691 -16.640  1.00 43.26           O  
ANISOU 2687  O   LEU D   4     5944   5402   5091    418   -240   -340       O  
ATOM   2688  CB  LEU D   4      -1.748  -8.041 -14.822  1.00 36.76           C  
ANISOU 2688  CB  LEU D   4     5559   4160   4248     -3    494     68       C  
ATOM   2689  CG  LEU D   4      -0.815  -8.331 -13.650  1.00 41.81           C  
ANISOU 2689  CG  LEU D   4     6268   4676   4943   -262    834    242       C  
ATOM   2690  CD1 LEU D   4      -0.155  -9.654 -13.813  1.00 55.04           C  
ANISOU 2690  CD1 LEU D   4     8062   6274   6578   -329    836    183       C  
ATOM   2691  CD2 LEU D   4       0.251  -7.244 -13.615  1.00 51.12           C  
ANISOU 2691  CD2 LEU D   4     7663   5917   5842   -168   1063    507       C  
ATOM   2692  N   LYS D   5      -5.085  -7.722 -14.563  1.00 35.65           N  
ANISOU 2692  N   LYS D   5     4608   4169   4769    -43     96   -369       N  
ATOM   2693  CA  LYS D   5      -6.272  -6.974 -14.969  1.00 38.79           C  
ANISOU 2693  CA  LYS D   5     4723   4758   5257    182   -115   -421       C  
ATOM   2694  C   LYS D   5      -6.622  -5.942 -13.912  1.00 40.01           C  
ANISOU 2694  C   LYS D   5     4758   4766   5676    122    190   -226       C  
ATOM   2695  O   LYS D   5      -7.037  -6.300 -12.803  1.00 40.72           O  
ANISOU 2695  O   LYS D   5     4664   4694   6113   -214    369   -327       O  
ATOM   2696  CB  LYS D   5      -7.466  -7.901 -15.210  1.00 44.17           C  
ANISOU 2696  CB  LYS D   5     5034   5584   6164     48   -412   -830       C  
ATOM   2697  CG  LYS D   5      -8.638  -7.188 -15.871  1.00 46.45           C  
ANISOU 2697  CG  LYS D   5     4992   6199   6459    357   -713   -881       C  
ATOM   2698  CD  LYS D   5      -9.965  -7.742 -15.372  1.00 68.85           C  
ANISOU 2698  CD  LYS D   5     7349   9092   9718    104   -814  -1234       C  
ATOM   2699  CE  LYS D   5     -11.013  -6.626 -15.285  1.00 74.85           C  
ANISOU 2699  CE  LYS D   5     7766  10024  10651    375   -873  -1105       C  
ATOM   2700  NZ  LYS D   5     -12.013  -6.786 -14.174  1.00 67.05           N  
ANISOU 2700  NZ  LYS D   5     6399   8887  10191     62   -713  -1291       N  
ATOM   2701  N   GLU D   6      -6.507  -4.671 -14.281  1.00 38.02           N  
ANISOU 2701  N   GLU D   6     4619   4559   5269    447    280     42       N  
ATOM   2702  CA  GLU D   6      -6.839  -3.559 -13.400  1.00 37.46           C  
ANISOU 2702  CA  GLU D   6     4465   4326   5441    419    631    223       C  
ATOM   2703  C   GLU D   6      -8.326  -3.247 -13.460  1.00 41.17           C  
ANISOU 2703  C   GLU D   6     4516   4913   6213    576    462    126       C  
ATOM   2704  O   GLU D   6      -8.953  -3.337 -14.517  1.00 45.18           O  
ANISOU 2704  O   GLU D   6     4863   5714   6589    903     73     54       O  
ATOM   2705  CB  GLU D   6      -6.043  -2.316 -13.799  1.00 40.54           C  
ANISOU 2705  CB  GLU D   6     5189   4658   5555    704    891    550       C  
ATOM   2706  CG  GLU D   6      -4.573  -2.571 -13.865  1.00 37.32           C  
ANISOU 2706  CG  GLU D   6     5158   4194   4827    581   1038    631       C  
ATOM   2707  CD  GLU D   6      -4.129  -2.963 -15.269  1.00 48.33           C  
ANISOU 2707  CD  GLU D   6     6757   5778   5829    896    704    627       C  
ATOM   2708  OE1 GLU D   6      -4.994  -3.384 -16.078  1.00 41.41           O  
ANISOU 2708  OE1 GLU D   6     5682   5120   4932   1104    298    479       O  
ATOM   2709  OE2 GLU D   6      -2.911  -2.890 -15.549  1.00 43.34           O1-
ANISOU 2709  OE2 GLU D   6     6464   5105   4900    906    852    745       O1-
ATOM   2710  N   SER D   7      -8.892  -2.873 -12.311  1.00 40.58           N  
ANISOU 2710  N   SER D   7     4243   4646   6529    339    759    118       N  
ATOM   2711  CA  SER D   7     -10.241  -2.352 -12.249  1.00 44.10           C  
ANISOU 2711  CA  SER D   7     4292   5164   7301    510    700     81       C  
ATOM   2712  C   SER D   7     -10.231  -1.123 -11.353  1.00 43.19           C  
ANISOU 2712  C   SER D   7     4242   4766   7403    471   1228    314       C  
ATOM   2713  O   SER D   7      -9.347  -0.956 -10.510  1.00 46.27           O  
ANISOU 2713  O   SER D   7     4890   4930   7761    146   1615    382       O  
ATOM   2714  CB  SER D   7     -11.238  -3.418 -11.756  1.00 45.31           C  
ANISOU 2714  CB  SER D   7     4039   5368   7810    186    508   -296       C  
ATOM   2715  OG  SER D   7     -10.993  -3.766 -10.410  1.00 48.03           O  
ANISOU 2715  OG  SER D   7     4429   5416   8404   -305    864   -364       O  
ATOM   2716  N   GLY D   8     -11.175  -0.231 -11.595  1.00 34.83           N  
ANISOU 2716  N   GLY D   8     4098   4737   4399   -326   -240   -184       N  
ATOM   2717  CA  GLY D   8     -11.242   0.986 -10.837  1.00 37.64           C  
ANISOU 2717  CA  GLY D   8     4469   5102   4731   -312    -72    -82       C  
ATOM   2718  C   GLY D   8     -12.621   1.594 -10.905  1.00 38.34           C  
ANISOU 2718  C   GLY D   8     4380   5141   5045   -296    -81    -52       C  
ATOM   2719  O   GLY D   8     -13.564   1.013 -11.453  1.00 39.62           O  
ANISOU 2719  O   GLY D   8     4379   5250   5425   -307   -231   -114       O  
ATOM   2720  N   PRO D   9     -12.749   2.813 -10.379  1.00 34.64           N  
ANISOU 2720  N   PRO D   9     3927   4677   4558   -264     61     29       N  
ATOM   2721  CA  PRO D   9     -14.079   3.431 -10.255  1.00 43.02           C  
ANISOU 2721  CA  PRO D   9     4809   5670   5866   -244    104     80       C  
ATOM   2722  C   PRO D   9     -14.602   4.014 -11.551  1.00 44.57           C  
ANISOU 2722  C   PRO D   9     4917   5930   6087   -161   -117     66       C  
ATOM   2723  O   PRO D   9     -15.810   4.275 -11.653  1.00 41.97           O  
ANISOU 2723  O   PRO D   9     4390   5537   6019   -142   -156     88       O  
ATOM   2724  CB  PRO D   9     -13.844   4.561  -9.240  1.00 42.99           C  
ANISOU 2724  CB  PRO D   9     4900   5647   5786   -217    335    152       C  
ATOM   2725  CG  PRO D   9     -12.400   4.960  -9.510  1.00 39.29           C  
ANISOU 2725  CG  PRO D   9     4617   5266   5045   -199    290    126       C  
ATOM   2726  CD  PRO D   9     -11.688   3.650  -9.787  1.00 34.35           C  
ANISOU 2726  CD  PRO D   9     4054   4674   4322   -245    188     64       C  
ATOM   2727  N   GLY D  10     -13.737   4.257 -12.527  1.00 42.23           N  
ANISOU 2727  N   GLY D  10     4764   5749   5532    -86   -246     50       N  
ATOM   2728  CA  GLY D  10     -14.119   5.091 -13.664  1.00 35.94           C  
ANISOU 2728  CA  GLY D  10     3949   5026   4681     52   -401     87       C  
ATOM   2729  C   GLY D  10     -13.878   6.571 -13.359  1.00 40.26           C  
ANISOU 2729  C   GLY D  10     4538   5569   5191    101   -211    217       C  
ATOM   2730  O   GLY D  10     -12.734   7.010 -13.320  1.00 44.62           O  
ANISOU 2730  O   GLY D  10     5237   6146   5571    113   -100    259       O  
ATOM   2731  N   ILE D  11     -14.951   7.308 -13.120  1.00 41.05           N  
ANISOU 2731  N   ILE D  11     4485   5609   5503    126   -170    275       N  
ATOM   2732  CA  ILE D  11     -14.833   8.707 -12.767  1.00 36.13           C  
ANISOU 2732  CA  ILE D  11     3884   4948   4896    170     17    383       C  
ATOM   2733  C   ILE D  11     -14.865   8.851 -11.251  1.00 48.25           C  
ANISOU 2733  C   ILE D  11     5418   6373   6540     70    262    366       C  
ATOM   2734  O   ILE D  11     -15.295   7.955 -10.515  1.00 44.61           O  
ANISOU 2734  O   ILE D  11     4904   5862   6185     -8    311    317       O  
ATOM   2735  CB  ILE D  11     -15.908   9.583 -13.443  1.00 38.82           C  
ANISOU 2735  CB  ILE D  11     4084   5285   5379    294    -66    471       C  
ATOM   2736  CG1 ILE D  11     -17.302   9.347 -12.869  1.00 46.15           C  
ANISOU 2736  CG1 ILE D  11     4777   6115   6642    248    -60    453       C  
ATOM   2737  CG2 ILE D  11     -15.918   9.355 -14.954  1.00 39.62           C  
ANISOU 2737  CG2 ILE D  11     4233   5511   5308    447   -346    475       C  
ATOM   2738  CD1 ILE D  11     -18.255  10.485 -13.200  1.00 45.02           C  
ANISOU 2738  CD1 ILE D  11     4489   5935   6681    364    -62    563       C  
ATOM   2739  N   LEU D  12     -14.396  10.005 -10.783  1.00 41.54           N  
ANISOU 2739  N   LEU D  12     4642   5475   5668     94    424    407       N  
ATOM   2740  CA  LEU D  12     -14.159  10.279  -9.375  1.00 45.84           C  
ANISOU 2740  CA  LEU D  12     5264   5926   6225     45    628    356       C  
ATOM   2741  C   LEU D  12     -14.273  11.782  -9.164  1.00 38.81           C  
ANISOU 2741  C   LEU D  12     4366   4949   5432    109    758    401       C  
ATOM   2742  O   LEU D  12     -13.906  12.556 -10.050  1.00 39.11           O  
ANISOU 2742  O   LEU D  12     4393   4999   5468    168    712    474       O  
ATOM   2743  CB  LEU D  12     -12.769   9.777  -8.972  1.00 48.25           C  
ANISOU 2743  CB  LEU D  12     5740   6260   6331    -13    613    272       C  
ATOM   2744  CG  LEU D  12     -12.555   9.196  -7.588  1.00 52.21           C  
ANISOU 2744  CG  LEU D  12     6356   6720   6761    -53    722    189       C  
ATOM   2745  CD1 LEU D  12     -13.570   8.089  -7.295  1.00 51.39           C  
ANISOU 2745  CD1 LEU D  12     6166   6606   6752    -77    767    218       C  
ATOM   2746  CD2 LEU D  12     -11.148   8.647  -7.528  1.00 46.25           C  
ANISOU 2746  CD2 LEU D  12     5732   6010   5830    -96    631    117       C  
ATOM   2747  N   GLN D  13     -14.840  12.212  -7.951  1.00 39.59           N  
ANISOU 2747  N   GLN D  13     4478   4941   5624    121    953    367       N  
ATOM   2748  CA  GLN D  13     -14.823  13.644  -7.690  1.00 37.30           C  
ANISOU 2748  CA  GLN D  13     4201   4543   5428    182   1072    373       C  
ATOM   2749  C   GLN D  13     -13.545  14.034  -6.952  1.00 38.30           C  
ANISOU 2749  C   GLN D  13     4506   4613   5435    158   1091    236       C  
ATOM   2750  O   GLN D  13     -12.934  13.200  -6.275  1.00 41.28           O  
ANISOU 2750  O   GLN D  13     5013   5028   5644    115   1056    135       O  
ATOM   2751  CB  GLN D  13     -16.049  14.056  -6.863  1.00 38.63           C  
ANISOU 2751  CB  GLN D  13     4305   4609   5763    242   1274    395       C  
ATOM   2752  CG  GLN D  13     -17.373  13.725  -7.523  1.00 51.62           C  
ANISOU 2752  CG  GLN D  13     5717   6273   7623    266   1241    521       C  
ATOM   2753  CD  GLN D  13     -17.594  14.484  -8.817  1.00 57.42           C  
ANISOU 2753  CD  GLN D  13     6322   7038   8456    330   1102    631       C  
ATOM   2754  OE1 GLN D  13     -17.179  15.638  -8.957  1.00 63.83           O  
ANISOU 2754  OE1 GLN D  13     7179   7790   9285    381   1163    659       O  
ATOM   2755  NE2 GLN D  13     -18.249  13.836  -9.777  1.00 64.34           N  
ANISOU 2755  NE2 GLN D  13     7042   7998   9407    344    904    692       N  
ATOM   2756  N   PRO D  14     -13.102  15.283  -7.079  1.00 37.52           N  
ANISOU 2756  N   PRO D  14     4400   4405   5450    189   1128    227       N  
ATOM   2757  CA  PRO D  14     -11.910  15.718  -6.342  1.00 38.92           C  
ANISOU 2757  CA  PRO D  14     4706   4486   5595    164   1104     59       C  
ATOM   2758  C   PRO D  14     -12.050  15.449  -4.850  1.00 43.29           C  
ANISOU 2758  C   PRO D  14     5436   5006   6006    198   1165   -113       C  
ATOM   2759  O   PRO D  14     -13.152  15.484  -4.289  1.00 40.06           O  
ANISOU 2759  O   PRO D  14     5040   4577   5605    266   1323    -86       O  
ATOM   2760  CB  PRO D  14     -11.835  17.218  -6.644  1.00 50.18           C  
ANISOU 2760  CB  PRO D  14     6050   5747   7270    208   1183     89       C  
ATOM   2761  CG  PRO D  14     -12.507  17.346  -7.991  1.00 53.08           C  
ANISOU 2761  CG  PRO D  14     6262   6185   7720    252   1195    327       C  
ATOM   2762  CD  PRO D  14     -13.624  16.340  -7.964  1.00 43.84           C  
ANISOU 2762  CD  PRO D  14     5060   5149   6446    258   1175    374       C  
ATOM   2763  N   SER D  15     -10.912  15.132  -4.227  1.00 39.88           N  
ANISOU 2763  N   SER D  15     5144   4568   5439    172   1042   -278       N  
ATOM   2764  CA  SER D  15     -10.780  14.874  -2.790  1.00 39.50           C  
ANISOU 2764  CA  SER D  15     5326   4499   5182    248   1052   -463       C  
ATOM   2765  C   SER D  15     -11.315  13.505  -2.397  1.00 43.86           C  
ANISOU 2765  C   SER D  15     5962   5184   5520    267   1120   -384       C  
ATOM   2766  O   SER D  15     -11.168  13.094  -1.243  1.00 46.92           O  
ANISOU 2766  O   SER D  15     6571   5578   5678    362   1146   -493       O  
ATOM   2767  CB  SER D  15     -11.468  15.954  -1.940  1.00 41.11           C  
ANISOU 2767  CB  SER D  15     5618   4562   5438    369   1205   -563       C  
ATOM   2768  OG  SER D  15     -10.774  17.183  -2.048  1.00 50.17           O  
ANISOU 2768  OG  SER D  15     6720   5546   6798    355   1117   -696       O  
ATOM   2769  N   GLN D  16     -11.917  12.777  -3.333  1.00 39.10           N  
ANISOU 2769  N   GLN D  16     5191   4672   4992    198   1143   -199       N  
ATOM   2770  CA  GLN D  16     -12.273  11.398  -3.042  1.00 42.62           C  
ANISOU 2770  CA  GLN D  16     5678   5207   5308    193   1190   -130       C  
ATOM   2771  C   GLN D  16     -11.019  10.531  -3.073  1.00 45.07           C  
ANISOU 2771  C   GLN D  16     6077   5595   5451    134   1003   -199       C  
ATOM   2772  O   GLN D  16      -9.956  10.943  -3.557  1.00 39.58           O  
ANISOU 2772  O   GLN D  16     5357   4892   4789     81    838   -268       O  
ATOM   2773  CB  GLN D  16     -13.322  10.905  -4.041  1.00 40.62           C  
ANISOU 2773  CB  GLN D  16     5192   4996   5246    137   1224     44       C  
ATOM   2774  CG  GLN D  16     -14.682  11.542  -3.760  1.00 42.42           C  
ANISOU 2774  CG  GLN D  16     5323   5133   5660    214   1438    124       C  
ATOM   2775  CD  GLN D  16     -15.809  11.021  -4.627  1.00 54.64           C  
ANISOU 2775  CD  GLN D  16     6612   6698   7452    172   1437    273       C  
ATOM   2776  OE1 GLN D  16     -15.586  10.480  -5.706  1.00 48.04           O  
ANISOU 2776  OE1 GLN D  16     5666   5946   6640     96   1232    300       O  
ATOM   2777  NE2 GLN D  16     -17.041  11.174  -4.142  1.00 57.22           N  
ANISOU 2777  NE2 GLN D  16     6839   6930   7974    239   1662    359       N  
ATOM   2778  N   THR D  17     -11.133   9.326  -2.530  1.00 39.62           N  
ANISOU 2778  N   THR D  17     5478   4959   4615    154   1053   -163       N  
ATOM   2779  CA  THR D  17     -10.017   8.387  -2.564  1.00 39.97           C  
ANISOU 2779  CA  THR D  17     5595   5075   4515    108    888   -208       C  
ATOM   2780  C   THR D  17     -10.146   7.485  -3.783  1.00 37.53           C  
ANISOU 2780  C   THR D  17     5107   4836   4317     -6    820    -94       C  
ATOM   2781  O   THR D  17     -11.220   6.933  -4.041  1.00 39.12           O  
ANISOU 2781  O   THR D  17     5194   5034   4634    -21    924     13       O  
ATOM   2782  CB  THR D  17      -9.966   7.553  -1.281  1.00 45.83           C  
ANISOU 2782  CB  THR D  17     6565   5829   5018    222    979   -224       C  
ATOM   2783  OG1 THR D  17      -9.529   8.372  -0.188  1.00 51.68           O  
ANISOU 2783  OG1 THR D  17     7529   6522   5584    358    952   -389       O  
ATOM   2784  CG2 THR D  17      -9.003   6.395  -1.429  1.00 42.97           C  
ANISOU 2784  CG2 THR D  17     6239   5539   4550    171    830   -224       C  
ATOM   2785  N   LEU D  18      -9.050   7.341  -4.534  1.00 33.65           N  
ANISOU 2785  N   LEU D  18     4583   4388   3813    -74    642   -129       N  
ATOM   2786  CA  LEU D  18      -8.981   6.396  -5.646  1.00 35.92           C  
ANISOU 2786  CA  LEU D  18     4763   4746   4139   -148    559    -57       C  
ATOM   2787  C   LEU D  18      -8.587   5.019  -5.126  1.00 32.49           C  
ANISOU 2787  C   LEU D  18     4420   4342   3583   -158    545    -63       C  
ATOM   2788  O   LEU D  18      -7.544   4.875  -4.478  1.00 37.04           O  
ANISOU 2788  O   LEU D  18     5125   4922   4028   -132    477   -136       O  
ATOM   2789  CB  LEU D  18      -7.979   6.878  -6.696  1.00 32.52           C  
ANISOU 2789  CB  LEU D  18     4276   4335   3744   -179    437    -62       C  
ATOM   2790  CG  LEU D  18      -7.657   5.911  -7.835  1.00 33.49           C  
ANISOU 2790  CG  LEU D  18     4351   4535   3841   -214    346    -14       C  
ATOM   2791  CD1 LEU D  18      -8.882   5.462  -8.613  1.00 32.01           C  
ANISOU 2791  CD1 LEU D  18     4060   4385   3717   -213    332     45       C  
ATOM   2792  CD2 LEU D  18      -6.657   6.562  -8.787  1.00 34.40           C  
ANISOU 2792  CD2 LEU D  18     4433   4646   3990   -200    304     17       C  
ATOM   2793  N   SER D  19      -9.425   4.018  -5.399  1.00 35.34           N  
ANISOU 2793  N   SER D  19     4698   4705   4024   -188    597     10       N  
ATOM   2794  CA  SER D  19      -9.201   2.640  -4.977  1.00 30.86           C  
ANISOU 2794  CA  SER D  19     4190   4136   3400   -197    619     33       C  
ATOM   2795  C   SER D  19      -9.114   1.758  -6.207  1.00 36.64           C  
ANISOU 2795  C   SER D  19     4803   4898   4220   -276    487     32       C  
ATOM   2796  O   SER D  19     -10.073   1.663  -6.983  1.00 36.69           O  
ANISOU 2796  O   SER D  19     4656   4889   4398   -307    459     51       O  
ATOM   2797  CB  SER D  19     -10.324   2.146  -4.051  1.00 37.87           C  
ANISOU 2797  CB  SER D  19     5081   4944   4366   -146    846    126       C  
ATOM   2798  OG  SER D  19     -10.096   2.629  -2.748  1.00 55.53           O  
ANISOU 2798  OG  SER D  19     7526   7166   6408    -23    967    114       O  
ATOM   2799  N   LEU D  20      -7.964   1.130  -6.391  1.00 35.64           N  
ANISOU 2799  N   LEU D  20     4750   4810   3982   -292    389     -5       N  
ATOM   2800  CA  LEU D  20      -7.686   0.339  -7.576  1.00 35.35           C  
ANISOU 2800  CA  LEU D  20     4648   4803   3980   -337    263    -30       C  
ATOM   2801  C   LEU D  20      -7.485  -1.107  -7.162  1.00 30.45           C  
ANISOU 2801  C   LEU D  20     4061   4138   3370   -358    291    -19       C  
ATOM   2802  O   LEU D  20      -6.957  -1.377  -6.084  1.00 36.15           O  
ANISOU 2802  O   LEU D  20     4901   4844   3989   -318    365     10       O  
ATOM   2803  CB  LEU D  20      -6.418   0.848  -8.286  1.00 29.10           C  
ANISOU 2803  CB  LEU D  20     3901   4071   3086   -322    165    -61       C  
ATOM   2804  CG  LEU D  20      -6.557   2.249  -8.907  1.00 35.83           C  
ANISOU 2804  CG  LEU D  20     4705   4944   3965   -291    159    -42       C  
ATOM   2805  CD1 LEU D  20      -5.194   2.892  -9.179  1.00 40.96           C  
ANISOU 2805  CD1 LEU D  20     5385   5593   4583   -270    140    -41       C  
ATOM   2806  CD2 LEU D  20      -7.385   2.185 -10.171  1.00 35.18           C  
ANISOU 2806  CD2 LEU D  20     4542   4901   3925   -268     87    -28       C  
ATOM   2807  N   THR D  21      -7.875  -2.028  -8.036  1.00 31.65           N  
ANISOU 2807  N   THR D  21     4120   4264   3643   -400    214    -52       N  
ATOM   2808  CA  THR D  21      -7.592  -3.447  -7.862  1.00 32.11           C  
ANISOU 2808  CA  THR D  21     4192   4257   3753   -425    228    -53       C  
ATOM   2809  C   THR D  21      -6.859  -3.998  -9.080  1.00 35.02           C  
ANISOU 2809  C   THR D  21     4572   4665   4068   -431     68   -145       C  
ATOM   2810  O   THR D  21      -7.239  -3.719 -10.218  1.00 34.78           O  
ANISOU 2810  O   THR D  21     4489   4674   4053   -419    -61   -217       O  
ATOM   2811  CB  THR D  21      -8.869  -4.222  -7.671  1.00 36.70           C  
ANISOU 2811  CB  THR D  21     4628   4705   4613   -468    308    -25       C  
ATOM   2812  OG1 THR D  21      -9.488  -3.778  -6.466  1.00 38.36           O  
ANISOU 2812  OG1 THR D  21     4855   4867   4854   -428    523     92       O  
ATOM   2813  CG2 THR D  21      -8.576  -5.740  -7.591  1.00 38.41           C  
ANISOU 2813  CG2 THR D  21     4838   4818   4938   -497    329    -26       C  
ATOM   2814  N   CYS D  22      -5.825  -4.799  -8.825  1.00 31.07           N  
ANISOU 2814  N   CYS D  22     4158   4154   3495   -423     81   -139       N  
ATOM   2815  CA  CYS D  22      -5.139  -5.593  -9.842  1.00 34.05           C  
ANISOU 2815  CA  CYS D  22     4559   4536   3844   -414    -22   -219       C  
ATOM   2816  C   CYS D  22      -5.385  -7.068  -9.531  1.00 33.93           C  
ANISOU 2816  C   CYS D  22     4508   4391   3994   -452     15   -229       C  
ATOM   2817  O   CYS D  22      -4.858  -7.596  -8.545  1.00 40.04           O  
ANISOU 2817  O   CYS D  22     5339   5121   4752   -441    124   -140       O  
ATOM   2818  CB  CYS D  22      -3.650  -5.256  -9.860  1.00 35.43           C  
ANISOU 2818  CB  CYS D  22     4830   4777   3856   -366    -17   -191       C  
ATOM   2819  SG  CYS D  22      -2.678  -6.229 -11.002  1.00 40.34           S  
ANISOU 2819  SG  CYS D  22     5502   5391   4433   -321    -73   -260       S  
ATOM   2820  N   SER D  23      -6.209  -7.723 -10.352  1.00 35.87           N  
ANISOU 2820  N   SER D  23     4654   4559   4416   -484    -89   -340       N  
ATOM   2821  CA  SER D  23      -6.477  -9.155 -10.233  1.00 40.30           C  
ANISOU 2821  CA  SER D  23     5146   4951   5213   -530    -68   -377       C  
ATOM   2822  C   SER D  23      -5.561  -9.888 -11.202  1.00 41.60           C  
ANISOU 2822  C   SER D  23     5399   5125   5280   -488   -184   -501       C  
ATOM   2823  O   SER D  23      -5.477  -9.503 -12.371  1.00 39.78           O  
ANISOU 2823  O   SER D  23     5220   4983   4912   -429   -340   -625       O  
ATOM   2824  CB  SER D  23      -7.938  -9.462 -10.558  1.00 45.67           C  
ANISOU 2824  CB  SER D  23     5629   5497   6228   -592   -145   -462       C  
ATOM   2825  OG  SER D  23      -8.801  -8.738  -9.690  1.00 53.51           O  
ANISOU 2825  OG  SER D  23     6533   6472   7326   -613      1   -330       O  
ATOM   2826  N   PHE D  24      -4.867 -10.924 -10.730  1.00 36.83           N  
ANISOU 2826  N   PHE D  24     4834   4432   4730   -492    -91   -455       N  
ATOM   2827  CA  PHE D  24      -3.889 -11.604 -11.581  1.00 41.37           C  
ANISOU 2827  CA  PHE D  24     5503   5007   5208   -436   -161   -559       C  
ATOM   2828  C   PHE D  24      -4.099 -13.114 -11.568  1.00 43.96           C  
ANISOU 2828  C   PHE D  24     5768   5128   5810   -475   -152   -629       C  
ATOM   2829  O   PHE D  24      -4.777 -13.668 -10.696  1.00 39.05           O  
ANISOU 2829  O   PHE D  24     5031   4353   5454   -542    -36   -538       O  
ATOM   2830  CB  PHE D  24      -2.446 -11.271 -11.159  1.00 39.99           C  
ANISOU 2830  CB  PHE D  24     5444   4934   4818   -375    -65   -434       C  
ATOM   2831  CG  PHE D  24      -2.164 -11.522  -9.710  1.00 39.14           C  
ANISOU 2831  CG  PHE D  24     5338   4782   4752   -388     77   -261       C  
ATOM   2832  CD1 PHE D  24      -1.779 -12.776  -9.283  1.00 42.69           C  
ANISOU 2832  CD1 PHE D  24     5792   5100   5327   -380    154   -214       C  
ATOM   2833  CD2 PHE D  24      -2.288 -10.501  -8.773  1.00 41.58           C  
ANISOU 2833  CD2 PHE D  24     5665   5175   4957   -380    130   -148       C  
ATOM   2834  CE1 PHE D  24      -1.526 -13.028  -7.938  1.00 40.84           C  
ANISOU 2834  CE1 PHE D  24     5596   4834   5088   -344    284    -34       C  
ATOM   2835  CE2 PHE D  24      -2.031 -10.743  -7.425  1.00 41.65           C  
ANISOU 2835  CE2 PHE D  24     5729   5156   4942   -340    242     -1       C  
ATOM   2836  CZ  PHE D  24      -1.649 -12.015  -7.015  1.00 44.67           C  
ANISOU 2836  CZ  PHE D  24     6130   5421   5421   -312    319     67       C  
ATOM   2837  N   SER D  25      -3.508 -13.779 -12.563  1.00 37.22           N  
ANISOU 2837  N   SER D  25     4992   4248   4902   -418   -250   -786       N  
ATOM   2838  CA  SER D  25      -3.592 -15.231 -12.674  1.00 44.10           C  
ANISOU 2838  CA  SER D  25     5811   4901   6044   -445   -256   -887       C  
ATOM   2839  C   SER D  25      -2.311 -15.740 -13.314  1.00 50.56           C  
ANISOU 2839  C   SER D  25     6784   5746   6682   -344   -248   -945       C  
ATOM   2840  O   SER D  25      -1.578 -14.987 -13.955  1.00 42.03           O  
ANISOU 2840  O   SER D  25     5834   4837   5299   -245   -267   -950       O  
ATOM   2841  CB  SER D  25      -4.805 -15.680 -13.498  1.00 47.66           C  
ANISOU 2841  CB  SER D  25     6142   5210   6756   -486   -475  -1140       C  
ATOM   2842  OG  SER D  25      -4.624 -15.377 -14.871  1.00 60.77           O  
ANISOU 2842  OG  SER D  25     7943   6986   8159   -370   -695  -1362       O  
ATOM   2843  N   GLY D  26      -2.048 -17.032 -13.139  1.00 50.40           N  
ANISOU 2843  N   GLY D  26     6736   5531   6883   -358   -187   -972       N  
ATOM   2844  CA  GLY D  26      -0.832 -17.625 -13.647  1.00 48.34           C  
ANISOU 2844  CA  GLY D  26     6605   5263   6498   -256   -143  -1011       C  
ATOM   2845  C   GLY D  26       0.341 -17.581 -12.693  1.00 51.47           C  
ANISOU 2845  C   GLY D  26     7030   5712   6813   -227     47   -756       C  
ATOM   2846  O   GLY D  26       1.408 -18.116 -13.021  1.00 46.11           O  
ANISOU 2846  O   GLY D  26     6428   5008   6086   -142    108   -759       O  
ATOM   2847  N   PHE D  27       0.183 -16.957 -11.528  1.00 44.92           N  
ANISOU 2847  N   PHE D  27     6149   4952   5968   -275    129   -548       N  
ATOM   2848  CA  PHE D  27       1.228 -16.933 -10.514  1.00 48.16           C  
ANISOU 2848  CA  PHE D  27     6589   5407   6304   -226    248   -330       C  
ATOM   2849  C   PHE D  27       0.584 -16.594  -9.177  1.00 46.20           C  
ANISOU 2849  C   PHE D  27     6301   5164   6086   -263    326   -148       C  
ATOM   2850  O   PHE D  27      -0.590 -16.218  -9.109  1.00 41.93           O  
ANISOU 2850  O   PHE D  27     5698   4611   5623   -332    314   -179       O  
ATOM   2851  CB  PHE D  27       2.346 -15.940 -10.876  1.00 43.98           C  
ANISOU 2851  CB  PHE D  27     6123   5058   5530   -152    221   -302       C  
ATOM   2852  CG  PHE D  27       1.982 -14.484 -10.684  1.00 38.04           C  
ANISOU 2852  CG  PHE D  27     5364   4472   4618   -179    168   -267       C  
ATOM   2853  CD1 PHE D  27       1.270 -13.800 -11.656  1.00 41.55           C  
ANISOU 2853  CD1 PHE D  27     5821   4987   4979   -192     86   -399       C  
ATOM   2854  CD2 PHE D  27       2.400 -13.789  -9.560  1.00 41.07           C  
ANISOU 2854  CD2 PHE D  27     5742   4934   4928   -168    183   -114       C  
ATOM   2855  CE1 PHE D  27       0.956 -12.452 -11.500  1.00 43.47           C  
ANISOU 2855  CE1 PHE D  27     6052   5365   5099   -209     55   -355       C  
ATOM   2856  CE2 PHE D  27       2.089 -12.448  -9.393  1.00 38.85           C  
ANISOU 2856  CE2 PHE D  27     5454   4780   4526   -189    136   -103       C  
ATOM   2857  CZ  PHE D  27       1.361 -11.775 -10.362  1.00 37.98           C  
ANISOU 2857  CZ  PHE D  27     5338   4729   4364   -217     89   -211       C  
ATOM   2858  N   SER D  28       1.369 -16.728  -8.111  1.00 40.24           N  
ANISOU 2858  N   SER D  28     5595   4430   5266   -191    405     41       N  
ATOM   2859  CA  SER D  28       0.892 -16.442  -6.764  1.00 39.75           C  
ANISOU 2859  CA  SER D  28     5561   4384   5159   -162    497    227       C  
ATOM   2860  C   SER D  28       1.877 -15.534  -6.041  1.00 39.68           C  
ANISOU 2860  C   SER D  28     5639   4548   4889    -69    421    314       C  
ATOM   2861  O   SER D  28       3.092 -15.657  -6.217  1.00 40.67           O  
ANISOU 2861  O   SER D  28     5774   4704   4974    -12    352    312       O  
ATOM   2862  CB  SER D  28       0.706 -17.741  -5.969  1.00 44.42           C  
ANISOU 2862  CB  SER D  28     6150   4778   5950   -116    673    390       C  
ATOM   2863  OG  SER D  28       0.259 -17.460  -4.658  1.00 48.06           O  
ANISOU 2863  OG  SER D  28     6684   5260   6316    -36    801    595       O  
ATOM   2864  N   LEU D  29       1.355 -14.616  -5.230  1.00 41.17           N  
ANISOU 2864  N   LEU D  29     5879   4831   4933    -48    425    378       N  
ATOM   2865  CA  LEU D  29       2.215 -13.809  -4.373  1.00 39.25           C  
ANISOU 2865  CA  LEU D  29     5727   4721   4464     58    318    433       C  
ATOM   2866  C   LEU D  29       2.627 -14.564  -3.111  1.00 41.56           C  
ANISOU 2866  C   LEU D  29     6139   4970   4681    218    375    617       C  
ATOM   2867  O   LEU D  29       3.198 -13.976  -2.186  1.00 48.16           O  
ANISOU 2867  O   LEU D  29     7084   5907   5306    346    259    658       O  
ATOM   2868  CB  LEU D  29       1.511 -12.491  -4.022  1.00 43.84           C  
ANISOU 2868  CB  LEU D  29     6342   5413   4902     40    287    399       C  
ATOM   2869  CG  LEU D  29       1.771 -11.333  -4.987  1.00 43.65           C  
ANISOU 2869  CG  LEU D  29     6236   5488   4859    -44    156    248       C  
ATOM   2870  CD1 LEU D  29       1.037 -10.074  -4.545  1.00 41.05           C  
ANISOU 2870  CD1 LEU D  29     5940   5243   4413    -52    141    225       C  
ATOM   2871  CD2 LEU D  29       3.260 -11.041  -5.164  1.00 41.95           C  
ANISOU 2871  CD2 LEU D  29     5990   5317   4631      1     13    214       C  
ATOM   2872  N   SER D  30       2.321 -15.854  -3.051  1.00 39.18           N  
ANISOU 2872  N   SER D  30     5826   4507   4554    231    543    723       N  
ATOM   2873  CA  SER D  30       2.932 -16.751  -2.084  1.00 40.58           C  
ANISOU 2873  CA  SER D  30     6109   4624   4686    403    603    913       C  
ATOM   2874  C   SER D  30       4.302 -17.233  -2.534  1.00 45.79           C  
ANISOU 2874  C   SER D  30     6713   5276   5408    432    468    872       C  
ATOM   2875  O   SER D  30       5.007 -17.888  -1.756  1.00 56.27           O  
ANISOU 2875  O   SER D  30     8120   6573   6687    594    463   1023       O  
ATOM   2876  CB  SER D  30       2.021 -17.956  -1.855  1.00 48.44           C  
ANISOU 2876  CB  SER D  30     7086   5406   5913    406    883   1069       C  
ATOM   2877  OG  SER D  30       0.980 -17.606  -0.974  1.00 51.44           O  
ANISOU 2877  OG  SER D  30     7556   5783   6207    471   1057   1206       O  
ATOM   2878  N   THR D  31       4.676 -16.952  -3.776  1.00 40.42           N  
ANISOU 2878  N   THR D  31     5907   4614   4838    304    381    691       N  
ATOM   2879  CA  THR D  31       5.936 -17.424  -4.325  1.00 44.64           C  
ANISOU 2879  CA  THR D  31     6371   5115   5476    334    309    659       C  
ATOM   2880  C   THR D  31       7.018 -16.395  -4.058  1.00 38.44           C  
ANISOU 2880  C   THR D  31     5562   4468   4575    394     95    625       C  
ATOM   2881  O   THR D  31       6.853 -15.223  -4.391  1.00 37.07           O  
ANISOU 2881  O   THR D  31     5354   4398   4332    321     13    515       O  
ATOM   2882  CB  THR D  31       5.808 -17.683  -5.826  1.00 42.93           C  
ANISOU 2882  CB  THR D  31     6058   4830   5424    209    360    491       C  
ATOM   2883  OG1 THR D  31       4.709 -18.576  -6.051  1.00 45.43           O  
ANISOU 2883  OG1 THR D  31     6370   4993   5900    142    506    478       O  
ATOM   2884  CG2 THR D  31       7.083 -18.304  -6.354  1.00 48.95           C  
ANISOU 2884  CG2 THR D  31     6763   5530   6307    269    352    485       C  
ATOM   2885  N   SER D  31A      8.101 -16.827  -3.422  1.00 38.83           N  
ANISOU 2885  N   SER D  31A    5613   4502   4639    534     -4    720       N  
ATOM   2886  CA  SER D  31A      9.185 -15.903  -3.126  1.00 39.09           C  
ANISOU 2886  CA  SER D  31A    5577   4628   4648    594   -248    668       C  
ATOM   2887  C   SER D  31A      9.747 -15.342  -4.425  1.00 40.13           C  
ANISOU 2887  C   SER D  31A    5532   4750   4966    476   -239    541       C  
ATOM   2888  O   SER D  31A      9.881 -16.061  -5.422  1.00 38.82           O  
ANISOU 2888  O   SER D  31A    5310   4492   4947    431    -81    526       O  
ATOM   2889  CB  SER D  31A     10.281 -16.609  -2.336  1.00 46.42           C  
ANISOU 2889  CB  SER D  31A    6505   5515   5616    774   -378    786       C  
ATOM   2890  OG  SER D  31A     10.744 -17.726  -3.065  1.00 59.94           O  
ANISOU 2890  OG  SER D  31A    8129   7093   7554    761   -228    834       O  
ATOM   2891  N   GLY D  31B     10.054 -14.048  -4.414  1.00 37.44           N  
ANISOU 2891  N   GLY D  31B    5117   4490   4619    445   -390    452       N  
ATOM   2892  CA  GLY D  31B     10.574 -13.364  -5.582  1.00 38.08           C  
ANISOU 2892  CA  GLY D  31B    5035   4553   4881    361   -340    373       C  
ATOM   2893  C   GLY D  31B      9.544 -12.679  -6.455  1.00 37.21           C  
ANISOU 2893  C   GLY D  31B    4964   4497   4678    241   -212    291       C  
ATOM   2894  O   GLY D  31B      9.931 -11.940  -7.375  1.00 42.35           O  
ANISOU 2894  O   GLY D  31B    5507   5143   5440    202   -156    250       O  
ATOM   2895  N   MET D  32       8.258 -12.907  -6.226  1.00 34.27           N  
ANISOU 2895  N   MET D  32     4731   4159   4130    198   -148    284       N  
ATOM   2896  CA  MET D  32       7.217 -12.257  -7.012  1.00 32.94           C  
ANISOU 2896  CA  MET D  32     4588   4041   3886     98    -65    202       C  
ATOM   2897  C   MET D  32       6.905 -10.881  -6.422  1.00 37.25           C  
ANISOU 2897  C   MET D  32     5137   4680   4338     76   -181    167       C  
ATOM   2898  O   MET D  32       7.046 -10.665  -5.218  1.00 34.06           O  
ANISOU 2898  O   MET D  32     4786   4306   3852    142   -314    192       O  
ATOM   2899  CB  MET D  32       5.940 -13.093  -7.023  1.00 36.99           C  
ANISOU 2899  CB  MET D  32     5198   4516   4339     55     43    201       C  
ATOM   2900  CG  MET D  32       6.071 -14.436  -7.725  1.00 40.86           C  
ANISOU 2900  CG  MET D  32     5688   4886   4953     63    153    191       C  
ATOM   2901  SD  MET D  32       6.387 -14.200  -9.475  1.00 40.95           S  
ANISOU 2901  SD  MET D  32     5666   4898   4994     50    217     62       S  
ATOM   2902  CE  MET D  32       6.413 -15.911 -10.023  1.00 43.52           C  
ANISOU 2902  CE  MET D  32     6030   5058   5448     82    319     17       C  
ATOM   2903  N   GLY D  33       6.461  -9.953  -7.276  1.00 31.47           N  
ANISOU 2903  N   GLY D  33     4368   3990   3600      5   -134    103       N  
ATOM   2904  CA  GLY D  33       6.048  -8.636  -6.805  1.00 32.14           C  
ANISOU 2904  CA  GLY D  33     4452   4142   3618    -23   -219     62       C  
ATOM   2905  C   GLY D  33       5.339  -7.874  -7.904  1.00 36.27           C  
ANISOU 2905  C   GLY D  33     4955   4702   4125    -89   -122     20       C  
ATOM   2906  O   GLY D  33       5.447  -8.214  -9.085  1.00 33.73           O  
ANISOU 2906  O   GLY D  33     4618   4362   3836    -86    -15     16       O  
ATOM   2907  N   VAL D  34       4.597  -6.843  -7.500  1.00 30.85           N  
ANISOU 2907  N   VAL D  34     4289   4068   3363   -122   -163    -11       N  
ATOM   2908  CA  VAL D  34       3.702  -6.130  -8.414  1.00 29.64           C  
ANISOU 2908  CA  VAL D  34     4132   3958   3171   -168    -86    -38       C  
ATOM   2909  C   VAL D  34       3.820  -4.631  -8.168  1.00 32.20           C  
ANISOU 2909  C   VAL D  34     4395   4296   3544   -180   -136    -57       C  
ATOM   2910  O   VAL D  34       3.777  -4.181  -7.021  1.00 31.04           O  
ANISOU 2910  O   VAL D  34     4277   4153   3365   -170   -242    -90       O  
ATOM   2911  CB  VAL D  34       2.231  -6.582  -8.248  1.00 35.85           C  
ANISOU 2911  CB  VAL D  34     4998   4767   3855   -207    -48    -54       C  
ATOM   2912  CG1 VAL D  34       1.314  -5.758  -9.171  1.00 38.41           C  
ANISOU 2912  CG1 VAL D  34     5303   5139   4152   -238    -16    -89       C  
ATOM   2913  CG2 VAL D  34       2.075  -8.092  -8.551  1.00 33.46           C  
ANISOU 2913  CG2 VAL D  34     4728   4406   3580   -206      1    -53       C  
ATOM   2914  N   SER D  35       3.933  -3.851  -9.250  1.00 29.97           N  
ANISOU 2914  N   SER D  35     4046   4011   3330   -181    -51    -36       N  
ATOM   2915  CA  SER D  35       4.012  -2.400  -9.181  1.00 29.32           C  
ANISOU 2915  CA  SER D  35     3883   3908   3349   -194    -62    -40       C  
ATOM   2916  C   SER D  35       2.731  -1.788  -9.729  1.00 32.43           C  
ANISOU 2916  C   SER D  35     4328   4366   3628   -210      2    -36       C  
ATOM   2917  O   SER D  35       2.044  -2.394 -10.564  1.00 28.72           O  
ANISOU 2917  O   SER D  35     3925   3947   3040   -194     57    -29       O  
ATOM   2918  CB  SER D  35       5.192  -1.863 -10.024  1.00 29.80           C  
ANISOU 2918  CB  SER D  35     3802   3882   3638   -158     37     32       C  
ATOM   2919  OG  SER D  35       6.366  -1.721  -9.250  1.00 31.92           O  
ANISOU 2919  OG  SER D  35     3939   4052   4138   -161    -80      5       O  
ATOM   2920  N   TRP D  36       2.427  -0.572  -9.266  1.00 28.32           N  
ANISOU 2920  N   TRP D  36     3769   3830   3162   -231    -27    -58       N  
ATOM   2921  CA  TRP D  36       1.435   0.290  -9.893  1.00 28.15           C  
ANISOU 2921  CA  TRP D  36     3753   3845   3098   -229     45    -30       C  
ATOM   2922  C   TRP D  36       2.164   1.422 -10.607  1.00 32.06           C  
ANISOU 2922  C   TRP D  36     4136   4264   3781   -196    143     46       C  
ATOM   2923  O   TRP D  36       3.072   2.034 -10.033  1.00 32.57           O  
ANISOU 2923  O   TRP D  36     4088   4222   4064   -216     98     22       O  
ATOM   2924  CB  TRP D  36       0.482   0.886  -8.849  1.00 28.44           C  
ANISOU 2924  CB  TRP D  36     3828   3895   3085   -263    -14    -92       C  
ATOM   2925  CG  TRP D  36      -0.579  -0.069  -8.398  1.00 28.46           C  
ANISOU 2925  CG  TRP D  36     3922   3953   2937   -278    -21   -111       C  
ATOM   2926  CD1 TRP D  36      -0.560  -0.816  -7.256  1.00 32.89           C  
ANISOU 2926  CD1 TRP D  36     4562   4509   3427   -271    -63   -138       C  
ATOM   2927  CD2 TRP D  36      -1.784  -0.427  -9.095  1.00 28.16           C  
ANISOU 2927  CD2 TRP D  36     3893   3961   2845   -288     22    -93       C  
ATOM   2928  NE1 TRP D  36      -1.690  -1.603  -7.184  1.00 34.32           N  
ANISOU 2928  NE1 TRP D  36     4783   4708   3549   -286     -2   -114       N  
ATOM   2929  CE2 TRP D  36      -2.461  -1.380  -8.293  1.00 33.37           C  
ANISOU 2929  CE2 TRP D  36     4601   4612   3465   -309     28   -105       C  
ATOM   2930  CE3 TRP D  36      -2.368  -0.022 -10.298  1.00 33.48           C  
ANISOU 2930  CE3 TRP D  36     4537   4673   3512   -261     44    -66       C  
ATOM   2931  CZ2 TRP D  36      -3.691  -1.927  -8.656  1.00 33.22           C  
ANISOU 2931  CZ2 TRP D  36     4553   4592   3477   -333     50   -105       C  
ATOM   2932  CZ3 TRP D  36      -3.585  -0.577 -10.666  1.00 34.27           C  
ANISOU 2932  CZ3 TRP D  36     4632   4799   3591   -271     13    -92       C  
ATOM   2933  CH2 TRP D  36      -4.236  -1.521  -9.840  1.00 33.81           C  
ANISOU 2933  CH2 TRP D  36     4575   4703   3569   -322     15   -118       C  
ATOM   2934  N   ILE D  37       1.756   1.702 -11.846  1.00 30.84           N  
ANISOU 2934  N   ILE D  37     4010   4149   3560   -127    270    139       N  
ATOM   2935  CA  ILE D  37       2.343   2.747 -12.685  1.00 34.43           C  
ANISOU 2935  CA  ILE D  37     4379   4524   4179    -56    436    270       C  
ATOM   2936  C   ILE D  37       1.203   3.503 -13.360  1.00 37.44           C  
ANISOU 2936  C   ILE D  37     4820   4970   4436      4    490    329       C  
ATOM   2937  O   ILE D  37       0.193   2.902 -13.745  1.00 37.60           O  
ANISOU 2937  O   ILE D  37     4954   5109   4223     32    421    289       O  
ATOM   2938  CB  ILE D  37       3.286   2.154 -13.765  1.00 31.14           C  
ANISOU 2938  CB  ILE D  37     3979   4087   3766     52    598    381       C  
ATOM   2939  CG1 ILE D  37       4.397   1.290 -13.144  1.00 34.96           C  
ANISOU 2939  CG1 ILE D  37     4390   4504   4389      3    538    330       C  
ATOM   2940  CG2 ILE D  37       3.909   3.249 -14.601  1.00 32.78           C  
ANISOU 2940  CG2 ILE D  37     4096   4184   4174    152    836    564       C  
ATOM   2941  CD1 ILE D  37       4.279  -0.178 -13.495  1.00 44.81           C  
ANISOU 2941  CD1 ILE D  37     5777   5840   5410     39    511    285       C  
ATOM   2942  N   ARG D  38       1.363   4.808 -13.556  1.00 31.14           N  
ANISOU 2942  N   ARG D  38     3927   4078   3827     32    606    427       N  
ATOM   2943  CA  ARG D  38       0.288   5.548 -14.203  1.00 31.44           C  
ANISOU 2943  CA  ARG D  38     4020   4176   3749    110    656    503       C  
ATOM   2944  C   ARG D  38       0.816   6.402 -15.347  1.00 33.90           C  
ANISOU 2944  C   ARG D  38     4309   4414   4156    264    904    722       C  
ATOM   2945  O   ARG D  38       2.008   6.707 -15.437  1.00 35.55           O  
ANISOU 2945  O   ARG D  38     4401   4476   4631    276   1062    816       O  
ATOM   2946  CB  ARG D  38      -0.472   6.418 -13.212  1.00 31.65           C  
ANISOU 2946  CB  ARG D  38     3982   4163   3879     16    569    419       C  
ATOM   2947  CG  ARG D  38       0.329   7.564 -12.628  1.00 31.84           C  
ANISOU 2947  CG  ARG D  38     3848   3998   4253    -35    628    424       C  
ATOM   2948  CD  ARG D  38      -0.588   8.394 -11.703  1.00 36.64           C  
ANISOU 2948  CD  ARG D  38     4441   4579   4904    -97    542    318       C  
ATOM   2949  NE  ARG D  38       0.099   9.543 -11.132  1.00 35.79           N  
ANISOU 2949  NE  ARG D  38     4184   4266   5149   -141    562    277       N  
ATOM   2950  CZ  ARG D  38      -0.448  10.373 -10.252  1.00 43.29           C  
ANISOU 2950  CZ  ARG D  38     5118   5147   6183   -182    493    157       C  
ATOM   2951  NH1 ARG D  38      -1.693  10.207  -9.828  1.00 40.43           N  
ANISOU 2951  NH1 ARG D  38     4872   4905   5586   -181    439     99       N  
ATOM   2952  NH2 ARG D  38       0.272  11.390  -9.787  1.00 36.94           N  
ANISOU 2952  NH2 ARG D  38     4168   4128   5741   -217    483     87       N  
ATOM   2953  N   GLN D  39      -0.113   6.800 -16.207  1.00 33.85           N  
ANISOU 2953  N   GLN D  39     4409   4500   3954    397    943    815       N  
ATOM   2954  CA  GLN D  39       0.204   7.612 -17.370  1.00 35.94           C  
ANISOU 2954  CA  GLN D  39     4706   4716   4235    600   1203   1061       C  
ATOM   2955  C   GLN D  39      -0.954   8.545 -17.683  1.00 36.46           C  
ANISOU 2955  C   GLN D  39     4804   4827   4221    681   1187   1132       C  
ATOM   2956  O   GLN D  39      -1.994   8.090 -18.178  1.00 43.19           O  
ANISOU 2956  O   GLN D  39     5800   5847   4763    768   1028   1078       O  
ATOM   2957  CB  GLN D  39       0.475   6.723 -18.578  1.00 37.18           C  
ANISOU 2957  CB  GLN D  39     5066   4983   4078    806   1285   1138       C  
ATOM   2958  CG  GLN D  39       0.986   7.473 -19.783  1.00 45.16           C  
ANISOU 2958  CG  GLN D  39     6149   5935   5077   1067   1620   1433       C  
ATOM   2959  CD  GLN D  39       1.293   6.536 -20.911  1.00 49.65           C  
ANISOU 2959  CD  GLN D  39     6964   6616   5287   1304   1704   1484       C  
ATOM   2960  OE1 GLN D  39       0.684   5.478 -21.019  1.00 48.59           O  
ANISOU 2960  OE1 GLN D  39     6979   6639   4845   1304   1447   1283       O  
ATOM   2961  NE2 GLN D  39       2.270   6.888 -21.733  1.00 43.97           N  
ANISOU 2961  NE2 GLN D  39     6280   5791   4634   1511   2079   1748       N  
ATOM   2962  N   PRO D  40      -0.824   9.840 -17.417  1.00 42.67           N  
ANISOU 2962  N   PRO D  40     5629   5032   5552    840   1073   2213       N  
ATOM   2963  CA  PRO D  40      -1.785  10.797 -17.983  1.00 46.32           C  
ANISOU 2963  CA  PRO D  40     6067   5386   6148   1096   1034   2587       C  
ATOM   2964  C   PRO D  40      -1.845  10.649 -19.494  1.00 58.60           C  
ANISOU 2964  C   PRO D  40     7750   7268   7246   1309    857   2908       C  
ATOM   2965  O   PRO D  40      -0.857  10.291 -20.139  1.00 63.27           O  
ANISOU 2965  O   PRO D  40     8506   8047   7487   1261    951   2937       O  
ATOM   2966  CB  PRO D  40      -1.223  12.160 -17.557  1.00 52.44           C  
ANISOU 2966  CB  PRO D  40     6899   5709   7318   1038   1400   2752       C  
ATOM   2967  CG  PRO D  40      -0.484  11.838 -16.282  1.00 52.96           C  
ANISOU 2967  CG  PRO D  40     6946   5624   7553    746   1524   2318       C  
ATOM   2968  CD  PRO D  40       0.179  10.504 -16.573  1.00 49.37           C  
ANISOU 2968  CD  PRO D  40     6510   5556   6694    629   1377   2114       C  
ATOM   2969  N   SER D  41      -3.032  10.898 -20.049  1.00 61.12           N  
ANISOU 2969  N   SER D  41     7993   7671   7558   1564    592   3146       N  
ATOM   2970  CA  SER D  41      -3.298  10.670 -21.469  1.00 68.56           C  
ANISOU 2970  CA  SER D  41     9078   8981   7990   1805    306   3416       C  
ATOM   2971  C   SER D  41      -2.277  11.370 -22.356  1.00 79.35           C  
ANISOU 2971  C   SER D  41    10720  10347   9082   1888    616   3808       C  
ATOM   2972  O   SER D  41      -2.199  12.604 -22.381  1.00 68.96           O  
ANISOU 2972  O   SER D  41     9423   8712   8065   1971    888   4184       O  
ATOM   2973  CB  SER D  41      -4.711  11.148 -21.818  1.00 72.07           C  
ANISOU 2973  CB  SER D  41     9355   9432   8594   2084    -12   3693       C  
ATOM   2974  OG  SER D  41      -5.097  10.721 -23.114  1.00 73.84           O  
ANISOU 2974  OG  SER D  41     9710  10074   8271   2308   -428   3860       O  
ATOM   2975  N   GLY D  42      -1.503  10.569 -23.090  1.00 78.64           N  
ANISOU 2975  N   GLY D  42    10838  10592   8449   1871    607   3715       N  
ATOM   2976  CA  GLY D  42      -0.523  11.098 -24.020  1.00 75.10           C  
ANISOU 2976  CA  GLY D  42    10616  10181   7738   1916    921   3986       C  
ATOM   2977  C   GLY D  42       0.696  11.706 -23.364  1.00 78.65           C  
ANISOU 2977  C   GLY D  42    11002  10276   8603   1664   1423   3986       C  
ATOM   2978  O   GLY D  42       1.355  12.558 -23.970  1.00 86.51           O  
ANISOU 2978  O   GLY D  42    12065  11151   9655   1671   1704   4231       O  
ATOM   2979  N   LYS D  43       1.019  11.291 -22.144  1.00 68.17           N  
ANISOU 2979  N   LYS D  43     9530   8778   7596   1425   1512   3689       N  
ATOM   2980  CA  LYS D  43       2.114  11.893 -21.393  1.00 72.30           C  
ANISOU 2980  CA  LYS D  43     9954   8934   8582   1152   1898   3633       C  
ATOM   2981  C   LYS D  43       3.045  10.785 -20.905  1.00 56.10           C  
ANISOU 2981  C   LYS D  43     7847   7037   6430    924   1930   3227       C  
ATOM   2982  O   LYS D  43       3.067   9.658 -21.419  1.00 60.47           O  
ANISOU 2982  O   LYS D  43     8487   7972   6518    998   1753   3045       O  
ATOM   2983  CB  LYS D  43       1.578  12.769 -20.248  1.00 65.46           C  
ANISOU 2983  CB  LYS D  43     8939   7601   8331   1055   1940   3574       C  
ATOM   2984  CG  LYS D  43       0.806  14.004 -20.722  1.00 69.56           C  
ANISOU 2984  CG  LYS D  43     9470   7907   9052   1272   1950   3936       C  
ATOM   2985  CD  LYS D  43       1.694  14.895 -21.583  1.00 79.99           C  
ANISOU 2985  CD  LYS D  43    10856   9145  10390   1265   2217   4203       C  
ATOM   2986  CE  LYS D  43       0.956  16.119 -22.151  1.00 94.07           C  
ANISOU 2986  CE  LYS D  43    12660  10740  12342   1490   2230   4577       C  
ATOM   2987  NZ  LYS D  43       1.274  17.410 -21.463  1.00 75.52           N  
ANISOU 2987  NZ  LYS D  43    10207   7848  10637   1347   2496   4585       N  
ATOM   2988  N   GLY D  44       3.846  11.096 -19.893  1.00 56.71           N  
ANISOU 2988  N   GLY D  44     7775   6803   6969    643   2126   3043       N  
ATOM   2989  CA  GLY D  44       4.863  10.170 -19.446  1.00 49.44           C  
ANISOU 2989  CA  GLY D  44     6765   6004   6016    436   2162   2708       C  
ATOM   2990  C   GLY D  44       4.345   9.122 -18.480  1.00 48.80           C  
ANISOU 2990  C   GLY D  44     6606   6029   5906    345   1838   2224       C  
ATOM   2991  O   GLY D  44       3.191   9.132 -18.037  1.00 50.83           O  
ANISOU 2991  O   GLY D  44     6848   6242   6223    412   1614   2122       O  
ATOM   2992  N   LEU D  45       5.232   8.187 -18.147  1.00 44.39           N  
ANISOU 2992  N   LEU D  45     5977   5602   5288    202   1844   1954       N  
ATOM   2993  CA  LEU D  45       4.935   7.120 -17.207  1.00 45.40           C  
ANISOU 2993  CA  LEU D  45     6035   5814   5401    107   1587   1537       C  
ATOM   2994  C   LEU D  45       5.532   7.467 -15.846  1.00 36.51           C  
ANISOU 2994  C   LEU D  45     4778   4410   4684   -145   1630   1324       C  
ATOM   2995  O   LEU D  45       6.665   7.961 -15.772  1.00 40.38           O  
ANISOU 2995  O   LEU D  45     5176   4757   5407   -293   1827   1397       O  
ATOM   2996  CB  LEU D  45       5.498   5.789 -17.727  1.00 40.60           C  
ANISOU 2996  CB  LEU D  45     5455   5520   4452    151   1538   1377       C  
ATOM   2997  CG  LEU D  45       4.726   5.226 -18.925  1.00 43.54           C  
ANISOU 2997  CG  LEU D  45     6005   6187   4352    399   1374   1443       C  
ATOM   2998  CD1 LEU D  45       5.603   4.323 -19.764  1.00 38.95           C  
ANISOU 2998  CD1 LEU D  45     5520   5860   3420    486   1489   1382       C  
ATOM   2999  CD2 LEU D  45       3.484   4.467 -18.479  1.00 39.22           C  
ANISOU 2999  CD2 LEU D  45     5427   5696   3778    417   1004   1188       C  
ATOM   3000  N   GLU D  46       4.752   7.231 -14.781  1.00 36.76           N  
ANISOU 3000  N   GLU D  46     4799   4364   4805   -187   1445   1071       N  
ATOM   3001  CA  GLU D  46       5.150   7.537 -13.408  1.00 41.92           C  
ANISOU 3001  CA  GLU D  46     5403   4783   5742   -386   1435    826       C  
ATOM   3002  C   GLU D  46       4.932   6.312 -12.524  1.00 37.32           C  
ANISOU 3002  C   GLU D  46     4807   4358   5014   -420   1237    522       C  
ATOM   3003  O   GLU D  46       3.794   5.844 -12.361  1.00 32.31           O  
ANISOU 3003  O   GLU D  46     4202   3798   4275   -309   1128    470       O  
ATOM   3004  CB  GLU D  46       4.367   8.737 -12.850  1.00 37.60           C  
ANISOU 3004  CB  GLU D  46     4919   3910   5458   -367   1499    854       C  
ATOM   3005  CG  GLU D  46       4.822   9.170 -11.469  1.00 47.74           C  
ANISOU 3005  CG  GLU D  46     6222   4936   6981   -561   1483    560       C  
ATOM   3006  CD  GLU D  46       4.045  10.360 -10.924  1.00 53.71           C  
ANISOU 3006  CD  GLU D  46     7081   5334   7993   -512   1584    539       C  
ATOM   3007  OE1 GLU D  46       2.849  10.523 -11.262  1.00 46.70           O  
ANISOU 3007  OE1 GLU D  46     6218   4452   7075   -300   1618    689       O  
ATOM   3008  OE2 GLU D  46       4.666  11.177 -10.208  1.00 52.66           O1-
ANISOU 3008  OE2 GLU D  46     6989   4889   8130   -682   1624    374       O1-
ATOM   3009  N   TRP D  47       6.015   5.822 -11.922  1.00 34.72           N  
ANISOU 3009  N   TRP D  47     4407   4060   4727   -572   1194    353       N  
ATOM   3010  CA  TRP D  47       5.946   4.672 -11.037  1.00 31.06           C  
ANISOU 3010  CA  TRP D  47     3941   3724   4138   -596   1023    116       C  
ATOM   3011  C   TRP D  47       5.470   5.097  -9.648  1.00 35.78           C  
ANISOU 3011  C   TRP D  47     4633   4143   4819   -655    972    -72       C  
ATOM   3012  O   TRP D  47       5.983   6.064  -9.072  1.00 36.75           O  
ANISOU 3012  O   TRP D  47     4785   4047   5132   -780    999   -150       O  
ATOM   3013  CB  TRP D  47       7.315   4.002 -10.947  1.00 34.75           C  
ANISOU 3013  CB  TRP D  47     4283   4295   4626   -697    983     46       C  
ATOM   3014  CG  TRP D  47       7.365   2.880  -9.939  1.00 34.23           C  
ANISOU 3014  CG  TRP D  47     4220   4326   4458   -713    802   -156       C  
ATOM   3015  CD1 TRP D  47       6.957   1.575 -10.118  1.00 33.99           C  
ANISOU 3015  CD1 TRP D  47     4200   4462   4254   -606    728   -193       C  
ATOM   3016  CD2 TRP D  47       7.839   2.973  -8.595  1.00 32.45           C  
ANISOU 3016  CD2 TRP D  47     4012   4019   4299   -833    665   -332       C  
ATOM   3017  NE1 TRP D  47       7.154   0.854  -8.948  1.00 35.41           N  
ANISOU 3017  NE1 TRP D  47     4390   4655   4408   -646    592   -331       N  
ATOM   3018  CE2 TRP D  47       7.697   1.689  -8.004  1.00 36.91           C  
ANISOU 3018  CE2 TRP D  47     4600   4725   4699   -771    538   -415       C  
ATOM   3019  CE3 TRP D  47       8.373   4.016  -7.830  1.00 32.89           C  
ANISOU 3019  CE3 TRP D  47     4084   3884   4531   -986    613   -439       C  
ATOM   3020  CZ2 TRP D  47       8.080   1.431  -6.689  1.00 34.47           C  
ANISOU 3020  CZ2 TRP D  47     4347   4412   4338   -828    370   -556       C  
ATOM   3021  CZ3 TRP D  47       8.747   3.758  -6.522  1.00 42.05           C  
ANISOU 3021  CZ3 TRP D  47     5307   5046   5623  -1056    402   -644       C  
ATOM   3022  CH2 TRP D  47       8.594   2.479  -5.962  1.00 34.50           C  
ANISOU 3022  CH2 TRP D  47     4392   4274   4441   -962    287   -679       C  
ATOM   3023  N   LEU D  48       4.492   4.367  -9.108  1.00 35.16           N  
ANISOU 3023  N   LEU D  48     4610   4143   4607   -566    911   -152       N  
ATOM   3024  CA  LEU D  48       3.843   4.743  -7.848  1.00 37.61           C  
ANISOU 3024  CA  LEU D  48     5049   4308   4932   -558    942   -300       C  
ATOM   3025  C   LEU D  48       4.343   3.950  -6.639  1.00 32.73           C  
ANISOU 3025  C   LEU D  48     4502   3770   4164   -623    822   -490       C  
ATOM   3026  O   LEU D  48       4.791   4.546  -5.644  1.00 32.39           O  
ANISOU 3026  O   LEU D  48     4588   3604   4114   -704    783   -667       O  
ATOM   3027  CB  LEU D  48       2.323   4.592  -8.000  1.00 33.97           C  
ANISOU 3027  CB  LEU D  48     4576   3857   4476   -394   1020   -204       C  
ATOM   3028  CG  LEU D  48       1.809   5.445  -9.167  1.00 36.27           C  
ANISOU 3028  CG  LEU D  48     4805   4078   4899   -297   1089     14       C  
ATOM   3029  CD1 LEU D  48       0.331   5.188  -9.406  1.00 38.08           C  
ANISOU 3029  CD1 LEU D  48     4943   4347   5179   -134   1094    123       C  
ATOM   3030  CD2 LEU D  48       2.072   6.937  -8.923  1.00 40.56           C  
ANISOU 3030  CD2 LEU D  48     5440   4325   5646   -332   1229     14       C  
ATOM   3031  N   ALA D  49       4.284   2.627  -6.711  1.00 37.35           N  
ANISOU 3031  N   ALA D  49     5022   4544   4624   -581    743   -459       N  
ATOM   3032  CA  ALA D  49       4.571   1.767  -5.568  1.00 31.62           C  
ANISOU 3032  CA  ALA D  49     4375   3897   3742   -593    647   -563       C  
ATOM   3033  C   ALA D  49       4.774   0.342  -6.062  1.00 31.81           C  
ANISOU 3033  C   ALA D  49     4274   4081   3732   -559    565   -488       C  
ATOM   3034  O   ALA D  49       4.313  -0.029  -7.143  1.00 30.59           O  
ANISOU 3034  O   ALA D  49     4017   3972   3634   -508    591   -400       O  
ATOM   3035  CB  ALA D  49       3.441   1.808  -4.530  1.00 34.81           C  
ANISOU 3035  CB  ALA D  49     4940   4240   4046   -497    782   -596       C  
ATOM   3036  N   HIS D  50       5.447  -0.460  -5.234  1.00 29.95           N  
ANISOU 3036  N   HIS D  50     4069   3917   3395   -573    445   -533       N  
ATOM   3037  CA  HIS D  50       5.684  -1.865  -5.505  1.00 32.86           C  
ANISOU 3037  CA  HIS D  50     4339   4379   3765   -524    378   -470       C  
ATOM   3038  C   HIS D  50       5.465  -2.633  -4.204  1.00 30.89           C  
ANISOU 3038  C   HIS D  50     4216   4143   3376   -472    353   -443       C  
ATOM   3039  O   HIS D  50       5.816  -2.149  -3.125  1.00 30.13           O  
ANISOU 3039  O   HIS D  50     4274   4055   3118   -487    289   -510       O  
