CNRS Nantes University US2B US2B
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***  CELL ADHESION 26-OCT-17 6BFI  ***

elNémo ID: 2403190753153850494

Job options:

ID        	=	 2403190753153850494
JOBID     	=	 CELL ADHESION 26-OCT-17 6BFI
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    CELL ADHESION                           26-OCT-17   6BFI              
TITLE     VINCULIN HOMOLOG IN A SPONGE (PHYLUM PORIFERA) REVEALS VERTEBRATE-LIKE
TITLE    2 CELL ADHESIONS INVOLVED IN EARLY MULTICELLULAR EVOLUTION             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: VIN1;                                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: VINCULIN HOMOLOG;                                           
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: OSCARELLA PEARSEI;                              
SOURCE   3 ORGANISM_TAXID: 1940113;                                             
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    VINCULIN, CELL ADHESION                                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.I.WEIS,J.V.CHODAPARAMBIL                                            
REVDAT   5   13-MAR-24 6BFI    1       REMARK                                   
REVDAT   4   01-JAN-20 6BFI    1       REMARK                                   
REVDAT   3   08-AUG-18 6BFI    1       JRNL                                     
REVDAT   2   20-JUN-18 6BFI    1       JRNL                                     
REVDAT   1   13-JUN-18 6BFI    0                                                
JRNL        AUTH   P.W.MILLER,S.POKUTTA,J.M.MITCHELL,J.V.CHODAPARAMBIL,         
JRNL        AUTH 2 D.N.CLARKE,W.J.NELSON,W.I.WEIS,S.A.NICHOLS                   
JRNL        TITL   ANALYSIS OF A VINCULIN HOMOLOG IN A SPONGE (PHYLUM PORIFERA) 
JRNL        TITL 2 REVEALS THAT VERTEBRATE-LIKE CELL ADHESIONS EMERGED EARLY IN 
JRNL        TITL 3 ANIMAL EVOLUTION.                                            
JRNL        REF    J. BIOL. CHEM.                V. 293 11674 2018              
JRNL        REFN                   ESSN 1083-351X                               
JRNL        PMID   29880641                                                     
JRNL        DOI    10.1074/JBC.RA117.001325                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 36.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 69167                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.110                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 6991                            
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 36.5219 -  7.1295    0.93     2085   208  0.1285 0.1420        
REMARK   3     2  7.1295 -  5.6657    0.91     2066   210  0.1914 0.2433        
REMARK   3     3  5.6657 -  4.9515    0.94     2077   246  0.1877 0.2354        
REMARK   3     4  4.9515 -  4.4997    0.95     2161   217  0.1601 0.2253        
REMARK   3     5  4.4997 -  4.1777    0.90     1963   274  0.1640 0.2217        
REMARK   3     6  4.1777 -  3.9317    0.89     1970   208  0.1840 0.2134        
REMARK   3     7  3.9317 -  3.7350    0.94     2115   253  0.1962 0.2435        
REMARK   3     8  3.7350 -  3.5725    0.93     2087   237  0.2067 0.2693        
REMARK   3     9  3.5725 -  3.4351    0.94     2081   264  0.2206 0.2785        
REMARK   3    10  3.4351 -  3.3166    0.94     2122   212  0.2317 0.2852        
REMARK   3    11  3.3166 -  3.2130    0.93     2066   246  0.2501 0.2968        
REMARK   3    12  3.2130 -  3.1212    0.87     1936   211  0.2713 0.3200        
REMARK   3    13  3.1212 -  3.0391    0.91     2075   232  0.2789 0.3243        
REMARK   3    14  3.0391 -  2.9650    0.92     2014   253  0.2740 0.3342        
REMARK   3    15  2.9650 -  2.8976    0.94     2153   231  0.2666 0.2951        
REMARK   3    16  2.8976 -  2.8360    0.95     2105   231  0.2525 0.3185        
REMARK   3    17  2.8360 -  2.7792    0.94     2091   251  0.2629 0.3256        
REMARK   3    18  2.7792 -  2.7268    0.94     2182   193  0.2727 0.3475        
REMARK   3    19  2.7268 -  2.6781    0.95     2099   226  0.2934 0.3510        
REMARK   3    20  2.6781 -  2.6327    0.94     2119   225  0.3132 0.3547        
REMARK   3    21  2.6327 -  2.5903    0.86     1917   206  0.3051 0.3435        
REMARK   3    22  2.5903 -  2.5504    0.90     2044   229  0.3133 0.3758        
REMARK   3    23  2.5504 -  2.5129    0.92     2017   230  0.3056 0.3516        
REMARK   3    24  2.5129 -  2.4776    0.93     2086   235  0.3222 0.3730        
REMARK   3    25  2.4776 -  2.4441    0.93     2096   259  0.3211 0.3849        
REMARK   3    26  2.4441 -  2.4124    0.94     2049   225  0.3276 0.3700        
REMARK   3    27  2.4124 -  2.3822    0.93     2103   239  0.3566 0.3751        
REMARK   3    28  2.3822 -  2.3535    0.94     2099   266  0.3672 0.4130        
REMARK   3    29  2.3535 -  2.3261    0.94     2104   246  0.3717 0.4017        
REMARK   3    30  2.3261 -  2.3000    0.94     2094   228  0.3983 0.4264        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.260           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002          12358                                  
REMARK   3   ANGLE     :  0.451          16672                                  
REMARK   3   CHIRALITY :  0.033           1981                                  
REMARK   3   PLANARITY :  0.003           2181                                  
REMARK   3   DIHEDRAL  : 11.407           7836                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 130 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -30.3141  22.0110 -28.9117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9556 T22:   0.4790                                     
REMARK   3      T33:   0.4012 T12:  -0.0413                                     
REMARK   3      T13:  -0.0000 T23:   0.0313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9427 L22:   5.0815                                     
REMARK   3      L33:   3.9138 L12:  -1.3368                                     
REMARK   3      L13:   0.6319 L23:   0.5726                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1986 S12:  -0.3836 S13:  -0.0664                       
REMARK   3      S21:   1.2878 S22:   0.0773 S23:  -0.1607                       
REMARK   3      S31:   0.1252 S32:   0.0275 S33:   0.1152                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 131 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -27.0613 -15.5944 -45.1306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7528 T22:   0.4294                                     
REMARK   3      T33:   0.4084 T12:   0.1171                                     
REMARK   3      T13:  -0.0033 T23:   0.1163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9298 L22:   7.2995                                     
REMARK   3      L33:   3.8547 L12:  -2.6135                                     
REMARK   3      L13:  -0.1818 L23:   3.2897                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1847 S12:  -0.2420 S13:  -0.3134                       
REMARK   3      S21:   0.7218 S22:   0.2384 S23:   0.2828                       
REMARK   3      S31:   0.2553 S32:   0.1622 S33:  -0.0448                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 266 THROUGH 370 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8905  11.4454 -85.6847              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9957 T22:   0.5463                                     
REMARK   3      T33:   0.4021 T12:  -0.0291                                     
REMARK   3      T13:   0.1008 T23:  -0.0149                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3582 L22:   3.6298                                     
REMARK   3      L33:   5.0610 L12:   2.7382                                     
REMARK   3      L13:  -1.2048 L23:  -3.5134                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0593 S12:   0.3236 S13:   0.1833                       
REMARK   3      S21:  -0.2166 S22:   0.2973 S23:  -0.0214                       
REMARK   3      S31:  -0.6374 S32:   0.3572 S33:  -0.2345                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 495 THROUGH 627 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -37.0273 -13.0084 -89.3092              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9595 T22:   0.4288                                     
REMARK   3      T33:   0.4452 T12:   0.0022                                     
REMARK   3      T13:  -0.0726 T23:   0.0753                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8074 L22:   2.0904                                     
REMARK   3      L33:   3.1422 L12:  -0.6619                                     
REMARK   3      L13:   0.0555 L23:  -0.3247                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1124 S12:   0.1471 S13:  -0.4599                       
REMARK   3      S21:  -0.8583 S22:   0.0715 S23:   0.3030                       
REMARK   3      S31:   0.4600 S32:  -0.0723 S33:  -0.1357                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 646 THROUGH 836 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2162  24.0668 -58.5357              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7908 T22:   0.5116                                     
REMARK   3      T33:   0.4342 T12:   0.2365                                     
REMARK   3      T13:   0.0602 T23:   0.1195                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7606 L22:   4.3649                                     
REMARK   3      L33:   3.9150 L12:   1.2294                                     
REMARK   3      L13:  -0.3612 L23:   2.6086                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2680 S12:   0.3027 S13:   0.4664                       
REMARK   3      S21:  -0.0253 S22:  -0.2958 S23:   0.0418                       
REMARK   3      S31:  -0.7730 S32:  -0.3685 S33:   0.0483                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 371 THROUGH 494 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.6227 -20.7133 -68.4208              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6986 T22:   0.4189                                     
REMARK   3      T33:   0.4358 T12:   0.1098                                     
REMARK   3      T13:  -0.0447 T23:   0.0515                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2129 L22:   8.8263                                     
REMARK   3      L33:   4.5003 L12:  -0.4202                                     
REMARK   3      L13:   0.3598 L23:  -3.2140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0385 S12:   0.0227 S13:  -0.2111                       
REMARK   3      S21:  -0.4200 S22:   0.1198 S23:   0.1877                       
REMARK   3      S31:   0.2945 S32:  -0.0768 S33:  -0.1587                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 130 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -55.0872 -44.7760 -74.6542              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0786 T22:   0.4962                                     
REMARK   3      T33:   0.4460 T12:   0.0505                                     
REMARK   3      T13:   0.0455 T23:   0.0493                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1436 L22:   3.6861                                     
REMARK   3      L33:   3.5574 L12:   0.4955                                     
REMARK   3      L13:  -0.4456 L23:   0.6388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1320 S12:   0.3503 S13:   0.0572                       
REMARK   3      S21:  -0.9018 S22:  -0.0337 S23:  -0.0348                       
REMARK   3      S31:  -0.3246 S32:   0.1277 S33:   0.1539                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 131 THROUGH 258 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -52.1889  -6.9447 -58.2603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6725 T22:   0.3829                                     
REMARK   3      T33:   0.4706 T12:  -0.0192                                     
REMARK   3      T13:   0.0013 T23:   0.1551                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6007 L22:   6.0229                                     
REMARK   3      L33:   4.3564 L12:   2.1165                                     
REMARK   3      L13:   0.0277 L23:   2.4280                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2520 S12:   0.2329 S13:   0.2955                       
REMARK   3      S21:  -0.8834 S22:   0.2090 S23:   0.3638                       
REMARK   3      S31:  -0.2649 S32:   0.1243 S33:   0.0244                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 266 THROUGH 370 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -39.4990 -34.4118 -17.6659              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8240 T22:   0.4761                                     
REMARK   3      T33:   0.3599 T12:   0.0662                                     
REMARK   3      T13:  -0.0468 T23:  -0.0077                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3653 L22:   7.7921                                     
REMARK   3      L33:   6.4093 L12:  -2.5596                                     
REMARK   3      L13:   2.2133 L23:  -5.7364                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0521 S12:  -0.0849 S13:   0.0480                       
REMARK   3      S21:  -0.1602 S22:   0.0100 S23:  -0.3223                       
REMARK   3      S31:   0.3081 S32:   0.4719 S33:   0.0244                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 371 THROUGH 494 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -49.9115  -2.1721 -35.0973              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6749 T22:   0.3618                                     
REMARK   3      T33:   0.4128 T12:  -0.0041                                     
REMARK   3      T13:   0.0705 T23:   0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6761 L22:   8.7027                                     
REMARK   3      L33:   4.7136 L12:   0.7588                                     
REMARK   3      L13:  -0.4557 L23:  -1.6240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0385 S12:  -0.0151 S13:   0.2432                       
REMARK   3      S21:   0.5417 S22:   0.1088 S23:   0.0869                       
REMARK   3      S31:  -0.3743 S32:  -0.0330 S33:  -0.1273                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 495 THROUGH 627 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -62.4504 -10.0850 -14.4920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2833 T22:   0.4993                                     
REMARK   3      T33:   0.4798 T12:   0.1025                                     
REMARK   3      T13:   0.1780 T23:   0.0869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0877 L22:   3.2495                                     
REMARK   3      L33:   2.4963 L12:  -0.1731                                     
REMARK   3      L13:  -0.4257 L23:   0.3098                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1865 S12:   0.0118 S13:   0.4068                       
REMARK   3      S21:   1.2036 S22:   0.0100 S23:   0.1687                       
REMARK   3      S31:  -0.5120 S32:  -0.0865 S33:  -0.1425                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 647 THROUGH 836 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -53.0981 -46.8672 -45.1307              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7047 T22:   0.4031                                     
REMARK   3      T33:   0.4052 T12:  -0.1156                                     
REMARK   3      T13:   0.0066 T23:   0.0775                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5769 L22:   4.1813                                     
REMARK   3      L33:   3.9739 L12:  -0.8330                                     
REMARK   3      L13:   1.1553 L23:   1.9059                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1933 S12:  -0.3210 S13:  -0.3948                       
REMARK   3      S21:  -0.0040 S22:  -0.4026 S23:   0.1815                       
REMARK   3      S31:   0.7022 S32:  -0.0695 S33:   0.2128                       
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 6BFI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-OCT-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000230813.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JAN-14                          
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               : SSRL                               
REMARK 200  BEAMLINE                       : BL12-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0059                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL SI(111)             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 74722                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 36.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.8                               
REMARK 200  DATA REDUNDANCY                : 13.40                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MRBUMP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM / POTASSIUM TARTRATE, PH    
REMARK 280  8.0, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 289K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     GLU A   259                                                      
REMARK 465     VAL A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     GLY A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     ALA A   265                                                      
REMARK 465     GLU A   628                                                      
REMARK 465     GLU A   629                                                      
REMARK 465     GLU A   630                                                      
REMARK 465     GLU A   631                                                      
REMARK 465     GLU A   632                                                      
REMARK 465     PRO A   633                                                      
REMARK 465     PRO A   634                                                      
REMARK 465     GLU A   635                                                      
REMARK 465     LEU A   636                                                      
REMARK 465     PRO A   637                                                      
REMARK 465     PRO A   638                                                      
REMARK 465     PRO A   639                                                      
REMARK 465     PRO A   640                                                      
REMARK 465     GLU A   641                                                      
REMARK 465     ASP A   642                                                      
REMARK 465     PRO A   643                                                      
REMARK 465     ALA A   644                                                      
REMARK 465     SER A   645                                                      
REMARK 465     LEU A   646                                                      
REMARK 465     GLY A   714                                                      
REMARK 465     GLU A   715                                                      
REMARK 465     VAL A   716                                                      
REMARK 465     GLY A   837                                                      
REMARK 465     GLN A   838                                                      
REMARK 465     GLY A   839                                                      
REMARK 465     ARG A   840                                                      
REMARK 465     ARG A   841                                                      
REMARK 465     ILE A   842                                                      
REMARK 465     SER A   843                                                      
REMARK 465     VAL A   844                                                      
REMARK 465     SER A   845                                                      
REMARK 465     TYR A   846                                                      
REMARK 465     LYS B   218                                                      
REMARK 465     ASP B   219                                                      
REMARK 465     GLU B   259                                                      
REMARK 465     VAL B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     GLY B   262                                                      
REMARK 465     ALA B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     ALA B   265                                                      
REMARK 465     GLU B   628                                                      
REMARK 465     GLU B   629                                                      
REMARK 465     GLU B   630                                                      
REMARK 465     GLU B   631                                                      
REMARK 465     GLU B   632                                                      
REMARK 465     PRO B   633                                                      
REMARK 465     PRO B   634                                                      
REMARK 465     GLU B   635                                                      
REMARK 465     LEU B   636                                                      
REMARK 465     PRO B   637                                                      
REMARK 465     PRO B   638                                                      
REMARK 465     PRO B   639                                                      
REMARK 465     PRO B   640                                                      
REMARK 465     GLU B   641                                                      
REMARK 465     ASP B   642                                                      
REMARK 465     PRO B   643                                                      
REMARK 465     ALA B   644                                                      
REMARK 465     SER B   645                                                      
REMARK 465     GLY B   714                                                      
REMARK 465     GLU B   715                                                      
REMARK 465     VAL B   716                                                      
REMARK 465     GLY B   837                                                      
REMARK 465     GLN B   838                                                      
REMARK 465     GLY B   839                                                      
REMARK 465     ARG B   840                                                      
REMARK 465     ARG B   841                                                      
REMARK 465     ILE B   842                                                      
REMARK 465     SER B   843                                                      
REMARK 465     VAL B   844                                                      
REMARK 465     SER B   845                                                      
REMARK 465     TYR B   846                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A 626    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 627    CG   CD1  CD2                                       
REMARK 470     ARG A 717    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 626    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 627    CG   CD1  CD2                                       
REMARK 470     ARG B 717    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A   5       33.06   -147.35                                   
REMARK 500    LEU A  36      125.56   -170.31                                   
REMARK 500    GLU A 256       26.40    -79.79                                   
REMARK 500    SER A 284     -140.68    -77.79                                   
REMARK 500    ASN A 378       77.35   -153.77                                   
REMARK 500    ASN A 398       36.55   -150.77                                   
REMARK 500    SER A 427       12.31   -140.06                                   
REMARK 500    ASN A 462       68.14   -150.89                                   
REMARK 500    PRO A 620      -75.17    -58.89                                   
REMARK 500    TRP A 832       62.04   -113.49                                   
REMARK 500    PHE B   5       40.25   -153.82                                   
REMARK 500    VAL B 150       51.37   -115.31                                   
REMARK 500    SER B 221       35.06    -89.75                                   
REMARK 500    SER B 222      175.71     61.10                                   
REMARK 500    SER B 284     -139.03    -84.12                                   
REMARK 500    PRO B 397        0.87    -67.99                                   
REMARK 500    ASN B 398       35.85   -146.21                                   
REMARK 500    ASP B 495      109.34    -58.54                                   
REMARK 500    GLU B 521      107.26    -55.02                                   
REMARK 500    GLU B 626     -155.07    -84.47                                   
REMARK 500    MET B 781      104.71    -58.26                                   
REMARK 500    CYS B 818       33.73    -88.35                                   
REMARK 500    LEU B 831      -62.29   -103.57                                   
REMARK 500    TRP B 832       70.76     61.61                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  6BFI A    1   846  PDB    6BFI     6BFI             1    846             
DBREF  6BFI B    1   846  PDB    6BFI     6BFI             1    846             
SEQRES   1 A  846  MET PRO VAL LYS PHE HIS THR LYS THR LEU GLU SER VAL          
SEQRES   2 A  846  ILE ASP PRO VAL ALA GLN GLN VAL GLY GLN LEU VAL LEU          
SEQRES   3 A  846  PHE HIS GLU GLN ALA GLU SER GLY LEU LEU LYS GLU ASP          
SEQRES   4 A  846  LEU THR PRO LEU VAL GLN GLY VAL GLY ILE ALA VAL THR          
SEQRES   5 A  846  ASN LEU VAL GLN VAL ALA ALA SER MET VAL GLU THR SER          
SEQRES   6 A  846  ASN ASP GLU ASP PHE LYS ALA GLU LEU PRO PRO SER MET          
SEQRES   7 A  846  GLN GLU VAL GLN GLN ALA ALA VAL PHE LEU SER ASP ALA          
SEQRES   8 A  846  ALA ARG LEU LEU LYS ALA ASP GLN GLY SER PRO GLU GLY          
SEQRES   9 A  846  LYS ARG LYS LEU LEU ASP GLY ALA ARG GLY VAL ILE ASN          
SEQRES  10 A  846  GLY MET SER ASP LEU LEU MET CYS ALA ASP ARG SER GLU          
SEQRES  11 A  846  VAL ARG LYS MET VAL LYS VAL CYS ARG SER VAL GLN GLU          
SEQRES  12 A  846  TYR LEU ASP VAL ALA LYS VAL ILE ASP VAL GLU ALA ASP          
SEQRES  13 A  846  LEU ALA THR PHE LEU GLN ASN LEU THR PRO GLY MET THR          
SEQRES  14 A  846  SER MET MET LYS VAL VAL GLU GLN ARG HIS PRO GLU LEU          
SEQRES  15 A  846  THR ASN LEU ALA HIS ALA GLN MET LEU LYS SER GLU LEU          
SEQRES  16 A  846  GLY THR VAL ARG GLU GLN ILE PRO ILE LEU ILE SER SER          
SEQRES  17 A  846  ILE ARG VAL CYS CYS LEU VAL ILE VAL LYS ASP GLY SER          
SEQRES  18 A  846  SER GLY MET LYS ASP ALA ALA PHE GLY ARG ASP TYR VAL          
SEQRES  19 A  846  ILE GLN LYS LEU PHE ILE ALA ILE GLU GLU ILE ILE ARG          
SEQRES  20 A  846  VAL LEU GLN LEU THR THR THR PHE GLU GLU GLU GLU VAL          
SEQRES  21 A  846  GLY GLY ALA GLY ALA ALA SER ALA ALA SER LEU ALA HIS          
SEQRES  22 A  846  MET PHE HIS GLN ALA GLN ASP ALA LEU ALA SER GLY ASP          
SEQRES  23 A  846  ILE SER ARG SER THR LEU ASP ALA VAL ARG LYS CYS ILE          
SEQRES  24 A  846  SER GLU GLY ARG ARG VAL ALA ALA LEU ALA ALA THR ASP          
SEQRES  25 A  846  GLU THR ARG ALA LYS LEU LEU ALA ALA ALA ASP GLU LEU          
SEQRES  26 A  846  ASP GLN ILE LEU LYS GLU LEU GLU GLU LEU GLN ALA LYS          
SEQRES  27 A  846  GLY LEU GLY ASP SER ARG GLN ALA ARG ALA LEU ALA HIS          
SEQRES  28 A  846  ALA ALA ALA VAL LYS LEU GLN GLU LEU GLU GLN GLU ILE          
SEQRES  29 A  846  ARG LYS ALA LEU ALA GLU ARG VAL ALA THR ASP PHE VAL          
SEQRES  30 A  846  ASN VAL GLY GLY PRO ILE LYS ALA LEU GLU ASP ALA ALA          
SEQRES  31 A  846  LEU ALA SER PRO SER ASP PRO ASN ARG GLN ALA ASN PHE          
SEQRES  32 A  846  ALA GLN LYS ALA LYS GLU PHE GLU ALA HIS THR ALA ARG          
SEQRES  33 A  846  LEU ALA ASP THR ALA GLU LEU VAL ALA SER SER GLY GLY          
SEQRES  34 A  846  CYS SER ASP ALA VAL ALA ALA GLU LEU ARG LYS GLU ALA          
SEQRES  35 A  846  ALA LYS LEU ARG ASP ILE SER THR ALA VAL VAL PRO ALA          
SEQRES  36 A  846  ALA ARG VAL VAL LEU GLU ASN PRO GLY ASN GLN ALA ALA          
SEQRES  37 A  846  LYS ASP TYR LEU ARG THR VAL LYS GLU LYS TRP LEU GLU          
SEQRES  38 A  846  ALA ALA GLU SER MET GLY ARG SER VAL ASP GLY VAL ILE          
SEQRES  39 A  846  ASP SER LEU GLU PHE MET LYS VAL SER GLU ALA ARG ILE          
SEQRES  40 A  846  GLN ALA ASP VAL LYS GLU ALA LYS ARG ILE ALA LEU ALA          
SEQRES  41 A  846  GLU GLU ASP SER MET LYS LEU ILE ALA LYS ALA SER SER          
SEQRES  42 A  846  VAL ALA ARG GLN ALA ASN ARG VAL ILE GLN VAL ALA LYS          
SEQRES  43 A  846  VAL GLU ALA ASP ASN SER GLU ASN PRO GLU PHE VAL ALA          
SEQRES  44 A  846  LYS LEU SER SER ALA SER GLU SER LEU ALA LYS SER ILE          
SEQRES  45 A  846  SER PRO MET VAL ILE GLU ALA LYS ALA VAL VAL THR SER          
SEQRES  46 A  846  PRO GLN ASN LYS ASP ILE GLN ARG LYS PHE CYS SER SER          
SEQRES  47 A  846  ALA ASP LYS VAL VAL GLU GLY VAL ALA ALA VAL ARG SER          
SEQRES  48 A  846  VAL ILE GLU ASP ASN TRP VAL PRO PRO ARG PRO PRO LEU          
SEQRES  49 A  846  PRO GLU LEU GLU GLU GLU GLU GLU PRO PRO GLU LEU PRO          
SEQRES  50 A  846  PRO PRO PRO GLU ASP PRO ALA SER LEU LEU PRO ALA GLU          
SEQRES  51 A  846  MET GLN GLU ALA GLU GLU MET LEU ARG ALA PRO LEU PRO          
SEQRES  52 A  846  PRO LYS ASP GLN ASN PRO ILE HIS HIS ALA ALA ALA SER          
SEQRES  53 A  846  VAL PHE ARG GLU ALA ASP GLN TRP ASP GLU LYS GLY ASN          
SEQRES  54 A  846  ASP LEU ILE SER LEU VAL LYS GLN MET ALA ARG LYS MET          
SEQRES  55 A  846  ALA MET MET SER LYS TYR THR ARG GLY GLU SER GLY GLU          
SEQRES  56 A  846  VAL ARG SER LYS ALA ASP LEU ILE ARG MET ALA LYS GLU          
SEQRES  57 A  846  ILE ALA LEU ASN ALA GLN GLU LEU LEU LYS LEU ALA ARG          
SEQRES  58 A  846  GLN ILE ALA ASN ALA CYS MET ASP LYS ARG ALA LYS THR          
SEQRES  59 A  846  ASN LEU LEU GLN LEU LEU ASP ARG ILE PRO THR ILE SER          
SEQRES  60 A  846  THR GLN LEU LYS ILE LEU ALA THR VAL LYS ALA THR SER          
SEQRES  61 A  846  MET GLY GLY GLY ASP ALA ARG ALA ASP ALA ASP ALA THR          
SEQRES  62 A  846  ASP MET LEU VAL GLY ASN ALA GLU ASN LEU MET ARG THR          
SEQRES  63 A  846  VAL LYS ASP VAL ILE ARG ALA SER GLU ALA ALA CYS ILE          
SEQRES  64 A  846  ARG LEU ARG PRO ASP SER PRO ILE ALA SER ILE LEU TRP          
SEQRES  65 A  846  ARG LYS LYS GLY GLY GLN GLY ARG ARG ILE SER VAL SER          
SEQRES  66 A  846  TYR                                                          
SEQRES   1 B  846  MET PRO VAL LYS PHE HIS THR LYS THR LEU GLU SER VAL          
SEQRES   2 B  846  ILE ASP PRO VAL ALA GLN GLN VAL GLY GLN LEU VAL LEU          
SEQRES   3 B  846  PHE HIS GLU GLN ALA GLU SER GLY LEU LEU LYS GLU ASP          
SEQRES   4 B  846  LEU THR PRO LEU VAL GLN GLY VAL GLY ILE ALA VAL THR          
SEQRES   5 B  846  ASN LEU VAL GLN VAL ALA ALA SER MET VAL GLU THR SER          
SEQRES   6 B  846  ASN ASP GLU ASP PHE LYS ALA GLU LEU PRO PRO SER MET          
SEQRES   7 B  846  GLN GLU VAL GLN GLN ALA ALA VAL PHE LEU SER ASP ALA          
SEQRES   8 B  846  ALA ARG LEU LEU LYS ALA ASP GLN GLY SER PRO GLU GLY          
SEQRES   9 B  846  LYS ARG LYS LEU LEU ASP GLY ALA ARG GLY VAL ILE ASN          
SEQRES  10 B  846  GLY MET SER ASP LEU LEU MET CYS ALA ASP ARG SER GLU          
SEQRES  11 B  846  VAL ARG LYS MET VAL LYS VAL CYS ARG SER VAL GLN GLU          
SEQRES  12 B  846  TYR LEU ASP VAL ALA LYS VAL ILE ASP VAL GLU ALA ASP          
SEQRES  13 B  846  LEU ALA THR PHE LEU GLN ASN LEU THR PRO GLY MET THR          
SEQRES  14 B  846  SER MET MET LYS VAL VAL GLU GLN ARG HIS PRO GLU LEU          
SEQRES  15 B  846  THR ASN LEU ALA HIS ALA GLN MET LEU LYS SER GLU LEU          
SEQRES  16 B  846  GLY THR VAL ARG GLU GLN ILE PRO ILE LEU ILE SER SER          
SEQRES  17 B  846  ILE ARG VAL CYS CYS LEU VAL ILE VAL LYS ASP GLY SER          
SEQRES  18 B  846  SER GLY MET LYS ASP ALA ALA PHE GLY ARG ASP TYR VAL          
SEQRES  19 B  846  ILE GLN LYS LEU PHE ILE ALA ILE GLU GLU ILE ILE ARG          
SEQRES  20 B  846  VAL LEU GLN LEU THR THR THR PHE GLU GLU GLU GLU VAL          
SEQRES  21 B  846  GLY GLY ALA GLY ALA ALA SER ALA ALA SER LEU ALA HIS          
SEQRES  22 B  846  MET PHE HIS GLN ALA GLN ASP ALA LEU ALA SER GLY ASP          
SEQRES  23 B  846  ILE SER ARG SER THR LEU ASP ALA VAL ARG LYS CYS ILE          
SEQRES  24 B  846  SER GLU GLY ARG ARG VAL ALA ALA LEU ALA ALA THR ASP          
SEQRES  25 B  846  GLU THR ARG ALA LYS LEU LEU ALA ALA ALA ASP GLU LEU          
SEQRES  26 B  846  ASP GLN ILE LEU LYS GLU LEU GLU GLU LEU GLN ALA LYS          
SEQRES  27 B  846  GLY LEU GLY ASP SER ARG GLN ALA ARG ALA LEU ALA HIS          
SEQRES  28 B  846  ALA ALA ALA VAL LYS LEU GLN GLU LEU GLU GLN GLU ILE          
SEQRES  29 B  846  ARG LYS ALA LEU ALA GLU ARG VAL ALA THR ASP PHE VAL          
SEQRES  30 B  846  ASN VAL GLY GLY PRO ILE LYS ALA LEU GLU ASP ALA ALA          
SEQRES  31 B  846  LEU ALA SER PRO SER ASP PRO ASN ARG GLN ALA ASN PHE          
SEQRES  32 B  846  ALA GLN LYS ALA LYS GLU PHE GLU ALA HIS THR ALA ARG          
SEQRES  33 B  846  LEU ALA ASP THR ALA GLU LEU VAL ALA SER SER GLY GLY          
SEQRES  34 B  846  CYS SER ASP ALA VAL ALA ALA GLU LEU ARG LYS GLU ALA          
SEQRES  35 B  846  ALA LYS LEU ARG ASP ILE SER THR ALA VAL VAL PRO ALA          
SEQRES  36 B  846  ALA ARG VAL VAL LEU GLU ASN PRO GLY ASN GLN ALA ALA          
SEQRES  37 B  846  LYS ASP TYR LEU ARG THR VAL LYS GLU LYS TRP LEU GLU          
SEQRES  38 B  846  ALA ALA GLU SER MET GLY ARG SER VAL ASP GLY VAL ILE          
SEQRES  39 B  846  ASP SER LEU GLU PHE MET LYS VAL SER GLU ALA ARG ILE          
SEQRES  40 B  846  GLN ALA ASP VAL LYS GLU ALA LYS ARG ILE ALA LEU ALA          
SEQRES  41 B  846  GLU GLU ASP SER MET LYS LEU ILE ALA LYS ALA SER SER          
SEQRES  42 B  846  VAL ALA ARG GLN ALA ASN ARG VAL ILE GLN VAL ALA LYS          
SEQRES  43 B  846  VAL GLU ALA ASP ASN SER GLU ASN PRO GLU PHE VAL ALA          
SEQRES  44 B  846  LYS LEU SER SER ALA SER GLU SER LEU ALA LYS SER ILE          
SEQRES  45 B  846  SER PRO MET VAL ILE GLU ALA LYS ALA VAL VAL THR SER          
SEQRES  46 B  846  PRO GLN ASN LYS ASP ILE GLN ARG LYS PHE CYS SER SER          
SEQRES  47 B  846  ALA ASP LYS VAL VAL GLU GLY VAL ALA ALA VAL ARG SER          
SEQRES  48 B  846  VAL ILE GLU ASP ASN TRP VAL PRO PRO ARG PRO PRO LEU          
SEQRES  49 B  846  PRO GLU LEU GLU GLU GLU GLU GLU PRO PRO GLU LEU PRO          
SEQRES  50 B  846  PRO PRO PRO GLU ASP PRO ALA SER LEU LEU PRO ALA GLU          
SEQRES  51 B  846  MET GLN GLU ALA GLU GLU MET LEU ARG ALA PRO LEU PRO          
SEQRES  52 B  846  PRO LYS ASP GLN ASN PRO ILE HIS HIS ALA ALA ALA SER          
SEQRES  53 B  846  VAL PHE ARG GLU ALA ASP GLN TRP ASP GLU LYS GLY ASN          
SEQRES  54 B  846  ASP LEU ILE SER LEU VAL LYS GLN MET ALA ARG LYS MET          
SEQRES  55 B  846  ALA MET MET SER LYS TYR THR ARG GLY GLU SER GLY GLU          
SEQRES  56 B  846  VAL ARG SER LYS ALA ASP LEU ILE ARG MET ALA LYS GLU          
SEQRES  57 B  846  ILE ALA LEU ASN ALA GLN GLU LEU LEU LYS LEU ALA ARG          
SEQRES  58 B  846  GLN ILE ALA ASN ALA CYS MET ASP LYS ARG ALA LYS THR          
SEQRES  59 B  846  ASN LEU LEU GLN LEU LEU ASP ARG ILE PRO THR ILE SER          
SEQRES  60 B  846  THR GLN LEU LYS ILE LEU ALA THR VAL LYS ALA THR SER          
SEQRES  61 B  846  MET GLY GLY GLY ASP ALA ARG ALA ASP ALA ASP ALA THR          
SEQRES  62 B  846  ASP MET LEU VAL GLY ASN ALA GLU ASN LEU MET ARG THR          
SEQRES  63 B  846  VAL LYS ASP VAL ILE ARG ALA SER GLU ALA ALA CYS ILE          
SEQRES  64 B  846  ARG LEU ARG PRO ASP SER PRO ILE ALA SER ILE LEU TRP          
SEQRES  65 B  846  ARG LYS LYS GLY GLY GLN GLY ARG ARG ILE SER VAL SER          
SEQRES  66 B  846  TYR                                                          
FORMUL   3  HOH   *133(H2 O)                                                    
HELIX    1 AA1 THR A    7  SER A   33  1                                  27    
HELIX    2 AA2 LEU A   40  SER A   60  1                                  21    
HELIX    3 AA3 ASP A   67  ASP A   98  1                                  32    
HELIX    4 AA4 SER A  101  ASP A  146  1                                  46    
HELIX    5 AA5 VAL A  147  ILE A  151  5                                   5    
HELIX    6 AA6 VAL A  153  HIS A  179  1                                  27    