ATOM   3040  CB  HIS D  50       7.098  -2.080  -6.030  1.00 33.39           C  
ANISOU 3040  CB  HIS D  50     4260   4517   3909   -566    266   -485       C  
ATOM   3041  CG  HIS D  50       7.358  -3.464  -6.537  1.00 32.74           C  
ANISOU 3041  CG  HIS D  50     4078   4491   3871   -485    238   -443       C  
ATOM   3042  ND1 HIS D  50       7.001  -3.854  -7.810  1.00 30.88           N  
ANISOU 3042  ND1 HIS D  50     3784   4269   3680   -432    312   -439       N  
ATOM   3043  CD2 HIS D  50       7.990  -4.525  -5.981  1.00 37.18           C  
ANISOU 3043  CD2 HIS D  50     4602   5082   4444   -433    134   -414       C  
ATOM   3044  CE1 HIS D  50       7.378  -5.107  -8.009  1.00 34.43           C  
ANISOU 3044  CE1 HIS D  50     4176   4726   4179   -358    273   -450       C  
ATOM   3045  NE2 HIS D  50       7.975  -5.540  -6.910  1.00 34.83           N  
ANISOU 3045  NE2 HIS D  50     4222   4774   4238   -353    178   -412       N  
ATOM   3046  N   ILE D  51       4.898  -3.832  -4.318  1.00 31.30           N  
ANISOU 3046  N   ILE D  51     4219   4186   3485   -408    396   -344       N  
ATOM   3047  CA  ILE D  51       4.670  -4.701  -3.166  1.00 31.00           C  
ANISOU 3047  CA  ILE D  51     4293   4144   3342   -340    422   -237       C  
ATOM   3048  C   ILE D  51       5.247  -6.073  -3.487  1.00 32.69           C  
ANISOU 3048  C   ILE D  51     4390   4351   3680   -302    325   -164       C  
ATOM   3049  O   ILE D  51       4.972  -6.634  -4.556  1.00 29.35           O  
ANISOU 3049  O   ILE D  51     3830   3871   3452   -308    339   -188       O  
ATOM   3050  CB  ILE D  51       3.173  -4.787  -2.801  1.00 30.75           C  
ANISOU 3050  CB  ILE D  51     4304   4024   3353   -296    658   -135       C  
ATOM   3051  CG1 ILE D  51       2.985  -5.564  -1.470  1.00 29.45           C  
ANISOU 3051  CG1 ILE D  51     4300   3858   3030   -208    756     30       C  
ATOM   3052  CG2 ILE D  51       2.341  -5.351  -3.950  1.00 30.91           C  
ANISOU 3052  CG2 ILE D  51     4114   3965   3665   -321    689   -106       C  
ATOM   3053  CD1 ILE D  51       1.685  -5.271  -0.703  1.00 32.41           C  
ANISOU 3053  CD1 ILE D  51     4779   4175   3360   -139   1069    137       C  
ATOM   3054  N   PHE D  52       6.043  -6.613  -2.563  1.00 34.92           N  
ANISOU 3054  N   PHE D  52     4744   4683   3841   -244    208    -86       N  
ATOM   3055  CA  PHE D  52       6.685  -7.909  -2.735  1.00 36.17           C  
ANISOU 3055  CA  PHE D  52     4795   4803   4144   -172    123      7       C  
ATOM   3056  C   PHE D  52       5.870  -9.005  -2.046  1.00 37.29           C  
ANISOU 3056  C   PHE D  52     5016   4822   4329    -96    256    218       C  
ATOM   3057  O   PHE D  52       4.986  -8.739  -1.226  1.00 34.73           O  
ANISOU 3057  O   PHE D  52     4843   4490   3862    -83    416    319       O  
ATOM   3058  CB  PHE D  52       8.106  -7.897  -2.167  1.00 31.52           C  
ANISOU 3058  CB  PHE D  52     4183   4332   3461   -130   -114     19       C  
ATOM   3059  CG  PHE D  52       9.057  -7.005  -2.917  1.00 37.18           C  
ANISOU 3059  CG  PHE D  52     4736   5127   4262   -218   -221   -144       C  
ATOM   3060  CD1 PHE D  52       9.633  -7.427  -4.099  1.00 32.40           C  
ANISOU 3060  CD1 PHE D  52     3919   4498   3893   -197   -185   -185       C  
ATOM   3061  CD2 PHE D  52       9.399  -5.766  -2.411  1.00 34.35           C  
ANISOU 3061  CD2 PHE D  52     4446   4845   3762   -314   -334   -255       C  
ATOM   3062  CE1 PHE D  52      10.523  -6.607  -4.797  1.00 34.42           C  
ANISOU 3062  CE1 PHE D  52     4006   4822   4250   -267   -211   -278       C  
ATOM   3063  CE2 PHE D  52      10.280  -4.939  -3.094  1.00 44.63           C  
ANISOU 3063  CE2 PHE D  52     5560   6173   5222   -418   -402   -366       C  
ATOM   3064  CZ  PHE D  52      10.848  -5.366  -4.288  1.00 37.02           C  
ANISOU 3064  CZ  PHE D  52     4359   5204   4504   -391   -318   -347       C  
ATOM   3065  N   TRP D  53       6.222 -10.258  -2.373  1.00 31.39           N  
ANISOU 3065  N   TRP D  53     3420   4478   4027  -1010    280   -136       N  
ATOM   3066  CA  TRP D  53       5.533 -11.437  -1.841  1.00 34.04           C  
ANISOU 3066  CA  TRP D  53     3756   4731   4448  -1050    248     25       C  
ATOM   3067  C   TRP D  53       5.487 -11.437  -0.322  1.00 34.66           C  
ANISOU 3067  C   TRP D  53     4016   4802   4352  -1060    367    137       C  
ATOM   3068  O   TRP D  53       4.541 -11.974   0.274  1.00 38.50           O  
ANISOU 3068  O   TRP D  53     4470   5270   4889  -1077    465    357       O  
ATOM   3069  CB  TRP D  53       6.236 -12.711  -2.341  1.00 32.86           C  
ANISOU 3069  CB  TRP D  53     3591   4516   4377  -1032    -46    -30       C  
ATOM   3070  CG  TRP D  53       7.552 -12.928  -1.653  1.00 32.68           C  
ANISOU 3070  CG  TRP D  53     3701   4531   4186  -1011   -151   -102       C  
ATOM   3071  CD1 TRP D  53       7.779 -13.765  -0.596  1.00 37.96           C  
ANISOU 3071  CD1 TRP D  53     4494   5138   4791  -1053   -218    -22       C  
ATOM   3072  CD2 TRP D  53       8.813 -12.304  -1.947  1.00 34.78           C  
ANISOU 3072  CD2 TRP D  53     3961   4915   4340   -957   -212   -217       C  
ATOM   3073  NE1 TRP D  53       9.096 -13.697  -0.209  1.00 37.92           N  
ANISOU 3073  NE1 TRP D  53     4577   5196   4635  -1027   -316   -103       N  
ATOM   3074  CE2 TRP D  53       9.755 -12.815  -1.030  1.00 35.83           C  
ANISOU 3074  CE2 TRP D  53     4217   5048   4348   -976   -323   -199       C  
ATOM   3075  CE3 TRP D  53       9.246 -11.372  -2.913  1.00 34.68           C  
ANISOU 3075  CE3 TRP D  53     3821   5022   4335   -904   -195   -292       C  
ATOM   3076  CZ2 TRP D  53      11.091 -12.423  -1.035  1.00 35.64           C  
ANISOU 3076  CZ2 TRP D  53     4178   5144   4220   -956   -429   -224       C  
ATOM   3077  CZ3 TRP D  53      10.574 -10.998  -2.924  1.00 32.16           C  
ANISOU 3077  CZ3 TRP D  53     3472   4831   3918   -883   -299   -296       C  
ATOM   3078  CH2 TRP D  53      11.483 -11.512  -1.988  1.00 37.57           C  
ANISOU 3078  CH2 TRP D  53     4266   5518   4492   -916   -420   -250       C  
ATOM   3079  N   ASP D  54       6.482 -10.839   0.333  1.00 37.57           N  
ANISOU 3079  N   ASP D  54     4575   5187   4513  -1044    344     25       N  
ATOM   3080  CA  ASP D  54       6.534 -10.874   1.790  1.00 41.57           C  
ANISOU 3080  CA  ASP D  54     5316   5664   4816  -1019    420    107       C  
ATOM   3081  C   ASP D  54       5.918  -9.629   2.443  1.00 43.78           C  
ANISOU 3081  C   ASP D  54     5795   5954   4886   -903    660    133       C  
ATOM   3082  O   ASP D  54       6.178  -9.375   3.625  1.00 40.36           O  
ANISOU 3082  O   ASP D  54     5651   5479   4206   -829    690    145       O  
ATOM   3083  CB  ASP D  54       7.980 -11.065   2.261  1.00 41.13           C  
ANISOU 3083  CB  ASP D  54     5405   5585   4638  -1065    199     -4       C  
ATOM   3084  CG  ASP D  54       8.881  -9.902   1.903  1.00 42.83           C  
ANISOU 3084  CG  ASP D  54     5682   5820   4772  -1093    101   -139       C  
ATOM   3085  OD1 ASP D  54       8.490  -9.042   1.076  1.00 39.44           O  
ANISOU 3085  OD1 ASP D  54     5157   5422   4405  -1077    181   -186       O  
ATOM   3086  OD2 ASP D  54      10.000  -9.841   2.454  1.00 42.32           O1-
ANISOU 3086  OD2 ASP D  54     5750   5736   4593  -1148    -81   -169       O1-
ATOM   3087  N   ASP D  55       5.099  -8.870   1.705  1.00 39.58           N  
ANISOU 3087  N   ASP D  55     5150   5465   4425   -854    818    141       N  
ATOM   3088  CA  ASP D  55       4.407  -7.676   2.192  1.00 42.21           C  
ANISOU 3088  CA  ASP D  55     5686   5808   4542   -686   1056    169       C  
ATOM   3089  C   ASP D  55       5.347  -6.493   2.410  1.00 43.81           C  
ANISOU 3089  C   ASP D  55     6201   5912   4532   -676    915    -38       C  
ATOM   3090  O   ASP D  55       4.988  -5.527   3.098  1.00 41.55           O  
ANISOU 3090  O   ASP D  55     6240   5570   3978   -497   1037    -48       O  
ATOM   3091  CB  ASP D  55       3.628  -7.961   3.476  1.00 40.70           C  
ANISOU 3091  CB  ASP D  55     5647   5660   4158   -507   1282    398       C  
ATOM   3092  CG  ASP D  55       2.298  -7.241   3.526  1.00 47.61           C  
ANISOU 3092  CG  ASP D  55     6505   6641   4945   -286   1620    578       C  
ATOM   3093  OD1 ASP D  55       1.783  -6.834   2.469  1.00 49.61           O  
ANISOU 3093  OD1 ASP D  55     6536   6936   5378   -328   1676    564       O  
ATOM   3094  OD2 ASP D  55       1.773  -7.069   4.644  1.00 53.67           O1-
ANISOU 3094  OD2 ASP D  55     7489   7466   5437    -34   1841    749       O1-
ATOM   3095  N   ASP D  56       6.550  -6.556   1.847  1.00 40.37           N  
ANISOU 3095  N   ASP D  56     5688   5451   4200   -846    637   -171       N  
ATOM   3096  CA  ASP D  56       7.472  -5.427   1.818  1.00 43.87           C  
ANISOU 3096  CA  ASP D  56     6335   5806   4527   -910    432   -299       C  
ATOM   3097  C   ASP D  56       6.981  -4.425   0.771  1.00 38.22           C  
ANISOU 3097  C   ASP D  56     5499   5120   3903   -895    517   -352       C  
ATOM   3098  O   ASP D  56       6.725  -4.802  -0.373  1.00 37.98           O  
ANISOU 3098  O   ASP D  56     5112   5203   4114   -939    567   -343       O  
ATOM   3099  CB  ASP D  56       8.873  -5.948   1.493  1.00 39.97           C  
ANISOU 3099  CB  ASP D  56     5690   5346   4150  -1086    133   -322       C  
ATOM   3100  CG  ASP D  56       9.960  -4.910   1.650  1.00 54.53           C  
ANISOU 3100  CG  ASP D  56     7722   7100   5899  -1207   -152   -359       C  
ATOM   3101  OD1 ASP D  56       9.651  -3.722   1.850  1.00 53.87           O  
ANISOU 3101  OD1 ASP D  56     7906   6887   5673  -1169   -161   -409       O  
ATOM   3102  OD2 ASP D  56      11.144  -5.300   1.551  1.00 56.35           O1-
ANISOU 3102  OD2 ASP D  56     7825   7384   6200  -1340   -395   -308       O1-
ATOM   3103  N   LYS D  57       6.792  -3.168   1.168  1.00 36.21           N  
ANISOU 3103  N   LYS D  57     5578   4744   3436   -808    523   -410       N  
ATOM   3104  CA  LYS D  57       6.188  -2.159   0.302  1.00 38.75           C  
ANISOU 3104  CA  LYS D  57     5834   5078   3811   -764    630   -454       C  
ATOM   3105  C   LYS D  57       7.178  -1.029   0.065  1.00 38.56           C  
ANISOU 3105  C   LYS D  57     5976   4927   3749   -906    312   -537       C  
ATOM   3106  O   LYS D  57       7.775  -0.519   1.019  1.00 41.50           O  
ANISOU 3106  O   LYS D  57     6765   5108   3896   -918     80   -569       O  
ATOM   3107  CB  LYS D  57       4.895  -1.606   0.929  1.00 46.02           C  
ANISOU 3107  CB  LYS D  57     7019   5969   4496   -479    937   -411       C  
ATOM   3108  CG  LYS D  57       3.911  -2.688   1.355  1.00 36.18           C  
ANISOU 3108  CG  LYS D  57     5603   4865   3279   -346   1232   -227       C  
ATOM   3109  CD  LYS D  57       2.663  -2.131   2.084  1.00 38.68           C  
ANISOU 3109  CD  LYS D  57     6161   5215   3319      2   1572    -98       C  
ATOM   3110  CE  LYS D  57       1.853  -3.240   2.723  1.00 50.43           C  
ANISOU 3110  CE  LYS D  57     7478   6861   4823    117   1820    173       C  
ATOM   3111  NZ  LYS D  57       2.584  -4.019   3.775  1.00 53.33           N  
ANISOU 3111  NZ  LYS D  57     8028   7167   5067     86   1677    183       N  
ATOM   3112  N   ARG D  58       7.349  -0.633  -1.202  1.00 37.11           N  
ANISOU 3112  N   ARG D  58     5474   4838   3789  -1019    269   -546       N  
ATOM   3113  CA  ARG D  58       8.199   0.487  -1.575  1.00 39.97           C  
ANISOU 3113  CA  ARG D  58     5913   5107   4167  -1178    -34   -555       C  
ATOM   3114  C   ARG D  58       7.352   1.515  -2.313  1.00 33.44           C  
ANISOU 3114  C   ARG D  58     5083   4264   3358  -1095    116   -610       C  
ATOM   3115  O   ARG D  58       6.488   1.151  -3.116  1.00 33.88           O  
ANISOU 3115  O   ARG D  58     4831   4480   3562  -1005    403   -611       O  
ATOM   3116  CB  ARG D  58       9.365   0.031  -2.467  1.00 44.68           C  
ANISOU 3116  CB  ARG D  58     6078   5883   5016  -1378   -240   -450       C  
ATOM   3117  CG  ARG D  58      10.105  -1.164  -1.903  1.00 46.30           C  
ANISOU 3117  CG  ARG D  58     6215   6153   5225  -1419   -332   -389       C  
ATOM   3118  CD  ARG D  58      10.794  -0.841  -0.587  1.00 48.22           C  
ANISOU 3118  CD  ARG D  58     6887   6179   5255  -1506   -613   -372       C  
ATOM   3119  NE  ARG D  58      11.408  -2.036  -0.020  1.00 51.09           N  
ANISOU 3119  NE  ARG D  58     7182   6612   5618  -1529   -666   -317       N  
ATOM   3120  CZ  ARG D  58      12.623  -2.478  -0.324  1.00 56.29           C  
ANISOU 3120  CZ  ARG D  58     7572   7410   6407  -1671   -891   -174       C  
ATOM   3121  NH1 ARG D  58      13.397  -1.842  -1.192  1.00 48.89           N  
ANISOU 3121  NH1 ARG D  58     6370   6584   5624  -1809  -1085    -29       N  
ATOM   3122  NH2 ARG D  58      13.075  -3.585   0.261  1.00 50.59           N  
ANISOU 3122  NH2 ARG D  58     6830   6737   5656  -1657   -915   -141       N  
ATOM   3123  N   TYR D  59       7.589   2.793  -2.038  1.00 34.84           N  
ANISOU 3123  N   TYR D  59     5627   4226   3385  -1129   -112   -648       N  
ATOM   3124  CA  TYR D  59       6.752   3.851  -2.581  1.00 34.89           C  
ANISOU 3124  CA  TYR D  59     5722   4179   3356  -1016     19   -711       C  
ATOM   3125  C   TYR D  59       7.591   4.914  -3.272  1.00 38.48           C  
ANISOU 3125  C   TYR D  59     6138   4550   3934  -1252   -339   -665       C  
ATOM   3126  O   TYR D  59       8.732   5.190  -2.884  1.00 39.14           O  
ANISOU 3126  O   TYR D  59     6360   4499   4013  -1470   -760   -580       O  
ATOM   3127  CB  TYR D  59       5.942   4.568  -1.507  1.00 37.56           C  
ANISOU 3127  CB  TYR D  59     6671   4288   3311   -730    107   -803       C  
ATOM   3128  CG  TYR D  59       4.882   3.725  -0.860  1.00 37.68           C  
ANISOU 3128  CG  TYR D  59     6704   4426   3186   -441    522   -775       C  
ATOM   3129  CD1 TYR D  59       3.610   3.630  -1.413  1.00 38.44           C  
ANISOU 3129  CD1 TYR D  59     6555   4704   3348   -252    935   -730       C  
ATOM   3130  CD2 TYR D  59       5.131   3.076   0.339  1.00 39.53           C  
ANISOU 3130  CD2 TYR D  59     7203   4597   3221   -358    486   -754       C  
ATOM   3131  CE1 TYR D  59       2.610   2.871  -0.792  1.00 39.29           C  
ANISOU 3131  CE1 TYR D  59     6633   4947   3348     -2   1298   -612       C  
ATOM   3132  CE2 TYR D  59       4.150   2.311   0.952  1.00 46.00           C  
ANISOU 3132  CE2 TYR D  59     8004   5555   3920    -93    865   -663       C  
ATOM   3133  CZ  TYR D  59       2.893   2.216   0.374  1.00 44.29           C  
ANISOU 3133  CZ  TYR D  59     7499   5536   3794     75   1264   -569       C  
ATOM   3134  OH  TYR D  59       1.898   1.475   0.977  1.00 42.76           O  
ANISOU 3134  OH  TYR D  59     7233   5506   3510    319   1623   -389       O  
ATOM   3135  N   ASN D  60       6.976   5.568  -4.237  1.00 36.66           N  
ANISOU 3135  N   ASN D  60     5739   4383   3808  -1210   -190   -692       N  
ATOM   3136  CA  ASN D  60       7.569   6.778  -4.787  1.00 40.11           C  
ANISOU 3136  CA  ASN D  60     6220   4697   4322  -1404   -525   -635       C  
ATOM   3137  C   ASN D  60       7.654   7.832  -3.685  1.00 44.44           C  
ANISOU 3137  C   ASN D  60     7494   4841   4552  -1364   -853   -709       C  
ATOM   3138  O   ASN D  60       6.618   8.190  -3.108  1.00 46.34           O  
ANISOU 3138  O   ASN D  60     8157   4945   4505  -1051   -631   -854       O  
ATOM   3139  CB  ASN D  60       6.744   7.296  -5.958  1.00 34.80           C  
ANISOU 3139  CB  ASN D  60     5282   4154   3787  -1324   -270   -671       C  
ATOM   3140  CG  ASN D  60       7.439   8.433  -6.692  1.00 38.58           C  
ANISOU 3140  CG  ASN D  60     5690   4561   4408  -1558   -616   -561       C  
ATOM   3141  OD1 ASN D  60       8.110   9.267  -6.077  1.00 42.81           O  
ANISOU 3141  OD1 ASN D  60     6624   4809   4834  -1713  -1058   -510       O  
ATOM   3142  ND2 ASN D  60       7.290   8.464  -8.009  1.00 39.97           N  
ANISOU 3142  ND2 ASN D  60     5371   4984   4832  -1590   -451   -501       N  
ATOM   3143  N   PRO D  61       8.847   8.342  -3.360  1.00 46.05           N  
ANISOU 3143  N   PRO D  61     6172   6193   5133  -1796   -954   -596       N  
ATOM   3144  CA  PRO D  61       8.985   9.208  -2.174  1.00 43.59           C  
ANISOU 3144  CA  PRO D  61     6394   5618   4550  -2136   -880   -765       C  
ATOM   3145  C   PRO D  61       8.139  10.467  -2.208  1.00 51.51           C  
ANISOU 3145  C   PRO D  61     7867   6050   5657  -2132   -528   -838       C  
ATOM   3146  O   PRO D  61       7.597  10.871  -1.171  1.00 55.65           O  
ANISOU 3146  O   PRO D  61     8866   6233   6046  -2169   -308  -1004       O  
ATOM   3147  CB  PRO D  61      10.478   9.547  -2.185  1.00 53.46           C  
ANISOU 3147  CB  PRO D  61     7513   7222   5578  -2563  -1159   -742       C  
ATOM   3148  CG  PRO D  61      11.103   8.317  -2.768  1.00 55.72           C  
ANISOU 3148  CG  PRO D  61     7195   7977   5998  -2230  -1340   -558       C  
ATOM   3149  CD  PRO D  61      10.162   7.930  -3.885  1.00 44.27           C  
ANISOU 3149  CD  PRO D  61     5526   6470   4825  -1968  -1272   -515       C  
ATOM   3150  N   SER D  62       8.025  11.115  -3.363  1.00 44.93           N  
ANISOU 3150  N   SER D  62     6924   5098   5048  -2077   -450   -705       N  
ATOM   3151  CA  SER D  62       7.272  12.360  -3.435  1.00 55.33           C  
ANISOU 3151  CA  SER D  62     8696   5836   6492  -2028    -99   -719       C  
ATOM   3152  C   SER D  62       5.777  12.139  -3.262  1.00 54.70           C  
ANISOU 3152  C   SER D  62     8680   5486   6617  -1509    233   -677       C  
ATOM   3153  O   SER D  62       5.053  13.092  -2.962  1.00 54.26           O  
ANISOU 3153  O   SER D  62     9068   4914   6633  -1395    586   -719       O  
ATOM   3154  CB  SER D  62       7.525  13.057  -4.769  1.00 57.15           C  
ANISOU 3154  CB  SER D  62     8750   6050   6913  -2077   -116   -512       C  
ATOM   3155  OG  SER D  62       6.926  12.315  -5.817  1.00 57.50           O  
ANISOU 3155  OG  SER D  62     8272   6368   7207  -1666   -136   -296       O  
ATOM   3156  N   LEU D  63       5.305  10.910  -3.439  1.00 45.46           N  
ANISOU 3156  N   LEU D  63     7084   4648   5540  -1198    148   -592       N  
ATOM   3157  CA  LEU D  63       3.888  10.599  -3.369  1.00 45.68           C  
ANISOU 3157  CA  LEU D  63     7071   4536   5749   -746    433   -516       C  
ATOM   3158  C   LEU D  63       3.522   9.755  -2.162  1.00 48.79           C  
ANISOU 3158  C   LEU D  63     7578   4984   5974   -686    466   -659       C  
ATOM   3159  O   LEU D  63       2.350   9.403  -2.011  1.00 46.40           O  
ANISOU 3159  O   LEU D  63     7217   4624   5788   -348    697   -597       O  
ATOM   3160  CB  LEU D  63       3.446   9.858  -4.633  1.00 44.69           C  
ANISOU 3160  CB  LEU D  63     6370   4752   5860   -475    345   -285       C  
ATOM   3161  CG  LEU D  63       3.575  10.663  -5.918  1.00 50.29           C  
ANISOU 3161  CG  LEU D  63     6919   5452   6739   -477    346    -80       C  
ATOM   3162  CD1 LEU D  63       3.538   9.712  -7.092  1.00 41.79           C  
ANISOU 3162  CD1 LEU D  63     5251   4856   5770   -364    155     71       C  
ATOM   3163  CD2 LEU D  63       2.480  11.719  -6.008  1.00 58.31           C  
ANISOU 3163  CD2 LEU D  63     8180   6039   7935   -185    728     68       C  
ATOM   3164  N   LYS D  64       4.494   9.394  -1.323  1.00 46.75           N  
ANISOU 3164  N   LYS D  64     7440   4893   5430  -1014    229   -811       N  
ATOM   3165  CA  LYS D  64       4.248   8.391  -0.291  1.00 44.85           C  
ANISOU 3165  CA  LYS D  64     7219   4799   5024   -957    197   -875       C  
ATOM   3166  C   LYS D  64       3.119   8.796   0.654  1.00 52.32           C  
ANISOU 3166  C   LYS D  64     8569   5399   5912   -794    587   -986       C  
ATOM   3167  O   LYS D  64       2.374   7.929   1.123  1.00 45.85           O  
ANISOU 3167  O   LYS D  64     7650   4682   5089   -585    667   -947       O  
ATOM   3168  CB  LYS D  64       5.533   8.120   0.497  1.00 55.54           C  
ANISOU 3168  CB  LYS D  64     8649   6412   6040  -1356   -122   -973       C  
ATOM   3169  CG  LYS D  64       5.354   7.174   1.677  1.00 59.59           C  
ANISOU 3169  CG  LYS D  64     9236   7071   6334  -1332   -164  -1003       C  
ATOM   3170  CD  LYS D  64       6.657   6.521   2.104  1.00 68.69           C  
ANISOU 3170  CD  LYS D  64    10217   8649   7233  -1600   -562   -954       C  
ATOM   3171  CE  LYS D  64       6.456   5.620   3.322  1.00 66.36           C  
ANISOU 3171  CE  LYS D  64    10022   8489   6702  -1574   -598   -930       C  
ATOM   3172  NZ  LYS D  64       5.033   5.220   3.555  1.00 73.89           N  
ANISOU 3172  NZ  LYS D  64    11068   9204   7801  -1241   -278   -924       N  
ATOM   3173  N   SER D  65       2.951  10.095   0.920  1.00 50.64           N  
ANISOU 3173  N   SER D  65     8820   4762   5660   -875    862  -1120       N  
ATOM   3174  CA  SER D  65       1.917  10.504   1.869  1.00 52.45           C  
ANISOU 3174  CA  SER D  65     9457   4658   5814   -693   1282  -1255       C  
ATOM   3175  C   SER D  65       0.515  10.222   1.349  1.00 51.09           C  
ANISOU 3175  C   SER D  65     8994   4467   5950   -166   1562  -1049       C  
ATOM   3176  O   SER D  65      -0.438  10.243   2.132  1.00 50.81           O  
ANISOU 3176  O   SER D  65     9152   4294   5857     46   1895  -1113       O  
ATOM   3177  CB  SER D  65       2.043  11.988   2.225  1.00 51.13           C  
ANISOU 3177  CB  SER D  65     9908   3964   5556   -872   1570  -1466       C  
ATOM   3178  OG  SER D  65       2.001  12.827   1.084  1.00 54.69           O  
ANISOU 3178  OG  SER D  65    10301   4169   6309   -743   1657  -1308       O  
ATOM   3179  N   ARG D  66       0.367   9.950   0.051  1.00 44.27           N  
ANISOU 3179  N   ARG D  66     7646   3795   5379     24   1434   -798       N  
ATOM   3180  CA  ARG D  66      -0.949   9.763  -0.535  1.00 46.34           C  
ANISOU 3180  CA  ARG D  66     7586   4115   5906    470   1676   -570       C  
ATOM   3181  C   ARG D  66      -1.236   8.327  -0.907  1.00 42.12           C  
ANISOU 3181  C   ARG D  66     6539   4040   5425    534   1456   -435       C  
ATOM   3182  O   ARG D  66      -2.366   8.031  -1.306  1.00 46.42           O  
ANISOU 3182  O   ARG D  66     6784   4720   6134    832   1633   -251       O  
ATOM   3183  CB  ARG D  66      -1.122  10.616  -1.801  1.00 49.60           C  
ANISOU 3183  CB  ARG D  66     7831   4414   6600    652   1750   -344       C  
ATOM   3184  CG  ARG D  66      -0.371  11.931  -1.861  1.00 60.07           C  
ANISOU 3184  CG  ARG D  66     9602   5314   7907    452   1812   -437       C  
ATOM   3185  CD  ARG D  66      -0.564  12.480  -3.259  1.00 58.60           C  
ANISOU 3185  CD  ARG D  66     9120   5137   8007    643   1818   -123       C  
ATOM   3186  NE  ARG D  66      -1.984  12.559  -3.581  1.00 58.47           N  
ANISOU 3186  NE  ARG D  66     8865   5136   8216   1160   2138    140       N  
ATOM   3187  CZ  ARG D  66      -2.478  12.623  -4.809  1.00 55.80           C  
ANISOU 3187  CZ  ARG D  66     8071   5026   8104   1399   2114    494       C  
ATOM   3188  NH1 ARG D  66      -1.693  12.562  -5.875  1.00 49.68           N  
ANISOU 3188  NH1 ARG D  66     7030   4482   7363   1174   1795    609       N  
ATOM   3189  NH2 ARG D  66      -3.793  12.719  -4.972  1.00 45.10           N  
ANISOU 3189  NH2 ARG D  66     6482   3737   6916   1864   2414    753       N  
ATOM   3190  N   LEU D  67      -0.257   7.437  -0.784  1.00 37.04           N  
ANISOU 3190  N   LEU D  67     5794   3639   4643    260   1094   -512       N  
ATOM   3191  CA  LEU D  67      -0.328   6.115  -1.374  1.00 30.42           C  
ANISOU 3191  CA  LEU D  67     4503   3164   3891    296    874   -394       C  
ATOM   3192  C   LEU D  67      -0.338   5.041  -0.297  1.00 38.34           C  
ANISOU 3192  C   LEU D  67     5596   4268   4703    216    808   -467       C  
ATOM   3193  O   LEU D  67       0.386   5.140   0.701  1.00 35.19           O  
ANISOU 3193  O   LEU D  67     5513   3801   4055      8    721   -607       O  
ATOM   3194  CB  LEU D  67       0.869   5.866  -2.301  1.00 33.68           C  
ANISOU 3194  CB  LEU D  67     4672   3780   4345    111    521   -378       C  
ATOM   3195  CG  LEU D  67       1.048   6.785  -3.519  1.00 34.45           C  
ANISOU 3195  CG  LEU D  67     4621   3857   4612    132    519   -267       C  
ATOM   3196  CD1 LEU D  67       2.360   6.423  -4.253  1.00 35.61           C  
ANISOU 3196  CD1 LEU D  67     4533   4264   4733    -90    168   -282       C  
ATOM   3197  CD2 LEU D  67      -0.135   6.732  -4.470  1.00 42.83           C  
ANISOU 3197  CD2 LEU D  67     5342   5038   5893    408    685    -54       C  
ATOM   3198  N   THR D  68      -1.148   4.006  -0.526  1.00 36.20           N  
ANISOU 3198  N   THR D  68     5042   4183   4530    344    840   -352       N  
ATOM   3199  CA  THR D  68      -1.108   2.773   0.253  1.00 34.54           C  
ANISOU 3199  CA  THR D  68     4858   4081   4186    261    737   -360       C  
ATOM   3200  C   THR D  68      -1.256   1.604  -0.713  1.00 33.67           C  
ANISOU 3200  C   THR D  68     4360   4182   4250    285    589   -255       C  
ATOM   3201  O   THR D  68      -2.293   1.479  -1.372  1.00 35.29           O  
ANISOU 3201  O   THR D  68     4314   4494   4600    395    742   -154       O  
ATOM   3202  CB  THR D  68      -2.235   2.729   1.275  1.00 37.86           C  
ANISOU 3202  CB  THR D  68     5458   4437   4492    352   1044   -352       C  
ATOM   3203  OG1 THR D  68      -2.151   3.878   2.143  1.00 39.28           O  
ANISOU 3203  OG1 THR D  68     6047   4384   4495    334   1241   -498       O  
ATOM   3204  CG2 THR D  68      -2.121   1.460   2.103  1.00 37.81           C  
ANISOU 3204  CG2 THR D  68     5507   4528   4329    232    923   -323       C  
ATOM   3205  N   ILE D  69      -0.246   0.759  -0.798  1.00 31.13           N  
ANISOU 3205  N   ILE D  69     3988   3938   3903    180    313   -276       N  
ATOM   3206  CA  ILE D  69      -0.338  -0.466  -1.591  1.00 31.77           C  
ANISOU 3206  CA  ILE D  69     3798   4147   4128    190    211   -226       C  
ATOM   3207  C   ILE D  69      -0.555  -1.634  -0.636  1.00 34.52           C  
ANISOU 3207  C   ILE D  69     4299   4437   4381    154    215   -180       C  
ATOM   3208  O   ILE D  69      -0.070  -1.627   0.499  1.00 35.54           O  
ANISOU 3208  O   ILE D  69     4687   4499   4316    109    159   -176       O  
ATOM   3209  CB  ILE D  69       0.911  -0.664  -2.485  1.00 32.82           C  
ANISOU 3209  CB  ILE D  69     3751   4384   4334    158    -48   -269       C  
ATOM   3210  CG1 ILE D  69       0.680  -1.712  -3.579  1.00 32.01           C  
ANISOU 3210  CG1 ILE D  69     3376   4393   4393    171    -78   -272       C  
ATOM   3211  CG2 ILE D  69       2.180  -0.966  -1.683  1.00 34.38           C  
ANISOU 3211  CG2 ILE D  69     4104   4576   4382    108   -267   -279       C  
ATOM   3212  CD1 ILE D  69       1.760  -1.631  -4.693  1.00 30.41           C  
ANISOU 3212  CD1 ILE D  69     2948   4342   4264    166   -260   -331       C  
ATOM   3213  N   SER D  70      -1.316  -2.630  -1.085  1.00 31.89           N  
ANISOU 3213  N   SER D  70     3817   4143   4158    137    284   -131       N  
ATOM   3214  CA  SER D  70      -1.575  -3.812  -0.269  1.00 32.87           C  
ANISOU 3214  CA  SER D  70     4103   4172   4214     78    303    -58       C  
ATOM   3215  C   SER D  70      -1.934  -4.986  -1.178  1.00 31.39           C  
ANISOU 3215  C   SER D  70     3749   3989   4188      4    301    -61       C  
ATOM   3216  O   SER D  70      -2.069  -4.840  -2.395  1.00 33.47           O  
ANISOU 3216  O   SER D  70     3756   4382   4578    -16    293   -129       O  
ATOM   3217  CB  SER D  70      -2.681  -3.517   0.753  1.00 36.41           C  
ANISOU 3217  CB  SER D  70     4699   4620   4516     53    548      7       C  
ATOM   3218  OG  SER D  70      -3.908  -3.291   0.086  1.00 37.48           O  
ANISOU 3218  OG  SER D  70     4589   4900   4752     56    752     40       O  
ATOM   3219  N   LYS D  71      -2.094  -6.168  -0.570  1.00 29.33           N  
ANISOU 3219  N   LYS D  71     3665   3577   3901    -67    317     14       N  
ATOM   3220  CA  LYS D  71      -2.399  -7.370  -1.328  1.00 32.72           C  
ANISOU 3220  CA  LYS D  71     4039   3927   4468   -187    341    -18       C  
ATOM   3221  C   LYS D  71      -3.346  -8.266  -0.547  1.00 40.44           C  
ANISOU 3221  C   LYS D  71     5195   4794   5376   -358    492    103       C  
ATOM   3222  O   LYS D  71      -3.413  -8.197   0.681  1.00 40.97           O  
ANISOU 3222  O   LYS D  71     5470   4809   5289   -335    525    231       O  
ATOM   3223  CB  LYS D  71      -1.114  -8.143  -1.677  1.00 38.24           C  
ANISOU 3223  CB  LYS D  71     4811   4444   5272    -65    166    -66       C  
ATOM   3224  CG  LYS D  71      -0.316  -8.638  -0.465  1.00 37.97           C  
ANISOU 3224  CG  LYS D  71     5049   4228   5152     64     61     96       C  
ATOM   3225  CD  LYS D  71       0.890  -9.450  -0.901  1.00 40.33           C  
ANISOU 3225  CD  LYS D  71     5363   4372   5588    253    -75     90       C  
ATOM   3226  CE  LYS D  71       1.770  -9.892   0.273  1.00 43.01           C  
ANISOU 3226  CE  LYS D  71     5903   4607   5834    427   -210    325       C  
ATOM   3227  NZ  LYS D  71       1.079 -10.627   1.393  1.00 43.35           N  
ANISOU 3227  NZ  LYS D  71     6236   4457   5777    327   -113    529       N  
ATOM   3228  N   ASP D  72      -4.107  -9.075  -1.286  1.00 33.85           N  
ANISOU 3228  N   ASP D  72     4277   3961   4624   -580    587     57       N  
ATOM   3229  CA  ASP D  72      -4.813 -10.254  -0.773  1.00 39.15           C  
ANISOU 3229  CA  ASP D  72     5154   4455   5265   -816    706    154       C  
ATOM   3230  C   ASP D  72      -4.335 -11.471  -1.562  1.00 37.34           C  
ANISOU 3230  C   ASP D  72     5062   3933   5194   -906    667     34       C  
ATOM   3231  O   ASP D  72      -4.881 -11.800  -2.618  1.00 42.63           O  
ANISOU 3231  O   ASP D  72     5584   4698   5914  -1149    730   -113       O  
ATOM   3232  CB  ASP D  72      -6.332 -10.101  -0.845  1.00 42.41           C  
ANISOU 3232  CB  ASP D  72     5361   5165   5590  -1085    902    211       C  
ATOM   3233  CG  ASP D  72      -7.057 -11.226  -0.121  1.00 49.34           C  
ANISOU 3233  CG  ASP D  72     6469   5884   6394  -1372   1030    346       C  
ATOM   3234  OD1 ASP D  72      -6.366 -12.171   0.318  1.00 51.94           O  
ANISOU 3234  OD1 ASP D  72     7145   5816   6772  -1347    968    391       O  
ATOM   3235  OD2 ASP D  72      -8.293 -11.151   0.059  1.00 55.06           O1-
ANISOU 3235  OD2 ASP D  72     7025   6888   7008  -1604   1200    441       O1-
ATOM   3236  N   THR D  73      -3.308 -12.138  -1.033  1.00 42.66           N  
ANISOU 3236  N   THR D  73     6020   4260   5927   -706    576    106       N  
ATOM   3237  CA  THR D  73      -2.712 -13.273  -1.732  1.00 45.84           C  
ANISOU 3237  CA  THR D  73     6601   4311   6508   -690    579    -10       C  
ATOM   3238  C   THR D  73      -3.710 -14.408  -1.942  1.00 42.72           C  
ANISOU 3238  C   THR D  73     6405   3693   6133  -1089    764    -47       C  
ATOM   3239  O   THR D  73      -3.690 -15.071  -2.985  1.00 46.47           O  
ANISOU 3239  O   THR D  73     6926   4015   6714  -1243    830   -272       O  
ATOM   3240  CB  THR D  73      -1.490 -13.761  -0.958  1.00 49.78           C  
ANISOU 3240  CB  THR D  73     7347   4504   7063   -340    466    164       C  
ATOM   3241  OG1 THR D  73      -0.576 -12.664  -0.803  1.00 47.82           O  
ANISOU 3241  OG1 THR D  73     6884   4532   6754    -59    280    185       O  
ATOM   3242  CG2 THR D  73      -0.805 -14.913  -1.679  1.00 52.76           C  
ANISOU 3242  CG2 THR D  73     7920   4472   7655   -224    517     52       C  
ATOM   3243  N   SER D  74      -4.590 -14.656  -0.963  1.00 43.27           N  
ANISOU 3243  N   SER D  74     6611   3752   6078  -1302    862    159       N  
ATOM   3244  CA  SER D  74      -5.565 -15.731  -1.104  1.00 50.52           C  
ANISOU 3244  CA  SER D  74     7726   4479   6992  -1756   1036    146       C  
ATOM   3245  C   SER D  74      -6.552 -15.489  -2.242  1.00 46.42           C  
ANISOU 3245  C   SER D  74     6882   4340   6416  -2150   1110    -66       C  
ATOM   3246  O   SER D  74      -7.156 -16.450  -2.738  1.00 50.89           O  
ANISOU 3246  O   SER D  74     7605   4744   6986  -2584   1232   -177       O  
ATOM   3247  CB  SER D  74      -6.308 -15.928   0.222  1.00 51.67           C  
ANISOU 3247  CB  SER D  74     8027   4627   6977  -1914   1124    443       C  
ATOM   3248  OG  SER D  74      -7.242 -14.877   0.418  1.00 54.44           O  
ANISOU 3248  OG  SER D  74     8007   5524   7151  -2014   1170    486       O  
ATOM   3249  N   ARG D  75      -6.739 -14.241  -2.660  1.00 43.59           N  
ANISOU 3249  N   ARG D  75     6086   4485   5991  -2033   1041   -106       N  
ATOM   3250  CA  ARG D  75      -7.669 -13.889  -3.726  1.00 49.61           C  
ANISOU 3250  CA  ARG D  75     6462   5711   6676  -2359   1084   -231       C  
ATOM   3251  C   ARG D  75      -6.967 -13.409  -4.987  1.00 50.51           C  
ANISOU 3251  C   ARG D  75     6358   5966   6866  -2212    970   -462       C  
ATOM   3252  O   ARG D  75      -7.638 -12.943  -5.913  1.00 49.55           O  
ANISOU 3252  O   ARG D  75     5862   6306   6660  -2431    971   -528       O  
ATOM   3253  CB  ARG D  75      -8.649 -12.817  -3.247  1.00 50.99           C  
ANISOU 3253  CB  ARG D  75     6264   6404   6705  -2344   1138    -28       C  
ATOM   3254  CG  ARG D  75      -9.609 -13.348  -2.219  1.00 49.29           C  
ANISOU 3254  CG  ARG D  75     6176   6188   6364  -2614   1292    180       C  
ATOM   3255  CD  ARG D  75     -11.026 -12.911  -2.492  1.00 71.37           C  
ANISOU 3255  CD  ARG D  75     8517   9593   9008  -2911   1412    289       C  
ATOM   3256  NE  ARG D  75     -11.648 -12.426  -1.268  1.00 77.72           N  
ANISOU 3256  NE  ARG D  75     9268  10575   9686  -2792   1547    537       N  
ATOM   3257  CZ  ARG D  75     -12.139 -13.226  -0.333  1.00 72.92           C  
ANISOU 3257  CZ  ARG D  75     8905   9824   8977  -3051   1667    687       C  
ATOM   3258  NH1 ARG D  75     -12.115 -14.542  -0.467  1.00 81.39           N  
ANISOU 3258  NH1 ARG D  75    10314  10530  10079  -3450   1672    633       N  
ATOM   3259  NH2 ARG D  75     -12.656 -12.696   0.769  1.00 89.95           N  
ANISOU 3259  NH2 ARG D  75    10999  12186  10992  -2913   1807    894       N  
ATOM   3260  N   ASN D  76      -5.641 -13.508  -5.043  1.00 43.39           N  
ANISOU 3260  N   ASN D  76     6607   3547   6333  -1303   -543    428       N  
ATOM   3261  CA  ASN D  76      -4.882 -13.106  -6.225  1.00 43.44           C  
ANISOU 3261  CA  ASN D  76     6393   3747   6366  -1212   -667    -35       C  
ATOM   3262  C   ASN D  76      -5.184 -11.650  -6.586  1.00 43.18           C  
ANISOU 3262  C   ASN D  76     6102   4218   6086  -1223   -513    -56       C  
ATOM   3263  O   ASN D  76      -5.478 -11.324  -7.739  1.00 45.25           O  
ANISOU 3263  O   ASN D  76     6090   4728   6374  -1377   -502   -260       O  
ATOM   3264  CB  ASN D  76      -5.174 -14.047  -7.407  1.00 42.87           C  
ANISOU 3264  CB  ASN D  76     6180   3511   6598  -1452   -756   -327       C  
ATOM   3265  CG  ASN D  76      -4.391 -15.370  -7.340  1.00 47.00           C  
ANISOU 3265  CG  ASN D  76     6924   3502   7430  -1329   -982   -498       C  
ATOM   3266  OD1 ASN D  76      -3.494 -15.545  -6.519  1.00 51.53           O  
ANISOU 3266  OD1 ASN D  76     7734   3868   7976  -1023  -1108   -415       O  
ATOM   3267  ND2 ASN D  76      -4.751 -16.307  -8.208  1.00 57.38           N  
ANISOU 3267  ND2 ASN D  76     8149   4597   9057  -1562  -1043   -751       N  
ATOM   3268  N   LYS D  77      -5.117 -10.763  -5.583  1.00 36.00           N  
ANISOU 3268  N   LYS D  77     5281   3462   4936  -1058   -398    161       N  
ATOM   3269  CA  LYS D  77      -5.350  -9.337  -5.797  1.00 34.19           C  
ANISOU 3269  CA  LYS D  77     4842   3624   4524  -1029   -256    151       C  
ATOM   3270  C   LYS D  77      -4.252  -8.498  -5.161  1.00 34.70           C  
ANISOU 3270  C   LYS D  77     5005   3787   4393   -738   -293     54       C  
ATOM   3271  O   LYS D  77      -3.716  -8.842  -4.105  1.00 37.79           O  
ANISOU 3271  O   LYS D  77     5634   4030   4696   -565   -348    147       O  
ATOM   3272  CB  LYS D  77      -6.694  -8.896  -5.213  1.00 40.01           C  
ANISOU 3272  CB  LYS D  77     5509   4504   5188  -1169    -11    483       C  
ATOM   3273  CG  LYS D  77      -7.894  -9.429  -5.951  1.00 47.69           C  
ANISOU 3273  CG  LYS D  77     6289   5506   6327  -1485     54    554       C  
ATOM   3274  CD  LYS D  77      -9.185  -8.890  -5.329  1.00 52.20           C  
ANISOU 3274  CD  LYS D  77     6742   6282   6810  -1591    306    853       C  
ATOM   3275  CE  LYS D  77     -10.389  -9.502  -6.009  1.00 51.28           C  
ANISOU 3275  CE  LYS D  77     6408   6219   6855  -1927    364    917       C  
ATOM   3276  NZ  LYS D  77     -10.070  -9.660  -7.449  1.00 71.45           N  
ANISOU 3276  NZ  LYS D  77     8778   8841   9528  -2010    191    615       N  
ATOM   3277  N   VAL D  78      -3.919  -7.388  -5.834  1.00 32.33           N  
ANISOU 3277  N   VAL D  78     4510   3751   4022   -703   -270   -124       N  
ATOM   3278  CA  VAL D  78      -3.089  -6.313  -5.295  1.00 34.27           C  
ANISOU 3278  CA  VAL D  78     4790   4136   4095   -494   -249   -219       C  
ATOM   3279  C   VAL D  78      -3.902  -5.031  -5.392  1.00 33.49           C  
ANISOU 3279  C   VAL D  78     4519   4251   3954   -550    -47    -91       C  
ATOM   3280  O   VAL D  78      -4.662  -4.842  -6.346  1.00 36.02           O  
ANISOU 3280  O   VAL D  78     4631   4687   4370   -720     -3    -37       O  
ATOM   3281  CB  VAL D  78      -1.749  -6.186  -6.067  1.00 37.93           C  
ANISOU 3281  CB  VAL D  78     5182   4673   4557   -407   -427   -584       C  
ATOM   3282  CG1 VAL D  78      -1.076  -4.851  -5.804  1.00 44.94           C  
ANISOU 3282  CG1 VAL D  78     6025   5750   5300   -290   -368   -692       C  
ATOM   3283  CG2 VAL D  78      -0.823  -7.324  -5.685  1.00 43.83           C  
ANISOU 3283  CG2 VAL D  78     6108   5197   5347   -247   -633   -727       C  
ATOM   3284  N   PHE D  79      -3.763  -4.148  -4.397  1.00 33.99           N  
ANISOU 3284  N   PHE D  79     4656   4375   3881   -397     67    -53       N  
ATOM   3285  CA  PHE D  79      -4.607  -2.968  -4.322  1.00 33.48           C  
ANISOU 3285  CA  PHE D  79     4443   4449   3827   -409    268     63       C  
ATOM   3286  C   PHE D  79      -3.756  -1.713  -4.240  1.00 32.43           C  
ANISOU 3286  C   PHE D  79     4290   4384   3648   -276    282   -133       C  
ATOM   3287  O   PHE D  79      -2.643  -1.744  -3.720  1.00 36.33           O  
ANISOU 3287  O   PHE D  79     4918   4858   4027   -152    187   -327       O  
ATOM   3288  CB  PHE D  79      -5.506  -3.002  -3.085  1.00 30.11           C  
ANISOU 3288  CB  PHE D  79     4095   4040   3308   -376    455    274       C  
ATOM   3289  CG  PHE D  79      -6.330  -4.252  -2.961  1.00 34.83           C  
ANISOU 3289  CG  PHE D  79     4741   4552   3941   -542    466    498       C  
ATOM   3290  CD1 PHE D  79      -7.515  -4.394  -3.665  1.00 36.29           C  
ANISOU 3290  CD1 PHE D  79     4717   4804   4266   -737    550    642       C  
ATOM   3291  CD2 PHE D  79      -5.925  -5.281  -2.122  1.00 39.90           C  
ANISOU 3291  CD2 PHE D  79     5634   5046   4481   -511    387    579       C  
ATOM   3292  CE1 PHE D  79      -8.277  -5.543  -3.546  1.00 35.81           C  
ANISOU 3292  CE1 PHE D  79     4692   4657   4258   -936    572    828       C  
ATOM   3293  CE2 PHE D  79      -6.682  -6.432  -1.996  1.00 44.35           C  
ANISOU 3293  CE2 PHE D  79     6263   5477   5112   -698    404    813       C  
ATOM   3294  CZ  PHE D  79      -7.862  -6.566  -2.706  1.00 41.25           C  
ANISOU 3294  CZ  PHE D  79     5656   5144   4873   -929    507    921       C  
ATOM   3295  N   LEU D  80      -4.312  -0.599  -4.711  1.00 31.88           N  
ANISOU 3295  N   LEU D  80     4046   4385   3682   -301    399    -72       N  
ATOM   3296  CA  LEU D  80      -3.722   0.717  -4.491  1.00 26.07           C  
ANISOU 3296  CA  LEU D  80     3299   3650   2958   -195    460   -220       C  
ATOM   3297  C   LEU D  80      -4.800   1.701  -4.054  1.00 36.92           C  
ANISOU 3297  C   LEU D  80     4571   5021   4436   -125    672    -86       C  
ATOM   3298  O   LEU D  80      -5.884   1.750  -4.648  1.00 36.19           O  
ANISOU 3298  O   LEU D  80     4307   4972   4471   -194    728    129       O  
ATOM   3299  CB  LEU D  80      -3.018   1.228  -5.759  1.00 29.75           C  
ANISOU 3299  CB  LEU D  80     3645   4156   3503   -297    350   -313       C  
ATOM   3300  CG  LEU D  80      -2.270   2.552  -5.574  1.00 32.28           C  
ANISOU 3300  CG  LEU D  80     3971   4429   3863   -238    402   -473       C  
ATOM   3301  CD1 LEU D  80      -1.086   2.413  -4.625  1.00 36.98           C  
ANISOU 3301  CD1 LEU D  80     4727   5025   4297   -130    346   -768       C  
ATOM   3302  CD2 LEU D  80      -1.800   3.078  -6.937  1.00 32.58           C  
ANISOU 3302  CD2 LEU D  80     3868   4532   3978   -398    322   -460       C  
ATOM   3303  N   LYS D  81      -4.491   2.479  -3.012  1.00 32.92           N  
ANISOU 3303  N   LYS D  81     4146   4485   3877     21    783   -248       N  
ATOM   3304  CA  LYS D  81      -5.307   3.587  -2.539  1.00 36.44           C  
ANISOU 3304  CA  LYS D  81     4489   4902   4456    131    987   -232       C  
ATOM   3305  C   LYS D  81      -4.536   4.887  -2.759  1.00 36.02           C  
ANISOU 3305  C   LYS D  81     4424   4710   4553    178    990   -428       C  
ATOM   3306  O   LYS D  81      -3.363   4.987  -2.373  1.00 37.53           O  
ANISOU 3306  O   LYS D  81     4741   4895   4625    188    920   -685       O  
ATOM   3307  CB  LYS D  81      -5.625   3.389  -1.049  1.00 36.19           C  
ANISOU 3307  CB  LYS D  81     4552   4972   4226    241   1137   -310       C  
ATOM   3308  CG  LYS D  81      -6.136   4.605  -0.311  1.00 51.04           C  
ANISOU 3308  CG  LYS D  81     6344   6842   6208    393   1354   -456       C  
ATOM   3309  CD  LYS D  81      -6.572   4.247   1.125  1.00 61.68           C  
ANISOU 3309  CD  LYS D  81     7751   8400   7284    463   1517   -517       C  
ATOM   3310  CE  LYS D  81      -6.868   2.750   1.286  1.00 59.82           C  
ANISOU 3310  CE  LYS D  81     7610   8293   6825    334   1452   -254       C  
ATOM   3311  NZ  LYS D  81      -7.079   2.368   2.719  1.00 79.54           N  
ANISOU 3311  NZ  LYS D  81    10204  11028   8991    372   1588   -275       N  
ATOM   3312  N   ILE D  82      -5.161   5.860  -3.418  1.00 34.29           N  
ANISOU 3312  N   ILE D  82     4048   4375   4606    197   1056   -295       N  
ATOM   3313  CA  ILE D  82      -4.573   7.192  -3.555  1.00 34.83           C  
ANISOU 3313  CA  ILE D  82     4117   4238   4881    232   1088   -442       C  
ATOM   3314  C   ILE D  82      -5.532   8.204  -2.942  1.00 33.64           C  
ANISOU 3314  C   ILE D  82     3868   3947   4966    421   1289   -464       C  
ATOM   3315  O   ILE D  82      -6.681   8.340  -3.392  1.00 37.43           O  
ANISOU 3315  O   ILE D  82     4176   4427   5621    480   1337   -203       O  
ATOM   3316  CB  ILE D  82      -4.257   7.570  -5.012  1.00 36.81           C  
ANISOU 3316  CB  ILE D  82     4282   4420   5282     80    956   -246       C  
ATOM   3317  CG1 ILE D  82      -3.529   6.440  -5.740  1.00 35.26           C  
ANISOU 3317  CG1 ILE D  82     4120   4425   4854   -101    770   -237       C  
ATOM   3318  CG2 ILE D  82      -3.450   8.872  -5.028  1.00 40.69           C  
ANISOU 3318  CG2 ILE D  82     4819   4668   5972     67    990   -411       C  
ATOM   3319  CD1 ILE D  82      -2.996   6.881  -7.125  1.00 34.66           C  
ANISOU 3319  CD1 ILE D  82     3955   4363   4853   -286    654   -106       C  
ATOM   3320  N   THR D  82A     -5.071   8.911  -1.909  1.00 41.71           N  
ANISOU 3320  N   THR D  82A    6761   5442   3644   1102   1119   -430       N  
ATOM   3321  CA  THR D  82A     -5.957   9.788  -1.155  1.00 40.90           C  
ANISOU 3321  CA  THR D  82A    6787   5374   3378   1409   1226   -484       C  
ATOM   3322  C   THR D  82A     -6.169  11.123  -1.866  1.00 41.55           C  
ANISOU 3322  C   THR D  82A    6874   5246   3667   1314   1128   -638       C  
ATOM   3323  O   THR D  82A     -5.339  11.561  -2.669  1.00 45.22           O  
ANISOU 3323  O   THR D  82A    7293   5535   4355   1067    936   -762       O  
ATOM   3324  CB  THR D  82A     -5.412  10.039   0.255  1.00 48.90           C  
ANISOU 3324  CB  THR D  82A    8048   6509   4024   1758   1123   -714       C  
ATOM   3325  OG1 THR D  82A     -4.189  10.782   0.177  1.00 60.74           O  
ANISOU 3325  OG1 THR D  82A    9634   7838   5606   1647    774  -1072       O  
ATOM   3326  CG2 THR D  82A     -5.166   8.719   0.993  1.00 53.25           C  
ANISOU 3326  CG2 THR D  82A    8601   7285   4347   1894   1243   -522       C  
ATOM   3327  N   SER D  82B     -7.315  11.751  -1.566  1.00 43.81           N  
ANISOU 3327  N   SER D  82B    7198   5553   3896   1533   1293   -586       N  
ATOM   3328  CA  SER D  82B     -7.692  13.099  -2.003  1.00 43.39           C  
ANISOU 3328  CA  SER D  82B    7176   5310   4000   1533   1236   -722       C  
ATOM   3329  C   SER D  82B     -7.232  13.431  -3.422  1.00 42.34           C  
ANISOU 3329  C   SER D  82B    6896   4977   4216   1178   1116   -704       C  
ATOM   3330  O   SER D  82B     -6.320  14.238  -3.603  1.00 44.63           O  
ANISOU 3330  O   SER D  82B    7233   5070   4654   1085    904   -918       O  
ATOM   3331  CB  SER D  82B     -7.133  14.134  -1.034  1.00 43.77           C  
ANISOU 3331  CB  SER D  82B    7461   5275   3894   1779   1028  -1098       C  
ATOM   3332  OG  SER D  82B     -7.757  15.397  -1.237  1.00 51.14           O  
ANISOU 3332  OG  SER D  82B    8433   6036   4962   1863   1026  -1201       O  
ATOM   3333  N   VAL D  82C     -7.884  12.848  -4.426  1.00 36.62           N  
ANISOU 3333  N   VAL D  82C    5980   4291   3642   1015   1247   -443       N  
ATOM   3334  CA  VAL D  82C     -7.449  13.043  -5.819  1.00 35.40           C  
ANISOU 3334  CA  VAL D  82C    5700   4007   3743    750   1155   -392       C  
ATOM   3335  C   VAL D  82C     -7.768  14.462  -6.289  1.00 39.01           C  
ANISOU 3335  C   VAL D  82C    6178   4274   4371    779   1140   -450       C  
ATOM   3336  O   VAL D  82C     -8.621  15.170  -5.736  1.00 40.10           O  
ANISOU 3336  O   VAL D  82C    6390   4392   4454    982   1224   -492       O  
ATOM   3337  CB  VAL D  82C     -8.118  11.998  -6.723  1.00 36.15           C  
ANISOU 3337  CB  VAL D  82C    5603   4214   3919    635   1252   -149       C  
ATOM   3338  CG1 VAL D  82C     -7.660  10.589  -6.338  1.00 39.26           C  
ANISOU 3338  CG1 VAL D  82C    5956   4740   4220    579   1249    -92       C  
ATOM   3339  CG2 VAL D  82C     -9.634  12.123  -6.635  1.00 40.51           C  
ANISOU 3339  CG2 VAL D  82C    6076   4816   4498    785   1430     -3       C  
ATOM   3340  N   ASP D  83      -7.053  14.886  -7.327  1.00 41.21           N  
ANISOU 3340  N   ASP D  83     6383   4407   4866    597   1050   -426       N  
ATOM   3341  CA  ASP D  83      -7.332  16.129  -8.023  1.00 35.95           C  
ANISOU 3341  CA  ASP D  83     5690   3552   4418    605   1067   -392       C  
ATOM   3342  C   ASP D  83      -7.152  15.830  -9.512  1.00 37.78           C  
ANISOU 3342  C   ASP D  83     5773   3814   4768    458   1098   -169       C  
ATOM   3343  O   ASP D  83      -6.821  14.707  -9.891  1.00 38.73           O  
ANISOU 3343  O   ASP D  83     5831   4086   4799    363   1080    -96       O  
ATOM   3344  CB  ASP D  83      -6.415  17.257  -7.529  1.00 40.42           C  
ANISOU 3344  CB  ASP D  83     6338   3846   5175    609    910   -619       C  
ATOM   3345  CG  ASP D  83      -4.935  16.946  -7.753  1.00 46.59           C  
ANISOU 3345  CG  ASP D  83     7060   4545   6098    419    764   -660       C  
ATOM   3346  OD1 ASP D  83      -4.631  16.170  -8.673  1.00 57.51           O1-
ANISOU 3346  OD1 ASP D  83     8332   6045   7474    283    821   -460       O1-
ATOM   3347  OD2 ASP D  83      -4.078  17.478  -7.016  1.00 65.87           O  
ANISOU 3347  OD2 ASP D  83     9558   6801   8670    425    575   -905       O  
ATOM   3348  N   THR D  84      -7.373  16.831 -10.364  1.00 45.72           N  
ANISOU 3348  N   THR D  84     6728   4680   5962    477   1146    -58       N  
ATOM   3349  CA  THR D  84      -7.395  16.553 -11.803  1.00 48.46           C  
ANISOU 3349  CA  THR D  84     6958   5117   6338    438   1197    174       C  
ATOM   3350  C   THR D  84      -6.079  15.975 -12.310  1.00 49.70           C  
ANISOU 3350  C   THR D  84     7068   5294   6524    304   1138    222       C  
ATOM   3351  O   THR D  84      -6.073  15.230 -13.300  1.00 46.05           O  
ANISOU 3351  O   THR D  84     6538   5001   5958    308   1152    361       O  
ATOM   3352  CB  THR D  84      -7.752  17.820 -12.569  1.00 49.47           C  
ANISOU 3352  CB  THR D  84     7049   5088   6658    524   1281    318       C  
ATOM   3353  OG1 THR D  84      -6.923  18.891 -12.112  1.00 47.01           O  
ANISOU 3353  OG1 THR D  84     6764   4479   6620    479   1241    230       O  
ATOM   3354  CG2 THR D  84      -9.221  18.173 -12.318  1.00 59.79           C  
ANISOU 3354  CG2 THR D  84     8376   6440   7903    676   1353    315       C  
ATOM   3355  N   ALA D  85      -4.959  16.267 -11.640  1.00 47.12           N  
ANISOU 3355  N   ALA D  85     6768   4799   6336    208   1051     92       N  
ATOM   3356  CA  ALA D  85      -3.678  15.696 -12.066  1.00 45.69           C  
ANISOU 3356  CA  ALA D  85     6518   4634   6206     84   1007    153       C  
ATOM   3357  C   ALA D  85      -3.606  14.177 -11.909  1.00 50.41           C  
ANISOU 3357  C   ALA D  85     7133   5482   6539     41    960    109       C  
ATOM   3358  O   ALA D  85      -2.672  13.555 -12.436  1.00 46.02           O  
ANISOU 3358  O   ALA D  85     6517   4985   5982    -34    940    183       O  
ATOM   3359  CB  ALA D  85      -2.530  16.353 -11.293  1.00 45.27           C  
ANISOU 3359  CB  ALA D  85     6460   4319   6424    -10    883     -6       C  
ATOM   3360  N   ASP D  86      -4.562  13.559 -11.216  1.00 35.05           N  
ANISOU 3360  N   ASP D  86     5245   3671   4402    100    959     18       N  
ATOM   3361  CA  ASP D  86      -4.607  12.120 -11.055  1.00 36.62           C  
ANISOU 3361  CA  ASP D  86     5426   4064   4422     65    929      7       C  
ATOM   3362  C   ASP D  86      -5.377  11.430 -12.177  1.00 34.13           C  
ANISOU 3362  C   ASP D  86     5018   3899   4052    107    952    140       C  
ATOM   3363  O   ASP D  86      -5.455  10.194 -12.185  1.00 37.76           O  
ANISOU 3363  O   ASP D  86     5432   4483   4432     76    904    128       O  
ATOM   3364  CB  ASP D  86      -5.232  11.784  -9.677  1.00 36.07           C  
ANISOU 3364  CB  ASP D  86     5435   4046   4224    137    944   -109       C  
ATOM   3365  CG  ASP D  86      -4.406  12.337  -8.504  1.00 45.50           C  
ANISOU 3365  CG  ASP D  86     6750   5128   5409    156    857   -306       C  
ATOM   3366  OD1 ASP D  86      -3.180  12.092  -8.488  1.00 41.12           O  
ANISOU 3366  OD1 ASP D  86     6186   4534   4903     49    750   -365       O  
ATOM   3367  OD2 ASP D  86      -4.961  13.047  -7.620  1.00 43.63           O1-
ANISOU 3367  OD2 ASP D  86     6614   4840   5125    302    875   -421       O1-
ATOM   3368  N   THR D  87      -5.988  12.196 -13.086  1.00 32.01           N  
ANISOU 3368  N   THR D  87     4715   3610   3837    200   1003    249       N  
ATOM   3369  CA  THR D  87      -6.582  11.626 -14.291  1.00 36.84           C  
ANISOU 3369  CA  THR D  87     5246   4371   4382    289    968    338       C  
ATOM   3370  C   THR D  87      -5.502  10.926 -15.110  1.00 34.63           C  
ANISOU 3370  C   THR D  87     4950   4181   4025    270    911    377       C  
ATOM   3371  O   THR D  87      -4.538  11.561 -15.536  1.00 38.37           O  
ANISOU 3371  O   THR D  87     5438   4593   4549    270    976    480       O  
ATOM   3372  CB  THR D  87      -7.257  12.720 -15.126  1.00 43.26           C  
ANISOU 3372  CB  THR D  87     6044   5153   5238    433   1035    464       C  
ATOM   3373  OG1 THR D  87      -8.358  13.279 -14.398  1.00 38.57           O  
ANISOU 3373  OG1 THR D  87     5455   4490   4709    473   1088    426       O  
ATOM   3374  CG2 THR D  87      -7.750  12.182 -16.477  1.00 36.51           C  
ANISOU 3374  CG2 THR D  87     5124   4478   4268    588    954    530       C  
ATOM   3375  N   ALA D  88      -5.642   9.614 -15.303  1.00 35.54           N  
ANISOU 3375  N   ALA D  88     5019   4424   4059    263    799    304       N  
ATOM   3376  CA  ALA D  88      -4.572   8.842 -15.935  1.00 36.61           C  
ANISOU 3376  CA  ALA D  88     5155   4649   4104    261    741    309       C  
ATOM   3377  C   ALA D  88      -5.098   7.465 -16.313  1.00 37.15           C  
ANISOU 3377  C   ALA D  88     5157   4833   4124    303    576    199       C  
ATOM   3378  O   ALA D  88      -6.165   7.038 -15.859  1.00 36.22           O  
ANISOU 3378  O   ALA D  88     4965   4690   4108    280    520    133       O  
ATOM   3379  CB  ALA D  88      -3.369   8.692 -14.994  1.00 34.27           C  
ANISOU 3379  CB  ALA D  88     4898   4272   3854     94    768    271       C  
ATOM   3380  N   THR D  89      -4.314   6.757 -17.128  1.00 32.11           N  
ANISOU 3380  N   THR D  89     4529   4303   3370    375    500    183       N  
ATOM   3381  CA  THR D  89      -4.438   5.309 -17.225  1.00 34.56           C  
ANISOU 3381  CA  THR D  89     4779   4664   3689    369    320     34       C  
ATOM   3382  C   THR D  89      -3.569   4.705 -16.133  1.00 34.27           C  
ANISOU 3382  C   THR D  89     4754   4558   3710    170    364     13       C  
ATOM   3383  O   THR D  89      -2.406   5.101 -15.970  1.00 34.70           O  
ANISOU 3383  O   THR D  89     4870   4604   3710    116    461     83       O  
ATOM   3384  CB  THR D  89      -3.979   4.785 -18.594  1.00 33.74           C  
ANISOU 3384  CB  THR D  89     4703   4720   3397    591    198     -7       C  
ATOM   3385  OG1 THR D  89      -4.692   5.463 -19.630  1.00 40.18           O  
ANISOU 3385  OG1 THR D  89     5533   5635   4100    834    166     32       O  
ATOM   3386  CG2 THR D  89      -4.306   3.315 -18.692  1.00 39.60           C  
ANISOU 3386  CG2 THR D  89     5365   5464   4218    596    -42   -213       C  
ATOM   3387  N   TYR D  90      -4.127   3.758 -15.389  1.00 30.79           N  
ANISOU 3387  N   TYR D  90     4232   4060   3407     77    297    -62       N  
ATOM   3388  CA  TYR D  90      -3.444   3.104 -14.279  1.00 34.55           C  
ANISOU 3388  CA  TYR D  90     4717   4488   3922    -71    343    -64       C  
ATOM   3389  C   TYR D  90      -3.143   1.658 -14.660  1.00 31.64           C  
ANISOU 3389  C   TYR D  90     4280   4138   3604    -67    190   -154       C  
ATOM   3390  O   TYR D  90      -4.021   0.946 -15.163  1.00 34.36           O  
ANISOU 3390  O   TYR D  90     4507   4454   4093     -7     38   -238       O  
ATOM   3391  CB  TYR D  90      -4.299   3.181 -13.000  1.00 30.57           C  
ANISOU 3391  CB  TYR D  90     4172   3904   3538   -136    445    -14       C  
ATOM   3392  CG  TYR D  90      -4.242   4.564 -12.377  1.00 29.88           C  
ANISOU 3392  CG  TYR D  90     4194   3787   3372   -134    584     31       C  
ATOM   3393  CD1 TYR D  90      -5.078   5.584 -12.830  1.00 28.41           C  
ANISOU 3393  CD1 TYR D  90     4008   3583   3205    -53    623     62       C  
ATOM   3394  CD2 TYR D  90      -3.336   4.865 -11.366  1.00 31.31           C  
ANISOU 3394  CD2 TYR D  90     4476   3945   3474   -192    644     16       C  
ATOM   3395  CE1 TYR D  90      -5.022   6.865 -12.285  1.00 29.51           C  
ANISOU 3395  CE1 TYR D  90     4242   3659   3312    -41    730     82       C  
ATOM   3396  CE2 TYR D  90      -3.279   6.141 -10.805  1.00 30.09           C  
ANISOU 3396  CE2 TYR D  90     4417   3728   3288   -170    715      0       C  
ATOM   3397  CZ  TYR D  90      -4.127   7.140 -11.279  1.00 34.02           C  
ANISOU 3397  CZ  TYR D  90     4911   4185   3831   -100    763     34       C  
ATOM   3398  OH  TYR D  90      -4.071   8.419 -10.759  1.00 32.88           O  
ANISOU 3398  OH  TYR D  90     4854   3943   3696    -70    815      0       O  
ATOM   3399  N   TYR D  91      -1.897   1.232 -14.429  1.00 31.36           N  
ANISOU 3399  N   TYR D  91     4300   4130   3486   -125    208   -153       N  
ATOM   3400  CA  TYR D  91      -1.396  -0.067 -14.853  1.00 37.96           C  
ANISOU 3400  CA  TYR D  91     5093   4983   4345   -102     70   -243       C  
ATOM   3401  C   TYR D  91      -0.819  -0.792 -13.660  1.00 28.61           C  
ANISOU 3401  C   TYR D  91     3896   3743   3230   -239    128   -202       C  
ATOM   3402  O   TYR D  91      -0.171  -0.169 -12.815  1.00 31.75           O  
ANISOU 3402  O   TYR D  91     4372   4150   3541   -312    251   -132       O  
ATOM   3403  CB  TYR D  91      -0.252   0.046 -15.898  1.00 33.91           C  
ANISOU 3403  CB  TYR D  91     4663   4594   3627     19     53   -252       C  
ATOM   3404  CG  TYR D  91      -0.596   0.661 -17.230  1.00 28.85           C  
ANISOU 3404  CG  TYR D  91     4059   4063   2841    240     12   -260       C  
ATOM   3405  CD1 TYR D  91      -1.200  -0.097 -18.221  1.00 34.56           C  
ANISOU 3405  CD1 TYR D  91     4748   4837   3545    430   -210   -428       C  
ATOM   3406  CD2 TYR D  91      -0.283   1.996 -17.511  1.00 37.34           C  
ANISOU 3406  CD2 TYR D  91     5197   5182   3810    288    180   -102       C  
ATOM   3407  CE1 TYR D  91      -1.495   0.450 -19.474  1.00 40.54           C  
ANISOU 3407  CE1 TYR D  91     5562   5739   4102    705   -263   -442       C  
ATOM   3408  CE2 TYR D  91      -0.581   2.559 -18.759  1.00 38.36           C  
ANISOU 3408  CE2 TYR D  91     5362   5434   3777    540    174    -60       C  
ATOM   3409  CZ  TYR D  91      -1.181   1.770 -19.733  1.00 35.48           C  
ANISOU 3409  CZ  TYR D  91     4993   5171   3318    767    -47   -232       C  
ATOM   3410  OH  TYR D  91      -1.507   2.290 -20.959  1.00 42.61           O  
ANISOU 3410  OH  TYR D  91     5952   6233   4007   1079    -74   -205       O  
ATOM   3411  N   CYS D  92      -1.000  -2.112 -13.610  1.00 28.38           N  
ANISOU 3411  N   CYS D  92     3764   3648   3371   -253     19   -256       N  
ATOM   3412  CA  CYS D  92      -0.198  -2.935 -12.717  1.00 30.87           C  
ANISOU 3412  CA  CYS D  92     4078   3937   3715   -339     65   -205       C  
ATOM   3413  C   CYS D  92       0.763  -3.781 -13.556  1.00 38.80           C  
ANISOU 3413  C   CYS D  92     5095   4981   4667   -282    -68   -312       C  
ATOM   3414  O   CYS D  92       0.483  -4.104 -14.710  1.00 33.56           O  
ANISOU 3414  O   CYS D  92     4407   4331   4014   -156   -231   -449       O  
ATOM   3415  CB  CYS D  92      -1.081  -3.788 -11.783  1.00 32.90           C  
ANISOU 3415  CB  CYS D  92     4190   4064   4248   -392    107   -111       C  
ATOM   3416  SG  CYS D  92      -2.218  -4.925 -12.545  1.00 40.15           S  
ANISOU 3416  SG  CYS D  92     4878   4807   5571   -361   -100   -208       S  
ATOM   3417  N   ALA D  93       1.930  -4.083 -12.993  1.00 28.76           N  
ANISOU 3417  N   ALA D  93     3874   3744   3308   -337     -8   -262       N  
ATOM   3418  CA  ALA D  93       2.973  -4.780 -13.733  1.00 33.92           C  
ANISOU 3418  CA  ALA D  93     4549   4454   3885   -266    -97   -338       C  
ATOM   3419  C   ALA D  93       3.740  -5.693 -12.781  1.00 34.94           C  
ANISOU 3419  C   ALA D  93     4655   4543   4078   -350    -67   -280       C  
ATOM   3420  O   ALA D  93       3.998  -5.322 -11.639  1.00 33.82           O  
ANISOU 3420  O   ALA D  93     4545   4410   3895   -435     49   -171       O  
ATOM   3421  CB  ALA D  93       3.912  -3.773 -14.411  1.00 29.33           C  
ANISOU 3421  CB  ALA D  93     4062   4007   3075   -198    -22   -299       C  
ATOM   3422  N   ARG D  94       4.119  -6.877 -13.257  1.00 31.88           N  
ANISOU 3422  N   ARG D  94     4222   4117   3774   -293   -188   -367       N  
ATOM   3423  CA  ARG D  94       4.808  -7.856 -12.422  1.00 31.48           C  
ANISOU 3423  CA  ARG D  94     4136   4017   3809   -353   -164   -300       C  
ATOM   3424  C   ARG D  94       6.314  -7.785 -12.630  1.00 35.62           C  
ANISOU 3424  C   ARG D  94     4734   4666   4135   -322   -138   -293       C  
ATOM   3425  O   ARG D  94       6.784  -7.599 -13.761  1.00 35.09           O  
ANISOU 3425  O   ARG D  94     4707   4687   3937   -200   -183   -371       O  
ATOM   3426  CB  ARG D  94       4.332  -9.281 -12.735  1.00 31.85           C  
ANISOU 3426  CB  ARG D  94     4058   3895   4149   -315   -318   -393       C  
ATOM   3427  CG  ARG D  94       4.958 -10.340 -11.825  1.00 30.85           C  
ANISOU 3427  CG  ARG D  94     3878   3694   4151   -367   -270   -281       C  
ATOM   3428  CD  ARG D  94       4.549 -11.786 -12.188  1.00 31.44           C  
ANISOU 3428  CD  ARG D  94     3802   3545   4600   -331   -439   -378       C  
ATOM   3429  NE  ARG D  94       5.125 -12.287 -13.431  1.00 37.53           N  
ANISOU 3429  NE  ARG D  94     4617   4338   5305   -187   -641   -622       N  
ATOM   3430  CZ  ARG D  94       5.190 -13.573 -13.749  1.00 48.54           C  
ANISOU 3430  CZ  ARG D  94     5915   5552   6975   -127   -814   -750       C  
ATOM   3431  NH1 ARG D  94       4.669 -14.504 -12.965  1.00 42.75           N  
ANISOU 3431  NH1 ARG D  94     5003   4570   6669   -224   -802   -629       N  
ATOM   3432  NH2 ARG D  94       5.801 -13.938 -14.876  1.00 39.43           N  
ANISOU 3432  NH2 ARG D  94     4841   4463   5678     62   -990   -989       N  
ATOM   3433  N   ARG D  95       7.072  -7.996 -11.552  1.00 29.04           N  
ANISOU 3433  N   ARG D  95     3906   3845   3282   -397    -65   -186       N  
ATOM   3434  CA  ARG D  95       8.511  -8.231 -11.658  1.00 33.84           C  
ANISOU 3434  CA  ARG D  95     4533   4536   3789   -373    -66   -174       C  
ATOM   3435  C   ARG D  95       8.835  -9.524 -10.925  1.00 41.03           C  
ANISOU 3435  C   ARG D  95     5392   5376   4820   -385    -89   -128       C  
ATOM   3436  O   ARG D  95       8.362  -9.737  -9.799  1.00 33.88           O  
ANISOU 3436  O   ARG D  95     4468   4421   3985   -433    -28    -21       O  
ATOM   3437  CB  ARG D  95       9.349  -7.087 -11.062  1.00 31.73           C  
ANISOU 3437  CB  ARG D  95     4306   4354   3397   -440     10   -100       C  
ATOM   3438  CG  ARG D  95      10.866  -7.276 -11.246  1.00 35.69           C  
ANISOU 3438  CG  ARG D  95     4778   4925   3860   -418      7    -70       C  
ATOM   3439  CD  ARG D  95      11.567  -7.877 -10.029  1.00 41.96           C  
ANISOU 3439  CD  ARG D  95     5556   5720   4666   -461    -19    -23       C  
ATOM   3440  NE  ARG D  95      12.955  -8.200 -10.354  1.00 37.51           N  
ANISOU 3440  NE  ARG D  95     4935   5212   4104   -428    -33      4       N  
ATOM   3441  CZ  ARG D  95      13.867  -8.577  -9.468  1.00 39.16           C  
ANISOU 3441  CZ  ARG D  95     5114   5446   4318   -446    -74     42       C  
ATOM   3442  NH1 ARG D  95      13.567  -8.722  -8.185  1.00 33.87           N  
ANISOU 3442  NH1 ARG D  95     4488   4773   3609   -463   -102     60       N  
ATOM   3443  NH2 ARG D  95      15.113  -8.818  -9.879  1.00 34.18           N  
ANISOU 3443  NH2 ARG D  95     4406   4862   3720   -412    -79     77       N  
ATOM   3444  N   VAL D  96       9.647 -10.379 -11.556  1.00 36.14           N  
ANISOU 3444  N   VAL D  96     4753   4764   4214   -306   -156   -187       N  
ATOM   3445  CA  VAL D  96      10.069 -11.658 -10.986  1.00 35.78           C  
ANISOU 3445  CA  VAL D  96     4653   4640   4304   -300   -181   -141       C  
ATOM   3446  C   VAL D  96      11.561 -11.591 -10.684  1.00 39.11           C  
ANISOU 3446  C   VAL D  96     5093   5184   4582   -292   -146    -79       C  
ATOM   3447  O   VAL D  96      12.331 -11.008 -11.456  1.00 38.50           O  
ANISOU 3447  O   VAL D  96     5036   5214   4380   -244   -134   -111       O  
ATOM   3448  CB  VAL D  96       9.776 -12.835 -11.942  1.00 35.29           C  
ANISOU 3448  CB  VAL D  96     4535   4446   4428   -195   -325   -293       C  
ATOM   3449  CG1 VAL D  96      10.030 -14.179 -11.249  1.00 43.08           C  
ANISOU 3449  CG1 VAL D  96     5438   5290   5641   -203   -339   -216       C  
ATOM   3450  CG2 VAL D  96       8.359 -12.758 -12.502  1.00 34.37           C  
ANISOU 3450  CG2 VAL D  96     4376   4207   4476   -183   -421   -409       C  
ATOM   3451  N   VAL D  97      11.970 -12.230  -9.583  1.00 38.35           N  
ANISOU 3451  N   VAL D  97     4973   5070   4529   -316   -120     33       N  
ATOM   3452  CA  VAL D  97      13.380 -12.315  -9.208  1.00 32.05           C  
ANISOU 3452  CA  VAL D  97     4168   4374   3636   -299   -122     84       C  
ATOM   3453  C   VAL D  97      14.223 -12.761 -10.402  1.00 34.42           C  
ANISOU 3453  C   VAL D  97     4440   4703   3934   -205   -159      6       C  
ATOM   3454  O   VAL D  97      13.847 -13.671 -11.151  1.00 34.38           O  
ANISOU 3454  O   VAL D  97     4424   4605   4032   -116   -220    -89       O  
ATOM   3455  CB  VAL D  97      13.549 -13.282  -8.021  1.00 37.15           C  
ANISOU 3455  CB  VAL D  97     4789   4984   4343   -277   -104    215       C  
ATOM   3456  CG1 VAL D  97      12.863 -14.598  -8.309  1.00 36.25           C  
ANISOU 3456  CG1 VAL D  97     4608   4686   4481   -238   -117    226       C  
ATOM   3457  CG2 VAL D  97      15.014 -13.463  -7.659  1.00 38.72           C  
ANISOU 3457  CG2 VAL D  97     4967   5287   4457   -242   -138    252       C  
ATOM   3458  N   ALA D  98      15.370 -12.110 -10.572  1.00 36.48           N  
ANISOU 3458  N   ALA D  98     4677   5083   4100   -200   -130     43       N  
ATOM   3459  CA  ALA D  98      16.264 -12.350 -11.703  1.00 35.62           C  
ANISOU 3459  CA  ALA D  98     4534   5042   3956    -68   -109     25       C  
ATOM   3460  C   ALA D  98      17.578 -11.649 -11.397  1.00 37.28           C  
ANISOU 3460  C   ALA D  98     4654   5346   4163   -110    -63    140       C  
ATOM   3461  O   ALA D  98      17.678 -10.899 -10.428  1.00 39.17           O  
ANISOU 3461  O   ALA D  98     4874   5583   4426   -236    -93    174       O  
ATOM   3462  CB  ALA D  98      15.651 -11.849 -13.014  1.00 40.48           C  
ANISOU 3462  CB  ALA D  98     5199   5693   4488     42    -81    -55       C  
ATOM   3463  N   THR D  99      18.600 -11.891 -12.237  1.00 41.21           N  
ANISOU 3463  N   THR D  99     5083   5919   4654     22     -1    192       N  
ATOM   3464  CA  THR D  99      19.822 -11.104 -12.077  1.00 40.81           C  
ANISOU 3464  CA  THR D  99     4889   5926   4692    -24     54    330       C  
ATOM   3465  C   THR D  99      19.611  -9.665 -12.536  1.00 40.13           C  
ANISOU 3465  C   THR D  99     4763   5842   4641    -75    142    398       C  
ATOM   3466  O   THR D  99      20.308  -8.756 -12.071  1.00 42.77           O  
ANISOU 3466  O   THR D  99     4960   6145   5145   -189    135    483       O  
ATOM   3467  CB  THR D  99      20.996 -11.730 -12.846  1.00 43.16           C  
ANISOU 3467  CB  THR D  99     5092   6305   5002    152    141    423       C  
ATOM   3468  OG1 THR D  99      20.654 -11.848 -14.227  1.00 50.96           O  
ANISOU 3468  OG1 THR D  99     6152   7366   5846    374    247    405       O  
ATOM   3469  CG2 THR D  99      21.323 -13.108 -12.291  1.00 56.01           C  
ANISOU 3469  CG2 THR D  99     6738   7905   6637    192     48    369       C  
ATOM   3470  N   ASP D 100      18.675  -9.449 -13.452  1.00 40.65           N  
ANISOU 3470  N   ASP D 100     4930   5930   4584     21    205    355       N  
ATOM   3471  CA  ASP D 100      18.295  -8.126 -13.931  1.00 36.99           C  
ANISOU 3471  CA  ASP D 100     4448   5465   4141     -2    303    433       C  
ATOM   3472  C   ASP D 100      17.011  -7.682 -13.229  1.00 39.87           C  
ANISOU 3472  C   ASP D 100     4923   5743   4481   -151    205    304       C  
ATOM   3473  O   ASP D 100      16.364  -8.465 -12.528  1.00 38.09           O  
ANISOU 3473  O   ASP D 100     4784   5473   4214   -200     94    184       O  
ATOM   3474  CB  ASP D 100      18.113  -8.145 -15.458  1.00 44.12           C  
ANISOU 3474  CB  ASP D 100     5400   6486   4876    268    445    487       C  
ATOM   3475  CG  ASP D 100      19.329  -8.717 -16.209  1.00 48.80           C  
ANISOU 3475  CG  ASP D 100     5906   7197   5439    491    572    624       C  
ATOM   3476  OD1 ASP D 100      20.484  -8.354 -15.887  1.00 45.74           O  
ANISOU 3476  OD1 ASP D 100     5329   6794   5257    418    653    807       O  
ATOM   3477  OD2 ASP D 100      19.132  -9.557 -17.118  1.00 43.73           O  
ANISOU 3477  OD2 ASP D 100     5375   6657   4583    761    575    532       O  
ATOM   3478  N   TRP D 100A     16.628  -6.414 -13.420  1.00 34.50           N  
ANISOU 3478  N   TRP D 100A    4227   5031   3852   -206    268    360       N  
ATOM   3479  CA  TRP D 100A     15.396  -5.904 -12.807  1.00 36.73           C  
ANISOU 3479  CA  TRP D 100A    4612   5241   4104   -320    196    250       C  
ATOM   3480  C   TRP D 100A     14.530  -5.258 -13.879  1.00 31.76           C  
ANISOU 3480  C   TRP D 100A    4038   4641   3389   -217    292    275       C  
ATOM   3481  O   TRP D 100A     14.802  -4.137 -14.312  1.00 38.15           O  
ANISOU 3481  O   TRP D 100A    4771   5435   4287   -213    404    411       O  
ATOM   3482  CB  TRP D 100A     15.684  -4.916 -11.663  1.00 37.85           C  
ANISOU 3482  CB  TRP D 100A    4694   5287   4399   -494    121    239       C  
ATOM   3483  CG  TRP D 100A     14.600  -4.955 -10.540  1.00 32.07           C  
ANISOU 3483  CG  TRP D 100A    4094   4516   3577   -567     17    101       C  
ATOM   3484  CD1 TRP D 100A     14.748  -5.445  -9.274  1.00 39.09           C  
ANISOU 3484  CD1 TRP D 100A    5018   5408   4427   -598    -97     34       C  
ATOM   3485  CD2 TRP D 100A     13.238  -4.487 -10.629  1.00 35.14           C  
ANISOU 3485  CD2 TRP D 100A    4584   4876   3893   -572     46     52       C  
ATOM   3486  NE1 TRP D 100A     13.567  -5.318  -8.569  1.00 38.45           N  
ANISOU 3486  NE1 TRP D 100A    5054   5310   4243   -603   -110    -29       N  
ATOM   3487  CE2 TRP D 100A     12.624  -4.741  -9.380  1.00 34.89           C  
ANISOU 3487  CE2 TRP D 100A    4636   4830   3791   -604    -27    -24       C  
ATOM   3488  CE3 TRP D 100A     12.477  -3.898 -11.644  1.00 32.32           C  
ANISOU 3488  CE3 TRP D 100A    4251   4519   3511   -522    136     80       C  
ATOM   3489  CZ2 TRP D 100A     11.291  -4.414  -9.119  1.00 36.33           C  
ANISOU 3489  CZ2 TRP D 100A    4905   4985   3914   -603      2    -59       C  
ATOM   3490  CZ3 TRP D 100A     11.151  -3.570 -11.380  1.00 32.72           C  
ANISOU 3490  CZ3 TRP D 100A    4390   4534   3508   -541    130     16       C  
ATOM   3491  CH2 TRP D 100A     10.569  -3.840 -10.127  1.00 29.43           C  
ANISOU 3491  CH2 TRP D 100A    4036   4091   3055   -588     71    -48       C  
ATOM   3492  N   TYR D 100B     13.463  -5.946 -14.276  1.00 29.98           N  
ANISOU 3492  N   TYR D 100B    3926   4437   3029   -128    234    148       N  
ATOM   3493  CA  TYR D 100B     12.565  -5.425 -15.296  1.00 33.17           C  
ANISOU 3493  CA  TYR D 100B    4392   4886   3324      6    280    138       C  
ATOM   3494  C   TYR D 100B     11.174  -6.009 -15.073  1.00 38.19           C  
ANISOU 3494  C   TYR D 100B    5112   5459   3941    -17    143    -41       C  
ATOM   3495  O   TYR D 100B     11.026  -7.123 -14.550  1.00 34.02           O  
ANISOU 3495  O   TYR D 100B    4585   4870   3471    -56     38   -137       O  
ATOM   3496  CB  TYR D 100B     13.103  -5.759 -16.701  1.00 33.63           C  
ANISOU 3496  CB  TYR D 100B    4459   5094   3226    298    364    197       C  
ATOM   3497  CG  TYR D 100B     13.253  -7.251 -16.890  1.00 36.45           C  
ANISOU 3497  CG  TYR D 100B    4858   5476   3515    419    239     40       C  
ATOM   3498  CD1 TYR D 100B     14.402  -7.910 -16.475  1.00 33.40           C  
ANISOU 3498  CD1 TYR D 100B    4401   5092   3196    388    255     94       C  
ATOM   3499  CD2 TYR D 100B     12.242  -7.999 -17.479  1.00 39.15           C  
ANISOU 3499  CD2 TYR D 100B    5294   5812   3769    568     79   -177       C  
ATOM   3500  CE1 TYR D 100B     14.527  -9.291 -16.623  1.00 38.56           C  
ANISOU 3500  CE1 TYR D 100B    5092   5740   3820    502    136    -52       C  
ATOM   3501  CE2 TYR D 100B     12.376  -9.364 -17.664  1.00 37.24           C  
ANISOU 3501  CE2 TYR D 100B    5074   5544   3532    683    -67   -347       C  
ATOM   3502  CZ  TYR D 100B     13.513 -10.007 -17.215  1.00 35.50           C  
ANISOU 3502  CZ  TYR D 100B    4796   5322   3371    646    -26   -276       C  
ATOM   3503  OH  TYR D 100B     13.630 -11.377 -17.381  1.00 44.66           O  
ANISOU 3503  OH  TYR D 100B    5974   6428   4566    763   -173   -447       O  
ATOM   3504  N   PHE D 100C     10.150  -5.235 -15.430  1.00 34.23           N  
ANISOU 3504  N   PHE D 100C    3995   4991   4020    260    334   -280       N  
ATOM   3505  CA  PHE D 100C      8.795  -5.771 -15.421  1.00 35.89           C  
ANISOU 3505  CA  PHE D 100C    4657   5098   3880    217    167   -290       C  
ATOM   3506  C   PHE D 100C      8.626  -6.758 -16.561  1.00 46.39           C  
ANISOU 3506  C   PHE D 100C    6351   6480   4795    503    196   -164       C  
ATOM   3507  O   PHE D 100C      9.079  -6.501 -17.679  1.00 43.26           O  
ANISOU 3507  O   PHE D 100C    5905   6155   4378    703    452     46       O  
ATOM   3508  CB  PHE D 100C      7.773  -4.656 -15.564  1.00 32.61           C  
ANISOU 3508  CB  PHE D 100C    4198   4536   3657    -24    253   -196       C  
ATOM   3509  CG  PHE D 100C      7.773  -3.713 -14.420  1.00 33.56           C  
ANISOU 3509  CG  PHE D 100C    4051   4568   4134   -274    174   -348       C  
ATOM   3510  CD1 PHE D 100C      7.406  -4.156 -13.150  1.00 31.37           C  
ANISOU 3510  CD1 PHE D 100C    3912   4262   3745   -321    -91   -573       C  
ATOM   3511  CD2 PHE D 100C      8.159  -2.392 -14.590  1.00 39.57           C  
ANISOU 3511  CD2 PHE D 100C    4458   5240   5336   -426    375   -265       C  
ATOM   3512  CE1 PHE D 100C      7.431  -3.287 -12.084  1.00 30.71           C  
ANISOU 3512  CE1 PHE D 100C    3637   4100   3933   -462   -200   -742       C  
ATOM   3513  CE2 PHE D 100C      8.172  -1.510 -13.521  1.00 36.34           C  
ANISOU 3513  CE2 PHE D 100C    3828   4714   5264   -632    242   -456       C  
ATOM   3514  CZ  PHE D 100C      7.807  -1.964 -12.263  1.00 36.41           C  
ANISOU 3514  CZ  PHE D 100C    3998   4732   5103   -624    -72   -711       C  
ATOM   3515  N   ASP D 101       7.975  -7.899 -16.297  1.00 37.72           N  
ANISOU 3515  N   ASP D 101     5647   5316   3368    551    -52   -288       N  
ATOM   3516  CA  ASP D 101       7.848  -8.868 -17.382  1.00 40.50           C  
ANISOU 3516  CA  ASP D 101     6367   5680   3343    845    -96   -228       C  
ATOM   3517  C   ASP D 101       6.447  -8.970 -17.974  1.00 47.38           C  
ANISOU 3517  C   ASP D 101     7505   6396   4101    770   -235   -234       C  
ATOM   3518  O   ASP D 101       6.320  -9.447 -19.107  1.00 47.73           O  
ANISOU 3518  O   ASP D 101     7817   6450   3869   1060   -280   -189       O  
ATOM   3519  CB  ASP D 101       8.362 -10.259 -16.944  1.00 45.23           C  
ANISOU 3519  CB  ASP D 101     7247   6292   3647   1049   -280   -372       C  
ATOM   3520  CG  ASP D 101       7.436 -10.993 -15.968  1.00 42.80           C  
ANISOU 3520  CG  ASP D 101     7198   5765   3299    835   -499   -526       C  
ATOM   3521  OD1 ASP D 101       6.797 -10.347 -15.121  1.00 42.72           O  
ANISOU 3521  OD1 ASP D 101     7057   5675   3499    548   -502   -568       O  
ATOM   3522  OD2 ASP D 101       7.411 -12.246 -16.010  1.00 47.92           O1-
ANISOU 3522  OD2 ASP D 101     8001   6274   3932    902   -576   -534       O1-
ATOM   3523  N  AVAL D 102       5.406  -8.534 -17.259  0.55 39.21           N  
ANISOU 3523  N  AVAL D 102     6395   5230   3271    435   -321   -308       N  
ATOM   3524  N  BVAL D 102       5.416  -8.506 -17.271  0.45 40.44           N  
ANISOU 3524  N  BVAL D 102     6546   5390   3432    436   -316   -304       N  
ATOM   3525  CA AVAL D 102       4.029  -8.548 -17.763  0.55 39.86           C  
ANISOU 3525  CA AVAL D 102     6623   5184   3338    344   -472   -350       C  
ATOM   3526  CA BVAL D 102       4.064  -8.502 -17.815  0.45 41.10           C  
ANISOU 3526  CA BVAL D 102     6774   5350   3493    356   -462   -341       C  
ATOM   3527  C  AVAL D 102       3.295  -7.321 -17.225  0.55 39.26           C  
ANISOU 3527  C  AVAL D 102     6272   5078   3569     55   -386   -318       C  
ATOM   3528  C  BVAL D 102       3.317  -7.305 -17.243  0.45 39.45           C  
ANISOU 3528  C  BVAL D 102     6294   5105   3592     60   -381   -315       C  
ATOM   3529  O  AVAL D 102       3.374  -7.016 -16.032  0.55 37.41           O  
ANISOU 3529  O  AVAL D 102     5880   4817   3517   -160   -345   -364       O  
ATOM   3530  O  BVAL D 102       3.435  -6.989 -16.056  0.45 37.68           O  
ANISOU 3530  O  BVAL D 102     5907   4858   3552   -151   -337   -358       O  
ATOM   3531  CB AVAL D 102       3.274  -9.840 -17.358  0.55 41.09           C  
ANISOU 3531  CB AVAL D 102     7058   5147   3409    241   -726   -527       C  
ATOM   3532  CB BVAL D 102       3.333  -9.832 -17.517  0.45 41.40           C  
ANISOU 3532  CB BVAL D 102     7108   5200   3422    281   -725   -519       C  
ATOM   3533  CG1AVAL D 102       1.849  -9.810 -17.890  0.55 44.03           C  
ANISOU 3533  CG1AVAL D 102     7464   5387   3879    121   -914   -619       C  
ATOM   3534  CG1BVAL D 102       3.172 -10.046 -16.025  0.45 39.23           C  
ANISOU 3534  CG1BVAL D 102     6782   4822   3303     10   -697   -580       C  
ATOM   3535  CG2AVAL D 102       3.975 -11.090 -17.879  0.55 44.11           C  
ANISOU 3535  CG2AVAL D 102     7644   5514   3600    521   -790   -542       C  
ATOM   3536  CG2BVAL D 102       1.985  -9.875 -18.229  0.45 44.12           C  
ANISOU 3536  CG2BVAL D 102     7526   5422   3816    220   -933   -613       C  
ATOM   3537  N   TRP D 103       2.548  -6.638 -18.097  1.00 36.65           N  
ANISOU 3537  N   TRP D 103     5930   4746   3249    112   -384   -258       N  
ATOM   3538  CA  TRP D 103       1.731  -5.496 -17.697  1.00 36.02           C  
ANISOU 3538  CA  TRP D 103     5636   4631   3417   -108   -323   -234       C  
ATOM   3539  C   TRP D 103       0.256  -5.817 -17.904  1.00 36.79           C  
ANISOU 3539  C   TRP D 103     5804   4644   3529   -189   -566   -374       C  
ATOM   3540  O   TRP D 103      -0.107  -6.632 -18.757  1.00 38.19           O  
ANISOU 3540  O   TRP D 103     6190   4792   3530    -10   -787   -478       O  
ATOM   3541  CB  TRP D 103       2.040  -4.236 -18.530  1.00 38.74           C  
ANISOU 3541  CB  TRP D 103     5889   5032   3800     54    -83    -34       C  
ATOM   3542  CG  TRP D 103       3.362  -3.605 -18.302  1.00 37.83           C  
ANISOU 3542  CG  TRP D 103     5566   4954   3855     47    207    111       C  
ATOM   3543  CD1 TRP D 103       4.587  -4.197 -18.439  1.00 42.45           C  
ANISOU 3543  CD1 TRP D 103     6139   5623   4367    199    304    153       C  
ATOM   3544  CD2 TRP D 103       3.610  -2.239 -17.957  1.00 33.72           C  
ANISOU 3544  CD2 TRP D 103     4784   4368   3661   -111    434    217       C  
ATOM   3545  NE1 TRP D 103       5.586  -3.281 -18.188  1.00 38.86           N  
ANISOU 3545  NE1 TRP D 103     5364   5168   4232    116    579    268       N  
ATOM   3546  CE2 TRP D 103       5.011  -2.074 -17.883  1.00 34.55           C  
ANISOU 3546  CE2 TRP D 103     4674   4504   3950    -92    654    302       C  
ATOM   3547  CE3 TRP D 103       2.786  -1.136 -17.713  1.00 34.75           C  
ANISOU 3547  CE3 TRP D 103     4835   4401   3966   -256    465    236       C  
ATOM   3548  CZ2 TRP D 103       5.607  -0.850 -17.566  1.00 36.52           C  
ANISOU 3548  CZ2 TRP D 103     4608   4646   4622   -263    889    385       C  
ATOM   3549  CZ3 TRP D 103       3.380   0.079 -17.394  1.00 40.99           C  
ANISOU 3549  CZ3 TRP D 103     5387   5083   5105   -393    699    332       C  
ATOM   3550  CH2 TRP D 103       4.780   0.212 -17.329  1.00 42.92           C  
ANISOU 3550  CH2 TRP D 103     5398   5317   5593   -417    903    398       C  
ATOM   3551  N   GLY D 104      -0.600  -5.153 -17.144  1.00 38.24           N  
ANISOU 3551  N   GLY D 104     5794   4788   3947   -435   -543   -401       N  
ATOM   3552  CA  GLY D 104      -2.017  -5.257 -17.416  1.00 38.92           C  
ANISOU 3552  CA  GLY D 104     5839   4825   4125   -501   -746   -530       C  
ATOM   3553  C   GLY D 104      -2.435  -4.349 -18.557  1.00 42.49           C  
ANISOU 3553  C   GLY D 104     6301   5361   4482   -239   -786   -489       C  
ATOM   3554  O   GLY D 104      -1.653  -3.547 -19.065  1.00 41.06           O  
ANISOU 3554  O   GLY D 104     6172   5242   4186    -38   -576   -306       O  
ATOM   3555  N   ALA D 105      -3.701  -4.483 -18.960  1.00 39.03           N  
ANISOU 3555  N   ALA D 105     5805   4908   4115   -223  -1049   -663       N  
ATOM   3556  CA  ALA D 105      -4.235  -3.657 -20.038  1.00 45.30           C  
ANISOU 3556  CA  ALA D 105     6652   5790   4768    110  -1146   -667       C  
ATOM   3557  C   ALA D 105      -4.426  -2.198 -19.630  1.00 50.09           C  
ANISOU 3557  C   ALA D 105     7106   6439   5486     64   -897   -505       C  
ATOM   3558  O   ALA D 105      -4.518  -1.329 -20.505  1.00 45.52           O  
ANISOU 3558  O   ALA D 105     6654   5912   4731    397   -851   -413       O  
ATOM   3559  CB  ALA D 105      -5.564  -4.235 -20.522  1.00 46.11           C  
ANISOU 3559  CB  ALA D 105     6678   5875   4967    153  -1574   -973       C  
ATOM   3560  N   GLY D 106      -4.499  -1.909 -18.334  1.00 40.59           N  
ANISOU 3560  N   GLY D 106     5688   5195   4538   -287   -736   -470       N  
ATOM   3561  CA  GLY D 106      -4.726  -0.550 -17.884  1.00 34.18           C  
ANISOU 3561  CA  GLY D 106     4760   4392   3836   -319   -544   -355       C  
ATOM   3562  C   GLY D 106      -6.188  -0.233 -17.640  1.00 38.52           C  
ANISOU 3562  C   GLY D 106     5108   4991   4538   -364   -692   -491       C  
ATOM   3563  O   GLY D 106      -7.069  -0.708 -18.357  1.00 38.16           O  
ANISOU 3563  O   GLY D 106     5023   5000   4476   -232   -979   -671       O  
ATOM   3564  N   THR D 107      -6.463   0.569 -16.619  1.00 35.92           N  
ANISOU 3564  N   THR D 107     4632   4645   4369   -523   -524   -433       N  
ATOM   3565  CA  THR D 107      -7.810   1.047 -16.361  1.00 36.35           C  
ANISOU 3565  CA  THR D 107     4475   4773   4563   -516   -603   -526       C  
ATOM   3566  C   THR D 107      -7.780   2.571 -16.383  1.00 31.84           C  
ANISOU 3566  C   THR D 107     3978   4194   3925   -340   -445   -394       C  
ATOM   3567  O   THR D 107      -6.852   3.194 -15.853  1.00 32.95           O  
ANISOU 3567  O   THR D 107     4216   4222   4080   -418   -228   -257       O  
ATOM   3568  CB  THR D 107      -8.349   0.501 -15.021  1.00 40.14           C  
ANISOU 3568  CB  THR D 107     4738   5228   5287   -824   -516   -571       C  
ATOM   3569  OG1 THR D 107      -9.723   0.865 -14.870  1.00 38.56           O  
ANISOU 3569  OG1 THR D 107     4269   5124   5259   -798   -574   -660       O  
ATOM   3570  CG2 THR D 107      -7.549   1.040 -13.836  1.00 35.79           C  
ANISOU 3570  CG2 THR D 107     4275   4599   4726   -929   -262   -441       C  
ATOM   3571  N   THR D 108      -8.772   3.167 -17.040  1.00 38.62           N  
ANISOU 3571  N   THR D 108     4798   5150   4725    -80   -581   -460       N  
ATOM   3572  CA  THR D 108      -8.833   4.614 -17.210  1.00 40.22           C  
ANISOU 3572  CA  THR D 108     5139   5315   4830    153   -438   -331       C  
ATOM   3573  C   THR D 108      -9.587   5.247 -16.047  1.00 34.03           C  
ANISOU 3573  C   THR D 108     4162   4554   4214     35   -357   -357       C  
ATOM   3574  O   THR D 108     -10.711   4.841 -15.740  1.00 37.38           O  
ANISOU 3574  O   THR D 108     4308   5121   4774     -3   -491   -506       O  
ATOM   3575  CB  THR D 108      -9.528   4.961 -18.526  1.00 45.14           C  
ANISOU 3575  CB  THR D 108     5887   6041   5224    604   -638   -394       C  
ATOM   3576  OG1 THR D 108      -8.750   4.473 -19.622  1.00 43.54           O  
ANISOU 3576  OG1 THR D 108     5950   5804   4787    812   -669   -336       O  
ATOM   3577  CG2 THR D 108      -9.720   6.463 -18.661  1.00 43.03           C  
ANISOU 3577  CG2 THR D 108     5801   5707   4840    880   -470   -250       C  
ATOM   3578  N   VAL D 109      -8.974   6.241 -15.414  1.00 31.02           N  
ANISOU 3578  N   VAL D 109     3916   4018   3853     -4   -137   -224       N  
ATOM   3579  CA  VAL D 109      -9.600   6.998 -14.330  1.00 35.25           C  
ANISOU 3579  CA  VAL D 109     4364   4552   4478    -20    -59   -243       C  
ATOM   3580  C   VAL D 109      -9.648   8.469 -14.723  1.00 39.99           C  
ANISOU 3580  C   VAL D 109     5188   5032   4975    253     28   -144       C  
ATOM   3581  O   VAL D 109      -8.640   9.029 -15.166  1.00 40.50           O  
ANISOU 3581  O   VAL D 109     5486   4880   5024    270    171     -4       O  
ATOM   3582  CB  VAL D 109      -8.828   6.840 -13.010  1.00 37.77           C  
ANISOU 3582  CB  VAL D 109     4691   4749   4913   -281     67   -234       C  
ATOM   3583  CG1 VAL D 109      -9.458   7.712 -11.926  1.00 40.81           C  
ANISOU 3583  CG1 VAL D 109     5067   5122   5319   -193    139   -257       C  
ATOM   3584  CG2 VAL D 109      -8.766   5.375 -12.602  1.00 35.15           C  
ANISOU 3584  CG2 VAL D 109     4212   4498   4646   -508     27   -298       C  
ATOM   3585  N   THR D 110     -10.800   9.110 -14.527  1.00 37.84           N  
ANISOU 3585  N   THR D 110     4840   4874   4662    470    -23   -202       N  
ATOM   3586  CA  THR D 110     -10.931  10.539 -14.799  1.00 35.98           C  
ANISOU 3586  CA  THR D 110     4864   4498   4309    764     64   -111       C  
ATOM   3587  C   THR D 110     -11.441  11.218 -13.539  1.00 45.15           C  
ANISOU 3587  C   THR D 110     5980   5643   5534    769    122   -158       C  
ATOM   3588  O   THR D 110     -12.493  10.838 -13.016  1.00 38.87           O  
ANISOU 3588  O   THR D 110     4908   5091   4768    809     56   -262       O  
ATOM   3589  CB  THR D 110     -11.885  10.815 -15.962  1.00 40.21           C  
ANISOU 3589  CB  THR D 110     5444   5203   4630   1194    -88   -148       C  
ATOM   3590  OG1 THR D 110     -11.434  10.119 -17.128  1.00 43.88           O  
ANISOU 3590  OG1 THR D 110     6004   5694   4977   1271   -171   -127       O  
ATOM   3591  CG2 THR D 110     -11.916  12.308 -16.270  1.00 46.15           C  
ANISOU 3591  CG2 THR D 110     6558   5752   5223   1535     51    -13       C  
ATOM   3592  N   VAL D 111     -10.695  12.202 -13.049  1.00 38.60           N  
ANISOU 3592  N   VAL D 111     5406   4508   4752    739    250    -89       N  
ATOM   3593  CA  VAL D 111     -11.150  13.019 -11.923  1.00 37.87           C  
ANISOU 3593  CA  VAL D 111     5373   4358   4657    848    272   -151       C  
ATOM   3594  C   VAL D 111     -11.874  14.227 -12.494  1.00 45.02           C  
ANISOU 3594  C   VAL D 111     6494   5215   5398   1248    284   -100       C  
ATOM   3595  O   VAL D 111     -11.300  14.986 -13.281  1.00 42.52           O  
ANISOU 3595  O   VAL D 111     6474   4620   5060   1340    379     27       O  
ATOM   3596  CB  VAL D 111      -9.985  13.462 -11.022  1.00 36.68           C  
ANISOU 3596  CB  VAL D 111     5396   3870   4670    637    316   -181       C  
ATOM   3597  CG1 VAL D 111     -10.523  14.309  -9.821  1.00 38.17           C  
ANISOU 3597  CG1 VAL D 111     5711   3999   4793    842    288   -285       C  
ATOM   3598  CG2 VAL D 111      -9.180  12.272 -10.543  1.00 34.42           C  
ANISOU 3598  CG2 VAL D 111     4941   3636   4501    311    285   -238       C  
ATOM   3599  N   CYS D 112     -13.124  14.425 -12.084  1.00 41.43           N  
ANISOU 3599  N   CYS D 112     5898   5013   4830   1512    227   -181       N  
ATOM   3600  CA  CYS D 112     -13.935  15.498 -12.637  1.00 46.93           C  
ANISOU 3600  CA  CYS D 112     6785   5722   5325   1966    206   -157       C  
ATOM   3601  C   CYS D 112     -13.426  16.854 -12.137  1.00 53.87           C  
ANISOU 3601  C   CYS D 112     8091   6185   6192   2067    309   -104       C  
ATOM   3602  O   CYS D 112     -12.675  16.943 -11.164  1.00 49.00           O  
ANISOU 3602  O   CYS D 112     7543   5342   5734   1819    337   -151       O  
ATOM   3603  CB  CYS D 112     -15.406  15.296 -12.252  1.00 52.79           C  
ANISOU 3603  CB  CYS D 112     7181   6876   6003   2220    121   -276       C  
ATOM   3604  SG  CYS D 112     -16.152  13.741 -12.884  1.00 61.99           S  
ANISOU 3604  SG  CYS D 112     7771   8472   7310   2085    -48   -400       S  
ATOM   3605  N   SER D 113     -13.820  17.920 -12.838  1.00 56.23           N  
ANISOU 3605  N   SER D 113     8706   6355   6305   2463    340    -27       N  
ATOM   3606  CA  SER D 113     -13.357  19.257 -12.467  1.00 65.10           C  
ANISOU 3606  CA  SER D 113    10274   7005   7456   2560    441     24       C  
ATOM   3607  C   SER D 113     -13.857  19.658 -11.087  1.00 72.45           C  
ANISOU 3607  C   SER D 113    11198   7976   8355   2670    366   -130       C  
ATOM   3608  O   SER D 113     -13.110  20.237 -10.290  1.00 81.82           O  
ANISOU 3608  O   SER D 113    12614   8777   9698   2523    363   -193       O  
ATOM   3609  CB  SER D 113     -13.823  20.284 -13.495  1.00 71.78           C  
ANISOU 3609  CB  SER D 113    11507   7712   8053   3042    515    156       C  
ATOM   3610  OG  SER D 113     -15.239  20.353 -13.525  1.00 80.68           O  
ANISOU 3610  OG  SER D 113    12489   9268   8897   3506    369     52       O  
ATOM   3611  N   GLY D 114     -15.117  19.364 -10.793  1.00 84.89           N  
ANISOU 3611  N   GLY D 114     8034  11074  13147    169  -1200   1086       N  
ATOM   3612  CA  GLY D 114     -15.771  19.871  -9.607  1.00 88.33           C  
ANISOU 3612  CA  GLY D 114     8926  11309  13326    -53  -1360    806       C  
ATOM   3613  C   GLY D 114     -17.257  19.989  -9.863  1.00 93.98           C  
ANISOU 3613  C   GLY D 114     9889  11913  13906    116  -1038    400       C  
ATOM   3614  O   GLY D 114     -17.686  20.796 -10.696  1.00 93.57           O  
ANISOU 3614  O   GLY D 114     9782  11785  13985    174   -935    324       O  
ATOM   3615  N   SER D 115     -18.037  19.176  -9.149  1.00 98.11           N  
ANISOU 3615  N   SER D 115    10652  12420  14205    178   -898    186       N  
ATOM   3616  CA  SER D 115     -19.462  19.017  -9.415  1.00 92.20           C  
ANISOU 3616  CA  SER D 115    10058  11579  13394    374   -566   -138       C  
ATOM   3617  C   SER D 115     -20.178  20.361  -9.483  1.00 97.38           C  
ANISOU 3617  C   SER D 115    10893  12007  14101    297   -529   -394       C  
ATOM   3618  O   SER D 115     -19.915  21.271  -8.692  1.00103.07           O  
ANISOU 3618  O   SER D 115    11832  12590  14740     52   -736   -488       O  
ATOM   3619  CB  SER D 115     -20.094  18.139  -8.329  1.00 89.39           C  
ANISOU 3619  CB  SER D 115     9962  11228  12774    356   -479   -285       C  
ATOM   3620  OG  SER D 115     -21.426  17.777  -8.652  1.00 85.38           O  
ANISOU 3620  OG  SER D 115     9516  10646  12279    568   -153   -520       O  
ATOM   3621  N   ASP D 116     -21.081  20.480 -10.455  1.00 88.92           N  
ANISOU 3621  N   ASP D 116     9726  10866  13194    501   -296   -504       N  
ATOM   3622  CA  ASP D 116     -21.983  21.616 -10.556  1.00 87.16           C  
ANISOU 3622  CA  ASP D 116     9631  10376  13110    475   -229   -752       C  
ATOM   3623  C   ASP D 116     -23.284  21.384  -9.802  1.00 79.76           C  
ANISOU 3623  C   ASP D 116     8952   9287  12067    548     38  -1099       C  
ATOM   3624  O   ASP D 116     -24.262  22.102 -10.039  1.00 78.91           O  
ANISOU 3624  O   ASP D 116     8879   8938  12166    610    179  -1308       O  
ATOM   3625  CB  ASP D 116     -22.277  21.923 -12.024  1.00 83.07           C  
ANISOU 3625  CB  ASP D 116     8851   9849  12861    616   -167   -624       C  
ATOM   3626  CG  ASP D 116     -21.888  23.330 -12.405  1.00 92.00           C  
ANISOU 3626  CG  ASP D 116     9904  10827  14223    446   -389   -529       C  
ATOM   3627  OD1 ASP D 116     -21.621  24.137 -11.487  1.00 89.81           O  
ANISOU 3627  OD1 ASP D 116     9817  10371  13935    245   -567   -657       O  
ATOM   3628  OD2 ASP D 116     -21.848  23.628 -13.617  1.00 93.81           O  
ANISOU 3628  OD2 ASP D 116     9900  11110  14634    494   -406   -320       O  
ATOM   3629  N   TYR D 117     -23.303  20.402  -8.893  1.00 68.42           N  
ANISOU 3629  N   TYR D 117     7667   7983  10347    534    108  -1128       N  
ATOM   3630  CA  TYR D 117     -24.552  19.964  -8.273  1.00 76.92           C  
ANISOU 3630  CA  TYR D 117     8924   8981  11322    624    416  -1382       C  
ATOM   3631  C   TYR D 117     -25.218  21.088  -7.487  1.00 76.62           C  
ANISOU 3631  C   TYR D 117     9167   8692  11253    518    542  -1747       C  
ATOM   3632  O   TYR D 117     -26.443  21.241  -7.539  1.00 72.99           O  
ANISOU 3632  O   TYR D 117     8717   8057  10960    661    845  -1966       O  
ATOM   3633  CB  TYR D 117     -24.296  18.761  -7.363  1.00 71.45           C  
ANISOU 3633  CB  TYR D 117     8343   8497  10308    565    411  -1279       C  
ATOM   3634  CG  TYR D 117     -25.487  18.394  -6.504  1.00 74.99           C  
ANISOU 3634  CG  TYR D 117     9006   8900  10587    591    729  -1506       C  
ATOM   3635  CD1 TYR D 117     -26.580  17.723  -7.040  1.00 68.07           C  
ANISOU 3635  CD1 TYR D 117     7971   7973   9920    823    986  -1517       C  
ATOM   3636  CD2 TYR D 117     -25.531  18.755  -5.160  1.00 73.59           C  
ANISOU 3636  CD2 TYR D 117     9198   8730  10032    367    775  -1705       C  
ATOM   3637  CE1 TYR D 117     -27.675  17.396  -6.255  1.00 76.51           C  
ANISOU 3637  CE1 TYR D 117     9183   9009  10880    842   1302  -1675       C  
ATOM   3638  CE2 TYR D 117     -26.625  18.439  -4.367  1.00 80.85           C  
ANISOU 3638  CE2 TYR D 117    10302   9647  10769    387   1133  -1902       C  
ATOM   3639  CZ  TYR D 117     -27.694  17.763  -4.919  1.00 81.75           C  
ANISOU 3639  CZ  TYR D 117    10193   9717  11152    631   1407  -1867       C  
ATOM   3640  OH  TYR D 117     -28.778  17.449  -4.128  1.00 90.28           O  
ANISOU 3640  OH  TYR D 117    11406  10804  12092    646   1784  -2013       O  
ATOM   3641  N   GLU D 118     -24.430  21.875  -6.745  1.00 74.17           N  
ANISOU 3641  N   GLU D 118     9081   8338  10762    269    308  -1822       N  
ATOM   3642  CA  GLU D 118     -25.003  22.957  -5.945  1.00 81.24           C  
ANISOU 3642  CA  GLU D 118    10293   8967  11607    170    429  -2238       C  
ATOM   3643  C   GLU D 118     -25.790  23.933  -6.811  1.00 77.24           C  
ANISOU 3643  C   GLU D 118     9605   8138  11604    327    546  -2385       C  
ATOM   3644  O   GLU D 118     -26.884  24.372  -6.432  1.00 79.09           O  
ANISOU 3644  O   GLU D 118     9958   8137  11954    421    867  -2734       O  
ATOM   3645  CB  GLU D 118     -23.901  23.698  -5.189  1.00 82.71           C  
ANISOU 3645  CB  GLU D 118    10744   9121  11562   -144     52  -2268       C  
ATOM   3646  CG  GLU D 118     -24.425  24.747  -4.219  1.00 93.26           C  
ANISOU 3646  CG  GLU D 118    12495  10176  12763   -262    173  -2771       C  
ATOM   3647  CD  GLU D 118     -23.315  25.567  -3.587  1.00105.76           C  
ANISOU 3647  CD  GLU D 118    14353  11670  14163   -594   -286  -2802       C  
ATOM   3648  OE1 GLU D 118     -22.147  25.408  -4.005  1.00108.08           O  
ANISOU 3648  OE1 GLU D 118    14436  12103  14529   -722   -702  -2380       O  
ATOM   3649  OE2 GLU D 118     -23.612  26.375  -2.679  1.00101.88           O  
ANISOU 3649  OE2 GLU D 118    14282  10954  13474   -725   -229  -3252       O  
ATOM   3650  N   PHE D 119     -25.249  24.279  -7.980  1.00 75.29           N  
ANISOU 3650  N   PHE D 119     9049   7878  11680    351    296  -2096       N  
ATOM   3651  CA  PHE D 119     -25.904  25.238  -8.861  1.00 75.24           C  
ANISOU 3651  CA  PHE D 119     8849   7565  12174    450    318  -2149       C  
ATOM   3652  C   PHE D 119     -27.090  24.608  -9.580  1.00 77.68           C  
ANISOU 3652  C   PHE D 119     8949   7851  12713    704    610  -2121       C  
ATOM   3653  O   PHE D 119     -28.188  25.177  -9.611  1.00 74.05           O  
ANISOU 3653  O   PHE D 119     8462   7081  12594    810    815  -2346       O  
ATOM   3654  CB  PHE D 119     -24.889  25.774  -9.870  1.00 74.48           C  
ANISOU 3654  CB  PHE D 119     8497   7516  12287    347    -58  -1784       C  
ATOM   3655  CG  PHE D 119     -25.492  26.630 -10.944  1.00 76.07           C  
ANISOU 3655  CG  PHE D 119     8454   7455  12995    419    -98  -1714       C  
ATOM   3656  CD1 PHE D 119     -25.639  26.138 -12.230  1.00 71.53           C  
ANISOU 3656  CD1 PHE D 119     7583   7042  12553    540    -95  -1395       C  
ATOM   3657  CD2 PHE D 119     -25.902  27.928 -10.673  1.00 77.45           C  
ANISOU 3657  CD2 PHE D 119     8707   7204  13518    350   -166  -1964       C  
ATOM   3658  CE1 PHE D 119     -26.182  26.914 -13.225  1.00 71.81           C  
ANISOU 3658  CE1 PHE D 119     7406   6850  13027    558   -187  -1273       C  
ATOM   3659  CE2 PHE D 119     -26.450  28.717 -11.670  1.00 77.66           C  
ANISOU 3659  CE2 PHE D 119     8475   6961  14073    393   -256  -1841       C  
ATOM   3660  CZ  PHE D 119     -26.591  28.204 -12.949  1.00 74.79           C  
ANISOU 3660  CZ  PHE D 119     7818   6795  13806    481   -281  -1468       C  
ATOM   3661  N   LEU D 120     -26.878  23.429 -10.172  1.00 76.31           N  
ANISOU 3661  N   LEU D 120     8614   7976  12403    803    611  -1842       N  
ATOM   3662  CA  LEU D 120     -27.914  22.789 -10.975  1.00 78.32           C  
ANISOU 3662  CA  LEU D 120     8675   8202  12881   1014    795  -1773       C  
ATOM   3663  C   LEU D 120     -29.088  22.331 -10.129  1.00 68.48           C  
ANISOU 3663  C   LEU D 120     7550   6852  11616   1121   1156  -2028       C  
ATOM   3664  O   LEU D 120     -30.206  22.208 -10.642  1.00 73.68           O  
ANISOU 3664  O   LEU D 120     8047   7339  12609   1274   1315  -2033       O  
ATOM   3665  CB  LEU D 120     -27.325  21.601 -11.735  1.00 67.77           C  
ANISOU 3665  CB  LEU D 120     7188   7190  11370   1091    700  -1469       C  
ATOM   3666  CG  LEU D 120     -26.465  21.934 -12.949  1.00 71.86           C  
ANISOU 3666  CG  LEU D 120     7499   7829  11976   1052    450  -1177       C  
ATOM   3667  CD1 LEU D 120     -25.764  20.686 -13.440  1.00 65.93           C  
ANISOU 3667  CD1 LEU D 120     6648   7408  10996   1144    429   -964       C  
ATOM   3668  CD2 LEU D 120     -27.330  22.535 -14.045  1.00 71.77           C  
ANISOU 3668  CD2 LEU D 120     7326   7606  12337   1111    426  -1117       C  
ATOM   3669  N   LYS D 121     -28.858  22.073  -8.842  1.00 74.30           N  
ANISOU 3669  N   LYS D 121     8563   7700  11967   1022   1277  -2206       N  
ATOM   3670  CA  LYS D 121     -29.929  21.632  -7.956  1.00 83.13           C  
ANISOU 3670  CA  LYS D 121     9803   8774  13007   1099   1668  -2424       C  
ATOM   3671  C   LYS D 121     -31.095  22.617  -7.918  1.00 86.12           C  
ANISOU 3671  C   LYS D 121    10134   8768  13819   1202   1941  -2712       C  
ATOM   3672  O   LYS D 121     -32.189  22.248  -7.480  1.00 85.32           O  
ANISOU 3672  O   LYS D 121    10010   8598  13811   1322   2315  -2836       O  
ATOM   3673  CB  LYS D 121     -29.361  21.405  -6.551  1.00 86.16           C  
ANISOU 3673  CB  LYS D 121    10548   9355  12834    908   1713  -2565       C  
ATOM   3674  CG  LYS D 121     -30.223  20.569  -5.626  1.00 93.74           C  
ANISOU 3674  CG  LYS D 121    11631  10427  13560    946   2093  -2658       C  
ATOM   3675  CD  LYS D 121     -29.827  20.761  -4.160  1.00104.30           C  
ANISOU 3675  CD  LYS D 121    13405  11895  14328    712   2174  -2889       C  
ATOM   3676  CE  LYS D 121     -29.425  22.201  -3.818  1.00 97.28           C  
ANISOU 3676  CE  LYS D 121    12763  10774  13426    580   2076  -3227       C  
ATOM   3677  NZ  LYS D 121     -30.439  23.230  -4.206  1.00100.89           N  
ANISOU 3677  NZ  LYS D 121    13092  10832  14410    765   2348  -3528       N  
ATOM   3678  N   SER D 122     -30.897  23.847  -8.396  1.00 80.57           N  
ANISOU 3678  N   SER D 122     9372   7796  13445   1163   1758  -2786       N  
ATOM   3679  CA  SER D 122     -31.943  24.861  -8.420  1.00 85.50           C  
ANISOU 3679  CA  SER D 122     9903   7988  14595   1270   1973  -3047       C  
ATOM   3680  C   SER D 122     -32.526  25.095  -9.815  1.00 78.53           C  
ANISOU 3680  C   SER D 122     8631   6889  14318   1385   1811  -2779       C  
ATOM   3681  O   SER D 122     -33.304  26.037 -10.000  1.00 79.63           O  
ANISOU 3681  O   SER D 122     8623   6618  15013   1458   1892  -2921       O  
ATOM   3682  CB  SER D 122     -31.408  26.173  -7.834  1.00 88.32           C  
ANISOU 3682  CB  SER D 122    10493   8106  14958   1126   1863  -3360       C  
ATOM   3683  OG  SER D 122     -30.387  26.744  -8.635  1.00 89.69           O  
ANISOU 3683  OG  SER D 122    10567   8277  15235    987   1383  -3105       O  
ATOM   3684  N   TRP D 123     -32.170  24.264 -10.792  1.00 74.76           N  
ANISOU 3684  N   TRP D 123     7993   6663  13748   1394   1575  -2400       N  
ATOM   3685  CA  TRP D 123     -32.783  24.277 -12.112  1.00 71.02           C  
ANISOU 3685  CA  TRP D 123     7207   6044  13732   1474   1412  -2124       C  
ATOM   3686  C   TRP D 123     -34.115  23.519 -12.099  1.00 80.23           C  
ANISOU 3686  C   TRP D 123     8225   7103  15155   1646   1687  -2116       C  
ATOM   3687  O   TRP D 123     -34.367  22.663 -11.244  1.00 71.07           O  
ANISOU 3687  O   TRP D 123     7183   6107  13712   1701   1970  -2224       O  
ATOM   3688  CB  TRP D 123     -31.842  23.631 -13.129  1.00 73.72           C  
ANISOU 3688  CB  TRP D 123     7494   6725  13791   1413   1088  -1772       C  
ATOM   3689  CG  TRP D 123     -30.772  24.534 -13.644  1.00 74.02           C  
ANISOU 3689  CG  TRP D 123     7514   6797  13813   1250    765  -1630       C  
ATOM   3690  CD1 TRP D 123     -30.123  25.517 -12.950  1.00 70.79           C  
ANISOU 3690  CD1 TRP D 123     7241   6276  13379   1115    691  -1800       C  
ATOM   3691  CD2 TRP D 123     -30.165  24.491 -14.943  1.00 70.38           C  
ANISOU 3691  CD2 TRP D 123     6900   6517  13323   1185    470  -1271       C  
ATOM   3692  NE1 TRP D 123     -29.176  26.111 -13.751  1.00 71.80           N  
ANISOU 3692  NE1 TRP D 123     7263   6484  13535    968    346  -1524       N  
ATOM   3693  CE2 TRP D 123     -29.180  25.498 -14.977  1.00 68.57           C  
ANISOU 3693  CE2 TRP D 123     6672   6280  13100   1010    237  -1194       C  
ATOM   3694  CE3 TRP D 123     -30.373  23.712 -16.086  1.00 65.28           C  
ANISOU 3694  CE3 TRP D 123     6134   6038  12630   1247    379  -1014       C  
ATOM   3695  CZ2 TRP D 123     -28.399  25.743 -16.111  1.00 80.93           C  
ANISOU 3695  CZ2 TRP D 123     8087   8034  14630    897    -38   -831       C  
ATOM   3696  CZ3 TRP D 123     -29.593  23.954 -17.212  1.00 84.47           C  
ANISOU 3696  CZ3 TRP D 123     8467   8664  14964   1138    122   -707       C  
ATOM   3697  CH2 TRP D 123     -28.619  24.960 -17.215  1.00 79.26           C  
ANISOU 3697  CH2 TRP D 123     7774   8026  14314    966    -63   -600       C  
ATOM   3698  N   THR D 124     -34.970  23.836 -13.070  1.00 71.18           N  
ANISOU 3698  N   THR D 124     6800   5676  14571   1704   1566  -1936       N  
ATOM   3699  CA  THR D 124     -36.199  23.074 -13.256  1.00 73.36           C  
ANISOU 3699  CA  THR D 124     6949   5950  14972   1753   1668  -1768       C  
ATOM   3700  C   THR D 124     -35.897  21.702 -13.844  1.00 72.94           C  
ANISOU 3700  C   THR D 124     6903   6180  14632   1797   1522  -1547       C  
ATOM   3701  O   THR D 124     -34.900  21.508 -14.545  1.00 67.86           O  
ANISOU 3701  O   THR D 124     6300   5728  13757   1763   1261  -1424       O  
ATOM   3702  CB  THR D 124     -37.177  23.832 -14.162  1.00 77.20           C  
ANISOU 3702  CB  THR D 124     7188   6143  16001   1678   1463  -1550       C  
ATOM   3703  OG1 THR D 124     -36.873  23.583 -15.543  1.00 74.66           O  
ANISOU 3703  OG1 THR D 124     6756   5859  15751   1633   1060  -1233       O  
ATOM   3704  CG2 THR D 124     -37.119  25.313 -13.885  1.00 75.92           C  
ANISOU 3704  CG2 THR D 124     6988   5680  16178   1630   1472  -1734       C  
ATOM   3705  N   VAL D 125     -36.765  20.734 -13.532  1.00 60.79           N  
ANISOU 3705  N   VAL D 125     5839   6046  11211    286     21    274       N  
ATOM   3706  CA  VAL D 125     -36.597  19.390 -14.077  1.00 68.78           C  
ANISOU 3706  CA  VAL D 125     6685   7291  12157    210   -241    -13       C  
ATOM   3707  C   VAL D 125     -36.613  19.430 -15.600  1.00 64.88           C  
ANISOU 3707  C   VAL D 125     6131   7241  11278    777   -498     -9       C  
ATOM   3708  O   VAL D 125     -35.826  18.742 -16.265  1.00 59.62           O  
ANISOU 3708  O   VAL D 125     5531   6685  10437    775   -612    -13       O  
ATOM   3709  CB  VAL D 125     -37.677  18.448 -13.517  1.00 65.84           C  
ANISOU 3709  CB  VAL D 125     5956   6933  12127    -65   -280   -516       C  
ATOM   3710  CG1 VAL D 125     -37.870  17.257 -14.436  1.00 69.51           C  
ANISOU 3710  CG1 VAL D 125     6116   7726  12568    -25   -494   -973       C  
ATOM   3711  CG2 VAL D 125     -37.283  17.980 -12.136  1.00 69.95           C  
ANISOU 3711  CG2 VAL D 125     6679   7009  12889   -540     27   -450       C  
ATOM   3712  N   GLU D 126     -37.490  20.256 -16.172  1.00 63.74           N  
ANISOU 3712  N   GLU D 126     5887   7396  10936   1361   -578     18       N  
ATOM   3713  CA  GLU D 126     -37.545  20.401 -17.622  1.00 64.09           C  
ANISOU 3713  CA  GLU D 126     5922   7964  10464   2126   -805     61       C  
ATOM   3714  C   GLU D 126     -36.196  20.848 -18.179  1.00 63.72           C  
ANISOU 3714  C   GLU D 126     6409   7636  10165   2268   -523    609       C  
ATOM   3715  O   GLU D 126     -35.630  20.188 -19.057  1.00 66.59           O  
ANISOU 3715  O   GLU D 126     6784   8243  10275   2410   -712    554       O  
ATOM   3716  CB  GLU D 126     -38.652  21.386 -18.018  1.00 69.96           C  
ANISOU 3716  CB  GLU D 126     6570   9084  10928   2915   -850    106       C  
ATOM   3717  CG  GLU D 126     -40.085  21.074 -17.506  1.00 86.31           C  
ANISOU 3717  CG  GLU D 126     8028  11492  13271   2821  -1110   -539       C  
ATOM   3718  CD  GLU D 126     -40.228  21.058 -15.982  1.00 87.85           C  
ANISOU 3718  CD  GLU D 126     8240  11054  14085   1990   -825   -561       C  
ATOM   3719  OE1 GLU D 126     -40.795  20.081 -15.444  1.00 91.68           O  
ANISOU 3719  OE1 GLU D 126     8310  11549  14977   1477   -914  -1151       O  
ATOM   3720  OE2 GLU D 126     -39.766  22.015 -15.322  1.00 90.49           O  
ANISOU 3720  OE2 GLU D 126     9007  10864  14511   1862   -435    -27       O  
ATOM   3721  N   ASP D 127     -35.655  21.959 -17.660  1.00 66.62           N  
ANISOU 3721  N   ASP D 127     7190   7460  10661   2179      0   1066       N  
ATOM   3722  CA  ASP D 127     -34.350  22.443 -18.113  1.00 67.41           C  
ANISOU 3722  CA  ASP D 127     7755   7197  10661   2212    433   1463       C  
ATOM   3723  C   ASP D 127     -33.240  21.439 -17.834  1.00 54.85           C  
ANISOU 3723  C   ASP D 127     6102   5508   9230   1571    301   1272       C  
ATOM   3724  O   ASP D 127     -32.275  21.357 -18.601  1.00 57.48           O  
ANISOU 3724  O   ASP D 127     6671   5790   9381   1688    428   1435       O  
ATOM   3725  CB  ASP D 127     -34.003  23.769 -17.440  1.00 67.29           C  
ANISOU 3725  CB  ASP D 127     8073   6566  10929   2062   1141   1771       C  
ATOM   3726  CG  ASP D 127     -34.455  24.973 -18.239  1.00 73.90           C  
ANISOU 3726  CG  ASP D 127     9310   7305  11462   2941   1620   2237       C  
ATOM   3727  OD1 ASP D 127     -35.339  24.827 -19.112  1.00 80.59           O  
ANISOU 3727  OD1 ASP D 127    10079   8722  11820   3757   1255   2272       O  
ATOM   3728  OD2 ASP D 127     -33.912  26.071 -17.989  1.00 78.30           O  
ANISOU 3728  OD2 ASP D 127    10255   7232  12263   2862   2427   2521       O  
ATOM   3729  N   LEU D 128     -33.335  20.696 -16.730  1.00 55.26           N  
ANISOU 3729  N   LEU D 128     5890   5514   9594    963    115    960       N  
ATOM   3730  CA  LEU D 128     -32.330  19.675 -16.474  1.00 55.04           C  
ANISOU 3730  CA  LEU D 128     5836   5461   9615    527      2    813       C  
ATOM   3731  C   LEU D 128     -32.345  18.616 -17.566  1.00 52.42           C  
ANISOU 3731  C   LEU D 128     5388   5498   9031    748   -362    669       C  
ATOM   3732  O   LEU D 128     -31.286  18.227 -18.072  1.00 49.51           O  
ANISOU 3732  O   LEU D 128     5169   5117   8528    701   -351    750       O  
ATOM   3733  CB  LEU D 128     -32.535  19.052 -15.096  1.00 53.48           C  
ANISOU 3733  CB  LEU D 128     5470   5157   9693     42    -40    575       C  
ATOM   3734  CG  LEU D 128     -32.078  19.989 -13.977  1.00 49.14           C  
ANISOU 3734  CG  LEU D 128     5015   4321   9335   -227    307    635       C  
ATOM   3735  CD1 LEU D 128     -32.520  19.493 -12.619  1.00 60.59           C  
ANISOU 3735  CD1 LEU D 128     6341   5722  10960   -518    280    449       C  
ATOM   3736  CD2 LEU D 128     -30.569  20.186 -14.036  1.00 50.94           C  
ANISOU 3736  CD2 LEU D 128     5368   4483   9506   -380    511    637       C  
ATOM   3737  N   GLN D 129     -33.537  18.179 -17.985  1.00 51.76           N  
ANISOU 3737  N   GLN D 129     4984   5788   8893    999   -669    372       N  
ATOM   3738  CA  GLN D 129     -33.609  17.167 -19.037  1.00 52.48           C  
ANISOU 3738  CA  GLN D 129     4859   6305   8775   1190   -999     74       C  
ATOM   3739  C   GLN D 129     -33.179  17.733 -20.385  1.00 54.03           C  
ANISOU 3739  C   GLN D 129     5296   6754   8480   1854  -1030    372       C  
ATOM   3740  O   GLN D 129     -32.546  17.026 -21.180  1.00 57.55           O  
ANISOU 3740  O   GLN D 129     5763   7373   8732   1906  -1175    313       O  
ATOM   3741  CB  GLN D 129     -35.016  16.589 -19.150  1.00 55.44           C  
ANISOU 3741  CB  GLN D 129     4693   7103   9267   1275  -1274   -536       C  
ATOM   3742  CG  GLN D 129     -35.316  15.470 -18.178  1.00 66.95           C  
ANISOU 3742  CG  GLN D 129     5922   8296  11221    614  -1148   -952       C  
ATOM   3743  CD  GLN D 129     -34.707  14.149 -18.615  1.00 75.70           C  
ANISOU 3743  CD  GLN D 129     6974   9420  12368    366  -1162  -1197       C  
ATOM   3744  OE1 GLN D 129     -34.363  13.310 -17.782  1.00 74.78           O  
ANISOU 3744  OE1 GLN D 129     6977   8887  12550   -102   -870  -1224       O  