HELIX    7 AA7 PRO A  180  LEU A  182  5                                   3    
HELIX    8 AA8 ASN A  184  ILE A  216  1                                  33    
HELIX    9 AA9 VAL A  217  ASP A  219  5                                   3    
HELIX   10 AB1 GLY A  223  GLN A  250  1                                  28    
HELIX   11 AB2 THR A  254  GLU A  258  5                                   5    
HELIX   12 AB3 SER A  267  SER A  284  1                                  18    
HELIX   13 AB4 SER A  288  ALA A  307  1                                  20    
HELIX   14 AB5 THR A  311  GLY A  339  1                                  29    
HELIX   15 AB6 SER A  343  PHE A  376  1                                  34    
HELIX   16 AB7 GLY A  380  LEU A  391  1                                  12    
HELIX   17 AB8 ASN A  398  GLY A  428  1                                  31    
HELIX   18 AB9 SER A  431  THR A  450  1                                  20    
HELIX   19 AC1 ALA A  451  GLU A  461  1                                  11    
HELIX   20 AC2 ASN A  465  ILE A  494  1                                  30    
HELIX   21 AC3 ASP A  495  ALA A  520  1                                  26    
HELIX   22 AC4 ASP A  523  ASN A  551  1                                  29    
HELIX   23 AC5 ASN A  554  LYS A  570  1                                  17    
HELIX   24 AC6 SER A  571  SER A  585  1                                  15    
HELIX   25 AC7 ASN A  588  ASN A  616  1                                  29    
HELIX   26 AC8 PRO A  648  ALA A  660  1                                  13    
HELIX   27 AC9 ASN A  668  GLN A  683  1                                  16    
HELIX   28 AD1 ASN A  689  GLY A  711  1                                  23    
HELIX   29 AD2 SER A  718  ALA A  746  1                                  29    
HELIX   30 AD3 ASP A  749  ASP A  761  1                                  13    
HELIX   31 AD4 ARG A  762  THR A  779  1                                  18    
HELIX   32 AD5 ASP A  785  CYS A  818  1                                  34    
HELIX   33 AD6 SER A  825  ILE A  830  5                                   6    
HELIX   34 AD7 THR B    7  SER B   33  1                                  27    
HELIX   35 AD8 LEU B   40  SER B   65  1                                  26    
HELIX   36 AD9 ASP B   67  ASP B   98  1                                  32    
HELIX   37 AE1 SER B  101  LEU B  145  1                                  45    
HELIX   38 AE2 ASP B  146  ILE B  151  5                                   6    
HELIX   39 AE3 VAL B  153  HIS B  179  1                                  27    
HELIX   40 AE4 PRO B  180  LEU B  182  5                                   3    
HELIX   41 AE5 ASN B  184  VAL B  217  1                                  34    
HELIX   42 AE6 GLY B  223  GLN B  250  1                                  28    
HELIX   43 AE7 SER B  267  SER B  284  1                                  18    
HELIX   44 AE8 SER B  288  ALA B  307  1                                  20    
HELIX   45 AE9 THR B  311  LYS B  338  1                                  28    
HELIX   46 AF1 SER B  343  PHE B  376  1                                  34    
HELIX   47 AF2 GLY B  380  LEU B  391  1                                  12    
HELIX   48 AF3 ASN B  398  GLY B  428  1                                  31    
HELIX   49 AF4 SER B  431  THR B  450  1                                  20    
HELIX   50 AF5 ALA B  451  ASN B  462  1                                  12    
HELIX   51 AF6 ASN B  465  ILE B  494  1                                  30    
HELIX   52 AF7 ASP B  495  ALA B  520  1                                  26    
HELIX   53 AF8 ASP B  523  ASN B  551  1                                  29    
HELIX   54 AF9 ASN B  554  SER B  585  1                                  32    
HELIX   55 AG1 ASN B  588  ASN B  616  1                                  29    
HELIX   56 AG2 PRO B  648  ALA B  660  1                                  13    
HELIX   57 AG3 ASN B  668  GLN B  683  1                                  16    
HELIX   58 AG4 ASN B  689  THR B  709  1                                  21    
HELIX   59 AG5 SER B  718  CYS B  747  1                                  30    
HELIX   60 AG6 ASP B  749  ASP B  761  1                                  13    
HELIX   61 AG7 ARG B  762  MET B  781  1                                  20    
HELIX   62 AG8 ASP B  785  CYS B  818  1                                  34    
HELIX   63 AG9 SER B  825  ILE B  830  5                                   6    
CRYST1   50.344   93.676  101.634 114.81  93.29  90.23 P 1           2          
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      0.019863  0.000079  0.001296        0.00000                         
SCALE2      0.000000  0.010675  0.004948        0.00000                         
SCALE3      0.000000  0.000000  0.010863        0.00000                         
ATOM      1  N   MET A   1     -43.004 -36.941 -70.359  1.00107.47           N  
ANISOU    1  N   MET A   1    16541  12297  11996  -1279   1659    796       N  
ATOM      2  CA  MET A   1     -44.236 -36.244 -70.005  1.00105.74           C  
ANISOU    2  CA  MET A   1    16599  11865  11714  -1212   1463    809       C  
ATOM      3  C   MET A   1     -45.133 -37.135 -69.151  1.00 99.33           C  
ANISOU    3  C   MET A   1    15683  11107  10952   -955   1266    764       C  
ATOM      4  O   MET A   1     -45.876 -37.965 -69.679  1.00101.31           O  
ANISOU    4  O   MET A   1    16010  11340  11144   -757   1242    778       O  
ATOM      5  CB  MET A   1     -44.973 -35.791 -71.265  1.00111.42           C  
ANISOU    5  CB  MET A   1    17713  12366  12254  -1187   1506    891       C  
ATOM      6  CG  MET A   1     -44.145 -34.895 -72.169  1.00118.95           C  
ANISOU    6  CG  MET A   1    18835  13237  13125  -1454   1723    955       C  
ATOM      7  SD  MET A   1     -44.341 -35.315 -73.911  1.00123.07           S  
ANISOU    7  SD  MET A   1    19642  13696  13423  -1398   1890   1042       S  
ATOM      8  CE  MET A   1     -43.833 -37.033 -73.895  1.00121.58           C  
ANISOU    8  CE  MET A   1    19079  13792  13324  -1228   1983    961       C  
ATOM      9  N   PRO A   2     -45.061 -36.964 -67.834  1.00 91.59           N  
ANISOU    9  N   PRO A   2    14539  10193  10067   -978   1133    705       N  
ATOM     10  CA  PRO A   2     -45.829 -37.828 -66.931  1.00 82.23           C  
ANISOU   10  CA  PRO A   2    13252   9070   8921   -763    973    667       C  
ATOM     11  C   PRO A   2     -47.324 -37.571 -67.030  1.00 73.14           C  
ANISOU   11  C   PRO A   2    12361   7727   7703   -618    853    665       C  
ATOM     12  O   PRO A   2     -47.780 -36.525 -67.497  1.00 75.17           O  
ANISOU   12  O   PRO A   2    12873   7790   7898   -679    844    688       O  
ATOM     13  CB  PRO A   2     -45.299 -37.453 -65.540  1.00 83.15           C  
ANISOU   13  CB  PRO A   2    13184   9290   9118   -875    870    606       C  
ATOM     14  CG  PRO A   2     -44.003 -36.738 -65.788  1.00 88.06           C  
ANISOU   14  CG  PRO A   2    13704   9976   9780  -1139    993    605       C  
ATOM     15  CD  PRO A   2     -44.181 -36.042 -67.100  1.00 94.15           C  
ANISOU   15  CD  PRO A   2    14755  10557  10460  -1225   1135    664       C  
ATOM     16  N   VAL A   3     -48.094 -38.561 -66.573  1.00 66.05           N  
ANISOU   16  N   VAL A   3    11389   6882   6826   -419    761    639       N  
ATOM     17  CA  VAL A   3     -49.544 -38.427 -66.542  1.00 59.28           C  
ANISOU   17  CA  VAL A   3    10706   5881   5935   -274    644    617       C  
ATOM     18  C   VAL A   3     -49.929 -37.350 -65.535  1.00 58.63           C  
ANISOU   18  C   VAL A   3    10692   5704   5882   -337    548    561       C  
ATOM     19  O   VAL A   3     -49.275 -37.177 -64.496  1.00 57.34           O  
ANISOU   19  O   VAL A   3    10389   5636   5761   -443    531    518       O  
ATOM     20  CB  VAL A   3     -50.203 -39.779 -66.211  1.00 54.20           C  
ANISOU   20  CB  VAL A   3     9945   5327   5320    -87    594    592       C  
ATOM     21  CG1 VAL A   3     -49.744 -40.294 -64.851  1.00 51.08           C  
ANISOU   21  CG1 VAL A   3     9333   5081   4994    -92    555    560       C  
ATOM     22  CG2 VAL A   3     -51.722 -39.670 -66.273  1.00 51.28           C  
ANISOU   22  CG2 VAL A   3     9717   4832   4935     49    485    557       C  
ATOM     23  N   LYS A   4     -50.986 -36.604 -65.848  1.00 58.54           N  
ANISOU   23  N   LYS A   4    10900   5501   5842   -266    481    554       N  
ATOM     24  CA  LYS A   4     -51.419 -35.479 -65.035  1.00 57.21           C  
ANISOU   24  CA  LYS A   4    10839   5195   5703   -307    413    490       C  
ATOM     25  C   LYS A   4     -52.860 -35.672 -64.583  1.00 53.00           C  
ANISOU   25  C   LYS A   4    10327   4607   5204   -105    309    425       C  
ATOM     26  O   LYS A   4     -53.682 -36.258 -65.294  1.00 52.32           O  
ANISOU   26  O   LYS A   4    10264   4510   5107     52    271    449       O  
ATOM     27  CB  LYS A   4     -51.293 -34.158 -65.808  1.00 57.03           C  
ANISOU   27  CB  LYS A   4    11082   4950   5637   -411    442    541       C  
ATOM     28  CG  LYS A   4     -49.876 -33.810 -66.238  1.00 57.43           C  
ANISOU   28  CG  LYS A   4    11118   5041   5660   -656    575    594       C  
ATOM     29  CD  LYS A   4     -48.983 -33.556 -65.038  1.00 57.98           C  
ANISOU   29  CD  LYS A   4    11013   5225   5792   -840    582    514       C  
ATOM     30  CE  LYS A   4     -47.581 -33.158 -65.469  1.00 64.10           C  
ANISOU   30  CE  LYS A   4    11737   6053   6565  -1104    716    552       C  
ATOM     31  NZ  LYS A   4     -46.724 -32.808 -64.300  1.00 67.31           N  
ANISOU   31  NZ  LYS A   4    11969   6574   7031  -1304    690    462       N  
ATOM     32  N   PHE A   5     -53.158 -35.168 -63.377  1.00 53.15           N  
ANISOU   32  N   PHE A   5    10331   4599   5264   -122    271    328       N  
ATOM     33  CA  PHE A   5     -54.524 -35.166 -62.864  1.00 55.90           C  
ANISOU   33  CA  PHE A   5    10695   4885   5659     52    204    245       C  
ATOM     34  C   PHE A   5     -54.786 -33.952 -61.981  1.00 58.70           C  
ANISOU   34  C   PHE A   5    11169   5093   6042      8    192    144       C  
ATOM     35  O   PHE A   5     -55.560 -34.040 -61.022  1.00 62.11           O  
ANISOU   35  O   PHE A   5    11547   5543   6509     90    179     38       O  
ATOM     36  CB  PHE A   5     -54.840 -36.452 -62.085  1.00 57.48           C  
ANISOU   36  CB  PHE A   5    10689   5276   5875    125    206    204       C  
ATOM     37  CG  PHE A   5     -53.629 -37.266 -61.733  1.00 53.89           C  
ANISOU   37  CG  PHE A   5    10077   5011   5386     11    248    250       C  
ATOM     38  CD1 PHE A   5     -52.753 -36.844 -60.744  1.00 54.67           C  
ANISOU   38  CD1 PHE A   5    10132   5177   5464   -145    249    213       C  
ATOM     39  CD2 PHE A   5     -53.373 -38.461 -62.384  1.00 51.33           C  
ANISOU   39  CD2 PHE A   5     9648   4799   5056     69    278    322       C  
ATOM     40  CE1 PHE A   5     -51.638 -37.599 -60.416  1.00 55.38           C  
ANISOU   40  CE1 PHE A   5    10049   5456   5536   -223    259    260       C  
ATOM     41  CE2 PHE A   5     -52.263 -39.220 -62.063  1.00 52.30           C  
ANISOU   41  CE2 PHE A   5     9614   5087   5169      2    313    366       C  
ATOM     42  CZ  PHE A   5     -51.394 -38.789 -61.078  1.00 55.28           C  
ANISOU   42  CZ  PHE A   5     9923   5545   5536   -135    294    341       C  
ATOM     43  N   HIS A   6     -54.155 -32.818 -62.290  1.00 61.93           N  
ANISOU   43  N   HIS A   6    11753   5345   6434   -132    214    169       N  
ATOM     44  CA  HIS A   6     -54.350 -31.578 -61.548  1.00 62.36           C  
ANISOU   44  CA  HIS A   6    11966   5213   6513   -187    213     66       C  
ATOM     45  C   HIS A   6     -55.641 -30.864 -61.923  1.00 57.97           C  
ANISOU   45  C   HIS A   6    11582   4423   6021     30    161     40       C  
ATOM     46  O   HIS A   6     -55.914 -29.787 -61.382  1.00 59.58           O  
ANISOU   46  O   HIS A   6    11945   4430   6261     23    169    -52       O  
ATOM     47  CB  HIS A   6     -53.160 -30.639 -61.774  1.00 63.87           C  
ANISOU   47  CB  HIS A   6    12293   5305   6671   -443    265    100       C  
ATOM     48  CG  HIS A   6     -52.899 -30.333 -63.217  1.00 67.35           C  
ANISOU   48  CG  HIS A   6    12892   5619   7079   -460    292    245       C  
ATOM     49  ND1 HIS A   6     -53.247 -29.132 -63.798  1.00 66.86           N  
ANISOU   49  ND1 HIS A   6    13132   5254   7020   -443    285    281       N  
ATOM     50  CD2 HIS A   6     -52.328 -31.074 -64.196  1.00 68.43           C  
ANISOU   50  CD2 HIS A   6    12952   5882   7165   -490    334    364       C  
ATOM     51  CE1 HIS A   6     -52.898 -29.145 -65.072  1.00 68.48           C  
ANISOU   51  CE1 HIS A   6    13450   5410   7159   -475    317    427       C  
ATOM     52  NE2 HIS A   6     -52.340 -30.312 -65.339  1.00 71.53           N  
ANISOU   52  NE2 HIS A   6    13607   6061   7510   -508    356    470       N  
ATOM     53  N   THR A   7     -56.441 -31.445 -62.813  1.00 58.31           N  
ANISOU   53  N   THR A   7    11591   4482   6081    226    101    109       N  
ATOM     54  CA  THR A   7     -57.637 -30.818 -63.351  1.00 58.41           C  
ANISOU   54  CA  THR A   7    11741   4293   6160    455     16    107       C  
ATOM     55  C   THR A   7     -58.787 -31.816 -63.307  1.00 59.54           C  
ANISOU   55  C   THR A   7    11674   4583   6367    664    -42     58       C  
ATOM     56  O   THR A   7     -58.594 -33.005 -63.580  1.00 59.96           O  
ANISOU   56  O   THR A   7    11564   4840   6379    641    -36    103       O  
ATOM     57  CB  THR A   7     -57.375 -30.327 -64.788  1.00 61.58           C  
ANISOU   57  CB  THR A   7    12368   4535   6493    456    -29    268       C  
ATOM     58  OG1 THR A   7     -56.815 -29.006 -64.752  1.00 62.91           O  
ANISOU   58  OG1 THR A   7    12799   4456   6649    324     15    284       O  
ATOM     59  CG2 THR A   7     -58.640 -30.314 -65.617  1.00 66.18           C  
ANISOU   59  CG2 THR A   7    13002   5029   7115    733   -169    307       C  
ATOM     60  N   LYS A   8     -59.979 -31.329 -62.940  1.00 59.29           N  
ANISOU   60  N   LYS A   8    11640   4442   6447    864    -87    -44       N  
ATOM     61  CA  LYS A   8     -61.149 -32.199 -62.854  1.00 60.10           C  
ANISOU   61  CA  LYS A   8    11518   4684   6634   1046   -131   -112       C  
ATOM     62  C   LYS A   8     -61.468 -32.861 -64.189  1.00 63.73           C  
ANISOU   62  C   LYS A   8    11952   5201   7062   1140   -250      4       C  
ATOM     63  O   LYS A   8     -61.981 -33.985 -64.214  1.00 63.90           O  
ANISOU   63  O   LYS A   8    11767   5407   7107   1183   -263    -27       O  
ATOM     64  CB  LYS A   8     -62.358 -31.409 -62.354  1.00 59.40           C  
ANISOU   64  CB  LYS A   8    11424   4452   6692   1258   -153   -245       C  
ATOM     65  CG  LYS A   8     -62.241 -30.948 -60.913  1.00 64.69           C  
ANISOU   65  CG  LYS A   8    12095   5099   7386   1176    -16   -402       C  
ATOM     66  CD  LYS A   8     -63.410 -30.057 -60.520  1.00 69.43           C  
ANISOU   66  CD  LYS A   8    12712   5526   8142   1406    -16   -542       C  
ATOM     67  CE  LYS A   8     -63.323 -29.647 -59.061  1.00 62.75           C  
ANISOU   67  CE  LYS A   8    11884   4663   7294   1315    144   -721       C  
ATOM     68  NZ  LYS A   8     -64.476 -28.792 -58.664  1.00 77.59           N  
ANISOU   68  NZ  LYS A   8    13772   6369   9339   1556    175   -879       N  
ATOM     69  N   THR A   9     -61.186 -32.183 -65.303  1.00 63.33           N  
ANISOU   69  N   THR A   9    12132   4987   6943   1160   -333    134       N  
ATOM     70  CA  THR A   9     -61.352 -32.811 -66.610  1.00 65.33           C  
ANISOU   70  CA  THR A   9    12405   5302   7116   1217   -443    247       C  
ATOM     71  C   THR A   9     -60.334 -33.926 -66.816  1.00 64.16           C  
ANISOU   71  C   THR A   9    12174   5350   6854   1024   -344    302       C  
ATOM     72  O   THR A   9     -60.675 -35.002 -67.327  1.00 69.83           O  
ANISOU   72  O   THR A   9    12768   6217   7548   1063   -386    307       O  
ATOM     73  CB  THR A   9     -61.229 -31.762 -67.716  1.00 64.01           C  
ANISOU   73  CB  THR A   9    12553   4899   6868   1270   -542    387       C  
ATOM     74  OG1 THR A   9     -62.264 -30.783 -67.563  1.00 62.57           O  
ANISOU   74  OG1 THR A   9    12439   4524   6812   1500   -654    340       O  
ATOM     75  CG2 THR A   9     -61.344 -32.410 -69.088  1.00 60.56           C  
ANISOU   75  CG2 THR A   9    12172   4535   6302   1310   -655    503       C  
ATOM     76  N   LEU A  10     -59.080 -33.685 -66.422  1.00 62.61           N  
ANISOU   76  N   LEU A  10    12038   5152   6597    815   -213    333       N  
ATOM     77  CA  LEU A  10     -58.044 -34.707 -66.537  1.00 61.59           C  
ANISOU   77  CA  LEU A  10    11804   5210   6387    653   -111    378       C  
ATOM     78  C   LEU A  10     -58.425 -35.965 -65.769  1.00 58.97           C  
ANISOU   78  C   LEU A  10    11209   5082   6115    686    -83    289       C  
ATOM     79  O   LEU A  10     -58.452 -37.063 -66.332  1.00 51.78           O  
ANISOU   79  O   LEU A  10    10213   4294   5167    702    -85    316       O  
ATOM     80  CB  LEU A  10     -56.710 -34.158 -66.033  1.00 59.51           C  
ANISOU   80  CB  LEU A  10    11593   4929   6088    431     10    399       C  
ATOM     81  CG  LEU A  10     -55.826 -33.445 -67.054  1.00 58.82           C  
ANISOU   81  CG  LEU A  10    11733   4719   5898    301     54    524       C  
ATOM     82  CD1 LEU A  10     -54.644 -32.791 -66.362  1.00 61.23           C  
ANISOU   82  CD1 LEU A  10    12052   5006   6206     66    165    508       C  
ATOM     83  CD2 LEU A  10     -55.346 -34.428 -68.104  1.00 56.50           C  
ANISOU   83  CD2 LEU A  10    11406   4557   5503    271     98    610       C  
ATOM     84  N   GLU A  11     -58.719 -35.821 -64.476  1.00 62.22           N  
ANISOU   84  N   GLU A  11    11517   5518   6607    686    -46    180       N  
ATOM     85  CA  GLU A  11     -59.121 -36.971 -63.673  1.00 61.37           C  
ANISOU   85  CA  GLU A  11    11193   5582   6541    705     -5    105       C  
ATOM     86  C   GLU A  11     -60.394 -37.606 -64.216  1.00 61.67           C  
ANISOU   86  C   GLU A  11    11138   5652   6642    864    -86     67       C  
ATOM     87  O   GLU A  11     -60.498 -38.838 -64.304  1.00 57.49           O  
ANISOU   87  O   GLU A  11    10482   5256   6104    851    -62     65       O  
ATOM     88  CB  GLU A  11     -59.306 -36.543 -62.217  1.00 62.73           C  
ANISOU   88  CB  GLU A  11    11318   5755   6761    676     55    -10       C  
ATOM     89  CG  GLU A  11     -60.094 -37.526 -61.368  1.00 65.99           C  
ANISOU   89  CG  GLU A  11    11547   6303   7223    722    102    -99       C  
ATOM     90  CD  GLU A  11     -60.335 -37.014 -59.960  1.00 69.59           C  
ANISOU   90  CD  GLU A  11    11993   6750   7696    692    176   -221       C  
ATOM     91  OE1 GLU A  11     -59.483 -36.258 -59.444  1.00 67.27           O  
ANISOU   91  OE1 GLU A  11    11807   6409   7344    576    199   -224       O  
ATOM     92  OE2 GLU A  11     -61.379 -37.365 -59.371  1.00 72.84           O  
ANISOU   92  OE2 GLU A  11    12292   7206   8175    770    221   -324       O  
ATOM     93  N   SER A  12     -61.363 -36.777 -64.608  1.00 66.51           N  
ANISOU   93  N   SER A  12    11812   6137   7323   1015   -192     35       N  
ATOM     94  CA  SER A  12     -62.649 -37.289 -65.072  1.00 66.88           C  
ANISOU   94  CA  SER A  12    11731   6230   7450   1168   -295    -20       C  
ATOM     95  C   SER A  12     -62.494 -38.166 -66.306  1.00 64.08           C  
ANISOU   95  C   SER A  12    11400   5945   7003   1151   -364     62       C  
ATOM     96  O   SER A  12     -63.196 -39.173 -66.449  1.00 57.05           O  
ANISOU   96  O   SER A  12    10354   5168   6153   1179   -392      5       O  
ATOM     97  CB  SER A  12     -63.603 -36.129 -65.350  1.00 65.79           C  
ANISOU   97  CB  SER A  12    11659   5933   7406   1358   -422    -53       C  
ATOM     98  OG  SER A  12     -64.844 -36.596 -65.848  1.00 70.27           O  
ANISOU   98  OG  SER A  12    12069   6568   8064   1509   -551   -111       O  
ATOM     99  N   VAL A  13     -61.584 -37.805 -67.203  1.00 57.48           N  
ANISOU   99  N   VAL A  13    10766   5038   6036   1088   -376    186       N  
ATOM    100  CA  VAL A  13     -61.356 -38.578 -68.425  1.00 59.86           C  
ANISOU  100  CA  VAL A  13    11130   5395   6218   1063   -419    257       C  
ATOM    101  C   VAL A  13     -60.436 -39.767 -68.184  1.00 60.61           C  
ANISOU  101  C   VAL A  13    11138   5627   6266    923   -267    266       C  
ATOM    102  O   VAL A  13     -60.718 -40.885 -68.614  1.00 61.83           O  
ANISOU  102  O   VAL A  13    11218   5873   6401    925   -275    238       O  
ATOM    103  CB  VAL A  13     -60.809 -37.657 -69.541  1.00 64.34           C  
ANISOU  103  CB  VAL A  13    11978   5822   6647   1054   -474    388       C  
ATOM    104  CG1 VAL A  13     -60.224 -38.486 -70.676  1.00 53.98           C  
ANISOU  104  CG1 VAL A  13    10755   4581   5175    977   -447    458       C  
ATOM    105  CG2 VAL A  13     -61.895 -36.721 -70.056  1.00 61.38           C  
ANISOU  105  CG2 VAL A  13    11706   5310   6306   1241   -675    398       C  
ATOM    106  N   ILE A  14     -59.324 -39.547 -67.493  1.00 58.38           N  
ANISOU  106  N   ILE A  14    10860   5354   5969    804   -136    299       N  
ATOM    107  CA  ILE A  14     -58.284 -40.563 -67.384  1.00 57.78           C  
ANISOU  107  CA  ILE A  14    10712   5394   5847    696     -7    330       C  
ATOM    108  C   ILE A  14     -58.674 -41.677 -66.413  1.00 60.55           C  
ANISOU  108  C   ILE A  14    10871   5858   6279    706     41    254       C  
ATOM    109  O   ILE A  14     -58.287 -42.838 -66.609  1.00 59.55           O  
ANISOU  109  O   ILE A  14    10690   5809   6127    679    107    268       O  
ATOM    110  CB  ILE A  14     -56.948 -39.900 -66.989  1.00 57.69           C  
ANISOU  110  CB  ILE A  14    10744   5371   5803    565     93    390       C  
ATOM    111  CG1 ILE A  14     -56.461 -39.006 -68.134  1.00 65.93           C  
ANISOU  111  CG1 ILE A  14    12003   6302   6745    519     86    481       C  
ATOM    112  CG2 ILE A  14     -55.891 -40.934 -66.629  1.00 54.41           C  
ANISOU  112  CG2 ILE A  14    10199   5096   5380    485    213    412       C  
ATOM    113  CD1 ILE A  14     -55.124 -38.355 -67.876  1.00 69.24           C  
ANISOU  113  CD1 ILE A  14    12455   6713   7139    354    198    533       C  
ATOM    114  N   ASP A  15     -59.446 -41.364 -65.370  1.00 60.44           N  
ANISOU  114  N   ASP A  15    10768   5839   6356    745     24    173       N  
ATOM    115  CA  ASP A  15     -59.790 -42.380 -64.374  1.00 68.78           C  
ANISOU  115  CA  ASP A  15    11672   6992   7468    730     93    112       C  
ATOM    116  C   ASP A  15     -60.501 -43.588 -64.981  1.00 61.77           C  
ANISOU  116  C   ASP A  15    10722   6150   6600    762     77     78       C  
ATOM    117  O   ASP A  15     -60.008 -44.720 -64.814  1.00 57.53           O  
ANISOU  117  O   ASP A  15    10147   5670   6041    713    161    104       O  
ATOM    118  CB  ASP A  15     -60.597 -41.728 -63.245  1.00 81.34           C  
ANISOU  118  CB  ASP A  15    13201   8564   9140    761     98     16       C  
ATOM    119  CG  ASP A  15     -61.008 -42.717 -62.177  1.00 88.20           C  
ANISOU  119  CG  ASP A  15    13942   9525  10044    727    190    -42       C  
ATOM    120  OD1 ASP A  15     -60.156 -43.074 -61.336  1.00 95.59           O  
ANISOU  120  OD1 ASP A  15    14879  10519  10923    646    267      0       O  
ATOM    121  OD2 ASP A  15     -62.185 -43.135 -62.175  1.00 92.33           O  
ANISOU  121  OD2 ASP A  15    14366  10067  10649    776    183   -128       O  
ATOM    122  N   PRO A  16     -61.625 -43.440 -65.699  1.00 58.87           N  
ANISOU  122  N   PRO A  16    10341   5753   6274    843    -37     20       N  
ATOM    123  CA  PRO A  16     -62.296 -44.642 -66.223  1.00 56.80           C  
ANISOU  123  CA  PRO A  16    10010   5541   6030    839    -56    -33       C  
ATOM    124  C   PRO A  16     -61.483 -45.381 -67.272  1.00 59.50           C  
ANISOU  124  C   PRO A  16    10465   5884   6259    798    -34     33       C  
ATOM    125  O   PRO A  16     -61.552 -46.615 -67.329  1.00 61.72           O  
ANISOU  125  O   PRO A  16    10708   6198   6545    754     27      2       O  
ATOM    126  CB  PRO A  16     -63.605 -44.091 -66.806  1.00 57.35           C  
ANISOU  126  CB  PRO A  16    10031   5592   6168    940   -221   -109       C  
ATOM    127  CG  PRO A  16     -63.291 -42.682 -67.151  1.00 58.35           C  
ANISOU  127  CG  PRO A  16    10294   5623   6252   1012   -304    -42       C  
ATOM    128  CD  PRO A  16     -62.342 -42.210 -66.090  1.00 56.90           C  
ANISOU  128  CD  PRO A  16    10138   5420   6060    946   -169     -2       C  
ATOM    129  N   VAL A  17     -60.712 -44.671 -68.098  1.00 55.80           N  
ANISOU  129  N   VAL A  17    10148   5367   5685    803    -62    118       N  
ATOM    130  CA  VAL A  17     -59.898 -45.345 -69.104  1.00 58.81           C  
ANISOU  130  CA  VAL A  17    10642   5754   5949    762     -6    167       C  
ATOM    131  C   VAL A  17     -58.790 -46.153 -68.440  1.00 56.58           C  
ANISOU  131  C   VAL A  17    10302   5517   5679    705    164    206       C  
ATOM    132  O   VAL A  17     -58.502 -47.288 -68.842  1.00 57.48           O  
ANISOU  132  O   VAL A  17    10429   5645   5767    692    238    194       O  
ATOM    133  CB  VAL A  17     -59.334 -44.325 -70.111  1.00 60.35           C  
ANISOU  133  CB  VAL A  17    11025   5887   6019    763    -49    253       C  
ATOM    134  CG1 VAL A  17     -58.558 -45.037 -71.210  1.00 56.25           C  
ANISOU  134  CG1 VAL A  17    10628   5380   5364    717     36    285       C  
ATOM    135  CG2 VAL A  17     -60.459 -43.489 -70.704  1.00 64.41           C  
ANISOU  135  CG2 VAL A  17    11608   6343   6522    852   -247    234       C  
ATOM    136  N   ALA A  18     -58.148 -45.584 -67.416  1.00 58.47           N  
ANISOU  136  N   ALA A  18    10483   5773   5958    680    216    248       N  
ATOM    137  CA  ALA A  18     -57.153 -46.340 -66.663  1.00 54.88           C  
ANISOU  137  CA  ALA A  18     9952   5378   5524    648    338    290       C  
ATOM    138  C   ALA A  18     -57.785 -47.550 -65.990  1.00 55.84           C  
ANISOU  138  C   ALA A  18     9991   5515   5708    661    373    241       C  
ATOM    139  O   ALA A  18     -57.158 -48.612 -65.883  1.00 58.27           O  
ANISOU  139  O   ALA A  18    10285   5837   6019    667    463    272       O  
ATOM    140  CB  ALA A  18     -56.477 -45.440 -65.629  1.00 52.66           C  
ANISOU  140  CB  ALA A  18     9622   5125   5261    604    350    329       C  
ATOM    141  N   GLN A  19     -59.034 -47.410 -65.538  1.00 52.96           N  
ANISOU  141  N   GLN A  19     9576   5142   5404    668    312    162       N  
ATOM    142  CA  GLN A  19     -59.742 -48.546 -64.958  1.00 54.34           C  
ANISOU  142  CA  GLN A  19     9685   5322   5638    649    364    109       C  
ATOM    143  C   GLN A  19     -59.950 -49.648 -65.997  1.00 56.58           C  
ANISOU  143  C   GLN A  19    10024   5571   5905    643    377     73       C  
ATOM    144  O   GLN A  19     -59.711 -50.831 -65.723  1.00 51.96           O  
ANISOU  144  O   GLN A  19     9448   4960   5333    625    474     84       O  
ATOM    145  CB  GLN A  19     -61.075 -48.073 -64.375  1.00 53.58           C  
ANISOU  145  CB  GLN A  19     9500   5237   5622    647    314     12       C  
ATOM    146  CG  GLN A  19     -61.657 -48.977 -63.302  1.00 57.97           C  
ANISOU  146  CG  GLN A  19     9982   5809   6234    592    413    -28       C  
ATOM    147  CD  GLN A  19     -62.497 -50.097 -63.875  1.00 63.98           C  
ANISOU  147  CD  GLN A  19    10721   6547   7042    548    425   -104       C  
ATOM    148  OE1 GLN A  19     -62.845 -50.087 -65.056  1.00 70.93           O  
ANISOU  148  OE1 GLN A  19    11621   7414   7914    566    329   -150       O  
ATOM    149  NE2 GLN A  19     -62.832 -51.072 -63.039  1.00 63.31           N  
ANISOU  149  NE2 GLN A  19    10613   6451   6992    476    541   -118       N  
ATOM    150  N   GLN A  20     -60.378 -49.269 -67.206  1.00 58.49           N  
ANISOU  150  N   GLN A  20    10325   5796   6101    660    276     32       N  
ATOM    151  CA  GLN A  20     -60.607 -50.252 -68.263  1.00 62.50           C  
ANISOU  151  CA  GLN A  20    10910   6272   6566    639    274    -22       C  
ATOM    152  C   GLN A  20     -59.313 -50.949 -68.668  1.00 59.84           C  
ANISOU  152  C   GLN A  20    10667   5907   6162    649    405     42       C  
ATOM    153  O   GLN A  20     -59.292 -52.169 -68.873  1.00 56.21           O  
ANISOU  153  O   GLN A  20    10249   5398   5709    631    485      3       O  
ATOM    154  CB  GLN A  20     -61.246 -49.576 -69.477  1.00 64.69           C  
ANISOU  154  CB  GLN A  20    11256   6550   6772    661    112    -66       C  
ATOM    155  CG  GLN A  20     -62.681 -49.128 -69.275  1.00 66.20           C  
ANISOU  155  CG  GLN A  20    11325   6773   7056    675    -34   -157       C  
ATOM    156  CD  GLN A  20     -63.244 -48.424 -70.495  1.00 75.89           C  
ANISOU  156  CD  GLN A  20    12631   8002   8202    726   -231   -177       C  
ATOM    157  OE1 GLN A  20     -62.544 -47.666 -71.167  1.00 77.12           O  
ANISOU  157  OE1 GLN A  20    12939   8126   8237    763   -260    -89       O  
ATOM    158  NE2 GLN A  20     -64.512 -48.679 -70.793  1.00 81.40           N  
ANISOU  158  NE2 GLN A  20    13227   8739   8961    721   -371   -291       N  
ATOM    159  N   VAL A  21     -58.227 -50.186 -68.803  1.00 63.81           N  
ANISOU  159  N   VAL A  21    11202   6433   6610    675    437    132       N  
ATOM    160  CA  VAL A  21     -56.938 -50.771 -69.168  1.00 64.67           C  
ANISOU  160  CA  VAL A  21    11357   6537   6679    697    576    185       C  
ATOM    161  C   VAL A  21     -56.470 -51.735 -68.084  1.00 67.15           C  
ANISOU  161  C   VAL A  21    11586   6845   7082    726    676    222       C  
ATOM    162  O   VAL A  21     -56.017 -52.855 -68.368  1.00 68.34           O  
ANISOU  162  O   VAL A  21    11781   6944   7241    762    782    215       O  
ATOM    163  CB  VAL A  21     -55.909 -49.656 -69.424  1.00 68.38           C  
ANISOU  163  CB  VAL A  21    11840   7049   7092    692    597    268       C  
ATOM    164  CG1 VAL A  21     -54.500 -50.172 -69.226  1.00 73.12           C  
ANISOU  164  CG1 VAL A  21    12381   7684   7717    721    748    329       C  
ATOM    165  CG2 VAL A  21     -56.087 -49.091 -70.822  1.00 69.76           C  
ANISOU  165  CG2 VAL A  21    12174   7198   7134    670    550    251       C  
ATOM    166  N   GLY A  22     -56.574 -51.309 -66.823  1.00 63.73           N  
ANISOU  166  N   GLY A  22    11053   6454   6708    718    643    263       N  
ATOM    167  CA  GLY A  22     -56.274 -52.208 -65.724  1.00 60.23           C  
ANISOU  167  CA  GLY A  22    10562   6001   6323    745    711    311       C  
ATOM    168  C   GLY A  22     -57.071 -53.493 -65.797  1.00 57.20           C  
ANISOU  168  C   GLY A  22    10238   5521   5973    729    759    249       C  
ATOM    169  O   GLY A  22     -56.541 -54.579 -65.549  1.00 53.11           O  
ANISOU  169  O   GLY A  22     9757   4941   5483    778    852    292       O  
ATOM    170  N   GLN A  23     -58.354 -53.393 -66.162  1.00 57.09           N  
ANISOU  170  N   GLN A  23    10235   5489   5967    659    693    145       N  
ATOM    171  CA  GLN A  23     -59.154 -54.601 -66.329  1.00 60.32           C  
ANISOU  171  CA  GLN A  23    10699   5807   6414    605    740     65       C  
ATOM    172  C   GLN A  23     -58.660 -55.450 -67.494  1.00 59.82           C  
ANISOU  172  C   GLN A  23    10762   5662   6307    632    804     29       C  
ATOM    173  O   GLN A  23     -58.781 -56.680 -67.454  1.00 56.06           O  
ANISOU  173  O   GLN A  23    10363   5073   5864    613    895     -2       O  
ATOM    174  CB  GLN A  23     -60.627 -54.245 -66.513  1.00 61.79           C  
ANISOU  174  CB  GLN A  23    10825   6021   6633    518    639    -55       C  
ATOM    175  CG  GLN A  23     -61.317 -53.827 -65.226  1.00 62.90           C  
ANISOU  175  CG  GLN A  23    10848   6211   6841    478    639    -55       C  
ATOM    176  CD  GLN A  23     -62.814 -54.053 -65.273  1.00 68.78           C  
ANISOU  176  CD  GLN A  23    11508   6962   7663    378    602   -191       C  
ATOM    177  OE1 GLN A  23     -63.397 -54.210 -66.346  1.00 71.84           O  
ANISOU  177  OE1 GLN A  23    11904   7345   8048    347    517   -289       O  
ATOM    178  NE2 GLN A  23     -63.445 -54.082 -64.104  1.00 70.60           N  
ANISOU  178  NE2 GLN A  23    11652   7215   7959    318    669   -205       N  
ATOM    179  N   LEU A  24     -58.103 -54.823 -68.535  1.00 63.19           N  
ANISOU  179  N   LEU A  24    11231   6129   6648    668    775     28       N  
ATOM    180  CA  LEU A  24     -57.493 -55.600 -69.612  1.00 64.73           C  
ANISOU  180  CA  LEU A  24    11558   6253   6784    699    871    -11       C  
ATOM    181  C   LEU A  24     -56.309 -56.409 -69.100  1.00 65.58           C  
ANISOU  181  C   LEU A  24    11662   6306   6948    803   1023     74       C  
ATOM    182  O   LEU A  24     -56.162 -57.593 -69.433  1.00 66.41           O  
ANISOU  182  O   LEU A  24    11874   6288   7072    831   1132     28       O  
ATOM    183  CB  LEU A  24     -57.058 -54.681 -70.753  1.00 66.19           C  
ANISOU  183  CB  LEU A  24    11803   6501   6846    707    835    -13       C  
ATOM    184  CG  LEU A  24     -58.163 -54.192 -71.687  1.00 67.00           C  
ANISOU  184  CG  LEU A  24    11978   6622   6856    633    679   -108       C  
ATOM    185  CD1 LEU A  24     -57.609 -53.195 -72.695  1.00 69.77           C  
ANISOU  185  CD1 LEU A  24    12422   7023   7063    646    651    -70       C  
ATOM    186  CD2 LEU A  24     -58.808 -55.376 -72.392  1.00 64.49           C  
ANISOU  186  CD2 LEU A  24    11777   6216   6509    572    694   -243       C  
ATOM    187  N   VAL A  25     -55.455 -55.789 -68.282  1.00 66.41           N  
ANISOU  187  N   VAL A  25    11646   6498   7087    866   1023    193       N  
ATOM    188  CA  VAL A  25     -54.334 -56.526 -67.701  1.00 64.94           C  
ANISOU  188  CA  VAL A  25    11424   6283   6970    988   1130    284       C  
ATOM    189  C   VAL A  25     -54.839 -57.649 -66.800  1.00 63.95           C  
ANISOU  189  C   VAL A  25    11350   6035   6911    995   1159    304       C  
ATOM    190  O   VAL A  25     -54.318 -58.773 -66.829  1.00 68.78           O  
ANISOU  190  O   VAL A  25    12037   6526   7571   1092   1267    324       O  
ATOM    191  CB  VAL A  25     -53.399 -55.564 -66.945  1.00 64.06           C  
ANISOU  191  CB  VAL A  25    11152   6312   6875   1028   1085    397       C  
ATOM    192  CG1 VAL A  25     -52.287 -56.337 -66.252  1.00 64.25           C  
ANISOU  192  CG1 VAL A  25    11108   6327   6979   1170   1153    499       C  
ATOM    193  CG2 VAL A  25     -52.820 -54.532 -67.901  1.00 66.22           C  
ANISOU  193  CG2 VAL A  25    11400   6678   7084   1000   1092    382       C  
ATOM    194  N   LEU A  26     -55.871 -57.368 -65.997  1.00 61.75           N  
ANISOU  194  N   LEU A  26    11046   5775   6639    893   1079    297       N  
ATOM    195  CA  LEU A  26     -56.408 -58.381 -65.093  1.00 62.70           C  
ANISOU  195  CA  LEU A  26    11236   5778   6809    866   1127    323       C  
ATOM    196  C   LEU A  26     -56.974 -59.571 -65.861  1.00 64.13           C  
ANISOU  196  C   LEU A  26    11571   5785   7010    818   1214    215       C  
ATOM    197  O   LEU A  26     -56.805 -60.722 -65.446  1.00 62.99           O  
ANISOU  197  O   LEU A  26    11539   5482   6911    860   1311    259       O  
ATOM    198  CB  LEU A  26     -57.481 -57.768 -64.193  1.00 63.59           C  
ANISOU  198  CB  LEU A  26    11282   5959   6918    743   1055    308       C  
ATOM    199  CG  LEU A  26     -57.079 -56.657 -63.218  1.00 64.52           C  
ANISOU  199  CG  LEU A  26    11282   6226   7008    765    977    396       C  