ATOM   3745  NE2 GLN D 129     -34.474  14.002 -19.918  1.00 77.28           N  
ANISOU 3745  NE2 GLN D 129     7076  10082  12206    759  -1445  -1299       N  
ATOM   3746  N   LYS D 130     -33.543  18.991 -20.671  1.00 57.21           N  
ANISOU 3746  N   LYS D 130     5926   7155   8656   2430   -826    716       N  
ATOM   3747  CA  LYS D 130     -33.044  19.667 -21.866  1.00 60.88           C  
ANISOU 3747  CA  LYS D 130     6802   7700   8629   3165   -629   1144       C  
ATOM   3748  C   LYS D 130     -31.526  19.583 -21.947  1.00 57.93           C  
ANISOU 3748  C   LYS D 130     6797   6855   8359   2778   -295   1413       C  
ATOM   3749  O   LYS D 130     -30.968  19.210 -22.985  1.00 66.49           O  
ANISOU 3749  O   LYS D 130     8019   8131   9112   3093   -372   1488       O  
ATOM   3750  CB  LYS D 130     -33.492  21.131 -21.881  1.00 64.82           C  
ANISOU 3750  CB  LYS D 130     7654   8000   8974   3776   -175   1596       C  
ATOM   3751  CG  LYS D 130     -34.970  21.338 -21.659  1.00 70.25           C  
ANISOU 3751  CG  LYS D 130     7964   9146   9583   4160   -475   1326       C  
ATOM   3752  CD  LYS D 130     -35.447  22.712 -22.111  1.00 73.84           C  
ANISOU 3752  CD  LYS D 130     8835   9583   9636   5140    -49   1841       C  
ATOM   3753  CE  LYS D 130     -36.894  22.935 -21.678  1.00 76.61           C  
ANISOU 3753  CE  LYS D 130     8752  10371   9986   5418   -352   1519       C  
ATOM   3754  NZ  LYS D 130     -37.292  24.373 -21.692  1.00 81.13           N  
ANISOU 3754  NZ  LYS D 130     9824  10670  10332   5857    216   1987       N  
ATOM   3755  N   ARG D 131     -30.840  19.925 -20.851  1.00 56.84           N  
ANISOU 3755  N   ARG D 131     6767   6163   8666   2116     66   1480       N  
ATOM   3756  CA  ARG D 131     -29.384  19.840 -20.836  1.00 61.60           C  
ANISOU 3756  CA  ARG D 131     7588   6414   9403   1722    367   1563       C  
ATOM   3757  C   ARG D 131     -28.911  18.413 -21.063  1.00 63.86           C  
ANISOU 3757  C   ARG D 131     7656   6984   9625   1443    -90   1293       C  
ATOM   3758  O   ARG D 131     -27.885  18.194 -21.716  1.00 59.94           O  
ANISOU 3758  O   ARG D 131     7345   6419   9011   1449     20   1387       O  
ATOM   3759  CB  ARG D 131     -28.836  20.388 -19.517  1.00 64.64           C  
ANISOU 3759  CB  ARG D 131     7950   6366  10246   1098    741   1466       C  
ATOM   3760  CG  ARG D 131     -27.310  20.455 -19.439  1.00 69.58           C  
ANISOU 3760  CG  ARG D 131     8682   6715  11041    710   1098   1380       C  
ATOM   3761  CD  ARG D 131     -26.675  20.985 -20.724  1.00 69.75           C  
ANISOU 3761  CD  ARG D 131     9112   6509  10882   1127   1561   1682       C  
ATOM   3762  NE  ARG D 131     -26.508  22.434 -20.708  1.00 82.29           N  
ANISOU 3762  NE  ARG D 131    11029   7526  12712   1234   2446   1875       N  
ATOM   3763  CZ  ARG D 131     -25.654  23.085 -19.929  1.00 88.40           C  
ANISOU 3763  CZ  ARG D 131    11722   7893  13975    664   3028   1567       C  
ATOM   3764  NH1 ARG D 131     -24.818  22.441 -19.128  1.00 89.66           N  
ANISOU 3764  NH1 ARG D 131    11479   8260  14327     56   2745   1066       N  
ATOM   3765  NH2 ARG D 131     -25.629  24.414 -19.964  1.00 92.76           N  
ANISOU 3765  NH2 ARG D 131    12585   7846  14815    761   3971   1708       N  
ATOM   3766  N   LEU D 132     -29.659  17.431 -20.554  1.00 61.06           N  
ANISOU 3766  N   LEU D 132     6930   6891   9378   1204   -506    947       N  
ATOM   3767  CA  LEU D 132     -29.274  16.035 -20.727  1.00 59.26           C  
ANISOU 3767  CA  LEU D 132     6532   6839   9146    942   -791    687       C  
ATOM   3768  C   LEU D 132     -29.436  15.594 -22.176  1.00 67.54           C  
ANISOU 3768  C   LEU D 132     7527   8309   9824   1416  -1055    608       C  
ATOM   3769  O   LEU D 132     -28.611  14.834 -22.697  1.00 60.96           O  
ANISOU 3769  O   LEU D 132     6748   7514   8899   1311  -1126    579       O  
ATOM   3770  CB  LEU D 132     -30.113  15.153 -19.807  1.00 50.83           C  
ANISOU 3770  CB  LEU D 132     5143   5805   8364    588   -937    323       C  
ATOM   3771  CG  LEU D 132     -29.435  13.962 -19.154  1.00 57.29           C  
ANISOU 3771  CG  LEU D 132     5968   6464   9336    162   -887    203       C  
ATOM   3772  CD1 LEU D 132     -28.105  14.368 -18.580  1.00 48.47           C  
ANISOU 3772  CD1 LEU D 132     5104   5134   8181      6   -690    452       C  
ATOM   3773  CD2 LEU D 132     -30.361  13.403 -18.079  1.00 66.29           C  
ANISOU 3773  CD2 LEU D 132     6930   7463  10793   -104   -784    -51       C  
ATOM   3774  N   LEU D 133     -30.496  16.059 -22.839  1.00 64.66           N  
ANISOU 3774  N   LEU D 133     7033   8341   9196   2009  -1220    538       N  
ATOM   3775  CA  LEU D 133     -30.725  15.741 -24.242  1.00 66.76           C  
ANISOU 3775  CA  LEU D 133     7201   9181   8983   2638  -1512    395       C  
ATOM   3776  C   LEU D 133     -29.818  16.524 -25.181  1.00 79.10           C  
ANISOU 3776  C   LEU D 133     9311  10599  10143   3174  -1206    948       C  
ATOM   3777  O   LEU D 133     -29.782  16.218 -26.377  1.00 78.55           O  
ANISOU 3777  O   LEU D 133     9250  10989   9607   3739  -1412    897       O  
ATOM   3778  CB  LEU D 133     -32.188  15.993 -24.608  1.00 67.54           C  
ANISOU 3778  CB  LEU D 133     6907   9919   8836   3246  -1822     37       C  
ATOM   3779  CG  LEU D 133     -33.063  14.742 -24.687  1.00 78.14           C  
ANISOU 3779  CG  LEU D 133     7538  11790  10363   2997  -2235   -837       C  
ATOM   3780  CD1 LEU D 133     -32.831  14.025 -26.005  1.00 83.47           C  
ANISOU 3780  CD1 LEU D 133     8030  13061  10622   3392  -2540  -1157       C  
ATOM   3781  CD2 LEU D 133     -32.771  13.810 -23.518  1.00 78.67           C  
ANISOU 3781  CD2 LEU D 133     7512  11289  11089   2004  -2037  -1028       C  
ATOM   3782  N   ALA D 134     -29.105  17.530 -24.677  1.00 74.85           N  
ANISOU 3782  N   ALA D 134     9214   9432   9796   3022   -648   1410       N  
ATOM   3783  CA  ALA D 134     -28.066  18.184 -25.460  1.00 71.04           C  
ANISOU 3783  CA  ALA D 134     9275   8609   9108   3348   -142   1868       C  
ATOM   3784  C   ALA D 134     -26.734  17.459 -25.336  1.00 73.47           C  
ANISOU 3784  C   ALA D 134     9605   8644   9666   2695    -89   1775       C  
ATOM   3785  O   ALA D 134     -25.968  17.388 -26.303  1.00 77.10           O  
ANISOU 3785  O   ALA D 134    10348   9066   9880   2963     75   1958       O  
ATOM   3786  CB  ALA D 134     -27.909  19.638 -25.013  1.00 71.23           C  
ANISOU 3786  CB  ALA D 134     9720   8018   9326   3443    612   2274       C  
ATOM   3787  N   LEU D 135     -26.465  16.907 -24.155  1.00 71.21           N  
ANISOU 3787  N   LEU D 135     9035   8208   9814   1928   -217   1495       N  
ATOM   3788  CA  LEU D 135     -25.180  16.283 -23.870  1.00 58.45           C  
ANISOU 3788  CA  LEU D 135     7415   6398   8395   1392   -158   1385       C  
ATOM   3789  C   LEU D 135     -25.019  14.967 -24.624  1.00 74.08           C  
ANISOU 3789  C   LEU D 135     9250   8737  10158   1421   -586   1211       C  
ATOM   3790  O   LEU D 135     -23.961  14.699 -25.206  1.00 69.67           O  
ANISOU 3790  O   LEU D 135     8861   8088   9523   1376   -474   1285       O  
ATOM   3791  CB  LEU D 135     -25.058  16.084 -22.356  1.00 61.08           C  
ANISOU 3791  CB  LEU D 135     7506   6598   9104    793   -181   1150       C  
ATOM   3792  CG  LEU D 135     -23.769  15.749 -21.616  1.00 64.43           C  
ANISOU 3792  CG  LEU D 135     7864   6899   9717    322    -66    968       C  
ATOM   3793  CD1 LEU D 135     -24.062  15.786 -20.140  1.00 59.52           C  
ANISOU 3793  CD1 LEU D 135     7029   6276   9310     18    -97    775       C  
ATOM   3794  CD2 LEU D 135     -23.301  14.361 -21.972  1.00 69.81           C  
ANISOU 3794  CD2 LEU D 135     8468   7812  10245    251   -399    864       C  
ATOM   3795  N   ASP D 136     -26.058  14.134 -24.622  1.00 65.66           N  
ANISOU 3795  N   ASP D 136     7841   8056   9050   1455  -1013    908       N  
ATOM   3796  CA  ASP D 136     -25.932  12.801 -25.207  1.00 75.69           C  
ANISOU 3796  CA  ASP D 136     8911   9612  10237   1362  -1318    619       C  
ATOM   3797  C   ASP D 136     -25.588  12.838 -26.694  1.00 82.01           C  
ANISOU 3797  C   ASP D 136     9884  10679  10598   1890  -1387    737       C  
ATOM   3798  O   ASP D 136     -24.687  12.089 -27.110  1.00 84.41           O  
ANISOU 3798  O   ASP D 136    10250  10944  10877   1704  -1407    715       O  
ATOM   3799  CB  ASP D 136     -27.212  12.005 -24.923  1.00 81.40           C  
ANISOU 3799  CB  ASP D 136     9172  10642  11114   1257  -1594    121       C  
ATOM   3800  CG  ASP D 136     -27.476  11.840 -23.432  1.00 87.33           C  
ANISOU 3800  CG  ASP D 136     9842  11054  12286    761  -1430     53       C  
ATOM   3801  OD1 ASP D 136     -26.622  12.263 -22.622  1.00 81.66           O  
ANISOU 3801  OD1 ASP D 136     9372   9986  11671    536  -1201    344       O  
ATOM   3802  OD2 ASP D 136     -28.542  11.299 -23.066  1.00 94.88           O1-
ANISOU 3802  OD2 ASP D 136    10460  12123  13468    623  -1496   -356       O1-
ATOM   3803  N   PRO D 137     -26.230  13.663 -27.538  1.00 81.69           N  
ANISOU 3803  N   PRO D 137     9961  10931  10145   2633  -1398    888       N  
ATOM   3804  CA  PRO D 137     -25.794  13.742 -28.947  1.00 79.51           C  
ANISOU 3804  CA  PRO D 137     9957  10899   9356   3269  -1383   1079       C  
ATOM   3805  C   PRO D 137     -24.322  14.072 -29.130  1.00 77.89           C  
ANISOU 3805  C   PRO D 137    10236  10120   9240   3074   -898   1488       C  
ATOM   3806  O   PRO D 137     -23.638  13.423 -29.931  1.00 81.20           O  
ANISOU 3806  O   PRO D 137    10725  10645   9483   3113   -979   1461       O  
ATOM   3807  CB  PRO D 137     -26.689  14.851 -29.510  1.00 85.55           C  
ANISOU 3807  CB  PRO D 137    10906  11962   9638   4224  -1298   1320       C  
ATOM   3808  CG  PRO D 137     -27.949  14.698 -28.757  1.00 84.71           C  
ANISOU 3808  CG  PRO D 137    10283  12177   9725   4080  -1641    887       C  
ATOM   3809  CD  PRO D 137     -27.533  14.330 -27.349  1.00 80.98           C  
ANISOU 3809  CD  PRO D 137     9698  11124   9945   3053  -1505    805       C  
ATOM   3810  N   MET D 138     -23.815  15.073 -28.407  1.00 69.09           N  
ANISOU 3810  N   MET D 138     9407   8408   8437   2838   -355   1776       N  
ATOM   3811  CA  MET D 138     -22.422  15.475 -28.577  1.00 71.12           C  
ANISOU 3811  CA  MET D 138    10033   8121   8868   2615    212   1997       C  
ATOM   3812  C   MET D 138     -21.458  14.368 -28.161  1.00 71.15           C  
ANISOU 3812  C   MET D 138     9778   8114   9140   1923    -26   1695       C  
ATOM   3813  O   MET D 138     -20.401  14.192 -28.779  1.00 69.10           O  
ANISOU 3813  O   MET D 138     9715   7687   8851   1876    190   1760       O  
ATOM   3814  CB  MET D 138     -22.149  16.749 -27.787  1.00 71.62           C  
ANISOU 3814  CB  MET D 138    10307   7586   9319   2409    898   2149       C  
ATOM   3815  CG  MET D 138     -21.231  17.684 -28.520  1.00 82.45           C  
ANISOU 3815  CG  MET D 138    12230   8382  10714   2662   1774   2468       C  
ATOM   3816  SD  MET D 138     -21.633  19.410 -28.263  1.00109.13           S  
ANISOU 3816  SD  MET D 138    16054  11136  14276   3008   2745   2814       S  
ATOM   3817  CE  MET D 138     -20.531  20.138 -29.467  1.00 89.74           C  
ANISOU 3817  CE  MET D 138    14114   8284  11700   3212   3717   2952       C  
ATOM   3818  N   MET D 139     -21.794  13.618 -27.114  1.00 63.13           N  
ANISOU 3818  N   MET D 139     8365   7255   8365   1447   -401   1389       N  
ATOM   3819  CA  MET D 139     -20.953  12.489 -26.735  1.00 66.31           C  
ANISOU 3819  CA  MET D 139     8587   7694   8914    976   -589   1165       C  
ATOM   3820  C   MET D 139     -20.975  11.409 -27.807  1.00 74.56           C  
ANISOU 3820  C   MET D 139     9587   9055   9688   1156   -908   1082       C  
ATOM   3821  O   MET D 139     -19.922  10.909 -28.221  1.00 73.64           O  
ANISOU 3821  O   MET D 139     9565   8865   9548   1024   -849   1091       O  
ATOM   3822  CB  MET D 139     -21.400  11.910 -25.398  1.00 65.13           C  
ANISOU 3822  CB  MET D 139     8138   7604   9003    600   -791    937       C  
ATOM   3823  CG  MET D 139     -20.472  10.814 -24.915  1.00 57.81           C  
ANISOU 3823  CG  MET D 139     7122   6701   8145    286   -869    789       C  
ATOM   3824  SD  MET D 139     -21.255   9.718 -23.730  1.00 62.55           S  
ANISOU 3824  SD  MET D 139     7511   7372   8885     91  -1019    606       S  
ATOM   3825  CE  MET D 139     -22.244   8.711 -24.833  1.00 60.88           C  
ANISOU 3825  CE  MET D 139     7155   7363   8614    200  -1232    406       C  
ATOM   3826  N   GLU D 140     -22.173  11.029 -28.263  1.00 75.18           N  
ANISOU 3826  N   GLU D 140     9456   9532   9576   1448  -1241    905       N  
ATOM   3827  CA  GLU D 140     -22.274  10.019 -29.311  1.00 79.75           C  
ANISOU 3827  CA  GLU D 140     9891  10495   9914   1615  -1531    671       C  
ATOM   3828  C   GLU D 140     -21.589  10.477 -30.587  1.00 76.41           C  
ANISOU 3828  C   GLU D 140     9835  10101   9098   2104  -1386    963       C  
ATOM   3829  O   GLU D 140     -21.123   9.649 -31.377  1.00 80.61           O  
ANISOU 3829  O   GLU D 140    10342  10807   9478   2116  -1524    842       O  
ATOM   3830  CB  GLU D 140     -23.738   9.681 -29.582  1.00 76.78           C  
ANISOU 3830  CB  GLU D 140     9097  10653   9422   1875  -1881    234       C  
ATOM   3831  CG  GLU D 140     -23.930   8.293 -30.158  1.00 86.88           C  
ANISOU 3831  CG  GLU D 140    10007  12281  10722   1715  -2124   -300       C  
ATOM   3832  CD  GLU D 140     -23.074   7.257 -29.452  1.00 87.21           C  
ANISOU 3832  CD  GLU D 140    10093  11888  11156   1064  -1926   -307       C  
ATOM   3833  OE1 GLU D 140     -22.427   6.447 -30.151  1.00 86.29           O  
ANISOU 3833  OE1 GLU D 140     9995  11827  10964    998  -1945   -398       O  
ATOM   3834  OE2 GLU D 140     -23.031   7.271 -28.200  1.00 79.14           O1-
ANISOU 3834  OE2 GLU D 140     9114  10496  10460    702  -1733   -199       O1-
ATOM   3835  N   GLN D 141     -21.517  11.789 -30.802  1.00 78.70           N  
ANISOU 3835  N   GLN D 141    10509  10160   9232   2528  -1009   1361       N  
ATOM   3836  CA  GLN D 141     -20.742  12.309 -31.919  1.00 74.95           C  
ANISOU 3836  CA  GLN D 141    10518   9524   8438   3003   -640   1720       C  
ATOM   3837  C   GLN D 141     -19.268  11.964 -31.765  1.00 75.07           C  
ANISOU 3837  C   GLN D 141    10652   9097   8775   2431   -365   1738       C  
ATOM   3838  O   GLN D 141     -18.659  11.394 -32.675  1.00 75.25           O  
ANISOU 3838  O   GLN D 141    10788   9212   8591   2547   -409   1751       O  
ATOM   3839  CB  GLN D 141     -20.945  13.819 -32.034  1.00 76.47           C  
ANISOU 3839  CB  GLN D 141    11178   9377   8500   3552    -50   2168       C  
ATOM   3840  CG  GLN D 141     -20.176  14.464 -33.168  1.00 85.08           C  
ANISOU 3840  CG  GLN D 141    12881  10156   9291   4092    573   2581       C  
ATOM   3841  CD  GLN D 141     -20.846  15.723 -33.683  1.00 90.98           C  
ANISOU 3841  CD  GLN D 141    13960  10916   9694   4732   1078   2799       C  
ATOM   3842  OE1 GLN D 141     -20.585  16.824 -33.194  1.00 91.60           O  
ANISOU 3842  OE1 GLN D 141    14328  10394  10080   4612   1804   3012       O  
ATOM   3843  NE2 GLN D 141     -21.696  15.570 -34.695  1.00 95.04           N  
ANISOU 3843  NE2 GLN D 141    14417  12138   9554   5434    764   2683       N  
ATOM   3844  N   GLU D 142     -18.680  12.284 -30.606  1.00 71.13           N  
ANISOU 3844  N   GLU D 142    10072   8195   8760   1840   -106   1666       N  
ATOM   3845  CA  GLU D 142     -17.244  12.081 -30.429  1.00 70.89           C  
ANISOU 3845  CA  GLU D 142    10073   7852   9011   1377    167   1567       C  
ATOM   3846  C   GLU D 142     -16.884  10.601 -30.443  1.00 59.97           C  
ANISOU 3846  C   GLU D 142     8421   6773   7594   1094   -312   1333       C  
ATOM   3847  O   GLU D 142     -15.757  10.242 -30.804  1.00 57.00           O  
ANISOU 3847  O   GLU D 142     8117   6276   7266    926   -175   1293       O  
ATOM   3848  CB  GLU D 142     -16.765  12.718 -29.123  1.00 57.43           C  
ANISOU 3848  CB  GLU D 142     8198   5855   7769    885    472   1365       C  
ATOM   3849  CG  GLU D 142     -16.797  14.233 -29.103  1.00 61.64           C  
ANISOU 3849  CG  GLU D 142     9020   5911   8490   1028   1192   1525       C  
ATOM   3850  CD  GLU D 142     -16.022  14.821 -27.932  1.00 55.35           C  
ANISOU 3850  CD  GLU D 142     7957   4859   8214    454   1574   1119       C  
ATOM   3851  OE1 GLU D 142     -15.151  14.121 -27.367  1.00 62.68           O  
ANISOU 3851  OE1 GLU D 142     8538   6000   9278     55   1340    732       O  
ATOM   3852  OE2 GLU D 142     -16.321  15.966 -27.540  1.00 62.16           O1-
ANISOU 3852  OE2 GLU D 142     8919   5377   9321    451   2099   1137       O1-
ATOM   3853  N   ILE D 143     -17.819   9.733 -30.049  1.00 70.41           N  
ANISOU 3853  N   ILE D 143     9440   8434   8877   1031   -776   1151       N  
ATOM   3854  CA  ILE D 143     -17.565   8.297 -30.083  1.00 65.26           C  
ANISOU 3854  CA  ILE D 143     8592   7968   8236    792  -1060    939       C  
ATOM   3855  C   ILE D 143     -17.553   7.785 -31.517  1.00 71.55           C  
ANISOU 3855  C   ILE D 143     9473   8999   8713   1099  -1199    930       C  
ATOM   3856  O   ILE D 143     -16.704   6.967 -31.890  1.00 65.42           O  
ANISOU 3856  O   ILE D 143     8719   8199   7939    932  -1209    880       O  
ATOM   3857  CB  ILE D 143     -18.600   7.548 -29.226  1.00 63.46           C  
ANISOU 3857  CB  ILE D 143     8054   7896   8162    608  -1291    696       C  
ATOM   3858  CG1 ILE D 143     -18.378   7.837 -27.742  1.00 57.98           C  
ANISOU 3858  CG1 ILE D 143     7309   7002   7719    337  -1152    713       C  
ATOM   3859  CG2 ILE D 143     -18.570   6.056 -29.521  1.00 65.51           C  
ANISOU 3859  CG2 ILE D 143     8162   8280   8449    444  -1417    456       C  
ATOM   3860  CD1 ILE D 143     -19.523   7.386 -26.870  1.00 59.63           C  
ANISOU 3860  CD1 ILE D 143     7312   7260   8086    232  -1239    549       C  
ATOM   3861  N   GLU D 144     -18.487   8.253 -32.346  1.00 80.10           N  
ANISOU 3861  N   GLU D 144    10591  10381   9464   1627  -1319    955       N  
ATOM   3862  CA  GLU D 144     -18.548   7.762 -33.720  1.00 86.58           C  
ANISOU 3862  CA  GLU D 144    11437  11580   9879   2038  -1504    865       C  
ATOM   3863  C   GLU D 144     -17.328   8.191 -34.530  1.00 81.09           C  
ANISOU 3863  C   GLU D 144    11205  10580   9026   2221  -1143   1224       C  
ATOM   3864  O   GLU D 144     -16.956   7.509 -35.491  1.00 85.98           O  
ANISOU 3864  O   GLU D 144    11856  11401   9412   2358  -1260   1147       O  
ATOM   3865  CB  GLU D 144     -19.841   8.229 -34.388  1.00 95.14           C  
ANISOU 3865  CB  GLU D 144    12409  13221  10518   2745  -1748    747       C  
ATOM   3866  CG  GLU D 144     -20.381   7.271 -35.444  1.00102.18           C  
ANISOU 3866  CG  GLU D 144    12947  14810  11066   3043  -2164    249       C  
ATOM   3867  CD  GLU D 144     -20.879   5.960 -34.850  1.00104.73           C  
ANISOU 3867  CD  GLU D 144    12691  15263  11839   2386  -2380   -393       C  
ATOM   3868  OE1 GLU D 144     -21.179   5.924 -33.637  1.00103.49           O  
ANISOU 3868  OE1 GLU D 144    12407  14783  12130   1912  -2274   -427       O  
ATOM   3869  OE2 GLU D 144     -20.986   4.967 -35.602  1.00107.33           O1-
ANISOU 3869  OE2 GLU D 144    12709  15987  12086   2364  -2572   -884       O1-
ATOM   3870  N   GLU D 145     -16.693   9.308 -34.162  1.00 76.79           N  
ANISOU 3870  N   GLU D 145    11001   9521   8656   2190   -630   1548       N  
ATOM   3871  CA  GLU D 145     -15.420   9.671 -34.779  1.00 64.96           C  
ANISOU 3871  CA  GLU D 145     9898   7601   7184   2201   -128   1776       C  
ATOM   3872  C   GLU D 145     -14.339   8.646 -34.458  1.00 69.81           C  
ANISOU 3872  C   GLU D 145    10297   8138   8091   1590   -244   1537       C  
ATOM   3873  O   GLU D 145     -13.534   8.289 -35.330  1.00 63.86           O  
ANISOU 3873  O   GLU D 145     9727   7316   7219   1650   -125   1592       O  
ATOM   3874  CB  GLU D 145     -14.997  11.068 -34.324  1.00 68.61           C  
ANISOU 3874  CB  GLU D 145    10668   7467   7934   2168    591   1992       C  
ATOM   3875  CG  GLU D 145     -16.157  12.048 -34.240  1.00 74.19           C  
ANISOU 3875  CG  GLU D 145    11534   8218   8436   2698    711   2223       C  
ATOM   3876  CD  GLU D 145     -15.747  13.442 -33.798  1.00 79.29           C  
ANISOU 3876  CD  GLU D 145    12508   8175   9442   2632   1578   2408       C  
ATOM   3877  OE1 GLU D 145     -16.382  14.420 -34.250  1.00 78.17           O  
ANISOU 3877  OE1 GLU D 145    12777   7899   9024   3302   2002   2772       O  
ATOM   3878  OE2 GLU D 145     -14.817  13.556 -32.967  1.00 73.97           O1-
ANISOU 3878  OE2 GLU D 145    11631   7150   9325   1930   1860   2112       O1-
ATOM   3879  N   ILE D 146     -14.306   8.157 -33.213  1.00 55.48           N  
ANISOU 3879  N   ILE D 146     8124   6350   6606   1085   -450   1295       N  
ATOM   3880  CA  ILE D 146     -13.332   7.137 -32.838  1.00 60.33           C  
ANISOU 3880  CA  ILE D 146     8556   6970   7396    673   -555   1100       C  
ATOM   3881  C   ILE D 146     -13.601   5.847 -33.609  1.00 62.99           C  
ANISOU 3881  C   ILE D 146     8811   7604   7520    742   -896   1009       C  
ATOM   3882  O   ILE D 146     -12.672   5.177 -34.081  1.00 57.71           O  
ANISOU 3882  O   ILE D 146     8194   6894   6840    626   -861    982       O  
ATOM   3883  CB  ILE D 146     -13.366   6.899 -31.315  1.00 49.27           C  
ANISOU 3883  CB  ILE D 146     6857   5611   6252    341   -666    913       C  
ATOM   3884  CG1 ILE D 146     -12.677   8.034 -30.552  1.00 55.41           C  
ANISOU 3884  CG1 ILE D 146     7603   6158   7293    172   -297    811       C  
ATOM   3885  CG2 ILE D 146     -12.651   5.589 -30.961  1.00 50.04           C  
ANISOU 3885  CG2 ILE D 146     6808   5835   6370    145   -820    772       C  
ATOM   3886  CD1 ILE D 146     -11.393   8.505 -31.155  1.00 56.55           C  
ANISOU 3886  CD1 ILE D 146     7876   6043   7568     81    132    728       C  
ATOM   3887  N   ARG D 147     -14.879   5.486 -33.755  1.00 65.41           N  
ANISOU 3887  N   ARG D 147     8935   8228   7691    909  -1193    871       N  
ATOM   3888  CA  ARG D 147     -15.231   4.266 -34.469  1.00 64.39           C  
ANISOU 3888  CA  ARG D 147     8615   8405   7444    911  -1442    598       C  
ATOM   3889  C   ARG D 147     -14.847   4.369 -35.938  1.00 68.31           C  
ANISOU 3889  C   ARG D 147     9335   9057   7562   1302  -1441    690       C  
ATOM   3890  O   ARG D 147     -14.404   3.387 -36.541  1.00 68.44           O  
ANISOU 3890  O   ARG D 147     9294   9164   7544   1186  -1510    533       O  
ATOM   3891  CB  ARG D 147     -16.728   3.981 -34.321  1.00 61.27           C  
ANISOU 3891  CB  ARG D 147     7863   8368   7050    988  -1692    239       C  
ATOM   3892  CG  ARG D 147     -17.176   3.722 -32.894  1.00 62.25           C  
ANISOU 3892  CG  ARG D 147     7804   8291   7558    612  -1617    144       C  
ATOM   3893  CD  ARG D 147     -18.601   3.197 -32.826  1.00 66.04           C  
ANISOU 3893  CD  ARG D 147     7869   9068   8155    578  -1758   -357       C  
ATOM   3894  NE  ARG D 147     -18.990   2.879 -31.455  1.00 72.33           N  
ANISOU 3894  NE  ARG D 147     8575   9569   9338    234  -1559   -406       N  
ATOM   3895  CZ  ARG D 147     -18.793   1.704 -30.869  1.00 68.34           C  
ANISOU 3895  CZ  ARG D 147     8047   8784   9133   -100  -1266   -531       C  
ATOM   3896  NH1 ARG D 147     -18.195   0.708 -31.501  1.00 62.09           N  
ANISOU 3896  NH1 ARG D 147     7281   7954   8357   -211  -1150   -644       N  
ATOM   3897  NH2 ARG D 147     -19.201   1.526 -29.615  1.00 61.05           N  
ANISOU 3897  NH2 ARG D 147     7132   7582   8484   -271  -1010   -505       N  
ATOM   3898  N   GLN D 148     -15.002   5.556 -36.524  1.00 64.67           N  
ANISOU 3898  N   GLN D 148     9182   8595   6795   1826  -1287    974       N  
ATOM   3899  CA  GLN D 148     -14.616   5.751 -37.916  1.00 69.08           C  
ANISOU 3899  CA  GLN D 148    10072   9266   6911   2351  -1179   1151       C  
ATOM   3900  C   GLN D 148     -13.115   5.563 -38.091  1.00 64.75           C  
ANISOU 3900  C   GLN D 148     9778   8255   6571   2019   -839   1318       C  
ATOM   3901  O   GLN D 148     -12.670   4.836 -38.985  1.00 63.09           O  
ANISOU 3901  O   GLN D 148     9608   8186   6176   2083   -922   1246       O  
ATOM   3902  CB  GLN D 148     -15.041   7.140 -38.388  1.00 71.74           C  
ANISOU 3902  CB  GLN D 148    10823   9569   6865   3093   -884   1532       C  
ATOM   3903  CG  GLN D 148     -16.061   7.127 -39.507  1.00 88.69           C  
ANISOU 3903  CG  GLN D 148    12919  12445   8333   3942  -1201   1400       C  
ATOM   3904  CD  GLN D 148     -15.422   6.893 -40.859  1.00 82.59           C  
ANISOU 3904  CD  GLN D 148    12401  11756   7224   4273  -1026   1450       C  
ATOM   3905  OE1 GLN D 148     -14.213   7.060 -41.023  1.00 83.28           O  
ANISOU 3905  OE1 GLN D 148    12900  11270   7471   4088   -584   1782       O  
ATOM   3906  NE2 GLN D 148     -16.235   6.523 -41.844  1.00 86.59           N  
ANISOU 3906  NE2 GLN D 148    12633  12983   7285   4776  -1331   1056       N  
ATOM   3907  N   LYS D 149     -12.319   6.218 -37.240  1.00 62.57           N  
ANISOU 3907  N   LYS D 149     9611   7471   6691   1657   -450   1451       N  
ATOM   3908  CA  LYS D 149     -10.868   6.053 -37.288  1.00 62.45           C  
ANISOU 3908  CA  LYS D 149     9706   7089   6933   1305   -129   1449       C  
ATOM   3909  C   LYS D 149     -10.464   4.584 -37.249  1.00 66.98           C  
ANISOU 3909  C   LYS D 149    10001   7879   7568    967   -484   1212       C  
ATOM   3910  O   LYS D 149      -9.575   4.155 -37.995  1.00 58.85           O  
ANISOU 3910  O   LYS D 149     9110   6759   6491    936   -367   1230       O  
ATOM   3911  CB  LYS D 149     -10.208   6.802 -36.127  1.00 64.49           C  
ANISOU 3911  CB  LYS D 149     9867   6979   7656    899    225   1350       C  
ATOM   3912  CG  LYS D 149      -8.712   6.505 -35.991  1.00 61.99           C  
ANISOU 3912  CG  LYS D 149     9462   6454   7636    501    464   1133       C  
ATOM   3913  CD  LYS D 149      -8.011   7.426 -35.000  1.00 64.88           C  
ANISOU 3913  CD  LYS D 149     9648   6552   8451    163    890    846       C  
ATOM   3914  CE  LYS D 149      -8.581   7.303 -33.602  1.00 67.44           C  
ANISOU 3914  CE  LYS D 149     9587   7171   8868     -2    524    660       C  
ATOM   3915  NZ  LYS D 149      -7.672   7.929 -32.600  1.00 65.41           N  
ANISOU 3915  NZ  LYS D 149     8992   6857   9003   -340    828    185       N  
ATOM   3916  N   TYR D 150     -11.105   3.795 -36.386  1.00 59.27           N  
ANISOU 3916  N   TYR D 150     8676   7127   6716    731   -820   1005       N  
ATOM   3917  CA  TYR D 150     -10.687   2.409 -36.230  1.00 61.11           C  
ANISOU 3917  CA  TYR D 150     8726   7439   7054    444   -964    829       C  
ATOM   3918  C   TYR D 150     -11.250   1.492 -37.310  1.00 62.03           C  
ANISOU 3918  C   TYR D 150     8768   7848   6952    576  -1172    650       C  
ATOM   3919  O   TYR D 150     -10.659   0.439 -37.573  1.00 62.41           O  
ANISOU 3919  O   TYR D 150     8777   7870   7065    382  -1153    549       O  
ATOM   3920  CB  TYR D 150     -11.050   1.914 -34.828  1.00 57.68           C  
ANISOU 3920  CB  TYR D 150     8047   7012   6854    202  -1036    714       C  
ATOM   3921  CG  TYR D 150      -9.970   2.265 -33.826  1.00 54.91           C  
ANISOU 3921  CG  TYR D 150     7677   6520   6668     61   -872    741       C  
ATOM   3922  CD1 TYR D 150      -9.979   3.489 -33.164  1.00 56.46           C  
ANISOU 3922  CD1 TYR D 150     7846   6632   6974     60   -749    742       C  
ATOM   3923  CD2 TYR D 150      -8.924   1.386 -33.567  1.00 55.82           C  
ANISOU 3923  CD2 TYR D 150     7753   6650   6807    -25   -824    686       C  
ATOM   3924  CE1 TYR D 150      -8.981   3.823 -32.262  1.00 50.45           C  
ANISOU 3924  CE1 TYR D 150     6931   5876   6362    -63   -615    568       C  
ATOM   3925  CE2 TYR D 150      -7.922   1.708 -32.665  1.00 59.57           C  
ANISOU 3925  CE2 TYR D 150     8096   7187   7352    -48   -737    563       C  
ATOM   3926  CZ  TYR D 150      -7.957   2.930 -32.018  1.00 57.66           C  
ANISOU 3926  CZ  TYR D 150     7739   6933   7236    -86   -649    444       C  
ATOM   3927  OH  TYR D 150      -6.963   3.252 -31.123  1.00 55.76           O  
ANISOU 3927  OH  TYR D 150     7234   6883   7068   -106   -579    131       O  
ATOM   3928  N   GLN D 151     -12.350   1.870 -37.965  1.00 58.51           N  
ANISOU 3928  N   GLN D 151     8266   7740   6223    948  -1359    547       N  
ATOM   3929  CA  GLN D 151     -12.812   1.081 -39.102  1.00 67.39           C  
ANISOU 3929  CA  GLN D 151     9228   9292   7084   1140  -1576    221       C  
ATOM   3930  C   GLN D 151     -11.825   1.165 -40.259  1.00 67.31           C  
ANISOU 3930  C   GLN D 151     9561   9222   6794   1381  -1448    437       C  
ATOM   3931  O   GLN D 151     -11.531   0.152 -40.908  1.00 58.11           O  
ANISOU 3931  O   GLN D 151     8286   8192   5602   1257  -1515    203       O  
ATOM   3932  CB  GLN D 151     -14.206   1.536 -39.543  1.00 73.47           C  
ANISOU 3932  CB  GLN D 151     9778  10622   7514   1630  -1860    -47       C  
ATOM   3933  CG  GLN D 151     -15.092   0.440 -40.175  1.00 76.84           C  
ANISOU 3933  CG  GLN D 151     9678  11642   7875   1622  -2140   -775       C  
ATOM   3934  CD  GLN D 151     -15.446  -0.727 -39.241  1.00 89.34           C  
ANISOU 3934  CD  GLN D 151    10866  13016  10063    930  -2006  -1213       C  
ATOM   3935  OE1 GLN D 151     -14.646  -1.159 -38.407  1.00 83.64           O  
ANISOU 3935  OE1 GLN D 151    10338  11731   9709    492  -1715   -922       O  
ATOM   3936  NE2 GLN D 151     -16.660  -1.250 -39.398  1.00 88.61           N  
ANISOU 3936  NE2 GLN D 151    10208  13404  10056    897  -2151  -1969       N  
ATOM   3937  N   SER D 152     -11.287   2.362 -40.517  1.00 62.94           N  
ANISOU 3937  N   SER D 152     9443   8392   6079   1702  -1159    867       N  
ATOM   3938  CA  SER D 152     -10.323   2.544 -41.596  1.00 59.41           C  
ANISOU 3938  CA  SER D 152     9400   7770   5403   1952   -887   1108       C  
ATOM   3939  C   SER D 152      -8.976   1.911 -41.279  1.00 60.23           C  
ANISOU 3939  C   SER D 152     9510   7472   5904   1383   -692   1109       C  
ATOM   3940  O   SER D 152      -8.168   1.716 -42.192  1.00 66.89           O  
ANISOU 3940  O   SER D 152    10594   8203   6618   1475   -517   1200       O  
ATOM   3941  CB  SER D 152     -10.157   4.033 -41.897  1.00 60.82           C  
ANISOU 3941  CB  SER D 152    10099   7620   5389   2452   -406   1552       C  
ATOM   3942  OG  SER D 152     -11.397   4.588 -42.291  1.00 67.58           O  
ANISOU 3942  OG  SER D 152    10991   8936   5749   3159   -593   1591       O  
ATOM   3943  N   LYS D 153      -8.714   1.597 -40.009  1.00 58.34           N  
ANISOU 3943  N   LYS D 153     9016   7063   6089    886   -714   1003       N  
ATOM   3944  CA  LYS D 153      -7.572   0.770 -39.638  1.00 63.81           C  
ANISOU 3944  CA  LYS D 153     9620   7570   7055    479   -631    926       C  
ATOM   3945  C   LYS D 153      -7.871  -0.722 -39.750  1.00 66.72           C  
ANISOU 3945  C   LYS D 153     9755   8156   7438    304   -856    694       C  
ATOM   3946  O   LYS D 153      -6.955  -1.512 -40.013  1.00 57.90           O  
ANISOU 3946  O   LYS D 153     8670   6935   6392    137   -764    676       O  
ATOM   3947  CB  LYS D 153      -7.130   1.080 -38.200  1.00 61.32           C  
ANISOU 3947  CB  LYS D 153     9135   7098   7068    203   -538    885       C  
ATOM   3948  CG  LYS D 153      -6.303   2.348 -38.042  1.00 77.97           C  
ANISOU 3948  CG  LYS D 153    11379   8896   9351    175   -141    922       C  
ATOM   3949  CD  LYS D 153      -6.654   3.080 -36.749  1.00 70.54           C  
ANISOU 3949  CD  LYS D 153    10235   7956   8612     73   -125    826       C  
ATOM   3950  CE  LYS D 153      -5.532   2.993 -35.726  1.00 66.01           C  
ANISOU 3950  CE  LYS D 153     9361   7426   8294   -184    -45    519       C  
ATOM   3951  NZ  LYS D 153      -4.381   3.864 -36.117  1.00 68.55           N  
ANISOU 3951  NZ  LYS D 153     9728   7445   8871   -327    458    311       N  
ATOM   3952  N   ARG D 154      -9.131  -1.124 -39.560  1.00 59.03           N  
ANISOU 3952  N   ARG D 154     8531   7450   6446    323  -1065    462       N  
ATOM   3953  CA  ARG D 154      -9.501  -2.533 -39.478  1.00 63.01           C  
ANISOU 3953  CA  ARG D 154     8782   8033   7126     64  -1072    139       C  
ATOM   3954  C   ARG D 154      -9.767  -3.162 -40.838  1.00 60.02           C  
ANISOU 3954  C   ARG D 154     8301   7967   6536    169  -1182   -181       C  
ATOM   3955  O   ARG D 154      -9.435  -4.333 -41.051  1.00 54.38           O  
ANISOU 3955  O   ARG D 154     7499   7167   5995    -93  -1032   -381       O  
ATOM   3956  CB  ARG D 154     -10.741  -2.708 -38.593  1.00 59.79           C  
ANISOU 3956  CB  ARG D 154     8092   7708   6917    -46  -1106   -106       C  
ATOM   3957  CG  ARG D 154     -10.459  -3.254 -37.207  1.00 67.36           C  
ANISOU 3957  CG  ARG D 154     9071   8334   8187   -278   -844     25       C  
ATOM   3958  CD  ARG D 154     -11.716  -3.870 -36.606  1.00 70.06           C  
ANISOU 3958  CD  ARG D 154     9154   8663   8801   -447   -695   -320       C  
ATOM   3959  NE  ARG D 154     -12.828  -2.930 -36.665  1.00 76.43           N  
ANISOU 3959  NE  ARG D 154     9764   9767   9509   -299   -976   -489       N  
ATOM   3960  CZ  ARG D 154     -13.010  -1.924 -35.818  1.00 70.03           C  
ANISOU 3960  CZ  ARG D 154     9033   8906   8670   -186  -1064   -226       C  
ATOM   3961  NH1 ARG D 154     -12.185  -1.714 -34.804  1.00 67.05           N  
ANISOU 3961  NH1 ARG D 154     8857   8265   8352   -208   -924    131       N  
ATOM   3962  NH2 ARG D 154     -14.039  -1.102 -35.999  1.00 72.85           N  
ANISOU 3962  NH2 ARG D 154     9224   9552   8904      5  -1301   -378       N  
ATOM   3963  N   GLN D 155     -10.375  -2.414 -41.758  1.00 58.79           N  
ANISOU 3963  N   GLN D 155     8157   8211   5969    620  -1410   -255       N  
ATOM   3964  CA  GLN D 155     -10.754  -2.997 -43.042  1.00 65.16           C  
ANISOU 3964  CA  GLN D 155     8776   9510   6474    840  -1587   -686       C  
ATOM   3965  C   GLN D 155      -9.585  -3.514 -43.880  1.00 66.84           C  
ANISOU 3965  C   GLN D 155     9236   9552   6609    785  -1443   -542       C  
ATOM   3966  O   GLN D 155      -9.738  -4.596 -44.472  1.00 62.98           O  
ANISOU 3966  O   GLN D 155     8469   9291   6171    613  -1465  -1018       O  
ATOM   3967  CB  GLN D 155     -11.590  -1.991 -43.841  1.00 68.38           C  
ANISOU 3967  CB  GLN D 155     9203  10492   6286   1576  -1868   -733       C  
ATOM   3968  CG  GLN D 155     -12.474  -2.654 -44.890  1.00 68.84           C  
ANISOU 3968  CG  GLN D 155     8785  11362   6009   1866  -2184  -1487       C  
ATOM   3969  CD  GLN D 155     -13.501  -3.595 -44.282  1.00 73.32           C  
ANISOU 3969  CD  GLN D 155     8672  12134   7053   1360  -2224  -2282       C  
ATOM   3970  OE1 GLN D 155     -14.157  -3.261 -43.294  1.00 75.86           O  
ANISOU 3970  OE1 GLN D 155     8858  12325   7638   1206  -2206  -2284       O  
ATOM   3971  NE2 GLN D 155     -13.650  -4.777 -44.876  1.00 79.27           N  
ANISOU 3971  NE2 GLN D 155     8990  13164   7964   1076  -2190  -3007       N  
ATOM   3972  N   PRO D 156      -8.428  -2.840 -43.989  1.00 70.37           N  
ANISOU 3972  N   PRO D 156    10149   9599   6989    879  -1237     -1       N  
ATOM   3973  CA  PRO D 156      -7.341  -3.448 -44.778  1.00 68.69           C  
ANISOU 3973  CA  PRO D 156    10123   9224   6752    779  -1085     67       C  
ATOM   3974  C   PRO D 156      -6.756  -4.688 -44.123  1.00 62.29           C  
ANISOU 3974  C   PRO D 156     9148   8117   6404    212   -922    -51       C  
ATOM   3975  O   PRO D 156      -6.179  -5.529 -44.823  1.00 59.72           O  
ANISOU 3975  O   PRO D 156     8841   7767   6083     90   -834   -164       O  
ATOM   3976  CB  PRO D 156      -6.307  -2.321 -44.909  1.00 67.69           C  
ANISOU 3976  CB  PRO D 156    10488   8680   6550    972   -789    584       C  
ATOM   3977  CG  PRO D 156      -6.650  -1.307 -43.895  1.00 72.99           C  
ANISOU 3977  CG  PRO D 156    11182   9183   7367    990   -725    767       C  
ATOM   3978  CD  PRO D 156      -7.968  -1.638 -43.264  1.00 71.81           C  
ANISOU 3978  CD  PRO D 156    10632   9390   7263    937  -1040    459       C  
ATOM   3979  N   ILE D 157      -6.897  -4.835 -42.805  1.00 56.32           N  
ANISOU 3979  N   ILE D 157     8269   7139   5989    -55   -833     -1       N  
ATOM   3980  CA  ILE D 157      -6.489  -6.070 -42.149  1.00 61.09           C  
ANISOU 3980  CA  ILE D 157     8787   7482   6941   -408   -581    -68       C  
ATOM   3981  C   ILE D 157      -7.459  -7.190 -42.500  1.00 62.96           C  
ANISOU 3981  C   ILE D 157     8698   7882   7341   -609   -490   -612       C  
ATOM   3982  O   ILE D 157      -7.053  -8.286 -42.904  1.00 68.75           O  
ANISOU 3982  O   ILE D 157     9411   8480   8232   -820   -237   -781       O  
ATOM   3983  CB  ILE D 157      -6.417  -5.862 -40.631  1.00 54.55           C  
ANISOU 3983  CB  ILE D 157     7971   6435   6322   -465   -469    155       C  
ATOM   3984  CG1 ILE D 157      -5.555  -4.649 -40.302  1.00 59.62           C  
ANISOU 3984  CG1 ILE D 157     8787   7002   6863   -317   -536    467       C  
ATOM   3985  CG2 ILE D 157      -5.858  -7.111 -39.960  1.00 55.71           C  
ANISOU 3985  CG2 ILE D 157     8162   6308   6695   -607   -112    210       C  
ATOM   3986  CD1 ILE D 157      -5.296  -4.498 -38.843  1.00 61.02           C  
ANISOU 3986  CD1 ILE D 157     8912   7095   7179   -315   -464    588       C  
ATOM   3987  N   LEU D 158      -8.761  -6.920 -42.348  1.00 55.46           N  
ANISOU 3987  N   LEU D 158     7448   7224   6402   -568   -640   -974       N  
ATOM   3988  CA  LEU D 158      -9.796  -7.889 -42.693  1.00 56.37           C  
ANISOU 3988  CA  LEU D 158     7108   7559   6751   -808   -506  -1723       C  
ATOM   3989  C   LEU D 158      -9.714  -8.292 -44.159  1.00 67.83           C  
ANISOU 3989  C   LEU D 158     8390   9433   7948   -715   -662  -2156       C  
ATOM   3990  O   LEU D 158      -9.897  -9.468 -44.500  1.00 69.87           O  
ANISOU 3990  O   LEU D 158     8361   9664   8521  -1063   -348  -2726       O  
ATOM   3991  CB  LEU D 158     -11.168  -7.295 -42.376  1.00 62.51           C  
ANISOU 3991  CB  LEU D 158     7531   8708   7511   -695   -732  -2103       C  
ATOM   3992  CG  LEU D 158     -11.640  -7.423 -40.927  1.00 67.00           C  
ANISOU 3992  CG  LEU D 158     8092   8858   8508   -944   -407  -2003       C  
ATOM   3993  CD1 LEU D 158     -12.894  -6.588 -40.683  1.00 68.80           C  
ANISOU 3993  CD1 LEU D 158     8009   9486   8646   -768   -715  -2296       C  
ATOM   3994  CD2 LEU D 158     -11.900  -8.884 -40.599  1.00 69.86           C  
ANISOU 3994  CD2 LEU D 158     8276   8821   9447  -1417    264  -2459       C  
ATOM   3995  N   ASP D 159      -9.437  -7.331 -45.044  1.00 67.52           N  
ANISOU 3995  N   ASP D 159     8551   9762   7340   -213  -1059  -1909       N  
ATOM   3996  CA  ASP D 159      -9.312  -7.644 -46.465  1.00 68.06           C  
ANISOU 3996  CA  ASP D 159     8521  10297   7042     19  -1224  -2266       C  
ATOM   3997  C   ASP D 159      -8.097  -8.523 -46.735  1.00 62.35           C  
ANISOU 3997  C   ASP D 159     8042   9114   6534   -309   -900  -2058       C  
ATOM   3998  O   ASP D 159      -8.165  -9.452 -47.547  1.00 72.23           O  
ANISOU 3998  O   ASP D 159     9022  10591   7829   -466   -818  -2614       O  
ATOM   3999  CB  ASP D 159      -9.228  -6.354 -47.282  1.00 74.49           C  
ANISOU 3999  CB  ASP D 159     9662  11500   7143    777  -1571  -1891       C  
ATOM   4000  CG  ASP D 159     -10.471  -5.494 -47.150  1.00 78.70           C  
ANISOU 4000  CG  ASP D 159     9958  12584   7359   1246  -1898  -2110       C  
ATOM   4001  OD1 ASP D 159     -11.495  -5.991 -46.635  1.00 84.07           O  
ANISOU 4001  OD1 ASP D 159    10085  13497   8361    954  -1939  -2752       O  
ATOM   4002  OD2 ASP D 159     -10.417  -4.312 -47.546  1.00 85.78           O1-
ANISOU 4002  OD2 ASP D 159    11248  13633   7712   1925  -2028  -1639       O1-
ATOM   4003  N   ALA D 160      -6.976  -8.244 -46.064  1.00 58.90           N  
ANISOU 4003  N   ALA D 160     8060   8088   6231   -402   -709  -1341       N  
ATOM   4004  CA  ALA D 160      -5.763  -9.029 -46.270  1.00 64.44           C  
ANISOU 4004  CA  ALA D 160     8988   8393   7103   -641   -418  -1127       C  
ATOM   4005  C   ALA D 160      -5.885 -10.427 -45.678  1.00 66.30           C  
ANISOU 4005  C   ALA D 160     9031   8297   7864  -1110     46  -1420       C  
ATOM   4006  O   ALA D 160      -5.286 -11.376 -46.199  1.00 57.19           O  
ANISOU 4006  O   ALA D 160     7911   6973   6844  -1309    318  -1533       O  
ATOM   4007  CB  ALA D 160      -4.559  -8.308 -45.664  1.00 54.76           C  
ANISOU 4007  CB  ALA D 160     8180   6754   5871   -562   -350   -444       C  
ATOM   4008  N   ILE D 161      -6.631 -10.570 -44.580  1.00 62.63           N  
ANISOU 4008  N   ILE D 161     8420   7664   7711  -1261    244  -1509       N  
ATOM   4009  CA  ILE D 161      -6.874 -11.893 -44.020  1.00 63.32           C  
ANISOU 4009  CA  ILE D 161     8401   7331   8327  -1643    894  -1788       C  
ATOM   4010  C   ILE D 161      -7.711 -12.723 -44.981  1.00 63.64           C  
ANISOU 4010  C   ILE D 161     7944   7658   8576  -1941   1058  -2721       C  
ATOM   4011  O   ILE D 161      -7.408 -13.893 -45.240  1.00 73.36           O  
ANISOU 4011  O   ILE D 161     9155   8562  10156  -2257   1614  -2979       O  
ATOM   4012  CB  ILE D 161      -7.548 -11.764 -42.642  1.00 65.33           C  
ANISOU 4012  CB  ILE D 161     8660   7322   8840  -1670   1138  -1667       C  
ATOM   4013  CG1 ILE D 161      -6.525 -11.312 -41.601  1.00 61.10           C  
ANISOU 4013  CG1 ILE D 161     8570   6498   8146  -1385   1127   -857       C  
ATOM   4014  CG2 ILE D 161      -8.191 -13.084 -42.230  1.00 66.71           C  
ANISOU 4014  CG2 ILE D 161     8680   7053   9614  -2056   1970  -2142       C  
ATOM   4015  CD1 ILE D 161      -7.140 -10.860 -40.306  1.00 60.72           C  
ANISOU 4015  CD1 ILE D 161     8547   6342   8183  -1276   1191   -678       C  
ATOM   4016  N   GLU D 162      -8.766 -12.126 -45.537  1.00 69.01           N  
ANISOU 4016  N   GLU D 162     8180   9008   9032  -1802    598  -3308       N  
ATOM   4017  CA  GLU D 162      -9.682 -12.824 -46.431  1.00 77.51           C  
ANISOU 4017  CA  GLU D 162     8601  10582  10268  -2029    669  -4435       C  
ATOM   4018  C   GLU D 162      -9.118 -12.998 -47.841  1.00 81.78           C  
ANISOU 4018  C   GLU D 162     9098  11567  10406  -1853    384  -4648       C  
ATOM   4019  O   GLU D 162      -9.672 -13.787 -48.619  1.00 87.87           O  
ANISOU 4019  O   GLU D 162     9298  12740  11349  -2090    526  -5662       O  
ATOM   4020  CB  GLU D 162     -11.020 -12.070 -46.465  1.00 82.41           C  
ANISOU 4020  CB  GLU D 162     8703  11919  10691  -1797    208  -5040       C  
ATOM   4021  CG  GLU D 162     -12.133 -12.725 -47.278  1.00103.76           C  
ANISOU 4021  CG  GLU D 162    10531  15323  13570  -1974    244  -6408       C  
ATOM   4022  CD  GLU D 162     -13.052 -13.589 -46.431  1.00115.31           C  
ANISOU 4022  CD  GLU D 162    11579  16351  15882  -2483   1047  -6867       C  
ATOM   4023  OE1 GLU D 162     -13.169 -14.802 -46.721  1.00110.85           O  
ANISOU 4023  OE1 GLU D 162    10677  15592  15851  -2864   1752  -7354       O  
ATOM   4024  OE2 GLU D 162     -13.649 -13.056 -45.470  1.00111.02           O1-
ANISOU 4024  OE2 GLU D 162    11065  15652  15466  -2478   1044  -6729       O1-
ATOM   4025  N   ALA D 163      -8.024 -12.307 -48.172  1.00 75.98           N  
ANISOU 4025  N   ALA D 163     8925  10756   9187  -1468     60  -3795       N  
ATOM   4026  CA  ALA D 163      -7.366 -12.395 -49.480  1.00 79.86           C  
ANISOU 4026  CA  ALA D 163     9508  11577   9258  -1238   -157  -3845       C  
ATOM   4027  C   ALA D 163      -8.306 -12.012 -50.618  1.00 99.95           C  
ANISOU 4027  C   ALA D 163    11562  15178  11236   -762   -690  -4630       C  
ATOM   4028  O   ALA D 163      -8.795 -10.884 -50.679  1.00105.70           O  
ANISOU 4028  O   ALA D 163    12351  16374  11437   -169  -1158  -4437       O  
ATOM   4029  CB  ALA D 163      -6.811 -13.794 -49.708  1.00 78.72           C  
ANISOU 4029  CB  ALA D 163     9305  11001   9604  -1772    428  -4136       C  
TER    4030      ALA D 163                                                      
ATOM   4031  N   ARG E   0      18.482  11.279  -3.917  1.00 64.84           N  
ANISOU 4031  N   ARG E   0     9477   8457   6704  -2340   -425   -681       N  
ATOM   4032  CA  ARG E   0      18.353  11.952  -5.209  1.00 66.08           C  
ANISOU 4032  CA  ARG E   0     9658   8390   7059  -2320   -388   -650       C  
ATOM   4033  C   ARG E   0      17.750  11.024  -6.264  1.00 62.05           C  
ANISOU 4033  C   ARG E   0     8882   7946   6748  -2030   -231   -525       C  
ATOM   4034  O   ARG E   0      18.290   9.949  -6.525  1.00 62.39           O  
ANISOU 4034  O   ARG E   0     8630   8239   6837  -2004   -240   -348       O  
ATOM   4035  CB  ARG E   0      19.712  12.456  -5.695  1.00 75.97           C  
ANISOU 4035  CB  ARG E   0    10826   9710   8330  -2684   -564   -522       C  
ATOM   4036  CG  ARG E   0      19.669  13.029  -7.106  1.00 80.50           C  
ANISOU 4036  CG  ARG E   0    11425  10079   9084  -2688   -513   -440       C  
ATOM   4037  CD  ARG E   0      21.062  13.187  -7.712  1.00 93.39           C  
ANISOU 4037  CD  ARG E   0    12836  11912  10735  -3053   -636   -260       C  
ATOM   4038  NE  ARG E   0      20.995  13.552  -9.123  1.00 92.08           N  
ANISOU 4038  NE  ARG E   0    12677  11588  10721  -3035   -555   -147       N  
ATOM   4039  CZ  ARG E   0      20.962  14.798  -9.578  1.00 93.32           C  
ANISOU 4039  CZ  ARG E   0    13207  11386  10865  -3238   -579   -187       C  
ATOM   4040  NH1 ARG E   0      21.052  15.837  -8.760  1.00 92.32           N  
ANISOU 4040  NH1 ARG E   0    13491  10999  10588  -3503   -686   -349       N  
ATOM   4041  NH2 ARG E   0      20.838  15.009 -10.886  1.00 86.00           N  
ANISOU 4041  NH2 ARG E   0    12291  10331  10054  -3175   -496    -59       N  
ATOM   4042  N   ASP E   1      16.641  11.446  -6.874  1.00 54.14           N  
ANISOU 4042  N   ASP E   1     7999   6726   5847  -1797   -102   -625       N  
ATOM   4043  CA  ASP E   1      15.991  10.635  -7.899  1.00 58.95           C  
ANISOU 4043  CA  ASP E   1     8370   7404   6623  -1551     28   -535       C  
ATOM   4044  C   ASP E   1      16.888  10.528  -9.126  1.00 53.45           C  
ANISOU 4044  C   ASP E   1     7499   6750   6059  -1652    -35   -331       C  
ATOM   4045  O   ASP E   1      17.584  11.482  -9.477  1.00 51.48           O  
ANISOU 4045  O   ASP E   1     7383   6370   5808  -1863   -135   -298       O  
ATOM   4046  CB  ASP E   1      14.660  11.264  -8.312  1.00 55.37           C  
ANISOU 4046  CB  ASP E   1     8060   6754   6224  -1274    139   -695       C  
ATOM   4047  CG  ASP E   1      13.559  11.035  -7.304  1.00 64.62           C  
ANISOU 4047  CG  ASP E   1     9267   8005   7280  -1100    273   -886       C  
ATOM   4048  OD1 ASP E   1      13.838  10.499  -6.207  1.00 60.11           O  
ANISOU 4048  OD1 ASP E   1     8690   7585   6563  -1228    276   -897       O  
ATOM   4049  OD2 ASP E   1      12.401  11.380  -7.625  1.00 65.98           O  
ANISOU 4049  OD2 ASP E   1     9457   8124   7488   -824    378  -1022       O  
ATOM   4050  N   ILE E   2      16.868   9.375  -9.794  1.00 47.16           N  
ANISOU 4050  N   ILE E   2     6430   6130   5357  -1519     36   -200       N  
ATOM   4051  CA  ILE E   2      17.524   9.272 -11.097  1.00 45.73           C  
ANISOU 4051  CA  ILE E   2     6089   5995   5290  -1546     20    -33       C  
ATOM   4052  C   ILE E   2      16.579   9.810 -12.160  1.00 46.46           C  
ANISOU 4052  C   ILE E   2     6286   5883   5484  -1366     91    -80       C  
ATOM   4053  O   ILE E   2      15.509   9.242 -12.404  1.00 50.28           O  
ANISOU 4053  O   ILE E   2     6703   6384   6016  -1131    192   -146       O  
ATOM   4054  CB  ILE E   2      17.955   7.833 -11.417  1.00 47.26           C  
ANISOU 4054  CB  ILE E   2     6003   6436   5517  -1444     59    112       C  
ATOM   4055  CG1 ILE E   2      18.852   7.283 -10.308  1.00 44.41           C  
ANISOU 4055  CG1 ILE E   2     5559   6288   5027  -1547    -35    167       C  
ATOM   4056  CG2 ILE E   2      18.674   7.790 -12.786  1.00 47.93           C  
ANISOU 4056  CG2 ILE E   2     5924   6598   5691  -1455     62    266       C  
ATOM   4057  CD1 ILE E   2      19.544   5.992 -10.663  1.00 49.79           C  
ANISOU 4057  CD1 ILE E   2     6006   7196   5716  -1411    -29    329       C  
ATOM   4058  N   VAL E   3      16.974  10.909 -12.792  1.00 48.69           N  
ANISOU 4058  N   VAL E   3     6740   5984   5777  -1494     28    -40       N  
ATOM   4059  CA  VAL E   3      16.221  11.521 -13.877  1.00 45.69           C  
ANISOU 4059  CA  VAL E   3     6505   5394   5461  -1310     61    -48       C  
ATOM   4060  C   VAL E   3      16.762  11.012 -15.200  1.00 41.89           C  
ANISOU 4060  C   VAL E   3     5822   5046   5049  -1322     90    140       C  
ATOM   4061  O   VAL E   3      17.975  11.054 -15.443  1.00 45.50           O  
ANISOU 4061  O   VAL E   3     6182   5622   5482  -1580     53    284       O  
ATOM   4062  CB  VAL E   3      16.293  13.054 -13.808  1.00 53.95           C  
ANISOU 4062  CB  VAL E   3     7967   6092   6441  -1431    -20   -103       C  
ATOM   4063  CG1 VAL E   3      15.372  13.671 -14.843  1.00 52.18           C  
ANISOU 4063  CG1 VAL E   3     7939   5634   6254  -1147     -1   -114       C  
ATOM   4064  CG2 VAL E   3      15.904  13.516 -12.413  1.00 52.31           C  
ANISOU 4064  CG2 VAL E   3     7976   5770   6131  -1429    -45   -308       C  
ATOM   4065  N   LEU E   4      15.860  10.544 -16.057  1.00 44.42           N  
ANISOU 4065  N   LEU E   4     6063   5382   5433  -1048    156    128       N  
ATOM   4066  CA  LEU E   4      16.201  10.044 -17.383  1.00 43.85           C  
ANISOU 4066  CA  LEU E   4     5839   5422   5399  -1012    192    276       C  
ATOM   4067  C   LEU E   4      15.818  11.094 -18.413  1.00 46.52           C  
ANISOU 4067  C   LEU E   4     6427   5529   5722   -935    160    316       C  
ATOM   4068  O   LEU E   4      14.637  11.423 -18.559  1.00 47.14           O  
ANISOU 4068  O   LEU E   4     6623   5480   5807   -666    148    201       O  
ATOM   4069  CB  LEU E   4      15.467   8.738 -17.676  1.00 43.51           C  
ANISOU 4069  CB  LEU E   4     5577   5551   5404   -791    269    230       C  
ATOM   4070  CG  LEU E   4      15.771   7.595 -16.713  1.00 42.22           C  
ANISOU 4070  CG  LEU E   4     5245   5566   5232   -836    305    213       C  
ATOM   4071  CD1 LEU E   4      15.114   6.281 -17.179  1.00 37.44           C  
ANISOU 4071  CD1 LEU E   4     4501   5071   4654   -675    385    184       C  
ATOM   4072  CD2 LEU E   4      17.272   7.446 -16.531  1.00 40.82           C  
ANISOU 4072  CD2 LEU E   4     4959   5533   5017  -1028    269    358       C  
ATOM   4073  N   THR E   5      16.810  11.620 -19.120  1.00 46.54           N  
ANISOU 4073  N   THR E   5     6503   5499   5680  -1164    148    484       N  
ATOM   4074  CA  THR E   5      16.589  12.630 -20.149  1.00 45.24           C  
ANISOU 4074  CA  THR E   5     6643   5085   5462  -1131    118    568       C  
ATOM   4075  C   THR E   5      16.639  11.954 -21.511  1.00 45.29           C  
ANISOU 4075  C   THR E   5     6475   5272   5462  -1016    181    691       C  
ATOM   4076  O   THR E   5      17.696  11.493 -21.949  1.00 48.03           O  
ANISOU 4076  O   THR E   5     6623   5843   5784  -1212    247    827       O  
ATOM   4077  CB  THR E   5      17.605  13.758 -20.039  1.00 45.23           C  
ANISOU 4077  CB  THR E   5     6914   4896   5376  -1529     76    677       C  
ATOM   4078  OG1 THR E   5      17.746  14.135 -18.663  1.00 52.13           O  
ANISOU 4078  OG1 THR E   5     7889   5677   6241  -1684     16    545       O  
ATOM   4079  CG2 THR E   5      17.176  14.949 -20.873  1.00 49.30           C  
ANISOU 4079  CG2 THR E   5     7894   5030   5809  -1466     30    746       C  
ATOM   4080  N   GLN E   6      15.483  11.884 -22.157  1.00 49.10           N  
ANISOU 4080  N   GLN E   6     7014   5694   5948   -682    158    626       N  
ATOM   4081  CA  GLN E   6      15.282  11.150 -23.397  1.00 44.95           C  
ANISOU 4081  CA  GLN E   6     6339   5344   5397   -529    198    691       C  
ATOM   4082  C   GLN E   6      15.160  12.158 -24.526  1.00 60.10           C  
ANISOU 4082  C   GLN E   6     8582   7053   7200   -477    148    824       C  
ATOM   4083  O   GLN E   6      14.279  13.024 -24.495  1.00 58.71           O  
ANISOU 4083  O   GLN E   6     8685   6628   6995   -261     51    765       O  
ATOM   4084  CB  GLN E   6      14.028  10.272 -23.303  1.00 43.66           C  
ANISOU 4084  CB  GLN E   6     5983   5315   5291   -231    187    512       C  
ATOM   4085  CG  GLN E   6      13.866   9.291 -24.425  1.00 50.14           C  
ANISOU 4085  CG  GLN E   6     6633   6339   6077   -123    223    539       C  
ATOM   4086  CD  GLN E   6      12.724   8.317 -24.217  1.00 48.30           C  
ANISOU 4086  CD  GLN E   6     6195   6264   5893     54    217    352       C  
ATOM   4087  OE1 GLN E   6      12.191   8.168 -23.109  1.00 39.77           O  
ANISOU 4087  OE1 GLN E   6     5036   5196   4880     63    223    215       O  
ATOM   4088  NE2 GLN E   6      12.314   7.667 -25.296  1.00 45.04           N  
ANISOU 4088  NE2 GLN E   6     5706   5985   5421    165    207    341       N  
ATOM   4089  N   SER E   7      16.060  12.066 -25.498  1.00 57.52           N  
ANISOU 4089  N   SER E   7     8238   6832   6785   -654    220   1007       N  
ATOM   4090  CA  SER E   7      16.030  12.938 -26.658  1.00 64.60           C  
ANISOU 4090  CA  SER E   7     9468   7546   7531   -639    191   1170       C  
ATOM   4091  C   SER E   7      16.110  12.095 -27.920  1.00 68.50           C  
ANISOU 4091  C   SER E   7     9786   8304   7939   -536    260   1242       C  
ATOM   4092  O   SER E   7      16.691  11.005 -27.909  1.00 67.25           O  
ANISOU 4092  O   SER E   7     9288   8446   7820   -600    367   1220       O  
ATOM   4093  CB  SER E   7      17.186  13.951 -26.635  1.00 60.06           C  
ANISOU 4093  CB  SER E   7     9150   6805   6866  -1071    232   1355       C  
ATOM   4094  OG  SER E   7      18.435  13.302 -26.783  1.00 71.17           O  
ANISOU 4094  OG  SER E   7    10226   8557   8259  -1373    372   1454       O  
ATOM   4095  N   PRO E   8      15.498  12.557 -29.019  1.00 67.18           N  
ANISOU 4095  N   PRO E   8     9871   8022   7630   -335    192   1319       N  
ATOM   4096  CA  PRO E   8      14.647  13.750 -29.062  1.00 60.84           C  
ANISOU 4096  CA  PRO E   8     9490   6860   6766   -128     40   1330       C  
ATOM   4097  C   PRO E   8      13.254  13.400 -28.567  1.00 61.48           C  
ANISOU 4097  C   PRO E   8     9417   6993   6951    277    -81   1092       C  