ATOM    200  CD1 LEU A  26     -58.310 -56.079 -62.531  1.00 63.63           C  
ANISOU  200  CD1 LEU A  26    11117   6163   6896    641    937    335       C  
ATOM    201  CD2 LEU A  26     -56.085 -57.168 -62.192  1.00 63.92           C  
ANISOU  201  CD2 LEU A  26    11220   6138   6929    869   1005    547       C  
ATOM    202  N   PHE A  27     -57.661 -59.312 -66.977  1.00 64.11           N  
ANISOU  202  N   PHE A  27    11595   5799   6967    725   1171     74       N  
ATOM    203  CA  PHE A  27     -58.172 -60.401 -67.805  1.00 60.64           C  
ANISOU  203  CA  PHE A  27    11311   5202   6528    657   1240    -55       C  
ATOM    204  C   PHE A  27     -57.036 -61.189 -68.441  1.00 64.88           C  
ANISOU  204  C   PHE A  27    11967   5623   7061    798   1373    -43       C  
ATOM    205  O   PHE A  27     -57.083 -62.427 -68.493  1.00 65.31           O  
ANISOU  205  O   PHE A  27    12175   5481   7159    802   1486    -81       O  
ATOM    206  CB  PHE A  27     -59.098 -59.849 -68.888  1.00 61.99           C  
ANISOU  206  CB  PHE A  27    11476   5446   6631    535   1126   -206       C  
ATOM    207  CG  PHE A  27     -60.524 -59.690 -68.451  1.00 61.32           C  
ANISOU  207  CG  PHE A  27    11304   5400   6593    375   1035   -284       C  
ATOM    208  CD1 PHE A  27     -61.170 -60.697 -67.756  1.00 61.41           C  
ANISOU  208  CD1 PHE A  27    11360   5287   6687    269   1121   -310       C  
ATOM    209  CD2 PHE A  27     -61.222 -58.529 -68.742  1.00 56.73           C  
ANISOU  209  CD2 PHE A  27    10597   4975   5985    333    873   -332       C  
ATOM    210  CE1 PHE A  27     -62.488 -60.548 -67.359  1.00 61.94           C  
ANISOU  210  CE1 PHE A  27    11315   5407   6814    107   1062   -397       C  
ATOM    211  CE2 PHE A  27     -62.537 -58.373 -68.345  1.00 56.52           C  
ANISOU  211  CE2 PHE A  27    10449   4998   6028    206    797   -417       C  
ATOM    212  CZ  PHE A  27     -63.170 -59.382 -67.654  1.00 59.04           C  
ANISOU  212  CZ  PHE A  27    10782   5215   6435     84    899   -456       C  
ATOM    213  N   HIS A  28     -56.013 -60.491 -68.943  1.00 66.29           N  
ANISOU  213  N   HIS A  28    12081   5912   7194    910   1378      0       N  
ATOM    214  CA  HIS A  28     -54.882 -61.189 -69.545  1.00 67.06           C  
ANISOU  214  CA  HIS A  28    12256   5920   7304   1060   1529      0       C  
ATOM    215  C   HIS A  28     -54.206 -62.112 -68.543  1.00 67.20           C  
ANISOU  215  C   HIS A  28    12280   5815   7436   1210   1615    122       C  
ATOM    216  O   HIS A  28     -53.817 -63.233 -68.887  1.00 67.01           O  
ANISOU  216  O   HIS A  28    12396   5606   7458   1306   1752     86       O  
ATOM    217  CB  HIS A  28     -53.870 -60.195 -70.105  1.00 67.40           C  
ANISOU  217  CB  HIS A  28    12189   6127   7293   1136   1538     37       C  
ATOM    218  CG  HIS A  28     -52.638 -60.845 -70.650  1.00 67.14           C  
ANISOU  218  CG  HIS A  28    12186   6031   7294   1302   1717     33       C  
ATOM    219  ND1 HIS A  28     -52.666 -61.715 -71.718  1.00 65.50           N  
ANISOU  219  ND1 HIS A  28    12169   5677   7041   1309   1853   -108       N  
ATOM    220  CD2 HIS A  28     -51.342 -60.766 -70.263  1.00 69.08           C  
ANISOU  220  CD2 HIS A  28    12281   6343   7622   1472   1788    140       C  
ATOM    221  CE1 HIS A  28     -51.441 -62.135 -71.974  1.00 68.82           C  
ANISOU  221  CE1 HIS A  28    12558   6070   7521   1489   2020    -89       C  
ATOM    222  NE2 HIS A  28     -50.618 -61.575 -71.105  1.00 70.92           N  
ANISOU  222  NE2 HIS A  28    12600   6472   7875   1594   1978     63       N  
ATOM    223  N   GLU A  29     -54.046 -61.659 -67.298  1.00 72.75           N  
ANISOU  223  N   GLU A  29    12853   6611   8178   1241   1530    268       N  
ATOM    224  CA  GLU A  29     -53.493 -62.545 -66.282  1.00 78.08           C  
ANISOU  224  CA  GLU A  29    13562   7168   8937   1384   1577    404       C  
ATOM    225  C   GLU A  29     -54.494 -63.603 -65.838  1.00 72.27           C  
ANISOU  225  C   GLU A  29    13018   6217   8224   1282   1623    381       C  
ATOM    226  O   GLU A  29     -54.084 -64.655 -65.336  1.00 71.73           O  
ANISOU  226  O   GLU A  29    13072   5964   8220   1406   1702    469       O  
ATOM    227  CB  GLU A  29     -53.003 -61.737 -65.081  1.00 88.25           C  
ANISOU  227  CB  GLU A  29    14675   8630  10226   1433   1458    563       C  
ATOM    228  CG  GLU A  29     -51.649 -61.082 -65.306  1.00 98.82           C  
ANISOU  228  CG  GLU A  29    15826  10133  11588   1579   1447    620       C  
ATOM    229  CD  GLU A  29     -50.842 -60.959 -64.029  1.00106.58           C  
ANISOU  229  CD  GLU A  29    16682  11207  12608   1703   1355    795       C  
ATOM    230  OE1 GLU A  29     -50.291 -59.867 -63.773  1.00108.57           O  
ANISOU  230  OE1 GLU A  29    16746  11668  12839   1686   1262    834       O  
ATOM    231  OE2 GLU A  29     -50.766 -61.955 -63.277  1.00112.69           O  
ANISOU  231  OE2 GLU A  29    17561  11836  13421   1808   1367    895       O  
ATOM    232  N   GLN A  30     -55.792 -63.350 -66.019  1.00 63.18           N  
ANISOU  232  N   GLN A  30    11895   5082   7031   1059   1576    266       N  
ATOM    233  CA  GLN A  30     -56.799 -64.356 -65.706  1.00 63.38           C  
ANISOU  233  CA  GLN A  30    12089   4908   7086    916   1641    217       C  
ATOM    234  C   GLN A  30     -56.755 -65.509 -66.699  1.00 71.85           C  
ANISOU  234  C   GLN A  30    13368   5747   8184    926   1772     93       C  
ATOM    235  O   GLN A  30     -57.023 -66.657 -66.328  1.00 76.03           O  
ANISOU  235  O   GLN A  30    14088   6034   8766    898   1875    106       O  
ATOM    236  CB  GLN A  30     -58.185 -63.713 -65.684  1.00 57.96           C  
ANISOU  236  CB  GLN A  30    11319   4333   6368    676   1553    107       C  
ATOM    237  CG  GLN A  30     -59.325 -64.661 -65.357  1.00 61.76           C  
ANISOU  237  CG  GLN A  30    11933   4640   6892    478   1629     36       C  
ATOM    238  CD  GLN A  30     -60.640 -63.933 -65.162  1.00 64.50           C  
ANISOU  238  CD  GLN A  30    12130   5140   7238    265   1541    -63       C  
ATOM    239  OE1 GLN A  30     -60.699 -62.902 -64.489  1.00 63.23           O  
ANISOU  239  OE1 GLN A  30    11804   5164   7056    282   1458      6       O  
ATOM    240  NE2 GLN A  30     -61.705 -64.462 -65.757  1.00 65.18           N  
ANISOU  240  NE2 GLN A  30    12263   5149   7354     63   1558   -237       N  
ATOM    241  N   ALA A  31     -56.418 -65.228 -67.958  1.00 78.77           N  
ANISOU  241  N   ALA A  31    14237   6679   9011    957   1781    -30       N  
ATOM    242  CA  ALA A  31     -56.224 -66.285 -68.942  1.00 84.33           C  
ANISOU  242  CA  ALA A  31    15152   7166   9722    987   1922   -162       C  
ATOM    243  C   ALA A  31     -54.816 -66.862 -68.906  1.00 93.66           C  
ANISOU  243  C   ALA A  31    16372   8239  10973   1271   2051    -66       C  
ATOM    244  O   ALA A  31     -54.619 -68.022 -69.286  1.00 96.85           O  
ANISOU  244  O   ALA A  31    16988   8385  11426   1337   2199   -132       O  
ATOM    245  CB  ALA A  31     -56.532 -65.764 -70.349  1.00 75.92           C  
ANISOU  245  CB  ALA A  31    14096   6209   8542    883   1882   -348       C  
ATOM    246  N   GLU A  32     -53.833 -66.078 -68.455  1.00100.38           N  
ANISOU  246  N   GLU A  32    17015   9281  11843   1441   1999     80       N  
ATOM    247  CA  GLU A  32     -52.474 -66.590 -68.318  1.00106.50           C  
ANISOU  247  CA  GLU A  32    17766   9986  12713   1729   2102    179       C  
ATOM    248  C   GLU A  32     -52.404 -67.672 -67.249  1.00108.01           C  
ANISOU  248  C   GLU A  32    18094   9943  13001   1842   2135    319       C  
ATOM    249  O   GLU A  32     -51.726 -68.691 -67.429  1.00110.56           O  
ANISOU  249  O   GLU A  32    18547  10046  13416   2046   2269    328       O  
ATOM    250  CB  GLU A  32     -51.513 -65.448 -67.990  1.00110.68           C  
ANISOU  250  CB  GLU A  32    18009  10798  13245   1845   2012    298       C  
ATOM    251  CG  GLU A  32     -50.053 -65.865 -67.890  1.00116.73           C  
ANISOU  251  CG  GLU A  32    18676  11546  14130   2147   2101    389       C  
ATOM    252  CD  GLU A  32     -49.416 -66.099 -69.247  1.00121.48           C  
ANISOU  252  CD  GLU A  32    19308  12113  14734   2234   2286    234       C  
ATOM    253  OE1 GLU A  32     -49.840 -65.444 -70.224  1.00122.29           O  
ANISOU  253  OE1 GLU A  32    19431  12320  14712   2060   2297     95       O  
ATOM    254  OE2 GLU A  32     -48.493 -66.936 -69.337  1.00123.95           O  
ANISOU  254  OE2 GLU A  32    19635  12293  15169   2486   2422    251       O  
ATOM    255  N   SER A  33     -53.098 -67.470 -66.131  1.00108.54           N  
ANISOU  255  N   SER A  33    18151  10043  13045   1719   2024    432       N  
ATOM    256  CA  SER A  33     -53.198 -68.488 -65.096  1.00105.52           C  
ANISOU  256  CA  SER A  33    17952   9423  12717   1781   2057    575       C  
ATOM    257  C   SER A  33     -54.149 -69.615 -65.471  1.00105.73           C  
ANISOU  257  C   SER A  33    18275   9138  12758   1615   2188    448       C  
ATOM    258  O   SER A  33     -54.306 -70.557 -64.686  1.00110.36           O  
ANISOU  258  O   SER A  33    19069   9479  13386   1639   2244    561       O  
ATOM    259  CB  SER A  33     -53.646 -67.853 -63.776  1.00 99.15           C  
ANISOU  259  CB  SER A  33    17055   8766  11849   1678   1918    728       C  
ATOM    260  OG  SER A  33     -54.948 -67.306 -63.889  1.00 94.26           O  
ANISOU  260  OG  SER A  33    16415   8238  11161   1375   1882    603       O  
ATOM    261  N   GLY A  34     -54.784 -69.541 -66.637  1.00104.26           N  
ANISOU  261  N   GLY A  34    18130   8955  12530   1436   2231    220       N  
ATOM    262  CA  GLY A  34     -55.670 -70.599 -67.088  1.00102.19           C  
ANISOU  262  CA  GLY A  34    18139   8408  12281   1250   2348     67       C  
ATOM    263  C   GLY A  34     -56.959 -70.706 -66.304  1.00 98.65           C  
ANISOU  263  C   GLY A  34    17744   7922  11816    964   2312     77       C  
ATOM    264  O   GLY A  34     -57.380 -71.816 -65.958  1.00 96.37           O  
ANISOU  264  O   GLY A  34    17709   7330  11575    881   2428     85       O  
ATOM    265  N   LEU A  35     -57.600 -69.576 -66.014  1.00 93.84           N  
ANISOU  265  N   LEU A  35    16906   7603  11146    809   2172     73       N  
ATOM    266  CA  LEU A  35     -58.841 -69.598 -65.253  1.00 92.03           C  
ANISOU  266  CA  LEU A  35    16684   7371  10911    537   2158     68       C  
ATOM    267  C   LEU A  35     -60.059 -69.552 -66.171  1.00 92.87           C  
ANISOU  267  C   LEU A  35    16772   7512  11004    244   2137   -186       C  
ATOM    268  O   LEU A  35     -61.004 -70.327 -65.990  1.00 96.68           O  
ANISOU  268  O   LEU A  35    17391   7817  11525      8   2220   -266       O  
ATOM    269  CB  LEU A  35     -58.863 -68.439 -64.252  1.00 87.48           C  
ANISOU  269  CB  LEU A  35    15872   7077  10289    551   2030    210       C  
ATOM    270  CG  LEU A  35     -59.618 -68.699 -62.944  1.00 88.46           C  
ANISOU  270  CG  LEU A  35    16061   7142  10407    391   2074    318       C  
ATOM    271  CD1 LEU A  35     -59.157 -70.002 -62.313  1.00 89.88           C  
ANISOU  271  CD1 LEU A  35    16542   6990  10619    492   2208    472       C  
ATOM    272  CD2 LEU A  35     -59.423 -67.543 -61.978  1.00 89.39           C  
ANISOU  272  CD2 LEU A  35    15971   7533  10461    448   1955    455       C  
ATOM    273  N   LEU A  36     -60.043 -68.655 -67.157  1.00 90.99           N  
ANISOU  273  N   LEU A  36    16369   7498  10706    250   2021   -309       N  
ATOM    274  CA  LEU A  36     -61.082 -68.583 -68.179  1.00 94.15           C  
ANISOU  274  CA  LEU A  36    16751   7950  11073     10   1959   -551       C  
ATOM    275  C   LEU A  36     -60.667 -67.627 -69.290  1.00101.36           C  
ANISOU  275  C   LEU A  36    17545   9080  11888    106   1839   -630       C  
ATOM    276  O   LEU A  36     -60.334 -66.467 -69.027  1.00 99.14           O  
ANISOU  276  O   LEU A  36    17058   9037  11573    209   1729   -527       O  
ATOM    277  CB  LEU A  36     -62.418 -68.144 -67.575  1.00 87.19           C  
ANISOU  277  CB  LEU A  36    15700   7205  10222   -246   1880   -597       C  
ATOM    278  CG  LEU A  36     -63.591 -68.040 -68.553  1.00 86.00           C  
ANISOU  278  CG  LEU A  36    15480   7138  10056   -498   1776   -847       C  
ATOM    279  CD1 LEU A  36     -63.701 -69.294 -69.406  1.00 88.91           C  
ANISOU  279  CD1 LEU A  36    16120   7238  10426   -614   1881  -1017       C  
ATOM    280  CD2 LEU A  36     -64.887 -67.794 -67.803  1.00 85.31           C  
ANISOU  280  CD2 LEU A  36    15210   7159  10044   -741   1741   -888       C  
ATOM    281  N   LYS A  37     -60.681 -68.104 -70.533  1.00111.28           N  
ANISOU  281  N   LYS A  37    18955  10244  13084     59   1868   -814       N  
ATOM    282  CA  LYS A  37     -60.282 -67.281 -71.670  1.00111.29           C  
ANISOU  282  CA  LYS A  37    18900  10428  12958    133   1776   -889       C  
ATOM    283  C   LYS A  37     -61.328 -66.203 -71.922  1.00107.72           C  
ANISOU  283  C   LYS A  37    18245  10235  12448    -31   1556   -962       C  
ATOM    284  O   LYS A  37     -62.477 -66.507 -72.261  1.00111.42           O  
ANISOU  284  O   LYS A  37    18725  10692  12919   -264   1480  -1128       O  
ATOM    285  CB  LYS A  37     -60.097 -68.151 -72.911  1.00117.14           C  
ANISOU  285  CB  LYS A  37    19897  10989  13623    104   1876  -1082       C  
ATOM    286  CG  LYS A  37     -59.549 -67.406 -74.115  1.00120.44           C  
ANISOU  286  CG  LYS A  37    20313  11570  13877    189   1825  -1151       C  
ATOM    287  CD  LYS A  37     -58.150 -66.878 -73.843  1.00120.37           C  
ANISOU  287  CD  LYS A  37    20210  11639  13885    470   1912   -970       C  
ATOM    288  CE  LYS A  37     -57.585 -66.160 -75.056  1.00120.88           C  
ANISOU  288  CE  LYS A  37    20295  11854  13779    528   1902  -1036       C  
ATOM    289  NZ  LYS A  37     -56.220 -65.628 -74.792  1.00120.67           N  
ANISOU  289  NZ  LYS A  37    20143  11919  13788    772   2000   -873       N  
ATOM    290  N   GLU A  38     -60.933 -64.945 -71.759  1.00 97.31           N  
ANISOU  290  N   GLU A  38    16739   9147  11090     91   1449   -843       N  
ATOM    291  CA  GLU A  38     -61.819 -63.808 -71.956  1.00 93.42           C  
ANISOU  291  CA  GLU A  38    16055   8889  10553     -8   1235   -886       C  
ATOM    292  C   GLU A  38     -61.449 -63.088 -73.245  1.00 83.89           C  
ANISOU  292  C   GLU A  38    14893   7802   9178     50   1140   -944       C  
ATOM    293  O   GLU A  38     -60.266 -62.844 -73.507  1.00 79.78           O  
ANISOU  293  O   GLU A  38    14425   7288   8600    221   1232   -856       O  
ATOM    294  CB  GLU A  38     -61.742 -62.844 -70.771  1.00 95.15           C  
ANISOU  294  CB  GLU A  38    16054   9257  10841     71   1184   -712       C  
ATOM    295  CG  GLU A  38     -63.014 -62.777 -69.943  1.00 97.93           C  
ANISOU  295  CG  GLU A  38    16255   9659  11296   -101   1123   -749       C  
ATOM    296  CD  GLU A  38     -64.199 -62.257 -70.733  1.00 98.25           C  
ANISOU  296  CD  GLU A  38    16183   9841  11308   -247    928   -916       C  
ATOM    297  OE1 GLU A  38     -64.949 -63.081 -71.297  1.00100.22           O  
ANISOU  297  OE1 GLU A  38    16508  10006  11566   -425    918  -1086       O  
ATOM    298  OE2 GLU A  38     -64.376 -61.021 -70.795  1.00 95.94           O  
ANISOU  298  OE2 GLU A  38    15729   9739  10986   -183    773   -879       O  
ATOM    299  N   ASP A  39     -62.459 -62.754 -74.045  1.00 81.62           N  
ANISOU  299  N   ASP A  39    14585   7617   8811    -97    955  -1089       N  
ATOM    300  CA  ASP A  39     -62.246 -62.006 -75.277  1.00 80.97           C  
ANISOU  300  CA  ASP A  39    14575   7655   8536    -59    836  -1134       C  
ATOM    301  C   ASP A  39     -62.144 -60.521 -74.950  1.00 74.12           C  
ANISOU  301  C   ASP A  39    13519   6985   7657     44    700   -987       C  
ATOM    302  O   ASP A  39     -63.106 -59.919 -74.461  1.00 72.41           O  
ANISOU  302  O   ASP A  39    13112   6880   7519    -15    539   -987       O  
ATOM    303  CB  ASP A  39     -63.379 -62.270 -76.265  1.00 88.21           C  
ANISOU  303  CB  ASP A  39    15560   8601   9356   -251    659  -1343       C  
ATOM    304  CG  ASP A  39     -63.180 -61.553 -77.587  1.00 92.55           C  
ANISOU  304  CG  ASP A  39    16237   9264   9663   -218    524  -1382       C  
ATOM    305  OD1 ASP A  39     -62.016 -61.295 -77.959  1.00 94.44           O  
ANISOU  305  OD1 ASP A  39    16598   9487   9797    -77    661  -1296       O  
ATOM    306  OD2 ASP A  39     -64.191 -61.248 -78.256  1.00 93.45           O  
ANISOU  306  OD2 ASP A  39    16329   9489   9690   -335    281  -1497       O  
ATOM    307  N   LEU A  40     -60.981 -59.933 -75.221  1.00 70.64           N  
ANISOU  307  N   LEU A  40    13130   6580   7129    193    779   -873       N  
ATOM    308  CA  LEU A  40     -60.712 -58.542 -74.882  1.00 68.04           C  
ANISOU  308  CA  LEU A  40    12657   6403   6792    286    684   -727       C  
ATOM    309  C   LEU A  40     -61.258 -57.557 -75.908  1.00 68.68           C  
ANISOU  309  C   LEU A  40    12781   6607   6709    254    468   -764       C  
ATOM    310  O   LEU A  40     -61.088 -56.346 -75.725  1.00 68.10           O  
ANISOU  310  O   LEU A  40    12622   6635   6619    326    381   -648       O  
ATOM    311  CB  LEU A  40     -59.205 -58.335 -74.721  1.00 65.74           C  
ANISOU  311  CB  LEU A  40    12389   6101   6490    434    868   -593       C  
ATOM    312  CG  LEU A  40     -58.515 -59.367 -73.827  1.00 62.30           C  
ANISOU  312  CG  LEU A  40    11936   5534   6200    506   1068   -543       C  
ATOM    313  CD1 LEU A  40     -57.011 -59.152 -73.794  1.00 62.94           C  
ANISOU  313  CD1 LEU A  40    12003   5632   6277    662   1228   -428       C  
ATOM    314  CD2 LEU A  40     -59.098 -59.314 -72.427  1.00 62.27           C  
ANISOU  314  CD2 LEU A  40    11760   5544   6356    482   1017   -470       C  
ATOM    315  N   THR A  41     -61.909 -58.040 -76.966  1.00 72.03           N  
ANISOU  315  N   THR A  41    13351   7016   7003    148    368   -922       N  
ATOM    316  CA  THR A  41     -62.361 -57.156 -78.039  1.00 73.14           C  
ANISOU  316  CA  THR A  41    13576   7267   6948    133    144   -945       C  
ATOM    317  C   THR A  41     -63.326 -56.071 -77.574  1.00 76.11           C  
ANISOU  317  C   THR A  41    13737   7770   7410    154   -103   -892       C  
ATOM    318  O   THR A  41     -63.139 -54.908 -77.971  1.00 78.83           O  
ANISOU  318  O   THR A  41    14119   8188   7644    236   -217   -789       O  
ATOM    319  CB  THR A  41     -62.969 -57.995 -79.170  1.00 75.71           C  
ANISOU  319  CB  THR A  41    14093   7559   7117     -3     59  -1143       C  
ATOM    320  OG1 THR A  41     -61.964 -58.853 -79.725  1.00 76.28           O  
ANISOU  320  OG1 THR A  41    14398   7504   7081      5    308  -1193       O  
ATOM    321  CG2 THR A  41     -63.523 -57.096 -80.268  1.00 78.01           C  
ANISOU  321  CG2 THR A  41    14482   7974   7183    -14   -218  -1157       C  
ATOM    322  N   PRO A  42     -64.359 -56.351 -76.767  1.00 79.88           N  
ANISOU  322  N   PRO A  42    13997   8272   8083     87   -183   -959       N  
ATOM    323  CA  PRO A  42     -65.264 -55.254 -76.369  1.00 80.39           C  
ANISOU  323  CA  PRO A  42    13845   8461   8238    135   -405   -922       C  
ATOM    324  C   PRO A  42     -64.577 -54.159 -75.568  1.00 77.52           C  
ANISOU  324  C   PRO A  42    13402   8117   7935    275   -338   -741       C  
ATOM    325  O   PRO A  42     -64.774 -52.968 -75.851  1.00 78.60           O  
ANISOU  325  O   PRO A  42    13526   8321   8017    363   -507   -670       O  
ATOM    326  CB  PRO A  42     -66.346 -55.978 -75.552  1.00 82.66           C  
ANISOU  326  CB  PRO A  42    13909   8756   8741     15   -413  -1043       C  
ATOM    327  CG  PRO A  42     -65.700 -57.238 -75.091  1.00 83.21           C  
ANISOU  327  CG  PRO A  42    14077   8678   8863    -55   -141  -1061       C  
ATOM    328  CD  PRO A  42     -64.808 -57.645 -76.217  1.00 82.84           C  
ANISOU  328  CD  PRO A  42    14318   8556   8604    -41    -69  -1078       C  
ATOM    329  N   LEU A  43     -63.769 -54.531 -74.573  1.00 75.15           N  
ANISOU  329  N   LEU A  43    13061   7752   7743    298   -105   -664       N  
ATOM    330  CA  LEU A  43     -63.077 -53.534 -73.761  1.00 72.68           C  
ANISOU  330  CA  LEU A  43    12671   7462   7482    406    -45   -508       C  
ATOM    331  C   LEU A  43     -62.128 -52.694 -74.609  1.00 69.55           C  
ANISOU  331  C   LEU A  43    12447   7071   6906    477    -46   -407       C  
ATOM    332  O   LEU A  43     -62.051 -51.467 -74.448  1.00 75.13           O  
ANISOU  332  O   LEU A  43    13122   7817   7606    546   -129   -311       O  
ATOM    333  CB  LEU A  43     -62.321 -54.231 -72.630  1.00 74.31           C  
ANISOU  333  CB  LEU A  43    12824   7604   7806    411    185   -449       C  
ATOM    334  CG  LEU A  43     -62.357 -53.599 -71.239  1.00 78.29           C  
ANISOU  334  CG  LEU A  43    13149   8149   8450    452    212   -364       C  
ATOM    335  CD1 LEU A  43     -63.789 -53.324 -70.813  1.00 78.74           C  
ANISOU  335  CD1 LEU A  43    13029   8266   8621    406     76   -455       C  
ATOM    336  CD2 LEU A  43     -61.668 -54.510 -70.235  1.00 80.14           C  
ANISOU  336  CD2 LEU A  43    13372   8313   8764    449    413   -309       C  
ATOM    337  N   VAL A  44     -61.405 -53.341 -75.527  1.00 64.99           N  
ANISOU  337  N   VAL A  44    12069   6444   6180    452     65   -433       N  
ATOM    338  CA  VAL A  44     -60.501 -52.618 -76.415  1.00 65.02           C  
ANISOU  338  CA  VAL A  44    12255   6455   5995    491    101   -347       C  
ATOM    339  C   VAL A  44     -61.283 -51.681 -77.326  1.00 67.35           C  
ANISOU  339  C   VAL A  44    12650   6801   6140    497   -156   -346       C  
ATOM    340  O   VAL A  44     -60.833 -50.570 -77.631  1.00 70.08           O  
ANISOU  340  O   VAL A  44    13085   7155   6386    544   -186   -227       O  
ATOM    341  CB  VAL A  44     -59.640 -53.612 -77.217  1.00 65.78           C  
ANISOU  341  CB  VAL A  44    12540   6489   5966    462    300   -405       C  
ATOM    342  CG1 VAL A  44     -58.900 -52.901 -78.335  1.00 63.55           C  
ANISOU  342  CG1 VAL A  44    12472   6224   5449    470    336   -344       C  
ATOM    343  CG2 VAL A  44     -58.658 -54.320 -76.294  1.00 64.26           C  
ANISOU  343  CG2 VAL A  44    12245   6243   5928    509    546   -363       C  
ATOM    344  N   GLN A  45     -62.468 -52.105 -77.769  1.00 67.78           N  
ANISOU  344  N   GLN A  45    12693   6885   6177    446   -353   -474       N  
ATOM    345  CA  GLN A  45     -63.313 -51.221 -78.566  1.00 70.37           C  
ANISOU  345  CA  GLN A  45    13087   7271   6379    478   -645   -468       C  
ATOM    346  C   GLN A  45     -63.749 -50.003 -77.761  1.00 70.83           C  
ANISOU  346  C   GLN A  45    12966   7358   6587    584   -771   -370       C  
ATOM    347  O   GLN A  45     -63.782 -48.884 -78.284  1.00 70.19           O  
ANISOU  347  O   GLN A  45    13003   7277   6390    661   -918   -270       O  
ATOM    348  CB  GLN A  45     -64.532 -51.981 -79.088  1.00 74.21           C  
ANISOU  348  CB  GLN A  45    13539   7807   6851    396   -850   -643       C  
ATOM    349  CG  GLN A  45     -64.248 -52.860 -80.294  1.00 81.82           C  
ANISOU  349  CG  GLN A  45    14773   8741   7572    296   -811   -747       C  
ATOM    350  CD  GLN A  45     -65.494 -53.548 -80.818  1.00 89.49           C  
ANISOU  350  CD  GLN A  45    15706   9772   8525    189  -1047   -935       C  
ATOM    351  OE1 GLN A  45     -66.455 -53.765 -80.078  1.00 90.92           O  
ANISOU  351  OE1 GLN A  45    15612   9999   8933    158  -1145  -1013       O  
ATOM    352  NE2 GLN A  45     -65.486 -53.891 -82.102  1.00 93.02           N  
ANISOU  352  NE2 GLN A  45    16426  10224   8692    117  -1133  -1017       N  
ATOM    353  N   GLY A  46     -64.087 -50.201 -76.485  1.00 73.33           N  
ANISOU  353  N   GLY A  46    13023   7686   7153    589   -704   -397       N  
ATOM    354  CA  GLY A  46     -64.464 -49.071 -75.651  1.00 75.92           C  
ANISOU  354  CA  GLY A  46    13188   8032   7627    689   -787   -325       C  
ATOM    355  C   GLY A  46     -63.332 -48.076 -75.479  1.00 76.69           C  
ANISOU  355  C   GLY A  46    13403   8072   7663    745   -671   -164       C  
ATOM    356  O   GLY A  46     -63.508 -46.869 -75.687  1.00 84.05           O  
ANISOU  356  O   GLY A  46    14396   8983   8558    832   -810    -80       O  
ATOM    357  N   VAL A  47     -62.148 -48.573 -75.107  1.00 70.66           N  
ANISOU  357  N   VAL A  47    12674   7277   6895    695   -418   -120       N  
ATOM    358  CA  VAL A  47     -60.993 -47.690 -74.958  1.00 68.45           C  
ANISOU  358  CA  VAL A  47    12482   6960   6565    715   -295     18       C  
ATOM    359  C   VAL A  47     -60.689 -46.977 -76.271  1.00 71.29           C  
ANISOU  359  C   VAL A  47    13109   7288   6690    719   -369     92       C  
ATOM    360  O   VAL A  47     -60.422 -45.769 -76.292  1.00 72.95           O  
ANISOU  360  O   VAL A  47    13402   7453   6863    755   -408    203       O  
ATOM    361  CB  VAL A  47     -59.775 -48.481 -74.448  1.00 62.54           C  
ANISOU  361  CB  VAL A  47    11698   6208   5857    668    -30     39       C  
ATOM    362  CG1 VAL A  47     -58.537 -47.602 -74.457  1.00 61.53           C  
ANISOU  362  CG1 VAL A  47    11645   6064   5670    661     94    165       C  
ATOM    363  CG2 VAL A  47     -60.043 -49.011 -73.054  1.00 62.60           C  
ANISOU  363  CG2 VAL A  47    11480   6235   6072    670     29      2       C  
ATOM    364  N   GLY A  48     -60.742 -47.708 -77.386  1.00 70.94           N  
ANISOU  364  N   GLY A  48    13231   7253   6469    672   -384     31       N  
ATOM    365  CA  GLY A  48     -60.456 -47.101 -78.674  1.00 73.72           C  
ANISOU  365  CA  GLY A  48    13878   7577   6556    662   -442    103       C  
ATOM    366  C   GLY A  48     -61.466 -46.045 -79.075  1.00 76.52           C  
ANISOU  366  C   GLY A  48    14303   7917   6853    749   -747    154       C  
ATOM    367  O   GLY A  48     -61.117 -45.073 -79.749  1.00 83.19           O  
ANISOU  367  O   GLY A  48    15383   8703   7524    765   -787    279       O  
ATOM    368  N   ILE A  49     -62.726 -46.215 -78.672  1.00 75.14           N  
ANISOU  368  N   ILE A  49    13927   7792   6832    809   -960     60       N  
ATOM    369  CA  ILE A  49     -63.739 -45.217 -78.993  1.00 74.87           C  
ANISOU  369  CA  ILE A  49    13914   7749   6782    931  -1269    102       C  
ATOM    370  C   ILE A  49     -63.559 -43.977 -78.125  1.00 72.18           C  
ANISOU  370  C   ILE A  49    13507   7330   6588   1024  -1246    214       C  
ATOM    371  O   ILE A  49     -63.716 -42.845 -78.601  1.00 75.21           O  
ANISOU  371  O   ILE A  49    14065   7634   6877   1117  -1401    329       O  
ATOM    372  CB  ILE A  49     -65.149 -45.822 -78.859  1.00 75.53           C  
ANISOU  372  CB  ILE A  49    13761   7932   7006    962  -1496    -55       C  
ATOM    373  CG1 ILE A  49     -65.509 -46.596 -80.130  1.00 76.96           C  
ANISOU  373  CG1 ILE A  49    14114   8172   6957    889  -1642   -142       C  
ATOM    374  CG2 ILE A  49     -66.186 -44.744 -78.575  1.00 77.07           C  
ANISOU  374  CG2 ILE A  49    13822   8126   7335   1131  -1760    -25       C  
ATOM    375  CD1 ILE A  49     -66.946 -47.070 -80.177  1.00 79.64           C  
ANISOU  375  CD1 ILE A  49    14226   8621   7412    903  -1915   -299       C  
ATOM    376  N   ALA A  50     -63.213 -44.163 -76.847  1.00 66.22           N  
ANISOU  376  N   ALA A  50    12528   6582   6051    997  -1054    184       N  
ATOM    377  CA  ALA A  50     -62.891 -43.010 -76.009  1.00 63.95           C  
ANISOU  377  CA  ALA A  50    12208   6213   5878   1055  -1002    275       C  
ATOM    378  C   ALA A  50     -61.705 -42.236 -76.575  1.00 65.33           C  
ANISOU  378  C   ALA A  50    12663   6289   5869    998   -881    426       C  
ATOM    379  O   ALA A  50     -61.730 -40.997 -76.638  1.00 69.45           O  
ANISOU  379  O   ALA A  50    13318   6700   6371   1065   -964    530       O  
ATOM    380  CB  ALA A  50     -62.603 -43.462 -74.577  1.00 61.76           C  
ANISOU  380  CB  ALA A  50    11676   5975   5817   1009   -807    213       C  
ATOM    381  N   VAL A  51     -60.663 -42.953 -77.006  1.00 61.27           N  
ANISOU  381  N   VAL A  51    12246   5808   5228    873   -672    435       N  
ATOM    382  CA  VAL A  51     -59.511 -42.305 -77.627  1.00 61.87           C  
ANISOU  382  CA  VAL A  51    12573   5811   5125    790   -524    565       C  
ATOM    383  C   VAL A  51     -59.932 -41.564 -78.889  1.00 61.96           C  
ANISOU  383  C   VAL A  51    12902   5744   4896    835   -716    659       C  
ATOM    384  O   VAL A  51     -59.536 -40.414 -79.113  1.00 65.75           O  
ANISOU  384  O   VAL A  51    13585   6103   5294    829   -709    794       O  
ATOM    385  CB  VAL A  51     -58.410 -43.340 -77.923  1.00 62.51           C  
ANISOU  385  CB  VAL A  51    12666   5960   5127    668   -259    530       C  
ATOM    386  CG1 VAL A  51     -57.322 -42.728 -78.795  1.00 62.15           C  
ANISOU  386  CG1 VAL A  51    12890   5857   4868    568    -98    648       C  
ATOM    387  CG2 VAL A  51     -57.823 -43.881 -76.624  1.00 60.05           C  
ANISOU  387  CG2 VAL A  51    12069   5705   5044    640    -77    481       C  
ATOM    388  N   THR A  52     -60.751 -42.206 -79.725  1.00 65.80           N  
ANISOU  388  N   THR A  52    13452   6291   5257    874   -901    590       N  
ATOM    389  CA  THR A  52     -61.162 -41.594 -80.986  1.00 73.29           C  
ANISOU  389  CA  THR A  52    14728   7182   5938    921  -1114    684       C  
ATOM    390  C   THR A  52     -61.965 -40.320 -80.751  1.00 75.75           C  
ANISOU  390  C   THR A  52    15063   7385   6333   1085  -1367    777       C  
ATOM    391  O   THR A  52     -61.781 -39.322 -81.456  1.00 74.95           O  
ANISOU  391  O   THR A  52    15280   7155   6043   1111  -1439    935       O  
ATOM    392  CB  THR A  52     -61.973 -42.594 -81.813  1.00 74.66           C  
ANISOU  392  CB  THR A  52    14925   7463   5978    926  -1299    563       C  
ATOM    393  OG1 THR A  52     -61.176 -43.758 -82.067  1.00 74.35           O  
ANISOU  393  OG1 THR A  52    14902   7490   5857    783  -1040    471       O  
ATOM    394  CG2 THR A  52     -62.399 -41.981 -83.140  1.00 70.51           C  
ANISOU  394  CG2 THR A  52    14759   6892   5140    977  -1552    667       C  
ATOM    395  N   ASN A  53     -62.852 -40.329 -79.755  1.00 81.82           N  
ANISOU  395  N   ASN A  53    15511   8191   7385   1201  -1487    683       N  
ATOM    396  CA  ASN A  53     -63.690 -39.159 -79.515  1.00 88.73           C  
ANISOU  396  CA  ASN A  53    16384   8961   8368   1390  -1724    749       C  
ATOM    397  C   ASN A  53     -62.897 -38.034 -78.860  1.00 86.12           C  
ANISOU  397  C   ASN A  53    16146   8464   8110   1372  -1552    863       C  
ATOM    398  O   ASN A  53     -63.137 -36.854 -79.144  1.00 89.47           O  
ANISOU  398  O   ASN A  53    16781   8724   8490   1487  -1695    990       O  
ATOM    399  CB  ASN A  53     -64.900 -39.545 -78.668  1.00 95.57           C  
ANISOU  399  CB  ASN A  53    16861   9931   9520   1513  -1874    590       C  
ATOM    400  CG  ASN A  53     -65.856 -40.452 -79.415  1.00105.23           C  
ANISOU  400  CG  ASN A  53    18006  11303  10675   1535  -2108    480       C  
ATOM    401  OD1 ASN A  53     -66.084 -40.286 -80.613  1.00112.39           O  
ANISOU  401  OD1 ASN A  53    19170  12199  11332   1571  -2318    550       O  
ATOM    402  ND2 ASN A  53     -66.412 -41.428 -78.711  1.00106.53           N  
ANISOU  402  ND2 ASN A  53    17830  11604  11045   1496  -2072    304       N  
ATOM    403  N   LEU A  54     -61.946 -38.371 -77.983  1.00 79.81           N  
ANISOU  403  N   LEU A  54    15203   7699   7424   1227  -1256    821       N  
ATOM    404  CA  LEU A  54     -61.067 -37.337 -77.444  1.00 75.98           C  
ANISOU  404  CA  LEU A  54    14822   7067   6979   1161  -1086    919       C  
ATOM    405  C   LEU A  54     -60.224 -36.712 -78.552  1.00 76.61           C  
ANISOU  405  C   LEU A  54    15301   7026   6781   1057  -1014   1087       C  
ATOM    406  O   LEU A  54     -60.026 -35.489 -78.584  1.00 67.18           O  
ANISOU  406  O   LEU A  54    14325   5640   5561   1072  -1027   1211       O  
ATOM    407  CB  LEU A  54     -60.183 -37.922 -76.343  1.00 70.70           C  
ANISOU  407  CB  LEU A  54    13906   6491   6464   1019   -812    837       C  
ATOM    408  CG  LEU A  54     -59.464 -36.908 -75.448  1.00 69.63           C  
ANISOU  408  CG  LEU A  54    13781   6237   6439    952   -670    885       C  
ATOM    409  CD1 LEU A  54     -60.458 -35.945 -74.811  1.00 66.97           C  
ANISOU  409  CD1 LEU A  54    13405   5775   6265   1127   -847    866       C  
ATOM    410  CD2 LEU A  54     -58.646 -37.619 -74.380  1.00 65.40           C  
ANISOU  410  CD2 LEU A  54    12983   5830   6038    823   -445    800       C  
ATOM    411  N   VAL A  55     -59.733 -37.540 -79.480  1.00 71.13           N  
ANISOU  411  N   VAL A  55    14727   6429   5871    944   -922   1088       N  
ATOM    412  CA  VAL A  55     -59.022 -37.030 -80.649  1.00 73.29           C  
ANISOU  412  CA  VAL A  55    15403   6604   5842    838   -844   1240       C  
ATOM    413  C   VAL A  55     -59.946 -36.177 -81.509  1.00 79.52           C  
ANISOU  413  C   VAL A  55    16494   7255   6464    998  -1159   1364       C  
ATOM    414  O   VAL A  55     -59.496 -35.241 -82.179  1.00 81.39           O  
ANISOU  414  O   VAL A  55    17101   7322   6501    945  -1128   1536       O  
ATOM    415  CB  VAL A  55     -58.411 -38.204 -81.446  1.00 73.23           C  
ANISOU  415  CB  VAL A  55    15444   6742   5638    702   -674   1181       C  
ATOM    416  CG1 VAL A  55     -57.943 -37.755 -82.826  1.00 76.45           C  
ANISOU  416  CG1 VAL A  55    16303   7064   5681    610   -631   1326       C  
ATOM    417  CG2 VAL A  55     -57.253 -38.814 -80.678  1.00 70.71           C  
ANISOU  417  CG2 VAL A  55    14881   6516   5467    551   -337   1105       C  
ATOM    418  N   GLN A  56     -61.249 -36.465 -81.489  1.00 83.43           N  
ANISOU  418  N   GLN A  56    16836   7817   7046   1195  -1470   1285       N  
ATOM    419  CA  GLN A  56     -62.195 -35.671 -82.266  1.00 85.07           C  
ANISOU  419  CA  GLN A  56    17293   7910   7120   1388  -1816   1402       C  
ATOM    420  C   GLN A  56     -62.382 -34.289 -81.649  1.00 86.03           C  
ANISOU  420  C   GLN A  56    17480   7805   7405   1519  -1879   1507       C  
ATOM    421  O   GLN A  56     -62.242 -33.268 -82.334  1.00 87.43           O  
ANISOU  421  O   GLN A  56    17995   7800   7426   1538  -1936   1669       O  
ATOM    422  CB  GLN A  56     -63.535 -36.402 -82.361  1.00 85.11           C  
ANISOU  422  CB  GLN A  56    17051   8079   7210   1556  -2134   1265       C  
ATOM    423  CG  GLN A  56     -64.318 -36.141 -83.638  1.00 88.70           C  
ANISOU  423  CG  GLN A  56    17797   8514   7393   1690  -2495   1364       C  
ATOM    424  CD  GLN A  56     -63.738 -36.861 -84.844  1.00 91.95           C  
ANISOU  424  CD  GLN A  56    18505   9007   7425   1510  -2416   1385       C  
ATOM    425  OE1 GLN A  56     -62.840 -37.694 -84.713  1.00 94.03           O  
ANISOU  425  OE1 GLN A  56    18701   9360   7665   1305  -2095   1297       O  
ATOM    426  NE2 GLN A  56     -64.253 -36.545 -86.028  1.00 92.52           N  
ANISOU  426  NE2 GLN A  56    18842   9066   7247   1580  -2682   1467       N  
ATOM    427  N   VAL A  57     -62.695 -34.236 -80.350  1.00 88.86           N  
ANISOU  427  N   VAL A  57    17480   8182   8101   1589  -1838   1383       N  
ATOM    428  CA  VAL A  57     -62.969 -32.948 -79.722  1.00 89.44           C  
ANISOU  428  CA  VAL A  57    17609   8030   8343   1732  -1900   1450       C  
ATOM    429  C   VAL A  57     -61.695 -32.121 -79.614  1.00 91.71           C  
ANISOU  429  C   VAL A  57    18167   8127   8551   1530  -1621   1574       C  
ATOM    430  O   VAL A  57     -61.749 -30.885 -79.561  1.00 97.25           O  
ANISOU  430  O   VAL A  57    19063   8596   9289   1599  -1662   1671       O  
ATOM    431  CB  VAL A  57     -63.643 -33.146 -78.349  1.00 87.09           C  
ANISOU  431  CB  VAL A  57    16868   7816   8408   1845  -1904   1264       C  
ATOM    432  CG1 VAL A  57     -64.845 -34.059 -78.480  1.00 87.99           C  
ANISOU  432  CG1 VAL A  57    16688   8139   8605   1993  -2144   1128       C  
ATOM    433  CG2 VAL A  57     -62.654 -33.682 -77.329  1.00 88.19           C  
ANISOU  433  CG2 VAL A  57    16791   8051   8666   1619  -1565   1162       C  
ATOM    434  N   ALA A  58     -60.532 -32.773 -79.581  1.00 93.70           N  
ANISOU  434  N   ALA A  58    18382   8496   8725   1266  -1318   1544       N  
ATOM    435  CA  ALA A  58     -59.281 -32.025 -79.574  1.00 96.43           C  
ANISOU  435  CA  ALA A  58    18962   8687   8989   1042  -1048   1655       C  
ATOM    436  C   ALA A  58     -58.912 -31.549 -80.977  1.00104.00           C  
ANISOU  436  C   ALA A  58    20252   9589   9673    943  -1030   1778       C  
ATOM    437  O   ALA A  58     -58.457 -30.412 -81.154  1.00104.36           O  
ANISOU  437  O   ALA A  58    20493   9458   9702    856   -943   1864       O  
ATOM    438  CB  ALA A  58     -58.166 -32.881 -78.977  1.00 87.94           C  
ANISOU  438  CB  ALA A  58    17624   7801   7987    805   -728   1544       C  
ATOM    439  N   ALA A  59     -59.116 -32.401 -81.984  1.00110.49           N  
ANISOU  439  N   ALA A  59    21141  10561  10280    946  -1106   1772       N  
ATOM    440  CA  ALA A  59     -58.821 -32.036 -83.364  1.00116.08           C  
ANISOU  440  CA  ALA A  59    22157  11234  10715    852  -1090   1869       C  
ATOM    441  C   ALA A  59     -59.761 -30.962 -83.894  1.00123.01           C  
ANISOU  441  C   ALA A  59    23224  11947  11567   1053  -1388   1967       C  
ATOM    442  O   ALA A  59     -59.400 -30.254 -84.841  1.00129.40           O  
ANISOU  442  O   ALA A  59    24330  12649  12186    963  -1343   2080       O  
ATOM    443  CB  ALA A  59     -58.886 -33.273 -84.262  1.00114.61           C  
ANISOU  443  CB  ALA A  59    21994  11249  10305    814  -1110   1812       C  
ATOM    444  N   SER A  60     -60.954 -30.823 -83.311  1.00117.94           N  
ANISOU  444  N   SER A  60    22414  11281  11115   1327  -1683   1928       N  
ATOM    445  CA  SER A  60     -61.847 -29.739 -83.699  1.00117.36           C  
ANISOU  445  CA  SER A  60    22487  11043  11060   1548  -1961   2019       C  
ATOM    446  C   SER A  60     -61.353 -28.376 -83.234  1.00119.55           C  
ANISOU  446  C   SER A  60    22903  11069  11452   1496  -1814   2097       C  
ATOM    447  O   SER A  60     -61.951 -27.360 -83.606  1.00125.24           O  
ANISOU  447  O   SER A  60    23793  11619  12174   1662  -2003   2191       O  
ATOM    448  CB  SER A  60     -63.253 -29.991 -83.148  1.00109.27           C  
ANISOU  448  CB  SER A  60    21196  10077  10244   1867  -2302   1936       C  
ATOM    449  OG  SER A  60     -63.246 -30.031 -81.731  1.00101.64           O  
ANISOU  449  OG  SER A  60    19964   9086   9570   1906  -2196   1836       O  
ATOM    450  N   MET A  61     -60.282 -28.326 -82.441  1.00117.67           N  
ANISOU  450  N   MET A  61    22600  10803  11307   1270  -1490   2058       N  
ATOM    451  CA  MET A  61     -59.763 -27.074 -81.909  1.00119.26           C  
ANISOU  451  CA  MET A  61    22923  10769  11623   1187  -1341   2108       C  
ATOM    452  C   MET A  61     -58.501 -26.592 -82.611  1.00125.54           C  
ANISOU  452  C   MET A  61    23994  11486  12218    878  -1059   2205       C  
ATOM    453  O   MET A  61     -58.034 -25.488 -82.311  1.00128.01           O  
ANISOU  453  O   MET A  61    24454  11588  12594    780   -936   2256       O  
ATOM    454  CB  MET A  61     -59.477 -27.214 -80.410  1.00114.08           C  
ANISOU  454  CB  MET A  61    21995  10115  11234   1143  -1193   1985       C  
ATOM    455  CG  MET A  61     -60.669 -27.661 -79.591  1.00113.66           C  
ANISOU  455  CG  MET A  61    21657  10127  11403   1434  -1427   1874       C  
ATOM    456  SD  MET A  61     -60.306 -27.665 -77.827  1.00113.85           S  
ANISOU  456  SD  MET A  61    21422  10115  11723   1371  -1238   1733       S  
ATOM    457  CE  MET A  61     -58.921 -28.797 -77.758  1.00111.21           C  
ANISOU  457  CE  MET A  61    21001   9985  11268   1032   -924   1708       C  
ATOM    458  N   VAL A  62     -57.937 -27.382 -83.529  1.00130.07           N  
ANISOU  458  N   VAL A  62    24644  12220  12557    716   -941   2222       N  
ATOM    459  CA  VAL A  62     -56.737 -26.956 -84.240  1.00133.82           C  
ANISOU  459  CA  VAL A  62    25368  12632  12845    420   -654   2305       C  
ATOM    460  C   VAL A  62     -57.014 -25.735 -85.109  1.00141.44           C  
ANISOU  460  C   VAL A  62    26704  13369  13670    472   -768   2458       C  
ATOM    461  O   VAL A  62     -56.091 -24.977 -85.427  1.00145.72           O  
ANISOU  461  O   VAL A  62    27471  13774  14124    240   -534   2536       O  
ATOM    462  CB  VAL A  62     -56.167 -28.127 -85.075  1.00129.33           C  
ANISOU  462  CB  VAL A  62    24793  12289  12056    267   -503   2273       C  
ATOM    463  CG1 VAL A  62     -57.072 -28.443 -86.257  1.00130.25           C  
ANISOU  463  CG1 VAL A  62    25083  12459  11947    438   -778   2321       C  
ATOM    464  CG2 VAL A  62     -54.746 -27.822 -85.536  1.00128.82           C  
ANISOU  464  CG2 VAL A  62    24889  12195  11861    -71   -128   2321       C  
ATOM    465  N   GLU A  63     -58.273 -25.515 -85.489  1.00145.82           N  
ANISOU  465  N   GLU A  63    27323  13875  14208    774  -1126   2505       N  
ATOM    466  CA  GLU A  63     -58.655 -24.322 -86.234  1.00148.09           C  
ANISOU  466  CA  GLU A  63    27956  13928  14383    871  -1272   2661       C  
ATOM    467  C   GLU A  63     -59.120 -23.186 -85.334  1.00146.27           C  
ANISOU  467  C   GLU A  63    27714  13459  14405   1033  -1364   2675       C  
ATOM    468  O   GLU A  63     -58.952 -22.014 -85.692  1.00148.45           O  
ANISOU  468  O   GLU A  63    28297  13486  14622   1004  -1338   2801       O  
ATOM    469  CB  GLU A  63     -59.777 -24.645 -87.226  1.00154.32           C  
ANISOU  469  CB  GLU A  63    28836  14792  15005   1122  -1632   2716       C  
ATOM    470  CG  GLU A  63     -59.407 -25.611 -88.335  1.00156.23           C  
ANISOU  470  CG  GLU A  63    29182  15230  14947    973  -1569   2717       C  
ATOM    471  CD  GLU A  63     -60.563 -25.853 -89.289  1.00160.44           C  
ANISOU  471  CD  GLU A  63    29815  15830  15314   1216  -1957   2769       C  
ATOM    472  OE1 GLU A  63     -61.702 -25.467 -88.951  1.00161.93           O  
ANISOU  472  OE1 GLU A  63    29900  15961  15666   1520  -2284   2780       O  
ATOM    473  OE2 GLU A  63     -60.333 -26.422 -90.376  1.00162.68           O  
ANISOU  473  OE2 GLU A  63    30275  16227  15308   1103  -1935   2793       O  
ATOM    474  N   THR A  64     -59.697 -23.505 -84.173  1.00139.21           N  
ANISOU  474  N   THR A  64    26484  12622  13786   1200  -1457   2546       N  
ATOM    475  CA  THR A  64     -60.421 -22.505 -83.395  1.00133.71           C  
ANISOU  475  CA  THR A  64    25761  11710  13333   1429  -1601   2542       C  
ATOM    476  C   THR A  64     -59.499 -21.592 -82.595  1.00125.63           C  
ANISOU  476  C   THR A  64    24820  10482  12434   1211  -1319   2530       C  
ATOM    477  O   THR A  64     -59.808 -20.407 -82.429  1.00127.62           O  
ANISOU  477  O   THR A  64    25246  10469  12775   1322  -1380   2591       O  
ATOM    478  CB  THR A  64     -61.413 -23.193 -82.455  1.00129.49           C  
ANISOU  478  CB  THR A  64    24836  11317  13049   1689  -1793   2395       C  
ATOM    479  OG1 THR A  64     -60.699 -24.007 -81.516  1.00126.83           O  
ANISOU  479  OG1 THR A  64    24240  11129  12819   1495  -1557   2258       O  
ATOM    480  CG2 THR A  64     -62.372 -24.069 -83.248  1.00127.32           C  
ANISOU  480  CG2 THR A  64    24473  11243  12659   1897  -2095   2398       C  
ATOM    481  N   SER A  65     -58.382 -22.110 -82.088  1.00114.86           N  
ANISOU  481  N   SER A  65    23330   9229  11082    906  -1018   2449       N  
ATOM    482  CA  SER A  65     -57.477 -21.296 -81.290  1.00108.92           C  
ANISOU  482  CA  SER A  65    22631   8304  10450    671   -760   2420       C  
ATOM    483  C   SER A  65     -56.711 -20.328 -82.193  1.00110.71           C  
ANISOU  483  C   SER A  65    23253   8332  10479    452   -605   2568       C  
ATOM    484  O   SER A  65     -56.805 -20.369 -83.423  1.00115.39           O  
ANISOU  484  O   SER A  65    24075   8939  10829    466   -674   2691       O  
ATOM    485  CB  SER A  65     -56.520 -22.185 -80.499  1.00102.44           C  
ANISOU  485  CB  SER A  65    21537   7682   9704    414   -506   2292       C  
ATOM    486  OG  SER A  65     -55.312 -22.400 -81.209  1.00102.26           O  
ANISOU  486  OG  SER A  65    21636   7734   9484     83   -241   2348       O  
ATOM    487  N   ASN A  66     -55.936 -19.435 -81.569  1.00108.43           N  
ANISOU  487  N   ASN A  66    23057   7851  10289    232   -389   2552       N  
ATOM    488  CA  ASN A  66     -55.109 -18.481 -82.301  1.00115.24           C  
ANISOU  488  CA  ASN A  66    24287   8513  10988    -20   -203   2680       C  
ATOM    489  C   ASN A  66     -53.699 -18.405 -81.725  1.00119.75           C  
ANISOU  489  C   ASN A  66    24788   9103  11609   -437    155   2605       C  
ATOM    490  O   ASN A  66     -53.044 -17.364 -81.809  1.00122.59           O  
ANISOU  490  O   ASN A  66    25397   9236  11944   -656    322   2662       O  
ATOM    491  CB  ASN A  66     -55.751 -17.092 -82.322  1.00118.21           C  
ANISOU  491  CB  ASN A  66    24951   8542  11421    162   -348   2773       C  
ATOM    492  CG  ASN A  66     -56.401 -16.768 -83.659  1.00120.87           C  
ANISOU  492  CG  ASN A  66    25607   8789  11531    351   -555   2956       C  
ATOM    493  OD1 ASN A  66     -56.645 -17.655 -84.477  1.00119.00           O  
ANISOU  493  OD1 ASN A  66    25332   8767  11116    416   -657   2989       O  
ATOM    494  ND2 ASN A  66     -56.685 -15.488 -83.884  1.00124.60           N  
ANISOU  494  ND2 ASN A  66    26406   8934  12001    439   -621   3074       N  
ATOM    495  N   ASP A  67     -53.222 -19.498 -81.136  1.00121.05           N  
ANISOU  495  N   ASP A  67    24612   9535  11849   -554    271   2480       N  
ATOM    496  CA  ASP A  67     -51.839 -19.619 -80.694  1.00124.16           C  
ANISOU  496  CA  ASP A  67    24891  10006  12278   -955    603   2411       C  
ATOM    497  C   ASP A  67     -51.207 -20.806 -81.406  1.00127.13           C  
ANISOU  497  C   ASP A  67    25138  10674  12491  -1096    750   2414       C  
ATOM    498  O   ASP A  67     -51.747 -21.917 -81.370  1.00119.75           O  
ANISOU  498  O   ASP A  67    23982   9958  11558   -905    618   2363       O  
ATOM    499  CB  ASP A  67     -51.744 -19.779 -79.172  1.00116.26           C  
ANISOU  499  CB  ASP A  67    23589   9040  11543   -984    627   2247       C  
ATOM    500  CG  ASP A  67     -52.606 -20.907 -78.645  1.00104.00           C  
ANISOU  500  CG  ASP A  67    21727   7698  10088   -700    430   2157       C  
ATOM    501  OD1 ASP A  67     -53.642 -21.206 -79.275  1.00104.49           O  
ANISOU  501  OD1 ASP A  67    21835   7794  10073   -395    189   2214       O  
ATOM    502  OD2 ASP A  67     -52.247 -21.489 -77.599  1.00 96.43           O  
ANISOU  502  OD2 ASP A  67    20484   6872   9283   -791    510   2030       O  
ATOM    503  N   GLU A  68     -50.070 -20.565 -82.062  1.00142.19           N  
ANISOU  503  N   GLU A  68    27185  12581  14261  -1431   1035   2468       N  
ATOM    504  CA  GLU A  68     -49.455 -21.590 -82.898  1.00146.35           C  
ANISOU  504  CA  GLU A  68    27633  13361  14612  -1561   1203   2475       C  
ATOM    505  C   GLU A  68     -48.770 -22.680 -82.086  1.00139.23           C  
ANISOU  505  C   GLU A  68    26320  12730  13850  -1696   1366   2340       C  
ATOM    506  O   GLU A  68     -48.488 -23.752 -82.631  1.00137.71           O  
ANISOU  506  O   GLU A  68    26001  12775  13546  -1715   1459   2321       O  
ATOM    507  CB  GLU A  68     -48.452 -20.950 -83.859  1.00155.06           C  
ANISOU  507  CB  GLU A  68    29010  14374  15531  -1879   1479   2569       C  
ATOM    508  CG  GLU A  68     -49.080 -20.000 -84.865  1.00163.09           C  
ANISOU  508  CG  GLU A  68    30473  15139  16354  -1751   1329   2728       C  
ATOM    509  CD  GLU A  68     -49.898 -20.718 -85.920  1.00166.80           C  
ANISOU  509  CD  GLU A  68    31047  15724  16604  -1496   1123   2793       C  
ATOM    510  OE1 GLU A  68     -49.685 -21.933 -86.117  1.00165.54           O  
ANISOU  510  OE1 GLU A  68    30665  15840  16393  -1508   1192   2720       O  
ATOM    511  OE2 GLU A  68     -50.755 -20.067 -86.555  1.00170.31           O  
ANISOU  511  OE2 GLU A  68    31800  15982  16928  -1285    889   2915       O  
ATOM    512  N   ASP A  69     -48.490 -22.434 -80.804  1.00124.63           N  
ANISOU  512  N   ASP A  69    24271  10847  12237  -1789   1405   2243       N  
ATOM    513  CA  ASP A  69     -47.881 -23.467 -79.974  1.00115.20           C  
ANISOU  513  CA  ASP A  69    22689   9905  11179  -1903   1535   2125       C  
ATOM    514  C   ASP A  69     -48.828 -24.645 -79.780  1.00106.04           C  
ANISOU  514  C   ASP A  69    21333   8923  10036  -1577   1313   2080       C  
ATOM    515  O   ASP A  69     -48.416 -25.807 -79.878  1.00105.26           O  
ANISOU  515  O   ASP A  69    21012   9076   9905  -1615   1427   2037       O  
ATOM    516  CB  ASP A  69     -47.471 -22.875 -78.627  1.00114.50           C  
ANISOU  516  CB  ASP A  69    22462   9717  11324  -2070   1586   2029       C  
ATOM    517  CG  ASP A  69     -46.644 -21.613 -78.775  1.00114.60           C  
ANISOU  517  CG  ASP A  69    22687   9525  11332  -2390   1778   2062       C  
ATOM    518  OD1 ASP A  69     -45.750 -21.586 -79.648  1.00114.18           O  
ANISOU  518  OD1 ASP A  69    22705   9533  11144  -2640   2022   2116       O  
ATOM    519  OD2 ASP A  69     -46.894 -20.644 -78.027  1.00114.40           O  
ANISOU  519  OD2 ASP A  69    22759   9271  11435  -2395   1694   2025       O  
ATOM    520  N   PHE A  70     -50.102 -24.359 -79.510  1.00 99.83           N  
ANISOU  520  N   PHE A  70    20618   8008   9306  -1253   1005   2084       N  
ATOM    521  CA  PHE A  70     -51.104 -25.412 -79.378  1.00 93.94           C  
ANISOU  521  CA  PHE A  70    19697   7419   8579   -942    777   2039       C  
ATOM    522  C   PHE A  70     -51.265 -26.179 -80.687  1.00 93.46           C  
ANISOU  522  C   PHE A  70    19725   7506   8279   -871    758   2099       C  
ATOM    523  O   PHE A  70     -51.214 -27.417 -80.711  1.00 83.55           O  
ANISOU  523  O   PHE A  70    18262   6486   6999   -832    788   2041       O  
ATOM    524  CB  PHE A  70     -52.426 -24.783 -78.931  1.00 85.42           C  
ANISOU  524  CB  PHE A  70    18686   6157   7613   -623    467   2033       C  
ATOM    525  CG  PHE A  70     -53.563 -25.753 -78.812  1.00 82.89           C  
ANISOU  525  CG  PHE A  70    18186   5981   7325   -300    215   1983       C  
ATOM    526  CD1 PHE A  70     -53.534 -26.766 -77.871  1.00 79.22           C  
ANISOU  526  CD1 PHE A  70    17407   5696   6996   -277    236   1872       C  
ATOM    527  CD2 PHE A  70     -54.680 -25.625 -79.621  1.00 88.52           C  
ANISOU  527  CD2 PHE A  70    19049   6646   7940    -25    -51   2048       C  
ATOM    528  CE1 PHE A  70     -54.589 -27.650 -77.755  1.00 77.17           C  
ANISOU  528  CE1 PHE A  70    16987   5562   6771      4     14   1822       C  
ATOM    529  CE2 PHE A  70     -55.737 -26.506 -79.508  1.00 87.38           C  
ANISOU  529  CE2 PHE A  70    18723   6640   7838    251   -287   1992       C  
ATOM    530  CZ  PHE A  70     -55.691 -27.519 -78.572  1.00 78.80           C  
ANISOU  530  CZ  PHE A  70    17325   5727   6887    261   -247   1876       C  
ATOM    531  N   LYS A  71     -51.436 -25.449 -81.795  1.00 95.17           N  
ANISOU  531  N   LYS A  71    20271   7580   8309   -864    717   2212       N  
ATOM    532  CA  LYS A  71     -51.603 -26.086 -83.097  1.00 90.86           C  
ANISOU  532  CA  LYS A  71    19859   7154   7512   -812    691   2266       C  
ATOM    533  C   LYS A  71     -50.379 -26.900 -83.494  1.00 90.96           C  
ANISOU  533  C   LYS A  71    19762   7373   7427  -1084   1027   2229       C  
ATOM    534  O   LYS A  71     -50.496 -27.854 -84.271  1.00 90.24           O  
ANISOU  534  O   LYS A  71    19663   7451   7173  -1026   1027   2213       O  
ATOM    535  CB  LYS A  71     -51.898 -25.029 -84.161  1.00 96.65           C  
ANISOU  535  CB  LYS A  71    20996   7671   8056   -787    605   2406       C  
ATOM    536  CG  LYS A  71     -53.123 -24.183 -83.875  1.00 97.00           C  
ANISOU  536  CG  LYS A  71    21157   7505   8193   -494    274   2453       C  
ATOM    537  CD  LYS A  71     -53.196 -22.998 -84.818  1.00101.31           C  
ANISOU  537  CD  LYS A  71    22120   7806   8568   -513    239   2607       C  
ATOM    538  CE  LYS A  71     -54.414 -22.142 -84.528  1.00102.70           C  
ANISOU  538  CE  LYS A  71    22399   7768   8854   -197    -85   2655       C  
ATOM    539  NZ  LYS A  71     -54.430 -20.903 -85.354  1.00111.87           N  
ANISOU  539  NZ  LYS A  71    23983   8659   9863   -219   -107   2816       N  
ATOM    540  N   ALA A  72     -49.202 -26.542 -82.977  1.00 93.56           N  
ANISOU  540  N   ALA A  72    19997   7693   7858  -1383   1320   2205       N  
ATOM    541  CA  ALA A  72     -47.993 -27.297 -83.285  1.00 96.96           C  
ANISOU  541  CA  ALA A  72    20275   8334   8232  -1638   1661   2160       C  
ATOM    542  C   ALA A  72     -47.832 -28.520 -82.391  1.00 98.52           C  
ANISOU  542  C   ALA A  72    20084   8767   8583  -1590   1702   2044       C  
ATOM    543  O   ALA A  72     -47.324 -29.550 -82.847  1.00 98.64           O  
ANISOU  543  O   ALA A  72    19972   8995   8512  -1641   1880   1998       O  
ATOM    544  CB  ALA A  72     -46.764 -26.395 -83.158  1.00 99.12           C  
ANISOU  544  CB  ALA A  72    20587   8518   8557  -1999   1964   2180       C  
ATOM    545  N   GLU A  73     -48.261 -28.433 -81.130  1.00100.86           N  
ANISOU  545  N   GLU A  73    20203   9021   9098  -1487   1549   1993       N  
ATOM    546  CA  GLU A  73     -48.104 -29.536 -80.190  1.00 97.34           C  
ANISOU  546  CA  GLU A  73    19408   8779   8797  -1448   1584   1896       C  
ATOM    547  C   GLU A  73     -49.226 -30.562 -80.271  1.00 91.12           C  
ANISOU  547  C   GLU A  73    18554   8097   7970  -1126   1335   1859       C  
ATOM    548  O   GLU A  73     -49.077 -31.659 -79.722  1.00 91.05           O  
ANISOU  548  O   GLU A  73    18246   8294   8053  -1077   1378   1766       O  
ATOM    549  CB  GLU A  73     -48.016 -28.997 -78.758  1.00101.92           C  
ANISOU  549  CB  GLU A  73    19840   9265   9620  -1508   1543   1850       C  
ATOM    550  CG  GLU A  73     -46.791 -28.139 -78.484  1.00110.33           C  
ANISOU  550  CG  GLU A  73    20899  10264  10757  -1875   1806   1853       C  
ATOM    551  CD  GLU A  73     -46.879 -27.409 -77.158  1.00115.98           C  
ANISOU  551  CD  GLU A  73    21538  10838  11690  -1925   1711   1794       C  
ATOM    552  OE1 GLU A  73     -47.875 -27.615 -76.432  1.00116.43           O  
ANISOU  552  OE1 GLU A  73    21479  10893  11867  -1646   1447   1722       O  
ATOM    553  OE2 GLU A  73     -45.956 -26.628 -76.844  1.00119.90           O  
ANISOU  553  OE2 GLU A  73    22045  11256  12258  -2242   1896   1784       O  
ATOM    554  N   LEU A  74     -50.339 -30.241 -80.939  1.00 90.41           N  
ANISOU  554  N   LEU A  74    18686   7895   7772   -903   1065   1908       N  
ATOM    555  CA  LEU A  74     -51.469 -31.172 -80.962  1.00 91.23           C  
ANISOU  555  CA  LEU A  74    18706   8098   7858   -615    807   1860       C  
ATOM    556  C   LEU A  74     -51.212 -32.415 -81.817  1.00 93.04           C  
ANISOU  556  C   LEU A  74    18901   8540   7910   -627    921   1820       C  
ATOM    557  O   LEU A  74     -51.444 -33.535 -81.321  1.00 92.54           O  
ANISOU  557  O   LEU A  74    18616   8635   7911   -521    892   1735       O  
ATOM    558  CB  LEU A  74     -52.732 -30.425 -81.404  1.00 92.24           C  
ANISOU  558  CB  LEU A  74    19055   8055   7938   -380    476   1920       C  
ATOM    559  CG  LEU A  74     -54.067 -31.166 -81.410  1.00 88.42           C  
ANISOU  559  CG  LEU A  74    18488   7648   7460    -76    160   1873       C  
ATOM    560  CD1 LEU A  74     -54.446 -31.592 -80.004  1.00 82.26           C  
ANISOU  560  CD1 LEU A  74    17415   6911   6929     37     86   1781       C  
ATOM    561  CD2 LEU A  74     -55.150 -30.284 -82.020  1.00 92.06           C  
ANISOU  561  CD2 LEU A  74    19182   7941   7857    126   -138   1951       C  
ATOM    562  N   PRO A  75     -50.763 -32.312 -83.073  1.00 96.85           N  
ANISOU  562  N   PRO A  75    19603   9029   8168   -746   1057   1866       N  
ATOM    563  CA  PRO A  75     -50.701 -33.506 -83.946  1.00 94.92           C  
ANISOU  563  CA  PRO A  75    19359   8967   7741   -723   1133   1806       C  
ATOM    564  C   PRO A  75     -49.841 -34.627 -83.379  1.00 92.70           C  
ANISOU  564  C   PRO A  75    18779   8890   7552   -811   1400   1705       C  
ATOM    565  O   PRO A  75     -50.271 -35.791 -83.415  1.00 93.61           O  
ANISOU  565  O   PRO A  75    18791   9143   7635   -672   1336   1619       O  
ATOM    566  CB  PRO A  75     -50.121 -32.955 -85.259  1.00 97.68           C  
ANISOU  566  CB  PRO A  75    20004   9255   7854   -895   1299   1880       C  
ATOM    567  CG  PRO A  75     -50.548 -31.541 -85.273  1.00100.09           C  
ANISOU  567  CG  PRO A  75    20534   9322   8173   -876   1129   1995       C  
ATOM    568  CD  PRO A  75     -50.476 -31.083 -83.841  1.00 99.32           C  
ANISOU  568  CD  PRO A  75    20219   9158   8359   -879   1108   1975       C  
ATOM    569  N   PRO A  76     -48.626 -34.354 -82.868  1.00 92.50           N  
ANISOU  569  N   PRO A  76    18608   8896   7641  -1039   1703   1707       N  
ATOM    570  CA  PRO A  76     -47.820 -35.479 -82.352  1.00 91.56           C  
ANISOU  570  CA  PRO A  76    18118   9009   7662  -1079   1931   1580       C  
ATOM    571  C   PRO A  76     -48.509 -36.264 -81.249  1.00 87.05           C  
ANISOU  571  C   PRO A  76    17172   8551   7353   -851   1697   1449       C  
ATOM    572  O   PRO A  76     -48.474 -37.503 -81.257  1.00 89.93           O  
ANISOU  572  O   PRO A  76    17322   9088   7761   -752   1741   1331       O  
ATOM    573  CB  PRO A  76     -46.542 -34.792 -81.851  1.00 92.61           C  
ANISOU  573  CB  PRO A  76    18091   9152   7943  -1350   2208   1592       C  
ATOM    574  CG  PRO A  76     -46.447 -33.560 -82.658  1.00 94.26           C  
ANISOU  574  CG  PRO A  76    18698   9151   7965  -1513   2254   1731       C  
ATOM    575  CD  PRO A  76     -47.860 -33.094 -82.798  1.00 94.23           C  
ANISOU  575  CD  PRO A  76    18919   8978   7907  -1273   1856   1784       C  
ATOM    576  N   SER A  77     -49.147 -35.578 -80.299  1.00 80.33           N  
ANISOU  576  N   SER A  77    16256   7591   6674   -768   1465   1464       N  
ATOM    577  CA  SER A  77     -49.861 -36.284 -79.241  1.00 77.25           C  
ANISOU  577  CA  SER A  77    15538   7301   6513   -565   1258   1345       C  
ATOM    578  C   SER A  77     -51.061 -37.043 -79.796  1.00 74.17           C  
ANISOU  578  C   SER A  77    15246   6928   6007   -347   1032   1312       C  
ATOM    579  O   SER A  77     -51.346 -38.169 -79.359  1.00 69.79           O  
ANISOU  579  O   SER A  77    14426   6520   5572   -228    987   1190       O  
ATOM    580  CB  SER A  77     -50.292 -35.302 -78.150  1.00 75.49           C  
ANISOU  580  CB  SER A  77    15259   6948   6475   -536   1087   1359       C  
ATOM    581  OG  SER A  77     -51.051 -34.235 -78.689  1.00 77.32           O  
ANISOU  581  OG  SER A  77    15870   6941   6566   -487    919   1482       O  
ATOM    582  N   MET A  78     -51.771 -36.449 -80.764  1.00 71.72           N  
ANISOU  582  N   MET A  78    15323   6467   5461   -299    879   1422       N  
ATOM    583  CA  MET A  78     -52.902 -37.144 -81.380  1.00 74.83           C  
ANISOU  583  CA  MET A  78    15811   6893   5726   -112    642   1384       C  
ATOM    584  C   MET A  78     -52.460 -38.459 -82.014  1.00 79.32           C  
ANISOU  584  C   MET A  78    16319   7634   6184   -147    818   1283       C  
ATOM    585  O   MET A  78     -53.007 -39.529 -81.709  1.00 80.68           O  
ANISOU  585  O   MET A  78    16274   7922   6457    -22    720   1153       O  
ATOM    586  CB  MET A  78     -53.573 -36.246 -82.421  1.00 80.00           C  
ANISOU  586  CB  MET A  78    16920   7366   6110    -68    453   1538       C  
ATOM    587  CG  MET A  78     -54.352 -35.079 -81.839  1.00 81.35           C  
ANISOU  587  CG  MET A  78    17160   7346   6405     53    206   1620       C  
ATOM    588  SD  MET A  78     -55.422 -34.272 -83.052  1.00 90.83           S  
ANISOU  588  SD  MET A  78    18706   8405   7401    199   -112   1720       S  
ATOM    589  CE  MET A  78     -54.241 -33.783 -84.302  1.00 90.21           C  
ANISOU  589  CE  MET A  78    18910   8288   7078    -63    180   1802       C  
ATOM    590  N   GLN A  79     -51.464 -38.396 -82.904  1.00 84.04           N  
ANISOU  590  N   GLN A  79    17116   8238   6575   -324   1100   1334       N  
ATOM    591  CA  GLN A  79     -50.968 -39.602 -83.558  1.00 85.73           C  
ANISOU  591  CA  GLN A  79    17298   8600   6678   -356   1308   1225       C  
ATOM    592  C   GLN A  79     -50.420 -40.600 -82.545  1.00 84.83           C  
ANISOU  592  C   GLN A  79    16724   8642   6864   -320   1445   1081       C  
ATOM    593  O   GLN A  79     -50.567 -41.815 -82.727  1.00 79.39           O  
ANISOU  593  O   GLN A  79    15937   8053   6174   -237   1473    955       O  
ATOM    594  CB  GLN A  79     -49.895 -39.229 -84.582  1.00 89.50           C  
ANISOU  594  CB  GLN A  79    18047   9056   6903   -569   1637   1303       C  
ATOM    595  CG  GLN A  79     -49.519 -40.339 -85.549  1.00 93.88           C  
ANISOU  595  CG  GLN A  79    18690   9726   7256   -595   1850   1197       C  
ATOM    596  CD  GLN A  79     -48.577 -39.856 -86.638  1.00102.20           C  
ANISOU  596  CD  GLN A  79    19946  10764   8123   -799   2137   1241       C  
ATOM    597  OE1 GLN A  79     -47.796 -38.927 -86.431  1.00103.78           O  
ANISOU  597  OE1 GLN A  79    20120  10914   8397   -962   2304   1328       O  
ATOM    598  NE2 GLN A  79     -48.653 -40.480 -87.810  1.00106.26           N  
ANISOU  598  NE2 GLN A  79    20647  11319   8409   -802   2192   1166       N  
ATOM    599  N   GLU A  80     -49.800 -40.108 -81.471  1.00 88.14           N  
ANISOU  599  N   GLU A  80    16879   9076   7535   -380   1520   1096       N  
ATOM    600  CA  GLU A  80     -49.290 -40.996 -80.431  1.00 89.05           C  
ANISOU  600  CA  GLU A  80    16567   9337   7930   -330   1611    981       C  
ATOM    601  C   GLU A  80     -50.416 -41.817 -79.811  1.00 80.27           C  
ANISOU  601  C   GLU A  80    15304   8253   6943   -130   1354    890       C  
ATOM    602  O   GLU A  80     -50.394 -43.057 -79.838  1.00 80.67           O  
ANISOU  602  O   GLU A  80    15222   8394   7035    -51   1415    781       O  
ATOM    603  CB  GLU A  80     -48.565 -40.173 -79.363  1.00 98.54           C  
ANISOU  603  CB  GLU A  80    17546  10545   9350   -437   1670   1020       C  
ATOM    604  CG  GLU A  80     -47.838 -41.000 -78.315  1.00104.67           C  
ANISOU  604  CG  GLU A  80    17893  11486  10392   -402   1771    924       C  
ATOM    605  CD  GLU A  80     -46.517 -41.547 -78.817  1.00113.24           C  
ANISOU  605  CD  GLU A  80    18855  12699  11471   -501   2109    884       C  
ATOM    606  OE1 GLU A  80     -46.035 -41.071 -79.868  1.00119.17           O  
ANISOU  606  OE1 GLU A  80    19846  13411  12022   -650   2303    937       O  
ATOM    607  OE2 GLU A  80     -45.959 -42.451 -78.159  1.00114.96           O  
ANISOU  607  OE2 GLU A  80    18742  13055  11885   -424   2187    802       O  
ATOM    608  N   VAL A  81     -51.422 -41.136 -79.254  1.00 74.37           N  
ANISOU  608  N   VAL A  81    14580   7414   6262    -49   1078    929       N  
ATOM    609  CA  VAL A  81     -52.472 -41.851 -78.531  1.00 67.25           C  
ANISOU  609  CA  VAL A  81    13494   6548   5510    115    861    837       C  
ATOM    610  C   VAL A  81     -53.279 -42.735 -79.480  1.00 65.08           C  
ANISOU  610  C   VAL A  81    13373   6289   5067    196    758    769       C  
ATOM    611  O   VAL A  81     -53.690 -43.847 -79.114  1.00 59.92           O  
ANISOU  611  O   VAL A  81    12544   5704   4519    278    721    655       O  
ATOM    612  CB  VAL A  81     -53.361 -40.857 -77.757  1.00 63.25           C  
ANISOU  612  CB  VAL A  81    12973   5943   5116    185    617    880       C  
ATOM    613  CG1 VAL A  81     -54.079 -39.912 -78.703  1.00 66.59           C  
ANISOU  613  CG1 VAL A  81    13743   6224   5335    211    443    980       C  
ATOM    614  CG2 VAL A  81     -54.351 -41.597 -76.872  1.00 57.73           C  
ANISOU  614  CG2 VAL A  81    12036   5300   4597    328    445    775       C  
ATOM    615  N   GLN A  82     -53.498 -42.278 -80.719  1.00 67.95           N  
ANISOU  615  N   GLN A  82    14084   6582   5153    159    713    836       N  
ATOM    616  CA  GLN A  82     -54.191 -43.126 -81.685  1.00 69.06           C  
ANISOU  616  CA  GLN A  82    14390   6750   5100    210    613    758       C  
ATOM    617  C   GLN A  82     -53.380 -44.380 -81.992  1.00 72.75           C  
ANISOU  617  C   GLN A  82    14785   7311   5546    165    885    644       C  
ATOM    618  O   GLN A  82     -53.942 -45.474 -82.142  1.00 71.38           O  
ANISOU  618  O   GLN A  82    14571   7178   5373    228    820    517       O  
ATOM    619  CB  GLN A  82     -54.489 -42.344 -82.965  1.00 68.78           C  
ANISOU  619  CB  GLN A  82    14775   6626   4733    172    509    868       C  
ATOM    620  CG  GLN A  82     -55.690 -41.416 -82.845  1.00 69.41           C  
ANISOU  620  CG  GLN A  82    14944   6609   4820    292    149    949       C  
ATOM    621  CD  GLN A  82     -56.037 -40.730 -84.150  1.00 78.00           C  
ANISOU  621  CD  GLN A  82    16474   7605   5559    281      8   1070       C  
ATOM    622  OE1 GLN A  82     -55.329 -39.826 -84.598  1.00 76.99           O  
ANISOU  622  OE1 GLN A  82    16601   7376   5276    173    149   1213       O  
ATOM    623  NE2 GLN A  82     -57.134 -41.154 -84.767  1.00 77.87           N  
ANISOU  623  NE2 GLN A  82    16558   7622   5407    383   -279   1017       N  
ATOM    624  N   GLN A  83     -52.053 -44.244 -82.074  1.00 83.30           N  
ANISOU  624  N   GLN A  83    16092   8677   6882     55   1200    677       N  
ATOM    625  CA  GLN A  83     -51.207 -45.413 -82.288  1.00 81.58           C  
ANISOU  625  CA  GLN A  83    15768   8544   6685     43   1481    563       C  
ATOM    626  C   GLN A  83     -51.299 -46.381 -81.114  1.00 77.21           C  
ANISOU  626  C   GLN A  83    14857   8045   6433    157   1456    467       C  
ATOM    627  O   GLN A  83     -51.291 -47.603 -81.307  1.00 80.29           O  
ANISOU  627  O   GLN A  83    15210   8461   6836    214   1541    345       O  
ATOM    628  CB  GLN A  83     -49.759 -44.980 -82.519  1.00 84.68           C  
ANISOU  628  CB  GLN A  83    16143   8975   7058    -92   1822    617       C  
ATOM    629  CG  GLN A  83     -48.829 -46.123 -82.884  1.00 91.22           C  
ANISOU  629  CG  GLN A  83    16874   9887   7899    -87   2141    496       C  
ATOM    630  CD  GLN A  83     -49.326 -46.916 -84.078  1.00 96.81           C  
ANISOU  630  CD  GLN A  83    17884  10569   8332    -69   2152    396       C  
ATOM    631  OE1 GLN A  83     -49.355 -46.416 -85.204  1.00 99.58           O  
ANISOU  631  OE1 GLN A  83    18588  10881   8367   -171   2197    443       O  
ATOM    632  NE2 GLN A  83     -49.727 -48.158 -83.836  1.00 96.41           N  
ANISOU  632  NE2 GLN A  83    17718  10527   8385     51   2109    257       N  
ATOM    633  N   ALA A  84     -51.395 -45.855 -79.888  1.00 71.67           N  
ANISOU  633  N   ALA A  84    13918   7350   5965    187   1343    521       N  
ATOM    634  CA  ALA A  84     -51.570 -46.732 -78.732  1.00 67.83           C  
ANISOU  634  CA  ALA A  84    13132   6908   5735    290   1299    448       C  
ATOM    635  C   ALA A  84     -52.893 -47.490 -78.806  1.00 65.51           C  
ANISOU  635  C   ALA A  84    12887   6580   5425    376   1084    357       C  
ATOM    636  O   ALA A  84     -52.952 -48.690 -78.494  1.00 60.34           O  
ANISOU  636  O   ALA A  84    12114   5940   4873    437   1137    259       O  
ATOM    637  CB  ALA A  84     -51.487 -45.924 -77.439  1.00 65.83           C  
ANISOU  637  CB  ALA A  84    12660   6666   5686    288   1209    521       C  
ATOM    638  N   ALA A  85     -53.967 -46.809 -79.221  1.00 63.95           N  
ANISOU  638  N   ALA A  85    12860   6331   5105    379    837    386       N  
ATOM    639  CA  ALA A  85     -55.234 -47.505 -79.429  1.00 62.32           C  
ANISOU  639  CA  ALA A  85    12690   6115   4875    437    625    284       C  
ATOM    640  C   ALA A  85     -55.093 -48.608 -80.475  1.00 63.97           C  
ANISOU  640  C   ALA A  85    13069   6327   4911    409    741    171       C  
ATOM    641  O   ALA A  85     -55.651 -49.704 -80.314  1.00 60.22           O  
ANISOU  641  O   ALA A  85    12524   5850   4508    440    701     47       O  
ATOM    642  CB  ALA A  85     -56.321 -46.511 -79.837  1.00 60.66           C  
ANISOU  642  CB  ALA A  85    12632   5862   4552    461    332    341       C  
ATOM    643  N   VAL A  86     -54.346 -48.339 -81.552  1.00 65.50           N  
ANISOU  643  N   VAL A  86    13504   6516   4869    338    905    204       N  
ATOM    644  CA  VAL A  86     -54.080 -49.379 -82.545  1.00 69.95           C  
ANISOU  644  CA  VAL A  86    14246   7078   5254    307   1064     81       C  
ATOM    645  C   VAL A  86     -53.369 -50.562 -81.900  1.00 72.09           C  
ANISOU  645  C   VAL A  86    14293   7359   5740    360   1299    -13       C  
ATOM    646  O   VAL A  86     -53.688 -51.727 -82.179  1.00 71.84           O  
ANISOU  646  O   VAL A  86    14310   7294   5692    380   1326   -156       O  
ATOM    647  CB  VAL A  86     -53.268 -48.807 -83.721  1.00 72.96           C  
ANISOU  647  CB  VAL A  86    14918   7458   5345    210   1254    141       C  
ATOM    648  CG1 VAL A  86     -52.887 -49.919 -84.697  1.00 68.87           C  
ANISOU  648  CG1 VAL A  86    14583   6939   4645    180   1469     -9       C  
ATOM    649  CG2 VAL A  86     -54.053 -47.709 -84.425  1.00 72.03           C  
ANISOU  649  CG2 VAL A  86    15078   7305   4986    175    992    247       C  
ATOM    650  N   PHE A  87     -52.397 -50.284 -81.024  1.00 74.11           N  
ANISOU  650  N   PHE A  87    14307   7650   6199    385   1461     65       N  
ATOM    651  CA  PHE A  87     -51.719 -51.359 -80.307  1.00 71.05           C  
ANISOU  651  CA  PHE A  87    13690   7270   6034    469   1647      1       C  
ATOM    652  C   PHE A  87     -52.704 -52.184 -79.492  1.00 69.35           C  
ANISOU  652  C   PHE A  87    13355   7011   5984    537   1468    -67       C  
ATOM    653  O   PHE A  87     -52.556 -53.407 -79.379  1.00 72.35           O  
ANISOU  653  O   PHE A  87    13700   7341   6448    597   1585   -166       O  
ATOM    654  CB  PHE A  87     -50.628 -50.792 -79.400  1.00 72.16           C  
ANISOU  654  CB  PHE A  87    13566   7481   6369    482   1776    108       C  
ATOM    655  CG  PHE A  87     -49.338 -50.501 -80.108  1.00 79.07           C  
ANISOU  655  CG  PHE A  87    14477   8408   7156    422   2070    127       C  
ATOM    656  CD1 PHE A  87     -49.256 -50.567 -81.488  1.00 81.72           C  
ANISOU  656  CD1 PHE A  87    15113   8721   7216    351   2202     72       C  
ATOM    657  CD2 PHE A  87     -48.200 -50.176 -79.390  1.00 82.83           C  
ANISOU  657  CD2 PHE A  87    14683   8970   7820    425   2220    192       C  
ATOM    658  CE1 PHE A  87     -48.067 -50.304 -82.139  1.00 85.23           C  
ANISOU  658  CE1 PHE A  87    15588   9220   7578    280   2511     82       C  
ATOM    659  CE2 PHE A  87     -47.007 -49.913 -80.037  1.00 86.63           C  
ANISOU  659  CE2 PHE A  87    15159   9516   8243    353   2511    197       C  