ATOM   4098  O   PRO E   8      12.973  12.217 -28.381  1.00 67.52           O  
ANISOU 4098  O   PRO E   8     9788   8059   7809    333    -40    949       O  
ATOM   4099  CB  PRO E   8      14.622  14.096 -30.546  1.00 65.18           C  
ANISOU 4099  CB  PRO E   8    10297   7375   7093    -47     20   1520       C  
ATOM   4100  CG  PRO E   8      14.682  12.758 -31.171  1.00 63.60           C  
ANISOU 4100  CG  PRO E   8     9702   7576   6888     11    101   1461       C  
ATOM   4101  CD  PRO E   8      15.655  11.966 -30.357  1.00 55.28           C  
ANISOU 4101  CD  PRO E   8     8294   6733   5977   -271    253   1411       C  
ATOM   4102  N   ALA E   9      12.388  14.391 -28.359  1.00 58.47           N  
ANISOU 4102  N   ALA E   9     9344   6337   6536    558   -220   1046       N  
ATOM   4103  CA  ALA E   9      11.023  14.055 -27.979  1.00 61.49           C  
ANISOU 4103  CA  ALA E   9     9505   6868   6989    962   -322    815       C  
ATOM   4104  C   ALA E   9      10.241  13.455 -29.138  1.00 56.42           C  
ANISOU 4104  C   ALA E   9     8690   6498   6248   1232   -408    798       C  
ATOM   4105  O   ALA E   9       9.252  12.754 -28.907  1.00 57.16           O  
ANISOU 4105  O   ALA E   9     8437   6872   6407   1439   -457    594       O  
ATOM   4106  CB  ALA E   9      10.295  15.287 -27.441  1.00 66.83           C  
ANISOU 4106  CB  ALA E   9    10542   7215   7636   1270   -445    751       C  
ATOM   4107  N   SER E  10      10.656  13.716 -30.375  1.00 67.49           N  
ANISOU 4107  N   SER E  10    10328   7844   7470   1202   -427   1003       N  
ATOM   4108  CA  SER E  10       9.952  13.198 -31.536  1.00 66.02           C  
ANISOU 4108  CA  SER E  10    10022   7915   7147   1448   -530    988       C  
ATOM   4109  C   SER E  10      10.920  13.063 -32.702  1.00 59.78           C  
ANISOU 4109  C   SER E  10     9393   7141   6181   1218   -439   1213       C  
ATOM   4110  O   SER E  10      11.823  13.887 -32.879  1.00 67.34           O  
ANISOU 4110  O   SER E  10    10707   7830   7050    993   -365   1432       O  
ATOM   4111  CB  SER E  10       8.773  14.098 -31.935  1.00 70.40           C  
ANISOU 4111  CB  SER E  10    10807   8370   7571   1944   -761    974       C  
ATOM   4112  OG  SER E  10       7.771  14.125 -30.936  1.00 76.62           O  
ANISOU 4112  OG  SER E  10    11364   9250   8497   2210   -831    736       O  
ATOM   4113  N   LEU E  11      10.711  12.015 -33.490  1.00 66.03           N  
ANISOU 4113  N   LEU E  11     9926   8260   6901   1252   -435   1146       N  
ATOM   4114  CA  LEU E  11      11.497  11.698 -34.674  1.00 61.50           C  
ANISOU 4114  CA  LEU E  11     9452   7787   6128   1094   -337   1312       C  
ATOM   4115  C   LEU E  11      10.565  11.425 -35.842  1.00 68.69           C  
ANISOU 4115  C   LEU E  11    10374   8897   6829   1395   -513   1269       C  
ATOM   4116  O   LEU E  11       9.555  10.728 -35.688  1.00 70.22           O  
ANISOU 4116  O   LEU E  11    10264   9329   7088   1577   -634   1039       O  
ATOM   4117  CB  LEU E  11      12.418  10.497 -34.409  1.00 63.38           C  
ANISOU 4117  CB  LEU E  11     9366   8245   6472    799   -121   1246       C  
ATOM   4118  CG  LEU E  11      13.898  10.605 -34.791  1.00 67.59           C  
ANISOU 4118  CG  LEU E  11     9993   8779   6910    474     97   1458       C  
ATOM   4119  CD1 LEU E  11      14.548  11.871 -34.320  1.00 69.75           C  
ANISOU 4119  CD1 LEU E  11    10557   8753   7194    254    133   1649       C  
ATOM   4120  CD2 LEU E  11      14.634   9.423 -34.184  1.00 71.92           C  
ANISOU 4120  CD2 LEU E  11    10172   9546   7610    302    272   1343       C  
ATOM   4121  N   ALA E  12      10.895  11.998 -37.000  1.00 62.75           N  
ANISOU 4121  N   ALA E  12     9978   8065   5801   1419   -532   1495       N  
ATOM   4122  CA  ALA E  12      10.185  11.751 -38.249  1.00 64.73           C  
ANISOU 4122  CA  ALA E  12    10285   8522   5788   1674   -698   1488       C  
ATOM   4123  C   ALA E  12      11.171  11.087 -39.195  1.00 72.02           C  
ANISOU 4123  C   ALA E  12    11232   9607   6523   1424   -501   1587       C  
ATOM   4124  O   ALA E  12      12.155  11.711 -39.608  1.00 77.71           O  
ANISOU 4124  O   ALA E  12    12252  10174   7100   1216   -348   1841       O  
ATOM   4125  CB  ALA E  12       9.633  13.044 -38.845  1.00 67.54           C  
ANISOU 4125  CB  ALA E  12    11103   8640   5919   1992   -911   1679       C  
ATOM   4126  N   VAL E  13      10.919   9.825 -39.526  1.00 70.73           N  
ANISOU 4126  N   VAL E  13    10770   9757   6346   1428   -491   1378       N  
ATOM   4127  CA  VAL E  13      11.834   9.037 -40.338  1.00 75.32           C  
ANISOU 4127  CA  VAL E  13    11347  10516   6756   1242   -284   1413       C  
ATOM   4128  C   VAL E  13      11.099   8.499 -41.555  1.00 71.15           C  
ANISOU 4128  C   VAL E  13    10868  10227   5938   1437   -449   1315       C  
ATOM   4129  O   VAL E  13       9.878   8.310 -41.540  1.00 72.09           O  
ANISOU 4129  O   VAL E  13    10852  10467   6071   1652   -706   1134       O  
ATOM   4130  CB  VAL E  13      12.458   7.883 -39.525  1.00 73.07           C  
ANISOU 4130  CB  VAL E  13    10717  10337   6710   1038    -77   1237       C  
ATOM   4131  CG1 VAL E  13      13.319   8.434 -38.401  1.00 72.99           C  
ANISOU 4131  CG1 VAL E  13    10660  10138   6936    823     79   1352       C  
ATOM   4132  CG2 VAL E  13      11.359   6.985 -38.964  1.00 71.41           C  
ANISOU 4132  CG2 VAL E  13    10218  10246   6669   1144   -231    933       C  
ATOM   4133  N   SER E  14      11.856   8.263 -42.621  1.00 73.62           N  
ANISOU 4133  N   SER E  14    11360  10649   5964   1349   -297   1429       N  
ATOM   4134  CA  SER E  14      11.350   7.572 -43.794  1.00 68.60           C  
ANISOU 4134  CA  SER E  14    10779  10263   5021   1482   -412   1309       C  
ATOM   4135  C   SER E  14      11.482   6.066 -43.606  1.00 65.48           C  
ANISOU 4135  C   SER E  14    10109  10045   4725   1377   -296   1016       C  
ATOM   4136  O   SER E  14      12.382   5.587 -42.915  1.00 61.03           O  
ANISOU 4136  O   SER E  14     9394   9436   4360   1206    -45    995       O  
ATOM   4137  CB  SER E  14      12.108   8.010 -45.048  1.00 73.81           C  
ANISOU 4137  CB  SER E  14    11802  10961   5282   1444   -282   1561       C  
ATOM   4138  OG  SER E  14      12.021   9.412 -45.242  1.00 82.18           O  
ANISOU 4138  OG  SER E  14    13210  11790   6225   1514   -384   1856       O  
ATOM   4139  N   LEU E  15      10.558   5.325 -44.217  1.00 65.09           N  
ANISOU 4139  N   LEU E  15    10019  10194   4518   1483   -499    788       N  
ATOM   4140  CA  LEU E  15      10.628   3.867 -44.225  1.00 66.11           C  
ANISOU 4140  CA  LEU E  15    10012  10441   4664   1374   -408    503       C  
ATOM   4141  C   LEU E  15      11.993   3.380 -44.685  1.00 66.63           C  
ANISOU 4141  C   LEU E  15    10206  10522   4588   1290    -69    573       C  
ATOM   4142  O   LEU E  15      12.505   3.814 -45.719  1.00 68.34           O  
ANISOU 4142  O   LEU E  15    10667  10820   4480   1334     15    749       O  
ATOM   4143  CB  LEU E  15       9.547   3.291 -45.141  1.00 70.35           C  
ANISOU 4143  CB  LEU E  15    10592  11206   4934   1456   -681    283       C  
ATOM   4144  CG  LEU E  15       8.114   3.432 -44.659  1.00 71.27           C  
ANISOU 4144  CG  LEU E  15    10460  11433   5187   1523  -1013    125       C  
ATOM   4145  CD1 LEU E  15       7.142   3.127 -45.786  1.00 71.62           C  
ANISOU 4145  CD1 LEU E  15    10563  11770   4880   1612  -1313    -32       C  
ATOM   4146  CD2 LEU E  15       7.941   2.453 -43.522  1.00 66.17           C  
ANISOU 4146  CD2 LEU E  15     9536  10734   4870   1314   -930   -116       C  
ATOM   4147  N   GLY E  16      12.575   2.466 -43.908  1.00 65.18           N  
ANISOU 4147  N   GLY E  16     9855  10282   4628   1190    130    436       N  
ATOM   4148  CA  GLY E  16      13.872   1.908 -44.201  1.00 60.67           C  
ANISOU 4148  CA  GLY E  16     9334   9769   3949   1175    456    468       C  
ATOM   4149  C   GLY E  16      15.040   2.645 -43.584  1.00 62.79           C  
ANISOU 4149  C   GLY E  16     9487   9997   4373   1080    697    728       C  
ATOM   4150  O   GLY E  16      16.170   2.148 -43.653  1.00 74.63           O  
ANISOU 4150  O   GLY E  16    10928  11607   5821   1081    979    744       O  
ATOM   4151  N   GLN E  17      14.808   3.811 -42.988  1.00 65.33           N  
ANISOU 4151  N   GLN E  17     9776  10182   4866   1004    590    918       N  
ATOM   4152  CA  GLN E  17      15.861   4.633 -42.410  1.00 69.63           C  
ANISOU 4152  CA  GLN E  17    10245  10676   5536    842    786   1166       C  
ATOM   4153  C   GLN E  17      16.193   4.166 -40.988  1.00 62.29           C  
ANISOU 4153  C   GLN E  17     9021   9666   4980    767    856   1066       C  
ATOM   4154  O   GLN E  17      15.457   3.392 -40.374  1.00 53.93           O  
ANISOU 4154  O   GLN E  17     7856   8535   4101    830    730    837       O  
ATOM   4155  CB  GLN E  17      15.425   6.101 -42.409  1.00 73.68           C  
ANISOU 4155  CB  GLN E  17    10951  11009   6035    796    623   1399       C  
ATOM   4156  CG  GLN E  17      16.494   7.116 -42.037  1.00 83.93           C  
ANISOU 4156  CG  GLN E  17    12281  12230   7377    551    811   1681       C  
ATOM   4157  CD  GLN E  17      16.198   8.493 -42.603  1.00 91.33           C  
ANISOU 4157  CD  GLN E  17    13602  12982   8118    520    690   1945       C  
ATOM   4158  OE1 GLN E  17      15.116   9.048 -42.390  1.00 83.94           O  
ANISOU 4158  OE1 GLN E  17    12805  11842   7247    689    413   1923       O  
ATOM   4159  NE2 GLN E  17      17.150   9.041 -43.351  1.00 89.93           N  
ANISOU 4159  NE2 GLN E  17    13611  12886   7672    320    904   2199       N  
ATOM   4160  N   ARG E  18      17.336   4.638 -40.473  1.00 62.96           N  
ANISOU 4160  N   ARG E  18     8977   9788   5156    602   1060   1245       N  
ATOM   4161  CA  ARG E  18      17.721   4.440 -39.076  1.00 65.55           C  
ANISOU 4161  CA  ARG E  18     9043  10048   5813    514   1101   1201       C  
ATOM   4162  C   ARG E  18      17.047   5.445 -38.154  1.00 58.58           C  
ANISOU 4162  C   ARG E  18     8191   8912   5155    416    908   1262       C  
ATOM   4163  O   ARG E  18      17.043   6.649 -38.422  1.00 69.14           O  
ANISOU 4163  O   ARG E  18     9722  10138   6409    312    862   1464       O  
ATOM   4164  CB  ARG E  18      19.243   4.531 -38.923  1.00 76.12           C  
ANISOU 4164  CB  ARG E  18    10189  11606   7128    372   1379   1353       C  
ATOM   4165  CG  ARG E  18      19.867   3.256 -38.408  1.00 79.49           C  
ANISOU 4165  CG  ARG E  18    10370  12181   7651    516   1516   1188       C  
ATOM   4166  CD  ARG E  18      21.236   3.405 -37.784  1.00 80.33           C  
ANISOU 4166  CD  ARG E  18    10171  12520   7831    390   1717   1316       C  
ATOM   4167  NE  ARG E  18      22.069   4.278 -38.594  1.00 83.55           N  
ANISOU 4167  NE  ARG E  18    10587  13108   8050    176   1866   1518       N  
ATOM   4168  CZ  ARG E  18      22.976   3.836 -39.456  1.00 94.78           C  
ANISOU 4168  CZ  ARG E  18    11925  14757   9330    239   2041   1474       C  
ATOM   4169  NH1 ARG E  18      23.173   2.541 -39.651  1.00 93.34           N  
ANISOU 4169  NH1 ARG E  18    11667  14677   9120    552   2107   1271       N  
ATOM   4170  NH2 ARG E  18      23.684   4.714 -40.158  1.00 85.62           N  
ANISOU 4170  NH2 ARG E  18    10798  13701   8032    -14   2158   1636       N  
ATOM   4171  N   ALA E  19      16.484   4.945 -37.063  1.00 53.72           N  
ANISOU 4171  N   ALA E  19     7420   8189   4801    454    805   1087       N  
ATOM   4172  CA  ALA E  19      15.993   5.780 -35.979  1.00 55.12           C  
ANISOU 4172  CA  ALA E  19     7580   8156   5206    376    669   1112       C  
ATOM   4173  C   ALA E  19      16.864   5.533 -34.757  1.00 54.48           C  
ANISOU 4173  C   ALA E  19     7271   8091   5340    234    791   1114       C  
ATOM   4174  O   ALA E  19      17.114   4.378 -34.393  1.00 48.47           O  
ANISOU 4174  O   ALA E  19     6346   7425   4645    302    867    977       O  
ATOM   4175  CB  ALA E  19      14.525   5.480 -35.663  1.00 51.38           C  
ANISOU 4175  CB  ALA E  19     7091   7599   4832    528    446    904       C  
ATOM   4176  N   THR E  20      17.342   6.612 -34.138  1.00 48.75           N  
ANISOU 4176  N   THR E  20     6569   7257   4695     38    799   1270       N  
ATOM   4177  CA  THR E  20      18.152   6.504 -32.932  1.00 48.33           C  
ANISOU 4177  CA  THR E  20     6297   7242   4825   -120    876   1275       C  
ATOM   4178  C   THR E  20      17.536   7.362 -31.836  1.00 50.88           C  
ANISOU 4178  C   THR E  20     6702   7305   5327   -197    725   1253       C  
ATOM   4179  O   THR E  20      17.249   8.544 -32.049  1.00 50.52           O  
ANISOU 4179  O   THR E  20     6909   7061   5225   -262    643   1364       O  
ATOM   4180  CB  THR E  20      19.596   6.927 -33.196  1.00 57.00           C  
ANISOU 4180  CB  THR E  20     7299   8544   5814   -356   1064   1475       C  
ATOM   4181  OG1 THR E  20      20.126   6.148 -34.279  1.00 57.13           O  
ANISOU 4181  OG1 THR E  20     7243   8831   5631   -233   1226   1481       O  
ATOM   4182  CG2 THR E  20      20.450   6.690 -31.964  1.00 53.80           C  
ANISOU 4182  CG2 THR E  20     6611   8256   5576   -492   1117   1461       C  
ATOM   4183  N   ILE E  21      17.342   6.761 -30.667  1.00 42.35           N  
ANISOU 4183  N   ILE E  21     5447   6208   4434   -172    694   1108       N  
ATOM   4184  CA  ILE E  21      16.726   7.414 -29.515  1.00 44.75           C  
ANISOU 4184  CA  ILE E  21     5805   6300   4896   -214    572   1045       C  
ATOM   4185  C   ILE E  21      17.709   7.357 -28.355  1.00 45.86           C  
ANISOU 4185  C   ILE E  21     5775   6505   5147   -413    636   1072       C  
ATOM   4186  O   ILE E  21      18.193   6.277 -27.998  1.00 48.16           O  
ANISOU 4186  O   ILE E  21     5850   6972   5477   -367    711   1016       O  
ATOM   4187  CB  ILE E  21      15.388   6.751 -29.141  1.00 51.59           C  
ANISOU 4187  CB  ILE E  21     6624   7126   5853    -10    466    830       C  
ATOM   4188  CG1 ILE E  21      14.435   6.804 -30.339  1.00 53.44           C  
ANISOU 4188  CG1 ILE E  21     6982   7370   5952    182    372    796       C  
ATOM   4189  CG2 ILE E  21      14.782   7.394 -27.890  1.00 43.45           C  
ANISOU 4189  CG2 ILE E  21     5620   5927   4964    -29    374    748       C  
ATOM   4190  CD1 ILE E  21      13.129   6.102 -30.105  1.00 45.35           C  
ANISOU 4190  CD1 ILE E  21     5850   6394   4986    328    269    576       C  
ATOM   4191  N   SER E  22      18.010   8.516 -27.781  1.00 51.22           N  
ANISOU 4191  N   SER E  22     6581   7029   5852   -625    593   1156       N  
ATOM   4192  CA  SER E  22      19.000   8.641 -26.725  1.00 45.74           C  
ANISOU 4192  CA  SER E  22     5734   6419   5226   -869    625   1191       C  
ATOM   4193  C   SER E  22      18.317   8.705 -25.362  1.00 45.82           C  
ANISOU 4193  C   SER E  22     5769   6264   5376   -832    520   1038       C  
ATOM   4194  O   SER E  22      17.198   9.204 -25.232  1.00 45.95           O  
ANISOU 4194  O   SER E  22     5984   6052   5425   -694    425    945       O  
ATOM   4195  CB  SER E  22      19.855   9.890 -26.941  1.00 57.72           C  
ANISOU 4195  CB  SER E  22     7404   7877   6650  -1216    648   1372       C  
ATOM   4196  OG  SER E  22      20.731  10.110 -25.851  1.00 61.19           O  
ANISOU 4196  OG  SER E  22     7696   8410   7144  -1493    640   1383       O  
ATOM   4197  N   CYS E  23      19.008   8.187 -24.346  1.00 36.06           N  
ANISOU 4197  N   CYS E  23     4321   5180   4202   -931    538   1011       N  
ATOM   4198  CA  CYS E  23      18.575   8.319 -22.956  1.00 45.08           C  
ANISOU 4198  CA  CYS E  23     5496   6197   5437   -955    455    886       C  
ATOM   4199  C   CYS E  23      19.820   8.604 -22.129  1.00 52.61           C  
ANISOU 4199  C   CYS E  23     6320   7295   6376  -1243    446    960       C  
ATOM   4200  O   CYS E  23      20.777   7.826 -22.163  1.00 54.95           O  
ANISOU 4200  O   CYS E  23     6338   7895   6644  -1251    507   1025       O  
ATOM   4201  CB  CYS E  23      17.841   7.061 -22.466  1.00 49.89           C  
ANISOU 4201  CB  CYS E  23     5984   6862   6111   -725    466    742       C  
ATOM   4202  SG  CYS E  23      16.936   7.287 -20.899  1.00 55.90           S  
ANISOU 4202  SG  CYS E  23     6831   7461   6946   -721    390    572       S  
ATOM   4203  N   ARG E  24      19.832   9.750 -21.449  1.00 47.45           N  
ANISOU 4203  N   ARG E  24     5874   6438   5717  -1469    364    946       N  
ATOM   4204  CA  ARG E  24      20.901  10.136 -20.535  1.00 46.18           C  
ANISOU 4204  CA  ARG E  24     5616   6404   5525  -1797    316    982       C  
ATOM   4205  C   ARG E  24      20.381  10.102 -19.103  1.00 50.05           C  
ANISOU 4205  C   ARG E  24     6181   6777   6061  -1758    226    822       C  
ATOM   4206  O   ARG E  24      19.403  10.787 -18.785  1.00 50.37           O  
ANISOU 4206  O   ARG E  24     6518   6501   6118  -1681    180    709       O  
ATOM   4207  CB  ARG E  24      21.436  11.529 -20.879  1.00 53.57           C  
ANISOU 4207  CB  ARG E  24     6798   7180   6377  -2178    291   1088       C  
ATOM   4208  CG  ARG E  24      22.417  12.097 -19.859  1.00 63.81           C  
ANISOU 4208  CG  ARG E  24     8046   8574   7624  -2595    210   1092       C  
ATOM   4209  CD  ARG E  24      23.856  11.711 -20.153  1.00 74.54           C  
ANISOU 4209  CD  ARG E  24     8978  10427   8915  -2845    270   1236       C  
ATOM   4210  NE  ARG E  24      24.361  12.263 -21.405  1.00 81.64           N  
ANISOU 4210  NE  ARG E  24     9936  11348   9735  -2979    360   1362       N  
ATOM   4211  CZ  ARG E  24      25.142  13.331 -21.500  1.00 90.74           C  
ANISOU 4211  CZ  ARG E  24    11221  12456  10799  -3338    326   1394       C  
ATOM   4212  NH1 ARG E  24      25.557  13.984 -20.426  1.00 96.57           N  
ANISOU 4212  NH1 ARG E  24    12044  13141  11506  -3618    194   1309       N  
ATOM   4213  NH2 ARG E  24      25.527  13.748 -22.703  1.00 77.18           N  
ANISOU 4213  NH2 ARG E  24     9565  10761   9000  -3435    428   1513       N  
ATOM   4214  N   ALA E  25      21.042   9.316 -18.245  1.00 47.82           N  
ANISOU 4214  N   ALA E  25     5634   6763   5771  -1780    204    815       N  
ATOM   4215  CA  ALA E  25      20.683   9.206 -16.834  1.00 43.53           C  
ANISOU 4215  CA  ALA E  25     5155   6157   5228  -1767    125    682       C  
ATOM   4216  C   ALA E  25      21.511  10.171 -15.988  1.00 48.66           C  
ANISOU 4216  C   ALA E  25     5872   6820   5796  -2152     11    680       C  
ATOM   4217  O   ALA E  25      22.694  10.396 -16.254  1.00 49.83           O  
ANISOU 4217  O   ALA E  25     5828   7218   5888  -2428    -10    801       O  
ATOM   4218  CB  ALA E  25      20.887   7.774 -16.334  1.00 45.41           C  
ANISOU 4218  CB  ALA E  25     5140   6647   5467  -1556    145    685       C  
ATOM   4219  N   SER E  26      20.879  10.732 -14.958  1.00 52.81           N  
ANISOU 4219  N   SER E  26     6663   7105   6296  -2185    -58    528       N  
ATOM   4220  CA  SER E  26      21.564  11.674 -14.079  1.00 53.18           C  
ANISOU 4220  CA  SER E  26     6849   7117   6241  -2568   -184    487       C  
ATOM   4221  C   SER E  26      22.655  11.016 -13.237  1.00 55.47           C  
ANISOU 4221  C   SER E  26     6800   7823   6453  -2710   -275    532       C  
ATOM   4222  O   SER E  26      23.509  11.728 -12.700  1.00 56.80           O  
ANISOU 4222  O   SER E  26     6979   8084   6520  -3103   -396    529       O  
ATOM   4223  CB  SER E  26      20.545  12.375 -13.178  1.00 57.77           C  
ANISOU 4223  CB  SER E  26     7827   7335   6788  -2498   -222    285       C  
ATOM   4224  OG  SER E  26      19.909  11.446 -12.309  1.00 50.87           O  
ANISOU 4224  OG  SER E  26     6851   6562   5914  -2232   -193    184       O  
ATOM   4225  N   GLU E  27      22.638   9.690 -13.089  1.00 47.90           N  
ANISOU 4225  N   GLU E  27     5571   7108   5520  -2401   -235    569       N  
ATOM   4226  CA  GLU E  27      23.749   8.968 -12.479  1.00 51.32           C  
ANISOU 4226  CA  GLU E  27     5659   7974   5867  -2439   -329    648       C  
ATOM   4227  C   GLU E  27      23.788   7.563 -13.070  1.00 46.29           C  
ANISOU 4227  C   GLU E  27     4772   7534   5283  -2044   -230    746       C  
ATOM   4228  O   GLU E  27      22.867   7.141 -13.764  1.00 46.65           O  
ANISOU 4228  O   GLU E  27     4939   7365   5423  -1794   -101    724       O  
ATOM   4229  CB  GLU E  27      23.627   8.925 -10.948  1.00 58.31           C  
ANISOU 4229  CB  GLU E  27     6664   8857   6635  -2481   -457    535       C  
ATOM   4230  CG  GLU E  27      22.227   8.630 -10.449  1.00 55.06           C  
ANISOU 4230  CG  GLU E  27     6544   8126   6252  -2219   -372    400       C  
ATOM   4231  CD  GLU E  27      22.113   8.675  -8.937  1.00 71.09           C  
ANISOU 4231  CD  GLU E  27     8723  10161   8126  -2288   -477    286       C  
ATOM   4232  OE1 GLU E  27      22.642   7.762  -8.261  1.00 71.74           O  
ANISOU 4232  OE1 GLU E  27     8633  10516   8108  -2187   -552    357       O  
ATOM   4233  OE2 GLU E  27      21.498   9.633  -8.425  1.00 69.54           O1-
ANISOU 4233  OE2 GLU E  27     8846   9690   7885  -2416   -488    125       O1-
ATOM   4234  N   SER E  28      24.874   6.845 -12.789  1.00 47.53           N  
ANISOU 4234  N   SER E  28     4589   8111   5360  -1980   -302    845       N  
ATOM   4235  CA  SER E  28      25.080   5.515 -13.358  1.00 48.61           C  
ANISOU 4235  CA  SER E  28     4525   8429   5516  -1575   -216    937       C  
ATOM   4236  C   SER E  28      23.992   4.534 -12.924  1.00 44.18           C  
ANISOU 4236  C   SER E  28     4220   7589   4977  -1255   -160    873       C  
ATOM   4237  O   SER E  28      23.622   4.471 -11.747  1.00 53.55           O  
ANISOU 4237  O   SER E  28     5574   8683   6091  -1281   -239    807       O  
ATOM   4238  CB  SER E  28      26.452   4.986 -12.942  1.00 53.33           C  
ANISOU 4238  CB  SER E  28     4725   9548   5991  -1511   -335   1042       C  
ATOM   4239  OG  SER E  28      26.673   3.693 -13.475  1.00 55.89           O  
ANISOU 4239  OG  SER E  28     4911  10013   6313  -1055   -252   1121       O  
ATOM   4240  N   VAL E  29      23.484   3.756 -13.878  1.00 41.98           N  
ANISOU 4240  N   VAL E  29     3986   7189   4773   -985    -18    890       N  
ATOM   4241  CA  VAL E  29      22.498   2.730 -13.560  1.00 44.60           C  
ANISOU 4241  CA  VAL E  29     4557   7278   5110   -740     46    837       C  
ATOM   4242  C   VAL E  29      23.193   1.373 -13.594  1.00 51.57           C  
ANISOU 4242  C   VAL E  29     5342   8338   5913   -396     44    941       C  
ATOM   4243  O   VAL E  29      22.551   0.324 -13.744  1.00 47.27           O  
ANISOU 4243  O   VAL E  29     5007   7586   5365   -170    127    926       O  
ATOM   4244  CB  VAL E  29      21.286   2.782 -14.513  1.00 47.58           C  
ANISOU 4244  CB  VAL E  29     5113   7363   5603   -705    186    753       C  
ATOM   4245  CG1 VAL E  29      20.614   4.153 -14.430  1.00 43.13           C  
ANISOU 4245  CG1 VAL E  29     4674   6619   5095   -960    171    653       C  
ATOM   4246  CG2 VAL E  29      21.667   2.403 -15.931  1.00 37.66           C  
ANISOU 4246  CG2 VAL E  29     3726   6199   4385   -550    277    820       C  
ATOM   4247  N   GLU E  30      24.511   1.385 -13.415  1.00 48.19           N  
ANISOU 4247  N   GLU E  30     4609   8301   5401   -354    -60   1042       N  
ATOM   4248  CA  GLU E  30      25.293   0.161 -13.407  1.00 51.92           C  
ANISOU 4248  CA  GLU E  30     4972   8985   5772     53    -84   1142       C  
ATOM   4249  C   GLU E  30      25.207  -0.500 -12.025  1.00 46.46           C  
ANISOU 4249  C   GLU E  30     4479   8230   4944    179   -209   1167       C  
ATOM   4250  O   GLU E  30      24.943   0.152 -11.014  1.00 46.56           O  
ANISOU 4250  O   GLU E  30     4574   8202   4914    -90   -307   1119       O  
ATOM   4251  CB  GLU E  30      26.748   0.452 -13.759  1.00 51.10           C  
ANISOU 4251  CB  GLU E  30     4390   9416   5609     76   -148   1235       C  
ATOM   4252  CG  GLU E  30      26.881   0.942 -15.177  1.00 48.71           C  
ANISOU 4252  CG  GLU E  30     3922   9188   5396    -20      6   1237       C  
ATOM   4253  CD  GLU E  30      26.633  -0.144 -16.204  1.00 67.72           C  
ANISOU 4253  CD  GLU E  30     6449  11465   7816    389    165   1238       C  
ATOM   4254  OE1 GLU E  30      26.753  -1.329 -15.835  1.00 64.59           O  
ANISOU 4254  OE1 GLU E  30     6176  11030   7335    792    140   1265       O  
ATOM   4255  OE2 GLU E  30      26.325   0.192 -17.368  1.00 67.88           O1-
ANISOU 4255  OE2 GLU E  30     6481  11403   7907    308    306   1212       O1-
ATOM   4256  N   TYR E  30A     25.445  -1.815 -12.003  1.00 45.68           N  
ANISOU 4256  N   TYR E  30A    4501   8104   4751    607   -203   1245       N  
ATOM   4257  CA  TYR E  30A     25.366  -2.641 -10.799  1.00 42.76           C  
ANISOU 4257  CA  TYR E  30A    4405   7628   4216    790   -309   1305       C  
ATOM   4258  C   TYR E  30A     26.211  -3.893 -11.023  1.00 47.94           C  
ANISOU 4258  C   TYR E  30A    5056   8412   4746   1343   -343   1426       C  
ATOM   4259  O   TYR E  30A     26.565  -4.218 -12.158  1.00 48.37           O  
ANISOU 4259  O   TYR E  30A    4976   8546   4858   1576   -237   1426       O  
ATOM   4260  CB  TYR E  30A     23.908  -2.993 -10.489  1.00 49.49           C  
ANISOU 4260  CB  TYR E  30A    5732   7978   5094    645   -186   1226       C  
ATOM   4261  CG  TYR E  30A     23.609  -3.387  -9.061  1.00 54.85           C  
ANISOU 4261  CG  TYR E  30A    6710   8538   5593    621   -276   1268       C  
ATOM   4262  CD1 TYR E  30A     23.766  -2.484  -8.009  1.00 50.42           C  
ANISOU 4262  CD1 TYR E  30A    6048   8155   4955    355   -410   1239       C  
ATOM   4263  CD2 TYR E  30A     23.127  -4.654  -8.770  1.00 58.45           C  
ANISOU 4263  CD2 TYR E  30A    7605   8672   5931    832   -217   1332       C  
ATOM   4264  CE1 TYR E  30A     23.468  -2.857  -6.696  1.00 54.96           C  
ANISOU 4264  CE1 TYR E  30A    6923   8630   5329    333   -481   1278       C  
ATOM   4265  CE2 TYR E  30A     22.823  -5.029  -7.471  1.00 51.62           C  
ANISOU 4265  CE2 TYR E  30A    7058   7688   4869    784   -279   1390       C  
ATOM   4266  CZ  TYR E  30A     22.999  -4.128  -6.442  1.00 55.52           C  
ANISOU 4266  CZ  TYR E  30A    7416   8401   5280    548   -409   1364       C  
ATOM   4267  OH  TYR E  30A     22.702  -4.512  -5.157  1.00 61.10           O  
ANISOU 4267  OH  TYR E  30A    8455   9005   5755    506   -462   1424       O  
ATOM   4268  N   TYR E  30B     26.549  -4.589  -9.937  1.00 53.81           N  
ANISOU 4268  N   TYR E  30B    5973   9180   5292   1587   -494   1527       N  
ATOM   4269  CA  TYR E  30B     27.354  -5.800 -10.097  1.00 56.15           C  
ANISOU 4269  CA  TYR E  30B    6323   9570   5442   2197   -545   1646       C  
ATOM   4270  C   TYR E  30B     26.646  -6.814 -10.986  1.00 55.06           C  
ANISOU 4270  C   TYR E  30B    6622   8950   5350   2419   -346   1612       C  
ATOM   4271  O   TYR E  30B     25.589  -7.341 -10.618  1.00 57.46           O  
ANISOU 4271  O   TYR E  30B    7445   8759   5628   2286   -270   1592       O  
ATOM   4272  CB  TYR E  30B     27.680  -6.443  -8.748  1.00 53.68           C  
ANISOU 4272  CB  TYR E  30B    6246   9270   4878   2444   -749   1777       C  
ATOM   4273  CG  TYR E  30B     28.648  -7.617  -8.836  1.00 63.43           C  
ANISOU 4273  CG  TYR E  30B    7520  10650   5930   3161   -845   1912       C  
ATOM   4274  CD1 TYR E  30B     30.024  -7.409  -8.878  1.00 61.89           C  
ANISOU 4274  CD1 TYR E  30B    6740  11115   5660   3459  -1006   1966       C  
ATOM   4275  CD2 TYR E  30B     28.186  -8.930  -8.857  1.00 67.44           C  
ANISOU 4275  CD2 TYR E  30B    8666  10634   6326   3530   -772   1974       C  
ATOM   4276  CE1 TYR E  30B     30.916  -8.481  -8.943  1.00 66.69           C  
ANISOU 4276  CE1 TYR E  30B    7411  11756   6172   4012  -1016   1973       C  
ATOM   4277  CE2 TYR E  30B     29.071 -10.010  -8.926  1.00 68.50           C  
ANISOU 4277  CE2 TYR E  30B    8902  10801   6324   4152   -829   2032       C  
ATOM   4278  CZ  TYR E  30B     30.432  -9.776  -8.965  1.00 67.87           C  
ANISOU 4278  CZ  TYR E  30B    8230  11325   6234   4379   -935   2006       C  
ATOM   4279  OH  TYR E  30B     31.302 -10.842  -9.029  1.00 73.12           O  
ANISOU 4279  OH  TYR E  30B    8997  12008   6778   4936   -947   2004       O  
ATOM   4280  N   GLY E  30C     27.219  -7.088 -12.154  1.00 50.78           N  
ANISOU 4280  N   GLY E  30C    5872   8569   4854   2728   -255   1595       N  
ATOM   4281  CA  GLY E  30C     26.729  -8.119 -13.042  1.00 55.58           C  
ANISOU 4281  CA  GLY E  30C    6900   8754   5462   2997    -89   1550       C  
ATOM   4282  C   GLY E  30C     25.568  -7.733 -13.933  1.00 63.51           C  
ANISOU 4282  C   GLY E  30C    8042   9437   6652   2579    101   1403       C  
ATOM   4283  O   GLY E  30C     25.107  -8.576 -14.714  1.00 58.87           O  
ANISOU 4283  O   GLY E  30C    7816   8498   6054   2744    230   1343       O  
ATOM   4284  N   THR E  30D     25.092  -6.492 -13.866  1.00 49.40           N  
ANISOU 4284  N   THR E  30D    5997   7758   5016   2066    111   1336       N  
ATOM   4285  CA  THR E  30D     23.919  -6.107 -14.636  1.00 51.51           C  
ANISOU 4285  CA  THR E  30D    6395   7739   5439   1709    262   1201       C  
ATOM   4286  C   THR E  30D     23.962  -4.606 -14.882  1.00 52.30           C  
ANISOU 4286  C   THR E  30D    6072   8118   5681   1325    254   1156       C  
ATOM   4287  O   THR E  30D     24.713  -3.875 -14.233  1.00 57.47           O  
ANISOU 4287  O   THR E  30D    6413   9111   6312   1227    128   1215       O  
ATOM   4288  CB  THR E  30D     22.621  -6.524 -13.915  1.00 54.13           C  
ANISOU 4288  CB  THR E  30D    7195   7620   5751   1455    298   1153       C  
ATOM   4289  OG1 THR E  30D     21.477  -6.178 -14.712  1.00 52.30           O  
ANISOU 4289  OG1 THR E  30D    7029   7185   5658   1142    430   1012       O  
ATOM   4290  CG2 THR E  30D     22.523  -5.868 -12.544  1.00 49.47           C  
ANISOU 4290  CG2 THR E  30D    6546   7130   5121   1199    183   1191       C  
ATOM   4291  N   THR E  31      23.182  -4.170 -15.868  1.00 45.68           N  
ANISOU 4291  N   THR E  31     5254   7132   4970   1114    377   1052       N  
ATOM   4292  CA  THR E  31      22.884  -2.762 -16.105  1.00 45.90           C  
ANISOU 4292  CA  THR E  31     5049   7266   5126    729    380   1000       C  
ATOM   4293  C   THR E  31      21.377  -2.607 -15.997  1.00 51.12           C  
ANISOU 4293  C   THR E  31     5988   7570   5865    468    438    879       C  
ATOM   4294  O   THR E  31      20.630  -3.409 -16.562  1.00 50.52           O  
ANISOU 4294  O   THR E  31     6163   7245   5789    540    530    814       O  
ATOM   4295  CB  THR E  31      23.382  -2.302 -17.478  1.00 52.22           C  
ANISOU 4295  CB  THR E  31     5594   8274   5975    758    466   1004       C  
ATOM   4296  OG1 THR E  31      24.787  -2.568 -17.591  1.00 53.40           O  
ANISOU 4296  OG1 THR E  31     5436   8826   6029   1030    438   1108       O  
ATOM   4297  CG2 THR E  31      23.127  -0.807 -17.681  1.00 49.68           C  
ANISOU 4297  CG2 THR E  31     5110   8011   5756    359    455    978       C  
ATOM   4298  N   LEU E  32      20.919  -1.617 -15.244  1.00 46.10           N  
ANISOU 4298  N   LEU E  32     5312   6929   5277    171    385    836       N  
ATOM   4299  CA  LEU E  32      19.498  -1.571 -14.900  1.00 45.80           C  
ANISOU 4299  CA  LEU E  32     5503   6623   5278    -26    442    716       C  
ATOM   4300  C   LEU E  32      18.766  -0.541 -15.756  1.00 44.35           C  
ANISOU 4300  C   LEU E  32     5229   6403   5218   -198    488    618       C  
ATOM   4301  O   LEU E  32      18.189   0.427 -15.271  1.00 42.85           O  
ANISOU 4301  O   LEU E  32     5029   6182   5070   -392    464    545       O  
ATOM   4302  CB  LEU E  32      19.330  -1.314 -13.408  1.00 40.51           C  
ANISOU 4302  CB  LEU E  32     4912   5948   4534   -171    372    713       C  
ATOM   4303  CG  LEU E  32      20.007  -2.468 -12.657  1.00 52.85           C  
ANISOU 4303  CG  LEU E  32     6623   7518   5940     52    316    832       C  
ATOM   4304  CD1 LEU E  32      20.401  -2.047 -11.256  1.00 53.32           C  
ANISOU 4304  CD1 LEU E  32     6666   7708   5887    -46    191    873       C  
ATOM   4305  CD2 LEU E  32      19.139  -3.741 -12.641  1.00 46.16           C  
ANISOU 4305  CD2 LEU E  32     6148   6363   5029    104    422    812       C  
ATOM   4306  N   MET E  33      18.791  -0.794 -17.069  1.00 40.51           N  
ANISOU 4306  N   MET E  33     4712   5914   4766    -84    551    615       N  
ATOM   4307  CA  MET E  33      18.181   0.075 -18.065  1.00 37.95           C  
ANISOU 4307  CA  MET E  33     4329   5566   4526   -184    579    549       C  
ATOM   4308  C   MET E  33      17.324  -0.757 -19.010  1.00 42.11           C  
ANISOU 4308  C   MET E  33     4996   5955   5048   -106    655    463       C  
ATOM   4309  O   MET E  33      17.801  -1.748 -19.569  1.00 44.53           O  
ANISOU 4309  O   MET E  33     5376   6252   5291     78    699    494       O  
ATOM   4310  CB  MET E  33      19.264   0.837 -18.847  1.00 40.86           C  
ANISOU 4310  CB  MET E  33     4490   6136   4900   -177    566    652       C  
ATOM   4311  CG  MET E  33      18.748   1.661 -20.025  1.00 42.77           C  
ANISOU 4311  CG  MET E  33     4732   6332   5187   -244    595    622       C  
ATOM   4312  SD  MET E  33      17.635   2.984 -19.489  1.00 54.64           S  
ANISOU 4312  SD  MET E  33     6331   7667   6762   -440    531    523       S  
ATOM   4313  CE  MET E  33      18.570   3.791 -18.195  1.00 45.89           C  
ANISOU 4313  CE  MET E  33     5159   6641   5637   -629    444    583       C  
ATOM   4314  N   GLN E  34      16.074  -0.333 -19.209  1.00 37.17           N  
ANISOU 4314  N   GLN E  34     4404   5245   4473   -233    661    342       N  
ATOM   4315  CA  GLN E  34      15.110  -0.988 -20.083  1.00 34.48           C  
ANISOU 4315  CA  GLN E  34     4160   4823   4118   -228    704    233       C  
ATOM   4316  C   GLN E  34      14.594  -0.009 -21.138  1.00 37.35           C  
ANISOU 4316  C   GLN E  34     4424   5246   4523   -232    670    190       C  
ATOM   4317  O   GLN E  34      14.598   1.208 -20.938  1.00 36.02           O  
ANISOU 4317  O   GLN E  34     4171   5112   4404   -274    622    214       O  
ATOM   4318  CB  GLN E  34      13.931  -1.531 -19.273  1.00 34.21           C  
ANISOU 4318  CB  GLN E  34     4228   4700   4070   -391    735    116       C  
ATOM   4319  CG  GLN E  34      14.234  -2.857 -18.560  1.00 33.30           C  
ANISOU 4319  CG  GLN E  34     4341   4447   3863   -388    782    157       C  
ATOM   4320  CD  GLN E  34      15.279  -2.697 -17.473  1.00 41.91           C  
ANISOU 4320  CD  GLN E  34     5420   5576   4927   -312    743    289       C  
ATOM   4321  OE1 GLN E  34      16.278  -3.418 -17.476  1.00 40.15           O  
ANISOU 4321  OE1 GLN E  34     5288   5330   4637   -119    734    393       O  
ATOM   4322  NE2 GLN E  34      15.060  -1.758 -16.533  1.00 34.79           N  
ANISOU 4322  NE2 GLN E  34     4410   4751   4057   -437    711    273       N  
ATOM   4323  N   TRP E  35      14.084  -0.557 -22.246  1.00 35.42           N  
ANISOU 4323  N   TRP E  35     4236   4989   4233   -188    685    120       N  
ATOM   4324  CA  TRP E  35      13.441   0.236 -23.292  1.00 33.25           C  
ANISOU 4324  CA  TRP E  35     3897   4777   3960   -165    631     75       C  
ATOM   4325  C   TRP E  35      12.071  -0.360 -23.575  1.00 38.26           C  
ANISOU 4325  C   TRP E  35     4549   5423   4566   -250    612    -98       C  
ATOM   4326  O   TRP E  35      11.946  -1.582 -23.716  1.00 42.06           O  
ANISOU 4326  O   TRP E  35     5164   5834   4982   -305    656   -161       O  
ATOM   4327  CB  TRP E  35      14.256   0.249 -24.593  1.00 34.98           C  
ANISOU 4327  CB  TRP E  35     4138   5049   4103    -35    652    162       C  
ATOM   4328  CG  TRP E  35      15.500   1.095 -24.581  1.00 37.26           C  
ANISOU 4328  CG  TRP E  35     4344   5412   4401    -10    670    331       C  
ATOM   4329  CD1 TRP E  35      16.785   0.662 -24.396  1.00 42.31           C  
ANISOU 4329  CD1 TRP E  35     4931   6136   5008     57    736    437       C  
ATOM   4330  CD2 TRP E  35      15.580   2.516 -24.770  1.00 39.93           C  
ANISOU 4330  CD2 TRP E  35     4648   5762   4762    -70    618    412       C  
ATOM   4331  NE1 TRP E  35      17.658   1.726 -24.463  1.00 44.37           N  
ANISOU 4331  NE1 TRP E  35     5074   6511   5273    -15    734    573       N  
ATOM   4332  CE2 TRP E  35      16.943   2.874 -24.688  1.00 41.48           C  
ANISOU 4332  CE2 TRP E  35     4762   6060   4939   -114    666    564       C  
ATOM   4333  CE3 TRP E  35      14.631   3.518 -25.012  1.00 35.19           C  
ANISOU 4333  CE3 TRP E  35     4095   5096   4180    -76    532    369       C  
ATOM   4334  CZ2 TRP E  35      17.382   4.195 -24.831  1.00 39.83           C  
ANISOU 4334  CZ2 TRP E  35     4557   5851   4725   -246    638    678       C  
ATOM   4335  CZ3 TRP E  35      15.063   4.824 -25.140  1.00 38.09           C  
ANISOU 4335  CZ3 TRP E  35     4517   5414   4541   -133    498    486       C  
ATOM   4336  CH2 TRP E  35      16.429   5.151 -25.055  1.00 43.20           C  
ANISOU 4336  CH2 TRP E  35     5121   6126   5166   -256    556    641       C  
ATOM   4337  N   TYR E  36      11.054   0.501 -23.675  1.00 37.58           N  
ANISOU 4337  N   TYR E  36     4338   5432   4509   -257    539   -180       N  
ATOM   4338  CA  TYR E  36       9.668   0.094 -23.885  1.00 33.28           C  
ANISOU 4338  CA  TYR E  36     3709   5005   3932   -354    503   -356       C  
ATOM   4339  C   TYR E  36       9.120   0.697 -25.173  1.00 39.98           C  
ANISOU 4339  C   TYR E  36     4488   5980   4724   -221    388   -393       C  
ATOM   4340  O   TYR E  36       9.508   1.795 -25.576  1.00 40.90           O  
ANISOU 4340  O   TYR E  36     4614   6077   4848    -55    334   -286       O  
ATOM   4341  CB  TYR E  36       8.764   0.536 -22.710  1.00 38.90           C  
ANISOU 4341  CB  TYR E  36     4268   5813   4700   -436    516   -451       C  
ATOM   4342  CG  TYR E  36       8.931  -0.330 -21.500  1.00 33.20           C  
ANISOU 4342  CG  TYR E  36     3632   5005   3979   -626    627   -452       C  
ATOM   4343  CD1 TYR E  36       9.885  -0.031 -20.536  1.00 35.90           C  
ANISOU 4343  CD1 TYR E  36     4053   5228   4357   -593    666   -331       C  
ATOM   4344  CD2 TYR E  36       8.169  -1.489 -21.340  1.00 44.51           C  
ANISOU 4344  CD2 TYR E  36     5099   6469   5346   -867    685   -566       C  
ATOM   4345  CE1 TYR E  36      10.050  -0.849 -19.409  1.00 40.23           C  
ANISOU 4345  CE1 TYR E  36     4718   5697   4872   -743    752   -313       C  
ATOM   4346  CE2 TYR E  36       8.330  -2.313 -20.233  1.00 40.85           C  
ANISOU 4346  CE2 TYR E  36     4788   5886   4848  -1051    791   -540       C  
ATOM   4347  CZ  TYR E  36       9.275  -1.981 -19.268  1.00 45.75           C  
ANISOU 4347  CZ  TYR E  36     5491   6391   5500   -960    819   -407       C  
ATOM   4348  OH  TYR E  36       9.461  -2.786 -18.159  1.00 47.32           O  
ANISOU 4348  OH  TYR E  36     5873   6472   5635  -1111    906   -362       O  
ATOM   4349  N   GLN E  37       8.198  -0.025 -25.807  1.00 39.35           N  
ANISOU 4349  N   GLN E  37     4362   6027   4563   -318    341   -541       N  
ATOM   4350  CA  GLN E  37       7.429   0.479 -26.938  1.00 41.41           C  
ANISOU 4350  CA  GLN E  37     4519   6475   4741   -197    198   -606       C  
ATOM   4351  C   GLN E  37       5.962   0.570 -26.525  1.00 45.02           C  
ANISOU 4351  C   GLN E  37     4697   7206   5203   -276    132   -789       C  
ATOM   4352  O   GLN E  37       5.437  -0.338 -25.872  1.00 45.07           O  
ANISOU 4352  O   GLN E  37     4642   7272   5210   -548    207   -908       O  
ATOM   4353  CB  GLN E  37       7.567  -0.446 -28.158  1.00 46.32           C  
ANISOU 4353  CB  GLN E  37     5290   7090   5220   -249    170   -653       C  
ATOM   4354  CG  GLN E  37       6.748  -0.036 -29.383  1.00 47.27           C  
ANISOU 4354  CG  GLN E  37     5314   7435   5210   -138     -4   -728       C  
ATOM   4355  CD  GLN E  37       6.676  -1.147 -30.426  1.00 47.29           C  
ANISOU 4355  CD  GLN E  37     5472   7451   5044   -266    -34   -838       C  
ATOM   4356  OE1 GLN E  37       5.974  -2.135 -30.228  1.00 46.08           O  
ANISOU 4356  OE1 GLN E  37     5297   7358   4855   -540    -35  -1012       O  
ATOM   4357  NE2 GLN E  37       7.433  -1.008 -31.523  1.00 49.68           N  
ANISOU 4357  NE2 GLN E  37     5964   7689   5224    -98    -43   -741       N  
ATOM   4358  N   GLN E  38       5.290   1.658 -26.900  1.00 41.57           N  
ANISOU 4358  N   GLN E  38     4095   6950   4749    -35     -1   -808       N  
ATOM   4359  CA  GLN E  38       3.870   1.787 -26.582  1.00 39.48           C  
ANISOU 4359  CA  GLN E  38     3492   7039   4468    -46    -69   -995       C  
ATOM   4360  C   GLN E  38       3.131   2.375 -27.771  1.00 45.04           C  
ANISOU 4360  C   GLN E  38     4063   7996   5054    206   -282  -1042       C  
ATOM   4361  O   GLN E  38       3.477   3.455 -28.260  1.00 44.84           O  
ANISOU 4361  O   GLN E  38     4171   7857   5011    534   -373   -909       O  
ATOM   4362  CB  GLN E  38       3.641   2.645 -25.335  1.00 38.57           C  
ANISOU 4362  CB  GLN E  38     3260   6939   4456     82     -1  -1002       C  
ATOM   4363  CG  GLN E  38       2.182   2.651 -24.887  1.00 38.58           C  
ANISOU 4363  CG  GLN E  38     2855   7376   4427     63    -24  -1215       C  
ATOM   4364  CD  GLN E  38       1.917   3.685 -23.826  1.00 49.82           C  
ANISOU 4364  CD  GLN E  38     4184   8831   5915    304     31  -1238       C  
ATOM   4365  OE1 GLN E  38       2.572   4.733 -23.795  1.00 44.16           O  
ANISOU 4365  OE1 GLN E  38     3700   7841   5239    589     -5  -1108       O  
ATOM   4366  NE2 GLN E  38       0.944   3.414 -22.951  1.00 51.67           N  
ANISOU 4366  NE2 GLN E  38     4096   9401   6137    174    126  -1410       N  
ATOM   4367  N   LYS E  39       2.121   1.665 -28.224  1.00 45.85           N  
ANISOU 4367  N   LYS E  39     3926   8439   5057     32   -371  -1225       N  
ATOM   4368  CA  LYS E  39       1.153   2.110 -29.209  1.00 47.07           C  
ANISOU 4368  CA  LYS E  39     3849   8963   5074    250   -603  -1317       C  
ATOM   4369  C   LYS E  39      -0.066   2.690 -28.494  1.00 65.56           C  
ANISOU 4369  C   LYS E  39     5749  11720   7441    403   -647  -1466       C  
ATOM   4370  O   LYS E  39      -0.473   2.170 -27.449  1.00 59.11           O  
ANISOU 4370  O   LYS E  39     4732  11036   6693    126   -494  -1580       O  
ATOM   4371  CB  LYS E  39       0.746   0.940 -30.097  1.00 55.52           C  
ANISOU 4371  CB  LYS E  39     4883  10220   5994    -76   -686  -1460       C  
ATOM   4372  CG  LYS E  39       1.880   0.538 -31.031  1.00 60.23           C  
ANISOU 4372  CG  LYS E  39     5912  10458   6513    -93   -669  -1329       C  
ATOM   4373  CD  LYS E  39       2.083  -0.966 -31.060  1.00 60.78           C  
ANISOU 4373  CD  LYS E  39     6156  10402   6535   -543   -564  -1439       C  
ATOM   4374  CE  LYS E  39       2.925  -1.385 -32.263  1.00 65.73           C  
ANISOU 4374  CE  LYS E  39     7153  10807   7014   -498   -589  -1375       C  
ATOM   4375  NZ  LYS E  39       2.502  -0.764 -33.553  1.00 70.26           N  
ANISOU 4375  NZ  LYS E  39     7668  11628   7399   -247   -824  -1379       N  
ATOM   4376  N   PRO E  40      -0.627   3.781 -29.018  1.00 71.97           N  
ANISOU 4376  N   PRO E  40     6430  12736   8180    871   -843  -1457       N  
ATOM   4377  CA  PRO E  40      -1.755   4.442 -28.341  1.00 73.04           C  
ANISOU 4377  CA  PRO E  40     6140  13286   8324   1136   -882  -1603       C  
ATOM   4378  C   PRO E  40      -2.905   3.499 -28.008  1.00 69.59           C  
ANISOU 4378  C   PRO E  40     5252  13350   7839    754   -835  -1836       C  
ATOM   4379  O   PRO E  40      -3.462   2.842 -28.894  1.00 72.11           O  
ANISOU 4379  O   PRO E  40     5467  13906   8026    551   -954  -1920       O  
ATOM   4380  CB  PRO E  40      -2.191   5.515 -29.346  1.00 80.91           C  
ANISOU 4380  CB  PRO E  40     7125  14432   9185   1703  -1158  -1554       C  
ATOM   4381  CG  PRO E  40      -1.067   5.663 -30.323  1.00 71.89           C  
ANISOU 4381  CG  PRO E  40     6499  12825   7992   1738  -1210  -1326       C  
ATOM   4382  CD  PRO E  40      -0.087   4.554 -30.150  1.00 77.14           C  
ANISOU 4382  CD  PRO E  40     7398  13176   8735   1223  -1007  -1278       C  
ATOM   4383  N   GLY E  41      -3.268   3.429 -26.729  1.00 69.21           N  
ANISOU 4383  N   GLY E  41     5077  13350   7871    613   -621  -1903       N  
ATOM   4384  CA  GLY E  41      -4.349   2.579 -26.289  1.00 57.30           C  
ANISOU 4384  CA  GLY E  41     3299  12182   6290    213   -513  -2061       C  
ATOM   4385  C   GLY E  41      -3.943   1.196 -25.831  1.00 55.59           C  
ANISOU 4385  C   GLY E  41     3219  11800   6103   -433   -329  -2080       C  
ATOM   4386  O   GLY E  41      -4.823   0.365 -25.556  1.00 65.39           O  
ANISOU 4386  O   GLY E  41     4300  13289   7255   -825   -243  -2195       O  
ATOM   4387  N   GLN E  42      -2.654   0.918 -25.748  1.00 56.20           N  
ANISOU 4387  N   GLN E  42     3608  11463   6283   -551   -265  -1966       N  
ATOM   4388  CA  GLN E  42      -2.123  -0.366 -25.330  1.00 57.74           C  
ANISOU 4388  CA  GLN E  42     4039  11406   6496  -1111    -96  -1959       C  
ATOM   4389  C   GLN E  42      -1.124  -0.128 -24.213  1.00 58.37           C  
ANISOU 4389  C   GLN E  42     4387  11078   6713  -1062    100  -1815       C  
ATOM   4390  O   GLN E  42      -0.550   0.963 -24.104  1.00 50.80           O  
ANISOU 4390  O   GLN E  42     3555   9913   5834   -619     69  -1690       O  
ATOM   4391  CB  GLN E  42      -1.432  -1.083 -26.499  1.00 58.98           C  
ANISOU 4391  CB  GLN E  42     4520  11301   6588  -1266   -207  -1917       C  
ATOM   4392  CG  GLN E  42      -2.038  -2.429 -26.841  1.00 65.17           C  
ANISOU 4392  CG  GLN E  42     5303  12220   7241  -1829   -203  -2070       C  
ATOM   4393  CD  GLN E  42      -1.240  -3.157 -27.900  1.00 68.88           C  
ANISOU 4393  CD  GLN E  42     6200  12343   7629  -1949   -286  -2037       C  
ATOM   4394  OE1 GLN E  42      -0.211  -2.660 -28.373  1.00 65.09           O  
ANISOU 4394  OE1 GLN E  42     6026  11512   7192  -1578   -312  -1863       O  
ATOM   4395  NE2 GLN E  42      -1.732  -4.315 -28.315  1.00 67.14           N  
ANISOU 4395  NE2 GLN E  42     6056  12182   7270  -2433   -306  -2184       N  
ATOM   4396  N   PRO E  43      -0.892  -1.125 -23.364  1.00 52.60           N  
ANISOU 4396  N   PRO E  43     3825  10174   5988  -1510    298  -1808       N  
ATOM   4397  CA  PRO E  43       0.163  -1.008 -22.351  1.00 49.29           C  
ANISOU 4397  CA  PRO E  43     3746   9314   5666  -1456    461  -1640       C  
ATOM   4398  C   PRO E  43       1.527  -0.923 -23.012  1.00 48.22           C  
ANISOU 4398  C   PRO E  43     4042   8694   5585  -1247    396  -1447       C  
ATOM   4399  O   PRO E  43       1.686  -1.322 -24.176  1.00 48.03           O  
ANISOU 4399  O   PRO E  43     4132   8616   5501  -1263    278  -1449       O  
ATOM   4400  CB  PRO E  43       0.025  -2.311 -21.547  1.00 50.47           C  
ANISOU 4400  CB  PRO E  43     4026   9397   5755  -2016    650  -1674       C  
ATOM   4401  CG  PRO E  43      -0.679  -3.257 -22.482  1.00 53.74           C  
ANISOU 4401  CG  PRO E  43     4416   9961   6042  -2342    557  -1794       C  
ATOM   4402  CD  PRO E  43      -1.625  -2.398 -23.256  1.00 58.20           C  
ANISOU 4402  CD  PRO E  43     4564  10976   6572  -2031    373  -1905       C  
ATOM   4403  N   PRO E  44       2.539  -0.420 -22.305  1.00 46.64           N  
ANISOU 4403  N   PRO E  44     4074   8171   5477  -1066    475  -1287       N  
ATOM   4404  CA  PRO E  44       3.910  -0.530 -22.809  1.00 47.42           C  
ANISOU 4404  CA  PRO E  44     4545   7863   5611   -950    453  -1104       C  
ATOM   4405  C   PRO E  44       4.299  -1.992 -22.960  1.00 45.32           C  
ANISOU 4405  C   PRO E  44     4554   7388   5279  -1274    525  -1096       C  
ATOM   4406  O   PRO E  44       3.807  -2.865 -22.240  1.00 46.49           O  
ANISOU 4406  O   PRO E  44     4718   7567   5379  -1621    635  -1170       O  
ATOM   4407  CB  PRO E  44       4.745   0.149 -21.719  1.00 49.90           C  
ANISOU 4407  CB  PRO E  44     4983   7964   6013   -808    539   -974       C  
ATOM   4408  CG  PRO E  44       3.773   1.077 -21.035  1.00 47.07           C  
ANISOU 4408  CG  PRO E  44     4331   7887   5669   -676    546  -1092       C  
ATOM   4409  CD  PRO E  44       2.478   0.331 -21.037  1.00 46.09           C  
ANISOU 4409  CD  PRO E  44     3915   8134   5462   -950    580  -1281       C  
ATOM   4410  N   LYS E  45       5.197  -2.244 -23.913  1.00 46.41           N  
ANISOU 4410  N   LYS E  45     4940   7299   5394  -1150    471  -1003       N  
ATOM   4411  CA  LYS E  45       5.732  -3.567 -24.205  1.00 52.48           C  
ANISOU 4411  CA  LYS E  45     6050   7807   6083  -1342    528   -992       C  
ATOM   4412  C   LYS E  45       7.254  -3.519 -24.107  1.00 37.64           C  
ANISOU 4412  C   LYS E  45     4432   5620   4247  -1101    580   -796       C  
ATOM   4413  O   LYS E  45       7.889  -2.666 -24.729  1.00 40.76           O  
ANISOU 4413  O   LYS E  45     4786   6024   4676   -823    521   -698       O  
ATOM   4414  CB  LYS E  45       5.301  -4.031 -25.608  1.00 49.46           C  
ANISOU 4414  CB  LYS E  45     5700   7513   5579  -1401    411  -1112       C  
ATOM   4415  CG  LYS E  45       6.083  -5.210 -26.170  1.00 58.60           C  
ANISOU 4415  CG  LYS E  45     7286   8343   6635  -1463    456  -1097       C  
ATOM   4416  CD  LYS E  45       5.802  -5.398 -27.665  1.00 56.04           C  
ANISOU 4416  CD  LYS E  45     7003   8117   6172  -1438    325  -1208       C  
ATOM   4417  CE  LYS E  45       6.660  -6.508 -28.269  1.00 74.54           C  
ANISOU 4417  CE  LYS E  45     9813  10116   8393  -1423    383  -1208       C  
ATOM   4418  NZ  LYS E  45       6.142  -6.979 -29.592  1.00 80.51           N  
ANISOU 4418  NZ  LYS E  45    10667  10958   8964  -1530    262  -1381       N  
ATOM   4419  N   LEU E  46       7.831  -4.427 -23.320  1.00 41.66           N  
ANISOU 4419  N   LEU E  46     5209   5882   4738  -1212    690   -733       N  
ATOM   4420  CA  LEU E  46       9.279  -4.465 -23.151  1.00 37.35           C  
ANISOU 4420  CA  LEU E  46     4858   5117   4217   -966    732   -556       C  
ATOM   4421  C   LEU E  46       9.960  -4.861 -24.456  1.00 42.08           C  
ANISOU 4421  C   LEU E  46     5627   5624   4736   -784    705   -542       C  
ATOM   4422  O   LEU E  46       9.587  -5.858 -25.074  1.00 43.37           O  
ANISOU 4422  O   LEU E  46     6007   5687   4785   -917    704   -659       O  
ATOM   4423  CB  LEU E  46       9.650  -5.465 -22.064  1.00 42.54           C  
ANISOU 4423  CB  LEU E  46     5793   5539   4832  -1086    831   -498       C  
ATOM   4424  CG  LEU E  46      11.124  -5.527 -21.688  1.00 40.85           C  
ANISOU 4424  CG  LEU E  46     5723   5169   4630   -806    858   -316       C  
ATOM   4425  CD1 LEU E  46      11.571  -4.215 -21.084  1.00 41.40           C  
ANISOU 4425  CD1 LEU E  46     5518   5402   4812   -679    826   -215       C  
ATOM   4426  CD2 LEU E  46      11.381  -6.706 -20.753  1.00 43.38           C  
ANISOU 4426  CD2 LEU E  46     6397   5227   4859   -892    930   -264       C  
ATOM   4427  N   LEU E  47      10.957  -4.074 -24.867  1.00 36.11           N  
ANISOU 4427  N   LEU E  47     4789   4911   4019   -506    691   -408       N  
ATOM   4428  CA  LEU E  47      11.805  -4.377 -26.014  1.00 40.49           C  
ANISOU 4428  CA  LEU E  47     5483   5422   4480   -296    706   -369       C  
ATOM   4429  C   LEU E  47      13.185  -4.849 -25.586  1.00 41.50           C  
ANISOU 4429  C   LEU E  47     5750   5424   4597    -86    795   -232       C  
ATOM   4430  O   LEU E  47      13.706  -5.835 -26.122  1.00 42.93           O  
ANISOU 4430  O   LEU E  47     6184   5466   4659     52    848   -258       O  
ATOM   4431  CB  LEU E  47      11.976  -3.142 -26.907  1.00 39.65           C  
ANISOU 4431  CB  LEU E  47     5175   5506   4386   -149    644   -303       C  
ATOM   4432  CG  LEU E  47      10.804  -2.562 -27.689  1.00 49.13           C  
ANISOU 4432  CG  LEU E  47     6242   6872   5551   -217    523   -413       C  
ATOM   4433  CD1 LEU E  47      11.258  -1.298 -28.400  1.00 48.72           C  
ANISOU 4433  CD1 LEU E  47     6086   6931   5494    -33    477   -281       C  
ATOM   4434  CD2 LEU E  47      10.229  -3.546 -28.663  1.00 48.27           C  
ANISOU 4434  CD2 LEU E  47     6297   6755   5289   -308    486   -576       C  
ATOM   4435  N   ILE E  48      13.801  -4.123 -24.654  1.00 35.47           N  
ANISOU 4435  N   ILE E  48     4816   4726   3935    -36    801    -96       N  
ATOM   4436  CA  ILE E  48      15.194  -4.320 -24.271  1.00 42.08           C  
ANISOU 4436  CA  ILE E  48     5668   5563   4759    187    854     50       C  
ATOM   4437  C   ILE E  48      15.279  -4.246 -22.759  1.00 42.80           C  
ANISOU 4437  C   ILE E  48     5732   5612   4918    100    841    115       C  
ATOM   4438  O   ILE E  48      14.689  -3.353 -22.145  1.00 37.97           O  
ANISOU 4438  O   ILE E  48     4958   5074   4395    -70    798    103       O  
ATOM   4439  CB  ILE E  48      16.128  -3.258 -24.891  1.00 41.63           C  
ANISOU 4439  CB  ILE E  48     5369   5728   4719    322    858    174       C  
ATOM   4440  CG1 ILE E  48      15.928  -3.137 -26.411  1.00 47.69           C  
ANISOU 4440  CG1 ILE E  48     6162   6564   5393    381    869    120       C  
ATOM   4441  CG2 ILE E  48      17.579  -3.533 -24.514  1.00 42.54           C  
ANISOU 4441  CG2 ILE E  48     5422   5939   4801    543    912    309       C  
ATOM   4442  CD1 ILE E  48      16.559  -4.238 -27.210  1.00 50.33           C  
ANISOU 4442  CD1 ILE E  48     6694   6854   5578    610    956     84       C  
ATOM   4443  N   TYR E  49      16.006  -5.176 -22.152  1.00 42.79           N  
ANISOU 4443  N   TYR E  49     5915   5494   4850    248    874    181       N  
ATOM   4444  CA  TYR E  49      16.293  -5.097 -20.729  1.00 39.95           C  
ANISOU 4444  CA  TYR E  49     5538   5126   4515    208    848    270       C  
ATOM   4445  C   TYR E  49      17.795  -5.232 -20.523  1.00 36.76           C  
ANISOU 4445  C   TYR E  49     5056   4846   4064    517    838    418       C  
ATOM   4446  O   TYR E  49      18.522  -5.734 -21.388  1.00 42.68           O  
ANISOU 4446  O   TYR E  49     5843   5633   4740    786    881    434       O  
ATOM   4447  CB  TYR E  49      15.502  -6.161 -19.934  1.00 37.58           C  
ANISOU 4447  CB  TYR E  49     5572   4563   4144     45    877    215       C  
ATOM   4448  CG  TYR E  49      15.763  -7.610 -20.323  1.00 34.34           C  
ANISOU 4448  CG  TYR E  49     5574   3880   3593    211    922    199       C  
ATOM   4449  CD1 TYR E  49      15.120  -8.185 -21.416  1.00 41.43           C  
ANISOU 4449  CD1 TYR E  49     6661   4644   4435    133    955     56       C  
ATOM   4450  CD2 TYR E  49      16.594  -8.422 -19.556  1.00 37.22           C  