ATOM    660  CZ  PHE A  87     -46.941 -49.977 -81.412  1.00 86.20           C  
ANISOU  660  CZ  PHE A  87    15405   9432   7917    279   2674    142       C  
ATOM    661  N   LEU A  88     -53.718 -51.535 -78.914  1.00 67.32           N  
ANISOU  661  N   LEU A  88    13040   6759   5781    528   1200    -18       N  
ATOM    662  CA  LEU A  88     -54.732 -52.297 -78.191  1.00 64.89           C  
ANISOU  662  CA  LEU A  88    12622   6415   5618    563   1049    -91       C  
ATOM    663  C   LEU A  88     -55.540 -53.182 -79.133  1.00 63.76           C  
ANISOU  663  C   LEU A  88    12678   6219   5329    523    985   -240       C  
ATOM    664  O   LEU A  88     -55.861 -54.328 -78.791  1.00 61.46           O  
ANISOU  664  O   LEU A  88    12339   5866   5145    538   1016   -341       O  
ATOM    665  CB  LEU A  88     -55.651 -51.359 -77.410  1.00 65.04           C  
ANISOU  665  CB  LEU A  88    12522   6462   5727    563    801    -23       C  
ATOM    666  CG  LEU A  88     -55.050 -50.753 -76.142  1.00 59.79           C  
ANISOU  666  CG  LEU A  88    11630   5836   5251    598    842     86       C  
ATOM    667  CD1 LEU A  88     -56.148 -50.181 -75.263  1.00 63.16           C  
ANISOU  667  CD1 LEU A  88    11937   6270   5789    609    621    102       C  
ATOM    668  CD2 LEU A  88     -54.225 -51.784 -75.381  1.00 55.07           C  
ANISOU  668  CD2 LEU A  88    10875   5236   4814    657   1029     75       C  
ATOM    669  N   SER A  89     -55.880 -52.673 -80.322  1.00 63.18           N  
ANISOU  669  N   SER A  89    12849   6160   4999    460    889   -256       N  
ATOM    670  CA  SER A  89     -56.612 -53.493 -81.287  1.00 66.37           C  
ANISOU  670  CA  SER A  89    13460   6526   5230    403    811   -411       C  
ATOM    671  C   SER A  89     -55.806 -54.726 -81.687  1.00 67.08           C  
ANISOU  671  C   SER A  89    13643   6548   5298    410   1099   -530       C  
ATOM    672  O   SER A  89     -56.311 -55.859 -81.655  1.00 72.63           O  
ANISOU  672  O   SER A  89    14365   7175   6054    392   1094   -672       O  
ATOM    673  CB  SER A  89     -56.970 -52.661 -82.519  1.00 72.90           C  
ANISOU  673  CB  SER A  89    14561   7389   5747    343    657   -385       C  
ATOM    674  OG  SER A  89     -57.784 -51.557 -82.168  1.00 75.48           O  
ANISOU  674  OG  SER A  89    14810   7756   6111    367    376   -281       O  
ATOM    675  N   ASP A  90     -54.541 -54.519 -82.067  1.00 64.57           N  
ANISOU  675  N   ASP A  90    13380   6244   4911    433   1365   -480       N  
ATOM    676  CA  ASP A  90     -53.676 -55.644 -82.409  1.00 66.42           C  
ANISOU  676  CA  ASP A  90    13674   6409   5151    474   1669   -594       C  
ATOM    677  C   ASP A  90     -53.553 -56.618 -81.244  1.00 71.24           C  
ANISOU  677  C   ASP A  90    14051   6947   6068    575   1738   -616       C  
ATOM    678  O   ASP A  90     -53.556 -57.839 -81.442  1.00 71.69           O  
ANISOU  678  O   ASP A  90    14197   6891   6151    600   1859   -756       O  
ATOM    679  CB  ASP A  90     -52.297 -55.138 -82.828  1.00 68.60           C  
ANISOU  679  CB  ASP A  90    13966   6741   5359    491   1955   -525       C  
ATOM    680  CG  ASP A  90     -52.364 -54.090 -83.926  1.00 74.80           C  
ANISOU  680  CG  ASP A  90    15012   7584   5826    378   1906   -471       C  
ATOM    681  OD1 ASP A  90     -53.390 -54.030 -84.639  1.00 78.93           O  
ANISOU  681  OD1 ASP A  90    15766   8093   6132    305   1679   -527       O  
ATOM    682  OD2 ASP A  90     -51.383 -53.331 -84.078  1.00 71.95           O  
ANISOU  682  OD2 ASP A  90    14627   7281   5429    356   2091   -370       O  
ATOM    683  N   ALA A  91     -53.449 -56.095 -80.019  1.00 67.14           N  
ANISOU  683  N   ALA A  91    13261   6478   5771    631   1661   -478       N  
ATOM    684  CA  ALA A  91     -53.372 -56.959 -78.846  1.00 66.43           C  
ANISOU  684  CA  ALA A  91    12975   6321   5946    724   1702   -472       C  
ATOM    685  C   ALA A  91     -54.611 -57.835 -78.724  1.00 69.33           C  
ANISOU  685  C   ALA A  91    13415   6587   6340    666   1554   -590       C  
ATOM    686  O   ALA A  91     -54.506 -59.037 -78.446  1.00 72.08           O  
ANISOU  686  O   ALA A  91    13781   6806   6801    715   1676   -666       O  
ATOM    687  CB  ALA A  91     -53.186 -56.118 -77.585  1.00 59.14           C  
ANISOU  687  CB  ALA A  91    11785   5485   5202    765   1606   -308       C  
ATOM    688  N   ALA A  92     -55.795 -57.251 -78.929  1.00 66.86           N  
ANISOU  688  N   ALA A  92    13141   6325   5936    560   1292   -608       N  
ATOM    689  CA  ALA A  92     -57.022 -58.042 -78.907  1.00 66.39           C  
ANISOU  689  CA  ALA A  92    13129   6194   5902    471   1147   -741       C  
ATOM    690  C   ALA A  92     -56.974 -59.151 -79.951  1.00 72.07           C  
ANISOU  690  C   ALA A  92    14106   6798   6480    421   1273   -924       C  
ATOM    691  O   ALA A  92     -57.299 -60.311 -79.659  1.00 74.22           O  
ANISOU  691  O   ALA A  92    14407   6934   6861    397   1332  -1031       O  
ATOM    692  CB  ALA A  92     -58.235 -57.140 -79.131  1.00 67.81           C  
ANISOU  692  CB  ALA A  92    13291   6476   5997    383    838   -740       C  
ATOM    693  N   ARG A  93     -56.553 -58.815 -81.174  1.00 72.86           N  
ANISOU  693  N   ARG A  93    14420   6936   6326    396   1331   -966       N  
ATOM    694  CA  ARG A  93     -56.468 -59.821 -82.229  1.00 80.70           C  
ANISOU  694  CA  ARG A  93    15691   7822   7151    343   1467  -1159       C  
ATOM    695  C   ARG A  93     -55.539 -60.966 -81.833  1.00 81.60           C  
ANISOU  695  C   ARG A  93    15790   7780   7435    460   1777  -1205       C  
ATOM    696  O   ARG A  93     -55.950 -62.134 -81.772  1.00 82.78           O  
ANISOU  696  O   ARG A  93    16032   7769   7653    424   1820  -1346       O  
ATOM    697  CB  ARG A  93     -55.983 -59.178 -83.529  1.00 88.38           C  
ANISOU  697  CB  ARG A  93    16902   8872   7806    308   1526  -1171       C  
ATOM    698  CG  ARG A  93     -56.884 -58.099 -84.101  1.00 89.99           C  
ANISOU  698  CG  ARG A  93    17190   9205   7799    210   1209  -1124       C  
ATOM    699  CD  ARG A  93     -56.267 -57.506 -85.363  1.00 89.24           C  
ANISOU  699  CD  ARG A  93    17376   9165   7367    176   1309  -1113       C  
ATOM    700  NE  ARG A  93     -55.328 -58.433 -85.993  1.00 87.49           N  
ANISOU  700  NE  ARG A  93    17335   8850   7057    194   1658  -1248       N  
ATOM    701  CZ  ARG A  93     -54.011 -58.253 -86.040  1.00 85.91           C  
ANISOU  701  CZ  ARG A  93    17102   8660   6879    279   1981  -1183       C  
ATOM    702  NH1 ARG A  93     -53.467 -57.168 -85.505  1.00 81.46           N  
ANISOU  702  NH1 ARG A  93    16345   8196   6410    327   1989   -982       N  
ATOM    703  NH2 ARG A  93     -53.238 -59.155 -86.628  1.00 88.58           N  
ANISOU  703  NH2 ARG A  93    17594   8910   7152    310   2303  -1330       N  
ATOM    704  N   LEU A  94     -54.274 -60.641 -81.557  1.00 81.12           N  
ANISOU  704  N   LEU A  94    15609   7757   7454    603   1994  -1087       N  
ATOM    705  CA  LEU A  94     -53.263 -61.671 -81.340  1.00 79.27           C  
ANISOU  705  CA  LEU A  94    15363   7387   7370    753   2295  -1130       C  
ATOM    706  C   LEU A  94     -53.562 -62.495 -80.094  1.00 77.23           C  
ANISOU  706  C   LEU A  94    14956   6998   7389    821   2261  -1092       C  
ATOM    707  O   LEU A  94     -53.460 -63.727 -80.117  1.00 77.35           O  
ANISOU  707  O   LEU A  94    15095   6815   7481    873   2412  -1207       O  
ATOM    708  CB  LEU A  94     -51.881 -61.027 -81.241  1.00 75.38           C  
ANISOU  708  CB  LEU A  94    14708   7005   6929    885   2500  -1003       C  
ATOM    709  CG  LEU A  94     -51.505 -60.092 -82.392  1.00 76.46           C  
ANISOU  709  CG  LEU A  94    14990   7273   6789    800   2563  -1007       C  
ATOM    710  CD1 LEU A  94     -50.186 -59.392 -82.111  1.00 70.32           C  
ANISOU  710  CD1 LEU A  94    13992   6617   6108    899   2756   -872       C  
ATOM    711  CD2 LEU A  94     -51.443 -60.855 -83.705  1.00 76.98           C  
ANISOU  711  CD2 LEU A  94    15389   7241   6617    751   2746  -1219       C  
ATOM    712  N   LEU A  95     -53.933 -61.834 -78.994  1.00 77.05           N  
ANISOU  712  N   LEU A  95    14697   7069   7508    820   2074   -933       N  
ATOM    713  CA  LEU A  95     -54.221 -62.568 -77.768  1.00 74.32           C  
ANISOU  713  CA  LEU A  95    14234   6606   7397    871   2048   -880       C  
ATOM    714  C   LEU A  95     -55.475 -63.420 -77.904  1.00 75.56           C  
ANISOU  714  C   LEU A  95    14551   6621   7537    713   1945  -1031       C  
ATOM    715  O   LEU A  95     -55.545 -64.509 -77.323  1.00 76.64           O  
ANISOU  715  O   LEU A  95    14731   6566   7824    747   2036  -1057       O  
ATOM    716  CB  LEU A  95     -54.343 -61.604 -76.588  1.00 74.00           C  
ANISOU  716  CB  LEU A  95    13925   6711   7479    888   1883   -689       C  
ATOM    717  CG  LEU A  95     -53.019 -60.988 -76.131  1.00 75.95           C  
ANISOU  717  CG  LEU A  95    13977   7071   7811   1046   1994   -535       C  
ATOM    718  CD1 LEU A  95     -53.207 -60.177 -74.862  1.00 76.99           C  
ANISOU  718  CD1 LEU A  95    13874   7318   8060   1047   1827   -370       C  
ATOM    719  CD2 LEU A  95     -51.964 -62.067 -75.928  1.00 78.58           C  
ANISOU  719  CD2 LEU A  95    14306   7268   8283   1237   2231   -538       C  
ATOM    720  N   LYS A  96     -56.472 -62.954 -78.662  1.00 76.94           N  
ANISOU  720  N   LYS A  96    14817   6883   7535    535   1751  -1132       N  
ATOM    721  CA  LYS A  96     -57.602 -63.824 -78.973  1.00 76.91           C  
ANISOU  721  CA  LYS A  96    14965   6755   7501    360   1663  -1314       C  
ATOM    722  C   LYS A  96     -57.141 -65.046 -79.755  1.00 80.71           C  
ANISOU  722  C   LYS A  96    15723   7024   7920    375   1893  -1491       C  
ATOM    723  O   LYS A  96     -57.631 -66.160 -79.528  1.00 78.65           O  
ANISOU  723  O   LYS A  96    15570   6560   7753    300   1940  -1602       O  
ATOM    724  CB  LYS A  96     -58.669 -63.060 -79.757  1.00 81.55           C  
ANISOU  724  CB  LYS A  96    15589   7502   7897    188   1389  -1394       C  
ATOM    725  CG  LYS A  96     -59.863 -63.916 -80.154  1.00 85.17           C  
ANISOU  725  CG  LYS A  96    16176   7865   8319    -20   1270  -1604       C  
ATOM    726  CD  LYS A  96     -60.790 -63.185 -81.109  1.00 90.28           C  
ANISOU  726  CD  LYS A  96    16872   8684   8747   -162    983  -1692       C  
ATOM    727  CE  LYS A  96     -61.890 -64.106 -81.615  1.00 96.93           C  
ANISOU  727  CE  LYS A  96    17843   9444   9540   -387    865  -1931       C  
ATOM    728  NZ  LYS A  96     -62.745 -63.442 -82.638  1.00100.79           N  
ANISOU  728  NZ  LYS A  96    18392  10112   9793   -511    557  -2024       N  
ATOM    729  N   ALA A  97     -56.189 -64.860 -80.674  1.00 83.62           N  
ANISOU  729  N   ALA A  97    16218   7423   8132    466   2060  -1525       N  
ATOM    730  CA  ALA A  97     -55.660 -65.991 -81.431  1.00 86.78           C  
ANISOU  730  CA  ALA A  97    16885   7615   8471    505   2316  -1706       C  
ATOM    731  C   ALA A  97     -54.882 -66.943 -80.527  1.00 82.95           C  
ANISOU  731  C   ALA A  97    16340   6923   8254    705   2543  -1642       C  
ATOM    732  O   ALA A  97     -55.178 -68.141 -80.465  1.00 81.95           O  
ANISOU  732  O   ALA A  97    16388   6544   8204    674   2634  -1769       O  
ATOM    733  CB  ALA A  97     -54.783 -65.492 -82.581  1.00 75.99           C  
ANISOU  733  CB  ALA A  97    15651   6350   6872    559   2472  -1751       C  
ATOM    734  N   ASP A  98     -53.880 -66.427 -79.815  1.00 80.53           N  
ANISOU  734  N   ASP A  98    15794   6713   8091    910   2625  -1443       N  
ATOM    735  CA  ASP A  98     -53.058 -67.243 -78.931  1.00 82.43           C  
ANISOU  735  CA  ASP A  98    15955   6783   8582   1137   2806  -1354       C  
ATOM    736  C   ASP A  98     -52.815 -66.497 -77.629  1.00 75.11           C  
ANISOU  736  C   ASP A  98    14706   6007   7826   1230   2677  -1101       C  
ATOM    737  O   ASP A  98     -52.403 -65.335 -77.648  1.00 71.46           O  
ANISOU  737  O   ASP A  98    14059   5782   7309   1245   2613   -993       O  
ATOM    738  CB  ASP A  98     -51.721 -67.605 -79.589  1.00 91.44           C  
ANISOU  738  CB  ASP A  98    17151   7868   9723   1349   3115  -1414       C  
ATOM    739  CG  ASP A  98     -50.828 -68.432 -78.681  1.00 97.83           C  
ANISOU  739  CG  ASP A  98    17856   8507  10808   1627   3279  -1311       C  
ATOM    740  OD1 ASP A  98     -51.363 -69.138 -77.799  1.00101.42           O  
ANISOU  740  OD1 ASP A  98    18346   8781  11409   1625   3202  -1257       O  
ATOM    741  OD2 ASP A  98     -49.591 -68.380 -78.850  1.00 99.31           O  
ANISOU  741  OD2 ASP A  98    17924   8742  11066   1848   3484  -1281       O  
ATOM    742  N   GLN A  99     -53.058 -67.175 -76.504  1.00 75.06           N  
ANISOU  742  N   GLN A  99    14659   5850   8011   1281   2646  -1010       N  
ATOM    743  CA  GLN A  99     -52.874 -66.545 -75.200  1.00 73.87           C  
ANISOU  743  CA  GLN A  99    14237   5832   8000   1359   2519   -779       C  
ATOM    744  C   GLN A  99     -51.410 -66.203 -74.949  1.00 70.87           C  
ANISOU  744  C   GLN A  99    13654   5557   7715   1612   2640   -648       C  
ATOM    745  O   GLN A  99     -51.098 -65.163 -74.358  1.00 69.39           O  
ANISOU  745  O   GLN A  99    13223   5592   7551   1630   2524   -497       O  
ATOM    746  CB  GLN A  99     -53.414 -67.461 -74.099  1.00 78.97           C  
ANISOU  746  CB  GLN A  99    14936   6270   8800   1355   2489   -711       C  
ATOM    747  CG  GLN A  99     -52.982 -67.084 -72.686  1.00 80.25           C  
ANISOU  747  CG  GLN A  99    14867   6521   9102   1488   2405   -469       C  
ATOM    748  CD  GLN A  99     -53.436 -65.693 -72.278  1.00 82.65           C  
ANISOU  748  CD  GLN A  99    14953   7109   9341   1359   2195   -380       C  
ATOM    749  OE1 GLN A  99     -54.439 -65.180 -72.779  1.00 85.34           O  
ANISOU  749  OE1 GLN A  99    15326   7535   9566   1148   2074   -481       O  
ATOM    750  NE2 GLN A  99     -52.694 -65.073 -71.365  1.00 79.92           N  
ANISOU  750  NE2 GLN A  99    14385   6909   9073   1494   2142   -195       N  
ATOM    751  N   GLY A 100     -50.497 -67.059 -75.398  1.00 73.76           N  
ANISOU  751  N   GLY A 100    14108   5770   8148   1807   2878   -717       N  
ATOM    752  CA  GLY A 100     -49.085 -66.851 -75.152  1.00 74.69           C  
ANISOU  752  CA  GLY A 100    13997   5989   8393   2063   3003   -609       C  
ATOM    753  C   GLY A 100     -48.388 -65.993 -76.188  1.00 76.32           C  
ANISOU  753  C   GLY A 100    14124   6404   8471   2045   3120   -678       C  
ATOM    754  O   GLY A 100     -47.156 -65.983 -76.256  1.00 78.33           O  
ANISOU  754  O   GLY A 100    14206   6724   8832   2249   3292   -646       O  
ATOM    755  N   SER A 101     -49.159 -65.269 -76.991  1.00 75.21           N  
ANISOU  755  N   SER A 101    14103   6369   8104   1802   3028   -767       N  
ATOM    756  CA  SER A 101     -48.600 -64.430 -78.044  1.00 79.73           C  
ANISOU  756  CA  SER A 101    14664   7120   8508   1749   3141   -826       C  
ATOM    757  C   SER A 101     -47.665 -63.378 -77.456  1.00 79.60           C  
ANISOU  757  C   SER A 101    14311   7343   8589   1824   3120   -649       C  
ATOM    758  O   SER A 101     -48.120 -62.514 -76.692  1.00 68.25           O  
ANISOU  758  O   SER A 101    12733   6036   7163   1727   2886   -512       O  
ATOM    759  CB  SER A 101     -49.720 -63.754 -78.833  1.00 77.59           C  
ANISOU  759  CB  SER A 101    14586   6922   7973   1478   2973   -908       C  
ATOM    760  OG  SER A 101     -49.199 -62.837 -79.778  1.00 77.76           O  
ANISOU  760  OG  SER A 101    14621   7116   7810   1415   3065   -928       O  
ATOM    761  N   PRO A 102     -46.366 -63.413 -77.771  1.00 82.48           N  
ANISOU  761  N   PRO A 102    14531   7774   9035   1988   3363   -659       N  
ATOM    762  CA  PRO A 102     -45.468 -62.372 -77.241  1.00 81.41           C  
ANISOU  762  CA  PRO A 102    14056   7883   8993   2022   3338   -507       C  
ATOM    763  C   PRO A 102     -45.801 -60.986 -77.762  1.00 80.71           C  
ANISOU  763  C   PRO A 102    13992   7981   8693   1779   3241   -479       C  
ATOM    764  O   PRO A 102     -45.777 -60.012 -76.996  1.00 76.98           O  
ANISOU  764  O   PRO A 102    13318   7663   8269   1715   3064   -333       O  
ATOM    765  CB  PRO A 102     -44.081 -62.842 -77.699  1.00 84.00           C  
ANISOU  765  CB  PRO A 102    14244   8227   9444   2233   3660   -573       C  
ATOM    766  CG  PRO A 102     -44.347 -63.707 -78.893  1.00 84.89           C  
ANISOU  766  CG  PRO A 102    14695   8150   9408   2225   3878   -789       C  
ATOM    767  CD  PRO A 102     -45.659 -64.383 -78.624  1.00 83.14           C  
ANISOU  767  CD  PRO A 102    14739   7717   9134   2141   3681   -824       C  
ATOM    768  N   GLU A 103     -46.117 -60.871 -79.053  1.00 86.06           N  
ANISOU  768  N   GLU A 103    14941   8636   9123   1643   3350   -617       N  
ATOM    769  CA  GLU A 103     -46.528 -59.584 -79.597  1.00 90.02           C  
ANISOU  769  CA  GLU A 103    15523   9280   9398   1420   3238   -577       C  
ATOM    770  C   GLU A 103     -47.837 -59.113 -78.979  1.00 87.28           C  
ANISOU  770  C   GLU A 103    15224   8926   9013   1293   2889   -501       C  
ATOM    771  O   GLU A 103     -48.024 -57.910 -78.767  1.00 91.96           O  
ANISOU  771  O   GLU A 103    15740   9651   9549   1177   2735   -390       O  
ATOM    772  CB  GLU A 103     -46.659 -59.673 -81.118  1.00101.51           C  
ANISOU  772  CB  GLU A 103    17307  10697  10565   1310   3409   -738       C  
ATOM    773  CG  GLU A 103     -45.607 -60.546 -81.798  1.00114.13           C  
ANISOU  773  CG  GLU A 103    18931  12235  12198   1455   3787   -879       C  
ATOM    774  CD  GLU A 103     -44.242 -59.883 -81.898  1.00121.02           C  
ANISOU  774  CD  GLU A 103    19544  13289  13149   1498   4029   -820       C  
ATOM    775  OE1 GLU A 103     -44.036 -58.820 -81.275  1.00121.65           O  
ANISOU  775  OE1 GLU A 103    19399  13528  13294   1426   3892   -659       O  
ATOM    776  OE2 GLU A 103     -43.373 -60.429 -82.610  1.00125.42           O  
ANISOU  776  OE2 GLU A 103    20121  13827  13707   1595   4370   -948       O  
ATOM    777  N   GLY A 104     -48.749 -60.041 -78.680  1.00 80.68           N  
ANISOU  777  N   GLY A 104    14511   7928   8216   1308   2777   -566       N  
ATOM    778  CA  GLY A 104     -49.988 -59.655 -78.025  1.00 75.88           C  
ANISOU  778  CA  GLY A 104    13905   7323   7604   1193   2472   -506       C  
ATOM    779  C   GLY A 104     -49.756 -59.055 -76.652  1.00 71.75           C  
ANISOU  779  C   GLY A 104    13091   6900   7270   1247   2339   -328       C  
ATOM    780  O   GLY A 104     -50.338 -58.024 -76.307  1.00 67.82           O  
ANISOU  780  O   GLY A 104    12538   6502   6728   1136   2138   -248       O  
ATOM    781  N   LYS A 105     -48.894 -59.689 -75.855  1.00 71.09           N  
ANISOU  781  N   LYS A 105    12828   6788   7397   1426   2444   -268       N  
ATOM    782  CA  LYS A 105     -48.567 -59.166 -74.532  1.00 71.38           C  
ANISOU  782  CA  LYS A 105    12597   6930   7594   1479   2315   -103       C  
ATOM    783  C   LYS A 105     -47.851 -57.824 -74.633  1.00 67.20           C  
ANISOU  783  C   LYS A 105    11901   6605   7026   1410   2317    -24       C  
ATOM    784  O   LYS A 105     -48.206 -56.861 -73.936  1.00 62.64           O  
ANISOU  784  O   LYS A 105    11226   6124   6451   1319   2129     72       O  
ATOM    785  CB  LYS A 105     -47.710 -60.186 -73.779  1.00 78.64           C  
ANISOU  785  CB  LYS A 105    13378   7775   8726   1707   2419    -54       C  
ATOM    786  CG  LYS A 105     -47.352 -59.801 -72.354  1.00 84.65           C  
ANISOU  786  CG  LYS A 105    13885   8643   9636   1774   2267    115       C  
ATOM    787  CD  LYS A 105     -46.503 -60.886 -71.702  1.00 91.42           C  
ANISOU  787  CD  LYS A 105    14632   9414  10688   2028   2352    171       C  
ATOM    788  CE  LYS A 105     -46.192 -60.558 -70.251  1.00 91.74           C  
ANISOU  788  CE  LYS A 105    14451   9562  10843   2091   2168    344       C  
ATOM    789  NZ  LYS A 105     -45.404 -59.303 -70.125  1.00 90.39           N  
ANISOU  789  NZ  LYS A 105    14022   9644  10678   2026   2127    401       N  
ATOM    790  N   ARG A 106     -46.847 -57.741 -75.512  1.00 68.96           N  
ANISOU  790  N   ARG A 106    12104   6886   7214   1440   2547    -74       N  
ATOM    791  CA  ARG A 106     -46.064 -56.517 -75.647  1.00 69.31           C  
ANISOU  791  CA  ARG A 106    11990   7112   7231   1352   2590     -5       C  
ATOM    792  C   ARG A 106     -46.939 -55.346 -76.073  1.00 66.12           C  
ANISOU  792  C   ARG A 106    11753   6743   6626   1142   2431     17       C  
ATOM    793  O   ARG A 106     -46.901 -54.274 -75.460  1.00 64.76           O  
ANISOU  793  O   ARG A 106    11454   6673   6481   1058   2298    121       O  
ATOM    794  CB  ARG A 106     -44.926 -56.726 -76.647  1.00 77.22           C  
ANISOU  794  CB  ARG A 106    12969   8158   8213   1400   2908    -86       C  
ATOM    795  CG  ARG A 106     -43.975 -55.541 -76.758  1.00 85.68           C  
ANISOU  795  CG  ARG A 106    13848   9420   9286   1293   2997    -18       C  
ATOM    796  CD  ARG A 106     -42.977 -55.711 -77.898  1.00 93.57           C  
ANISOU  796  CD  ARG A 106    14858  10464  10230   1302   3348   -118       C  
ATOM    797  NE  ARG A 106     -43.593 -55.522 -79.210  1.00 97.84           N  
ANISOU  797  NE  ARG A 106    15771  10932  10470   1154   3428   -206       N  
ATOM    798  CZ  ARG A 106     -43.738 -54.340 -79.803  1.00 99.65           C  
ANISOU  798  CZ  ARG A 106    16139  11226  10496    943   3412   -158       C  
ATOM    799  NH1 ARG A 106     -43.316 -53.236 -79.200  1.00 99.63           N  
ANISOU  799  NH1 ARG A 106    15932  11350  10574    840   3337    -35       N  
ATOM    800  NH2 ARG A 106     -44.308 -54.260 -80.998  1.00 99.55           N  
ANISOU  800  NH2 ARG A 106    16490  11144  10191    829   3464   -231       N  
ATOM    801  N   LYS A 107     -47.737 -55.531 -77.128  1.00 66.45           N  
ANISOU  801  N   LYS A 107    12091   6695   6461   1062   2433    -83       N  
ATOM    802  CA  LYS A 107     -48.582 -54.439 -77.602  1.00 66.58           C  
ANISOU  802  CA  LYS A 107    12279   6738   6282    894   2261    -54       C  
ATOM    803  C   LYS A 107     -49.723 -54.155 -76.636  1.00 62.45           C  
ANISOU  803  C   LYS A 107    11711   6191   5826    870   1967      1       C  
ATOM    804  O   LYS A 107     -50.216 -53.021 -76.580  1.00 58.48           O  
ANISOU  804  O   LYS A 107    11237   5733   5248    770   1805     69       O  
ATOM    805  CB  LYS A 107     -49.122 -54.755 -78.996  1.00 73.87           C  
ANISOU  805  CB  LYS A 107    13532   7585   6950    823   2314   -176       C  
ATOM    806  CG  LYS A 107     -48.033 -55.059 -80.013  1.00 80.90           C  
ANISOU  806  CG  LYS A 107    14499   8493   7745    837   2642   -252       C  
ATOM    807  CD  LYS A 107     -48.595 -55.230 -81.412  1.00 86.98           C  
ANISOU  807  CD  LYS A 107    15638   9201   8209    740   2676   -370       C  
ATOM    808  CE  LYS A 107     -48.539 -53.924 -82.181  1.00 90.84           C  
ANISOU  808  CE  LYS A 107    16287   9768   8459    583   2661   -289       C  
ATOM    809  NZ  LYS A 107     -47.147 -53.396 -82.237  1.00 92.44           N  
ANISOU  809  NZ  LYS A 107    16328  10074   8720    566   2941   -229       N  
ATOM    810  N   LEU A 108     -50.152 -55.161 -75.868  1.00 61.39           N  
ANISOU  810  N   LEU A 108    11516   5976   5833    961   1911    -27       N  
ATOM    811  CA  LEU A 108     -51.170 -54.929 -74.849  1.00 56.66           C  
ANISOU  811  CA  LEU A 108    10849   5367   5312    933   1674     21       C  
ATOM    812  C   LEU A 108     -50.650 -53.990 -73.768  1.00 55.68           C  
ANISOU  812  C   LEU A 108    10497   5355   5302    935   1606    152       C  
ATOM    813  O   LEU A 108     -51.322 -53.018 -73.401  1.00 53.80           O  
ANISOU  813  O   LEU A 108    10252   5153   5037    854   1431    197       O  
ATOM    814  CB  LEU A 108     -51.621 -56.255 -74.236  1.00 57.91           C  
ANISOU  814  CB  LEU A 108    11006   5405   5592   1012   1672    -28       C  
ATOM    815  CG  LEU A 108     -52.710 -56.125 -73.164  1.00 54.81           C  
ANISOU  815  CG  LEU A 108    10547   5001   5277    968   1466      9       C  
ATOM    816  CD1 LEU A 108     -54.069 -55.878 -73.798  1.00 54.38           C  
ANISOU  816  CD1 LEU A 108    10639   4921   5101    846   1308    -82       C  
ATOM    817  CD2 LEU A 108     -52.752 -57.345 -72.264  1.00 58.85           C  
ANISOU  817  CD2 LEU A 108    11020   5403   5936   1055   1510     16       C  
ATOM    818  N   LEU A 109     -49.449 -54.261 -73.250  1.00 60.96           N  
ANISOU  818  N   LEU A 109    10978   6080   6104   1031   1735    205       N  
ATOM    819  CA  LEU A 109     -48.890 -53.395 -72.215  1.00 61.41           C  
ANISOU  819  CA  LEU A 109    10815   6256   6261   1016   1658    316       C  
ATOM    820  C   LEU A 109     -48.501 -52.032 -72.779  1.00 65.79           C  
ANISOU  820  C   LEU A 109    11382   6898   6715    881   1676    348       C  
ATOM    821  O   LEU A 109     -48.785 -50.994 -72.165  1.00 62.78           O  
ANISOU  821  O   LEU A 109    10956   6561   6338    796   1531    408       O  
ATOM    822  CB  LEU A 109     -47.685 -54.070 -71.560  1.00 59.24           C  
ANISOU  822  CB  LEU A 109    10317   6035   6154   1161   1767    361       C  
ATOM    823  CG  LEU A 109     -47.958 -55.372 -70.800  1.00 58.97           C  
ANISOU  823  CG  LEU A 109    10279   5896   6232   1309   1739    367       C  
ATOM    824  CD1 LEU A 109     -46.668 -55.951 -70.236  1.00 57.70           C  
ANISOU  824  CD1 LEU A 109     9894   5794   6234   1483   1828    427       C  
ATOM    825  CD2 LEU A 109     -48.979 -55.150 -69.694  1.00 54.24           C  
ANISOU  825  CD2 LEU A 109     9692   5275   5640   1254   1530    417       C  
ATOM    826  N   ASP A 110     -47.857 -52.017 -73.951  1.00 72.30           N  
ANISOU  826  N   ASP A 110    12291   7735   7444    852   1869    306       N  
ATOM    827  CA  ASP A 110     -47.408 -50.762 -74.550  1.00 80.35           C  
ANISOU  827  CA  ASP A 110    13353   8820   8356    706   1923    347       C  
ATOM    828  C   ASP A 110     -48.584 -49.847 -74.867  1.00 76.33           C  
ANISOU  828  C   ASP A 110    13066   8245   7692    599   1731    365       C  
ATOM    829  O   ASP A 110     -48.611 -48.687 -74.442  1.00 72.29           O  
ANISOU  829  O   ASP A 110    12522   7760   7184    507   1631    438       O  
ATOM    830  CB  ASP A 110     -46.591 -51.042 -75.811  1.00 89.81           C  
ANISOU  830  CB  ASP A 110    14639  10033   9452    690   2196    287       C  
ATOM    831  CG  ASP A 110     -45.101 -51.105 -75.539  1.00 96.05           C  
ANISOU  831  CG  ASP A 110    15143  10951  10401    724   2400    305       C  
ATOM    832  OD1 ASP A 110     -44.716 -51.452 -74.402  1.00 98.76           O  
ANISOU  832  OD1 ASP A 110    15226  11352  10946    828   2326    343       O  
ATOM    833  OD2 ASP A 110     -44.316 -50.804 -76.462  1.00101.56           O  
ANISOU  833  OD2 ASP A 110    15870  11700  11017    644   2632    280       O  
ATOM    834  N   GLY A 111     -49.563 -50.347 -75.625  1.00 74.01           N  
ANISOU  834  N   GLY A 111    12996   7860   7264    614   1670    294       N  
ATOM    835  CA  GLY A 111     -50.751 -49.552 -75.885  1.00 69.10           C  
ANISOU  835  CA  GLY A 111    12552   7184   6518    549   1452    310       C  
ATOM    836  C   GLY A 111     -51.518 -49.224 -74.621  1.00 65.24           C  
ANISOU  836  C   GLY A 111    11924   6693   6172    575   1242    343       C  
ATOM    837  O   GLY A 111     -52.166 -48.175 -74.535  1.00 63.71           O  
ANISOU  837  O   GLY A 111    11795   6476   5934    526   1082    386       O  
ATOM    838  N   ALA A 112     -51.447 -50.108 -73.623  1.00 63.17           N  
ANISOU  838  N   ALA A 112    11483   6443   6075    659   1249    326       N  
ATOM    839  CA  ALA A 112     -52.105 -49.857 -72.345  1.00 61.51           C  
ANISOU  839  CA  ALA A 112    11146   6240   5986    675   1085    354       C  
ATOM    840  C   ALA A 112     -51.561 -48.598 -71.682  1.00 57.13           C  
ANISOU  840  C   ALA A 112    10489   5747   5472    610   1049    437       C  
ATOM    841  O   ALA A 112     -52.323 -47.703 -71.300  1.00 55.03           O  
ANISOU  841  O   ALA A 112    10254   5455   5200    573    898    451       O  
ATOM    842  CB  ALA A 112     -51.932 -51.069 -71.431  1.00 65.07           C  
ANISOU  842  CB  ALA A 112    11458   6687   6578    769   1129    342       C  
ATOM    843  N   ARG A 113     -50.238 -48.513 -71.528  1.00 58.68           N  
ANISOU  843  N   ARG A 113    10552   6023   5721    594   1189    480       N  
ATOM    844  CA  ARG A 113     -49.652 -47.302 -70.963  1.00 62.26           C  
ANISOU  844  CA  ARG A 113    10914   6534   6208    497   1161    544       C  
ATOM    845  C   ARG A 113     -49.790 -46.120 -71.917  1.00 59.85           C  
ANISOU  845  C   ARG A 113    10806   6172   5762    381   1162    569       C  
ATOM    846  O   ARG A 113     -49.880 -44.965 -71.474  1.00 59.14           O  
ANISOU  846  O   ARG A 113    10731   6062   5678    297   1076    609       O  
ATOM    847  CB  ARG A 113     -48.184 -47.552 -70.621  1.00 68.58           C  
ANISOU  847  CB  ARG A 113    11491   7454   7111    498   1305    572       C  
ATOM    848  CG  ARG A 113     -47.494 -46.411 -69.900  1.00 74.20           C  
ANISOU  848  CG  ARG A 113    12072   8244   7876    374   1268    620       C  
ATOM    849  CD  ARG A 113     -46.069 -46.790 -69.542  1.00 80.02           C  
ANISOU  849  CD  ARG A 113    12538   9128   8736    388   1384    636       C  
ATOM    850  NE  ARG A 113     -45.398 -47.459 -70.652  1.00 85.61           N  
ANISOU  850  NE  ARG A 113    13245   9855   9427    432   1602    608       N  
ATOM    851  CZ  ARG A 113     -44.802 -46.824 -71.656  1.00 91.63           C  
ANISOU  851  CZ  ARG A 113    14071  10633  10113    303   1771    606       C  
ATOM    852  NH1 ARG A 113     -44.791 -45.498 -71.694  1.00 91.73           N  
ANISOU  852  NH1 ARG A 113    14162  10626  10064    118   1735    642       N  
ATOM    853  NH2 ARG A 113     -44.218 -47.516 -72.624  1.00 95.61           N  
ANISOU  853  NH2 ARG A 113    14577  11157  10594    352   1992    564       N  
ATOM    854  N   GLY A 114     -49.837 -46.395 -73.222  1.00 59.21           N  
ANISOU  854  N   GLY A 114    10908   6049   5539    375   1255    547       N  
ATOM    855  CA  GLY A 114     -49.831 -45.335 -74.211  1.00 58.51           C  
ANISOU  855  CA  GLY A 114    11043   5902   5287    264   1276    593       C  
ATOM    856  C   GLY A 114     -51.151 -44.605 -74.326  1.00 59.24           C  
ANISOU  856  C   GLY A 114    11321   5887   5301    279   1050    608       C  
ATOM    857  O   GLY A 114     -51.176 -43.429 -74.694  1.00 61.53           O  
ANISOU  857  O   GLY A 114    11770   6106   5501    196   1015    675       O  
ATOM    858  N   VAL A 115     -52.264 -45.284 -74.040  1.00 55.37           N  
ANISOU  858  N   VAL A 115    10813   5376   4849    386    899    546       N  
ATOM    859  CA  VAL A 115     -53.543 -44.579 -74.065  1.00 55.90           C  
ANISOU  859  CA  VAL A 115    10998   5361   4880    421    674    549       C  
ATOM    860  C   VAL A 115     -53.676 -43.673 -72.846  1.00 60.07           C  
ANISOU  860  C   VAL A 115    11404   5874   5545    412    587    577       C  
ATOM    861  O   VAL A 115     -54.235 -42.572 -72.933  1.00 58.44           O  
ANISOU  861  O   VAL A 115    11322   5578   5305    410    463    614       O  
ATOM    862  CB  VAL A 115     -54.715 -45.572 -74.175  1.00 52.47           C  
ANISOU  862  CB  VAL A 115    10556   4924   4455    514    549    456       C  
ATOM    863  CG1 VAL A 115     -54.694 -46.275 -75.528  1.00 53.86           C  
ANISOU  863  CG1 VAL A 115    10919   5092   4453    504    607    416       C  
ATOM    864  CG2 VAL A 115     -54.686 -46.580 -73.043  1.00 68.26           C  
ANISOU  864  CG2 VAL A 115    12326   6979   6629    559    593    402       C  
ATOM    865  N   ILE A 116     -53.150 -44.109 -71.699  1.00 61.78           N  
ANISOU  865  N   ILE A 116    11396   6170   5908    413    649    559       N  
ATOM    866  CA  ILE A 116     -53.199 -43.290 -70.492  1.00 60.96           C  
ANISOU  866  CA  ILE A 116    11190   6062   5910    387    579    569       C  
ATOM    867  C   ILE A 116     -52.309 -42.063 -70.651  1.00 60.84           C  
ANISOU  867  C   ILE A 116    11248   6012   5857    257    643    637       C  
ATOM    868  O   ILE A 116     -52.774 -40.918 -70.569  1.00 64.55           O  
ANISOU  868  O   ILE A 116    11841   6375   6312    233    549    658       O  
ATOM    869  CB  ILE A 116     -52.792 -44.120 -69.263  1.00 60.65           C  
ANISOU  869  CB  ILE A 116    10920   6126   5998    412    619    543       C  
ATOM    870  CG1 ILE A 116     -53.676 -45.362 -69.138  1.00 62.32           C  
ANISOU  870  CG1 ILE A 116    11092   6343   6243    515    580    482       C  
ATOM    871  CG2 ILE A 116     -52.879 -43.280 -67.999  1.00 48.82           C  
ANISOU  871  CG2 ILE A 116     9343   4629   4576    373    543    538       C  
ATOM    872  CD1 ILE A 116     -53.274 -46.286 -68.005  1.00 58.21           C  
ANISOU  872  CD1 ILE A 116    10394   5899   5824    550    625    479       C  
ATOM    873  N   ASN A 117     -51.011 -42.286 -70.887  1.00 62.07           N  
ANISOU  873  N   ASN A 117    11325   6250   6008    169    814    666       N  
ATOM    874  CA  ASN A 117     -50.093 -41.163 -71.054  1.00 64.14           C  
ANISOU  874  CA  ASN A 117    11639   6489   6244      6    902    721       C  
ATOM    875  C   ASN A 117     -50.492 -40.298 -72.244  1.00 64.67           C  
ANISOU  875  C   ASN A 117    12014   6408   6150    -39    890    780       C  
ATOM    876  O   ASN A 117     -50.409 -39.064 -72.183  1.00 71.04           O  
ANISOU  876  O   ASN A 117    12950   7104   6936   -140    867    827       O  
ATOM    877  CB  ASN A 117     -48.661 -41.674 -71.214  1.00 68.53           C  
ANISOU  877  CB  ASN A 117    12020   7182   6836    -74   1104    729       C  
ATOM    878  CG  ASN A 117     -48.108 -42.274 -69.934  1.00 69.36           C  
ANISOU  878  CG  ASN A 117    11826   7429   7100    -40   1085    696       C  
ATOM    879  OD1 ASN A 117     -48.550 -41.937 -68.835  1.00 71.81           O  
ANISOU  879  OD1 ASN A 117    12081   7731   7474    -29    945    678       O  
ATOM    880  ND2 ASN A 117     -47.131 -43.162 -70.070  1.00 66.64           N  
ANISOU  880  ND2 ASN A 117    11295   7212   6812    -13   1225    689       N  
ATOM    881  N   GLY A 118     -50.949 -40.929 -73.327  1.00 64.53           N  
ANISOU  881  N   GLY A 118    12141   6373   6005     36    895    779       N  
ATOM    882  CA  GLY A 118     -51.317 -40.182 -74.519  1.00 63.77           C  
ANISOU  882  CA  GLY A 118    12366   6145   5719      4    866    850       C  
ATOM    883  C   GLY A 118     -52.532 -39.299 -74.314  1.00 61.83           C  
ANISOU  883  C   GLY A 118    12264   5754   5473     92    631    871       C  
ATOM    884  O   GLY A 118     -52.546 -38.142 -74.746  1.00 61.55           O  
ANISOU  884  O   GLY A 118    12463   5574   5350     30    605    956       O  
ATOM    885  N   MET A 119     -53.574 -39.830 -73.669  1.00 60.78           N  
ANISOU  885  N   MET A 119    11999   5650   5445    240    468    794       N  
ATOM    886  CA  MET A 119     -54.715 -38.990 -73.315  1.00 64.57           C  
ANISOU  886  CA  MET A 119    12552   6010   5973    342    260    794       C  
ATOM    887  C   MET A 119     -54.284 -37.849 -72.405  1.00 63.38           C  
ANISOU  887  C   MET A 119    12386   5775   5919    258    286    815       C  
ATOM    888  O   MET A 119     -54.710 -36.697 -72.591  1.00 65.17           O  
ANISOU  888  O   MET A 119    12815   5831   6117    279    193    868       O  
ATOM    889  CB  MET A 119     -55.806 -39.826 -72.646  1.00 67.56           C  
ANISOU  889  CB  MET A 119    12734   6460   6474    486    130    688       C  
ATOM    890  CG  MET A 119     -56.666 -40.621 -73.618  1.00 76.35           C  
ANISOU  890  CG  MET A 119    13918   7600   7490    580     19    656       C  
ATOM    891  SD  MET A 119     -57.851 -41.697 -72.784  1.00 80.02           S  
ANISOU  891  SD  MET A 119    14125   8161   8120    694    -89    518       S  
ATOM    892  CE  MET A 119     -59.386 -41.175 -73.546  1.00 87.12           C  
ANISOU  892  CE  MET A 119    15140   8987   8975    839   -369    505       C  
ATOM    893  N   SER A 120     -53.421 -38.147 -71.428  1.00 58.90           N  
ANISOU  893  N   SER A 120    11597   5320   5463    164    406    772       N  
ATOM    894  CA  SER A 120     -52.916 -37.102 -70.544  1.00 62.88           C  
ANISOU  894  CA  SER A 120    12085   5761   6045     50    432    773       C  
ATOM    895  C   SER A 120     -52.271 -35.970 -71.335  1.00 65.88           C  
ANISOU  895  C   SER A 120    12718   5995   6320   -101    513    871       C  
ATOM    896  O   SER A 120     -52.576 -34.794 -71.114  1.00 66.90           O  
ANISOU  896  O   SER A 120    13013   5943   6463   -120    447    892       O  
ATOM    897  CB  SER A 120     -51.919 -37.685 -69.546  1.00 63.47           C  
ANISOU  897  CB  SER A 120    11886   6010   6221    -45    539    724       C  
ATOM    898  OG  SER A 120     -51.298 -36.645 -68.809  1.00 54.76           O  
ANISOU  898  OG  SER A 120    10782   4855   5168   -197    566    717       O  
ATOM    899  N   ASP A 121     -51.372 -36.306 -72.265  1.00 67.56           N  
ANISOU  899  N   ASP A 121    12978   6268   6424   -213    674    928       N  
ATOM    900  CA  ASP A 121     -50.711 -35.267 -73.050  1.00 73.75           C  
ANISOU  900  CA  ASP A 121    14017   6914   7092   -389    787   1028       C  
ATOM    901  C   ASP A 121     -51.706 -34.524 -73.933  1.00 72.14           C  
ANISOU  901  C   ASP A 121    14170   6492   6749   -284    643   1117       C  
ATOM    902  O   ASP A 121     -51.615 -33.297 -74.089  1.00 75.86           O  
ANISOU  902  O   ASP A 121    14886   6758   7178   -375    645   1193       O  
ATOM    903  CB  ASP A 121     -49.593 -35.877 -73.895  1.00 79.68           C  
ANISOU  903  CB  ASP A 121    14731   7794   7750   -523   1018   1058       C  
ATOM    904  CG  ASP A 121     -48.515 -36.527 -73.053  1.00 80.29           C  
ANISOU  904  CG  ASP A 121    14442   8084   7981   -612   1150    982       C  
ATOM    905  OD1 ASP A 121     -48.333 -36.109 -71.891  1.00 82.85           O  
ANISOU  905  OD1 ASP A 121    14610   8425   8446   -665   1093    934       O  
ATOM    906  OD2 ASP A 121     -47.846 -37.454 -73.556  1.00 85.70           O  
ANISOU  906  OD2 ASP A 121    15003   8918   8643   -621   1306    968       O  
ATOM    907  N   LEU A 122     -52.664 -35.254 -74.514  1.00 67.38           N  
ANISOU  907  N   LEU A 122    13604   5924   6074    -93    506   1108       N  
ATOM    908  CA  LEU A 122     -53.675 -34.634 -75.366  1.00 66.63           C  
ANISOU  908  CA  LEU A 122    13822   5649   5845     39    322   1192       C  
ATOM    909  C   LEU A 122     -54.428 -33.541 -74.620  1.00 66.80           C  
ANISOU  909  C   LEU A 122    13906   5484   5990    137    160   1189       C  
ATOM    910  O   LEU A 122     -54.614 -32.434 -75.140  1.00 68.60           O  
ANISOU  910  O   LEU A 122    14451   5483   6129    139    102   1300       O  
ATOM    911  CB  LEU A 122     -54.646 -35.694 -75.883  1.00 66.17           C  
ANISOU  911  CB  LEU A 122    13712   5699   5731    225    168   1142       C  
ATOM    912  CG  LEU A 122     -54.613 -35.961 -77.386  1.00 68.98           C  
ANISOU  912  CG  LEU A 122    14345   6046   5820    209    180   1225       C  
ATOM    913  CD1 LEU A 122     -55.781 -36.842 -77.795  1.00 72.15           C  
ANISOU  913  CD1 LEU A 122    14702   6530   6181    397    -35   1158       C  
ATOM    914  CD2 LEU A 122     -54.633 -34.652 -78.149  1.00 68.28           C  
ANISOU  914  CD2 LEU A 122    14656   5725   5563    171    134   1385       C  
ATOM    915  N   LEU A 123     -54.873 -33.832 -73.397  1.00 61.88           N  
ANISOU  915  N   LEU A 123    13004   4941   5568    225     97   1065       N  
ATOM    916  CA  LEU A 123     -55.515 -32.789 -72.605  1.00 66.48           C  
ANISOU  916  CA  LEU A 123    13636   5348   6278    312    -16   1036       C  
ATOM    917  C   LEU A 123     -54.513 -31.758 -72.093  1.00 66.46           C  
ANISOU  917  C   LEU A 123    13728   5218   6307     93    131   1057       C  
ATOM    918  O   LEU A 123     -54.895 -30.608 -71.834  1.00 69.24           O  
ANISOU  918  O   LEU A 123    14268   5336   6704    132     63   1074       O  
ATOM    919  CB  LEU A 123     -56.280 -33.418 -71.440  1.00 65.63           C  
ANISOU  919  CB  LEU A 123    13214   5370   6353    449    -96    886       C  
ATOM    920  CG  LEU A 123     -57.426 -34.353 -71.841  1.00 61.75           C  
ANISOU  920  CG  LEU A 123    12613   4986   5863    653   -254    842       C  
ATOM    921  CD1 LEU A 123     -57.891 -35.195 -70.661  1.00 58.32           C  
ANISOU  921  CD1 LEU A 123    11848   4717   5594    712   -253    696       C  
ATOM    922  CD2 LEU A 123     -58.587 -33.555 -72.418  1.00 60.73           C  
ANISOU  922  CD2 LEU A 123    12676   4677   5720    860   -473    889       C  
ATOM    923  N   MET A 124     -53.236 -32.134 -71.982  1.00 65.25           N  
ANISOU  923  N   MET A 124    13448   5206   6137   -136    331   1052       N  
ATOM    924  CA  MET A 124     -52.244 -31.267 -71.357  1.00 63.32           C  
ANISOU  924  CA  MET A 124    13222   4887   5948   -375    464   1041       C  
ATOM    925  C   MET A 124     -51.749 -30.164 -72.283  1.00 67.08           C  
ANISOU  925  C   MET A 124    14066   5129   6293   -538    554   1177       C  
ATOM    926  O   MET A 124     -51.350 -29.102 -71.796  1.00 69.16           O  
ANISOU  926  O   MET A 124    14449   5220   6610   -694    606   1170       O  
ATOM    927  CB  MET A 124     -51.055 -32.089 -70.858  1.00 65.47           C  
ANISOU  927  CB  MET A 124    13180   5423   6275   -553    626    979       C  
ATOM    928  CG  MET A 124     -51.123 -32.420 -69.381  1.00 67.37           C  
ANISOU  928  CG  MET A 124    13131   5795   6673   -525    571    843       C  
ATOM    929  SD  MET A 124     -51.442 -30.966 -68.362  1.00 76.06           S  
ANISOU  929  SD  MET A 124    14381   6658   7860   -580    503    775       S  
ATOM    930  CE  MET A 124     -50.006 -29.959 -68.725  1.00 78.90           C  
ANISOU  930  CE  MET A 124    14891   6915   8174   -941    687    836       C  
ATOM    931  N   CYS A 125     -51.735 -30.378 -73.601  1.00 67.19           N  
ANISOU  931  N   CYS A 125    14285   5121   6122   -526    586   1299       N  
ATOM    932  CA  CYS A 125     -51.376 -29.262 -74.474  1.00 77.77           C  
ANISOU  932  CA  CYS A 125    16032   6204   7315   -674    667   1447       C  
ATOM    933  C   CYS A 125     -52.456 -28.183 -74.447  1.00 79.94           C  
ANISOU  933  C   CYS A 125    16606   6166   7602   -487    463   1503       C  
ATOM    934  O   CYS A 125     -52.149 -26.983 -74.464  1.00 74.17           O  
ANISOU  934  O   CYS A 125    16160   5165   6857   -625    522   1572       O  
ATOM    935  CB  CYS A 125     -51.106 -29.750 -75.900  1.00 83.65           C  
ANISOU  935  CB  CYS A 125    16959   7002   7822   -711    758   1566       C  
ATOM    936  SG  CYS A 125     -52.387 -30.766 -76.659  1.00 90.94           S  
ANISOU  936  SG  CYS A 125    17895   8028   8631   -383    522   1574       S  
ATOM    937  N   ALA A 126     -53.725 -28.593 -74.368  1.00 78.23           N  
ANISOU  937  N   ALA A 126    16317   5976   7431   -172    227   1464       N  
ATOM    938  CA  ALA A 126     -54.808 -27.632 -74.187  1.00 74.54           C  
ANISOU  938  CA  ALA A 126    16055   5238   7029     53     24   1488       C  
ATOM    939  C   ALA A 126     -54.687 -26.915 -72.846  1.00 74.40           C  
ANISOU  939  C   ALA A 126    15939   5115   7215     -9     66   1361       C  
ATOM    940  O   ALA A 126     -54.801 -25.684 -72.773  1.00 75.92           O  
ANISOU  940  O   ALA A 126    16427   4991   7429    -17     50   1411       O  
ATOM    941  CB  ALA A 126     -56.159 -28.342 -74.302  1.00 72.22           C  
ANISOU  941  CB  ALA A 126    15612   5053   6774    388   -225   1441       C  
ATOM    942  N   ASP A 127     -54.456 -27.675 -71.768  1.00 70.94           N  
ANISOU  942  N   ASP A 127    15111   4927   6916    -55    120   1197       N  
ATOM    943  CA  ASP A 127     -54.302 -27.055 -70.453  1.00 69.05           C  
ANISOU  943  CA  ASP A 127    14782   4614   6839   -134    160   1061       C  
ATOM    944  C   ASP A 127     -53.143 -26.063 -70.440  1.00 71.21           C  
ANISOU  944  C   ASP A 127    15267   4713   7076   -462    336   1104       C  
ATOM    945  O   ASP A 127     -53.238 -24.990 -69.832  1.00 72.83           O  
ANISOU  945  O   ASP A 127    15642   4668   7362   -501    335   1053       O  
ATOM    946  CB  ASP A 127     -54.100 -28.131 -69.384  1.00 66.13           C  
ANISOU  946  CB  ASP A 127    13986   4568   6575   -160    195    904       C  
ATOM    947  CG  ASP A 127     -54.087 -27.559 -67.976  1.00 78.96           C  
ANISOU  947  CG  ASP A 127    15527   6137   8337   -218    211    748       C  
ATOM    948  OD1 ASP A 127     -55.172 -27.463 -67.366  1.00 77.41           O  
ANISOU  948  OD1 ASP A 127    15282   5887   8241     12     99    653       O  
ATOM    949  OD2 ASP A 127     -52.995 -27.204 -67.479  1.00 66.70           O  
ANISOU  949  OD2 ASP A 127    13951   4602   6790   -500    340    710       O  
ATOM    950  N   ARG A 128     -52.041 -26.404 -71.114  1.00 74.32           N  
ANISOU  950  N   ARG A 128    15652   5230   7356   -709    502   1185       N  
ATOM    951  CA  ARG A 128     -50.912 -25.486 -71.206  1.00 76.74           C  
ANISOU  951  CA  ARG A 128    16144   5383   7629  -1055    689   1228       C  
ATOM    952  C   ARG A 128     -51.279 -24.239 -71.998  1.00 77.24           C  
ANISOU  952  C   ARG A 128    16714   5038   7597  -1035    664   1380       C  
ATOM    953  O   ARG A 128     -50.821 -23.138 -71.673  1.00 79.55           O  
ANISOU  953  O   ARG A 128    17221   5078   7927  -1244    753   1372       O  
ATOM    954  CB  ARG A 128     -49.711 -26.185 -71.841  1.00 78.14           C  
ANISOU  954  CB  ARG A 128    16174   5801   7713  -1302    890   1278       C  
ATOM    955  CG  ARG A 128     -48.921 -27.064 -70.889  1.00 83.75           C  
ANISOU  955  CG  ARG A 128    16419   6856   8546  -1425    960   1131       C  
ATOM    956  CD  ARG A 128     -47.726 -27.681 -71.590  1.00 90.50           C  
ANISOU  956  CD  ARG A 128    17129   7928   9330  -1645   1174   1180       C  
ATOM    957  NE  ARG A 128     -48.135 -28.597 -72.650  1.00 95.15           N  
ANISOU  957  NE  ARG A 128    17748   8620   9785  -1457   1162   1267       N  
ATOM    958  CZ  ARG A 128     -47.299 -29.160 -73.514  1.00 98.73           C  
ANISOU  958  CZ  ARG A 128    18149   9225  10138  -1591   1357   1322       C  
ATOM    959  NH1 ARG A 128     -46.000 -28.897 -73.449  1.00100.16           N  
ANISOU  959  NH1 ARG A 128    18213   9487  10358  -1913   1581   1303       N  
ATOM    960  NH2 ARG A 128     -47.760 -29.983 -74.446  1.00 99.69           N  
ANISOU  960  NH2 ARG A 128    18330   9424  10123  -1412   1333   1381       N  
ATOM    961  N   SER A 129     -52.097 -24.393 -73.042  1.00 77.77           N  
ANISOU  961  N   SER A 129    16970   5043   7537   -788    533   1512       N  
ATOM    962  CA  SER A 129     -52.583 -23.226 -73.773  1.00 81.12           C  
ANISOU  962  CA  SER A 129    17691   5231   7901   -685    448   1596       C  
ATOM    963  C   SER A 129     -53.362 -22.294 -72.851  1.00 81.98           C  
ANISOU  963  C   SER A 129    17857   5108   8184   -516    323   1499       C  
ATOM    964  O   SER A 129     -53.105 -21.081 -72.805  1.00 84.92           O  
ANISOU  964  O   SER A 129    18448   5241   8577   -633    382   1508       O  
ATOM    965  CB  SER A 129     -53.447 -23.676 -74.954  1.00 81.47           C  
ANISOU  965  CB  SER A 129    17807   5348   7799   -411    273   1704       C  
ATOM    966  OG  SER A 129     -53.906 -22.571 -75.712  1.00 98.79           O  
ANISOU  966  OG  SER A 129    20302   7315   9921   -308    179   1805       O  
ATOM    967  N   GLU A 130     -54.309 -22.853 -72.090  1.00 79.65           N  
ANISOU  967  N   GLU A 130    17366   4878   8021   -245    167   1393       N  
ATOM    968  CA  GLU A 130     -55.105 -22.035 -71.177  1.00 85.86           C  
ANISOU  968  CA  GLU A 130    18177   5462   8982    -60     68   1275       C  
ATOM    969  C   GLU A 130     -54.219 -21.325 -70.159  1.00 85.99           C  
ANISOU  969  C   GLU A 130    18234   5352   9086   -367    241   1157       C  
ATOM    970  O   GLU A 130     -54.354 -20.114 -69.938  1.00 84.08           O  
ANISOU  970  O   GLU A 130    18187   4856   8903   -369    248   1127       O  
ATOM    971  CB  GLU A 130     -56.148 -22.900 -70.469  1.00 84.91           C  
ANISOU  971  CB  GLU A 130    17799   5473   8990    239    -81   1158       C  
ATOM    972  CG  GLU A 130     -57.026 -23.725 -71.399  1.00 87.88           C  
ANISOU  972  CG  GLU A 130    18096   6004   9292    517   -265   1249       C  
ATOM    973  CD  GLU A 130     -57.969 -22.879 -72.237  1.00 98.66           C  
ANISOU  973  CD  GLU A 130    19647   7202  10637    781   -450   1344       C  
ATOM    974  OE1 GLU A 130     -58.217 -21.708 -71.876  1.00102.42           O  
ANISOU  974  OE1 GLU A 130    20269   7433  11211    837   -455   1313       O  
ATOM    975  OE2 GLU A 130     -58.466 -23.391 -73.262  1.00104.23           O  
ANISOU  975  OE2 GLU A 130    20360   8019  11224    933   -595   1449       O  
ATOM    976  N   VAL A 131     -53.297 -22.063 -69.536  1.00 66.51           N  
ANISOU  976  N   VAL A 131    12648   6719   5905  -1655    879    272       N  
ATOM    977  CA  VAL A 131     -52.439 -21.461 -68.518  1.00 62.95           C  
ANISOU  977  CA  VAL A 131    11902   6318   5697  -1386    993    334       C  
ATOM    978  C   VAL A 131     -51.569 -20.368 -69.127  1.00 66.82           C  
ANISOU  978  C   VAL A 131    12464   6911   6015  -1492   1097    345       C  
ATOM    979  O   VAL A 131     -51.328 -19.328 -68.501  1.00 69.53           O  
ANISOU  979  O   VAL A 131    12611   7331   6476  -1376   1021    483       O  
ATOM    980  CB  VAL A 131     -51.595 -22.542 -67.817  1.00 59.89           C  
ANISOU  980  CB  VAL A 131    11392   5824   5539  -1145   1277    172       C  
ATOM    981  CG1 VAL A 131     -50.583 -21.905 -66.878  1.00 56.72           C  
ANISOU  981  CG1 VAL A 131    10696   5495   5361   -886   1372    209       C  
ATOM    982  CG2 VAL A 131     -52.498 -23.494 -67.049  1.00 56.06           C  
ANISOU  982  CG2 VAL A 131    10875   5213   5214  -1059   1162    205       C  
ATOM    983  N   ARG A 132     -51.097 -20.572 -70.360  1.00 72.14           N  
ANISOU  983  N   ARG A 132    13447   7577   6387  -1751   1294    188       N  
ATOM    984  CA  ARG A 132     -50.326 -19.526 -71.029  1.00 73.71           C  
ANISOU  984  CA  ARG A 132    13784   7859   6362  -1935   1423    190       C  
ATOM    985  C   ARG A 132     -51.160 -18.265 -71.226  1.00 73.95           C  
ANISOU  985  C   ARG A 132    13936   7922   6239  -2053   1025    472       C  
ATOM    986  O   ARG A 132     -50.664 -17.148 -71.034  1.00 73.10           O  
ANISOU  986  O   ARG A 132    13774   7867   6135  -2048   1036    574       O  
ATOM    987  CB  ARG A 132     -49.792 -20.028 -72.371  1.00 71.46           C  
ANISOU  987  CB  ARG A 132    13871   7550   5730  -2256   1725    -48       C  
ATOM    988  CG  ARG A 132     -48.571 -20.929 -72.266  1.00 72.65           C  
ANISOU  988  CG  ARG A 132    13864   7678   6063  -2134   2203   -380       C  
ATOM    989  CD  ARG A 132     -47.855 -21.038 -73.604  1.00 79.54           C  
ANISOU  989  CD  ARG A 132    15081   8561   6580  -2502   2578   -642       C  
ATOM    990  NE  ARG A 132     -48.755 -21.456 -74.676  1.00 83.33           N  
ANISOU  990  NE  ARG A 132    16022   8976   6663  -2830   2431   -634       N  
ATOM    991  CZ  ARG A 132     -48.894 -22.712 -75.090  1.00 84.08           C  
ANISOU  991  CZ  ARG A 132    16254   8964   6727  -2881   2587   -862       C  
ATOM    992  NH1 ARG A 132     -48.189 -23.682 -74.525  1.00 82.84           N  
ANISOU  992  NH1 ARG A 132    15819   8727   6931  -2598   2889  -1107       N  
ATOM    993  NH2 ARG A 132     -49.739 -22.998 -76.071  1.00 83.86           N  
ANISOU  993  NH2 ARG A 132    16656   8896   6311  -3212   2418   -848       N  
ATOM    994  N   LYS A 133     -52.433 -18.423 -71.603  1.00 75.02           N  
ANISOU  994  N   LYS A 133    14228   8014   6263  -2153    657    587       N  
ATOM    995  CA  LYS A 133     -53.307 -17.260 -71.744  1.00 79.14           C  
ANISOU  995  CA  LYS A 133    14825   8537   6708  -2203    212    846       C  
ATOM    996  C   LYS A 133     -53.473 -16.525 -70.415  1.00 75.48           C  
ANISOU  996  C   LYS A 133    13945   8103   6632  -1893     84    992       C  
ATOM    997  O   LYS A 133     -53.275 -15.302 -70.332  1.00 80.29           O  
ANISOU  997  O   LYS A 133    14567   8716   7225  -1886    -20   1143       O  
ATOM    998  CB  LYS A 133     -54.666 -17.696 -72.292  1.00 87.05           C  
ANISOU  998  CB  LYS A 133    15975   9500   7600  -2326   -184    895       C  
ATOM    999  CG  LYS A 133     -55.683 -16.574 -72.387  1.00 95.10           C  
ANISOU  999  CG  LYS A 133    17011  10501   8623  -2315   -714   1142       C  
ATOM   1000  CD  LYS A 133     -57.101 -17.116 -72.322  1.00101.56           C  
ANISOU 1000  CD  LYS A 133    17689  11317   9583  -2291  -1098   1143       C  
ATOM   1001  CE  LYS A 133     -57.376 -17.777 -70.976  1.00101.38           C  
ANISOU 1001  CE  LYS A 133    17189  11323  10006  -2029   -953   1057       C  
ATOM   1002  NZ  LYS A 133     -57.216 -16.823 -69.842  1.00 98.10           N  
ANISOU 1002  NZ  LYS A 133    16435  10929   9911  -1761   -960   1179       N  
ATOM   1003  N   MET A 134     -53.837 -17.262 -69.359  1.00 65.39           N  
ANISOU 1003  N   MET A 134    12331   6828   5685  -1660    105    944       N  
ATOM   1004  CA  MET A 134     -54.047 -16.642 -68.051  1.00 65.66           C  
ANISOU 1004  CA  MET A 134    11994   6891   6063  -1398      8   1057       C  
ATOM   1005  C   MET A 134     -52.796 -15.905 -67.584  1.00 65.80           C  
ANISOU 1005  C   MET A 134    11902   6959   6138  -1303    257   1057       C  
ATOM   1006  O   MET A 134     -52.857 -14.728 -67.199  1.00 60.87           O  
ANISOU 1006  O   MET A 134    11186   6348   5593  -1246    116   1199       O  
ATOM   1007  CB  MET A 134     -54.456 -17.704 -67.028  1.00 63.93           C  
ANISOU 1007  CB  MET A 134    11520   6653   6117  -1224     75    976       C  
ATOM   1008  CG  MET A 134     -55.569 -18.623 -67.499  1.00 68.63           C  
ANISOU 1008  CG  MET A 134    12218   7200   6657  -1360    -90    916       C  
ATOM   1009  SD  MET A 134     -56.280 -19.611 -66.168  1.00 70.96           S  
ANISOU 1009  SD  MET A 134    12234   7453   7276  -1207    -46    858       S  
ATOM   1010  CE  MET A 134     -57.686 -20.337 -67.008  1.00 72.41           C  
ANISOU 1010  CE  MET A 134    12544   7610   7359  -1456   -298    782       C  
ATOM   1011  N   VAL A 135     -51.647 -16.587 -67.622  1.00 52.61           N  
ANISOU 1011  N   VAL A 135    10226   5312   4452  -1287    627    876       N  
ATOM   1012  CA  VAL A 135     -50.383 -15.972 -67.227  1.00 55.61           C  
ANISOU 1012  CA  VAL A 135    10459   5764   4907  -1216    878    823       C  
ATOM   1013  C   VAL A 135     -50.092 -14.742 -68.074  1.00 58.49           C  
ANISOU 1013  C   VAL A 135    11072   6142   5009  -1459    860    906       C  
ATOM   1014  O   VAL A 135     -49.538 -13.757 -67.578  1.00 62.06           O  
ANISOU 1014  O   VAL A 135    11391   6640   5550  -1414    906    962       O  
ATOM   1015  CB  VAL A 135     -49.245 -17.010 -67.310  1.00 53.53           C  
ANISOU 1015  CB  VAL A 135    10136   5512   4690  -1162   1259    563       C  
ATOM   1016  CG1 VAL A 135     -47.884 -16.346 -67.153  1.00 53.57           C  
ANISOU 1016  CG1 VAL A 135     9985   5617   4752  -1152   1531    453       C  
ATOM   1017  CG2 VAL A 135     -49.435 -18.080 -66.246  1.00 51.56           C  
ANISOU 1017  CG2 VAL A 135     9658   5207   4725   -880   1243    525       C  
ATOM   1018  N   LYS A 136     -50.469 -14.770 -69.353  1.00 60.18           N  
ANISOU 1018  N   LYS A 136    11688   6302   4874  -1743    782    921       N  
ATOM   1019  CA  LYS A 136     -50.315 -13.590 -70.201  1.00 64.24           C  
ANISOU 1019  CA  LYS A 136    12544   6784   5082  -2008    712   1042       C  
ATOM   1020  C   LYS A 136     -51.089 -12.403 -69.633  1.00 66.15           C  
ANISOU 1020  C   LYS A 136    12701   6968   5464  -1881    324   1302       C  
ATOM   1021  O   LYS A 136     -50.535 -11.306 -69.466  1.00 57.37           O  
ANISOU 1021  O   LYS A 136    11610   5846   4341  -1922    381   1376       O  
ATOM   1022  CB  LYS A 136     -50.771 -13.922 -71.623  1.00 66.17           C  
ANISOU 1022  CB  LYS A 136    13284   6962   4898  -2333    614   1039       C  
ATOM   1023  CG  LYS A 136     -50.876 -12.747 -72.577  1.00 71.03           C  
ANISOU 1023  CG  LYS A 136    14348   7493   5148  -2621    423   1212       C  
ATOM   1024  CD  LYS A 136     -51.351 -13.237 -73.942  1.00 77.24           C  
ANISOU 1024  CD  LYS A 136    15531   8229   5588  -2900    286   1144       C  
ATOM   1025  CE  LYS A 136     -51.708 -12.090 -74.873  1.00 81.13           C  
ANISOU 1025  CE  LYS A 136    16332   8613   5881  -3080    -54   1278       C  
ATOM   1026  NZ  LYS A 136     -52.285 -12.589 -76.158  1.00 84.11           N  
ANISOU 1026  NZ  LYS A 136    17108   8924   5926  -3351   -249   1236       N  
ATOM   1027  N   VAL A 137     -52.368 -12.611 -69.302  1.00 67.27           N  
ANISOU 1027  N   VAL A 137    12725   7066   5768  -1729    -52   1412       N  
ATOM   1028  CA  VAL A 137     -53.166 -11.531 -68.715  1.00 68.27           C  
ANISOU 1028  CA  VAL A 137    12714   7128   6099  -1573   -412   1611       C  
ATOM   1029  C   VAL A 137     -52.514 -11.015 -67.434  1.00 66.03           C  
ANISOU 1029  C   VAL A 137    12065   6904   6120  -1362   -216   1591       C  
ATOM   1030  O   VAL A 137     -52.295  -9.803 -67.265  1.00 70.51           O  
ANISOU 1030  O   VAL A 137    12670   7416   6704  -1367   -278   1704       O  
ATOM   1031  CB  VAL A 137     -54.606 -12.009 -68.458  1.00 70.61           C  
ANISOU 1031  CB  VAL A 137    12836   7400   6594  -1437   -777   1649       C  
ATOM   1032  CG1 VAL A 137     -55.351 -11.006 -67.593  1.00 68.60           C  
ANISOU 1032  CG1 VAL A 137    12309   7093   6663  -1219  -1061   1776       C  
ATOM   1033  CG2 VAL A 137     -55.335 -12.230 -69.776  1.00 72.88           C  
ANISOU 1033  CG2 VAL A 137    13506   7620   6565  -1661  -1083   1701       C  
ATOM   1034  N   CYS A 138     -52.191 -11.932 -66.512  1.00 63.18           N  
ANISOU 1034  N   CYS A 138    11379   6639   5989  -1183      9   1448       N  
ATOM   1035  CA  CYS A 138     -51.593 -11.535 -65.238  1.00 57.73           C  
ANISOU 1035  CA  CYS A 138    10353   6015   5568   -987    159   1423       C  
ATOM   1036  C   CYS A 138     -50.306 -10.745 -65.446  1.00 54.86           C  
ANISOU 1036  C   CYS A 138    10065   5693   5088  -1110    413   1382       C  
ATOM   1037  O   CYS A 138     -50.030  -9.785 -64.715  1.00 55.47           O  
ANISOU 1037  O   CYS A 138     9990   5779   5305  -1038    410   1436       O  
ATOM   1038  CB  CYS A 138     -51.324 -12.770 -64.376  1.00 54.79           C  
ANISOU 1038  CB  CYS A 138     9722   5711   5384   -808    345   1282       C  
ATOM   1039  SG  CYS A 138     -52.789 -13.747 -63.969  1.00 53.15           S  
ANISOU 1039  SG  CYS A 138     9417   5453   5325   -712    122   1298       S  
ATOM   1040  N   ARG A 139     -49.501 -11.140 -66.433  1.00 58.60           N  
ANISOU 1040  N   ARG A 139    10765   6194   5306  -1323    664   1256       N  
ATOM   1041  CA  ARG A 139     -48.280 -10.403 -66.735  1.00 66.75           C  
ANISOU 1041  CA  ARG A 139    11872   7276   6214  -1506    951   1174       C  
ATOM   1042  C   ARG A 139     -48.595  -9.000 -67.232  1.00 71.89           C  
ANISOU 1042  C   ARG A 139    12835   7802   6677  -1693    759   1376       C  
ATOM   1043  O   ARG A 139     -47.918  -8.040 -66.850  1.00 77.92           O  
ANISOU 1043  O   ARG A 139    13537   8580   7490  -1741    882   1379       O  
ATOM   1044  CB  ARG A 139     -47.442 -11.155 -67.770  1.00 72.40           C  
ANISOU 1044  CB  ARG A 139    12779   8040   6690  -1733   1295    956       C  
ATOM   1045  CG  ARG A 139     -46.749 -12.406 -67.252  1.00 74.69           C  
ANISOU 1045  CG  ARG A 139    12739   8432   7209  -1533   1554    709       C  
ATOM   1046  CD  ARG A 139     -45.811 -12.103 -66.096  1.00 74.37           C  
ANISOU 1046  CD  ARG A 139    12275   8507   7475  -1331   1696    614       C  
ATOM   1047  NE  ARG A 139     -44.860 -13.191 -65.880  1.00 72.85           N  
ANISOU 1047  NE  ARG A 139    11822   8395   7463  -1184   1970    339       N  
ATOM   1048  CZ  ARG A 139     -44.077 -13.304 -64.812  1.00 65.47           C  
ANISOU 1048  CZ  ARG A 139    10485   7556   6833   -938   2034    231       C  
ATOM   1049  NH1 ARG A 139     -44.135 -12.401 -63.844  1.00 57.36           N  
ANISOU 1049  NH1 ARG A 139     9283   6572   5938   -843   1875    369       N  
ATOM   1050  NH2 ARG A 139     -43.239 -14.326 -64.711  1.00 67.02           N  
ANISOU 1050  NH2 ARG A 139    10462   7793   7210   -779   2236    -24       N  
ATOM   1051  N   SER A 140     -49.615  -8.856 -68.082  1.00 72.07           N  
ANISOU 1051  N   SER A 140    13209   7687   6488  -1802    433   1544       N  
ATOM   1052  CA  SER A 140     -49.956  -7.529 -68.588  1.00 74.08           C  
ANISOU 1052  CA  SER A 140    13768   7785   6594  -1934    180   1735       C  
ATOM   1053  C   SER A 140     -50.356  -6.594 -67.450  1.00 72.44           C  
ANISOU 1053  C   SER A 140    13309   7509   6704  -1697    -13   1871       C  
ATOM   1054  O   SER A 140     -49.811  -5.488 -67.318  1.00 67.74           O  
ANISOU 1054  O   SER A 140    12746   6872   6121  -1765     61   1888       O  
ATOM   1055  CB  SER A 140     -51.071  -7.623 -69.631  1.00 72.88           C  
ANISOU 1055  CB  SER A 140    13890   7529   6273  -1993   -225   1828       C  
ATOM   1056  OG  SER A 140     -52.316  -7.937 -69.036  1.00 71.61           O  
ANISOU 1056  OG  SER A 140    13530   7324   6355  -1741   -588   1944       O  
ATOM   1057  N   VAL A 141     -51.294  -7.029 -66.601  1.00 70.04           N  
ANISOU 1057  N   VAL A 141    12671   7224   6715  -1405   -233   1892       N  
ATOM   1058  CA  VAL A 141     -51.745  -6.146 -65.525  1.00 66.35           C  
ANISOU 1058  CA  VAL A 141    11939   6697   6574  -1184   -396   1969       C  
ATOM   1059  C   VAL A 141     -50.614  -5.886 -64.531  1.00 60.79           C  
ANISOU 1059  C   VAL A 141    10959   6121   6017  -1142    -46   1842       C  
ATOM   1060  O   VAL A 141     -50.434  -4.756 -64.048  1.00 57.80           O  
ANISOU 1060  O   VAL A 141    10560   5666   5737  -1130    -64   1900       O  
ATOM   1061  CB  VAL A 141     -52.997  -6.730 -64.843  1.00 67.50           C  
ANISOU 1061  CB  VAL A 141    11767   6856   7022   -927   -648   1963       C  
ATOM   1062  CG1 VAL A 141     -52.762  -8.163 -64.425  1.00 72.52           C  
ANISOU 1062  CG1 VAL A 141    12174   7665   7717   -863   -415   1797       C  
ATOM   1063  CG2 VAL A 141     -53.401  -5.884 -63.651  1.00 66.47           C  
ANISOU 1063  CG2 VAL A 141    11335   6680   7239   -715   -737   1984       C  
ATOM   1064  N   GLN A 142     -49.819  -6.916 -64.234  1.00 54.09           N  
ANISOU 1064  N   GLN A 142     9905   5456   5190  -1119    257   1660       N  
ATOM   1065  CA  GLN A 142     -48.686  -6.742 -63.332  1.00 57.87           C  
ANISOU 1065  CA  GLN A 142    10106   6074   5810  -1073    545   1522       C  
ATOM   1066  C   GLN A 142     -47.700  -5.714 -63.874  1.00 66.58           C  
ANISOU 1066  C   GLN A 142    11421   7152   6725  -1341    744   1504       C  
ATOM   1067  O   GLN A 142     -47.185  -4.878 -63.122  1.00 71.57           O  
ANISOU 1067  O   GLN A 142    11897   7808   7487  -1330    827   1479       O  
ATOM   1068  CB  GLN A 142     -47.993  -8.082 -63.108  1.00 59.01           C  
ANISOU 1068  CB  GLN A 142    10035   6382   6005   -990    784   1327       C  
ATOM   1069  CG  GLN A 142     -46.840  -8.024 -62.136  1.00 57.86           C  
ANISOU 1069  CG  GLN A 142     9560   6389   6036   -901   1012   1173       C  
ATOM   1070  CD  GLN A 142     -46.052  -9.312 -62.104  1.00 59.18           C  
ANISOU 1070  CD  GLN A 142     9551   6678   6255   -810   1221    971       C  
ATOM   1071  OE1 GLN A 142     -45.849  -9.957 -63.134  1.00 58.74           O  
ANISOU 1071  OE1 GLN A 142     9674   6612   6032   -939   1356    882       O  
ATOM   1072  NE2 GLN A 142     -45.607  -9.700 -60.918  1.00 58.42           N  
ANISOU 1072  NE2 GLN A 142     9127   6680   6391   -584   1234    892       N  
ATOM   1073  N   GLU A 143     -47.429  -5.758 -65.179  1.00 68.70           N  
ANISOU 1073  N   GLU A 143    12071   7368   6663  -1622    840   1503       N  
ATOM   1074  CA  GLU A 143     -46.543  -4.772 -65.787  1.00 72.18           C  
ANISOU 1074  CA  GLU A 143    12788   7762   6875  -1950   1058   1485       C  
ATOM   1075  C   GLU A 143     -47.141  -3.374 -65.714  1.00 66.41           C  
ANISOU 1075  C   GLU A 143    12298   6802   6133  -1980    785   1715       C  
ATOM   1076  O   GLU A 143     -46.424  -2.401 -65.456  1.00 63.31           O  
ANISOU 1076  O   GLU A 143    11915   6390   5750  -2118    949   1678       O  
ATOM   1077  CB  GLU A 143     -46.246  -5.150 -67.238  1.00 82.25           C  
ANISOU 1077  CB  GLU A 143    14494   9008   7748  -2285   1221   1438       C  
ATOM   1078  CG  GLU A 143     -45.340  -6.361 -67.396  1.00 88.87           C  
ANISOU 1078  CG  GLU A 143    15105  10058   8604  -2311   1602   1139       C  
ATOM   1079  CD  GLU A 143     -45.403  -6.958 -68.788  1.00 95.15           C  
ANISOU 1079  CD  GLU A 143    16325  10808   9020  -2592   1701   1092       C  
ATOM   1080  OE1 GLU A 143     -46.063  -6.361 -69.667  1.00100.66           O  
ANISOU 1080  OE1 GLU A 143    17362  11357   9526  -2704   1398   1222       O  
ATOM   1081  OE2 GLU A 143     -44.795  -8.028 -69.003  1.00 95.28           O  
ANISOU 1081  OE2 GLU A 143    16184  10962   9057  -2599   2000    837       O  
ATOM   1082  N   TYR A 144     -48.455  -3.251 -65.930  1.00 68.78           N  
ANISOU 1082  N   TYR A 144    12695   6950   6487  -1809    348   1889       N  
ATOM   1083  CA  TYR A 144     -49.066  -1.928 -65.874  1.00 74.17           C  
ANISOU 1083  CA  TYR A 144    13484   7432   7264  -1742     51   2032       C  
ATOM   1084  C   TYR A 144     -49.132  -1.372 -64.457  1.00 75.42           C  
ANISOU 1084  C   TYR A 144    13351   7556   7747  -1547     51   2060       C  
ATOM   1085  O   TYR A 144     -49.306  -0.160 -64.292  1.00 75.46           O  
ANISOU 1085  O   TYR A 144    13439   7394   7837  -1532    -77   2132       O  
ATOM   1086  CB  TYR A 144     -50.468  -1.951 -66.485  1.00 77.83           C  
ANISOU 1086  CB  TYR A 144    14077   7753   7744  -1596   -423   2172       C  
ATOM   1087  CG  TYR A 144     -51.053  -0.565 -66.666  1.00 80.46           C  
ANISOU 1087  CG  TYR A 144    14579   7848   8142  -1541   -734   2304       C  
ATOM   1088  CD1 TYR A 144     -50.456   0.354 -67.520  1.00 82.58           C  
ANISOU 1088  CD1 TYR A 144    15219   8009   8147  -1799   -671   2314       C  
ATOM   1089  CD2 TYR A 144     -52.194  -0.173 -65.978  1.00 78.67           C  
ANISOU 1089  CD2 TYR A 144    14150   7488   8252  -1239  -1076   2398       C  
ATOM   1090  CE1 TYR A 144     -50.980   1.621 -67.686  1.00 82.90           C  
ANISOU 1090  CE1 TYR A 144    15453   7803   8243  -1741   -961   2440       C  
ATOM   1091  CE2 TYR A 144     -52.726   1.092 -66.140  1.00 80.28           C  
ANISOU 1091  CE2 TYR A 144    14505   7452   8546  -1164  -1358   2502       C  
ATOM   1092  CZ  TYR A 144     -52.115   1.984 -66.995  1.00 84.32           C  
ANISOU 1092  CZ  TYR A 144    15413   7847   8777  -1409  -1308   2536       C  
ATOM   1093  OH  TYR A 144     -52.641   3.243 -67.157  1.00 94.76           O  
ANISOU 1093  OH  TYR A 144    16919   8902  10182  -1327  -1599   2647       O  
ATOM   1094  N   LEU A 145     -48.998  -2.223 -63.434  1.00 80.32           N  
ANISOU 1094  N   LEU A 145    13544   8377   8596  -1355    188   1930       N  
ATOM   1095  CA  LEU A 145     -49.008  -1.725 -62.060  1.00 75.35           C  
ANISOU 1095  CA  LEU A 145    12558   7785   8287  -1163    208   1873       C  
ATOM   1096  C   LEU A 145     -47.925  -0.675 -61.828  1.00 74.42           C  
ANISOU 1096  C   LEU A 145    12499   7657   8120  -1364    451   1813       C  
ATOM   1097  O   LEU A 145     -48.146   0.307 -61.108  1.00 74.61           O  
ANISOU 1097  O   LEU A 145    12467   7560   8321  -1294    373   1846       O  
ATOM   1098  CB  LEU A 145     -48.838  -2.883 -61.078  1.00 70.94           C  
ANISOU 1098  CB  LEU A 145    11561   7474   7919   -964    340   1712       C  
ATOM   1099  CG  LEU A 145     -50.093  -3.695 -60.765  1.00 69.33           C  
ANISOU 1099  CG  LEU A 145    11202   7260   7880   -731    103   1750       C  
ATOM   1100  CD1 LEU A 145     -49.762  -4.824 -59.805  1.00 67.59           C  
ANISOU 1100  CD1 LEU A 145    10643   7251   7788   -586    265   1605       C  
ATOM   1101  CD2 LEU A 145     -51.174  -2.793 -60.191  1.00 66.94           C  
ANISOU 1101  CD2 LEU A 145    10831   6785   7818   -580   -153   1833       C  
ATOM   1102  N   ASP A 146     -46.750  -0.855 -62.435  1.00 75.55           N  
ANISOU 1102  N   ASP A 146    12747   7922   8037  -1634    768   1695       N  
ATOM   1103  CA  ASP A 146     -45.612   0.011 -62.146  1.00 76.74           C  
ANISOU 1103  CA  ASP A 146    12875   8118   8166  -1855   1051   1577       C  
ATOM   1104  C   ASP A 146     -45.795   1.436 -62.656  1.00 80.73           C  
ANISOU 1104  C   ASP A 146    13835   8313   8524  -2070    957   1746       C  
ATOM   1105  O   ASP A 146     -45.019   2.315 -62.265  1.00 81.04           O  
ANISOU 1105  O   ASP A 146    13863   8346   8584  -2247   1159   1660       O  
ATOM   1106  CB  ASP A 146     -44.337  -0.590 -62.742  1.00 82.92           C  
ANISOU 1106  CB  ASP A 146    13618   9115   8771  -2108   1440   1360       C  
ATOM   1107  CG  ASP A 146     -43.148  -0.479 -61.807  1.00 90.01           C  
ANISOU 1107  CG  ASP A 146    14094  10252   9855  -2132   1718   1110       C  
ATOM   1108  OD1 ASP A 146     -43.292  -0.831 -60.618  1.00 89.11           O  
ANISOU 1108  OD1 ASP A 146    13585  10262  10012  -1840   1611   1061       O  
ATOM   1109  OD2 ASP A 146     -42.071  -0.036 -62.258  1.00 97.88           O  
ANISOU 1109  OD2 ASP A 146    15160  11313  10718  -2464   2041    951       O  
ATOM   1110  N   VAL A 147     -46.790   1.686 -63.510  1.00 80.63           N  
ANISOU 1110  N   VAL A 147    14127   8092   8416  -2004    615   1921       N  
ATOM   1111  CA  VAL A 147     -47.026   3.032 -64.023  1.00 77.08           C  
ANISOU 1111  CA  VAL A 147    13993   7395   7900  -2087    441   2016       C  
ATOM   1112  C   VAL A 147     -47.461   3.988 -62.916  1.00 76.14           C  
ANISOU 1112  C   VAL A 147    13747   7101   8082  -1907    312   2076       C  
ATOM   1113  O   VAL A 147     -47.246   5.201 -63.023  1.00 81.96           O  
ANISOU 1113  O   VAL A 147    14695   7655   8791  -2027    310   2098       O  
ATOM   1114  CB  VAL A 147     -48.064   2.970 -65.165  1.00 72.25           C  
ANISOU 1114  CB  VAL A 147    13668   6632   7150  -2009     58   2163       C  
ATOM   1115  CG1 VAL A 147     -48.415   4.357 -65.671  1.00 73.68           C  
ANISOU 1115  CG1 VAL A 147    14197   6524   7273  -2055   -174   2282       C  
ATOM   1116  CG2 VAL A 147     -47.542   2.114 -66.308  1.00 64.33           C  
ANISOU 1116  CG2 VAL A 147    12852   5778   5814  -2249    226   2073       C  
ATOM   1117  N   ALA A 148     -48.037   3.467 -61.832  1.00 71.65           N  
ANISOU 1117  N   ALA A 148    12858   6571   7793  -1642    230   2084       N  
ATOM   1118  CA  ALA A 148     -48.576   4.321 -60.779  1.00 68.19           C  
ANISOU 1118  CA  ALA A 148    12296   5948   7663  -1457    105   2107       C  
ATOM   1119  C   ALA A 148     -47.504   5.144 -60.074  1.00 70.28           C  
ANISOU 1119  C   ALA A 148    12490   6262   7953  -1654    419   1961       C  