ANISOU 4450  CD2 TYR E  49     6188   4099   3856    449    917    318       C  
ATOM   4451  CE1 TYR E  49      15.344  -9.514 -21.770  1.00 47.50           C  
ANISOU 4451  CE1 TYR E  49     7889   5104   5054    280    995     20       C  
ATOM   4452  CE2 TYR E  49      16.807  -9.759 -19.891  1.00 46.88           C  
ANISOU 4452  CE2 TYR E  49     7877   5007   4929    645    956    299       C  
ATOM   4453  CZ  TYR E  49      16.184 -10.297 -21.000  1.00 49.54           C  
ANISOU 4453  CZ  TYR E  49     8431   5175   5216    550   1002    143       C  
ATOM   4454  OH  TYR E  49      16.395 -11.611 -21.335  1.00 50.73           O  
ANISOU 4454  OH  TYR E  49     9115   4962   5199    740   1039    104       O  
ATOM   4455  N   ALA E  50      18.256  -4.754 -19.371  1.00 37.85           N  
ANISOU 4455  N   ALA E  50     5061   5093   4228    483    777    514       N  
ATOM   4456  CA  ALA E  50      19.677  -4.758 -19.041  1.00 36.87           C  
ANISOU 4456  CA  ALA E  50     4773   5184   4053    744    736    652       C  
ATOM   4457  C   ALA E  50      20.488  -4.101 -20.154  1.00 38.71           C  
ANISOU 4457  C   ALA E  50     4704   5696   4306    850    768    688       C  
ATOM   4458  O   ALA E  50      21.552  -4.585 -20.533  1.00 39.09           O  
ANISOU 4458  O   ALA E  50     4667   5916   4269   1162    797    753       O  
ATOM   4459  CB  ALA E  50      20.183  -6.175 -18.751  1.00 43.94           C  
ANISOU 4459  CB  ALA E  50     5971   5919   4806   1071    744    700       C  
ATOM   4460  N   ALA E  51      19.935  -3.017 -20.708  1.00 34.06           N  
ANISOU 4460  N   ALA E  51     3977   5156   3810    603    773    643       N  
ATOM   4461  CA  ALA E  51      20.575  -2.146 -21.693  1.00 50.13           C  
ANISOU 4461  CA  ALA E  51     5756   7437   5853    594    808    697       C  
ATOM   4462  C   ALA E  51      20.665  -2.772 -23.082  1.00 39.32           C  
ANISOU 4462  C   ALA E  51     4471   6072   4398    801    911    654       C  
ATOM   4463  O   ALA E  51      20.435  -2.076 -24.074  1.00 45.55           O  
ANISOU 4463  O   ALA E  51     5195   6920   5190    699    945    644       O  
ATOM   4464  CB  ALA E  51      21.975  -1.713 -21.231  1.00 42.89           C  
ANISOU 4464  CB  ALA E  51     4528   6862   4907    645    775    833       C  
ATOM   4465  N   SER E  52      20.990  -4.064 -23.189  1.00 44.03           N  
ANISOU 4465  N   SER E  52     5255   6583   4892   1106    959    627       N  
ATOM   4466  CA  SER E  52      21.255  -4.661 -24.502  1.00 41.28           C  
ANISOU 4466  CA  SER E  52     4996   6264   4426   1348   1067    574       C  
ATOM   4467  C   SER E  52      20.564  -5.997 -24.754  1.00 48.90           C  
ANISOU 4467  C   SER E  52     6407   6870   5304   1482   1093    437       C  
ATOM   4468  O   SER E  52      20.685  -6.520 -25.865  1.00 45.69           O  
ANISOU 4468  O   SER E  52     6136   6446   4777   1672   1178    360       O  
ATOM   4469  CB  SER E  52      22.765  -4.849 -24.708  1.00 42.41           C  
ANISOU 4469  CB  SER E  52     4881   6765   4467   1687   1138    675       C  
ATOM   4470  OG  SER E  52      23.303  -5.708 -23.714  1.00 52.28           O  
ANISOU 4470  OG  SER E  52     6213   7977   5673   1958   1088    717       O  
ATOM   4471  N   LYS E  53      19.846  -6.560 -23.784  1.00 41.61           N  
ANISOU 4471  N   LYS E  53     5744   5655   4412   1358   1031    400       N  
ATOM   4472  CA  LYS E  53      19.204  -7.859 -23.952  1.00 46.92           C  
ANISOU 4472  CA  LYS E  53     6897   5948   4981   1408   1056    277       C  
ATOM   4473  C   LYS E  53      17.816  -7.699 -24.566  1.00 52.37           C  
ANISOU 4473  C   LYS E  53     7696   6498   5703   1050   1041    124       C  
ATOM   4474  O   LYS E  53      17.039  -6.836 -24.152  1.00 48.71           O  
ANISOU 4474  O   LYS E  53     7038   6108   5362    737    983    118       O  
ATOM   4475  CB  LYS E  53      19.093  -8.583 -22.605  1.00 42.02           C  
ANISOU 4475  CB  LYS E  53     6541   5083   4343   1400   1009    328       C  
ATOM   4476  CG  LYS E  53      20.419  -8.761 -21.870  1.00 48.74           C  
ANISOU 4476  CG  LYS E  53     7275   6103   5143   1778    980    486       C  
ATOM   4477  CD  LYS E  53      20.222  -9.656 -20.644  1.00 53.87           C  
ANISOU 4477  CD  LYS E  53     8313   6437   5718   1800    929    539       C  
ATOM   4478  CE  LYS E  53      21.480  -9.768 -19.795  1.00 49.35           C  
ANISOU 4478  CE  LYS E  53     7599   6073   5079   2183    856    705       C  
ATOM   4479  NZ  LYS E  53      21.261 -10.602 -18.560  1.00 52.01           N  
ANISOU 4479  NZ  LYS E  53     8363   6087   5312   2204    793    782       N  
ATOM   4480  N   VAL E  54      17.488  -8.567 -25.524  1.00 47.30           N  
ANISOU 4480  N   VAL E  54     7378   5664   4931   1114   1083    -16       N  
ATOM   4481  CA  VAL E  54      16.276  -8.422 -26.326  1.00 45.77           C  
ANISOU 4481  CA  VAL E  54     7239   5424   4730    805   1049   -174       C  
ATOM   4482  C   VAL E  54      15.204  -9.372 -25.809  1.00 57.40           C  
ANISOU 4482  C   VAL E  54     9086   6563   6162    506   1024   -296       C  
ATOM   4483  O   VAL E  54      15.459 -10.566 -25.618  1.00 53.58           O  
ANISOU 4483  O   VAL E  54     9046   5759   5554    631   1064   -325       O  
ATOM   4484  CB  VAL E  54      16.578  -8.674 -27.813  1.00 58.44           C  
ANISOU 4484  CB  VAL E  54     8945   7079   6182   1009   1101   -266       C  
ATOM   4485  CG1 VAL E  54      15.366  -8.388 -28.656  1.00 56.79           C  
ANISOU 4485  CG1 VAL E  54     8734   6897   5949    701   1029   -417       C  
ATOM   4486  CG2 VAL E  54      17.734  -7.798 -28.252  1.00 55.23           C  
ANISOU 4486  CG2 VAL E  54     8172   7027   5785   1274   1162   -123       C  
ATOM   4487  N   GLU E  55      14.005  -8.845 -25.576  1.00 51.99           N  
ANISOU 4487  N   GLU E  55     8232   5958   5565    111    962   -368       N  
ATOM   4488  CA  GLU E  55      12.889  -9.662 -25.117  1.00 55.01           C  
ANISOU 4488  CA  GLU E  55     8895   6110   5898   -270    953   -491       C  
ATOM   4489  C   GLU E  55      12.438 -10.618 -26.225  1.00 69.78           C  
ANISOU 4489  C   GLU E  55    11136   7781   7595   -363    948   -681       C  
ATOM   4490  O   GLU E  55      12.700 -10.401 -27.411  1.00 60.67           O  
ANISOU 4490  O   GLU E  55     9928   6747   6377   -182    933   -740       O  
ATOM   4491  CB  GLU E  55      11.743  -8.756 -24.637  1.00 60.32           C  
ANISOU 4491  CB  GLU E  55     9194   7029   6696   -626    899   -531       C  
ATOM   4492  CG  GLU E  55      10.448  -9.442 -24.166  1.00 66.67           C  
ANISOU 4492  CG  GLU E  55    10156   7729   7447  -1103    905   -669       C  
ATOM   4493  CD  GLU E  55      10.579 -10.159 -22.822  1.00 75.61           C  
ANISOU 4493  CD  GLU E  55    11578   8604   8546  -1223    983   -575       C  
ATOM   4494  OE1 GLU E  55      11.580 -10.876 -22.609  1.00 73.82           O  
ANISOU 4494  OE1 GLU E  55    11713   8093   8244   -942   1021   -470       O  
ATOM   4495  OE2 GLU E  55       9.682  -9.989 -21.963  1.00 80.34           O1-
ANISOU 4495  OE2 GLU E  55    12039   9309   9176  -1572   1010   -600       O1-
ATOM   4496  N  ASER E  56      11.770 -11.697 -25.813  0.52 75.70           N  
ANISOU 4496  N  ASER E  56    12305   8213   8245   -676    966   -777       N  
ATOM   4497  N  BSER E  56      11.779 -11.703 -25.815  0.48 75.63           N  
ANISOU 4497  N  BSER E  56    12298   8202   8236   -673    966   -776       N  
ATOM   4498  CA ASER E  56      11.279 -12.697 -26.755  0.52 81.03           C  
ANISOU 4498  CA ASER E  56    13414   8644   8732   -851    951   -981       C  
ATOM   4499  CA BSER E  56      11.300 -12.698 -26.765  0.48 80.99           C  
ANISOU 4499  CA BSER E  56    13410   8637   8726   -842    951   -979       C  
ATOM   4500  C  ASER E  56      10.303 -12.069 -27.739  0.52 77.87           C  
ANISOU 4500  C  ASER E  56    12677   8578   8333  -1109    849  -1142       C  
ATOM   4501  C  BSER E  56      10.306 -12.079 -27.736  0.48 77.30           C  
ANISOU 4501  C  BSER E  56    12609   8502   8259  -1109    849  -1142       C  
ATOM   4502  O  ASER E  56       9.377 -11.351 -27.347  0.52 76.32           O  
ANISOU 4502  O  ASER E  56    12071   8678   8249  -1411    793  -1159       O  
ATOM   4503  O  BSER E  56       9.371 -11.379 -27.333  0.48 76.10           O  
ANISOU 4503  O  BSER E  56    12055   8642   8219  -1417    795  -1160       O  
ATOM   4504  CB ASER E  56      10.596 -13.843 -26.007  0.52 78.64           C  
ANISOU 4504  CB ASER E  56    13606   7952   8323  -1273    985  -1043       C  
ATOM   4505  CB BSER E  56      10.652 -13.869 -26.028  0.48 78.64           C  
ANISOU 4505  CB BSER E  56    13624   7938   8318  -1249    987  -1041       C  
ATOM   4506  OG ASER E  56       9.522 -13.355 -25.223  0.52 77.01           O  
ANISOU 4506  OG ASER E  56    13057   7985   8220  -1744    970  -1049       O  
ATOM   4507  OG BSER E  56      10.147 -14.821 -26.947  0.48 77.16           O  
ANISOU 4507  OG BSER E  56    13893   7492   7931  -1483    960  -1259       O  
ATOM   4508  N   GLY E  57      10.518 -12.336 -29.023  1.00 62.03           N  
ANISOU 4508  N   GLY E  57    10845   6546   6178   -951    820  -1264       N  
ATOM   4509  CA  GLY E  57       9.655 -11.842 -30.065  1.00 72.53           C  
ANISOU 4509  CA  GLY E  57    11921   8182   7456  -1151    698  -1419       C  
ATOM   4510  C   GLY E  57      10.108 -10.559 -30.732  1.00 63.92           C  
ANISOU 4510  C   GLY E  57    10377   7470   6439   -815    661  -1311       C  
ATOM   4511  O   GLY E  57       9.635 -10.258 -31.831  1.00 65.10           O  
ANISOU 4511  O   GLY E  57    10428   7828   6480   -859    559  -1426       O  
ATOM   4512  N   VAL E  58      11.001  -9.796 -30.114  1.00 60.09           N  
ANISOU 4512  N   VAL E  58     9641   7079   6110   -510    732  -1092       N  
ATOM   4513  CA  VAL E  58      11.382  -8.498 -30.682  1.00 58.12           C  
ANISOU 4513  CA  VAL E  58     8993   7166   5925   -274    701   -974       C  
ATOM   4514  C   VAL E  58      12.248  -8.723 -31.920  1.00 60.73           C  
ANISOU 4514  C   VAL E  58     9512   7494   6072     50    759   -989       C  
ATOM   4515  O   VAL E  58      13.248  -9.454 -31.850  1.00 48.13           O  
ANISOU 4515  O   VAL E  58     8186   5698   4405    325    883   -957       O  
ATOM   4516  CB  VAL E  58      12.112  -7.655 -29.638  1.00 50.34           C  
ANISOU 4516  CB  VAL E  58     7724   6267   5137   -112    759   -750       C  
ATOM   4517  CG1 VAL E  58      12.559  -6.368 -30.241  1.00 46.88           C  
ANISOU 4517  CG1 VAL E  58     6966   6110   4736     79    738   -623       C  
ATOM   4518  CG2 VAL E  58      11.215  -7.392 -28.445  1.00 42.85           C  
ANISOU 4518  CG2 VAL E  58     6597   5347   4337   -415    716   -753       C  
ATOM   4519  N   PRO E  59      11.907  -8.132 -33.062  1.00 48.67           N  
ANISOU 4519  N   PRO E  59     7857   6198   4436     60    676  -1039       N  
ATOM   4520  CA  PRO E  59      12.673  -8.369 -34.295  1.00 49.63           C  
ANISOU 4520  CA  PRO E  59     8176   6344   4337    347    749  -1068       C  
ATOM   4521  C   PRO E  59      14.110  -7.880 -34.179  1.00 53.64           C  
ANISOU 4521  C   PRO E  59     8533   6957   4890    720    912   -853       C  
ATOM   4522  O   PRO E  59      14.475  -7.092 -33.301  1.00 50.70           O  
ANISOU 4522  O   PRO E  59     7856   6687   4718    734    930   -669       O  
ATOM   4523  CB  PRO E  59      11.916  -7.574 -35.364  1.00 60.32           C  
ANISOU 4523  CB  PRO E  59     9356   7980   5583    250    601  -1116       C  
ATOM   4524  CG  PRO E  59      10.675  -7.055 -34.712  1.00 59.06           C  
ANISOU 4524  CG  PRO E  59     8918   7939   5583    -68    438  -1146       C  
ATOM   4525  CD  PRO E  59      10.609  -7.493 -33.306  1.00 49.80           C  
ANISOU 4525  CD  PRO E  59     7748   6572   4601   -220    498  -1123       C  
ATOM   4526  N   ALA E  60      14.936  -8.339 -35.131  1.00 47.87           N  
ANISOU 4526  N   ALA E  60     8008   6238   3942   1016   1032   -892       N  
ATOM   4527  CA  ALA E  60      16.357  -8.013 -35.127  1.00 49.11           C  
ANISOU 4527  CA  ALA E  60     7996   6568   4095   1373   1210   -713       C  
ATOM   4528  C   ALA E  60      16.626  -6.533 -35.354  1.00 48.65           C  
ANISOU 4528  C   ALA E  60     7523   6852   4110   1331   1208   -504       C  
ATOM   4529  O   ALA E  60      17.728  -6.061 -35.043  1.00 50.63           O  
ANISOU 4529  O   ALA E  60     7533   7287   4418   1500   1335   -324       O  
ATOM   4530  CB  ALA E  60      17.092  -8.807 -36.199  1.00 49.73           C  
ANISOU 4530  CB  ALA E  60     8368   6640   3886   1712   1358   -827       C  
ATOM   4531  N   ARG E  61      15.660  -5.795 -35.902  1.00 49.27           N  
ANISOU 4531  N   ARG E  61     7530   7024   4167   1108   1059   -524       N  
ATOM   4532  CA  ARG E  61      15.915  -4.402 -36.236  1.00 47.81           C  
ANISOU 4532  CA  ARG E  61     7068   7094   4002   1087   1055   -319       C  
ATOM   4533  C   ARG E  61      16.020  -3.524 -34.997  1.00 45.73           C  
ANISOU 4533  C   ARG E  61     6517   6842   4017    964   1022   -148       C  
ATOM   4534  O   ARG E  61      16.485  -2.385 -35.112  1.00 47.64           O  
ANISOU 4534  O   ARG E  61     6569   7248   4282    943   1050     44       O  
ATOM   4535  CB  ARG E  61      14.822  -3.873 -37.173  1.00 46.43           C  
ANISOU 4535  CB  ARG E  61     6944   7001   3697    950    878   -382       C  
ATOM   4536  CG  ARG E  61      13.399  -4.081 -36.686  1.00 48.87           C  
ANISOU 4536  CG  ARG E  61     7252   7201   4116    709    665   -542       C  
ATOM   4537  CD  ARG E  61      12.397  -3.543 -37.704  1.00 54.39           C  
ANISOU 4537  CD  ARG E  61     7955   8062   4648    639    470   -601       C  
ATOM   4538  NE  ARG E  61      11.038  -3.496 -37.174  1.00 49.60           N  
ANISOU 4538  NE  ARG E  61     7214   7469   4161    418    262   -728       N  
ATOM   4539  CZ  ARG E  61      10.143  -4.463 -37.312  1.00 56.06           C  
ANISOU 4539  CZ  ARG E  61     8153   8248   4898    222    155   -975       C  
ATOM   4540  NH1 ARG E  61      10.450  -5.615 -37.885  1.00 53.15           N  
ANISOU 4540  NH1 ARG E  61     8117   7739   4339    223    229  -1135       N  
ATOM   4541  NH2 ARG E  61       8.914  -4.283 -36.835  1.00 56.39           N  
ANISOU 4541  NH2 ARG E  61     7983   8402   5040      9    -22  -1074       N  
ATOM   4542  N   PHE E  62      15.612  -4.023 -33.823  1.00 42.54           N  
ANISOU 4542  N   PHE E  62     6115   6252   3796    861    969   -214       N  
ATOM   4543  CA  PHE E  62      15.766  -3.287 -32.570  1.00 38.68           C  
ANISOU 4543  CA  PHE E  62     5386   5766   3543    760    947    -75       C  
ATOM   4544  C   PHE E  62      17.062  -3.688 -31.872  1.00 47.27           C  
ANISOU 4544  C   PHE E  62     6407   6877   4677    934   1090     26       C  
ATOM   4545  O   PHE E  62      17.411  -4.870 -31.810  1.00 46.14           O  
ANISOU 4545  O   PHE E  62     6462   6611   4457   1107   1162    -65       O  
ATOM   4546  CB  PHE E  62      14.579  -3.538 -31.627  1.00 41.15           C  
ANISOU 4546  CB  PHE E  62     5714   5918   4003    542    819   -193       C  
ATOM   4547  CG  PHE E  62      13.284  -2.993 -32.134  1.00 42.16           C  
ANISOU 4547  CG  PHE E  62     5795   6116   4108    390    657   -284       C  
ATOM   4548  CD1 PHE E  62      12.919  -1.681 -31.880  1.00 38.55           C  
ANISOU 4548  CD1 PHE E  62     5133   5761   3756    345    568   -179       C  
ATOM   4549  CD2 PHE E  62      12.432  -3.792 -32.881  1.00 46.26           C  
ANISOU 4549  CD2 PHE E  62     6490   6608   4479    307    580   -484       C  
ATOM   4550  CE1 PHE E  62      11.727  -1.177 -32.362  1.00 40.84           C  
ANISOU 4550  CE1 PHE E  62     5364   6149   4004    287    403   -262       C  
ATOM   4551  CE2 PHE E  62      11.239  -3.296 -33.361  1.00 44.57           C  
ANISOU 4551  CE2 PHE E  62     6175   6535   4224    191    405   -572       C  
ATOM   4552  CZ  PHE E  62      10.888  -1.985 -33.108  1.00 45.34           C  
ANISOU 4552  CZ  PHE E  62     6038   6761   4428    215    315   -456       C  
ATOM   4553  N   SER E  63      17.766  -2.697 -31.333  1.00 44.41           N  
ANISOU 4553  N   SER E  63     5781   6670   4423    893   1116    210       N  
ATOM   4554  CA  SER E  63      19.019  -2.946 -30.636  1.00 46.14           C  
ANISOU 4554  CA  SER E  63     5852   7004   4677   1045   1221    316       C  
ATOM   4555  C   SER E  63      19.220  -1.877 -29.576  1.00 46.79           C  
ANISOU 4555  C   SER E  63     5691   7150   4937    846   1158    456       C  
ATOM   4556  O   SER E  63      18.830  -0.722 -29.758  1.00 48.66           O  
ANISOU 4556  O   SER E  63     5860   7411   5217    652   1095    524       O  
ATOM   4557  CB  SER E  63      20.215  -2.945 -31.600  1.00 49.96           C  
ANISOU 4557  CB  SER E  63     6227   7775   4981   1256   1390    395       C  
ATOM   4558  OG  SER E  63      20.099  -3.991 -32.539  1.00 68.21           O  
ANISOU 4558  OG  SER E  63     8804  10012   7101   1481   1459    243       O  
ATOM   4559  N   GLY E  64      19.839  -2.266 -28.471  1.00 42.41           N  
ANISOU 4559  N   GLY E  64     5046   6607   4461    913   1164    497       N  
ATOM   4560  CA  GLY E  64      20.147  -1.334 -27.408  1.00 42.42           C  
ANISOU 4560  CA  GLY E  64     4833   6683   4599    724   1100    613       C  
ATOM   4561  C   GLY E  64      21.622  -1.360 -27.075  1.00 41.01           C  
ANISOU 4561  C   GLY E  64     4390   6808   4382    849   1176    739       C  
ATOM   4562  O   GLY E  64      22.270  -2.404 -27.101  1.00 45.41           O  
ANISOU 4562  O   GLY E  64     4960   7442   4853   1155   1246    716       O  
ATOM   4563  N   SER E  65      22.146  -0.186 -26.742  1.00 42.31           N  
ANISOU 4563  N   SER E  65     4322   7153   4599    612   1151    867       N  
ATOM   4564  CA  SER E  65      23.565  -0.068 -26.443  1.00 49.78           C  
ANISOU 4564  CA  SER E  65     4937   8482   5497    655   1209    988       C  
ATOM   4565  C   SER E  65      23.756   1.019 -25.398  1.00 52.56           C  
ANISOU 4565  C   SER E  65     5142   8874   5957    318   1096   1070       C  
ATOM   4566  O   SER E  65      22.826   1.753 -25.059  1.00 45.17           O  
ANISOU 4566  O   SER E  65     4383   7662   5118     89   1000   1036       O  
ATOM   4567  CB  SER E  65      24.371   0.216 -27.715  1.00 56.18           C  
ANISOU 4567  CB  SER E  65     5574   9619   6151    685   1373   1068       C  
ATOM   4568  OG  SER E  65      24.076   1.504 -28.227  1.00 56.30           O  
ANISOU 4568  OG  SER E  65     5628   9595   6169    332   1366   1151       O  
ATOM   4569  N   GLY E  66      24.974   1.114 -24.886  1.00 52.97           N  
ANISOU 4569  N   GLY E  66     4863   9293   5972    305   1102   1164       N  
ATOM   4570  CA  GLY E  66      25.315   2.116 -23.897  1.00 57.01           C  
ANISOU 4570  CA  GLY E  66     5228   9883   6549    -45    986   1230       C  
ATOM   4571  C   GLY E  66      25.747   1.500 -22.579  1.00 58.04           C  
ANISOU 4571  C   GLY E  66     5238  10116   6699     96    871   1219       C  
ATOM   4572  O   GLY E  66      25.696   0.290 -22.370  1.00 56.09           O  
ANISOU 4572  O   GLY E  66     5075   9814   6422    474    876   1169       O  
ATOM   4573  N   SER E  67      26.185   2.384 -21.685  1.00 55.72           N  
ANISOU 4573  N   SER E  67     4789   9952   6430   -231    757   1269       N  
ATOM   4574  CA  SER E  67      26.683   1.989 -20.377  1.00 52.42           C  
ANISOU 4574  CA  SER E  67     4234   9686   5998   -152    617   1273       C  
ATOM   4575  C   SER E  67      26.774   3.228 -19.501  1.00 58.12           C  
ANISOU 4575  C   SER E  67     4926  10404   6752   -624    482   1285       C  
ATOM   4576  O   SER E  67      26.806   4.362 -19.991  1.00 51.31           O  
ANISOU 4576  O   SER E  67     4076   9519   5900  -1000    512   1319       O  
ATOM   4577  CB  SER E  67      28.051   1.301 -20.460  1.00 55.39           C  
ANISOU 4577  CB  SER E  67     4187  10609   6249    136    646   1351       C  
ATOM   4578  OG  SER E  67      29.054   2.216 -20.857  1.00 68.66           O  
ANISOU 4578  OG  SER E  67     5652  12564   7872   -176    632   1386       O  
ATOM   4579  N   GLY E  68      26.818   2.992 -18.190  1.00 48.22           N  
ANISOU 4579  N   GLY E  68     3685   9148   5489   -601    328   1257       N  
ATOM   4580  CA  GLY E  68      26.921   4.079 -17.240  1.00 54.13           C  
ANISOU 4580  CA  GLY E  68     4442   9887   6237  -1027    183   1239       C  
ATOM   4581  C   GLY E  68      25.696   4.968 -17.277  1.00 50.20           C  
ANISOU 4581  C   GLY E  68     4351   8888   5836  -1264    194   1149       C  
ATOM   4582  O   GLY E  68      24.643   4.599 -16.759  1.00 49.26           O  
ANISOU 4582  O   GLY E  68     4518   8432   5768  -1118    178   1054       O  
ATOM   4583  N   THR E  69      25.816   6.135 -17.909  1.00 51.54           N  
ANISOU 4583  N   THR E  69     4558   9015   6012  -1620    228   1183       N  
ATOM   4584  CA  THR E  69      24.734   7.107 -17.956  1.00 51.66           C  
ANISOU 4584  CA  THR E  69     4975   8560   6094  -1803    219   1104       C  
ATOM   4585  C   THR E  69      24.168   7.343 -19.350  1.00 54.17           C  
ANISOU 4585  C   THR E  69     5449   8688   6444  -1736    352   1138       C  
ATOM   4586  O   THR E  69      23.158   8.045 -19.468  1.00 52.80           O  
ANISOU 4586  O   THR E  69     5616   8128   6318  -1779    338   1071       O  
ATOM   4587  CB  THR E  69      25.203   8.453 -17.380  1.00 50.50           C  
ANISOU 4587  CB  THR E  69     4906   8388   5895  -2297    110   1104       C  
ATOM   4588  OG1 THR E  69      26.269   8.965 -18.183  1.00 57.69           O  
ANISOU 4588  OG1 THR E  69     5644   9541   6734  -2515    153   1201       O  
ATOM   4589  CG2 THR E  69      25.683   8.289 -15.947  1.00 56.25           C  
ANISOU 4589  CG2 THR E  69     5512   9299   6563  -2382    -51   1050       C  
ATOM   4590  N   ASP E  70      24.771   6.776 -20.400  1.00 50.67           N  
ANISOU 4590  N   ASP E  70     4776   8522   5954  -1597    476   1233       N  
ATOM   4591  CA  ASP E  70      24.409   7.082 -21.782  1.00 47.82           C  
ANISOU 4591  CA  ASP E  70     4555   8041   5574  -1580    598   1285       C  
ATOM   4592  C   ASP E  70      23.908   5.829 -22.490  1.00 49.47           C  
ANISOU 4592  C   ASP E  70     4759   8245   5793  -1141    692   1238       C  
ATOM   4593  O   ASP E  70      24.641   4.840 -22.597  1.00 52.61           O  
ANISOU 4593  O   ASP E  70     4895   8954   6140   -912    754   1263       O  
ATOM   4594  CB  ASP E  70      25.606   7.662 -22.535  1.00 51.98           C  
ANISOU 4594  CB  ASP E  70     4902   8851   5998  -1822    663   1397       C  
ATOM   4595  CG  ASP E  70      26.098   8.946 -21.921  1.00 74.98           C  
ANISOU 4595  CG  ASP E  70     7921  11680   8887  -2265    548   1399       C  
ATOM   4596  OD1 ASP E  70      25.258   9.829 -21.645  1.00 71.21           O1-
ANISOU 4596  OD1 ASP E  70     7805  10806   8445  -2452    488   1376       O1-
ATOM   4597  OD2 ASP E  70      27.324   9.068 -21.717  1.00 77.25           O  
ANISOU 4597  OD2 ASP E  70     7947  12303   9103  -2418    516   1419       O  
ATOM   4598  N   PHE E  71      22.683   5.884 -23.014  1.00 43.90           N  
ANISOU 4598  N   PHE E  71     4349   7199   5132  -1016    698   1164       N  
ATOM   4599  CA  PHE E  71      22.074   4.709 -23.622  1.00 47.90           C  
ANISOU 4599  CA  PHE E  71     4902   7659   5637   -664    762   1088       C  
ATOM   4600  C   PHE E  71      21.368   5.112 -24.904  1.00 45.84           C  
ANISOU 4600  C   PHE E  71     4840   7246   5333   -636    808   1096       C  
ATOM   4601  O   PHE E  71      20.934   6.254 -25.058  1.00 44.65           O  
ANISOU 4601  O   PHE E  71     4877   6900   5187   -819    754   1127       O  
ATOM   4602  CB  PHE E  71      21.098   4.023 -22.651  1.00 44.61           C  
ANISOU 4602  CB  PHE E  71     4620   7021   5310   -516    685    946       C  
ATOM   4603  CG  PHE E  71      21.774   3.535 -21.415  1.00 45.27           C  
ANISOU 4603  CG  PHE E  71     4555   7248   5399   -504    631    954       C  
ATOM   4604  CD1 PHE E  71      22.385   2.287 -21.385  1.00 42.61           C  
ANISOU 4604  CD1 PHE E  71     4094   7089   5006   -232    676    970       C  
ATOM   4605  CD2 PHE E  71      21.861   4.356 -20.300  1.00 43.78           C  
ANISOU 4605  CD2 PHE E  71     4378   7018   5241   -743    525    946       C  
ATOM   4606  CE1 PHE E  71      23.060   1.863 -20.260  1.00 44.41           C  
ANISOU 4606  CE1 PHE E  71     4193   7470   5209   -180    602    999       C  
ATOM   4607  CE2 PHE E  71      22.526   3.933 -19.165  1.00 44.03           C  
ANISOU 4607  CE2 PHE E  71     4271   7216   5243   -733    452    961       C  
ATOM   4608  CZ  PHE E  71      23.122   2.684 -19.144  1.00 46.66           C  
ANISOU 4608  CZ  PHE E  71     4463   7745   5520   -442    483    998       C  
ATOM   4609  N   SER E  72      21.261   4.163 -25.828  1.00 44.24           N  
ANISOU 4609  N   SER E  72     4630   7118   5062   -386    897   1064       N  
ATOM   4610  CA  SER E  72      20.581   4.443 -27.081  1.00 44.30           C  
ANISOU 4610  CA  SER E  72     4825   7016   4993   -337    922   1064       C  
ATOM   4611  C   SER E  72      19.790   3.220 -27.517  1.00 45.11           C  
ANISOU 4611  C   SER E  72     5021   7042   5077    -61    933    917       C  
ATOM   4612  O   SER E  72      20.188   2.081 -27.254  1.00 53.71           O  
ANISOU 4612  O   SER E  72     6032   8219   6156    115    986    864       O  
ATOM   4613  CB  SER E  72      21.573   4.871 -28.174  1.00 51.19           C  
ANISOU 4613  CB  SER E  72     5608   8135   5707   -434   1055   1220       C  
ATOM   4614  OG  SER E  72      22.306   3.760 -28.633  1.00 61.80           O  
ANISOU 4614  OG  SER E  72     6768   9755   6958   -204   1188   1206       O  
ATOM   4615  N   LEU E  73      18.647   3.472 -28.147  1.00 44.43           N  
ANISOU 4615  N   LEU E  73     5126   6781   4973    -27    864    847       N  
ATOM   4616  CA  LEU E  73      17.867   2.454 -28.835  1.00 42.89           C  
ANISOU 4616  CA  LEU E  73     5038   6542   4716    159    863    706       C  
ATOM   4617  C   LEU E  73      17.948   2.743 -30.328  1.00 47.05           C  
ANISOU 4617  C   LEU E  73     5657   7157   5063    209    910    768       C  
ATOM   4618  O   LEU E  73      17.720   3.881 -30.756  1.00 42.57           O  
ANISOU 4618  O   LEU E  73     5180   6540   4456    110    857    867       O  
ATOM   4619  CB  LEU E  73      16.407   2.452 -28.359  1.00 40.70           C  
ANISOU 4619  CB  LEU E  73     4853   6079   4534    146    728    556       C  
ATOM   4620  CG  LEU E  73      15.371   1.559 -29.070  1.00 42.95           C  
ANISOU 4620  CG  LEU E  73     5242   6330   4745    243    687    389       C  
ATOM   4621  CD1 LEU E  73      15.602   0.071 -28.791  1.00 37.89           C  
ANISOU 4621  CD1 LEU E  73     4647   5661   4088    311    762    288       C  
ATOM   4622  CD2 LEU E  73      13.952   1.949 -28.693  1.00 40.80           C  
ANISOU 4622  CD2 LEU E  73     4971   5983   4548    196    548    268       C  
ATOM   4623  N   ASN E  74      18.300   1.726 -31.108  1.00 44.06           N  
ANISOU 4623  N   ASN E  74     5299   6892   4550    377   1013    714       N  
ATOM   4624  CA  ASN E  74      18.450   1.843 -32.552  1.00 49.18           C  
ANISOU 4624  CA  ASN E  74     6045   7658   4981    444   1081    758       C  
ATOM   4625  C   ASN E  74      17.419   0.953 -33.229  1.00 47.48           C  
ANISOU 4625  C   ASN E  74     6016   7349   4675    578   1009    565       C  
ATOM   4626  O   ASN E  74      17.269  -0.215 -32.862  1.00 42.01           O  
ANISOU 4626  O   ASN E  74     5367   6582   4014    672   1022    414       O  
ATOM   4627  CB  ASN E  74      19.867   1.452 -32.963  1.00 47.77           C  
ANISOU 4627  CB  ASN E  74     5722   7756   4674    534   1289    846       C  
ATOM   4628  CG  ASN E  74      20.781   2.653 -33.128  1.00 69.10           C  
ANISOU 4628  CG  ASN E  74     8288  10641   7324    317   1374   1070       C  
ATOM   4629  OD1 ASN E  74      20.724   3.357 -34.137  1.00 59.58           O  
ANISOU 4629  OD1 ASN E  74     7211   9473   5955    234   1405   1174       O  
ATOM   4630  ND2 ASN E  74      21.604   2.915 -32.119  1.00 73.18           N  
ANISOU 4630  ND2 ASN E  74     8572  11270   7964    190   1400   1150       N  
ATOM   4631  N   ILE E  75      16.699   1.512 -34.195  1.00 40.56           N  
ANISOU 4631  N   ILE E  75     5276   6466   3669    570    917    571       N  
ATOM   4632  CA  ILE E  75      15.726   0.779 -34.998  1.00 41.41           C  
ANISOU 4632  CA  ILE E  75     5545   6545   3643    657    823    387       C  
ATOM   4633  C   ILE E  75      16.125   0.955 -36.449  1.00 45.78           C  
ANISOU 4633  C   ILE E  75     6232   7251   3912    742    898    458       C  
ATOM   4634  O   ILE E  75      16.114   2.081 -36.959  1.00 52.05           O  
ANISOU 4634  O   ILE E  75     7074   8082   4619    690    860    625       O  
ATOM   4635  CB  ILE E  75      14.289   1.282 -34.780  1.00 40.75           C  
ANISOU 4635  CB  ILE E  75     5470   6374   3641    596    595    303       C  
ATOM   4636  CG1 ILE E  75      14.008   1.528 -33.299  1.00 42.27           C  
ANISOU 4636  CG1 ILE E  75     5514   6450   4098    494    551    289       C  
ATOM   4637  CG2 ILE E  75      13.283   0.320 -35.417  1.00 51.60           C  
ANISOU 4637  CG2 ILE E  75     6949   7767   4891    621    486     74       C  
ATOM   4638  CD1 ILE E  75      12.687   2.253 -33.055  1.00 42.82           C  
ANISOU 4638  CD1 ILE E  75     5544   6492   4235    483    353    227       C  
ATOM   4639  N   HIS E  76      16.480  -0.150 -37.114  1.00 49.26           N  
ANISOU 4639  N   HIS E  76     6777   7759   4180    880   1009    334       N  
ATOM   4640  CA  HIS E  76      16.989  -0.110 -38.482  1.00 49.94           C  
ANISOU 4640  CA  HIS E  76     6993   8025   3956    982   1125    385       C  
ATOM   4641  C   HIS E  76      16.831  -1.459 -39.172  1.00 47.74           C  
ANISOU 4641  C   HIS E  76     6922   7734   3485   1142   1162    146       C  
ATOM   4642  O   HIS E  76      17.466  -2.437 -38.752  1.00 55.51           O  
ANISOU 4642  O   HIS E  76     7905   8679   4506   1275   1298     54       O  
ATOM   4643  CB  HIS E  76      18.465   0.281 -38.486  1.00 50.52           C  
ANISOU 4643  CB  HIS E  76     6900   8309   3987    993   1373    586       C  
ATOM   4644  CG  HIS E  76      19.026   0.536 -39.852  1.00 54.52           C  
ANISOU 4644  CG  HIS E  76     7511   9046   4157   1050   1525    681       C  
ATOM   4645  ND1 HIS E  76      20.317   0.199 -40.194  1.00 64.26           N  
ANISOU 4645  ND1 HIS E  76     8616  10557   5242   1163   1803    737       N  
ATOM   4646  CD2 HIS E  76      18.489   1.126 -40.946  1.00 51.08           C  
ANISOU 4646  CD2 HIS E  76     7288   8637   3482   1016   1445    741       C  
ATOM   4647  CE1 HIS E  76      20.544   0.545 -41.452  1.00 64.77           C  
ANISOU 4647  CE1 HIS E  76     8806  10744   5061   1134   1867    797       C  
ATOM   4648  NE2 HIS E  76      19.452   1.113 -41.931  1.00 54.39           N  
ANISOU 4648  NE2 HIS E  76     7734   9327   3604   1079   1689    833       N  
ATOM   4649  N   PRO E  77      16.024  -1.562 -40.243  1.00 50.66           N  
ANISOU 4649  N   PRO E  77     7503   8125   3621   1152   1036     36       N  
ATOM   4650  CA  PRO E  77      15.229  -0.507 -40.882  1.00 48.41           C  
ANISOU 4650  CA  PRO E  77     7264   7900   3231   1073    848    136       C  
ATOM   4651  C   PRO E  77      13.936  -0.213 -40.127  1.00 50.18           C  
ANISOU 4651  C   PRO E  77     7391   8000   3676    954    581     57       C  
ATOM   4652  O   PRO E  77      13.343  -1.123 -39.554  1.00 58.99           O  
ANISOU 4652  O   PRO E  77     8491   9010   4911    891    510   -154       O  
ATOM   4653  CB  PRO E  77      14.922  -1.100 -42.250  1.00 66.00           C  
ANISOU 4653  CB  PRO E  77     9755  10227   5094   1169    816    -14       C  
ATOM   4654  CG  PRO E  77      14.800  -2.570 -41.976  1.00 60.93           C  
ANISOU 4654  CG  PRO E  77     9224   9450   4476   1204    845   -297       C  
ATOM   4655  CD  PRO E  77      15.788  -2.873 -40.877  1.00 53.63           C  
ANISOU 4655  CD  PRO E  77     8136   8446   3796   1259   1046   -228       C  
ATOM   4656  N   VAL E  78      13.513   1.051 -40.114  1.00 55.02           N  
ANISOU 4656  N   VAL E  78     7955   8624   4325    928    446    228       N  
ATOM   4657  CA  VAL E  78      12.218   1.380 -39.537  1.00 50.14           C  
ANISOU 4657  CA  VAL E  78     7225   7958   3866    886    192    138       C  
ATOM   4658  C   VAL E  78      11.122   0.871 -40.461  1.00 55.84           C  
ANISOU 4658  C   VAL E  78     8038   8813   4365    916    -23    -64       C  
ATOM   4659  O   VAL E  78      11.128   1.136 -41.672  1.00 51.46           O  
ANISOU 4659  O   VAL E  78     7666   8380   3507   1013    -73     -9       O  
ATOM   4660  CB  VAL E  78      12.096   2.890 -39.289  1.00 52.71           C  
ANISOU 4660  CB  VAL E  78     7530   8231   4265    920    104    368       C  
ATOM   4661  CG1 VAL E  78      10.663   3.243 -38.940  1.00 58.85           C  
ANISOU 4661  CG1 VAL E  78     8194   9035   5133    976   -171    253       C  
ATOM   4662  CG2 VAL E  78      13.013   3.307 -38.151  1.00 51.16           C  
ANISOU 4662  CG2 VAL E  78     7216   7901   4320    817    275    509       C  
ATOM   4663  N   GLU E  79      10.193   0.114 -39.893  1.00 56.42           N  
ANISOU 4663  N   GLU E  79     7988   8886   4563    800   -147   -300       N  
ATOM   4664  CA  GLU E  79       9.029  -0.446 -40.558  1.00 58.04           C  
ANISOU 4664  CA  GLU E  79     8207   9255   4589    741   -378   -534       C  
ATOM   4665  C   GLU E  79       7.764   0.255 -40.073  1.00 53.22           C  
ANISOU 4665  C   GLU E  79     7327   8791   4103    746   -630   -568       C  
ATOM   4666  O   GLU E  79       7.780   1.030 -39.112  1.00 50.53           O  
ANISOU 4666  O   GLU E  79     6827   8370   4004    793   -604   -443       O  
ATOM   4667  CB  GLU E  79       8.963  -1.960 -40.309  1.00 56.45           C  
ANISOU 4667  CB  GLU E  79     8094   8957   4399    543   -306   -797       C  
ATOM   4668  CG  GLU E  79      10.289  -2.659 -40.608  1.00 68.92           C  
ANISOU 4668  CG  GLU E  79     9929  10376   5881    628    -32   -768       C  
ATOM   4669  CD  GLU E  79      10.126  -4.140 -40.899  1.00 84.23           C  
ANISOU 4669  CD  GLU E  79    12123  12204   7678    505    -12  -1052       C  
ATOM   4670  OE1 GLU E  79       8.963  -4.603 -40.949  1.00 85.56           O  
ANISOU 4670  OE1 GLU E  79    12268  12437   7804    282   -221  -1269       O  
ATOM   4671  OE2 GLU E  79      11.155  -4.821 -41.144  1.00 69.54           O1-
ANISOU 4671  OE2 GLU E  79    10497  10208   5716    635    208  -1065       O1-
ATOM   4672  N   GLU E  80       6.658  -0.002 -40.777  1.00 58.49           N  
ANISOU 4672  N   GLU E  80     7939   9708   4577    718   -884   -749       N  
ATOM   4673  CA  GLU E  80       5.401   0.650 -40.427  1.00 65.46           C  
ANISOU 4673  CA  GLU E  80     8510  10828   5534    782  -1140   -800       C  
ATOM   4674  C   GLU E  80       4.930   0.249 -39.037  1.00 54.30           C  
ANISOU 4674  C   GLU E  80     6813   9391   4427    575  -1081   -931       C  
ATOM   4675  O   GLU E  80       4.316   1.056 -38.334  1.00 60.54           O  
ANISOU 4675  O   GLU E  80     7344  10283   5374    695  -1168   -891       O  
ATOM   4676  CB  GLU E  80       4.324   0.331 -41.467  1.00 66.95           C  
ANISOU 4676  CB  GLU E  80     8640  11368   5429    764  -1437   -995       C  
ATOM   4677  CG  GLU E  80       4.674   0.720 -42.899  1.00 79.57           C  
ANISOU 4677  CG  GLU E  80    10540  13027   6666    973  -1524   -873       C  
ATOM   4678  CD  GLU E  80       5.338  -0.398 -43.687  1.00 81.08           C  
ANISOU 4678  CD  GLU E  80    11050  13124   6633    806  -1386   -999       C  
ATOM   4679  OE1 GLU E  80       5.818  -1.375 -43.072  1.00 81.66           O  
ANISOU 4679  OE1 GLU E  80    11182  12985   6859    586  -1174  -1119       O  
ATOM   4680  OE2 GLU E  80       5.354  -0.309 -44.933  1.00 83.31           O1-
ANISOU 4680  OE2 GLU E  80    11554  13542   6558    920  -1499   -984       O1-
ATOM   4681  N   ASP E  81       5.221  -0.976 -38.615  1.00 54.24           N  
ANISOU 4681  N   ASP E  81     6887   9234   4487    286   -923  -1082       N  
ATOM   4682  CA  ASP E  81       4.781  -1.415 -37.300  1.00 58.19           C  
ANISOU 4682  CA  ASP E  81     7167   9703   5240     53   -853  -1190       C  
ATOM   4683  C   ASP E  81       5.512  -0.713 -36.160  1.00 58.36           C  
ANISOU 4683  C   ASP E  81     7142   9501   5531    172   -671   -987       C  
ATOM   4684  O   ASP E  81       5.169  -0.938 -34.994  1.00 58.07           O  
ANISOU 4684  O   ASP E  81     6927   9445   5694     10   -605  -1052       O  
ATOM   4685  CB  ASP E  81       4.953  -2.927 -37.178  1.00 62.12           C  
ANISOU 4685  CB  ASP E  81     7872  10029   5702   -284   -735  -1382       C  
ATOM   4686  CG  ASP E  81       4.048  -3.519 -36.125  1.00 75.88           C  
ANISOU 4686  CG  ASP E  81     9385  11853   7593   -627   -742  -1554       C  
ATOM   4687  OD1 ASP E  81       2.947  -2.962 -35.923  1.00 75.59           O1-
ANISOU 4687  OD1 ASP E  81     8964  12170   7586   -640   -913  -1623       O1-
ATOM   4688  OD2 ASP E  81       4.437  -4.523 -35.492  1.00 79.87           O  
ANISOU 4688  OD2 ASP E  81    10095  12082   8168   -865   -571  -1614       O  
ATOM   4689  N   ASP E  82       6.489   0.139 -36.459  1.00 55.65           N  
ANISOU 4689  N   ASP E  82     6960   9008   5177    414   -588   -746       N  
ATOM   4690  CA  ASP E  82       7.313   0.778 -35.444  1.00 47.08           C  
ANISOU 4690  CA  ASP E  82     5866   7708   4316    477   -420   -559       C  
ATOM   4691  C   ASP E  82       6.841   2.181 -35.069  1.00 45.04           C  
ANISOU 4691  C   ASP E  82     5467   7501   4143    685   -537   -443       C  
ATOM   4692  O   ASP E  82       7.423   2.784 -34.165  1.00 46.73           O  
ANISOU 4692  O   ASP E  82     5686   7535   4535    709   -421   -312       O  
ATOM   4693  CB  ASP E  82       8.778   0.818 -35.917  1.00 44.20           C  
ANISOU 4693  CB  ASP E  82     5754   7160   3880    552   -231   -372       C  
ATOM   4694  CG  ASP E  82       9.297  -0.564 -36.351  1.00 52.96           C  
ANISOU 4694  CG  ASP E  82     7048   8202   4872    442   -107   -498       C  
ATOM   4695  OD1 ASP E  82       8.718  -1.580 -35.910  1.00 45.81           O  
ANISOU 4695  OD1 ASP E  82     6120   7276   4011    249   -124   -701       O  
ATOM   4696  OD2 ASP E  82      10.243  -0.638 -37.176  1.00 52.55           O1-
ANISOU 4696  OD2 ASP E  82     7188   8122   4655    550      9   -403       O1-
ATOM   4697  N   VAL E  83       5.817   2.721 -35.729  1.00 51.49           N  
ANISOU 4697  N   VAL E  83     6184   8556   4822    857   -773   -493       N  
ATOM   4698  CA  VAL E  83       5.312   4.044 -35.357  1.00 54.69           C  
ANISOU 4698  CA  VAL E  83     6503   8986   5292   1130   -894   -398       C  
ATOM   4699  C   VAL E  83       4.666   3.920 -33.984  1.00 51.35           C  
ANISOU 4699  C   VAL E  83     5780   8634   5097   1038   -853   -541       C  
ATOM   4700  O   VAL E  83       3.622   3.280 -33.835  1.00 58.48           O  
ANISOU 4700  O   VAL E  83     6394   9837   5990    917   -944   -762       O  
ATOM   4701  CB  VAL E  83       4.321   4.602 -36.386  1.00 61.03           C  
ANISOU 4701  CB  VAL E  83     7258  10064   5867   1407  -1181   -423       C  
ATOM   4702  CG1 VAL E  83       5.062   5.236 -37.552  1.00 62.91           C  
ANISOU 4702  CG1 VAL E  83     7872  10153   5879   1576  -1205   -190       C  
ATOM   4703  CG2 VAL E  83       3.353   3.529 -36.868  1.00 65.78           C  
ANISOU 4703  CG2 VAL E  83     7617  11033   6343   1232  -1326   -688       C  
ATOM   4704  N   ALA E  84       5.287   4.520 -32.979  1.00 52.28           N  
ANISOU 4704  N   ALA E  84     5965   8501   5397   1058   -711   -423       N  
ATOM   4705  CA  ALA E  84       4.864   4.319 -31.597  1.00 45.22           C  
ANISOU 4705  CA  ALA E  84     4836   7644   4700    938   -624   -547       C  
ATOM   4706  C   ALA E  84       5.619   5.305 -30.720  1.00 48.11           C  
ANISOU 4706  C   ALA E  84     5361   7712   5206   1032   -518   -385       C  
ATOM   4707  O   ALA E  84       6.470   6.067 -31.191  1.00 41.82           O  
ANISOU 4707  O   ALA E  84     4845   6686   4358   1134   -506   -181       O  
ATOM   4708  CB  ALA E  84       5.119   2.878 -31.151  1.00 46.44           C  
ANISOU 4708  CB  ALA E  84     4947   7782   4914    564   -470   -664       C  
ATOM   4709  N   MET E  85       5.301   5.278 -29.428  1.00 41.96           N  
ANISOU 4709  N   MET E  85     4413   6949   4582    958   -435   -483       N  
ATOM   4710  CA  MET E  85       6.088   5.964 -28.418  1.00 40.65           C  
ANISOU 4710  CA  MET E  85     4399   6501   4546    953   -316   -369       C  
ATOM   4711  C   MET E  85       7.100   4.984 -27.833  1.00 49.67           C  
ANISOU 4711  C   MET E  85     5591   7506   5773    636   -130   -332       C  
ATOM   4712  O   MET E  85       6.800   3.797 -27.665  1.00 43.83           O  
ANISOU 4712  O   MET E  85     4722   6891   5039    431    -75   -458       O  
ATOM   4713  CB  MET E  85       5.187   6.521 -27.305  1.00 43.45           C  
ANISOU 4713  CB  MET E  85     4567   6958   4983   1088   -327   -504       C  
ATOM   4714  CG  MET E  85       5.908   7.429 -26.336  1.00 43.98           C  
ANISOU 4714  CG  MET E  85     4847   6718   5144   1120   -244   -405       C  
ATOM   4715  SD  MET E  85       5.997   9.141 -26.936  1.00 66.11           S  
ANISOU 4715  SD  MET E  85     8002   9260   7857   1500   -393   -253       S  
ATOM   4716  CE  MET E  85       4.659   9.147 -28.115  1.00 39.94           C  
ANISOU 4716  CE  MET E  85     4490   6297   4388   1838   -610   -350       C  
ATOM   4717  N   TYR E  86       8.303   5.476 -27.541  1.00 42.39           N  
ANISOU 4717  N   TYR E  86     4873   6334   4899    592    -43   -157       N  
ATOM   4718  CA  TYR E  86       9.348   4.668 -26.926  1.00 44.08           C  
ANISOU 4718  CA  TYR E  86     5117   6448   5182    365    112   -105       C  
ATOM   4719  C   TYR E  86       9.779   5.324 -25.619  1.00 43.62           C  
ANISOU 4719  C   TYR E  86     5091   6247   5236    314    168    -65       C  
ATOM   4720  O   TYR E  86       9.845   6.553 -25.534  1.00 44.76           O  
ANISOU 4720  O   TYR E  86     5363   6264   5381    426    111      4       O  
ATOM   4721  CB  TYR E  86      10.542   4.491 -27.901  1.00 37.16           C  
ANISOU 4721  CB  TYR E  86     4396   5504   4220    336    168     60       C  
ATOM   4722  CG  TYR E  86      10.129   3.700 -29.115  1.00 41.20           C  
ANISOU 4722  CG  TYR E  86     4909   6152   4595    373    123    -12       C  
ATOM   4723  CD1 TYR E  86       9.535   4.329 -30.205  1.00 47.21           C  
ANISOU 4723  CD1 TYR E  86     5722   6992   5223    542    -16      4       C  
ATOM   4724  CD2 TYR E  86      10.277   2.325 -29.155  1.00 44.76           C  
ANISOU 4724  CD2 TYR E  86     5347   6634   5023    249    203   -106       C  
ATOM   4725  CE1 TYR E  86       9.117   3.616 -31.310  1.00 41.64           C  
ANISOU 4725  CE1 TYR E  86     5024   6435   4364    561    -79    -80       C  
ATOM   4726  CE2 TYR E  86       9.866   1.599 -30.258  1.00 44.63           C  
ANISOU 4726  CE2 TYR E  86     5378   6722   4859    257    152   -201       C  
ATOM   4727  CZ  TYR E  86       9.286   2.249 -31.331  1.00 44.08           C  
ANISOU 4727  CZ  TYR E  86     5324   6769   4655    400      8   -194       C  
ATOM   4728  OH  TYR E  86       8.871   1.524 -32.432  1.00 43.75           O  
ANISOU 4728  OH  TYR E  86     5335   6851   4437    392    -61   -303       O  
ATOM   4729  N   PHE E  87      10.046   4.507 -24.588  1.00 37.66           N  
ANISOU 4729  N   PHE E  87     4266   5492   4551    143    271   -112       N  
ATOM   4730  CA  PHE E  87      10.467   5.018 -23.284  1.00 37.80           C  
ANISOU 4730  CA  PHE E  87     4316   5402   4645     73    316    -89       C  
ATOM   4731  C   PHE E  87      11.672   4.239 -22.771  1.00 36.65           C  
ANISOU 4731  C   PHE E  87     4197   5208   4518    -88    411      8       C  
ATOM   4732  O   PHE E  87      11.704   3.012 -22.875  1.00 39.31           O  
ANISOU 4732  O   PHE E  87     4506   5596   4833   -147    467    -26       O  
ATOM   4733  CB  PHE E  87       9.364   4.867 -22.214  1.00 31.49           C  
ANISOU 4733  CB  PHE E  87     3379   4706   3880     60    338   -267       C  
ATOM   4734  CG  PHE E  87       8.117   5.640 -22.487  1.00 37.36           C  
ANISOU 4734  CG  PHE E  87     4028   5568   4600    276    248   -389       C  
ATOM   4735  CD1 PHE E  87       7.078   5.047 -23.194  1.00 41.38           C  
ANISOU 4735  CD1 PHE E  87     4347   6317   5060    312    201   -510       C  
ATOM   4736  CD2 PHE E  87       7.918   6.909 -21.951  1.00 35.51           C  
ANISOU 4736  CD2 PHE E  87     3888   5228   4376    451    206   -408       C  
ATOM   4737  CE1 PHE E  87       5.890   5.734 -23.424  1.00 42.98           C  
ANISOU 4737  CE1 PHE E  87     4397   6711   5224    557    101   -633       C  
ATOM   4738  CE2 PHE E  87       6.738   7.596 -22.175  1.00 37.53           C  
ANISOU 4738  CE2 PHE E  87     4051   5615   4592    736    119   -532       C  
ATOM   4739  CZ  PHE E  87       5.716   7.011 -22.902  1.00 39.47           C  
ANISOU 4739  CZ  PHE E  87     4044   6162   4792    806     63   -642       C  
ATOM   4740  N   CYS E  88      12.627   4.937 -22.156  1.00 33.08           N  
ANISOU 4740  N   CYS E  88     3815   4663   4093   -155    416    115       N  
ATOM   4741  CA  CYS E  88      13.618   4.260 -21.332  1.00 34.70           C  
ANISOU 4741  CA  CYS E  88     3995   4882   4309   -276    478    180       C  
ATOM   4742  C   CYS E  88      13.113   4.177 -19.896  1.00 34.72           C  
ANISOU 4742  C   CYS E  88     3987   4869   4337   -345    494     77       C  
ATOM   4743  O   CYS E  88      12.226   4.923 -19.485  1.00 36.64           O  
ANISOU 4743  O   CYS E  88     4240   5086   4594   -304    466    -31       O  
ATOM   4744  CB  CYS E  88      14.975   4.974 -21.345  1.00 43.86           C  
ANISOU 4744  CB  CYS E  88     5179   6028   5457   -364    468    341       C  
ATOM   4745  SG  CYS E  88      14.935   6.782 -21.169  1.00 43.88           S  
ANISOU 4745  SG  CYS E  88     5346   5862   5463   -432    384    368       S  
ATOM   4746  N   GLN E  89      13.715   3.274 -19.124  1.00 36.95           N  
ANISOU 4746  N   GLN E  89     4264   5174   4601   -421    540    115       N  
ATOM   4747  CA  GLN E  89      13.283   3.024 -17.757  1.00 32.01           C  
ANISOU 4747  CA  GLN E  89     3659   4545   3958   -506    570     36       C  
ATOM   4748  C   GLN E  89      14.472   2.520 -16.954  1.00 39.27           C  
ANISOU 4748  C   GLN E  89     4609   5478   4835   -558    565    152       C  
ATOM   4749  O   GLN E  89      15.183   1.620 -17.410  1.00 37.53           O  
ANISOU 4749  O   GLN E  89     4389   5283   4589   -492    583    243       O  
ATOM   4750  CB  GLN E  89      12.150   1.999 -17.732  1.00 34.29           C  
ANISOU 4750  CB  GLN E  89     3932   4873   4223   -541    642    -83       C  
ATOM   4751  CG  GLN E  89      11.606   1.762 -16.320  1.00 33.69           C  
ANISOU 4751  CG  GLN E  89     3883   4820   4097   -662    705   -160       C  
ATOM   4752  CD  GLN E  89      12.123   0.464 -15.732  1.00 41.93           C  
ANISOU 4752  CD  GLN E  89     5061   5804   5065   -746    756    -78       C  
ATOM   4753  OE1 GLN E  89      12.282  -0.538 -16.436  1.00 41.31           O  
ANISOU 4753  OE1 GLN E  89     5058   5669   4968   -729    776    -41       O  
ATOM   4754  NE2 GLN E  89      12.452   0.492 -14.440  1.00 40.92           N  
ANISOU 4754  NE2 GLN E  89     5009   5669   4869   -813    765    -46       N  
ATOM   4755  N   GLN E  90      14.713   3.106 -15.781  1.00 33.46           N  
ANISOU 4755  N   GLN E  90     3905   4739   4070   -646    530    144       N  
ATOM   4756  CA  GLN E  90      15.813   2.667 -14.928  1.00 33.52           C  
ANISOU 4756  CA  GLN E  90     3921   4806   4008   -684    492    250       C  
ATOM   4757  C   GLN E  90      15.290   1.978 -13.674  1.00 37.95           C  
ANISOU 4757  C   GLN E  90     4590   5347   4481   -739    535    198       C  
ATOM   4758  O   GLN E  90      14.291   2.407 -13.080  1.00 36.42           O  
ANISOU 4758  O   GLN E  90     4436   5130   4272   -807    582     67       O  
ATOM   4759  CB  GLN E  90      16.737   3.816 -14.516  1.00 37.20           C  
ANISOU 4759  CB  GLN E  90     4354   5318   4464   -795    391    300       C  
ATOM   4760  CG  GLN E  90      16.070   4.860 -13.603  1.00 36.73           C  
ANISOU 4760  CG  GLN E  90     4412   5163   4380   -895    368    167       C  
ATOM   4761  CD  GLN E  90      16.138   4.499 -12.130  1.00 40.08           C  
ANISOU 4761  CD  GLN E  90     4908   5632   4688   -966    355    137       C  
ATOM   4762  OE1 GLN E  90      16.928   3.652 -11.701  1.00 40.67           O  
ANISOU 4762  OE1 GLN E  90     4949   5812   4691   -955    319    247       O  
ATOM   4763  NE2 GLN E  90      15.251   5.098 -11.354  1.00 36.71           N  
ANISOU 4763  NE2 GLN E  90     4594   5136   4217  -1000    389    -15       N  
ATOM   4764  N  ASER E  91      15.996   0.919 -13.270  0.53 40.27           N  
ANISOU 4764  N  ASER E  91     4943   5664   4693   -686    525    308       N  
ATOM   4765  N  BSER E  91      15.985   0.914 -13.270  0.47 40.26           N  
ANISOU 4765  N  BSER E  91     4944   5662   4692   -686    526    307       N  
ATOM   4766  CA ASER E  91      15.667   0.122 -12.093  0.53 35.12           C  
ANISOU 4766  CA ASER E  91     4460   4972   3915   -740    564    308       C  
ATOM   4767  CA BSER E  91      15.657   0.141 -12.078  0.47 36.40           C  
ANISOU 4767  CA BSER E  91     4620   5133   4075   -743    564    306       C  
ATOM   4768  C  ASER E  91      16.819   0.100 -11.093  0.53 37.33           C  
ANISOU 4768  C  ASER E  91     4759   5348   4078   -712    447    425       C  
ATOM   4769  C  BSER E  91      16.840   0.076 -11.115  0.47 37.41           C  
ANISOU 4769  C  BSER E  91     4768   5357   4088   -707    446    428       C  
ATOM   4770  O  ASER E  91      16.901  -0.808 -10.261  0.53 38.50           O  
ANISOU 4770  O  ASER E  91     5082   5458   4086   -684    451    492       O  
ATOM   4771  O  BSER E  91      16.961  -0.861 -10.325  0.47 38.50           O  
ANISOU 4771  O  BSER E  91     5080   5459   4090   -670    448    501       O  
ATOM   4772  CB ASER E  91      15.301  -1.301 -12.510  0.53 38.78           C  
ANISOU 4772  CB ASER E  91     5079   5314   4340   -687    650    338       C  
ATOM   4773  CB BSER E  91      15.180  -1.261 -12.464  0.47 38.74           C  
ANISOU 4773  CB BSER E  91     5075   5308   4335   -705    658    325       C  
ATOM   4774  OG ASER E  91      14.278  -1.298 -13.487  0.53 38.06           O  
ANISOU 4774  OG ASER E  91     4938   5184   4338   -739    730    221       O  
ATOM   4775  OG BSER E  91      15.993  -1.848 -13.473  0.47 35.71           O  
ANISOU 4775  OG BSER E  91     4677   4907   3982   -515    629    418       O  
ATOM   4776  N   ARG E  92      17.722   1.081 -11.168  1.00 36.52           N  
ANISOU 4776  N   ARG E  92     4491   5376   4009   -736    332    456       N  
ATOM   4777  CA  ARG E  92      18.880   1.117 -10.277  1.00 43.82           C  
ANISOU 4777  CA  ARG E  92     5369   6470   4812   -733    189    557       C  
ATOM   4778  C   ARG E  92      18.498   1.574  -8.875  1.00 44.12           C  
ANISOU 4778  C   ARG E  92     5549   6496   4718   -892    155    477       C  
ATOM   4779  O   ARG E  92      18.936   0.985  -7.881  1.00 42.12           O  
ANISOU 4779  O   ARG E  92     5393   6315   4297   -853     82    556       O  
ATOM   4780  CB  ARG E  92      19.958   2.048 -10.844  1.00 36.72           C  
ANISOU 4780  CB  ARG E  92     4223   5756   3973   -794     84    604       C  
ATOM   4781  CG  ARG E  92      21.166   2.282  -9.916  1.00 40.14           C  
ANISOU 4781  CG  ARG E  92     4535   6446   4271   -858    -95    682       C  
ATOM   4782  CD  ARG E  92      21.974   1.007  -9.676  1.00 52.28           C  
ANISOU 4782  CD  ARG E  92     6023   8146   5694   -578   -156    831       C  
ATOM   4783  NE  ARG E  92      23.034   1.209  -8.693  1.00 54.64           N  
ANISOU 4783  NE  ARG E  92     6185   8740   5834   -618   -355    897       N  
ATOM   4784  CZ  ARG E  92      22.850   1.115  -7.380  1.00 53.25           C  
ANISOU 4784  CZ  ARG E  92     6197   8545   5490   -675   -439    880       C  
ATOM   4785  NH1 ARG E  92      21.655   0.882  -6.867  1.00 49.69           N  
ANISOU 4785  NH1 ARG E  92     6062   7808   5008   -724   -318    798       N  
ATOM   4786  NH2 ARG E  92      23.888   1.261  -6.564  1.00 58.43           N  
ANISOU 4786  NH2 ARG E  92     6701   9517   5981   -697   -650    943       N  
ATOM   4787  N   LYS E  93      17.701   2.626  -8.777  1.00 43.69           N  
ANISOU 4787  N   LYS E  93     5532   6355   4714  -1037    202    321       N  
ATOM   4788  CA  LYS E  93      17.311   3.171  -7.487  1.00 45.90           C  
ANISOU 4788  CA  LYS E  93     5961   6627   4852  -1170    188    212       C  
ATOM   4789  C   LYS E  93      15.811   3.407  -7.476  1.00 39.80           C  
ANISOU 4789  C   LYS E  93     5276   5733   4113  -1185    362     40       C  
ATOM   4790  O   LYS E  93      15.193   3.620  -8.526  1.00 42.26           O  
ANISOU 4790  O   LYS E  93     5502   5976   4579  -1123    437    -14       O  
ATOM   4791  CB  LYS E  93      18.073   4.478  -7.202  1.00 47.16           C  
ANISOU 4791  CB  LYS E  93     6086   6844   4990  -1328     36    164       C  
ATOM   4792  CG  LYS E  93      19.508   4.251  -6.727  1.00 48.67           C  
ANISOU 4792  CG  LYS E  93     6160   7266   5065  -1368   -156    304       C  
ATOM   4793  CD  LYS E  93      20.241   5.552  -6.414  1.00 65.38           C  
ANISOU 4793  CD  LYS E  93     8252   9453   7138  -1622   -314    240       C  
ATOM   4794  CE  LYS E  93      21.702   5.268  -6.081  1.00 73.96           C  
ANISOU 4794  CE  LYS E  93     9118  10873   8112  -1669   -518    382       C  
ATOM   4795  NZ  LYS E  93      22.484   6.509  -5.837  1.00 76.97           N  
ANISOU 4795  NZ  LYS E  93     9451  11356   8438  -2004   -682    320       N  
ATOM   4796  N   VAL E  94      15.232   3.309  -6.283  1.00 42.82           N  
ANISOU 4796  N   VAL E  94     5810   6134   4325  -1254    428    -41       N  
ATOM   4797  CA  VAL E  94      13.843   3.715  -6.042  1.00 41.40           C  
ANISOU 4797  CA  VAL E  94     5668   5930   4133  -1269    598   -235       C  
ATOM   4798  C   VAL E  94      13.818   5.220  -5.786  1.00 41.16           C  
ANISOU 4798  C   VAL E  94     5694   5846   4099  -1277    536   -398       C  
ATOM   4799  O   VAL E  94      14.645   5.714  -5.011  1.00 45.66           O  
ANISOU 4799  O   VAL E  94     6375   6427   4546  -1376    400   -392       O  
ATOM   4800  CB  VAL E  94      13.268   2.948  -4.851  1.00 40.22           C  
ANISOU 4800  CB  VAL E  94     5667   5852   3764  -1357    724   -248       C  
ATOM   4801  CG1 VAL E  94      11.978   3.590  -4.333  1.00 50.02           C  
ANISOU 4801  CG1 VAL E  94     6912   7159   4935  -1372    899   -477       C  
ATOM   4802  CG2 VAL E  94      13.027   1.488  -5.231  1.00 38.88           C  
ANISOU 4802  CG2 VAL E  94     5520   5656   3598  -1373    818   -111       C  
ATOM   4803  N   PRO E  95      12.901   5.980  -6.400  1.00 44.76           N  
ANISOU 4803  N   PRO E  95     6104   6236   4665  -1168    616   -549       N  
ATOM   4804  CA  PRO E  95      11.813   5.571  -7.298  1.00 44.26           C  
ANISOU 4804  CA  PRO E  95     5876   6214   4725  -1054    753   -595       C  
ATOM   4805  C   PRO E  95      12.261   5.125  -8.673  1.00 43.07           C  
ANISOU 4805  C   PRO E  95     5596   6019   4751  -1011    690   -449       C  
ATOM   4806  O   PRO E  95      13.173   5.724  -9.267  1.00 42.69           O  
ANISOU 4806  O   PRO E  95     5557   5880   4783  -1008    556   -368       O  
ATOM   4807  CB  PRO E  95      10.972   6.843  -7.423  1.00 43.21           C  
ANISOU 4807  CB  PRO E  95     5769   6030   4618   -891    785   -802       C  
ATOM   4808  CG  PRO E  95      11.955   7.944  -7.257  1.00 48.95           C  
ANISOU 4808  CG  PRO E  95     6698   6572   5331   -937    618   -796       C  
ATOM   4809  CD  PRO E  95      12.967   7.445  -6.252  1.00 40.52           C  
ANISOU 4809  CD  PRO E  95     5714   5566   4118  -1142    538   -692       C  
ATOM   4810  N   LEU E  96      11.607   4.077  -9.174  1.00 35.31           N  
ANISOU 4810  N   LEU E  96     4503   5106   3805  -1009    797   -425       N  
ATOM   4811  CA  LEU E  96      11.752   3.712 -10.578  1.00 36.14           C  
ANISOU 4811  CA  LEU E  96     4496   5175   4059   -938    762   -342       C  
ATOM   4812  C   LEU E  96      11.314   4.897 -11.438  1.00 33.38           C  
ANISOU 4812  C   LEU E  96     4084   4781   3818   -790    718   -437       C  
ATOM   4813  O   LEU E  96      10.328   5.574 -11.128  1.00 36.63           O  
ANISOU 4813  O   LEU E  96     4475   5241   4203   -697    776   -606       O  
ATOM   4814  CB  LEU E  96      10.876   2.491 -10.872  1.00 42.06           C  
ANISOU 4814  CB  LEU E  96     5183   6002   4798  -1002    890   -358       C  
ATOM   4815  CG  LEU E  96      11.222   1.218 -10.080  1.00 43.87           C  
ANISOU 4815  CG  LEU E  96     5570   6206   4894  -1144    942   -245       C  
ATOM   4816  CD1 LEU E  96      10.386   0.026 -10.564  1.00 41.91           C  
ANISOU 4816  CD1 LEU E  96     5321   5969   4634  -1265   1060   -260       C  
ATOM   4817  CD2 LEU E  96      12.705   0.893 -10.136  1.00 41.16           C  
ANISOU 4817  CD2 LEU E  96     5323   5770   4546  -1076    806    -55       C  
ATOM   4818  N   THR E  97      12.061   5.183 -12.503  1.00 37.16           N  
ANISOU 4818  N   THR E  97     4549   5174   4394   -743    619   -325       N  
ATOM   4819  CA  THR E  97      11.715   6.331 -13.330  1.00 40.71           C  
ANISOU 4819  CA  THR E  97     5016   5537   4915   -601    564   -381       C  
ATOM   4820  C   THR E  97      11.846   5.975 -14.803  1.00 32.97           C  
ANISOU 4820  C   THR E  97     3944   4560   4022   -535    536   -283       C  
ATOM   4821  O   THR E  97      12.612   5.090 -15.185  1.00 38.65           O  
ANISOU 4821  O   THR E  97     4621   5312   4753   -603    536   -153       O  
ATOM   4822  CB  THR E  97      12.584   7.570 -13.031  1.00 37.01           C  
ANISOU 4822  CB  THR E  97     4737   4900   4426   -657    456   -351       C  
ATOM   4823  OG1 THR E  97      13.965   7.231 -13.166  1.00 38.29           O  
ANISOU 4823  OG1 THR E  97     4876   5082   4591   -819    386   -174       O  
ATOM   4824  CG2 THR E  97      12.325   8.099 -11.609  1.00 39.44           C  
ANISOU 4824  CG2 THR E  97     5186   5181   4618   -695    475   -494       C  
ATOM   4825  N   PHE E  98      11.073   6.687 -15.616  1.00 36.17           N  
ANISOU 4825  N   PHE E  98     4338   4941   4465   -363    508   -354       N  
ATOM   4826  CA  PHE E  98      11.025   6.536 -17.060  1.00 33.83           C  
ANISOU 4826  CA  PHE E  98     3982   4655   4216   -273    469   -283       C  
ATOM   4827  C   PHE E  98      11.443   7.856 -17.688  1.00 35.97           C  
ANISOU 4827  C   PHE E  98     4432   4741   4493   -192    372   -213       C  
ATOM   4828  O   PHE E  98      11.214   8.932 -17.111  1.00 34.20           O  
ANISOU 4828  O   PHE E  98     4375   4377   4241   -124    337   -289       O  
ATOM   4829  CB  PHE E  98       9.599   6.224 -17.567  1.00 35.41           C  
ANISOU 4829  CB  PHE E  98     4014   5024   4418   -127    495   -425       C  
ATOM   4830  CG  PHE E  98       9.007   4.934 -17.044  1.00 42.24           C  
ANISOU 4830  CG  PHE E  98     4728   6068   5255   -272    603   -504       C  
ATOM   4831  CD1 PHE E  98       8.578   4.823 -15.729  1.00 45.48           C  
ANISOU 4831  CD1 PHE E  98     5116   6552   5611   -356    696   -604       C  
ATOM   4832  CD2 PHE E  98       8.836   3.850 -17.897  1.00 36.82           C  
ANISOU 4832  CD2 PHE E  98     3959   5461   4570   -345    617   -484       C  
ATOM   4833  CE1 PHE E  98       8.012   3.629 -15.261  1.00 41.83           C  
ANISOU 4833  CE1 PHE E  98     4559   6239   5097   -545    811   -657       C  
ATOM   4834  CE2 PHE E  98       8.273   2.667 -17.447  1.00 40.85           C  
ANISOU 4834  CE2 PHE E  98     4400   6086   5035   -534    717   -553       C  
ATOM   4835  CZ  PHE E  98       7.867   2.555 -16.134  1.00 34.05           C  
ANISOU 4835  CZ  PHE E  98     3523   5294   4119   -649    818   -627       C  
ATOM   4836  N   GLY E  99      12.007   7.777 -18.887  1.00 38.21           N  
ANISOU 4836  N   GLY E  99     4723   5007   4789   -196    339    -74       N  
ATOM   4837  CA  GLY E  99      12.142   8.964 -19.705  1.00 36.04           C  
ANISOU 4837  CA  GLY E  99     4647   4556   4490   -112    258      0       C  
ATOM   4838  C   GLY E  99      10.789   9.469 -20.166  1.00 43.24           C  
ANISOU 4838  C   GLY E  99     5576   5470   5384    190    205   -122       C  
ATOM   4839  O   GLY E  99       9.773   8.785 -20.068  1.00 37.50           O  
ANISOU 4839  O   GLY E  99     4630   4952   4668    299    237   -260       O  
ATOM   4840  N   ALA E 100      10.775  10.696 -20.691  1.00 44.74           N  
ANISOU 4840  N   ALA E 100     6038   5434   5527    323    117    -67       N  
ATOM   4841  CA  ALA E 100       9.509  11.349 -21.012  1.00 39.52           C  
ANISOU 4841  CA  ALA E 100     5426   4764   4824    695     40   -185       C  
ATOM   4842  C   ALA E 100       8.837  10.767 -22.250  1.00 46.32           C  
ANISOU 4842  C   ALA E 100     6093   5846   5660    862     -9   -175       C  
ATOM   4843  O   ALA E 100       7.638  11.002 -22.452  1.00 47.73           O  
ANISOU 4843  O   ALA E 100     6170   6162   5802   1182    -78   -306       O  
ATOM   4844  CB  ALA E 100       9.730  12.853 -21.202  1.00 48.16           C  
ANISOU 4844  CB  ALA E 100     6970   5482   5848    816    -54   -113       C  
ATOM   4845  N   GLY E 101       9.569  10.043 -23.078  1.00 42.09           N  
ANISOU 4845  N   GLY E 101     5498   5373   5120    674     18    -38       N  
ATOM   4846  CA  GLY E 101       9.047   9.376 -24.256  1.00 45.30           C  
ANISOU 4846  CA  GLY E 101     5748   5988   5476    778    -28    -39       C  
ATOM   4847  C   GLY E 101       9.508  10.037 -25.553  1.00 51.91           C  
ANISOU 4847  C   GLY E 101     6838   6680   6205    850   -105    148       C  
ATOM   4848  O   GLY E 101       9.704  11.257 -25.631  1.00 47.87           O  
ANISOU 4848  O   GLY E 101     6650   5898   5641    942   -167    244       O  
ATOM   4849  N   THR E 102       9.685   9.214 -26.588  1.00 44.86           N  
ANISOU 4849  N   THR E 102     5844   5948   5254    795    -96    201       N  
ATOM   4850  CA  THR E 102      10.022   9.671 -27.938  1.00 50.71           C  
ANISOU 4850  CA  THR E 102     6800   6619   5849    864   -156    372       C  
ATOM   4851  C   THR E 102       8.941   9.210 -28.909  1.00 48.32           C  
ANISOU 4851  C   THR E 102     6355   6559   5444   1091   -277    275       C  
ATOM   4852  O   THR E 102       8.642   8.016 -28.985  1.00 50.27           O  
ANISOU 4852  O   THR E 102     6345   7043   5713    996   -241    148       O  
ATOM   4853  CB  THR E 102      11.391   9.141 -28.380  1.00 45.71           C  
ANISOU 4853  CB  THR E 102     6188   5992   5186    584    -20    530       C  
ATOM   4854  OG1 THR E 102      12.419   9.727 -27.573  1.00 50.03           O  
ANISOU 4854  OG1 THR E 102     6853   6358   5796    357     60    633       O  
ATOM   4855  CG2 THR E 102      11.648   9.487 -29.841  1.00 53.12           C  
ANISOU 4855  CG2 THR E 102     7327   6919   5936    645    -56    694       C  
ATOM   4856  N   LYS E 103       8.369  10.150 -29.662  1.00 47.76           N  
ANISOU 4856  N   LYS E 103     6482   6422   5242   1382   -433    336       N  
ATOM   4857  CA  LYS E 103       7.325   9.838 -30.635  1.00 53.96           C  
ANISOU 4857  CA  LYS E 103     7129   7477   5895   1624   -593    250       C  
ATOM   4858  C   LYS E 103       7.967   9.541 -31.985  1.00 60.63           C  
ANISOU 4858  C   LYS E 103     8133   8339   6564   1537   -587    406       C  
ATOM   4859  O   LYS E 103       8.534  10.433 -32.627  1.00 61.73           O  
ANISOU 4859  O   LYS E 103     8628   8255   6573   1582   -606    622       O  
ATOM   4860  CB  LYS E 103       6.322  10.984 -30.747  1.00 58.34           C  
ANISOU 4860  CB  LYS E 103     7808   7991   6366   2065   -789    232       C  
ATOM   4861  CG  LYS E 103       4.944  10.561 -31.249  1.00 65.57           C  
ANISOU 4861  CG  LYS E 103     8390   9329   7197   2337   -970     48       C  
ATOM   4862  CD  LYS E 103       4.021  11.766 -31.378  1.00 64.76           C  
ANISOU 4862  CD  LYS E 103     8418   9200   6989   2866  -1177     46       C  
ATOM   4863  CE  LYS E 103       3.221  11.743 -32.665  1.00 78.73           C  
ANISOU 4863  CE  LYS E 103    10121  11259   8533   3166  -1418     48       C  
ATOM   4864  NZ  LYS E 103       2.009  10.891 -32.531  1.00 79.94           N  
ANISOU 4864  NZ  LYS E 103     9693  11977   8705   3215  -1508   -229       N  
ATOM   4865  N   LEU E 104       7.879   8.287 -32.415  1.00 60.70           N  
ANISOU 4865  N   LEU E 104     7916   8601   6547   1396   -552    294       N  
ATOM   4866  CA  LEU E 104       8.370   7.875 -33.721  1.00 59.62           C  
ANISOU 4866  CA  LEU E 104     7910   8530   6212   1345   -543    392       C  
ATOM   4867  C   LEU E 104       7.242   7.962 -34.739  1.00 57.35           C  
ANISOU 4867  C   LEU E 104     7594   8470   5725   1614   -780    321       C  
ATOM   4868  O   LEU E 104       6.195   7.329 -34.574  1.00 50.61           O  
ANISOU 4868  O   LEU E 104     6434   7897   4900   1654   -888     96       O  
ATOM   4869  CB  LEU E 104       8.933   6.457 -33.669  1.00 57.59           C  
ANISOU 4869  CB  LEU E 104     7499   8384   6001   1078   -380    294       C  
ATOM   4870  CG  LEU E 104       9.687   6.074 -34.942  1.00 58.73           C  
ANISOU 4870  CG  LEU E 104     7818   8569   5929   1031   -314    401       C  
ATOM   4871  CD1 LEU E 104      10.869   7.002 -35.168  1.00 69.86           C  
ANISOU 4871  CD1 LEU E 104     9481   9782   7280    971   -192    672       C  
ATOM   4872  CD2 LEU E 104      10.150   4.641 -34.826  1.00 52.14           C  
ANISOU 4872  CD2 LEU E 104     6866   7814   5132    843   -164    270       C  
ATOM   4873  N   GLU E 105       7.461   8.737 -35.794  1.00 62.25           N  
ANISOU 4873  N   GLU E 105     8531   8998   6123   1774   -866    518       N  
ATOM   4874  CA  GLU E 105       6.457   8.919 -36.824  1.00 61.15           C  
ANISOU 4874  CA  GLU E 105     8403   9080   5750   2071  -1123    482       C  
ATOM   4875  C   GLU E 105       7.085   8.698 -38.190  1.00 70.30           C  
ANISOU 4875  C   GLU E 105     9816  10263   6631   2005  -1099    626       C  
ATOM   4876  O   GLU E 105       8.266   8.988 -38.409  1.00 60.68           O  
ANISOU 4876  O   GLU E 105     8865   8823   5366   1833   -908    837       O  
ATOM   4877  CB  GLU E 105       5.825  10.312 -36.754  1.00 70.53           C  
ANISOU 4877  CB  GLU E 105     9793  10124   6881   2472  -1315    588       C  
ATOM   4878  CG  GLU E 105       4.615  10.388 -35.830  1.00 78.55           C  
ANISOU 4878  CG  GLU E 105    10450  11342   8052   2705  -1443    358       C  
ATOM   4879  CD  GLU E 105       3.447   9.535 -36.303  1.00 91.04           C  
ANISOU 4879  CD  GLU E 105    11612  13437   9541   2785  -1631    118       C  
ATOM   4880  OE1 GLU E 105       2.563   9.228 -35.470  1.00 92.27           O  
ANISOU 4880  OE1 GLU E 105    11357  13858   9842   2819  -1663   -110       O  
ATOM   4881  OE2 GLU E 105       3.421   9.162 -37.498  1.00 90.98           O1-
ANISOU 4881  OE2 GLU E 105    11682  13589   9297   2779  -1740    150       O1-
ATOM   4882  N   LEU E 106       6.280   8.174 -39.104  1.00 65.75           N  
ANISOU 4882  N   LEU E 106     9135   9997   5849   2125  -1291    499       N  
ATOM   4883  CA  LEU E 106       6.711   7.950 -40.471  1.00 68.94           C  
ANISOU 4883  CA  LEU E 106     9789  10469   5935   2104  -1298    605       C  
ATOM   4884  C   LEU E 106       6.399   9.182 -41.301  1.00 78.27           C  
ANISOU 4884  C   LEU E 106    11320  11571   6850   2445  -1504    832       C  
ATOM   4885  O   LEU E 106       5.277   9.695 -41.256  1.00 89.24           O  
ANISOU 4885  O   LEU E 106    12610  13092   8205   2786  -1778    768       O  
ATOM   4886  CB  LEU E 106       6.012   6.726 -41.052  1.00 71.38           C  
ANISOU 4886  CB  LEU E 106     9858  11142   6120   2028  -1417    336       C  
ATOM   4887  CG  LEU E 106       6.675   5.400 -40.697  1.00 68.08           C  
ANISOU 4887  CG  LEU E 106     9320  10715   5832   1673  -1171    178       C  
ATOM   4888  CD1 LEU E 106       5.944   4.290 -41.406  1.00 68.34           C  
ANISOU 4888  CD1 LEU E 106     9230  11053   5684   1584  -1317    -84       C  
ATOM   4889  CD2 LEU E 106       8.152   5.420 -41.069  1.00 72.13           C  
ANISOU 4889  CD2 LEU E 106    10119  11017   6269   1543   -890    384       C  
ATOM   4890  N   LYS E 107       7.397   9.660 -42.037  1.00 80.44           N  
ANISOU 4890  N   LYS E 107    12002  11640   6920   2362  -1367   1102       N  
ATOM   4891  CA  LYS E 107       7.203  10.768 -42.962  1.00 94.22           C  
ANISOU 4891  CA  LYS E 107    14183  13270   8348   2648  -1546   1356       C  
ATOM   4892  C   LYS E 107       6.050  10.454 -43.908  1.00103.39           C  
ANISOU 4892  C   LYS E 107    15194  14766   9324   2875  -1835   1195       C  
ATOM   4893  O   LYS E 107       6.083   9.449 -44.627  1.00 98.79           O  
ANISOU 4893  O   LYS E 107    14505  14456   8575   2733  -1827   1061       O  
ATOM   4894  CB  LYS E 107       8.498  11.020 -43.740  1.00 89.92           C  
ANISOU 4894  CB  LYS E 107    14028  12543   7594   2388  -1294   1631       C  
ATOM   4895  CG  LYS E 107       9.606  11.641 -42.892  1.00 88.53           C  
ANISOU 4895  CG  LYS E 107    14012  12016   7611   2118  -1025   1822       C  
ATOM   4896  CD  LYS E 107      10.588  12.451 -43.724  1.00 89.11           C  
ANISOU 4896  CD  LYS E 107    14514  11874   7470   1903   -857   2138       C  
ATOM   4897  CE  LYS E 107      11.694  13.034 -42.853  1.00 86.90           C  
ANISOU 4897  CE  LYS E 107    14363  11299   7355   1570   -604   2313       C  
ATOM   4898  NZ  LYS E 107      13.016  13.033 -43.539  1.00 95.34           N  
ANISOU 4898  NZ  LYS E 107    15539  12418   8270   1169   -301   2505       N  
ATOM   4899  N   ARG E 108       5.028  11.311 -43.884  1.00107.23           N  
ANISOU 4899  N   ARG E 108    15661  15227   9854   3215  -2074   1187       N  
ATOM   4900  CA  ARG E 108       3.740  11.079 -44.548  1.00103.48           C  
ANISOU 4900  CA  ARG E 108    14927  15119   9273   3448  -2363   1000       C  
ATOM   4901  C   ARG E 108       3.005   9.913 -43.902  1.00106.38           C  
ANISOU 4901  C   ARG E 108    14728  15900   9792   3351  -2436    651       C  
ATOM   4902  O   ARG E 108       2.245  10.104 -42.952  1.00108.59           O  
ANISOU 4902  O   ARG E 108    14689  16275  10293   3509  -2512    508       O  
ATOM   4903  CB  ARG E 108       3.916  10.825 -46.046  1.00100.80           C  
ANISOU 4903  CB  ARG E 108    14807  14892   8599   3374  -2409   1079       C  
ATOM   4904  CG  ARG E 108       4.408  12.033 -46.806  1.00112.98           C  
ANISOU 4904  CG  ARG E 108    16880  16086   9962   3475  -2380   1411       C  
ATOM   4905  CD  ARG E 108       4.523  11.751 -48.292  1.00123.43           C  
ANISOU 4905  CD  ARG E 108    18396  17566  10936   3405  -2430   1478       C  
ATOM   4906  NE  ARG E 108       5.063  12.902 -49.004  1.00129.42           N  
ANISOU 4906  NE  ARG E 108    19672  17993  11510   3448  -2376   1812       N  
ATOM   4907  CZ  ARG E 108       5.383  12.911 -50.291  1.00129.83           C  
ANISOU 4907  CZ  ARG E 108    19993  18099  11236   3366  -2367   1949       C  
ATOM   4908  NH1 ARG E 108       5.251  11.831 -51.044  1.00127.31           N  
ANISOU 4908  NH1 ARG E 108    19506  18135  10730   3247  -2407   1776       N  
ATOM   4909  NH2 ARG E 108       5.850  14.031 -50.835  1.00127.97           N  
ANISOU 4909  NH2 ARG E 108    20230  17548  10847   3386  -2313   2260       N  
ATOM   4910  N   TYR E 112      -1.198   1.219 -46.621  1.00108.32           N  
ANISOU 4910  N   TYR E 112    13256  18466   9436   1234  -3125  -1412       N  
ATOM   4911  CA  TYR E 112      -1.594  -0.046 -46.011  1.00105.51           C  
ANISOU 4911  CA  TYR E 112    12687  18198   9205    739  -3067  -1715       C  
ATOM   4912  C   TYR E 112      -1.223  -1.235 -46.900  1.00107.23           C  
ANISOU 4912  C   TYR E 112    13276  18300   9166    390  -3046  -1889       C  
ATOM   4913  O   TYR E 112      -1.665  -2.359 -46.661  1.00107.35           O  
ANISOU 4913  O   TYR E 112    13213  18352   9223    -54  -3042  -2150       O  
ATOM   4914  CB  TYR E 112      -3.101  -0.060 -45.721  1.00106.51           C  
ANISOU 4914  CB  TYR E 112    12263  18756   9448    653  -3273  -1874       C  
ATOM   4915  CG  TYR E 112      -3.515   0.683 -44.463  1.00105.68           C  
ANISOU 4915  CG  TYR E 112    11751  18748   9655    854  -3200  -1815       C  
ATOM   4916  CD1 TYR E 112      -3.104   0.247 -43.207  1.00105.02           C  
ANISOU 4916  CD1 TYR E 112    11586  18494   9824    610  -2954  -1880       C  
ATOM   4917  CD2 TYR E 112      -4.345   1.800 -44.529  1.00106.42           C  
ANISOU 4917  CD2 TYR E 112    11568  19097   9771   1296  -3372  -1709       C  
ATOM   4918  CE1 TYR E 112      -3.487   0.915 -42.053  1.00100.89           C  
ANISOU 4918  CE1 TYR E 112    10712  18059   9564    788  -2877  -1837       C  
ATOM   4919  CE2 TYR E 112      -4.734   2.474 -43.380  1.00100.15           C  
ANISOU 4919  CE2 TYR E 112    10442  18372   9238   1507  -3284  -1679       C  
ATOM   4920  CZ  TYR E 112      -4.301   2.026 -42.145  1.00 99.65           C  
ANISOU 4920  CZ  TYR E 112    10299  18146   9419   1242  -3035  -1744       C  
ATOM   4921  OH  TYR E 112      -4.683   2.688 -40.998  1.00 92.58           O  
ANISOU 4921  OH  TYR E 112     9099  17317   8760   1447  -2936  -1724       O  
ATOM   4922  N   GLU E 113      -0.407  -0.978 -47.926  1.00100.57           N  
ANISOU 4922  N   GLU E 113    12896  14449  10867    501   2622  -1943       N  
ATOM   4923  CA  GLU E 113       0.029  -2.036 -48.833  1.00105.99           C  
ANISOU 4923  CA  GLU E 113    13515  15308  11449    593   2623  -2243       C  
ATOM   4924  C   GLU E 113       1.002  -3.008 -48.176  1.00105.94           C  
ANISOU 4924  C   GLU E 113    13222  15277  11752    687   2515  -2590       C  
ATOM   4925  O   GLU E 113       1.124  -4.151 -48.632  1.00107.50           O  
ANISOU 4925  O   GLU E 113    13367  15537  11943    817   2401  -2841       O  
ATOM   4926  CB  GLU E 113       0.667  -1.420 -50.083  1.00103.54           C  
ANISOU 4926  CB  GLU E 113    13264  15213  10862    483   3014  -2272       C  
ATOM   4927  CG  GLU E 113       1.016  -2.411 -51.193  1.00109.02           C  
ANISOU 4927  CG  GLU E 113    13919  16126  11378    572   3043  -2571       C  
ATOM   4928  CD  GLU E 113      -0.191  -2.875 -51.999  1.00112.84           C  
ANISOU 4928  CD  GLU E 113    14627  16694  11553    687   2850  -2480       C  
ATOM   4929  OE1 GLU E 113      -1.343  -2.642 -51.564  1.00101.56           O  
ANISOU 4929  OE1 GLU E 113    13350  15138  10102    723   2629  -2220       O  
ATOM   4930  OE2 GLU E 113       0.022  -3.478 -53.076  1.00 94.00           O  
ANISOU 4930  OE2 GLU E 113    12245  14526   8944    741   2920  -2700       O  
ATOM   4931  N   PHE E 114       1.690  -2.580 -47.117  1.00106.02           N  
ANISOU 4931  N   PHE E 114    13045  15207  12032    642   2543  -2624       N  
ATOM   4932  CA  PHE E 114       2.600  -3.470 -46.405  1.00104.08           C  
ANISOU 4932  CA  PHE E 114    12524  14954  12066    782   2408  -2940       C  
ATOM   4933  C   PHE E 114       1.871  -4.663 -45.794  1.00 97.46           C  
ANISOU 4933  C   PHE E 114    11746  13939  11346    991   2028  -2937       C  
ATOM   4934  O   PHE E 114       2.467  -5.735 -45.630  1.00 96.28           O  
ANISOU 4934  O   PHE E 114    11447  13784  11349   1167   1908  -3212       O  
ATOM   4935  CB  PHE E 114       3.337  -2.685 -45.320  1.00 97.08           C  
ANISOU 4935  CB  PHE E 114    11429  14041  11416    705   2480  -2962       C  
ATOM   4936  CG  PHE E 114       2.436  -2.163 -44.236  1.00 96.15           C  
ANISOU 4936  CG  PHE E 114    11428  13725  11379    689   2292  -2656       C  
ATOM   4937  CD1 PHE E 114       1.689  -1.010 -44.434  1.00 94.14           C  
ANISOU 4937  CD1 PHE E 114    11382  13409  10978    516   2435  -2335       C  
ATOM   4938  CD2 PHE E 114       2.329  -2.824 -43.024  1.00 87.29           C  
ANISOU 4938  CD2 PHE E 114    10223  12478  10466    865   1983  -2682       C  
ATOM   4939  CE1 PHE E 114       0.859  -0.527 -43.445  1.00 94.50           C  
ANISOU 4939  CE1 PHE E 114    11522  13281  11104    505   2269  -2077       C  
ATOM   4940  CE2 PHE E 114       1.498  -2.344 -42.031  1.00 89.44           C  
ANISOU 4940  CE2 PHE E 114    10600  12586  10796    845   1827  -2411       C  
ATOM   4941  CZ  PHE E 114       0.763  -1.195 -42.242  1.00 93.31           C  
ANISOU 4941  CZ  PHE E 114    11270  13025  11157    658   1968  -2123       C  
ATOM   4942  N   LEU E 115       0.586  -4.497 -45.463  1.00 92.06           N  
ANISOU 4942  N   LEU E 115    11283  13098  10599    977   1854  -2636       N  
ATOM   4943  CA  LEU E 115      -0.184  -5.548 -44.804  1.00 84.96           C  
ANISOU 4943  CA  LEU E 115    10456  11995   9828   1135   1534  -2610       C  
ATOM   4944  C   LEU E 115      -0.295  -6.812 -45.650  1.00 91.75           C  
ANISOU 4944  C   LEU E 115    11348  12875  10638   1252   1458  -2845       C  
ATOM   4945  O   LEU E 115      -0.470  -7.904 -45.097  1.00 90.05           O  
ANISOU 4945  O   LEU E 115    11131  12477  10606   1409   1247  -2936       O  
ATOM   4946  CB  LEU E 115      -1.580  -5.025 -44.469  1.00 74.97           C  
ANISOU 4946  CB  LEU E 115     9408  10599   8478   1059   1412  -2267       C  
ATOM   4947  CG  LEU E 115      -1.667  -4.037 -43.305  1.00 77.36           C  
ANISOU 4947  CG  LEU E 115     9687  10804   8901    987   1402  -2041       C  
ATOM   4948  CD1 LEU E 115      -3.086  -3.534 -43.163  1.00 73.31           C  
ANISOU 4948  CD1 LEU E 115     9387  10187   8279    918   1300  -1728       C  
ATOM   4949  CD2 LEU E 115      -1.179  -4.659 -42.000  1.00 69.38           C  
ANISOU 4949  CD2 LEU E 115     8533   9667   8161   1135   1218  -2133       C  
ATOM   4950  N   LYS E 116      -0.200  -6.695 -46.974  1.00 96.88           N  
ANISOU 4950  N   LYS E 116    12038  13732  11040   1183   1638  -2948       N  
ATOM   4951  CA  LYS E 116      -0.279  -7.869 -47.832  1.00100.24           C  
ANISOU 4951  CA  LYS E 116    12475  14203  11410   1285   1580  -3216       C  
ATOM   4952  C   LYS E 116       0.962  -8.749 -47.733  1.00 99.03           C  
ANISOU 4952  C   LYS E 116    12100  14063  11464   1434   1601  -3572       C  
ATOM   4953  O   LYS E 116       0.936  -9.884 -48.221  1.00107.17           O  
ANISOU 4953  O   LYS E 116    13128  15063  12530   1551   1521  -3821       O  
ATOM   4954  CB  LYS E 116      -0.516  -7.422 -49.275  1.00105.61           C  
ANISOU 4954  CB  LYS E 116    13262  15145  11721   1184   1771  -3224       C  
ATOM   4955  CG  LYS E 116      -1.862  -6.725 -49.462  1.00101.40           C  
ANISOU 4955  CG  LYS E 116    12956  14609  10961   1102   1700  -2899       C  
ATOM   4956  CD  LYS E 116      -1.976  -6.047 -50.820  1.00105.91           C  
ANISOU 4956  CD  LYS E 116    13650  15467  11123   1032   1916  -2848       C  
ATOM   4957  CE  LYS E 116      -3.336  -5.382 -50.983  1.00 93.58           C  
ANISOU 4957  CE  LYS E 116    12308  13917   9332   1005   1813  -2531       C  
ATOM   4958  NZ  LYS E 116      -3.397  -4.505 -52.184  1.00102.35           N  
ANISOU 4958  NZ  LYS E 116    13574  15297  10018    967   2042  -2399       N  
ATOM   4959  N   SER E 117       2.034  -8.258 -47.106  1.00 95.24           N  
ANISOU 4959  N   SER E 117    11422  13633  11133   1439   1702  -3626       N  
ATOM   4960  CA  SER E 117       3.252  -9.027 -46.882  1.00100.67           C  
ANISOU 4960  CA  SER E 117    11865  14353  12033   1615   1698  -3969       C  
ATOM   4961  C   SER E 117       3.264  -9.749 -45.541  1.00 94.38           C  
ANISOU 4961  C   SER E 117    11030  13304  11524   1833   1424  -3945       C  
ATOM   4962  O   SER E 117       4.182 -10.536 -45.287  1.00102.58           O  
ANISOU 4962  O   SER E 117    11889  14340  12745   2046   1369  -4219       O  
ATOM   4963  CB  SER E 117       4.478  -8.111 -46.970  1.00100.41           C  
ANISOU 4963  CB  SER E 117    11592  14556  12003   1507   1968  -4098       C  
ATOM   4964  OG  SER E 117       5.666  -8.811 -46.643  1.00103.38           O  
ANISOU 4964  OG  SER E 117    11692  14990  12599   1701   1938  -4448       O  
ATOM   4965  N   TRP E 118       2.274  -9.508 -44.690  1.00 80.89           N  
ANISOU 4965  N   TRP E 118     9494  11392   9848   1804   1256  -3625       N  
ATOM   4966  CA  TRP E 118       2.240 -10.088 -43.358  1.00 83.82           C  
ANISOU 4966  CA  TRP E 118     9866  11530  10454   2007   1019  -3550       C  
ATOM   4967  C   TRP E 118       1.605 -11.471 -43.381  1.00 85.50           C  
ANISOU 4967  C   TRP E 118    10241  11477  10768   2169    845  -3602       C  
ATOM   4968  O   TRP E 118       0.789 -11.792 -44.250  1.00 90.34           O  
ANISOU 4968  O   TRP E 118    11003  12061  11262   2066    866  -3613       O  
ATOM   4969  CB  TRP E 118       1.448  -9.187 -42.412  1.00 77.88           C  
ANISOU 4969  CB  TRP E 118     9225  10679   9686   1889    944  -3189       C  
ATOM   4970  CG  TRP E 118       2.178  -7.960 -41.997  1.00 85.16           C  
ANISOU 4970  CG  TRP E 118     9965  11786  10605   1779   1081  -3162       C  
ATOM   4971  CD1 TRP E 118       3.223  -7.367 -42.645  1.00 85.83           C  
ANISOU 4971  CD1 TRP E 118     9841  12127  10643   1681   1324  -3378       C  
ATOM   4972  CD2 TRP E 118       1.893  -7.144 -40.860  1.00 77.96           C  
ANISOU 4972  CD2 TRP E 118     9059  10816   9748   1727   1010  -2926       C  
ATOM   4973  NE1 TRP E 118       3.621  -6.242 -41.966  1.00 82.60           N  
ANISOU 4973  NE1 TRP E 118     9299  11805  10280   1563   1414  -3304       N  
ATOM   4974  CE2 TRP E 118       2.817  -6.080 -40.868  1.00 83.44           C  
ANISOU 4974  CE2 TRP E 118     9532  11728  10444   1595   1214  -3032       C  
ATOM   4975  CE3 TRP E 118       0.950  -7.212 -39.831  1.00 84.21           C  
ANISOU 4975  CE3 TRP E 118    10013  11393  10591   1768    810  -2654       C  
ATOM   4976  CZ2 TRP E 118       2.828  -5.094 -39.886  1.00 74.85           C  
ANISOU 4976  CZ2 TRP E 118     8375  10648   9415   1510   1212  -2893       C  
ATOM   4977  CZ3 TRP E 118       0.961  -6.231 -38.858  1.00 79.43           C  
ANISOU 4977  CZ3 TRP E 118     9344  10814  10020   1697    801  -2501       C  
ATOM   4978  CH2 TRP E 118       1.893  -5.186 -38.893  1.00 83.88           C  
ANISOU 4978  CH2 TRP E 118     9682  11596  10593   1571    994  -2629       C  
ATOM   4979  N   THR E 119       1.986 -12.292 -42.405  1.00 94.05           N  
ANISOU 4979  N   THR E 119    11298  12365  12070   2431    678  -3641       N  
ATOM   4980  CA  THR E 119       1.333 -13.579 -42.217  1.00 92.85           C  
ANISOU 4980  CA  THR E 119    11340  11882  12057   2581    532  -3640       C  
ATOM   4981  C   THR E 119      -0.077 -13.374 -41.676  1.00 87.18           C  
ANISOU 4981  C   THR E 119    10863  10950  11310   2435    440  -3300       C  
ATOM   4982  O   THR E 119      -0.377 -12.365 -41.030  1.00 80.39           O  
ANISOU 4982  O   THR E 119    10010  10153  10383   2319    427  -3046       O  
ATOM   4983  CB  THR E 119       2.137 -14.462 -41.260  1.00 92.65           C  
ANISOU 4983  CB  THR E 119    11256  11688  12258   2935    392  -3728       C  
ATOM   4984  OG1 THR E 119       1.877 -14.065 -39.904  1.00 90.15           O  
ANISOU 4984  OG1 THR E 119    11005  11264  11985   2999    259  -3430       O  
ATOM   4985  CG2 THR E 119       3.626 -14.335 -41.545  1.00 94.34           C  
ANISOU 4985  CG2 THR E 119    11159  12188  12496   3077    472  -4046       C  
ATOM   4986  N   VAL E 120      -0.950 -14.346 -41.951  1.00 78.82           N  
ANISOU 4986  N   VAL E 120     9989   9636  10321   2433    387  -3325       N  
ATOM   4987  CA  VAL E 120      -2.338 -14.224 -41.510  1.00 81.01           C  
ANISOU 4987  CA  VAL E 120    10473   9720  10586   2277    316  -3051       C  
ATOM   4988  C   VAL E 120      -2.418 -14.191 -39.989  1.00 79.28           C  
ANISOU 4988  C   VAL E 120    10333   9292  10495   2404    196  -2779       C  
ATOM   4989  O   VAL E 120      -3.196 -13.420 -39.413  1.00 71.61           O  
ANISOU 4989  O   VAL E 120     9436   8317   9454   2256    164  -2506       O  
ATOM   4990  CB  VAL E 120      -3.199 -15.354 -42.105  1.00 77.22           C  
ANISOU 4990  CB  VAL E 120    10143   9005  10191   2237    305  -3196       C  
ATOM   4991  CG1 VAL E 120      -4.485 -15.528 -41.297  1.00 75.72           C  
ANISOU 4991  CG1 VAL E 120    10157   8526  10088   2139    224  -2938       C  
ATOM   4992  CG2 VAL E 120      -3.538 -15.031 -43.537  1.00 75.97           C  
ANISOU 4992  CG2 VAL E 120     9932   9120   9813   2045    401  -3378       C  
ATOM   4993  N   GLU E 121      -1.606 -15.009 -39.311  1.00 76.90           N  
ANISOU 4993  N   GLU E 121    10020   8832  10367   2702    124  -2852       N  
ATOM   4994  CA  GLU E 121      -1.633 -15.012 -37.850  1.00 79.35           C  
ANISOU 4994  CA  GLU E 121    10419   8973  10759   2866      4  -2591       C  
ATOM   4995  C   GLU E 121      -1.207 -13.661 -37.281  1.00 70.99           C  
ANISOU 4995  C   GLU E 121     9191   8209   9572   2802     -7  -2461       C  
ATOM   4996  O   GLU E 121      -1.770 -13.198 -36.281  1.00 74.93           O  
ANISOU 4996  O   GLU E 121     9782   8637  10051   2765    -76  -2187       O  
ATOM   4997  CB  GLU E 121      -0.746 -16.131 -37.304  1.00 84.10           C  
ANISOU 4997  CB  GLU E 121    11037   9382  11535   3253    -77  -2702       C  
ATOM   4998  CG  GLU E 121      -0.697 -16.179 -35.784  1.00 84.48           C  
ANISOU 4998  CG  GLU E 121    11191   9284  11624   3478   -210  -2430       C  
ATOM   4999  CD  GLU E 121       0.376 -17.113 -35.260  1.00 96.10           C  
ANISOU 4999  CD  GLU E 121    12642  10650  13220   3923   -306  -2544       C  
ATOM   5000  OE1 GLU E 121       1.379 -17.338 -35.973  1.00 96.10           O  
ANISOU 5000  OE1 GLU E 121    12435  10824  13256   4052   -279  -2863       O  
ATOM   5001  OE2 GLU E 121       0.218 -17.618 -34.128  1.00104.28           O1-
ANISOU 5001  OE2 GLU E 121    13876  11437  14308   4160   -404  -2312       O1-
ATOM   5002  N   ASP E 122      -0.215 -13.014 -37.902  1.00 72.62           N  
ANISOU 5002  N   ASP E 122     9145   8744   9702   2775     82  -2673       N  
ATOM   5003  CA  ASP E 122       0.182 -11.673 -37.481  1.00 73.77           C  
ANISOU 5003  CA  ASP E 122     9118   9162   9750   2663    118  -2592       C  
ATOM   5004  C   ASP E 122      -0.906 -10.651 -37.774  1.00 75.04           C  
ANISOU 5004  C   ASP E 122     9380   9366   9768   2334    197  -2368       C  
ATOM   5005  O   ASP E 122      -1.114  -9.718 -36.983  1.00 68.53           O  
ANISOU 5005  O   ASP E 122     8535   8598   8905   2250    176  -2173       O  
ATOM   5006  CB  ASP E 122       1.491 -11.270 -38.162  1.00 79.44           C  
ANISOU 5006  CB  ASP E 122     9542  10199  10443   2679    243  -2901       C  
ATOM   5007  CG  ASP E 122       2.704 -11.927 -37.528  1.00 86.15           C  
ANISOU 5007  CG  ASP E 122    10215  11089  11429   3035    134  -3109       C  
ATOM   5008  OD1 ASP E 122       2.540 -12.617 -36.498  1.00 89.08           O  
ANISOU 5008  OD1 ASP E 122    10716  11242  11889   3287    -44  -2971       O  
ATOM   5009  OD2 ASP E 122       3.821 -11.773 -38.070  1.00 98.67           O1-
ANISOU 5009  OD2 ASP E 122    11535  12930  13026   3077    232  -3414       O1-
ATOM   5010  N   LEU E 123      -1.617 -10.815 -38.889  1.00 67.42           N  
ANISOU 5010  N   LEU E 123     8518   8384   8716   2164    278  -2407       N  
ATOM   5011  CA  LEU E 123      -2.746  -9.937 -39.173  1.00 71.40           C  
ANISOU 5011  CA  LEU E 123     9133   8923   9074   1901    323  -2190       C  
ATOM   5012  C   LEU E 123      -3.877 -10.144 -38.171  1.00 65.94           C  
ANISOU 5012  C   LEU E 123     8629   7974   8451   1888    191  -1926       C  
ATOM   5013  O   LEU E 123      -4.471  -9.173 -37.690  1.00 58.59           O  
ANISOU 5013  O   LEU E 123     7727   7083   7450   1749    189  -1702       O  
ATOM   5014  CB  LEU E 123      -3.231 -10.166 -40.603  1.00 65.52           C  
ANISOU 5014  CB  LEU E 123     8444   8255   8196   1771    412  -2325       C  
ATOM   5015  CG  LEU E 123      -2.249  -9.690 -41.669  1.00 64.87           C  
ANISOU 5015  CG  LEU E 123     8198   8466   7982   1727    590  -2538       C  
ATOM   5016  CD1 LEU E 123      -2.589 -10.308 -43.009  1.00 67.71           C  
ANISOU 5016  CD1 LEU E 123     8614   8888   8225   1682    645  -2734       C  
ATOM   5017  CD2 LEU E 123      -2.267  -8.169 -41.756  1.00 66.96           C  
ANISOU 5017  CD2 LEU E 123     8425   8928   8089   1537    724  -2359       C  
ATOM   5018  N   GLN E 124      -4.188 -11.402 -37.837  1.00 63.91           N  
ANISOU 5018  N   GLN E 124     8506   7436   8340   2027    102  -1952       N  
ATOM   5019  CA  GLN E 124      -5.276 -11.668 -36.898  1.00 66.67           C  
ANISOU 5019  CA  GLN E 124     9046   7524   8762   1997     17  -1707       C  
ATOM   5020  C   GLN E 124      -4.964 -11.127 -35.509  1.00 59.67           C  
ANISOU 5020  C   GLN E 124     8137   6640   7894   2103    -59  -1501       C  
ATOM   5021  O   GLN E 124      -5.872 -10.681 -34.796  1.00 62.45           O  
ANISOU 5021  O   GLN E 124     8590   6914   8223   1992    -92  -1264       O  
ATOM   5022  CB  GLN E 124      -5.554 -13.169 -36.833  1.00 76.60           C  
ANISOU 5022  CB  GLN E 124    10465   8444  10194   2126    -16  -1790       C  
ATOM   5023  CG  GLN E 124      -6.158 -13.729 -38.108  1.00 75.25           C  
ANISOU 5023  CG  GLN E 124    10329   8248  10016   1982     48  -2000       C  
ATOM   5024  CD  GLN E 124      -6.319 -15.233 -38.071  1.00 75.97           C  
ANISOU 5024  CD  GLN E 124    10567   7978  10320   2102     47  -2128       C  
ATOM   5025  OE1 GLN E 124      -5.656 -15.923 -37.298  1.00 85.24           O  
ANISOU 5025  OE1 GLN E 124    11804   8949  11635   2356     10  -2098       O  
ATOM   5026  NE2 GLN E 124      -7.197 -15.752 -38.920  1.00 81.07           N  
ANISOU 5026  NE2 GLN E 124    11268   8543  10990   1932     92  -2286       N  
ATOM   5027  N   LYS E 125      -3.692 -11.161 -35.109  1.00 65.44           N  
ANISOU 5027  N   LYS E 125     8719   7485   8659   2325    -91  -1615       N  
ATOM   5028  CA  LYS E 125      -3.291 -10.568 -33.837  1.00 67.93           C  
ANISOU 5028  CA  LYS E 125     8969   7878   8964   2437   -173  -1474       C  
ATOM   5029  C   LYS E 125      -3.499  -9.059 -33.859  1.00 68.87           C  
ANISOU 5029  C   LYS E 125     8971   8230   8967   2192   -101  -1384       C  
ATOM   5030  O   LYS E 125      -4.059  -8.479 -32.920  1.00 62.75           O  
ANISOU 5030  O   LYS E 125     8250   7428   8165   2137   -150  -1171       O  
ATOM   5031  CB  LYS E 125      -1.826 -10.901 -33.553  1.00 68.04           C  
ANISOU 5031  CB  LYS E 125     8794   8026   9030   2735   -229  -1684       C  
ATOM   5032  CG  LYS E 125      -1.607 -12.184 -32.772  1.00 73.16           C  
ANISOU 5032  CG  LYS E 125     9592   8420   9786   3080   -356  -1645       C  
ATOM   5033  CD  LYS E 125      -0.165 -12.641 -32.897  1.00 81.11           C  
ANISOU 5033  CD  LYS E 125    10392   9576  10848   3384   -402  -1927       C  
ATOM   5034  CE  LYS E 125       0.000 -14.087 -32.471  1.00 73.76           C  
ANISOU 5034  CE  LYS E 125     9653   8337  10035   3741   -498  -1910       C  
ATOM   5035  NZ  LYS E 125       1.432 -14.478 -32.463  1.00 88.20           N  
ANISOU 5035  NZ  LYS E 125    11259  10341  11912   4089   -573  -2186       N  
ATOM   5036  N   ARG E 126      -3.050  -8.410 -34.936  1.00 64.68           N  
ANISOU 5036  N   ARG E 126     8292   7917   8364   2045     33  -1546       N  
ATOM   5037  CA  ARG E 126      -3.206  -6.966 -35.081  1.00 66.85           C  
ANISOU 5037  CA  ARG E 126     8483   8378   8540   1813    143  -1461       C  
ATOM   5038  C   ARG E 126      -4.672  -6.547 -35.054  1.00 65.60           C  
ANISOU 5038  C   ARG E 126     8512   8099   8314   1620    135  -1206       C  
ATOM   5039  O   ARG E 126      -4.997  -5.469 -34.543  1.00 58.04           O  
ANISOU 5039  O   ARG E 126     7532   7202   7316   1498    161  -1053       O  
ATOM   5040  CB  ARG E 126      -2.523  -6.512 -36.377  1.00 65.79           C  
ANISOU 5040  CB  ARG E 126     8213   8455   8327   1698    326  -1663       C  
ATOM   5041  CG  ARG E 126      -2.480  -5.005 -36.609  1.00 82.96           C  
ANISOU 5041  CG  ARG E 126    10307  10801  10411   1471    493  -1590       C  
ATOM   5042  CD  ARG E 126      -2.069  -4.699 -38.057  1.00 84.08           C  
ANISOU 5042  CD  ARG E 126    10405  11106  10437   1346    702  -1735       C  
ATOM   5043  NE  ARG E 126      -1.575  -3.343 -38.284  1.00 89.51           N  
ANISOU 5043  NE  ARG E 126    10982  11955  11074   1164    921  -1730       N  
ATOM   5044  CZ  ARG E 126      -0.510  -2.802 -37.706  1.00 90.69           C  
ANISOU 5044  CZ  ARG E 126    10901  12227  11331   1165    997  -1879       C  
ATOM   5045  NH1 ARG E 126       0.233  -3.479 -36.845  1.00 89.57           N  
ANISOU 5045  NH1 ARG E 126    10598  12108  11326   1376    844  -2047       N  
ATOM   5046  NH2 ARG E 126      -0.171  -1.554 -38.014  1.00 91.35           N  
ANISOU 5046  NH2 ARG E 126    10911  12416  11383    957   1240  -1872       N  
ATOM   5047  N   LEU E 127      -5.568  -7.387 -35.582  1.00 62.95           N  
ANISOU 5047  N   LEU E 127     8342   7598   7978   1593    101  -1185       N  
ATOM   5048  CA  LEU E 127      -6.993  -7.058 -35.579  1.00 67.30           C  
ANISOU 5048  CA  LEU E 127     9038   8058   8474   1421     82   -986       C  
ATOM   5049  C   LEU E 127      -7.569  -7.137 -34.170  1.00 64.82           C  
ANISOU 5049  C   LEU E 127     8815   7574   8240   1464    -20   -779       C  
ATOM   5050  O   LEU E 127      -8.301  -6.238 -33.735  1.00 57.23           O  
ANISOU 5050  O   LEU E 127     7875   6640   7229   1332    -18   -601       O  
ATOM   5051  CB  LEU E 127      -7.749  -7.998 -36.529  1.00 68.20           C  
ANISOU 5051  CB  LEU E 127     9264   8066   8582   1377     75  -1086       C  
ATOM   5052  CG  LEU E 127      -9.204  -7.765 -36.987  1.00 70.15           C  
ANISOU 5052  CG  LEU E 127     9613   8292   8747   1196     62   -989       C  
ATOM   5053  CD1 LEU E 127      -9.641  -8.962 -37.809  1.00 74.28           C  
ANISOU 5053  CD1 LEU E 127    10200   8710   9312   1195     46  -1185       C  
ATOM   5054  CD2 LEU E 127     -10.232  -7.497 -35.878  1.00 76.69           C  
ANISOU 5054  CD2 LEU E 127    10529   8978   9633   1128     -5   -756       C  
ATOM   5055  N   LEU E 128      -7.270  -8.220 -33.447  1.00 61.71           N  
ANISOU 5055  N   LEU E 128     8491   6997   7960   1660   -101   -793       N  
ATOM   5056  CA  LEU E 128      -7.808  -8.360 -32.099  1.00 57.85           C  
ANISOU 5056  CA  LEU E 128     8118   6346   7516   1716   -179   -581       C  
ATOM   5057  C   LEU E 128      -7.243  -7.299 -31.168  1.00 60.69           C  
ANISOU 5057  C   LEU E 128     8345   6891   7824   1753   -206   -506       C  
ATOM   5058  O   LEU E 128      -7.913  -6.896 -30.209  1.00 62.91           O  
ANISOU 5058  O   LEU E 128     8692   7123   8086   1707   -242   -315       O  
ATOM   5059  CB  LEU E 128      -7.522  -9.758 -31.553  1.00 64.79           C  
ANISOU 5059  CB  LEU E 128     9132   6974   8509   1954   -239   -592       C  
ATOM   5060  CG  LEU E 128      -8.451 -10.263 -30.442  1.00 70.34           C  
ANISOU 5060  CG  LEU E 128    10051   7413   9260   1971   -269   -356       C  
ATOM   5061  CD1 LEU E 128      -8.623 -11.774 -30.559  1.00 69.17           C  
ANISOU 5061  CD1 LEU E 128    10099   6931   9252   2086   -246   -395       C  
ATOM   5062  CD2 LEU E 128      -7.950  -9.879 -29.051  1.00 76.08           C  
ANISOU 5062  CD2 LEU E 128    10762   8214   9930   2153   -351   -207       C  
ATOM   5063  N   ALA E 129      -6.026  -6.822 -31.439  1.00 59.34           N  
ANISOU 5063  N   ALA E 129     7971   6942   7635   1820   -176   -681       N  
ATOM   5064  CA  ALA E 129      -5.446  -5.776 -30.602  1.00 58.72           C  
ANISOU 5064  CA  ALA E 129     7728   7057   7526   1831   -187   -671       C  
ATOM   5065  C   ALA E 129      -6.186  -4.452 -30.753  1.00 60.68           C  
ANISOU 5065  C   ALA E 129     7960   7380   7716   1565    -95   -551       C  
ATOM   5066  O   ALA E 129      -6.335  -3.724 -29.767  1.00 62.24           O  
ANISOU 5066  O   ALA E 129     8118   7628   7903   1542   -124   -452       O  
ATOM   5067  CB  ALA E 129      -3.963  -5.593 -30.920  1.00 56.36           C  
ANISOU 5067  CB  ALA E 129     7184   6983   7249   1939   -151   -938       C  
ATOM   5068  N   LEU E 130      -6.682  -4.136 -31.955  1.00 57.24           N  
ANISOU 5068  N   LEU E 130     7563   6955   7230   1385     12   -556       N  
ATOM   5069  CA  LEU E 130      -7.340  -2.847 -32.174  1.00 63.78           C  
ANISOU 5069  CA  LEU E 130     8391   7848   7995   1172    106   -432       C  
ATOM   5070  C   LEU E 130      -8.605  -2.666 -31.337  1.00 62.79           C  
ANISOU 5070  C   LEU E 130     8393   7595   7870   1109     30   -210       C  
ATOM   5071  O   LEU E 130      -9.002  -1.525 -31.083  1.00 52.25           O  
ANISOU 5071  O   LEU E 130     7029   6312   6510    983     84   -109       O  
ATOM   5072  CB  LEU E 130      -7.679  -2.665 -33.658  1.00 65.00           C  
ANISOU 5072  CB  LEU E 130     8595   8046   8054   1046    216   -462       C  
ATOM   5073  CG  LEU E 130      -6.510  -2.458 -34.622  1.00 65.38           C  
ANISOU 5073  CG  LEU E 130     8515   8259   8069   1042    359   -662       C  
ATOM   5074  CD1 LEU E 130      -6.966  -2.612 -36.069  1.00 66.21           C  
ANISOU 5074  CD1 LEU E 130     8715   8400   8042    967    434   -685       C  
ATOM   5075  CD2 LEU E 130      -5.887  -1.086 -34.402  1.00 65.67           C  
ANISOU 5075  CD2 LEU E 130     8417   8424   8113    931    508   -665       C  
ATOM   5076  N   ASP E 131      -9.247  -3.753 -30.889  1.00 58.51           N  
ANISOU 5076  N   ASP E 131     7992   6872   7368   1187    -71   -140       N  
ATOM   5077  CA  ASP E 131     -10.496  -3.584 -30.144  1.00 58.90           C  
ANISOU 5077  CA  ASP E 131     8152   6808   7420   1101   -113     53       C  
ATOM   5078  C   ASP E 131     -10.276  -3.008 -28.749  1.00 56.12           C  
ANISOU 5078  C   ASP E 131     7747   6503   7072   1156   -154    142       C  
ATOM   5079  O   ASP E 131     -11.024  -2.093 -28.359  1.00 57.48           O  
ANISOU 5079  O   ASP E 131     7917   6700   7225   1028   -132    258       O  
ATOM   5080  CB  ASP E 131     -11.270  -4.906 -30.105  1.00 66.62           C  
ANISOU 5080  CB  ASP E 131     9298   7560   8454   1132   -162     88       C  
ATOM   5081  CG  ASP E 131     -12.152  -5.091 -31.321  1.00 81.56           C  
ANISOU 5081  CG  ASP E 131    11235   9430  10324    989   -128     34       C  
ATOM   5082  OD1 ASP E 131     -12.450  -4.076 -31.997  1.00 87.02           O1-
ANISOU 5082  OD1 ASP E 131    11865  10273  10927    872    -84     47       O1-
ATOM   5083  OD2 ASP E 131     -12.555  -6.236 -31.592  1.00 90.39           O  
ANISOU 5083  OD2 ASP E 131    12453  10381  11510   1001   -142    -27       O  
ATOM   5084  N   PRO E 132      -9.321  -3.487 -27.941  1.00 55.60           N  
ANISOU 5084  N   PRO E 132     7637   6466   7023   1358   -224     84       N  
ATOM   5085  CA  PRO E 132      -9.062  -2.799 -26.659  1.00 52.89           C  
ANISOU 5085  CA  PRO E 132     7211   6234   6652   1413   -269    130       C  
ATOM   5086  C   PRO E 132      -8.542  -1.378 -26.829  1.00 53.65           C  
ANISOU 5086  C   PRO E 132     7104   6532   6749   1285   -183     26       C  
ATOM   5087  O   PRO E 132      -8.855  -0.510 -26.001  1.00 52.91           O  
ANISOU 5087  O   PRO E 132     6963   6497   6643   1219   -180     88       O  
ATOM   5088  CB  PRO E 132      -8.023  -3.691 -25.955  1.00 53.79           C  
ANISOU 5088  CB  PRO E 132     7304   6377   6758   1705   -377     52       C  
ATOM   5089  CG  PRO E 132      -7.931  -4.929 -26.736  1.00 56.28           C  
ANISOU 5089  CG  PRO E 132     7736   6527   7121   1796   -382     10       C  
ATOM   5090  CD  PRO E 132      -8.679  -4.806 -28.007  1.00 57.55           C  
ANISOU 5090  CD  PRO E 132     7943   6615   7307   1570   -283      2       C  
ATOM   5091  N   MET E 133      -7.736  -1.126 -27.868  1.00 47.76           N  
ANISOU 5091  N   MET E 133     6240   5882   6024   1244    -91   -140       N  
ATOM   5092  CA  MET E 133      -7.323   0.238 -28.206  1.00 50.81           C  
ANISOU 5092  CA  MET E 133     6470   6407   6430   1079     53   -226       C  
ATOM   5093  C   MET E 133      -8.524   1.153 -28.391  1.00 49.53           C  
ANISOU 5093  C   MET E 133     6408   6162   6248    884    127    -43       C  
ATOM   5094  O   MET E 133      -8.611   2.223 -27.776  1.00 46.94           O  
ANISOU 5094  O   MET E 133     6003   5882   5948    795    179    -25       O  
ATOM   5095  CB  MET E 133      -6.499   0.231 -29.499  1.00 42.67           C  
ANISOU 5095  CB  MET E 133     5359   5449   5406   1039    181   -391       C  
ATOM   5096  CG  MET E 133      -5.527  -0.897 -29.668  1.00 61.19           C  
ANISOU 5096  CG  MET E 133     7640   7839   7770   1239    108   -568       C  
ATOM   5097  SD  MET E 133      -4.174  -0.481 -30.803  1.00 68.39           S  
ANISOU 5097  SD  MET E 133     8341   8934   8711   1174    299   -846       S  
ATOM   5098  CE  MET E 133      -2.781  -1.303 -30.075  1.00 63.66           C  
ANISOU 5098  CE  MET E 133     7528   8485   8174   1456    164  -1109       C  
ATOM   5099  N   MET E 134      -9.445   0.763 -29.275  1.00 46.25           N  
ANISOU 5099  N   MET E 134     6151   5636   5786    826    133     68       N  
ATOM   5100  CA  MET E 134     -10.602   1.602 -29.564  1.00 47.76           C  
ANISOU 5100  CA  MET E 134     6428   5774   5944    679    186    227       C  
ATOM   5101  C   MET E 134     -11.460   1.789 -28.323  1.00 50.76           C  
ANISOU 5101  C   MET E 134     6843   6095   6348    671    103    355       C  
ATOM   5102  O   MET E 134     -11.973   2.889 -28.063  1.00 49.27           O  
ANISOU 5102  O   MET E 134     6637   5913   6172    569    162    432       O  
ATOM   5103  CB  MET E 134     -11.418   0.979 -30.697  1.00 51.67           C  
ANISOU 5103  CB  MET E 134     7058   6205   6369    656    169    276       C  
ATOM   5104  CG  MET E 134     -12.628   1.798 -31.136  1.00 55.28           C  
ANISOU 5104  CG  MET E 134     7594   6644   6768    548    201    423       C  
ATOM   5105  SD  MET E 134     -13.633   0.909 -32.343  1.00 64.79           S  
ANISOU 5105  SD  MET E 134     8916   7825   7878    548    134    422       S  
ATOM   5106  CE  MET E 134     -14.219  -0.447 -31.324  1.00 61.22           C  
ANISOU 5106  CE  MET E 134     8514   7220   7527    588     -4    420       C  
ATOM   5107  N   GLU E 135     -11.613   0.725 -27.533  1.00 46.52           N  
ANISOU 5107  N   GLU E 135     6368   5489   5818    784    -18    382       N  
ATOM   5108  CA  GLU E 135     -12.432   0.816 -26.331  1.00 51.43           C  
ANISOU 5108  CA  GLU E 135     7040   6061   6441    777    -77    508       C  
ATOM   5109  C   GLU E 135     -11.817   1.748 -25.301  1.00 46.08           C  
ANISOU 5109  C   GLU E 135     6220   5513   5774    793    -67    454       C  
ATOM   5110  O   GLU E 135     -12.552   2.460 -24.612  1.00 45.91           O  
ANISOU 5110  O   GLU E 135     6198   5490   5756    715    -56    537       O  
ATOM   5111  CB  GLU E 135     -12.659  -0.579 -25.748  1.00 48.28           C  
ANISOU 5111  CB  GLU E 135     6773   5537   6036    902   -171    565       C  
ATOM   5112  CG  GLU E 135     -13.755  -1.332 -26.490  1.00 59.80           C  
ANISOU 5112  CG  GLU E 135     8369   6838   7512    818   -165    625       C  
ATOM   5113  CD  GLU E 135     -15.012  -0.487 -26.733  1.00 72.75           C  
ANISOU 5113  CD  GLU E 135    10009   8484   9148    646   -128    708       C  
ATOM   5114  OE1 GLU E 135     -15.339   0.397 -25.902  1.00 74.10           O  
ANISOU 5114  OE1 GLU E 135    10134   8706   9316    602   -117    777       O  
ATOM   5115  OE2 GLU E 135     -15.644  -0.672 -27.797  1.00 82.52           O1-
ANISOU 5115  OE2 GLU E 135    11280   9696  10379    571   -117    684       O1-
ATOM   5116  N   GLN E 136     -10.483   1.775 -25.185  1.00 45.80           N  
ANISOU 5116  N   GLN E 136     6042   5609   5752    890    -68    283       N  
ATOM   5117  CA  GLN E 136      -9.862   2.734 -24.276  1.00 48.35           C  
ANISOU 5117  CA  GLN E 136     6187   6085   6096    885    -50    170       C  
ATOM   5118  C   GLN E 136     -10.151   4.168 -24.713  1.00 50.52           C  
ANISOU 5118  C   GLN E 136     6400   6357   6438    678    108    165       C  
ATOM   5119  O   GLN E 136     -10.480   5.027 -23.883  1.00 43.25           O  
ANISOU 5119  O   GLN E 136     5422   5468   5543    614    128    170       O  
ATOM   5120  CB  GLN E 136      -8.354   2.498 -24.184  1.00 46.13           C  
ANISOU 5120  CB  GLN E 136     5724   5974   5830   1023    -77    -64       C  
ATOM   5121  CG  GLN E 136      -7.617   3.673 -23.540  1.00 54.72           C  
ANISOU 5121  CG  GLN E 136     6573   7245   6974    961    -16   -261       C  
ATOM   5122  CD  GLN E 136      -6.263   3.308 -22.976  1.00 57.37           C  
ANISOU 5122  CD  GLN E 136     6699   7803   7298   1154   -111   -512       C  
ATOM   5123  OE1 GLN E 136      -6.087   2.253 -22.358  1.00 54.21           O  
ANISOU 5123  OE1 GLN E 136     6360   7437   6802   1400   -283   -477       O  
ATOM   5124  NE2 GLN E 136      -5.284   4.179 -23.201  1.00 52.65           N  
ANISOU 5124  NE2 GLN E 136     5851   7355   6800   1051     13   -776       N  
ATOM   5125  N   GLU E 137     -10.041   4.448 -26.014  1.00 44.65           N  
ANISOU 5125  N   GLU E 137     5682   5568   5715    582    233    159       N  
ATOM   5126  CA  GLU E 137     -10.305   5.804 -26.485  1.00 41.12           C  
ANISOU 5126  CA  GLU E 137     5220   5082   5323    412    407    189       C  
ATOM   5127  C   GLU E 137     -11.768   6.189 -26.297  1.00 46.97           C  
ANISOU 5127  C   GLU E 137     6094   5710   6043    355    380    392       C  
ATOM   5128  O   GLU E 137     -12.077   7.343 -25.974  1.00 48.23           O  
ANISOU 5128  O   GLU E 137     6218   5842   6265    259    474    413       O  
ATOM   5129  CB  GLU E 137      -9.919   5.939 -27.951  1.00 46.90           C  
ANISOU 5129  CB  GLU E 137     5992   5791   6036    351    553    175       C  
ATOM   5130  CG  GLU E 137      -8.463   5.661 -28.231  1.00 59.03           C  
ANISOU 5130  CG  GLU E 137     7372   7449   7609    384    616    -54       C  
ATOM   5131  CD  GLU E 137      -7.996   6.328 -29.508  1.00 62.08           C  
ANISOU 5131  CD  GLU E 137     7770   7821   7998    261    851    -83       C  
ATOM   5132  OE1 GLU E 137      -8.675   7.278 -29.962  1.00 61.76           O  
ANISOU 5132  OE1 GLU E 137     7843   7675   7948    152    984     71       O  
ATOM   5133  OE2 GLU E 137      -6.967   5.888 -30.067  1.00 60.13           O1-
ANISOU 5133  OE2 GLU E 137     7429   7665   7753    287    910   -252       O1-
ATOM   5134  N   ILE E 138     -12.684   5.241 -26.514  1.00 46.01           N  
ANISOU 5134  N   ILE E 138     6112   5519   5850    408    263    520       N  
ATOM   5135  CA  ILE E 138     -14.101   5.507 -26.289  1.00 45.09           C  
ANISOU 5135  CA  ILE E 138     6088   5323   5722    359    226    676       C  
ATOM   5136  C   ILE E 138     -14.381   5.702 -24.806  1.00 46.56           C  
ANISOU 5136  C   ILE E 138     6221   5536   5935    369    168    680       C  
ATOM   5137  O   ILE E 138     -15.156   6.583 -24.413  1.00 41.01           O  
ANISOU 5137  O   ILE E 138     5510   4807   5266    298    205    740       O  
ATOM   5138  CB  ILE E 138     -14.957   4.377 -26.889  1.00 42.89           C  
ANISOU 5138  CB  ILE E 138     5938   4978   5380    391    130    755       C  
ATOM   5139  CG1 ILE E 138     -14.890   4.399 -28.418  1.00 45.35           C  
ANISOU 5139  CG1 ILE E 138     6302   5296   5633    378    189    752       C  
ATOM   5140  CG2 ILE E 138     -16.391   4.455 -26.379  1.00 49.93           C  
ANISOU 5140  CG2 ILE E 138     6881   5814   6275    345     77    869       C  
ATOM   5141  CD1 ILE E 138     -15.583   3.219 -29.065  1.00 49.02           C  
ANISOU 5141  CD1 ILE E 138     6858   5722   6044    407     94    760       C  
ATOM   5142  N   GLU E 139     -13.748   4.897 -23.957  1.00 43.57           N  
ANISOU 5142  N   GLU E 139     5809   5219   5528    476     78    615       N  
ATOM   5143  CA  GLU E 139     -13.964   5.038 -22.521  1.00 47.64           C  
ANISOU 5143  CA  GLU E 139     6285   5792   6024    510     22    620       C  
ATOM   5144  C   GLU E 139     -13.494   6.394 -22.004  1.00 44.80           C  
ANISOU 5144  C   GLU E 139     5760   5528   5732    440    107    492       C  
ATOM   5145  O   GLU E 139     -14.115   6.965 -21.100  1.00 43.23           O  
ANISOU 5145  O   GLU E 139     5537   5350   5538    401    106    515       O  
ATOM   5146  CB  GLU E 139     -13.276   3.894 -21.781  1.00 45.95           C  
ANISOU 5146  CB  GLU E 139     6089   5638   5732    688    -94    587       C  
ATOM   5147  CG  GLU E 139     -13.550   3.858 -20.283  1.00 47.11           C  
ANISOU 5147  CG  GLU E 139     6238   5859   5801    760   -160    623       C  
ATOM   5148  CD  GLU E 139     -15.020   3.670 -19.907  1.00 50.09           C  
ANISOU 5148  CD  GLU E 139     6756   6118   6159    678   -149    803       C  
ATOM   5149  OE1 GLU E 139     -15.836   3.227 -20.748  1.00 53.46           O  
ANISOU 5149  OE1 GLU E 139     7290   6398   6623    600   -124    898       O  
ATOM   5150  OE2 GLU E 139     -15.347   3.959 -18.734  1.00 53.04           O1-
ANISOU 5150  OE2 GLU E 139     7114   6568   6472    694   -163    823       O1-
ATOM   5151  N   GLU E 140     -12.407   6.934 -22.560  1.00 43.88           N  
ANISOU 5151  N   GLU E 140     5524   5468   5682    406    201    337       N  
ATOM   5152  CA  GLU E 140     -11.964   8.256 -22.124  1.00 39.81           C  
ANISOU 5152  CA  GLU E 140     4845   5012   5269    305    320    185       C  
ATOM   5153  C   GLU E 140     -12.979   9.333 -22.494  1.00 43.89           C  
ANISOU 5153  C   GLU E 140     5435   5381   5860    170    442    306       C  
ATOM   5154  O   GLU E 140     -13.148  10.307 -21.749  1.00 40.81           O  
ANISOU 5154  O   GLU E 140     4958   5003   5547    101    504    234       O  
ATOM   5155  CB  GLU E 140     -10.588   8.575 -22.721  1.00 48.41           C  
ANISOU 5155  CB  GLU E 140     5784   6173   6435    268    436    -25       C  