ATOM   1120  O   ALA A 148     -47.837   6.130 -59.406  1.00 74.16           O  
ANISOU 1120  O   ALA A 148    12979   6551   8648  -1571    340   1966       O  
ATOM   1121  CB  ALA A 148     -49.335   3.474 -59.760  1.00 64.94           C  
ANISOU 1121  CB  ALA A 148    11385   5723   7566  -1113     10   2007       C  
ATOM   1122  N   LYS A 149     -46.229   4.777 -60.212  1.00 72.33           N  
ANISOU 1122  N   LYS A 149    12673   6781   8029  -1919    776   1805       N  
ATOM   1123  CA  LYS A 149     -45.173   5.494 -59.504  1.00 69.05           C  
ANISOU 1123  CA  LYS A 149    12123   6455   7656  -2120   1068   1627       C  
ATOM   1124  C   LYS A 149     -44.906   6.881 -60.079  1.00 73.48           C  
ANISOU 1124  C   LYS A 149    13143   6710   8065  -2405   1105   1705       C  
ATOM   1125  O   LYS A 149     -44.260   7.696 -59.413  1.00 77.59           O  
ANISOU 1125  O   LYS A 149    13612   7213   8655  -2571   1300   1584       O  
ATOM   1126  CB  LYS A 149     -43.886   4.668 -59.513  1.00 70.15           C  
ANISOU 1126  CB  LYS A 149    11977   6979   7699  -2297   1415   1393       C  
ATOM   1127  CG  LYS A 149     -44.059   3.272 -58.950  1.00 71.62           C  
ANISOU 1127  CG  LYS A 149    11719   7458   8035  -1993   1360   1304       C  
ATOM   1128  CD  LYS A 149     -42.727   2.575 -58.739  1.00 76.37           C  
ANISOU 1128  CD  LYS A 149    11971   8413   8631  -2105   1664   1041       C  
ATOM   1129  CE  LYS A 149     -42.929   1.211 -58.095  1.00 76.51           C  
ANISOU 1129  CE  LYS A 149    11600   8664   8807  -1775   1565    977       C  
ATOM   1130  NZ  LYS A 149     -41.639   0.542 -57.778  1.00 78.79           N  
ANISOU 1130  NZ  LYS A 149    11510   9273   9154  -1815   1794    712       N  
ATOM   1131  N   VAL A 150     -45.383   7.172 -61.293  1.00 70.06           N  
ANISOU 1131  N   VAL A 150    13062   6108   7449  -2410    887   1842       N  
ATOM   1132  CA  VAL A 150     -45.154   8.473 -61.917  1.00 78.02           C  
ANISOU 1132  CA  VAL A 150    14451   6882   8310  -2609    870   1875       C  
ATOM   1133  C   VAL A 150     -46.373   9.382 -61.835  1.00 79.14           C  
ANISOU 1133  C   VAL A 150    14770   6656   8642  -2336    469   2063       C  
ATOM   1134  O   VAL A 150     -46.347  10.492 -62.382  1.00 79.41           O  
ANISOU 1134  O   VAL A 150    15166   6444   8564  -2456    393   2128       O  
ATOM   1135  CB  VAL A 150     -44.706   8.311 -63.385  1.00 77.01           C  
ANISOU 1135  CB  VAL A 150    14664   6796   7801  -2870    937   1870       C  
ATOM   1136  CG1 VAL A 150     -43.841   9.487 -63.821  1.00 82.23           C  
ANISOU 1136  CG1 VAL A 150    15652   7338   8255  -3229   1143   1788       C  
ATOM   1137  CG2 VAL A 150     -43.957   7.002 -63.575  1.00 71.30           C  
ANISOU 1137  CG2 VAL A 150    13699   6425   6967  -2992   1226   1705       C  
ATOM   1138  N   ILE A 151     -47.436   8.952 -61.165  1.00 77.36           N  
ANISOU 1138  N   ILE A 151    14299   6378   8715  -1974    217   2134       N  
ATOM   1139  CA  ILE A 151     -48.650   9.755 -61.068  1.00 76.99           C  
ANISOU 1139  CA  ILE A 151    14343   5990   8919  -1678   -163   2267       C  
ATOM   1140  C   ILE A 151     -48.429  10.887 -60.073  1.00 75.67           C  
ANISOU 1140  C   ILE A 151    14157   5624   8970  -1701    -43   2186       C  
ATOM   1141  O   ILE A 151     -48.022  10.656 -58.929  1.00 71.93           O  
ANISOU 1141  O   ILE A 151    13402   5280   8647  -1726    192   2038       O  
ATOM   1142  CB  ILE A 151     -49.849   8.886 -60.660  1.00 73.85           C  
ANISOU 1142  CB  ILE A 151    13642   5619   8798  -1300   -437   2310       C  
ATOM   1143  CG1 ILE A 151     -50.027   7.724 -61.639  1.00 73.91           C  
ANISOU 1143  CG1 ILE A 151    13674   5833   8577  -1309   -534   2368       C  
ATOM   1144  CG2 ILE A 151     -51.116   9.726 -60.591  1.00 72.84           C  
ANISOU 1144  CG2 ILE A 151    13548   5146   8981   -981   -823   2397       C  
ATOM   1145  CD1 ILE A 151     -51.200   6.829 -61.298  1.00 70.25           C  
ANISOU 1145  CD1 ILE A 151    12912   5412   8368   -972   -798   2392       C  
ATOM   1146  N   ASP A 152     -48.702  12.117 -60.508  1.00 79.14           N  
ANISOU 1146  N   ASP A 152    14919   5737   9415  -1702   -208   2274       N  
ATOM   1147  CA  ASP A 152     -48.592  13.289 -59.647  1.00 84.14           C  
ANISOU 1147  CA  ASP A 152    15578   6125  10268  -1712   -121   2197       C  
ATOM   1148  C   ASP A 152     -49.825  14.178 -59.644  1.00 87.48           C  
ANISOU 1148  C   ASP A 152    16098   6140  11002  -1372   -499   2304       C  
ATOM   1149  O   ASP A 152     -49.963  14.999 -58.728  1.00 77.48           O  
ANISOU 1149  O   ASP A 152    14762   4654  10022  -1292   -443   2207       O  
ATOM   1150  CB  ASP A 152     -47.377  14.140 -60.045  1.00 90.20           C  
ANISOU 1150  CB  ASP A 152    16661   6878  10732  -2135    164   2139       C  
ATOM   1151  CG  ASP A 152     -46.095  13.677 -59.379  1.00 91.04           C  
ANISOU 1151  CG  ASP A 152    16524   7335  10732  -2445    616   1916       C  
ATOM   1152  OD1 ASP A 152     -45.894  12.452 -59.242  1.00 90.54           O  
ANISOU 1152  OD1 ASP A 152    16176   7593  10632  -2427    717   1861       O  
ATOM   1153  OD2 ASP A 152     -45.289  14.544 -58.983  1.00 90.97           O  
ANISOU 1153  OD2 ASP A 152    16595   7283  10688  -2705    865   1784       O  
ATOM   1154  N   VAL A 153     -50.712  14.060 -60.629  1.00 92.12           N  
ANISOU 1154  N   VAL A 153    16834   6616  11553  -1176   -875   2473       N  
ATOM   1155  CA  VAL A 153     -51.957  14.815 -60.672  1.00 93.42           C  
ANISOU 1155  CA  VAL A 153    17033   6416  12046   -813  -1268   2555       C  
ATOM   1156  C   VAL A 153     -53.102  13.822 -60.812  1.00 91.03           C  
ANISOU 1156  C   VAL A 153    16433   6227  11929   -475  -1579   2583       C  
ATOM   1157  O   VAL A 153     -52.948  12.753 -61.412  1.00 84.08           O  
ANISOU 1157  O   VAL A 153    15525   5629  10792   -571  -1580   2626       O  
ATOM   1158  CB  VAL A 153     -51.971  15.845 -61.825  1.00 95.24           C  
ANISOU 1158  CB  VAL A 153    17796   6352  12036   -918  -1486   2730       C  
ATOM   1159  CG1 VAL A 153     -53.088  16.864 -61.626  1.00100.63           C  
ANISOU 1159  CG1 VAL A 153    18503   6613  13118   -552  -1832   2774       C  
ATOM   1160  CG2 VAL A 153     -50.623  16.543 -61.934  1.00 92.98           C  
ANISOU 1160  CG2 VAL A 153    17840   6060  11427  -1365  -1122   2690       C  
ATOM   1161  N   GLU A 154     -54.260  14.181 -60.252  1.00101.54           N  
ANISOU 1161  N   GLU A 154    17523   7335  13721    -86  -1829   2528       N  
ATOM   1162  CA  GLU A 154     -55.406  13.278 -60.257  1.00106.88           C  
ANISOU 1162  CA  GLU A 154    17850   8128  14632    236  -2113   2500       C  
ATOM   1163  C   GLU A 154     -55.925  12.976 -61.657  1.00110.06           C  
ANISOU 1163  C   GLU A 154    18485   8548  14786    258  -2498   2679       C  
ATOM   1164  O   GLU A 154     -56.732  12.053 -61.810  1.00111.77           O  
ANISOU 1164  O   GLU A 154    18431   8923  15111    443  -2715   2655       O  
ATOM   1165  CB  GLU A 154     -56.531  13.853 -59.392  1.00120.90           C  
ANISOU 1165  CB  GLU A 154    19303   9654  16979    635  -2282   2346       C  
ATOM   1166  CG  GLU A 154     -56.405  13.496 -57.915  1.00125.14           C  
ANISOU 1166  CG  GLU A 154    19437  10293  17817    681  -1958   2100       C  
ATOM   1167  CD  GLU A 154     -57.481  14.135 -57.059  1.00131.94           C  
ANISOU 1167  CD  GLU A 154    19975  10907  19249   1047  -2067   1884       C  
ATOM   1168  OE1 GLU A 154     -57.980  15.218 -57.435  1.00139.05           O  
ANISOU 1168  OE1 GLU A 154    21051  11486  20297   1210  -2293   1931       O  
ATOM   1169  OE2 GLU A 154     -57.831  13.553 -56.009  1.00130.53           O  
ANISOU 1169  OE2 GLU A 154    19361  10857  19379   1163  -1918   1648       O  
ATOM   1170  N   ALA A 155     -55.488  13.719 -62.677  1.00110.96           N  
ANISOU 1170  N   ALA A 155    19107   8495  14560     50  -2591   2841       N  
ATOM   1171  CA  ALA A 155     -55.815  13.346 -64.049  1.00109.92           C  
ANISOU 1171  CA  ALA A 155    19265   8397  14104    -13  -2921   2998       C  
ATOM   1172  C   ALA A 155     -55.095  12.062 -64.446  1.00101.71           C  
ANISOU 1172  C   ALA A 155    18205   7748  12692   -287  -2678   2982       C  
ATOM   1173  O   ALA A 155     -55.698  11.153 -65.034  1.00108.63           O  
ANISOU 1173  O   ALA A 155    18999   8774  13503   -212  -2912   3010       O  
ATOM   1174  CB  ALA A 155     -55.458  14.487 -65.004  1.00109.69           C  
ANISOU 1174  CB  ALA A 155    19839   8067  13770   -207  -3055   3159       C  
ATOM   1175  N   ASP A 156     -53.801  11.970 -64.124  1.00 95.59           N  
ANISOU 1175  N   ASP A 156    17493   7138  11688   -611  -2206   2916       N  
ATOM   1176  CA  ASP A 156     -53.059  10.739 -64.377  1.00 96.67           C  
ANISOU 1176  CA  ASP A 156    17557   7648  11527   -849  -1932   2862       C  
ATOM   1177  C   ASP A 156     -53.624   9.580 -63.567  1.00 90.88           C  
ANISOU 1177  C   ASP A 156    16309   7142  11079   -609  -1927   2763       C  
ATOM   1178  O   ASP A 156     -53.660   8.441 -64.044  1.00 90.07           O  
ANISOU 1178  O   ASP A 156    16139   7280  10803   -660  -1933   2761       O  
ATOM   1179  CB  ASP A 156     -51.576  10.937 -64.060  1.00102.52           C  
ANISOU 1179  CB  ASP A 156    18395   8519  12040  -1217  -1432   2766       C  
ATOM   1180  CG  ASP A 156     -50.876  11.824 -65.070  1.00115.76           C  
ANISOU 1180  CG  ASP A 156    20619  10037  13327  -1549  -1382   2837       C  
ATOM   1181  OD1 ASP A 156     -51.398  11.974 -66.195  1.00124.22           O  
ANISOU 1181  OD1 ASP A 156    22038  10966  14193  -1553  -1709   2971       O  
ATOM   1182  OD2 ASP A 156     -49.799  12.366 -64.740  1.00117.06           O  
ANISOU 1182  OD2 ASP A 156    20880  10219  13379  -1827  -1020   2746       O  
ATOM   1183  N   LEU A 157     -54.066   9.848 -62.335  1.00 91.38           N  
ANISOU 1183  N   LEU A 157    16027   7118  11575   -362  -1901   2665       N  
ATOM   1184  CA  LEU A 157     -54.697   8.803 -61.537  1.00 87.97           C  
ANISOU 1184  CA  LEU A 157    15131   6866  11428   -135  -1916   2558       C  
ATOM   1185  C   LEU A 157     -56.035   8.384 -62.131  1.00 88.82           C  
ANISOU 1185  C   LEU A 157    15121   6938  11687    131  -2367   2600       C  
ATOM   1186  O   LEU A 157     -56.423   7.215 -62.022  1.00 90.83           O  
ANISOU 1186  O   LEU A 157    15110   7412  11989    202  -2396   2549       O  
ATOM   1187  CB  LEU A 157     -54.873   9.279 -60.094  1.00 87.35           C  
ANISOU 1187  CB  LEU A 157    14749   6666  11773     38  -1779   2407       C  
ATOM   1188  CG  LEU A 157     -55.602   8.360 -59.111  1.00 86.41           C  
ANISOU 1188  CG  LEU A 157    14147   6676  12008    273  -1791   2259       C  
ATOM   1189  CD1 LEU A 157     -54.997   6.961 -59.109  1.00 82.26           C  
ANISOU 1189  CD1 LEU A 157    13532   6499  11225    100  -1582   2259       C  
ATOM   1190  CD2 LEU A 157     -55.571   8.960 -57.712  1.00 86.85           C  
ANISOU 1190  CD2 LEU A 157    13985   6587  12429    362  -1598   2080       C  
ATOM   1191  N   ALA A 158     -56.744   9.314 -62.773  1.00 90.26           N  
ANISOU 1191  N   ALA A 158    15506   6843  11947    268  -2735   2688       N  
ATOM   1192  CA  ALA A 158     -58.006   8.968 -63.418  1.00 93.28           C  
ANISOU 1192  CA  ALA A 158    15785   7189  12467    500  -3210   2717       C  
ATOM   1193  C   ALA A 158     -57.775   8.071 -64.628  1.00 92.90           C  
ANISOU 1193  C   ALA A 158    15998   7333  11969    270  -3292   2822       C  
ATOM   1194  O   ALA A 158     -58.387   7.003 -64.747  1.00 94.69           O  
ANISOU 1194  O   ALA A 158    15984   7739  12254    353  -3430   2777       O  
ATOM   1195  CB  ALA A 158     -58.758  10.238 -63.820  1.00 99.36           C  
ANISOU 1195  CB  ALA A 158    16736   7594  13423    699  -3605   2786       C  
ATOM   1196  N   THR A 159     -56.886   8.487 -65.535  1.00 91.30           N  
ANISOU 1196  N   THR A 159    16294   7083  11312    -43  -3192   2940       N  
ATOM   1197  CA  THR A 159     -56.616   7.686 -66.727  1.00 92.64           C  
ANISOU 1197  CA  THR A 159    16751   7411  11036   -295  -3237   3006       C  
ATOM   1198  C   THR A 159     -56.018   6.332 -66.358  1.00 88.92           C  
ANISOU 1198  C   THR A 159    16032   7296  10458   -424  -2869   2901       C  
ATOM   1199  O   THR A 159     -56.454   5.286 -66.856  1.00 90.09           O  
ANISOU 1199  O   THR A 159    16116   7600  10514   -426  -3004   2892       O  
ATOM   1200  CB  THR A 159     -55.679   8.443 -67.667  1.00 94.96           C  
ANISOU 1200  CB  THR A 159    17626   7580  10876   -641  -3128   3105       C  
ATOM   1201  OG1 THR A 159     -54.396   8.587 -67.046  1.00 83.32           O  
ANISOU 1201  OG1 THR A 159    16138   6222   9296   -869  -2602   3024       O  
ATOM   1202  CG2 THR A 159     -56.243   9.824 -67.981  1.00102.20           C  
ANISOU 1202  CG2 THR A 159    18827   8107  11895   -509  -3497   3223       C  
ATOM   1203  N   PHE A 160     -55.006   6.339 -65.486  1.00 84.65           N  
ANISOU 1203  N   PHE A 160    15364   6873   9928   -541  -2412   2818       N  
ATOM   1204  CA  PHE A 160     -54.408   5.095 -65.012  1.00 78.86           C  
ANISOU 1204  CA  PHE A 160    14379   6454   9130   -635  -2068   2713       C  
ATOM   1205  C   PHE A 160     -55.455   4.188 -64.380  1.00 78.39           C  
ANISOU 1205  C   PHE A 160    13892   6487   9405   -348  -2249   2655       C  
ATOM   1206  O   PHE A 160     -55.448   2.973 -64.604  1.00 77.80           O  
ANISOU 1206  O   PHE A 160    13728   6628   9205   -406  -2188   2621       O  
ATOM   1207  CB  PHE A 160     -53.288   5.410 -64.018  1.00 76.52           C  
ANISOU 1207  CB  PHE A 160    13976   6226   8871   -760  -1623   2624       C  
ATOM   1208  CG  PHE A 160     -52.924   4.261 -63.118  1.00 77.35           C  
ANISOU 1208  CG  PHE A 160    13726   6597   9065   -741  -1344   2511       C  
ATOM   1209  CD1 PHE A 160     -52.038   3.285 -63.540  1.00 80.13           C  
ANISOU 1209  CD1 PHE A 160    14130   7203   9114   -972  -1063   2457       C  
ATOM   1210  CD2 PHE A 160     -53.455   4.169 -61.838  1.00 73.84           C  
ANISOU 1210  CD2 PHE A 160    12914   6130   9012   -497  -1356   2442       C  
ATOM   1211  CE1 PHE A 160     -51.698   2.233 -62.710  1.00 75.14           C  
ANISOU 1211  CE1 PHE A 160    13196   6793   8560   -939   -827   2360       C  
ATOM   1212  CE2 PHE A 160     -53.118   3.123 -61.006  1.00 68.75           C  
ANISOU 1212  CE2 PHE A 160    11998   5705   8418   -495  -1121   2351       C  
ATOM   1213  CZ  PHE A 160     -52.239   2.153 -61.441  1.00 72.48           C  
ANISOU 1213  CZ  PHE A 160    12526   6432   8580   -704   -865   2316       C  
ATOM   1214  N   LEU A 161     -56.365   4.762 -63.590  1.00 81.04           N  
ANISOU 1214  N   LEU A 161    13960   6650  10180    -48  -2458   2620       N  
ATOM   1215  CA  LEU A 161     -57.427   3.972 -62.976  1.00 78.76           C  
ANISOU 1215  CA  LEU A 161    13241   6432  10254    212  -2633   2527       C  
ATOM   1216  C   LEU A 161     -58.308   3.325 -64.038  1.00 83.07           C  
ANISOU 1216  C   LEU A 161    13845   7012  10705    246  -3019   2578       C  
ATOM   1217  O   LEU A 161     -58.565   2.114 -63.999  1.00 88.47           O  
ANISOU 1217  O   LEU A 161    14346   7888  11381    239  -3004   2530       O  
ATOM   1218  CB  LEU A 161     -58.254   4.860 -62.043  1.00 80.78           C  
ANISOU 1218  CB  LEU A 161    13202   6466  11024    515  -2784   2433       C  
ATOM   1219  CG  LEU A 161     -59.046   4.253 -60.880  1.00 80.28           C  
ANISOU 1219  CG  LEU A 161    12604   6465  11435    751  -2773   2252       C  
ATOM   1220  CD1 LEU A 161     -59.494   5.359 -59.937  1.00 77.32           C  
ANISOU 1220  CD1 LEU A 161    12006   5854  11518    977  -2782   2118       C  
ATOM   1221  CD2 LEU A 161     -60.249   3.449 -61.355  1.00 84.43           C  
ANISOU 1221  CD2 LEU A 161    12896   7055  12129    904  -3136   2211       C  
ATOM   1222  N   GLN A 162     -58.775   4.120 -65.006  1.00 85.69           N  
ANISOU 1222  N   GLN A 162    14462   7143  10955    267  -3382   2679       N  
ATOM   1223  CA  GLN A 162     -59.645   3.595 -66.051  1.00 86.88           C  
ANISOU 1223  CA  GLN A 162    14699   7299  11014    286  -3803   2725       C  
ATOM   1224  C   GLN A 162     -58.930   2.626 -66.982  1.00 83.51           C  
ANISOU 1224  C   GLN A 162    14582   7070  10080    -38  -3637   2775       C  
ATOM   1225  O   GLN A 162     -59.600   1.928 -67.750  1.00 76.76           O  
ANISOU 1225  O   GLN A 162    13772   6260   9133    -56  -3934   2789       O  
ATOM   1226  CB  GLN A 162     -60.255   4.740 -66.863  1.00 90.88           C  
ANISOU 1226  CB  GLN A 162    15484   7512  11536    374  -4251   2828       C  
ATOM   1227  CG  GLN A 162     -59.430   5.170 -68.063  1.00 93.20           C  
ANISOU 1227  CG  GLN A 162    16397   7727  11289     51  -4223   2977       C  
ATOM   1228  CD  GLN A 162     -60.112   6.253 -68.875  1.00102.35           C  
ANISOU 1228  CD  GLN A 162    17866   8564  12458    145  -4721   3094       C  
ATOM   1229  OE1 GLN A 162     -60.842   7.083 -68.333  1.00106.87           O  
ANISOU 1229  OE1 GLN A 162    18225   8931  13452    447  -4957   3067       O  
ATOM   1230  NE2 GLN A 162     -59.883   6.245 -70.185  1.00105.00           N  
ANISOU 1230  NE2 GLN A 162    18721   8839  12334   -116  -4886   3212       N  
ATOM   1231  N   ASN A 163     -57.597   2.573 -66.947  1.00 82.63           N  
ANISOU 1231  N   ASN A 163    14671   7070   9655   -301  -3174   2776       N  
ATOM   1232  CA  ASN A 163     -56.872   1.521 -67.647  1.00 83.83           C  
ANISOU 1232  CA  ASN A 163    15021   7434   9396   -588  -2935   2757       C  
ATOM   1233  C   ASN A 163     -56.626   0.298 -66.775  1.00 84.07           C  
ANISOU 1233  C   ASN A 163    14692   7711   9538   -554  -2629   2646       C  
ATOM   1234  O   ASN A 163     -56.465  -0.808 -67.306  1.00 80.64           O  
ANISOU 1234  O   ASN A 163    14331   7440   8870   -701  -2545   2613       O  
ATOM   1235  CB  ASN A 163     -55.529   2.043 -68.166  1.00 85.69           C  
ANISOU 1235  CB  ASN A 163    15645   7669   9245   -911  -2588   2772       C  
ATOM   1236  CG  ASN A 163     -55.682   3.260 -69.052  1.00 92.31           C  
ANISOU 1236  CG  ASN A 163    16915   8237   9922   -989  -2868   2891       C  
ATOM   1237  OD1 ASN A 163     -56.786   3.602 -69.472  1.00 96.23           O  
ANISOU 1237  OD1 ASN A 163    17461   8556  10545   -814  -3356   2972       O  
ATOM   1238  ND2 ASN A 163     -54.566   3.921 -69.345  1.00 94.58           N  
ANISOU 1238  ND2 ASN A 163    17522   8482   9932  -1261  -2570   2893       N  
ATOM   1239  N   LEU A 164     -56.602   0.469 -65.454  1.00 84.70           N  
ANISOU 1239  N   LEU A 164    14418   7801   9963   -373  -2467   2584       N  
ATOM   1240  CA  LEU A 164     -56.298  -0.621 -64.537  1.00 79.29           C  
ANISOU 1240  CA  LEU A 164    13435   7319   9374   -352  -2172   2489       C  
ATOM   1241  C   LEU A 164     -57.522  -1.448 -64.175  1.00 81.90           C  
ANISOU 1241  C   LEU A 164    13445   7671  10001   -145  -2442   2447       C  
ATOM   1242  O   LEU A 164     -57.400  -2.662 -63.977  1.00 80.58           O  
ANISOU 1242  O   LEU A 164    13124   7717   9777   -200  -2245   2354       O  
ATOM   1243  CB  LEU A 164     -55.662  -0.068 -63.257  1.00 75.76           C  
ANISOU 1243  CB  LEU A 164    12793   6859   9135   -294  -1874   2433       C  
ATOM   1244  CG  LEU A 164     -55.186  -1.098 -62.229  1.00 68.99           C  
ANISOU 1244  CG  LEU A 164    11582   6271   8359   -283  -1502   2273       C  
ATOM   1245  CD1 LEU A 164     -54.007  -1.886 -62.773  1.00 65.43           C  
ANISOU 1245  CD1 LEU A 164    11323   6009   7530   -531  -1182   2250       C  
ATOM   1246  CD2 LEU A 164     -54.830  -0.431 -60.910  1.00 68.39           C  
ANISOU 1246  CD2 LEU A 164    11230   6216   8539   -191  -1268   2158       C  
ATOM   1247  N   THR A 165     -58.696  -0.822 -64.085  1.00 86.25           N  
ANISOU 1247  N   THR A 165    13823   8050  10899     91  -2843   2447       N  
ATOM   1248  CA  THR A 165     -59.898  -1.563 -63.705  1.00 86.11           C  
ANISOU 1248  CA  THR A 165    13399   8089  11231    277  -3066   2334       C  
ATOM   1249  C   THR A 165     -60.272  -2.656 -64.702  1.00 85.84           C  
ANISOU 1249  C   THR A 165    13501   8168  10945    146  -3254   2360       C  
ATOM   1250  O   THR A 165     -60.514  -3.797 -64.266  1.00 86.62           O  
ANISOU 1250  O   THR A 165    13289   8501  11124    125  -3047   2187       O  
ATOM   1251  CB  THR A 165     -61.057  -0.584 -63.483  1.00 88.46           C  
ANISOU 1251  CB  THR A 165    13470   8142  11998    572  -3495   2310       C  
ATOM   1252  OG1 THR A 165     -60.761   0.260 -62.364  1.00 88.52           O  
ANISOU 1252  OG1 THR A 165    13276   8078  12278    686  -3237   2216       O  
ATOM   1253  CG2 THR A 165     -62.351  -1.338 -63.214  1.00 86.02           C  
ANISOU 1253  CG2 THR A 165    12661   7959  12065    725  -3683   2105       C  
ATOM   1254  N   PRO A 166     -60.343  -2.407 -66.020  1.00 86.26           N  
ANISOU 1254  N   PRO A 166    13962   8131  10682     20  -3547   2488       N  
ATOM   1255  CA  PRO A 166     -60.734  -3.501 -66.927  1.00 83.86           C  
ANISOU 1255  CA  PRO A 166    13795   7931  10137   -124  -3733   2497       C  
ATOM   1256  C   PRO A 166     -59.732  -4.642 -66.964  1.00 80.81           C  
ANISOU 1256  C   PRO A 166    13565   7740   9399   -368  -3284   2472       C  
ATOM   1257  O   PRO A 166     -60.135  -5.809 -67.056  1.00 86.71           O  
ANISOU 1257  O   PRO A 166    14148   8660  10139   -420  -3242   2343       O  
ATOM   1258  CB  PRO A 166     -60.859  -2.799 -68.287  1.00 84.37           C  
ANISOU 1258  CB  PRO A 166    14281   7864   9911   -241  -4047   2595       C  
ATOM   1259  CG  PRO A 166     -59.971  -1.621 -68.182  1.00 85.78           C  
ANISOU 1259  CG  PRO A 166    14666   7933   9995   -283  -3815   2651       C  
ATOM   1260  CD  PRO A 166     -60.100  -1.156 -66.763  1.00 86.94           C  
ANISOU 1260  CD  PRO A 166    14387   8044  10602    -27  -3682   2583       C  
ATOM   1261  N   GLY A 167     -58.434  -4.339 -66.891  1.00 79.08           N  
ANISOU 1261  N   GLY A 167    13537   7570   8939   -518  -2846   2474       N  
ATOM   1262  CA  GLY A 167     -57.441  -5.401 -66.839  1.00 77.78           C  
ANISOU 1262  CA  GLY A 167    13443   7593   8515   -708  -2393   2399       C  
ATOM   1263  C   GLY A 167     -57.550  -6.237 -65.578  1.00 71.07           C  
ANISOU 1263  C   GLY A 167    12065   6943   7993   -553  -2096   2193       C  
ATOM   1264  O   GLY A 167     -57.498  -7.471 -65.633  1.00 68.35           O  
ANISOU 1264  O   GLY A 167    11650   6753   7567   -626  -1919   2077       O  
ATOM   1265  N   MET A 168     -57.710  -5.579 -64.425  1.00 66.42           N  
ANISOU 1265  N   MET A 168    11141   6333   7762   -356  -2035   2144       N  
ATOM   1266  CA  MET A 168     -57.890  -6.303 -63.170  1.00 68.22           C  
ANISOU 1266  CA  MET A 168    10921   6726   8272   -237  -1772   1960       C  
ATOM   1267  C   MET A 168     -59.126  -7.191 -63.217  1.00 73.62           C  
ANISOU 1267  C   MET A 168    11373   7467   9132   -191  -1969   1854       C  
ATOM   1268  O   MET A 168     -59.087  -8.346 -62.771  1.00 74.43           O  
ANISOU 1268  O   MET A 168    11326   7718   9236   -234  -1724   1726       O  
ATOM   1269  CB  MET A 168     -57.983  -5.319 -62.003  1.00 63.28           C  
ANISOU 1269  CB  MET A 168    10021   6045   7979    -66  -1708   1917       C  
ATOM   1270  CG  MET A 168     -56.641  -4.843 -61.479  1.00 62.79           C  
ANISOU 1270  CG  MET A 168    10044   6023   7792   -128  -1362   1930       C  
ATOM   1271  SD  MET A 168     -55.735  -6.169 -60.665  1.00 62.91           S  
ANISOU 1271  SD  MET A 168     9891   6293   7719   -176   -915   1786       S  
ATOM   1272  CE  MET A 168     -54.232  -5.324 -60.182  1.00 62.09           C  
ANISOU 1272  CE  MET A 168     9857   6222   7514   -238   -624   1794       C  
ATOM   1273  N   THR A 169     -60.234  -6.672 -63.756  1.00 78.27           N  
ANISOU 1273  N   THR A 169    11931   7926   9882   -107  -2427   1897       N  
ATOM   1274  CA  THR A 169     -61.438  -7.488 -63.883  1.00 79.91           C  
ANISOU 1274  CA  THR A 169    11888   8202  10272    -91  -2639   1766       C  
ATOM   1275  C   THR A 169     -61.197  -8.681 -64.802  1.00 78.14           C  
ANISOU 1275  C   THR A 169    11936   8073   9680   -311  -2594   1770       C  
ATOM   1276  O   THR A 169     -61.629  -9.804 -64.504  1.00 76.23           O  
ANISOU 1276  O   THR A 169    11495   7958   9512   -368  -2459   1612       O  
ATOM   1277  CB  THR A 169     -62.599  -6.632 -64.391  1.00 86.99           C  
ANISOU 1277  CB  THR A 169    12696   8933  11424     62  -3205   1806       C  
ATOM   1278  OG1 THR A 169     -62.968  -5.682 -63.383  1.00 86.52           O  
ANISOU 1278  OG1 THR A 169    12290   8788  11795    286  -3195   1726       O  
ATOM   1279  CG2 THR A 169     -63.805  -7.496 -64.728  1.00 91.67           C  
ANISOU 1279  CG2 THR A 169    13042   9615  12175     38  -3468   1657       C  
ATOM   1280  N   SER A 170     -60.488  -8.462 -65.914  1.00 77.50           N  
ANISOU 1280  N   SER A 170    12340   7920   9185   -465  -2672   1934       N  
ATOM   1281  CA  SER A 170     -60.182  -9.556 -66.830  1.00 76.89           C  
ANISOU 1281  CA  SER A 170    12557   7922   8734   -697  -2588   1912       C  
ATOM   1282  C   SER A 170     -59.312 -10.618 -66.169  1.00 72.69           C  
ANISOU 1282  C   SER A 170    11935   7537   8147   -751  -2052   1776       C  
ATOM   1283  O   SER A 170     -59.428 -11.804 -66.495  1.00 73.80           O  
ANISOU 1283  O   SER A 170    12125   7752   8165   -874  -1953   1671       O  
ATOM   1284  CB  SER A 170     -59.493  -9.018 -68.083  1.00 81.68           C  
ANISOU 1284  CB  SER A 170    13734   8417   8884   -890  -2703   2093       C  
ATOM   1285  OG  SER A 170     -58.199  -8.527 -67.778  1.00 82.00           O  
ANISOU 1285  OG  SER A 170    13910   8454   8791   -931  -2318   2135       O  
ATOM   1286  N   MET A 171     -58.433 -10.217 -65.250  1.00 69.38           N  
ANISOU 1286  N   MET A 171    11398   7144   7819   -656  -1728   1773       N  
ATOM   1287  CA  MET A 171     -57.624 -11.200 -64.535  1.00 69.93           C  
ANISOU 1287  CA  MET A 171    11364   7332   7875   -660  -1288   1651       C  
ATOM   1288  C   MET A 171     -58.467 -11.973 -63.526  1.00 66.20           C  
ANISOU 1288  C   MET A 171    10534   6919   7699   -567  -1235   1515       C  
ATOM   1289  O   MET A 171     -58.386 -13.207 -63.445  1.00 63.88           O  
ANISOU 1289  O   MET A 171    10256   6676   7340   -635  -1046   1413       O  
ATOM   1290  CB  MET A 171     -56.450 -10.509 -63.841  1.00 69.95           C  
ANISOU 1290  CB  MET A 171    11334   7353   7890   -592  -1012   1680       C  
ATOM   1291  CG  MET A 171     -55.532 -11.458 -63.086  1.00 72.37           C  
ANISOU 1291  CG  MET A 171    11531   7767   8198   -557   -622   1563       C  
ATOM   1292  SD  MET A 171     -54.195 -10.613 -62.216  1.00 72.67           S  
ANISOU 1292  SD  MET A 171    11472   7855   8284   -477   -357   1571       S  
ATOM   1293  CE  MET A 171     -55.119  -9.696 -60.987  1.00 72.04           C  
ANISOU 1293  CE  MET A 171    11081   7739   8552   -311   -509   1594       C  
ATOM   1294  N   MET A 172     -59.298 -11.262 -62.757  1.00 62.89           N  
ANISOU 1294  N   MET A 172     9810   6477   7609   -431  -1382   1495       N  
ATOM   1295  CA  MET A 172     -60.058 -11.907 -61.692  1.00 63.84           C  
ANISOU 1295  CA  MET A 172     9596   6658   8003   -390  -1262   1339       C  
ATOM   1296  C   MET A 172     -61.119 -12.852 -62.244  1.00 62.05           C  
ANISOU 1296  C   MET A 172     9323   6453   7800   -509  -1426   1233       C  
ATOM   1297  O   MET A 172     -61.400 -13.891 -61.637  1.00 59.21           O  
ANISOU 1297  O   MET A 172     8854   6142   7501   -578  -1214   1102       O  
ATOM   1298  CB  MET A 172     -60.703 -10.857 -60.791  1.00 75.89           C  
ANISOU 1298  CB  MET A 172    10797   8153   9885   -240  -1345   1296       C  
ATOM   1299  CG  MET A 172     -59.710 -10.007 -60.025  1.00 86.44           C  
ANISOU 1299  CG  MET A 172    12146   9477  11219   -147  -1140   1362       C  
ATOM   1300  SD  MET A 172     -60.532  -8.771 -59.007  1.00 94.73           S  
ANISOU 1300  SD  MET A 172    12832  10466  12696     14  -1220   1273       S  
ATOM   1301  CE  MET A 172     -59.145  -7.744 -58.535  1.00 95.43           C  
ANISOU 1301  CE  MET A 172    13074  10523  12660     65  -1028   1387       C  
ATOM   1302  N   LYS A 173     -61.736 -12.509 -63.379  1.00 63.47           N  
ANISOU 1302  N   LYS A 173     9606   6586   7924   -552  -1820   1285       N  
ATOM   1303  CA  LYS A 173     -62.723 -13.422 -63.947  1.00 63.03           C  
ANISOU 1303  CA  LYS A 173     9500   6568   7880   -690  -1999   1166       C  
ATOM   1304  C   LYS A 173     -62.066 -14.707 -64.436  1.00 62.30           C  
ANISOU 1304  C   LYS A 173     9716   6503   7453   -872  -1750   1139       C  
ATOM   1305  O   LYS A 173     -62.663 -15.788 -64.344  1.00 59.14           O  
ANISOU 1305  O   LYS A 173     9236   6139   7095   -997  -1677    990       O  
ATOM   1306  CB  LYS A 173     -63.493 -12.744 -65.083  1.00 61.14           C  
ANISOU 1306  CB  LYS A 173     9331   6267   7632   -689  -2542   1239       C  
ATOM   1307  CG  LYS A 173     -62.684 -12.489 -66.345  1.00 62.28           C  
ANISOU 1307  CG  LYS A 173     9995   6342   7327   -799  -2673   1429       C  
ATOM   1308  CD  LYS A 173     -63.595 -12.147 -67.514  1.00 69.60           C  
ANISOU 1308  CD  LYS A 173    11049   7207   8188   -851  -3255   1489       C  
ATOM   1309  CE  LYS A 173     -62.850 -12.192 -68.838  1.00 65.27           C  
ANISOU 1309  CE  LYS A 173    11098   6602   7101  -1061  -3332   1644       C  
ATOM   1310  NZ  LYS A 173     -63.794 -12.281 -69.985  1.00 69.81           N  
ANISOU 1310  NZ  LYS A 173    11836   7146   7542  -1180  -3883   1666       N  
ATOM   1311  N   VAL A 174     -60.830 -14.612 -64.925  1.00 62.09           N  
ANISOU 1311  N   VAL A 174    10029   6448   7114   -898  -1590   1253       N  
ATOM   1312  CA  VAL A 174     -60.133 -15.777 -65.452  1.00 60.78           C  
ANISOU 1312  CA  VAL A 174    10150   6287   6656  -1048  -1340   1197       C  
ATOM   1313  C   VAL A 174     -59.633 -16.668 -64.321  1.00 56.10           C  
ANISOU 1313  C   VAL A 174     9440   5706   6170   -983   -939   1104       C  
ATOM   1314  O   VAL A 174     -59.772 -17.894 -64.380  1.00 60.55           O  
ANISOU 1314  O   VAL A 174    10085   6248   6673  -1091   -796    991       O  
ATOM   1315  CB  VAL A 174     -58.994 -15.319 -66.381  1.00 63.21           C  
ANISOU 1315  CB  VAL A 174    10833   6565   6621  -1116  -1280   1306       C  
ATOM   1316  CG1 VAL A 174     -57.873 -16.324 -66.388  1.00 64.25           C  
ANISOU 1316  CG1 VAL A 174    11131   6703   6579  -1165   -866   1213       C  
ATOM   1317  CG2 VAL A 174     -59.522 -15.108 -67.792  1.00 65.98           C  
ANISOU 1317  CG2 VAL A 174    11480   6878   6710  -1299  -1646   1365       C  
ATOM   1318  N   VAL A 175     -59.057 -16.076 -63.272  1.00 52.20           N  
ANISOU 1318  N   VAL A 175     8785   5227   5823   -815   -774   1153       N  
ATOM   1319  CA  VAL A 175     -58.589 -16.876 -62.143  1.00 52.20           C  
ANISOU 1319  CA  VAL A 175     8712   5219   5901   -747   -454   1090       C  
ATOM   1320  C   VAL A 175     -59.771 -17.487 -61.395  1.00 56.58           C  
ANISOU 1320  C   VAL A 175     9063   5771   6666   -810   -453    977       C  
ATOM   1321  O   VAL A 175     -59.771 -18.683 -61.066  1.00 61.27           O  
ANISOU 1321  O   VAL A 175     9751   6310   7218   -884   -261    897       O  
ATOM   1322  CB  VAL A 175     -57.702 -16.026 -61.215  1.00 50.83           C  
ANISOU 1322  CB  VAL A 175     8429   5074   5810   -576   -320   1166       C  
ATOM   1323  CG1 VAL A 175     -57.232 -16.852 -60.030  1.00 47.76           C  
ANISOU 1323  CG1 VAL A 175     8006   4665   5475   -502    -56   1120       C  
ATOM   1324  CG2 VAL A 175     -56.513 -15.475 -61.988  1.00 48.58           C  
ANISOU 1324  CG2 VAL A 175     8337   4801   5321   -564   -275   1239       C  
ATOM   1325  N   GLU A 176     -60.799 -16.676 -61.124  1.00 57.24           N  
ANISOU 1325  N   GLU A 176     8866   5895   6989   -793   -656    950       N  
ATOM   1326  CA  GLU A 176     -62.030 -17.187 -60.531  1.00 64.63           C  
ANISOU 1326  CA  GLU A 176     9561   6848   8148   -901   -645    789       C  
ATOM   1327  C   GLU A 176     -62.701 -18.236 -61.407  1.00 67.84           C  
ANISOU 1327  C   GLU A 176    10075   7243   8459  -1105   -737    683       C  
ATOM   1328  O   GLU A 176     -63.462 -19.063 -60.892  1.00 68.85           O  
ANISOU 1328  O   GLU A 176    10097   7366   8698  -1255   -609    531       O  
ATOM   1329  CB  GLU A 176     -63.001 -16.037 -60.264  1.00 68.54           C  
ANISOU 1329  CB  GLU A 176     9690   7389   8961   -825   -873    737       C  
ATOM   1330  CG  GLU A 176     -62.891 -15.440 -58.871  1.00 77.73           C  
ANISOU 1330  CG  GLU A 176    10646   8566  10321   -722   -659    709       C  
ATOM   1331  CD  GLU A 176     -63.426 -16.367 -57.792  1.00 88.61           C  
ANISOU 1331  CD  GLU A 176    11927   9952  11787   -876   -361    545       C  
ATOM   1332  OE1 GLU A 176     -64.218 -17.279 -58.121  1.00 95.98           O  
ANISOU 1332  OE1 GLU A 176    12839  10890  12740  -1063   -369    413       O  
ATOM   1333  OE2 GLU A 176     -63.056 -16.183 -56.613  1.00 91.83           O  
ANISOU 1333  OE2 GLU A 176    12312  10357  12224   -840   -117    546       O  
ATOM   1334  N   GLN A 177     -62.452 -18.210 -62.717  1.00 68.11           N  
ANISOU 1334  N   GLN A 177    10339   7269   8271  -1151   -943    748       N  
ATOM   1335  CA  GLN A 177     -62.879 -19.301 -63.583  1.00 65.30           C  
ANISOU 1335  CA  GLN A 177    10160   6893   7756  -1367   -993    645       C  
ATOM   1336  C   GLN A 177     -61.995 -20.529 -63.413  1.00 61.17           C  
ANISOU 1336  C   GLN A 177     9933   6275   7034  -1418   -633    620       C  
ATOM   1337  O   GLN A 177     -62.482 -21.660 -63.515  1.00 63.68           O  
ANISOU 1337  O   GLN A 177    10336   6540   7317  -1601   -542    487       O  
ATOM   1338  CB  GLN A 177     -62.871 -18.836 -65.043  1.00 70.03           C  
ANISOU 1338  CB  GLN A 177    10967   7505   8134  -1425  -1334    722       C  
ATOM   1339  CG  GLN A 177     -62.905 -19.950 -66.081  1.00 75.04           C  
ANISOU 1339  CG  GLN A 177    11912   8109   8491  -1659  -1332    633       C  
ATOM   1340  CD  GLN A 177     -64.189 -20.748 -66.037  1.00 83.22           C  
ANISOU 1340  CD  GLN A 177    12759   9177   9684  -1852  -1431    439       C  
ATOM   1341  OE1 GLN A 177     -65.220 -20.258 -65.576  1.00 87.70           O  
ANISOU 1341  OE1 GLN A 177    12939   9815  10566  -1823  -1628    367       O  
ATOM   1342  NE2 GLN A 177     -64.134 -21.988 -66.511  1.00 85.84           N  
ANISOU 1342  NE2 GLN A 177    13347   9450   9818  -2061  -1276    323       N  
ATOM   1343  N   ARG A 178     -60.710 -20.328 -63.118  1.00 56.36           N  
ANISOU 1343  N   ARG A 178     9465   5629   6321  -1252   -432    729       N  
ATOM   1344  CA  ARG A 178     -59.755 -21.430 -63.117  1.00 52.72           C  
ANISOU 1344  CA  ARG A 178     9281   5057   5694  -1247   -144    697       C  
ATOM   1345  C   ARG A 178     -59.835 -22.262 -61.841  1.00 53.25           C  
ANISOU 1345  C   ARG A 178     9317   5028   5886  -1224     93    654       C  
ATOM   1346  O   ARG A 178     -59.898 -23.495 -61.905  1.00 58.28           O  
ANISOU 1346  O   ARG A 178    10159   5534   6448  -1335    239    564       O  
ATOM   1347  CB  ARG A 178     -58.338 -20.889 -63.311  1.00 51.64           C  
ANISOU 1347  CB  ARG A 178     9257   4929   5435  -1078    -36    793       C  
ATOM   1348  CG  ARG A 178     -57.242 -21.931 -63.180  1.00 49.52           C  
ANISOU 1348  CG  ARG A 178     9195   4541   5079  -1000    253    736       C  
ATOM   1349  CD  ARG A 178     -57.351 -23.002 -64.256  1.00 56.20           C  