ATOM   5156  CG  GLU E 140      -9.469   7.725 -22.127  1.00 48.94           C  
ANISOU 5156  CG  GLU E 140     5713   6436   6445    429    304   -209       C  
ATOM   5157  CD  GLU E 140      -8.190   7.782 -22.939  1.00 59.29           C  
ANISOU 5157  CD  GLU E 140     6882   7818   7827    401    412   -414       C  
ATOM   5158  OE1 GLU E 140      -8.236   8.293 -24.079  1.00 60.46           O  
ANISOU 5158  OE1 GLU E 140     7092   7839   8039    262    594   -363       O  
ATOM   5159  OE2 GLU E 140      -7.152   7.284 -22.448  1.00 50.98           O1-
ANISOU 5159  OE2 GLU E 140     5660   6957   6752    536    316   -623       O1-
ATOM   5160  N   ILE E 141     -13.675   9.162 -23.621  1.00 35.27           N  
ANISOU 5160  N   ILE E 141     4499   4163   4739    152    469    477       N  
ATOM   5161  CA  ILE E 141     -14.731  10.092 -24.004  1.00 37.44           C  
ANISOU 5161  CA  ILE E 141     4858   4311   5055     82    553    612       C  
ATOM   5162  C   ILE E 141     -15.970   9.891 -23.135  1.00 36.48           C  
ANISOU 5162  C   ILE E 141     4772   4186   4901    106    436    706       C  
ATOM   5163  O   ILE E 141     -16.573  10.863 -22.673  1.00 42.51           O  
ANISOU 5163  O   ILE E 141     5508   4907   5737     56    494    716       O  
ATOM   5164  CB  ILE E 141     -15.068   9.942 -25.493  1.00 43.82           C  
ANISOU 5164  CB  ILE E 141     5811   5035   5803     93    595    748       C  
ATOM   5165  CG1 ILE E 141     -13.878  10.437 -26.340  1.00 47.23           C  
ANISOU 5165  CG1 ILE E 141     6213   5455   6276     39    777    660       C  
ATOM   5166  CG2 ILE E 141     -16.353  10.702 -25.819  1.00 42.09           C  
ANISOU 5166  CG2 ILE E 141     5690   4715   5588     87    620    907       C  
ATOM   5167  CD1 ILE E 141     -14.014  10.161 -27.818  1.00 50.03           C  
ANISOU 5167  CD1 ILE E 141     6712   5771   6526     70    820    777       C  
ATOM   5168  N   ARG E 142     -16.385   8.636 -22.924  1.00 40.62           N  
ANISOU 5168  N   ARG E 142     5364   4741   5329    176    292    770       N  
ATOM   5169  CA  ARG E 142     -17.530   8.409 -22.039  1.00 35.92           C  
ANISOU 5169  CA  ARG E 142     4796   4144   4707    175    217    845       C  
ATOM   5170  C   ARG E 142     -17.280   9.007 -20.664  1.00 44.52           C  
ANISOU 5170  C   ARG E 142     5771   5325   5820    165    229    742       C  
ATOM   5171  O   ARG E 142     -18.168   9.640 -20.081  1.00 41.44           O  
ANISOU 5171  O   ARG E 142     5360   4922   5463    120    251    765       O  
ATOM   5172  CB  ARG E 142     -17.850   6.920 -21.926  1.00 42.70           C  
ANISOU 5172  CB  ARG E 142     5753   4995   5477    234    105    913       C  
ATOM   5173  CG  ARG E 142     -18.092   6.220 -23.245  1.00 51.07           C  
ANISOU 5173  CG  ARG E 142     6907   5984   6514    240     83    968       C  
ATOM   5174  CD  ARG E 142     -19.317   5.306 -23.201  1.00 51.97           C  
ANISOU 5174  CD  ARG E 142     7105   6038   6604    216     21   1046       C  
ATOM   5175  NE  ARG E 142     -19.106   4.078 -23.960  1.00 66.54           N  
ANISOU 5175  NE  ARG E 142     9034   7831   8418    251    -24   1039       N  
ATOM   5176  CZ  ARG E 142     -19.832   3.699 -25.005  1.00 62.27           C  
ANISOU 5176  CZ  ARG E 142     8532   7256   7870    218    -45   1043       C  
ATOM   5177  NH1 ARG E 142     -20.826   4.443 -25.463  1.00 64.02           N  
ANISOU 5177  NH1 ARG E 142     8721   7505   8099    175    -42   1069       N  
ATOM   5178  NH2 ARG E 142     -19.548   2.547 -25.610  1.00 64.54           N  
ANISOU 5178  NH2 ARG E 142     8887   7492   8142    247    -77   1003       N  
ATOM   5179  N   GLN E 143     -16.069   8.835 -20.136  1.00 40.02           N  
ANISOU 5179  N   GLN E 143     5107   4870   5227    219    210    602       N  
ATOM   5180  CA  GLN E 143     -15.763   9.364 -18.811  1.00 43.54           C  
ANISOU 5180  CA  GLN E 143     5423   5452   5668    228    202    464       C  
ATOM   5181  C   GLN E 143     -15.791  10.887 -18.788  1.00 45.14           C  
ANISOU 5181  C   GLN E 143     5515   5616   6020    109    345    353       C  
ATOM   5182  O   GLN E 143     -16.337  11.481 -17.854  1.00 41.27           O  
ANISOU 5182  O   GLN E 143     4968   5167   5545     79    356    308       O  
ATOM   5183  CB  GLN E 143     -14.418   8.823 -18.338  1.00 41.57           C  
ANISOU 5183  CB  GLN E 143     5075   5371   5349    343    129    308       C  
ATOM   5184  CG  GLN E 143     -14.501   7.367 -17.884  1.00 40.99           C  
ANISOU 5184  CG  GLN E 143     5128   5332   5112    501    -14    427       C  
ATOM   5185  CD  GLN E 143     -13.219   6.888 -17.242  1.00 45.08           C  
ANISOU 5185  CD  GLN E 143     5542   6047   5537    672   -113    272       C  
ATOM   5186  OE1 GLN E 143     -12.392   7.691 -16.815  1.00 48.68           O  
ANISOU 5186  OE1 GLN E 143     5795   6667   6035    662    -92     41       O  
ATOM   5187  NE2 GLN E 143     -13.046   5.569 -17.166  1.00 43.78           N  
ANISOU 5187  NE2 GLN E 143     5512   5870   5253    839   -219    381       N  
ATOM   5188  N   LYS E 144     -15.213  11.537 -19.806  1.00 41.58           N  
ANISOU 5188  N   LYS E 144     5044   5072   5683     38    476    308       N  
ATOM   5189  CA  LYS E 144     -15.266  12.995 -19.888  1.00 39.81           C  
ANISOU 5189  CA  LYS E 144     4756   4746   5625    -79    653    228       C  
ATOM   5190  C   LYS E 144     -16.707  13.501 -19.862  1.00 42.28           C  
ANISOU 5190  C   LYS E 144     5164   4936   5964    -94    664    385       C  
ATOM   5191  O   LYS E 144     -17.024  14.462 -19.153  1.00 45.37           O  
ANISOU 5191  O   LYS E 144     5476   5308   6454   -147    736    294       O  
ATOM   5192  CB  LYS E 144     -14.550  13.465 -21.162  1.00 46.47           C  
ANISOU 5192  CB  LYS E 144     5630   5466   6561   -147    821    224       C  
ATOM   5193  CG  LYS E 144     -14.425  14.976 -21.294  1.00 51.42           C  
ANISOU 5193  CG  LYS E 144     6215   5941   7383   -275   1055    140       C  
ATOM   5194  CD  LYS E 144     -13.645  15.383 -22.564  1.00 52.11           C  
ANISOU 5194  CD  LYS E 144     6360   5897   7543   -349   1262    153       C  
ATOM   5195  CE  LYS E 144     -14.296  14.846 -23.830  1.00 54.97           C  
ANISOU 5195  CE  LYS E 144     6942   6169   7773   -263   1222    428       C  
ATOM   5196  NZ  LYS E 144     -13.556  15.291 -25.047  1.00 57.37           N  
ANISOU 5196  NZ  LYS E 144     7323   6356   8117   -329   1446    455       N  
ATOM   5197  N   TYR E 145     -17.598  12.850 -20.609  1.00 40.99           N  
ANISOU 5197  N   TYR E 145     5149   4706   5718    -41    588    591       N  
ATOM   5198  CA  TYR E 145     -18.991  13.279 -20.636  1.00 41.60           C  
ANISOU 5198  CA  TYR E 145     5287   4701   5818    -34    580    714       C  
ATOM   5199  C   TYR E 145     -19.761  12.840 -19.389  1.00 42.89           C  
ANISOU 5199  C   TYR E 145     5403   4973   5919    -23    477    696       C  
ATOM   5200  O   TYR E 145     -20.692  13.535 -18.971  1.00 44.38           O  
ANISOU 5200  O   TYR E 145     5564   5129   6168    -40    507    700       O  
ATOM   5201  CB  TYR E 145     -19.674  12.756 -21.897  1.00 43.36           C  
ANISOU 5201  CB  TYR E 145     5651   4854   5970     21    529    894       C  
ATOM   5202  CG  TYR E 145     -19.396  13.653 -23.079  1.00 48.66           C  
ANISOU 5202  CG  TYR E 145     6400   5390   6700     25    670    958       C  
ATOM   5203  CD1 TYR E 145     -18.227  13.529 -23.813  1.00 51.15           C  
ANISOU 5203  CD1 TYR E 145     6737   5692   7004      2    755    925       C  
ATOM   5204  CD2 TYR E 145     -20.279  14.660 -23.426  1.00 56.80           C  
ANISOU 5204  CD2 TYR E 145     7487   6302   7794     62    737   1052       C  
ATOM   5205  CE1 TYR E 145     -17.969  14.364 -24.878  1.00 53.18           C  
ANISOU 5205  CE1 TYR E 145     7092   5814   7299     -1    922   1002       C  
ATOM   5206  CE2 TYR E 145     -20.030  15.497 -24.483  1.00 58.75           C  
ANISOU 5206  CE2 TYR E 145     7845   6403   8073     90    887   1145       C  
ATOM   5207  CZ  TYR E 145     -18.873  15.349 -25.209  1.00 60.34           C  
ANISOU 5207  CZ  TYR E 145     8088   6586   8252     49    992   1128       C  
ATOM   5208  OH  TYR E 145     -18.627  16.196 -26.267  1.00 58.39           O  
ANISOU 5208  OH  TYR E 145     7981   6182   8023     71   1179   1242       O  
ATOM   5209  N   GLN E 146     -19.393  11.713 -18.789  1.00 42.78           N  
ANISOU 5209  N   GLN E 146     5391   5081   5781     16    372    682       N  
ATOM   5210  CA  GLN E 146     -20.036  11.320 -17.539  1.00 37.00           C  
ANISOU 5210  CA  GLN E 146     4638   4452   4967     27    310    677       C  
ATOM   5211  C   GLN E 146     -19.765  12.329 -16.434  1.00 38.93           C  
ANISOU 5211  C   GLN E 146     4739   4790   5261     -4    369    500       C  
ATOM   5212  O   GLN E 146     -20.621  12.569 -15.562  1.00 38.84           O  
ANISOU 5212  O   GLN E 146     4697   4830   5232    -23    372    488       O  
ATOM   5213  CB  GLN E 146     -19.572   9.924 -17.145  1.00 35.67           C  
ANISOU 5213  CB  GLN E 146     4538   4370   4645    104    208    720       C  
ATOM   5214  CG  GLN E 146     -20.458   9.304 -16.050  1.00 41.15           C  
ANISOU 5214  CG  GLN E 146     5281   5127   5229    113    173    787       C  
ATOM   5215  CD  GLN E 146     -21.944   9.409 -16.372  1.00 57.72           C  
ANISOU 5215  CD  GLN E 146     7413   7130   7388     32    206    879       C  
ATOM   5216  OE1 GLN E 146     -22.391   8.994 -17.440  1.00 63.81           O  
ANISOU 5216  OE1 GLN E 146     8251   7798   8196     16    188    962       O  
ATOM   5217  NE2 GLN E 146     -22.725   9.920 -15.415  1.00 58.25           N  
ANISOU 5217  NE2 GLN E 146     7417   7261   7454    -10    248    839       N  
ATOM   5218  N   CYS E 147     -18.590  12.941 -16.481  1.00 43.40           N  
ANISOU 5218  N   CYS E 147     5203   5386   5900    -22    429    336       N  
ATOM   5219  CA  CYS E 147     -18.206  13.954 -15.519  1.00 40.96           C  
ANISOU 5219  CA  CYS E 147     4729   5169   5665    -69    497    109       C  
ATOM   5220  C   CYS E 147     -19.159  15.141 -15.599  1.00 47.64           C  
ANISOU 5220  C   CYS E 147     5564   5865   6672   -143    615    112       C  
ATOM   5221  O   CYS E 147     -19.499  15.749 -14.579  1.00 48.77           O  
ANISOU 5221  O   CYS E 147     5605   6086   6840   -169    642    -24       O  
ATOM   5222  CB  CYS E 147     -16.765  14.369 -15.831  1.00 52.87           C  
ANISOU 5222  CB  CYS E 147     6120   6707   7263   -103    567    -87       C  
ATOM   5223  SG  CYS E 147     -15.492  13.548 -14.816  1.00 52.09           S  
ANISOU 5223  SG  CYS E 147     5881   6920   6989     11    423   -288       S  
ATOM   5224  N   LYS E 148     -19.629  15.460 -16.809  1.00 50.69           N  
ANISOU 5224  N   LYS E 148     6061   6046   7153   -153    679    267       N  
ATOM   5225  CA  LYS E 148     -20.610  16.524 -17.007  1.00 48.05           C  
ANISOU 5225  CA  LYS E 148     5744   5552   6959   -170    775    306       C  
ATOM   5226  C   LYS E 148     -22.034  16.052 -16.748  1.00 44.52           C  
ANISOU 5226  C   LYS E 148     5340   5145   6432   -122    675    432       C  
ATOM   5227  O   LYS E 148     -22.873  16.836 -16.286  1.00 46.04           O  
ANISOU 5227  O   LYS E 148     5478   5302   6712   -127    723    385       O  
ATOM   5228  CB  LYS E 148     -20.519  17.061 -18.440  1.00 51.51           C  
ANISOU 5228  CB  LYS E 148     6303   5772   7497   -159    881    437       C  
ATOM   5229  CG  LYS E 148     -19.120  17.443 -18.895  1.00 53.29           C  
ANISOU 5229  CG  LYS E 148     6502   5937   7807   -230   1018    329       C  
ATOM   5230  CD  LYS E 148     -19.143  18.021 -20.314  1.00 66.95           C  
ANISOU 5230  CD  LYS E 148     8391   7437   9610   -211   1156    496       C  
ATOM   5231  CE  LYS E 148     -18.199  17.272 -21.254  1.00 66.88           C  
ANISOU 5231  CE  LYS E 148     8444   7459   9509   -214   1155    548       C  
ATOM   5232  NZ  LYS E 148     -17.772  18.082 -22.439  1.00 68.34           N  
ANISOU 5232  NZ  LYS E 148     8756   7428   9784   -240   1373    637       N  
ATOM   5233  N   ARG E 149     -22.334  14.789 -17.053  1.00 41.51           N  
ANISOU 5233  N   ARG E 149     5043   4827   5902    -84    553    570       N  
ATOM   5234  CA  ARG E 149     -23.701  14.304 -16.900  1.00 36.45           C  
ANISOU 5234  CA  ARG E 149     4426   4215   5208    -69    485    663       C  
ATOM   5235  C   ARG E 149     -24.079  14.069 -15.444  1.00 36.43           C  
ANISOU 5235  C   ARG E 149     4347   4366   5129   -102    473    574       C  
ATOM   5236  O   ARG E 149     -25.236  14.295 -15.075  1.00 36.99           O  
ANISOU 5236  O   ARG E 149     4376   4453   5228   -116    486    572       O  
ATOM   5237  CB  ARG E 149     -23.894  13.026 -17.728  1.00 40.56           C  
ANISOU 5237  CB  ARG E 149     5058   4733   5622    -43    388    808       C  
ATOM   5238  CG  ARG E 149     -25.320  12.502 -17.763  1.00 46.61           C  
ANISOU 5238  CG  ARG E 149     5828   5520   6362    -52    336    872       C  
ATOM   5239  CD  ARG E 149     -25.459  11.151 -18.509  1.00 51.48           C  
ANISOU 5239  CD  ARG E 149     6540   6129   6890    -52    255    967       C  
ATOM   5240  NE  ARG E 149     -25.065  11.257 -19.911  1.00 55.70           N  
ANISOU 5240  NE  ARG E 149     7140   6588   7436      7    231   1027       N  
ATOM   5241  CZ  ARG E 149     -23.898  10.868 -20.407  1.00 60.12           C  
ANISOU 5241  CZ  ARG E 149     7766   7124   7953     25    228   1044       C  
ATOM   5242  NH1 ARG E 149     -22.980  10.289 -19.649  1.00 57.33           N  
ANISOU 5242  NH1 ARG E 149     7418   6822   7545     11    225   1003       N  
ATOM   5243  NH2 ARG E 149     -23.647  11.061 -21.699  1.00 64.13           N  
ANISOU 5243  NH2 ARG E 149     8335   7572   8458     77    228   1099       N  
ATOM   5244  N   GLN E 150     -23.132  13.627 -14.611  1.00 34.50           N  
ANISOU 5244  N   GLN E 150     4079   4254   4775    -99    449    495       N  
ATOM   5245  CA  GLN E 150     -23.468  13.214 -13.247  1.00 36.23           C  
ANISOU 5245  CA  GLN E 150     4267   4644   4855   -103    432    448       C  
ATOM   5246  C   GLN E 150     -24.156  14.301 -12.438  1.00 36.95           C  
ANISOU 5246  C   GLN E 150     4233   4779   5029   -144    510    307       C  
ATOM   5247  O   GLN E 150     -25.155  13.991 -11.758  1.00 38.07           O  
ANISOU 5247  O   GLN E 150     4372   4995   5099   -168    522    333       O  
ATOM   5248  CB  GLN E 150     -22.205  12.722 -12.527  1.00 39.40           C  
ANISOU 5248  CB  GLN E 150     4656   5206   5107    -42    378    369       C  
ATOM   5249  CG  GLN E 150     -22.490  11.895 -11.299  1.00 43.61           C  
ANISOU 5249  CG  GLN E 150     5238   5909   5421      1    345    408       C  
ATOM   5250  CD  GLN E 150     -23.335  10.682 -11.604  1.00 49.72           C  
ANISOU 5250  CD  GLN E 150     6177   6594   6122    -12    334    626       C  
ATOM   5251  OE1 GLN E 150     -23.049   9.922 -12.529  1.00 54.39           O  
ANISOU 5251  OE1 GLN E 150     6869   7070   6725     11    288    740       O  
ATOM   5252  NE2 GLN E 150     -24.412  10.518 -10.846  1.00 54.54           N  
ANISOU 5252  NE2 GLN E 150     6802   7251   6670    -65    395    661       N  
ATOM   5253  N   PRO E 151     -23.682  15.550 -12.414  1.00 41.67           N  
ANISOU 5253  N   PRO E 151     4722   5330   5780   -164    586    139       N  
ATOM   5254  CA  PRO E 151     -24.398  16.553 -11.602  1.00 44.89           C  
ANISOU 5254  CA  PRO E 151     5010   5770   6278   -197    666    -14       C  
ATOM   5255  C   PRO E 151     -25.821  16.787 -12.077  1.00 39.41           C  
ANISOU 5255  C   PRO E 151     4332   4960   5680   -192    687     87       C  
ATOM   5256  O   PRO E 151     -26.710  17.017 -11.250  1.00 44.32           O  
ANISOU 5256  O   PRO E 151     4875   5672   6292   -212    720      9       O  
ATOM   5257  CB  PRO E 151     -23.522  17.810 -11.735  1.00 42.53           C  
ANISOU 5257  CB  PRO E 151     4613   5376   6171   -229    766   -209       C  
ATOM   5258  CG  PRO E 151     -22.677  17.577 -12.951  1.00 50.35           C  
ANISOU 5258  CG  PRO E 151     5696   6228   7208   -219    761    -99       C  
ATOM   5259  CD  PRO E 151     -22.432  16.094 -12.965  1.00 39.96           C  
ANISOU 5259  CD  PRO E 151     4473   5042   5668   -171    626     45       C  
ATOM   5260  N   ILE E 152     -26.063  16.729 -13.389  1.00 38.27           N  
ANISOU 5260  N   ILE E 152     4278   4646   5617   -154    664    242       N  
ATOM   5261  CA  ILE E 152     -27.423  16.863 -13.910  1.00 36.76           C  
ANISOU 5261  CA  ILE E 152     4085   4388   5494   -115    650    323       C  
ATOM   5262  C   ILE E 152     -28.304  15.740 -13.394  1.00 43.21           C  
ANISOU 5262  C   ILE E 152     4899   5351   6170   -159    598    372       C  
ATOM   5263  O   ILE E 152     -29.420  15.968 -12.900  1.00 41.64           O  
ANISOU 5263  O   ILE E 152     4606   5210   6004   -175    629    308       O  
ATOM   5264  CB  ILE E 152     -27.404  16.878 -15.446  1.00 34.69           C  
ANISOU 5264  CB  ILE E 152     3931   3964   5287    -39    612    480       C  
ATOM   5265  CG1 ILE E 152     -26.428  17.922 -15.962  1.00 43.21           C  
ANISOU 5265  CG1 ILE E 152     5046   4874   6498    -17    710    453       C  
ATOM   5266  CG2 ILE E 152     -28.810  17.092 -16.002  1.00 39.28           C  
ANISOU 5266  CG2 ILE E 152     4483   4516   5928     41    572    533       C  
ATOM   5267  CD1 ILE E 152     -26.140  17.760 -17.431  1.00 42.26           C  
ANISOU 5267  CD1 ILE E 152     5065   4624   6369     53    687    625       C  
ATOM   5268  N   LEU E 153     -27.822  14.500 -13.523  1.00 37.59           N  
ANISOU 5268  N   LEU E 153     4291   4681   5308   -184    539    481       N  
ATOM   5269  CA  LEU E 153     -28.574  13.362 -13.016  1.00 38.65           C  
ANISOU 5269  CA  LEU E 153     4455   4911   5319   -246    532    538       C  
ATOM   5270  C   LEU E 153     -28.812  13.507 -11.522  1.00 37.79           C  
ANISOU 5270  C   LEU E 153     4278   4959   5121   -293    609    431       C  
ATOM   5271  O   LEU E 153     -29.913  13.239 -11.027  1.00 40.94           O  
ANISOU 5271  O   LEU E 153     4630   5425   5502   -357    664    413       O  
ATOM   5272  CB  LEU E 153     -27.815  12.063 -13.310  1.00 38.01           C  
ANISOU 5272  CB  LEU E 153     4522   4815   5103   -247    477    668       C  
ATOM   5273  CG  LEU E 153     -27.725  11.680 -14.791  1.00 42.78           C  
ANISOU 5273  CG  LEU E 153     5197   5292   5764   -214    405    767       C  
ATOM   5274  CD1 LEU E 153     -26.805  10.441 -14.989  1.00 40.61           C  
ANISOU 5274  CD1 LEU E 153     5065   4998   5368   -203    358    866       C  
ATOM   5275  CD2 LEU E 153     -29.097  11.474 -15.425  1.00 39.27           C  
ANISOU 5275  CD2 LEU E 153     4705   4827   5390   -244    389    778       C  
ATOM   5276  N   ASP E 154     -27.797  13.968 -10.789  1.00 39.63           N  
ANISOU 5276  N   ASP E 154     4488   5274   5297   -264    619    332       N  
ATOM   5277  CA  ASP E 154     -27.946  14.086  -9.340  1.00 46.91           C  
ANISOU 5277  CA  ASP E 154     5348   6387   6089   -288    682    218       C  
ATOM   5278  C   ASP E 154     -28.935  15.184  -8.975  1.00 47.41           C  
ANISOU 5278  C   ASP E 154     5254   6464   6296   -319    762     60       C  
ATOM   5279  O   ASP E 154     -29.678  15.055  -7.992  1.00 49.45           O  
ANISOU 5279  O   ASP E 154     5463   6864   6460   -368    834      2       O  
ATOM   5280  CB  ASP E 154     -26.578  14.348  -8.710  1.00 54.88           C  
ANISOU 5280  CB  ASP E 154     6338   7516   6999   -231    650    104       C  
ATOM   5281  CG  ASP E 154     -25.703  13.096  -8.671  1.00 64.94           C  
ANISOU 5281  CG  ASP E 154     7763   8844   8067   -168    571    247       C  
ATOM   5282  OD1 ASP E 154     -26.183  12.010  -9.077  1.00 64.95           O  
ANISOU 5282  OD1 ASP E 154     7902   8764   8011   -186    563    440       O  
ATOM   5283  OD2 ASP E 154     -24.523  13.212  -8.268  1.00 64.79           O  
ANISOU 5283  OD2 ASP E 154     7713   8946   7960    -94    517    146       O  
ATOM   5284  N   ALA E 155     -28.980  16.250  -9.774  1.00 48.44           N  
ANISOU 5284  N   ALA E 155     5316   6439   6652   -283    763     -1       N  
ATOM   5285  CA  ALA E 155     -29.929  17.331  -9.528  1.00 52.07           C  
ANISOU 5285  CA  ALA E 155     5633   6877   7273   -277    835   -146       C  
ATOM   5286  C   ALA E 155     -31.356  16.886  -9.807  1.00 52.70           C  
ANISOU 5286  C   ALA E 155     5678   6967   7377   -296    835    -83       C  
ATOM   5287  O   ALA E 155     -32.295  17.344  -9.140  1.00 51.41           O  
ANISOU 5287  O   ALA E 155     5384   6889   7261   -317    905   -218       O  
ATOM   5288  CB  ALA E 155     -29.578  18.543 -10.383  1.00 48.84           C  
ANISOU 5288  CB  ALA E 155     5204   6256   7099   -207    852   -191       C  
ATOM   5289  N   ILE E 156     -31.547  16.004 -10.795  1.00 43.21           N  
ANISOU 5289  N   ILE E 156     4570   5693   6153   -293    760     87       N  
ATOM   5290  CA  ILE E 156     -32.888  15.494 -11.068  1.00 41.60           C  
ANISOU 5290  CA  ILE E 156     4302   5525   5977   -330    760    102       C  
ATOM   5291  C   ILE E 156     -33.342  14.588  -9.938  1.00 54.49           C  
ANISOU 5291  C   ILE E 156     5935   7318   7450   -462    855     86       C  
ATOM   5292  O   ILE E 156     -34.440  14.749  -9.389  1.00 52.84           O  
ANISOU 5292  O   ILE E 156     5591   7208   7278   -519    938    -31       O  
ATOM   5293  CB  ILE E 156     -32.941  14.773 -12.425  1.00 49.60           C  
ANISOU 5293  CB  ILE E 156     5402   6438   7006   -299    656    248       C  
ATOM   5294  CG1 ILE E 156     -32.658  15.759 -13.561  1.00 47.71           C  
ANISOU 5294  CG1 ILE E 156     5175   6050   6904   -148    585    279       C  
ATOM   5295  CG2 ILE E 156     -34.298  14.095 -12.604  1.00 52.75           C  
ANISOU 5295  CG2 ILE E 156     5704   6912   7426   -367    662    213       C  
ATOM   5296  CD1 ILE E 156     -32.615  15.116 -14.939  1.00 46.68           C  
ANISOU 5296  CD1 ILE E 156     5134   5847   6753    -95    477    414       C  
ATOM   5297  N   GLU E 157     -32.487  13.650  -9.540  1.00 50.13           N  
ANISOU 5297  N   GLU E 157     5541   6794   6713   -502    860    202       N  
ATOM   5298  CA  GLU E 157     -32.896  12.693  -8.523  1.00 56.33           C  
ANISOU 5298  CA  GLU E 157     6384   7699   7322   -613    974    238       C  
ATOM   5299  C   GLU E 157     -33.064  13.336  -7.150  1.00 59.21           C  
ANISOU 5299  C   GLU E 157     6658   8242   7597   -629   1079     91       C  
ATOM   5300  O   GLU E 157     -33.805  12.802  -6.319  1.00 64.35           O  
ANISOU 5300  O   GLU E 157     7310   9004   8137   -731   1214     85       O  
ATOM   5301  CB  GLU E 157     -31.899  11.535  -8.472  1.00 65.08           C  
ANISOU 5301  CB  GLU E 157     7712   8772   8244   -602    946    422       C  
ATOM   5302  CG  GLU E 157     -32.466  10.260  -9.079  1.00 68.33           C  
ANISOU 5302  CG  GLU E 157     8223   9076   8662   -698    978    552       C  
ATOM   5303  CD  GLU E 157     -31.506   9.095  -9.004  1.00 84.51           C  
ANISOU 5303  CD  GLU E 157    10507  11061  10542   -667    963    738       C  
ATOM   5304  OE1 GLU E 157     -30.723   9.044  -8.031  1.00 88.16           O  
ANISOU 5304  OE1 GLU E 157    11060  11629  10808   -594    977    775       O  
ATOM   5305  OE2 GLU E 157     -31.538   8.233  -9.916  1.00 77.25           O  
ANISOU 5305  OE2 GLU E 157     9674   9997   9680   -700    931    831       O  
ATOM   5306  N   ALA E 158     -32.425  14.477  -6.900  1.00 56.54           N  
ANISOU 5306  N   ALA E 158     6236   7934   7312   -544   1041    -47       N  
ATOM   5307  CA  ALA E 158     -32.598  15.187  -5.634  1.00 50.34           C  
ANISOU 5307  CA  ALA E 158     5338   7332   6457   -555   1135   -236       C  
ATOM   5308  C   ALA E 158     -33.860  16.049  -5.594  1.00 62.89           C  
ANISOU 5308  C   ALA E 158     6725   8930   8240   -581   1207   -412       C  
ATOM   5309  O   ALA E 158     -34.090  16.737  -4.589  1.00 54.47           O  
ANISOU 5309  O   ALA E 158     5541   8012   7144   -591   1294   -603       O  
ATOM   5310  CB  ALA E 158     -31.376  16.061  -5.342  1.00 58.76           C  
ANISOU 5310  CB  ALA E 158     6372   8431   7522   -468   1078   -366       C  
ATOM   5311  N   LYS E 159     -34.682  16.032  -6.646  1.00 53.62           N  
ANISOU 5311  N   LYS E 159     5495   7626   7253   -576   1167   -372       N  
ATOM   5312  CA  LYS E 159     -35.955  16.746  -6.609  1.00 53.05           C  
ANISOU 5312  CA  LYS E 159     5214   7588   7354   -573   1222   -546       C  
ATOM   5313  C   LYS E 159     -36.997  16.025  -5.756  1.00 61.42           C  
ANISOU 5313  C   LYS E 159     6210   8823   8303   -722   1374   -597       C  
ATOM   5314  O   LYS E 159     -37.928  16.668  -5.248  1.00 55.80           O  
ANISOU 5314  O   LYS E 159     5305   8214   7681   -736   1461   -797       O  
ATOM   5315  CB  LYS E 159     -36.494  16.926  -8.027  1.00 55.42           C  
ANISOU 5315  CB  LYS E 159     5467   7732   7859   -483   1108   -497       C  
ATOM   5316  CG  LYS E 159     -35.680  17.907  -8.848  1.00 49.78           C  
ANISOU 5316  CG  LYS E 159     4801   6829   7283   -327   1008   -467       C  
ATOM   5317  CD  LYS E 159     -35.748  19.319  -8.318  1.00 50.14           C  
ANISOU 5317  CD  LYS E 159     4721   6852   7477   -247   1069   -668       C  
ATOM   5318  CE  LYS E 159     -35.121  20.293  -9.309  1.00 68.20           C  
ANISOU 5318  CE  LYS E 159     7074   8896   9944    -95   1007   -618       C  
ATOM   5319  NZ  LYS E 159     -35.238  21.704  -8.845  1.00 72.09           N  
ANISOU 5319  NZ  LYS E 159     7454   9312  10625    -17   1091   -822       N  
ATOM   5320  N   GLY E 160     -36.863  14.712  -5.581  1.00 51.57           N  
ANISOU 5320  N   GLY E 160     5125   7598   6872   -835   1429   -427       N  
ATOM   5321  CA  GLY E 160     -37.868  13.998  -4.819  1.00 59.48           C  
ANISOU 5321  CA  GLY E 160     6086   8730   7782  -1002   1619   -463       C  
ATOM   5322  C   GLY E 160     -39.182  13.895  -5.581  1.00 72.24           C  
ANISOU 5322  C   GLY E 160     7512  10322   9615  -1065   1631   -566       C  
ATOM   5323  O   GLY E 160     -39.260  14.125  -6.791  1.00 74.13           O  
ANISOU 5323  O   GLY E 160     7697  10441  10028   -968   1471   -557       O  
ATOM   5324  N   THR E 161     -40.233  13.549  -4.841  1.00 72.04           N  
ANISOU 5324  N   THR E 161     7374  10435   9564  -1226   1831   -682       N  
ATOM   5325  CA  THR E 161     -41.548  13.359  -5.443  1.00 79.93           C  
ANISOU 5325  CA  THR E 161     8149  11459  10762  -1311   1864   -833       C  
ATOM   5326  C   THR E 161     -42.125  14.682  -5.934  1.00 81.51           C  
ANISOU 5326  C   THR E 161     8084  11693  11193  -1132   1731  -1050       C  
ATOM   5327  O   THR E 161     -42.147  15.677  -5.201  1.00 75.90           O  
ANISOU 5327  O   THR E 161     7277  11068  10494  -1057   1770  -1191       O  
ATOM   5328  CB  THR E 161     -42.487  12.694  -4.441  1.00 70.78           C  
ANISOU 5328  CB  THR E 161     6927  10445   9522  -1548   2151   -924       C  
ATOM   5329  OG1 THR E 161     -41.835  11.535  -3.912  1.00 72.10           O  
ANISOU 5329  OG1 THR E 161     7398  10548   9450  -1672   2287   -680       O  
ATOM   5330  CG2 THR E 161     -43.813  12.298  -5.094  1.00 69.01           C  
ANISOU 5330  CG2 THR E 161     6455  10256   9511  -1676   2203  -1106       C  
ATOM   5331  N   LEU E 162     -42.592  14.683  -7.181  1.00 87.50           N  
ANISOU 5331  N   LEU E 162     8732  12387  12128  -1046   1575  -1080       N  
ATOM   5332  CA  LEU E 162     -43.103  15.882  -7.840  1.00 80.49           C  
ANISOU 5332  CA  LEU E 162     7633  11502  11446   -818   1420  -1238       C  
ATOM   5333  C   LEU E 162     -44.533  15.675  -8.333  1.00 74.66           C  
ANISOU 5333  C   LEU E 162     6600  10901  10867   -846   1415  -1458       C  
ATOM   5334  O   LEU E 162     -45.494  16.067  -7.670  1.00 75.48           O  
ANISOU 5334  O   LEU E 162     6461  11168  11050   -887   1534  -1699       O  
ATOM   5335  CB  LEU E 162     -42.195  16.268  -9.012  1.00 78.71           C  
ANISOU 5335  CB  LEU E 162     7564  11084  11258   -605   1194  -1059       C  
ATOM   5336  CG  LEU E 162     -40.722  16.526  -8.677  1.00 81.24           C  
ANISOU 5336  CG  LEU E 162     8140  11272  11454   -569   1182   -878       C  
ATOM   5337  CD1 LEU E 162     -39.806  16.157  -9.844  1.00 75.80           C  
ANISOU 5337  CD1 LEU E 162     7651  10411  10738   -485   1022   -656       C  
ATOM   5338  CD2 LEU E 162     -40.508  17.980  -8.267  1.00 82.54           C  
ANISOU 5338  CD2 LEU E 162     8237  11402  11723   -410   1180   -997       C  
TER    5339      LEU E 162                                                      
ATOM   5340  N   PRO F 612      21.243 -13.195  -7.909  1.00 65.99           N  
ANISOU 5340  N   PRO F 612     8065  10731   6277    732   -408    765       N  
ATOM   5341  CA  PRO F 612      19.872 -12.723  -8.121  1.00 50.97           C  
ANISOU 5341  CA  PRO F 612     6295   8475   4598    480   -188    768       C  
ATOM   5342  C   PRO F 612      19.542 -11.550  -7.215  1.00 41.03           C  
ANISOU 5342  C   PRO F 612     5033   7243   3313    311   -243    556       C  
ATOM   5343  O   PRO F 612      19.981 -11.506  -6.068  1.00 47.02           O  
ANISOU 5343  O   PRO F 612     5849   8242   3777    484   -383    447       O  
ATOM   5344  CB  PRO F 612      19.012 -13.940  -7.757  1.00 61.03           C  
ANISOU 5344  CB  PRO F 612     7935   9511   5741    683     68    961       C  
ATOM   5345  CG  PRO F 612      19.948 -14.878  -7.045  1.00 65.08           C  
ANISOU 5345  CG  PRO F 612     8570  10265   5891   1086    -12   1076       C  
ATOM   5346  CD  PRO F 612      21.275 -14.641  -7.653  1.00 59.71           C  
ANISOU 5346  CD  PRO F 612     7542   9910   5236   1094   -290   1003       C  
ATOM   5347  N   ILE F 613      18.782 -10.600  -7.738  1.00 43.61           N  
ANISOU 5347  N   ILE F 613     5288   7352   3929     10   -128    489       N  
ATOM   5348  CA  ILE F 613      18.312  -9.452  -6.974  1.00 39.11           C  
ANISOU 5348  CA  ILE F 613     4734   6737   3388   -184   -119    297       C  
ATOM   5349  C   ILE F 613      16.908  -9.806  -6.507  1.00 39.20           C  
ANISOU 5349  C   ILE F 613     5080   6472   3342   -167     94    398       C  
ATOM   5350  O   ILE F 613      15.962  -9.784  -7.300  1.00 41.16           O  
ANISOU 5350  O   ILE F 613     5358   6474   3807   -291    279    471       O  
ATOM   5351  CB  ILE F 613      18.316  -8.167  -7.807  1.00 38.96           C  
ANISOU 5351  CB  ILE F 613     4465   6615   3724   -487    -54    187       C  
ATOM   5352  CG1 ILE F 613      19.688  -7.962  -8.455  1.00 42.69           C  
ANISOU 5352  CG1 ILE F 613     4603   7296   4320   -506   -184    109       C  
ATOM   5353  CG2 ILE F 613      17.866  -6.972  -6.941  1.00 41.14           C  
ANISOU 5353  CG2 ILE F 613     4764   6825   4042   -691    -13    -30       C  
ATOM   5354  CD1 ILE F 613      19.746  -6.809  -9.474  1.00 42.93           C  
ANISOU 5354  CD1 ILE F 613     4416   7162   4734   -750    -14     71       C  
ATOM   5355  N   TRP F 614      16.766 -10.138  -5.225  1.00 41.07           N  
ANISOU 5355  N   TRP F 614     5558   6772   3277     15     81    384       N  
ATOM   5356  CA  TRP F 614      15.467 -10.602  -4.754  1.00 47.35           C  
ANISOU 5356  CA  TRP F 614     6687   7270   4032     49    339    491       C  
ATOM   5357  C   TRP F 614      14.479  -9.454  -4.596  1.00 43.78           C  
ANISOU 5357  C   TRP F 614     6244   6634   3757   -237    428    357       C  
ATOM   5358  O   TRP F 614      13.289  -9.617  -4.893  1.00 42.36           O  
ANISOU 5358  O   TRP F 614     6196   6170   3730   -331    660    412       O  
ATOM   5359  CB  TRP F 614      15.620 -11.381  -3.450  1.00 44.93           C  
ANISOU 5359  CB  TRP F 614     6684   7064   3325    404    363    572       C  
ATOM   5360  CG  TRP F 614      16.131 -12.763  -3.686  1.00 57.45           C  
ANISOU 5360  CG  TRP F 614     8381   8675   4771    722    442    790       C  
ATOM   5361  CD1 TRP F 614      17.428 -13.182  -3.644  1.00 61.59           C  
ANISOU 5361  CD1 TRP F 614     8784   9549   5069    988    223    818       C  
ATOM   5362  CD2 TRP F 614      15.348 -13.913  -4.031  1.00 51.98           C  
ANISOU 5362  CD2 TRP F 614     7927   7634   4189    801    798    982       C  
ATOM   5363  NE1 TRP F 614      17.500 -14.526  -3.926  1.00 60.02           N  
ANISOU 5363  NE1 TRP F 614     8772   9225   4808   1251    428   1064       N  
ATOM   5364  CE2 TRP F 614      16.237 -14.998  -4.168  1.00 64.28           C  
ANISOU 5364  CE2 TRP F 614     9530   9319   5574   1125    801   1154       C  
ATOM   5365  CE3 TRP F 614      13.975 -14.135  -4.210  1.00 51.42           C  
ANISOU 5365  CE3 TRP F 614     8017   7158   4361    628   1139    986       C  
ATOM   5366  CZ2 TRP F 614      15.803 -16.284  -4.489  1.00 58.88           C  
ANISOU 5366  CZ2 TRP F 614     9062   8327   4982   1262   1169   1338       C  
ATOM   5367  CZ3 TRP F 614      13.541 -15.406  -4.520  1.00 54.70           C  
ANISOU 5367  CZ3 TRP F 614     8609   7292   4885    745   1491   1117       C  
ATOM   5368  CH2 TRP F 614      14.455 -16.467  -4.666  1.00 70.13           C  
ANISOU 5368  CH2 TRP F 614    10618   9337   6691   1050   1522   1295       C  
ATOM   5369  N   LYS F 615      14.938  -8.293  -4.118  1.00 36.89           N  
ANISOU 5369  N   LYS F 615     5217   5922   2879   -377    268    149       N  
ATOM   5370  CA  LYS F 615      14.032  -7.153  -3.995  1.00 37.05           C  
ANISOU 5370  CA  LYS F 615     5250   5746   3080   -645    384     34       C  
ATOM   5371  C   LYS F 615      14.501  -6.032  -4.912  1.00 38.23           C  
ANISOU 5371  C   LYS F 615     5081   5906   3538   -890    362    -77       C  
ATOM   5372  O   LYS F 615      14.396  -6.188  -6.124  1.00 38.54           O  
ANISOU 5372  O   LYS F 615     5016   5854   3774   -914    447     54       O  
ATOM   5373  CB  LYS F 615      13.897  -6.717  -2.546  1.00 44.29           C  
ANISOU 5373  CB  LYS F 615     6322   6750   3757   -605    327   -122       C  
ATOM   5374  CG  LYS F 615      13.169  -7.794  -1.753  1.00 43.06           C  
ANISOU 5374  CG  LYS F 615     6547   6474   3339   -346    476     54       C  
ATOM   5375  CD  LYS F 615      12.693  -7.295  -0.454  1.00 49.44           C  
ANISOU 5375  CD  LYS F 615     7553   7291   3943   -315    492    -61       C  
ATOM   5376  CE  LYS F 615      11.874  -8.363   0.291  1.00 43.33           C  
ANISOU 5376  CE  LYS F 615     7196   6320   2947    -46    739    149       C  
ATOM   5377  NZ  LYS F 615      11.861  -7.963   1.676  1.00 49.94           N  
ANISOU 5377  NZ  LYS F 615     8201   7314   3459    110    672     35       N  
ATOM   5378  N   PHE F 616      14.990  -4.912  -4.387  1.00 38.95           N  
ANISOU 5378  N   PHE F 616     5018   6093   3687  -1057    292   -325       N  
ATOM   5379  CA  PHE F 616      15.564  -3.887  -5.260  1.00 38.44           C  
ANISOU 5379  CA  PHE F 616     4657   5991   3957  -1275    358   -426       C  
ATOM   5380  C   PHE F 616      17.078  -3.871  -5.111  1.00 46.67           C  
ANISOU 5380  C   PHE F 616     5406   7349   4976  -1254    146   -641       C  
ATOM   5381  O   PHE F 616      17.609  -4.340  -4.098  1.00 42.90           O  
ANISOU 5381  O   PHE F 616     4942   7166   4192  -1085    -77   -786       O  
ATOM   5382  CB  PHE F 616      15.006  -2.491  -4.926  1.00 43.16           C  
ANISOU 5382  CB  PHE F 616     5248   6394   4756  -1536    538   -597       C  
ATOM   5383  CG  PHE F 616      13.668  -2.219  -5.538  1.00 40.69           C  
ANISOU 5383  CG  PHE F 616     5112   5777   4572  -1575    789   -392       C  
ATOM   5384  CD1 PHE F 616      13.546  -1.965  -6.895  1.00 44.62           C  
ANISOU 5384  CD1 PHE F 616     5506   6148   5298  -1569    964   -220       C  
ATOM   5385  CD2 PHE F 616      12.524  -2.247  -4.754  1.00 44.44           C  
ANISOU 5385  CD2 PHE F 616     5848   6126   4911  -1574    850   -381       C  
ATOM   5386  CE1 PHE F 616      12.302  -1.743  -7.453  1.00 46.26           C  
ANISOU 5386  CE1 PHE F 616     5848   6163   5567  -1533   1168    -66       C  
ATOM   5387  CE2 PHE F 616      11.280  -2.026  -5.304  1.00 42.65           C  
ANISOU 5387  CE2 PHE F 616     5747   5670   4790  -1589   1064   -237       C  
ATOM   5388  CZ  PHE F 616      11.165  -1.777  -6.655  1.00 43.18           C  
ANISOU 5388  CZ  PHE F 616     5686   5666   5054  -1554   1209    -92       C  
ATOM   5389  N   PRO F 617      17.813  -3.325  -6.090  1.00 38.88           N  
ANISOU 5389  N   PRO F 617     4142   6333   4299  -1392    228   -680       N  
ATOM   5390  CA  PRO F 617      19.271  -3.290  -5.965  1.00 41.71           C  
ANISOU 5390  CA  PRO F 617     4172   6998   4677  -1397     43   -941       C  
ATOM   5391  C   PRO F 617      19.693  -2.560  -4.708  1.00 52.05           C  
ANISOU 5391  C   PRO F 617     5335   8521   5921  -1513    -76  -1390       C  
ATOM   5392  O   PRO F 617      19.145  -1.511  -4.365  1.00 56.47           O  
ANISOU 5392  O   PRO F 617     5912   8879   6664  -1750    106  -1552       O  
ATOM   5393  CB  PRO F 617      19.721  -2.545  -7.230  1.00 45.89           C  
ANISOU 5393  CB  PRO F 617     4467   7330   5640  -1584    285   -909       C  
ATOM   5394  CG  PRO F 617      18.668  -2.880  -8.229  1.00 39.32           C  
ANISOU 5394  CG  PRO F 617     3869   6230   4841  -1484    469   -505       C  
ATOM   5395  CD  PRO F 617      17.371  -2.873  -7.421  1.00 39.02           C  
ANISOU 5395  CD  PRO F 617     4136   6066   4623  -1476    499   -465       C  
ATOM   5396  N   ASP F 618      20.675  -3.138  -4.025  1.00 63.01           N  
ANISOU 5396  N   ASP F 618     6565  10349   7025  -1314   -384  -1606       N  
ATOM   5397  CA  ASP F 618      21.115  -2.679  -2.718  1.00 72.09           C  
ANISOU 5397  CA  ASP F 618     7558  11845   7986  -1309   -579  -2077       C  
ATOM   5398  C   ASP F 618      21.324  -1.167  -2.661  1.00 87.80           C  
ANISOU 5398  C   ASP F 618     9246  13696  10418  -1734   -381  -2516       C  
ATOM   5399  O   ASP F 618      20.613  -0.466  -1.934  1.00 97.89           O  
ANISOU 5399  O   ASP F 618    10639  14853  11702  -1870   -288  -2670       O  
ATOM   5400  CB  ASP F 618      22.408  -3.395  -2.329  1.00 81.02           C  
ANISOU 5400  CB  ASP F 618     8434  13532   8819  -1020   -923  -2298       C  
ATOM   5401  CG  ASP F 618      22.693  -3.309  -0.850  1.00104.56           C  
ANISOU 5401  CG  ASP F 618    11343  16990  11395   -816  -1194  -2711       C  
ATOM   5402  OD1 ASP F 618      21.783  -2.896  -0.098  1.00111.68           O  
ANISOU 5402  OD1 ASP F 618    12476  17758  12198   -862  -1118  -2737       O  
ATOM   5403  OD2 ASP F 618      23.825  -3.645  -0.439  1.00108.05           O  
ANISOU 5403  OD2 ASP F 618    11485  17973  11597   -581  -1488  -3024       O  
ATOM   5404  OXT ASP F 618      22.191  -0.612  -3.343  1.00 88.52           O  
ANISOU 5404  OXT ASP F 618     8981  13758  10896  -1954   -264  -2728       O  
TER    5405      ASP F 618                                                      
HETATM 5406  O   HOH A 201     -40.644  -0.601 -20.692  1.00 48.33           O  
HETATM 5407  O   HOH A 202     -21.400  -0.830 -25.234  1.00 45.12           O  
HETATM 5408  O   HOH A 203     -39.489 -17.418 -21.770  1.00 43.13           O  
HETATM 5409  O   HOH A 204     -27.778 -12.034  -0.120  1.00 46.98           O  
HETATM 5410  O   HOH A 205     -38.450 -20.086 -18.782  1.00 47.53           O  
HETATM 5411  O   HOH A 206     -32.529   4.876 -11.923  1.00 44.31           O  
HETATM 5412  O   HOH A 207     -35.776 -17.987 -31.978  1.00 43.82           O  
HETATM 5413  O   HOH A 208     -25.494 -12.981  -0.429  1.00 44.15           O  
HETATM 5414  O   HOH A 209     -29.910  -3.880 -37.885  1.00 48.30           O  
HETATM 5415  O   HOH A 210     -31.952   2.719  -5.112  1.00 39.16           O  
HETATM 5416  O   HOH A 211     -23.855   1.955 -24.651  1.00 50.70           O  
HETATM 5417  O   HOH A 212     -40.141  -6.584  -5.817  1.00 48.42           O  
HETATM 5418  O   HOH A 213     -26.011  -3.086 -30.967  1.00 47.60           O  
HETATM 5419  O   HOH A 214     -37.117 -12.951  -7.725  1.00 48.13           O  
HETATM 5420  O   HOH A 215     -29.149  -9.274  -3.363  1.00 48.74           O  
HETATM 5421  O   HOH A 216     -28.770   5.923  -3.667  1.00 53.15           O  
HETATM 5422  O   HOH A 217     -31.245 -18.085 -30.719  1.00 58.75           O  
HETATM 5423  O   HOH A 218     -23.615  -4.894  -8.734  1.00 38.72           O  
HETATM 5424  O   HOH A 219     -16.879  -9.535 -17.446  1.00 55.06           O  
HETATM 5425  O   HOH A 220     -38.843  -0.984 -30.256  1.00 54.46           O  
HETATM 5426  O   HOH A 221     -30.475 -20.431 -25.622  1.00 49.58           O  
HETATM 5427  O   HOH A 222     -41.082  -7.104 -11.664  1.00 39.23           O  
HETATM 5428  O   HOH A 223     -27.525 -19.914 -20.864  1.00 32.50           O  
HETATM 5429  O   HOH A 224     -28.722   0.626 -26.085  1.00 41.25           O  
HETATM 5430  O   HOH A 225     -31.238 -24.390 -25.141  1.00 49.58           O  
HETATM 5431  O   HOH A 226     -15.889  -7.866 -12.888  1.00 46.37           O  
HETATM 5432  O   HOH A 227     -26.355 -10.504  -5.631  1.00 35.70           O  
HETATM 5433  O   HOH A 228     -24.205 -10.392   0.994  1.00 45.75           O  
HETATM 5434  O   HOH A 229     -40.716 -21.416 -27.142  1.00 68.54           O  
HETATM 5435  O   HOH A 230     -29.360  -9.238  -5.936  1.00 34.57           O  
HETATM 5436  O   HOH A 231     -43.001  -7.088 -16.033  1.00 42.95           O  
HETATM 5437  O   HOH A 232     -34.137  -1.717  -3.649  1.00 37.72           O  
HETATM 5438  O   HOH A 233     -34.436 -14.717 -40.387  1.00 58.67           O  
HETATM 5439  O   HOH A 234     -24.423  -3.748 -33.051  1.00 51.56           O  
HETATM 5440  O   HOH A 235     -25.425  -5.467 -10.516  1.00 35.16           O  
HETATM 5441  O   HOH A 236     -25.670   4.249 -20.763  1.00 40.27           O  
HETATM 5442  O   HOH A 237     -19.887   6.539 -14.561  1.00 57.14           O  
HETATM 5443  O   HOH A 238     -30.269 -22.459 -21.276  1.00 39.91           O  
HETATM 5444  O   HOH A 239     -35.407   2.091  -2.853  1.00 44.03           O  
HETATM 5445  O   HOH A 240     -41.875  -6.794 -27.834  1.00 49.43           O  
HETATM 5446  O   HOH A 241     -28.189   7.647 -17.125  1.00 42.00           O  
HETATM 5447  O   HOH A 242     -37.354  -2.529 -32.349  1.00 48.85           O  
HETATM 5448  O   HOH A 243     -34.897   7.956 -22.441  1.00 53.80           O  
HETATM 5449  O   HOH A 244     -17.909  -7.234 -22.226  1.00 48.21           O  
HETATM 5450  O   HOH A 245     -24.583 -18.257 -23.560  1.00 41.08           O  
HETATM 5451  O   HOH A 246     -36.270 -22.316 -18.645  1.00 42.05           O  
HETATM 5452  O   HOH A 247     -20.367  -2.194 -27.809  1.00 56.65           O  
HETATM 5453  O   HOH A 248     -33.310 -26.506 -25.119  1.00 52.27           O  
HETATM 5454  O   HOH A 249     -29.295 -23.892 -23.231  1.00 50.22           O  
HETATM 5455  O   HOH B 201     -51.562 -28.520  -3.043  1.00 55.74           O  
HETATM 5456  O   HOH B 202     -31.404 -30.537  -2.690  1.00 53.42           O  
HETATM 5457  O   HOH B 203     -57.878 -14.812 -15.236  1.00 43.51           O  
HETATM 5458  O   HOH B 204     -40.112 -30.608   3.316  1.00 41.75           O  
HETATM 5459  O   HOH B 205     -31.858 -15.318   2.125  1.00 55.53           O  
HETATM 5460  O   HOH B 206     -33.751 -22.084 -19.441  1.00 34.99           O  
HETATM 5461  O   HOH B 207     -28.292 -33.117 -15.124  1.00 51.93           O  
HETATM 5462  O   HOH B 208     -41.855 -39.009  -3.653  1.00 47.58           O  
HETATM 5463  O   HOH B 209     -16.897 -25.262 -19.461  1.00 53.11           O  
HETATM 5464  O   HOH B 210     -44.350 -22.807  -5.161  1.00 40.68           O  
HETATM 5465  O   HOH B 211     -26.149 -17.503 -21.438  1.00 35.57           O  
HETATM 5466  O   HOH B 212     -31.511 -25.243   0.967  1.00 41.34           O  
HETATM 5467  O   HOH B 213     -22.898 -29.397 -18.375  1.00 39.89           O  
HETATM 5468  O   HOH B 214     -49.819 -29.945 -13.897  1.00 50.97           O  
HETATM 5469  O   HOH B 215     -19.662 -18.982 -18.788  1.00 41.40           O  
HETATM 5470  O   HOH B 216     -38.794 -11.489  -9.660  1.00 35.81           O  
HETATM 5471  O   HOH B 217     -33.496 -29.097 -19.373  1.00 40.92           O  
HETATM 5472  O   HOH B 218     -47.726 -26.515   3.410  1.00 55.92           O  
HETATM 5473  O   HOH B 219     -43.302 -18.124  -9.203  1.00 44.68           O  
HETATM 5474  O   HOH B 220     -29.700 -27.588 -19.493  1.00 33.77           O  
HETATM 5475  O   HOH B 221     -26.268 -23.870 -20.107  1.00 42.14           O  
HETATM 5476  O   HOH B 222     -45.648 -26.774 -15.512  1.00 51.27           O  
HETATM 5477  O   HOH B 223     -36.931 -29.687   0.281  1.00 41.30           O  
HETATM 5478  O   HOH B 224     -46.691 -15.583 -26.121  1.00 52.14           O  
HETATM 5479  O   HOH B 225     -43.142 -16.988 -11.448  1.00 39.00           O  
HETATM 5480  O   HOH B 226     -28.399 -26.281  -5.535  1.00 36.36           O  
HETATM 5481  O   HOH B 227     -16.030 -13.931 -15.835  1.00 45.70           O  
HETATM 5482  O   HOH B 228     -43.814 -38.069   0.079  1.00 44.30           O  
HETATM 5483  O   HOH B 229     -46.865 -22.157  -1.570  1.00 53.97           O  
HETATM 5484  O   HOH B 230     -37.993 -35.092 -19.516  1.00 56.05           O  
HETATM 5485  O   HOH B 231     -50.265 -25.238  -3.091  1.00 52.31           O  
HETATM 5486  O   HOH B 232     -38.085 -28.080 -20.427  1.00 51.77           O  
HETATM 5487  O   HOH B 233     -49.826 -14.646 -14.562  1.00 52.30           O  
HETATM 5488  O   HOH B 234     -41.659 -37.493 -15.569  1.00 58.29           O  
HETATM 5489  O   HOH B 235     -53.752 -13.870 -16.310  1.00 53.34           O  
HETATM 5490  O   HOH B 236     -18.718 -31.927 -15.556  1.00 60.39           O  
HETATM 5491  O   HOH B 237     -27.158 -25.876 -21.853  1.00 53.67           O  
HETATM 5492  O   HOH B 238     -30.234 -27.034   2.479  1.00 52.94           O  
HETATM 5493  O   HOH B 239     -33.503 -25.249   3.142  1.00 48.89           O  
HETATM 5494  O   HOH B 240     -25.807 -21.944 -22.080  1.00 44.30           O  
HETATM 5495  O   HOH C 701     -16.194  -7.753  -8.839  1.00 46.62           O  
HETATM 5496  O   HOH C 702     -15.787  -6.782  -5.867  1.00 48.77           O  
HETATM 5497  O   HOH C 703     -14.702 -10.362 -13.460  1.00 46.66           O  
HETATM 5498  O   HOH D 201       2.839 -11.598   2.757  1.00 46.28           O  
HETATM 5499  O   HOH D 202      -3.834  14.009 -15.578  1.00 42.32           O  
HETATM 5500  O   HOH D 203      -2.279 -17.754  -5.020  1.00 57.20           O  
HETATM 5501  O   HOH D 204      17.888 -11.509 -15.958  1.00 41.87           O  
HETATM 5502  O   HOH D 205     -12.932  13.660 -28.634  1.00 54.53           O  
HETATM 5503  O   HOH D 206       7.571  -5.172 -19.344  1.00 43.18           O  
HETATM 5504  O   HOH D 207      -9.445  10.974   0.103  1.00 46.67           O  
HETATM 5505  O   HOH D 208      13.158 -14.086 -13.647  1.00 39.46           O  
HETATM 5506  O   HOH D 209       3.619 -18.508  -8.444  1.00 50.01           O  
HETATM 5507  O   HOH D 210       2.140   1.247   3.590  1.00 39.09           O  
HETATM 5508  O   HOH D 211     -16.648   6.977  -8.478  1.00 48.41           O  
HETATM 5509  O   HOH D 212      -8.250  -3.573 -17.056  1.00 54.51           O  
HETATM 5510  O   HOH D 213     -18.919  15.626 -11.611  1.00 54.02           O  
HETATM 5511  O   HOH D 214      -1.600 -14.561  -4.950  1.00 44.30           O  
HETATM 5512  O   HOH D 215      15.869 -12.713 -16.903  1.00 44.84           O  
HETATM 5513  O   HOH D 216       1.879 -13.379   0.041  1.00 44.15           O  
HETATM 5514  O   HOH D 217      11.138  -9.679  -6.672  1.00 34.38           O  
HETATM 5515  O   HOH D 218       9.694 -13.502 -16.642  1.00 43.88           O  
HETATM 5516  O   HOH D 219      -8.533  17.368  -4.175  1.00 42.90           O  
HETATM 5517  O   HOH D 220     -14.682  -1.448 -11.134  1.00 54.76           O  
HETATM 5518  O   HOH D 221     -11.598  11.148 -19.643  1.00 45.47           O  
HETATM 5519  O   HOH D 222      -0.851  -6.134   2.236  1.00 36.51           O  
HETATM 5520  O   HOH D 223     -35.380  27.655 -19.690  1.00 52.09           O  
HETATM 5521  O   HOH D 224      -0.848 -11.150 -20.145  1.00 48.93           O  
HETATM 5522  O   HOH D 225     -17.702   3.200  -9.964  1.00 52.04           O  
HETATM 5523  O   HOH D 226     -11.512  -5.382  -5.485  1.00 53.13           O  
HETATM 5524  O   HOH D 227     -17.612   9.416  -7.271  1.00 54.00           O  
HETATM 5525  O   HOH D 228      -3.446   5.906   0.757  1.00 35.33           O  
HETATM 5526  O   HOH D 229     -11.393   2.959 -13.814  1.00 41.28           O  
HETATM 5527  O   HOH D 230      -9.734  -8.795  -0.281  1.00 56.28           O  
HETATM 5528  O   HOH D 231       0.042  13.356 -13.044  1.00 47.97           O  
HETATM 5529  O   HOH D 232      -6.785 -15.645 -10.022  1.00 54.05           O  
HETATM 5530  O   HOH D 233     -15.499  17.709 -15.087  1.00 58.74           O  
HETATM 5531  O   HOH D 234      -1.699  -8.961 -18.709  1.00 43.39           O  
HETATM 5532  O   HOH D 235      -8.280  -0.850  -3.638  1.00 44.50           O  
HETATM 5533  O   HOH D 236     -22.440  24.641  -8.018  1.00 61.28           O  
HETATM 5534  O   HOH D 237      10.441  -9.883 -14.285  1.00 37.71           O  
HETATM 5535  O   HOH D 238       9.181   3.208   0.274  1.00 49.99           O  
HETATM 5536  O   HOH D 239       1.600  11.179 -13.727  1.00 44.13           O  
HETATM 5537  O   HOH D 240       9.073   8.370 -14.319  1.00 34.14           O  
HETATM 5538  O   HOH D 241       9.118  -8.170  -7.551  1.00 32.10           O  
HETATM 5539  O   HOH D 242     -18.747  11.060  -9.349  1.00 57.47           O  
HETATM 5540  O   HOH D 243       0.109  -4.781   5.084  1.00 53.45           O  
HETATM 5541  O   HOH D 244     -16.894  22.583 -12.820  1.00 76.29           O  
HETATM 5542  O   HOH D 245      13.178   1.037  -1.392  1.00 53.81           O  
HETATM 5543  O   HOH D 246       2.436  -7.566 -20.837  1.00 49.40           O  
HETATM 5544  O   HOH D 247      -9.503  -6.214 -11.286  1.00 43.09           O  
HETATM 5545  O   HOH D 248      -6.263  17.267  -2.871  1.00 38.92           O  
HETATM 5546  O   HOH D 249      -3.571   0.750 -22.322  1.00 44.01           O  
HETATM 5547  O   HOH D 250       8.215 -19.654  -2.613  1.00 46.94           O  
HETATM 5548  O   HOH D 251       5.039  12.097   0.355  1.00 51.38           O  
HETATM 5549  O   HOH D 252      -8.957  18.952  -9.022  1.00 50.00           O  
HETATM 5550  O   HOH D 253      13.502  -8.912 -13.255  1.00 33.07           O  
HETATM 5551  O   HOH D 254     -11.063   1.476 -17.942  1.00 44.03           O  
HETATM 5552  O   HOH D 255      18.155 -14.148 -14.143  1.00 48.72           O  
HETATM 5553  O   HOH D 256      -2.116 -11.532   1.642  1.00 45.26           O  
HETATM 5554  O   HOH D 257       7.864   9.689 -17.918  1.00 50.15           O  
HETATM 5555  O   HOH D 258      11.763 -12.207 -15.178  1.00 45.63           O  
HETATM 5556  O   HOH D 259      -3.759 -18.545 -11.175  1.00 61.30           O  
HETATM 5557  O   HOH D 260     -12.229   4.845  -6.133  1.00 39.09           O  
HETATM 5558  O   HOH D 261     -33.824  26.254 -14.468  1.00 54.78           O  
HETATM 5559  O   HOH D 262       4.391 -14.967   0.727  1.00 50.30           O  
HETATM 5560  O   HOH D 263     -13.171  12.186 -30.772  1.00 49.29           O  
HETATM 5561  O   HOH D 264     -12.996  -1.022 -13.959  1.00 50.64           O  
HETATM 5562  O   HOH D 265       8.741   9.908 -10.326  1.00 43.84           O  
HETATM 5563  O   HOH D 266     -13.619   1.778 -14.474  1.00 49.86           O  
HETATM 5564  O   HOH D 267      -4.152 -13.648   1.967  1.00 55.19           O  
HETATM 5565  O   HOH D 268      -2.391 -21.594 -17.656  1.00 69.69           O  
HETATM 5566  O   HOH D 269       7.837  -7.260   5.281  1.00 52.18           O  
HETATM 5567  O   HOH D 270      -8.706  10.338 -19.768  1.00 54.74           O  
HETATM 5568  O   HOH D 271       1.891 -20.515  -9.320  1.00 60.22           O  
HETATM 5569  O   HOH D 272      -8.683  19.175  -5.923  1.00 51.76           O  
HETATM 5570  O   HOH D 273       0.695  -0.563   4.541  1.00 60.55           O  
HETATM 5571  O   HOH D 274       5.195 -18.925 -10.782  1.00 51.56           O  
HETATM 5572  O   HOH D 275     -11.266  14.188 -19.372  1.00 54.71           O  
HETATM 5573  O   HOH E 201      -9.522  -1.479 -23.692  1.00 48.63           O  
HETATM 5574  O   HOH E 202     -15.496  16.376 -18.240  1.00 54.19           O  
HETATM 5575  O   HOH E 203     -10.250   9.217 -26.339  1.00 45.97           O  
HETATM 5576  O   HOH E 204       8.511   7.390 -11.790  1.00 34.90           O  
HETATM 5577  O   HOH E 205      21.927   1.096 -29.732  1.00 51.34           O  
HETATM 5578  O   HOH E 206      13.100  12.317 -20.549  1.00 45.32           O  
HETATM 5579  O   HOH E 207      19.108  12.225 -24.124  1.00 48.43           O  
HETATM 5580  O   HOH E 208      17.732  -4.796 -15.659  1.00 40.33           O  
HETATM 5581  O   HOH E 209       7.403  -2.833 -33.875  1.00 47.08           O  
HETATM 5582  O   HOH E 210      20.615  -5.188 -28.261  1.00 39.57           O  
HETATM 5583  O   HOH E 211      11.562  13.079 -24.035  1.00 52.38           O  
HETATM 5584  O   HOH E 212       3.891   1.899 -45.726  1.00 70.64           O  
HETATM 5585  O   HOH E 213     -20.939   8.714 -20.667  1.00 46.41           O  
HETATM 5586  O   HOH E 214      15.450   7.247  -8.699  1.00 41.76           O  
HETATM 5587  O   HOH E 215      20.412   0.701 -23.880  1.00 40.81           O  
HETATM 5588  O   HOH E 216       6.196  -5.827 -21.490  1.00 47.79           O  
HETATM 5589  O   HOH E 217      13.055  10.565 -15.484  1.00 43.60           O  
HETATM 5590  O   HOH E 218       2.111  -0.962 -27.044  1.00 48.35           O  
HETATM 5591  O   HOH E 219      19.865  -2.984 -37.150  1.00 49.59           O  
HETATM 5592  O   HOH E 220       8.252   6.978 -45.490  1.00 65.19           O  
HETATM 5593  O   HOH E 221      28.890   6.317 -18.726  1.00 54.97           O  
HETATM 5594  O   HOH E 222     -19.103  -0.717 -24.082  1.00 49.42           O  
HETATM 5595  O   HOH F 701      17.364  -7.473  -3.154  1.00 44.80           O  
HETATM 5596  O   HOH F 702      18.989  -9.858  -3.557  1.00 52.76           O  
HETATM 5597  O   HOH F 703      17.237  -1.456  -2.231  1.00 51.35           O  
HETATM 5598  O   HOH F 704      15.814  -3.782  -1.686  1.00 45.72           O  
CONECT  159  756                                                                
CONECT  756  159                                                                
CONECT  944 2489                                                                
CONECT 1528 2074                                                                
CONECT 2074 1528                                                                
CONECT 2489  944                                                                
CONECT 2819 3416                                                                
CONECT 3416 2819                                                                
CONECT 3604 5223                                                                
CONECT 4202 4745                                                                
CONECT 4745 4202                                                                
CONECT 5223 3604                                                                
MASTER      601    0    0   14   58    0    0    6 5548    6   12   58          
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.