ANISOU 1349  CD  ARG A 178    10317   5296   5739  -1182    307    604       C  
ATOM   1350  NE  ARG A 178     -56.186 -23.882 -64.252  1.00 59.58           N  
ANISOU 1350  NE  ARG A 178    10928   5592   6117  -1066    580    525       N  
ATOM   1351  CZ  ARG A 178     -56.002 -24.889 -65.100  1.00 60.96           C  
ANISOU 1351  CZ  ARG A 178    11363   5651   6147  -1183    706    379       C  
ATOM   1352  NH1 ARG A 178     -56.912 -25.156 -66.029  1.00 60.49           N  
ANISOU 1352  NH1 ARG A 178    11436   5608   5940  -1451    576    306       N  
ATOM   1353  NH2 ARG A 178     -54.906 -25.632 -65.020  1.00 60.48           N  
ANISOU 1353  NH2 ARG A 178    11420   5452   6106  -1027    950    286       N  
ATOM   1354  N   HIS A 179     -59.831 -21.614 -60.669  1.00 48.84           N  
ANISOU 1354  N   HIS A 179     8551   4511   5495  -1100    138    717       N  
ATOM   1355  CA  HIS A 179     -59.643 -22.396 -59.446  1.00 52.11           C  
ANISOU 1355  CA  HIS A 179     9044   4808   5945  -1078    371    711       C  
ATOM   1356  C   HIS A 179     -60.774 -23.380 -59.123  1.00 56.65           C  
ANISOU 1356  C   HIS A 179     9653   5302   6568  -1329    457    578       C  
ATOM   1357  O   HIS A 179     -60.522 -24.355 -58.403  1.00 50.84           O  
ANISOU 1357  O   HIS A 179     9145   4400   5773  -1357    657    579       O  
ATOM   1358  CB  HIS A 179     -59.375 -21.475 -58.244  1.00 48.69           C  
ANISOU 1358  CB  HIS A 179     8422   4442   5635   -930    409    796       C  
ATOM   1359  CG  HIS A 179     -60.562 -20.695 -57.768  1.00 51.46           C  
ANISOU 1359  CG  HIS A 179     8457   4900   6193  -1027    329    728       C  
ATOM   1360  ND1 HIS A 179     -61.620 -21.274 -57.102  1.00 52.90           N  
ANISOU 1360  ND1 HIS A 179     8571   5052   6476  -1236    446    597       N  
ATOM   1361  CD2 HIS A 179     -60.833 -19.368 -57.821  1.00 57.34           C  
ANISOU 1361  CD2 HIS A 179     8930   5768   7088   -942    163    749       C  
ATOM   1362  CE1 HIS A 179     -62.504 -20.343 -56.789  1.00 54.53           C  
ANISOU 1362  CE1 HIS A 179     8430   5377   6911  -1268    364    512       C  
ATOM   1363  NE2 HIS A 179     -62.049 -19.178 -57.212  1.00 58.00           N  
ANISOU 1363  NE2 HIS A 179     8748   5898   7392  -1072    175    611       N  
ATOM   1364  N   PRO A 180     -62.011 -23.206 -59.609  1.00 59.73           N  
ANISOU 1364  N   PRO A 180     9840   5789   7067  -1525    307    456       N  
ATOM   1365  CA  PRO A 180     -63.001 -24.285 -59.445  1.00 54.26           C  
ANISOU 1365  CA  PRO A 180     9199   5016   6400  -1812    422    292       C  
ATOM   1366  C   PRO A 180     -62.715 -25.531 -60.273  1.00 72.75           C  
ANISOU 1366  C   PRO A 180    11900   7202   8541  -1926    489    242       C  
ATOM   1367  O   PRO A 180     -63.440 -26.525 -60.135  1.00 57.73           O  
ANISOU 1367  O   PRO A 180    10102   5197   6635  -2185    614    105       O  
ATOM   1368  CB  PRO A 180     -64.316 -23.627 -59.887  1.00 55.92           C  
ANISOU 1368  CB  PRO A 180     9024   5404   6820  -1954    184    150       C  
ATOM   1369  CG  PRO A 180     -64.103 -22.184 -59.652  1.00 55.03           C  
ANISOU 1369  CG  PRO A 180     8645   5418   6847  -1720     28    253       C  
ATOM   1370  CD  PRO A 180     -62.672 -21.953 -60.021  1.00 55.79           C  
ANISOU 1370  CD  PRO A 180     9003   5465   6729  -1492     34    446       C  
ATOM   1371  N   GLU A 181     -61.694 -25.519 -61.128  1.00 65.13           N  
ANISOU 1371  N   GLU A 181    11131   6207   7409  -1770    442    320       N  
ATOM   1372  CA  GLU A 181     -61.379 -26.672 -61.960  1.00 61.29           C  
ANISOU 1372  CA  GLU A 181    10985   5562   6741  -1873    531    238       C  
ATOM   1373  C   GLU A 181     -60.237 -27.517 -61.413  1.00 56.10           C  
ANISOU 1373  C   GLU A 181    10634   4670   6013  -1695    772    295       C  
ATOM   1374  O   GLU A 181     -60.011 -28.620 -61.919  1.00 57.84           O  
ANISOU 1374  O   GLU A 181    11156   4700   6122  -1772    891    203       O  
ATOM   1375  CB  GLU A 181     -61.036 -26.220 -63.386  1.00 65.68           C  
ANISOU 1375  CB  GLU A 181    11593   6220   7142  -1866    351    233       C  
ATOM   1376  CG  GLU A 181     -62.218 -25.654 -64.156  1.00 74.75           C  
ANISOU 1376  CG  GLU A 181    12536   7545   8322  -2064     40    164       C  
ATOM   1377  CD  GLU A 181     -61.845 -25.204 -65.558  1.00 79.24           C  
ANISOU 1377  CD  GLU A 181    13254   8187   8665  -2087   -157    189       C  
ATOM   1378  OE1 GLU A 181     -60.654 -24.910 -65.796  1.00 80.97           O  
ANISOU 1378  OE1 GLU A 181    13627   8381   8756  -1918    -46    276       O  
ATOM   1379  OE2 GLU A 181     -62.744 -25.147 -66.424  1.00 83.51           O  
ANISOU 1379  OE2 GLU A 181    13768   8814   9149  -2295   -426    108       O  
ATOM   1380  N   LEU A 182     -59.522 -27.038 -60.400  1.00 54.25           N  
ANISOU 1380  N   LEU A 182    10332   4432   5850  -1454    826    432       N  
ATOM   1381  CA  LEU A 182     -58.365 -27.759 -59.891  1.00 54.31           C  
ANISOU 1381  CA  LEU A 182    10599   4219   5818  -1232    977    493       C  
ATOM   1382  C   LEU A 182     -58.789 -28.868 -58.934  1.00 56.00           C  
ANISOU 1382  C   LEU A 182    11073   4178   6024  -1354   1124    487       C  
ATOM   1383  O   LEU A 182     -59.763 -28.733 -58.188  1.00 56.25           O  
ANISOU 1383  O   LEU A 182    11011   4256   6106  -1557   1152    480       O  
ATOM   1384  CB  LEU A 182     -57.405 -26.795 -59.193  1.00 55.62           C  
ANISOU 1384  CB  LEU A 182    10593   4490   6052   -937    934    636       C  
ATOM   1385  CG  LEU A 182     -56.800 -25.693 -60.070  1.00 50.72           C  
ANISOU 1385  CG  LEU A 182     9772   4082   5418   -821    828    651       C  
ATOM   1386  CD1 LEU A 182     -55.835 -24.829 -59.267  1.00 48.89           C  
ANISOU 1386  CD1 LEU A 182     9378   3936   5262   -560    812    770       C  
ATOM   1387  CD2 LEU A 182     -56.107 -26.286 -61.289  1.00 52.09           C  
ANISOU 1387  CD2 LEU A 182    10136   4179   5477   -807    901    540       C  
ATOM   1388  N   THR A 183     -58.054 -29.979 -58.974  1.00 63.05           N  
ANISOU 1388  N   THR A 183    12313   4783   6859  -1242   1233    475       N  
ATOM   1389  CA  THR A 183     -58.309 -31.105 -58.085  1.00 64.25           C  
ANISOU 1389  CA  THR A 183    12821   4621   6971  -1341   1361    499       C  
ATOM   1390  C   THR A 183     -57.612 -30.967 -56.742  1.00 65.80           C  
ANISOU 1390  C   THR A 183    13107   4712   7181  -1105   1340    683       C  
ATOM   1391  O   THR A 183     -57.974 -31.674 -55.796  1.00 61.01           O  
ANISOU 1391  O   THR A 183    12806   3872   6504  -1238   1426    742       O  
ATOM   1392  CB  THR A 183     -57.866 -32.416 -58.744  1.00 62.29           C  
ANISOU 1392  CB  THR A 183    12950   4051   6667  -1315   1462    399       C  
ATOM   1393  OG1 THR A 183     -56.505 -32.293 -59.181  1.00 61.83           O  
ANISOU 1393  OG1 THR A 183    12862   3970   6661   -943   1426    405       O  
ATOM   1394  CG2 THR A 183     -58.752 -32.746 -59.933  1.00 63.52           C  
ANISOU 1394  CG2 THR A 183    13102   4272   6759  -1644   1496    203       C  
ATOM   1395  N   ASN A 184     -56.625 -30.083 -56.644  1.00 66.44           N  
ANISOU 1395  N   ASN A 184    12960   4955   7330   -790   1227    769       N  
ATOM   1396  CA  ASN A 184     -55.909 -29.836 -55.401  1.00 66.06           C  
ANISOU 1396  CA  ASN A 184    12962   4849   7289   -560   1158    936       C  
ATOM   1397  C   ASN A 184     -56.565 -28.670 -54.671  1.00 65.86           C  
ANISOU 1397  C   ASN A 184    12652   5095   7275   -697   1133    992       C  
ATOM   1398  O   ASN A 184     -56.552 -27.538 -55.165  1.00 69.64           O  
ANISOU 1398  O   ASN A 184    12760   5866   7834   -654   1062    965       O  
ATOM   1399  CB  ASN A 184     -54.440 -29.532 -55.689  1.00 66.62           C  
ANISOU 1399  CB  ASN A 184    12905   4954   7453   -156   1057    955       C  
ATOM   1400  CG  ASN A 184     -53.573 -29.592 -54.452  1.00 68.72           C  
ANISOU 1400  CG  ASN A 184    13293   5089   7729    114    936   1112       C  
ATOM   1401  OD1 ASN A 184     -53.996 -29.212 -53.358  1.00 70.19           O  
ANISOU 1401  OD1 ASN A 184    13517   5315   7836      6    906   1232       O  
ATOM   1402  ND2 ASN A 184     -52.352 -30.070 -54.616  1.00 70.71           N  
ANISOU 1402  ND2 ASN A 184    13602   5183   8082    463    860   1092       N  
ATOM   1403  N   LEU A 185     -57.139 -28.948 -53.499  1.00 69.52           N  
ANISOU 1403  N   LEU A 185    13319   5442   7653   -877   1206   1060       N  
ATOM   1404  CA  LEU A 185     -57.813 -27.901 -52.740  1.00 66.88           C  
ANISOU 1404  CA  LEU A 185    12725   5344   7341  -1033   1233   1070       C  
ATOM   1405  C   LEU A 185     -56.842 -26.826 -52.269  1.00 63.55           C  
ANISOU 1405  C   LEU A 185    12085   5097   6963   -739   1094   1180       C  
ATOM   1406  O   LEU A 185     -57.225 -25.655 -52.160  1.00 66.65           O  
ANISOU 1406  O   LEU A 185    12131   5752   7440   -789   1082   1148       O  
ATOM   1407  CB  LEU A 185     -58.547 -28.509 -51.544  1.00 73.13           C  
ANISOU 1407  CB  LEU A 185    13844   5952   7991  -1328   1393   1097       C  
ATOM   1408  CG  LEU A 185     -59.777 -29.364 -51.852  1.00 77.98           C  
ANISOU 1408  CG  LEU A 185    14574   6474   8581  -1722   1577    933       C  
ATOM   1409  CD1 LEU A 185     -60.279 -30.049 -50.589  1.00 79.78           C  
ANISOU 1409  CD1 LEU A 185    15051   6617   8645  -1939   1704    911       C  
ATOM   1410  CD2 LEU A 185     -60.877 -28.516 -52.476  1.00 77.36           C  
ANISOU 1410  CD2 LEU A 185    14020   6696   8678  -1942   1615    750       C  
ATOM   1411  N   ALA A 186     -55.592 -27.199 -51.987  1.00 62.82           N  
ANISOU 1411  N   ALA A 186    12177   4854   6837   -427    977   1292       N  
ATOM   1412  CA  ALA A 186     -54.618 -26.222 -51.512  1.00 62.26           C  
ANISOU 1412  CA  ALA A 186    11890   4953   6812   -166    836   1375       C  
ATOM   1413  C   ALA A 186     -54.327 -25.170 -52.575  1.00 57.50           C  
ANISOU 1413  C   ALA A 186    10861   4634   6352    -64    798   1291       C  
ATOM   1414  O   ALA A 186     -54.264 -23.972 -52.272  1.00 59.92           O  
ANISOU 1414  O   ALA A 186    10891   5169   6708    -45    757   1309       O  
ATOM   1415  CB  ALA A 186     -53.333 -26.930 -51.083  1.00 61.66           C  
ANISOU 1415  CB  ALA A 186    12061   4652   6714    164    682   1477       C  
ATOM   1416  N   HIS A 187     -54.153 -25.598 -53.828  1.00 55.43           N  
ANISOU 1416  N   HIS A 187    10584   4342   6137    -24    820   1194       N  
ATOM   1417  CA  HIS A 187     -53.913 -24.650 -54.911  1.00 56.05           C  
ANISOU 1417  CA  HIS A 187    10346   4659   6292     16    794   1122       C  
ATOM   1418  C   HIS A 187     -55.090 -23.697 -55.075  1.00 57.07           C  
ANISOU 1418  C   HIS A 187    10245   4990   6450   -221    792   1095       C  
ATOM   1419  O   HIS A 187     -54.907 -22.481 -55.220  1.00 53.79           O  
ANISOU 1419  O   HIS A 187     9565   4779   6095   -170    726   1111       O  
ATOM   1420  CB  HIS A 187     -53.645 -25.404 -56.213  1.00 56.70           C  
ANISOU 1420  CB  HIS A 187    10531   4647   6366     32    850   1004       C  
ATOM   1421  CG  HIS A 187     -52.410 -26.245 -56.177  1.00 59.71           C  
ANISOU 1421  CG  HIS A 187    11064   4833   6789    313    854    981       C  
ATOM   1422  ND1 HIS A 187     -51.399 -26.042 -55.262  1.00 62.48           N  
ANISOU 1422  ND1 HIS A 187    11360   5173   7206    582    753   1060       N  
ATOM   1423  CD2 HIS A 187     -52.021 -27.293 -56.940  1.00 62.77           C  
ANISOU 1423  CD2 HIS A 187    11639   5022   7190    381    933    865       C  
ATOM   1424  CE1 HIS A 187     -50.440 -26.927 -55.465  1.00 64.68           C  
ANISOU 1424  CE1 HIS A 187    11757   5252   7567    830    747    992       C  
ATOM   1425  NE2 HIS A 187     -50.793 -27.699 -56.477  1.00 66.21           N  
ANISOU 1425  NE2 HIS A 187    12103   5320   7735    716    875    867       N  
ATOM   1426  N   ALA A 188     -56.311 -24.238 -55.053  1.00 60.35           N  
ANISOU 1426  N   ALA A 188    10751   5335   6845   -483    858   1036       N  
ATOM   1427  CA  ALA A 188     -57.494 -23.391 -55.150  1.00 58.98           C  
ANISOU 1427  CA  ALA A 188    10311   5341   6760   -686    835    974       C  
ATOM   1428  C   ALA A 188     -57.540 -22.386 -54.007  1.00 60.41           C  
ANISOU 1428  C   ALA A 188    10313   5638   7002   -654    838   1028       C  
ATOM   1429  O   ALA A 188     -57.907 -21.221 -54.207  1.00 57.38           O  
ANISOU 1429  O   ALA A 188     9631   5433   6736   -657    762   1001       O  
ATOM   1430  CB  ALA A 188     -58.756 -24.253 -55.163  1.00 55.25           C  
ANISOU 1430  CB  ALA A 188     9941   4771   6282   -989    931    862       C  
ATOM   1431  N   GLN A 189     -57.148 -22.814 -52.804  1.00 59.38           N  
ANISOU 1431  N   GLN A 189    10394   5387   6781   -623    911   1104       N  
ATOM   1432  CA  GLN A 189     -57.160 -21.908 -51.661  1.00 59.86           C  
ANISOU 1432  CA  GLN A 189    10334   5551   6859   -625    932   1141       C  
ATOM   1433  C   GLN A 189     -56.121 -20.803 -51.816  1.00 53.19           C  
ANISOU 1433  C   GLN A 189     9278   4863   6069   -377    805   1204       C  
ATOM   1434  O   GLN A 189     -56.378 -19.650 -51.450  1.00 51.66           O  
ANISOU 1434  O   GLN A 189     8844   4819   5963   -398    799   1181       O  
ATOM   1435  CB  GLN A 189     -56.927 -22.687 -50.368  1.00 64.57           C  
ANISOU 1435  CB  GLN A 189    11288   5963   7281   -675   1010   1225       C  
ATOM   1436  CG  GLN A 189     -57.116 -21.844 -49.122  1.00 67.78           C  
ANISOU 1436  CG  GLN A 189    11627   6469   7658   -763   1073   1232       C  
ATOM   1437  CD  GLN A 189     -58.479 -21.179 -49.081  1.00 72.89           C  
ANISOU 1437  CD  GLN A 189    11987   7253   8455  -1023   1221   1059       C  
ATOM   1438  OE1 GLN A 189     -59.511 -21.850 -49.104  1.00 77.82           O  
ANISOU 1438  OE1 GLN A 189    12678   7803   9085  -1290   1371    947       O  
ATOM   1439  NE2 GLN A 189     -58.488 -19.850 -49.032  1.00 75.20           N  
ANISOU 1439  NE2 GLN A 189    11941   7737   8895   -946   1178   1015       N  
ATOM   1440  N   MET A 190     -54.941 -21.132 -52.348  1.00 52.06           N  
ANISOU 1440  N   MET A 190     9212   4678   5891   -152    724   1256       N  
ATOM   1441  CA  MET A 190     -53.940 -20.099 -52.595  1.00 56.42           C  
ANISOU 1441  CA  MET A 190     9547   5387   6501     38    637   1280       C  
ATOM   1442  C   MET A 190     -54.436 -19.094 -53.629  1.00 59.94           C  
ANISOU 1442  C   MET A 190     9749   5985   7040    -34    604   1227       C  
ATOM   1443  O   MET A 190     -54.302 -17.876 -53.441  1.00 61.90           O  
ANISOU 1443  O   MET A 190     9796   6367   7355     -5    564   1240       O  
ATOM   1444  CB  MET A 190     -52.623 -20.735 -53.041  1.00 61.52           C  
ANISOU 1444  CB  MET A 190    10285   5961   7128    269    593   1288       C  
ATOM   1445  CG  MET A 190     -52.057 -21.736 -52.040  1.00 69.08           C  
ANISOU 1445  CG  MET A 190    11505   6728   8015    398    548   1359       C  
ATOM   1446  SD  MET A 190     -50.491 -22.483 -52.545  1.00 78.23           S  
ANISOU 1446  SD  MET A 190    12693   7784   9245    730    471   1318       S  
ATOM   1447  CE  MET A 190     -49.348 -21.169 -52.129  1.00 77.64           C  
ANISOU 1447  CE  MET A 190    12286   7958   9254    894    375   1314       C  
ATOM   1448  N   LEU A 191     -55.033 -19.585 -54.720  1.00 56.73           N  
ANISOU 1448  N   LEU A 191     9389   5538   6627   -138    599   1170       N  
ATOM   1449  CA  LEU A 191     -55.579 -18.681 -55.728  1.00 53.98           C  
ANISOU 1449  CA  LEU A 191     8867   5304   6339   -212    504   1140       C  
ATOM   1450  C   LEU A 191     -56.637 -17.762 -55.125  1.00 53.26           C  
ANISOU 1450  C   LEU A 191     8557   5288   6390   -307    466   1115       C  
ATOM   1451  O   LEU A 191     -56.594 -16.542 -55.318  1.00 56.65           O  
ANISOU 1451  O   LEU A 191     8813   5810   6900   -258    375   1137       O  
ATOM   1452  CB  LEU A 191     -56.153 -19.482 -56.898  1.00 48.86           C  
ANISOU 1452  CB  LEU A 191     8341   4593   5632   -340    477   1074       C  
ATOM   1453  CG  LEU A 191     -55.112 -20.223 -57.741  1.00 45.86           C  
ANISOU 1453  CG  LEU A 191     8152   4144   5130   -256    534   1054       C  
ATOM   1454  CD1 LEU A 191     -55.770 -21.098 -58.796  1.00 46.60           C  
ANISOU 1454  CD1 LEU A 191     8404   4160   5141   -422    527    969       C  
ATOM   1455  CD2 LEU A 191     -54.152 -19.232 -58.385  1.00 45.92           C  
ANISOU 1455  CD2 LEU A 191     8072   4269   5108   -163    506   1078       C  
ATOM   1456  N   LYS A 192     -57.586 -18.331 -54.376  1.00 52.16           N  
ANISOU 1456  N   LYS A 192     8431   5094   6292   -454    557   1049       N  
ATOM   1457  CA  LYS A 192     -58.632 -17.514 -53.765  1.00 59.00           C  
ANISOU 1457  CA  LYS A 192     9049   6031   7335   -555    568    965       C  
ATOM   1458  C   LYS A 192     -58.047 -16.480 -52.809  1.00 60.70           C  
ANISOU 1458  C   LYS A 192     9168   6313   7582   -449    603   1009       C  
ATOM   1459  O   LYS A 192     -58.501 -15.328 -52.773  1.00 63.09           O  
ANISOU 1459  O   LYS A 192     9230   6688   8055   -433    544    961       O  
ATOM   1460  CB  LYS A 192     -59.640 -18.404 -53.036  1.00 60.68           C  
ANISOU 1460  CB  LYS A 192     9318   6175   7563   -781    734    851       C  
ATOM   1461  CG  LYS A 192     -60.506 -19.249 -53.956  1.00 66.62           C  
ANISOU 1461  CG  LYS A 192    10088   6885   8339   -941    697    756       C  
ATOM   1462  CD  LYS A 192     -61.529 -20.057 -53.172  1.00 70.58           C  
ANISOU 1462  CD  LYS A 192    10628   7322   8865  -1216    904    613       C  
ATOM   1463  CE  LYS A 192     -60.856 -21.052 -52.240  1.00 72.94           C  
ANISOU 1463  CE  LYS A 192    11327   7457   8931  -1250   1082    709       C  
ATOM   1464  NZ  LYS A 192     -61.847 -21.864 -51.474  1.00 75.13           N  
ANISOU 1464  NZ  LYS A 192    11721   7644   9183  -1578   1319    576       N  
ATOM   1465  N   SER A 193     -57.032 -16.868 -52.033  1.00 57.97           N  
ANISOU 1465  N   SER A 193     9014   5930   7083   -368    675   1092       N  
ATOM   1466  CA  SER A 193     -56.445 -15.944 -51.067  1.00 58.62           C  
ANISOU 1466  CA  SER A 193     9024   6083   7167   -295    697   1122       C  
ATOM   1467  C   SER A 193     -55.761 -14.773 -51.766  1.00 57.46           C  
ANISOU 1467  C   SER A 193     8714   6030   7089   -153    577   1162       C  
ATOM   1468  O   SER A 193     -55.947 -13.610 -51.381  1.00 56.29           O  
ANISOU 1468  O   SER A 193     8392   5942   7053   -153    574   1128       O  
ATOM   1469  CB  SER A 193     -55.460 -16.685 -50.162  1.00 61.87           C  
ANISOU 1469  CB  SER A 193     9690   6429   7389   -226    729   1210       C  
ATOM   1470  OG  SER A 193     -54.425 -17.284 -50.920  1.00 67.70           O  
ANISOU 1470  OG  SER A 193    10533   7128   8062    -56    640   1277       O  
ATOM   1471  N   GLU A 194     -54.961 -15.056 -52.800  1.00 56.47           N  
ANISOU 1471  N   GLU A 194     8663   5902   6891    -55    503   1218       N  
ATOM   1472  CA  GLU A 194     -54.303 -13.965 -53.516  1.00 56.44           C  
ANISOU 1472  CA  GLU A 194     8555   5973   6915     21    425   1249       C  
ATOM   1473  C   GLU A 194     -55.318 -13.091 -54.245  1.00 54.88           C  
ANISOU 1473  C   GLU A 194     8229   5775   6849    -45    312   1228       C  
ATOM   1474  O   GLU A 194     -55.135 -11.871 -54.348  1.00 57.08           O  
ANISOU 1474  O   GLU A 194     8410   6081   7196    -12    253   1250       O  
ATOM   1475  CB  GLU A 194     -53.264 -14.517 -54.489  1.00 57.39           C  
ANISOU 1475  CB  GLU A 194     8793   6092   6920     93    422   1272       C  
ATOM   1476  CG  GLU A 194     -52.289 -15.513 -53.876  1.00 64.62           C  
ANISOU 1476  CG  GLU A 194     9817   6974   7760    210    483   1274       C  
ATOM   1477  CD  GLU A 194     -51.521 -14.953 -52.689  1.00 68.00           C  
ANISOU 1477  CD  GLU A 194    10164   7473   8198    294    481   1292       C  
ATOM   1478  OE1 GLU A 194     -51.250 -13.733 -52.665  1.00 70.51           O  
ANISOU 1478  OE1 GLU A 194    10335   7889   8566    280    470   1287       O  
ATOM   1479  OE2 GLU A 194     -51.186 -15.740 -51.777  1.00 68.56           O  
ANISOU 1479  OE2 GLU A 194    10350   7487   8214    363    473   1315       O  
ATOM   1480  N   LEU A 195     -56.394 -13.696 -54.757  1.00 55.79           N  
ANISOU 1480  N   LEU A 195     8346   5842   7009   -136    259   1182       N  
ATOM   1481  CA  LEU A 195     -57.490 -12.914 -55.320  1.00 58.89           C  
ANISOU 1481  CA  LEU A 195     8578   6224   7574   -173     93   1144       C  
ATOM   1482  C   LEU A 195     -58.036 -11.929 -54.294  1.00 61.89           C  
ANISOU 1482  C   LEU A 195     8734   6617   8165   -156    131   1070       C  
ATOM   1483  O   LEU A 195     -58.213 -10.739 -54.587  1.00 65.66           O  
ANISOU 1483  O   LEU A 195     9098   7073   8778    -91     -3   1083       O  
ATOM   1484  CB  LEU A 195     -58.598 -13.842 -55.818  1.00 61.56           C  
ANISOU 1484  CB  LEU A 195     8908   6531   7953   -292     37   1063       C  
ATOM   1485  CG  LEU A 195     -58.369 -14.543 -57.157  1.00 64.83           C  
ANISOU 1485  CG  LEU A 195     9524   6918   8190   -335    -65   1108       C  
ATOM   1486  CD1 LEU A 195     -59.474 -15.555 -57.421  1.00 69.92           C  
ANISOU 1486  CD1 LEU A 195    10155   7536   8877   -484    -90    999       C  
ATOM   1487  CD2 LEU A 195     -58.297 -13.520 -58.280  1.00 64.61           C  
ANISOU 1487  CD2 LEU A 195     9521   6887   8140   -301   -299   1189       C  
ATOM   1488  N   GLY A 196     -58.301 -12.412 -53.078  1.00 61.40           N  
ANISOU 1488  N   GLY A 196     8640   6567   8121   -227    324    985       N  
ATOM   1489  CA  GLY A 196     -58.733 -11.516 -52.018  1.00 59.62           C  
ANISOU 1489  CA  GLY A 196     8228   6357   8067   -241    421    881       C  
ATOM   1490  C   GLY A 196     -57.740 -10.398 -51.765  1.00 55.67           C  
ANISOU 1490  C   GLY A 196     7737   5879   7538   -133    405    955       C  
ATOM   1491  O   GLY A 196     -58.127  -9.236 -51.597  1.00 54.38           O  
ANISOU 1491  O   GLY A 196     7402   5689   7571    -92    366    892       O  
ATOM   1492  N   THR A 197     -56.443 -10.730 -51.753  1.00 51.99           N  
ANISOU 1492  N   THR A 197     7454   5450   6849    -83    432   1069       N  
ATOM   1493  CA  THR A 197     -55.418  -9.710 -51.546  1.00 52.57           C  
ANISOU 1493  CA  THR A 197     7523   5562   6889    -14    427   1117       C  
ATOM   1494  C   THR A 197     -55.508  -8.612 -52.601  1.00 53.89           C  
ANISOU 1494  C   THR A 197     7639   5677   7158     33    271   1160       C  
ATOM   1495  O   THR A 197     -55.524  -7.420 -52.271  1.00 57.61           O  
ANISOU 1495  O   THR A 197     8021   6116   7751     54    263   1131       O  
ATOM   1496  CB  THR A 197     -54.028 -10.348 -51.552  1.00 51.00           C  
ANISOU 1496  CB  THR A 197     7475   5423   6478     40    455   1197       C  
ATOM   1497  OG1 THR A 197     -53.849 -11.121 -50.360  1.00 52.98           O  
ANISOU 1497  OG1 THR A 197     7810   5691   6629     17    551   1179       O  
ATOM   1498  CG2 THR A 197     -52.948  -9.275 -51.621  1.00 47.93           C  
ANISOU 1498  CG2 THR A 197     7049   5091   6071     82    443   1222       C  
ATOM   1499  N   VAL A 198     -55.582  -8.995 -53.877  1.00 50.00           N  
ANISOU 1499  N   VAL A 198     7245   5153   6601     35    140   1231       N  
ATOM   1500  CA  VAL A 198     -55.652  -7.995 -54.942  1.00 54.88           C  
ANISOU 1500  CA  VAL A 198     7907   5692   7254     53    -41   1303       C  
ATOM   1501  C   VAL A 198     -56.909  -7.142 -54.794  1.00 61.21           C  
ANISOU 1501  C   VAL A 198     8526   6393   8340     98   -182   1236       C  
ATOM   1502  O   VAL A 198     -56.857  -5.901 -54.862  1.00 59.85           O  
ANISOU 1502  O   VAL A 198     8342   6128   8273    148   -267   1261       O  
ATOM   1503  CB  VAL A 198     -55.588  -8.677 -56.322  1.00 53.33           C  
ANISOU 1503  CB  VAL A 198     7896   5478   6890      7   -156   1378       C  
ATOM   1504  CG1 VAL A 198     -55.725  -7.647 -57.427  1.00 54.30           C  
ANISOU 1504  CG1 VAL A 198     8143   5492   6996     -6   -374   1475       C  
ATOM   1505  CG2 VAL A 198     -54.288  -9.447 -56.472  1.00 48.07           C  
ANISOU 1505  CG2 VAL A 198     7370   4897   5998    -15     10   1397       C  
ATOM   1506  N  AARG A 199     -58.059  -7.799 -54.591  0.40 62.82           N  
ANISOU 1506  N  AARG A 199     8574   6600   8694     80   -203   1129       N  
ATOM   1507  N  BARG A 199     -58.053  -7.792 -54.559  0.60 62.66           N  
ANISOU 1507  N  BARG A 199     8551   6581   8675     80   -198   1126       N  
ATOM   1508  CA AARG A 199     -59.324  -7.078 -54.475  0.40 64.06           C  
ANISOU 1508  CA AARG A 199     8482   6671   9187    140   -340   1011       C  
ATOM   1509  CA BARG A 199     -59.322  -7.073 -54.485  0.60 63.59           C  
ANISOU 1509  CA BARG A 199     8424   6611   9127    141   -343   1012       C  
ATOM   1510  C  AARG A 199     -59.277  -6.047 -53.356  0.40 64.82           C  
ANISOU 1510  C  AARG A 199     8433   6736   9460    183   -196    909       C  
ATOM   1511  C  BARG A 199     -59.336  -6.071 -53.335  0.60 64.81           C  
ANISOU 1511  C  BARG A 199     8420   6736   9470    182   -194    900       C  
ATOM   1512  O  AARG A 199     -59.744  -4.914 -53.526  0.40 73.51           O  
ANISOU 1512  O  AARG A 199     9425   7706  10801    289   -351    878       O  
ATOM   1513  O  BARG A 199     -59.902  -4.978 -53.464  0.60 74.15           O  
ANISOU 1513  O  BARG A 199     9470   7790  10915    288   -346    853       O  
ATOM   1514  CB AARG A 199     -60.475  -8.055 -54.237  0.40 66.51           C  
ANISOU 1514  CB AARG A 199     8604   7030   9638     65   -301    852       C  
ATOM   1515  CB BARG A 199     -60.480  -8.063 -54.351  0.60 66.49           C  
ANISOU 1515  CB BARG A 199     8611   7023   9629     68   -325    862       C  
ATOM   1516  CG AARG A 199     -60.790  -8.977 -55.401  0.40 76.89           C  
ANISOU 1516  CG AARG A 199    10027   8355  10834     13   -484    912       C  
ATOM   1517  CG BARG A 199     -61.394  -8.116 -55.569  0.60 79.07           C  
ANISOU 1517  CG BARG A 199    10144   8557  11341    102   -661    871       C  
ATOM   1518  CD AARG A 199     -62.143  -9.641 -55.200  0.40 72.26           C  
ANISOU 1518  CD AARG A 199     9179   7799  10479    -70   -485    710       C  
ATOM   1519  CD BARG A 199     -62.624  -8.978 -55.317  0.60 73.57           C  
ANISOU 1519  CD BARG A 199     9194   7918  10841      6   -623    665       C  
ATOM   1520  NE AARG A 199     -62.413 -10.671 -56.198  0.40 76.49           N  
ANISOU 1520  NE AARG A 199     9835   8356  10871   -162   -622    744       N  
ATOM   1521  NE BARG A 199     -62.368 -10.402 -55.518  0.60 83.50           N  
ANISOU 1521  NE BARG A 199    10644   9251  11832   -149   -494    696       N  
ATOM   1522  CZ AARG A 199     -62.218 -11.971 -55.997  0.40 75.15           C  
ANISOU 1522  CZ AARG A 199     9809   8238  10507   -308   -417    725       C  
ATOM   1523  CZ BARG A 199     -62.672 -11.065 -56.630  0.60 78.58           C  
ANISOU 1523  CZ BARG A 199    10118   8627  11110   -204   -699    737       C  
ATOM   1524  NH1AARG A 199     -61.753 -12.402 -54.833  0.40 73.93           N  
ANISOU 1524  NH1AARG A 199     9715   8112  10264   -368    -99    694       N  
ATOM   1525  NH1BARG A 199     -63.245 -10.434 -57.645  0.60 85.49           N  
ANISOU 1525  NH1BARG A 199    10930   9443  12110   -121  -1078    770       N  
ATOM   1526  NH2AARG A 199     -62.490 -12.839 -56.960  0.40 81.50           N  
ANISOU 1526  NH2AARG A 199    10730   9045  11191   -400   -547    738       N  
ATOM   1527  NH2BARG A 199     -62.405 -12.361 -56.727  0.60 81.10           N  
ANISOU 1527  NH2BARG A 199    10627   8988  11200   -345   -545    745       N  
ATOM   1528  N   GLU A 200     -58.719  -6.418 -52.203  1.00 67.28           N  
ANISOU 1528  N   GLU A 200     8766   7147   9650    103     84    853       N  
ATOM   1529  CA  GLU A 200     -58.657  -5.479 -51.091  1.00 69.40           C  
ANISOU 1529  CA  GLU A 200     8926   7396  10046    104    244    736       C  
ATOM   1530  C   GLU A 200     -57.566  -4.431 -51.271  1.00 66.48           C  
ANISOU 1530  C   GLU A 200     8699   6981   9580    152    201    852       C  
ATOM   1531  O   GLU A 200     -57.650  -3.364 -50.654  1.00 63.80           O  
ANISOU 1531  O   GLU A 200     8272   6567   9403    176    262    757       O  
ATOM   1532  CB  GLU A 200     -58.460  -6.218 -49.762  1.00 77.75           C  
ANISOU 1532  CB  GLU A 200    10012   8568  10962    -33    532    640       C  
ATOM   1533  CG  GLU A 200     -57.145  -6.963 -49.614  1.00 85.33           C  
ANISOU 1533  CG  GLU A 200    11222   9627  11574    -67    585    791       C  
ATOM   1534  CD  GLU A 200     -57.026  -7.670 -48.273  1.00 93.19           C  
ANISOU 1534  CD  GLU A 200    12301  10694  12412   -197    804    720       C  
ATOM   1535  OE1 GLU A 200     -56.497  -7.060 -47.319  1.00 95.29           O  
ANISOU 1535  OE1 GLU A 200    12595  10995  12615   -237    910    676       O  
ATOM   1536  OE2 GLU A 200     -57.475  -8.832 -48.171  1.00 95.78           O  
ANISOU 1536  OE2 GLU A 200    12701  11031  12661   -280    865    708       O  
ATOM   1537  N   GLN A 201     -56.565  -4.691 -52.115  1.00 60.84           N  
ANISOU 1537  N   GLN A 201     8198   6301   8618    145    122   1027       N  
ATOM   1538  CA  GLN A 201     -55.450  -3.764 -52.261  1.00 53.96           C  
ANISOU 1538  CA  GLN A 201     7459   5407   7635    135    132   1108       C  
ATOM   1539  C   GLN A 201     -55.651  -2.709 -53.344  1.00 54.23           C  
ANISOU 1539  C   GLN A 201     7596   5254   7756    186    -90   1205       C  
ATOM   1540  O   GLN A 201     -54.958  -1.685 -53.312  1.00 52.78           O  
ANISOU 1540  O   GLN A 201     7512   4999   7543    156    -61   1237       O  
ATOM   1541  CB  GLN A 201     -54.153  -4.527 -52.545  1.00 52.88           C  
ANISOU 1541  CB  GLN A 201     7478   5410   7203     77    208   1201       C  
ATOM   1542  CG  GLN A 201     -53.575  -5.236 -51.332  1.00 51.43           C  
ANISOU 1542  CG  GLN A 201     7254   5377   6911     44    386   1133       C  
ATOM   1543  CD  GLN A 201     -53.413  -4.316 -50.139  1.00 50.48           C  
ANISOU 1543  CD  GLN A 201     7055   5265   6862      7    500   1030       C  
ATOM   1544  OE1 GLN A 201     -52.639  -3.360 -50.177  1.00 49.79           O  
ANISOU 1544  OE1 GLN A 201     6998   5166   6753    -23    513   1038       O  
ATOM   1545  NE2 GLN A 201     -54.145  -4.601 -49.071  1.00 52.09           N  
ANISOU 1545  NE2 GLN A 201     7175   5483   7133    -28    608    914       N  
ATOM   1546  N   ILE A 202     -56.557  -2.919 -54.298  1.00 52.56           N  
ANISOU 1546  N   ILE A 202     7391   4947   7631    247   -327   1256       N  
ATOM   1547  CA  ILE A 202     -56.767  -1.914 -55.349  1.00 58.83           C  
ANISOU 1547  CA  ILE A 202     8352   5526   8474    298   -600   1379       C  
ATOM   1548  C   ILE A 202     -57.144  -0.540 -54.781  1.00 60.06           C  
ANISOU 1548  C   ILE A 202     8416   5490   8916    395   -638   1303       C  
ATOM   1549  O   ILE A 202     -56.441   0.455 -55.062  1.00 58.63           O  
ANISOU 1549  O   ILE A 202     8454   5174   8648    354   -656   1398       O  
ATOM   1550  CB  ILE A 202     -57.815  -2.393 -56.369  1.00 66.90           C  
ANISOU 1550  CB  ILE A 202     9375   6480   9564    360   -909   1428       C  
ATOM   1551  CG1 ILE A 202     -57.269  -3.572 -57.173  1.00 70.19           C  
ANISOU 1551  CG1 ILE A 202     9985   7037   9649    236   -877   1522       C  
ATOM   1552  CG2 ILE A 202     -58.221  -1.255 -57.293  1.00 69.47           C  
ANISOU 1552  CG2 ILE A 202     9876   6537   9984    448  -1262   1554       C  
ATOM   1553  CD1 ILE A 202     -55.950  -3.271 -57.842  1.00 72.34           C  
ANISOU 1553  CD1 ILE A 202    10583   7309   9596    107   -794   1660       C  
ATOM   1554  N   PRO A 203     -58.221  -0.409 -53.989  1.00 60.73           N  
ANISOU 1554  N   PRO A 203     8187   5538   9348    506   -625   1111       N  
ATOM   1555  CA  PRO A 203     -58.577   0.932 -53.496  1.00 61.53           C  
ANISOU 1555  CA  PRO A 203     8203   5425   9753    615   -652   1011       C  
ATOM   1556  C   PRO A 203     -57.537   1.517 -52.558  1.00 62.40           C  
ANISOU 1556  C   PRO A 203     8388   5582   9740    500   -355    962       C  
ATOM   1557  O   PRO A 203     -57.422   2.746 -52.465  1.00 70.89           O  
ANISOU 1557  O   PRO A 203     9544   6444  10949    543   -389    950       O  
ATOM   1558  CB  PRO A 203     -59.918   0.705 -52.787  1.00 60.35           C  
ANISOU 1558  CB  PRO A 203     7650   5284   9997    722   -621    752       C  
ATOM   1559  CG  PRO A 203     -59.867  -0.714 -52.355  1.00 55.66           C  
ANISOU 1559  CG  PRO A 203     6972   4963   9211    581   -405    698       C  
ATOM   1560  CD  PRO A 203     -59.133  -1.437 -53.443  1.00 57.72           C  
ANISOU 1560  CD  PRO A 203     7520   5301   9110    510   -536    942       C  
ATOM   1561  N   ILE A 204     -56.772   0.674 -51.863  1.00 60.42           N  
ANISOU 1561  N   ILE A 204     8127   5588   9240    356    -90    930       N  
ATOM   1562  CA  ILE A 204     -55.662   1.180 -51.062  1.00 57.94           C  
ANISOU 1562  CA  ILE A 204     7897   5346   8772    232    138    894       C  
ATOM   1563  C   ILE A 204     -54.631   1.841 -51.964  1.00 55.23           C  
ANISOU 1563  C   ILE A 204     7839   4916   8230    157     58   1071       C  
ATOM   1564  O   ILE A 204     -54.090   2.907 -51.643  1.00 58.02           O  
ANISOU 1564  O   ILE A 204     8281   5164   8599     93    137   1039       O  
ATOM   1565  CB  ILE A 204     -55.037   0.046 -50.229  1.00 54.78           C  
ANISOU 1565  CB  ILE A 204     7450   5229   8136    118    354    849       C  
ATOM   1566  CG1 ILE A 204     -56.126  -0.823 -49.599  1.00 56.81           C  
ANISOU 1566  CG1 ILE A 204     7504   5554   8525    142    427    711       C  
ATOM   1567  CG2 ILE A 204     -54.119   0.613 -49.160  1.00 56.23           C  
ANISOU 1567  CG2 ILE A 204     7655   5491   8217      1    557    758       C  
ATOM   1568  CD1 ILE A 204     -57.127  -0.060 -48.773  1.00 57.87           C  
ANISOU 1568  CD1 ILE A 204     7432   5569   8987    180    525    482       C  
ATOM   1569  N   LEU A 205     -54.349   1.217 -53.109  1.00 52.68           N  
ANISOU 1569  N   LEU A 205     7681   4632   7704    129    -74   1239       N  
ATOM   1570  CA  LEU A 205     -53.399   1.786 -54.056  1.00 50.04           C  
ANISOU 1570  CA  LEU A 205     7649   4215   7148      4   -111   1389       C  
ATOM   1571  C   LEU A 205     -53.879   3.138 -54.566  1.00 51.29           C  
ANISOU 1571  C   LEU A 205     7993   4029   7465     60   -312   1461       C  
ATOM   1572  O   LEU A 205     -53.144   4.132 -54.502  1.00 51.38           O  
ANISOU 1572  O   LEU A 205     8181   3926   7415    -60   -220   1474       O  
ATOM   1573  CB  LEU A 205     -53.175   0.820 -55.218  1.00 48.86           C  
ANISOU 1573  CB  LEU A 205     7654   4154   6755    -48   -200   1524       C  
ATOM   1574  CG  LEU A 205     -52.298   1.358 -56.347  1.00 52.86           C  
ANISOU 1574  CG  LEU A 205     8517   4566   7003   -225   -216   1665       C  
ATOM   1575  CD1 LEU A 205     -50.963   1.831 -55.801  1.00 53.21           C  
ANISOU 1575  CD1 LEU A 205     8566   4724   6929   -399     63   1583       C  
ATOM   1576  CD2 LEU A 205     -52.101   0.297 -57.419  1.00 52.83           C  
ANISOU 1576  CD2 LEU A 205     8654   4670   6750   -298   -254   1751       C  
ATOM   1577  N   ILE A 206     -55.119   3.202 -55.067  1.00 53.07           N  
ANISOU 1577  N   ILE A 206     8183   4069   7912    242   -606   1501       N  
ATOM   1578  CA  ILE A 206     -55.586   4.479 -55.603  1.00 61.51           C  
ANISOU 1578  CA  ILE A 206     9460   4762   9148    336   -867   1589       C  
ATOM   1579  C   ILE A 206     -55.637   5.539 -54.507  1.00 62.44           C  
ANISOU 1579  C   ILE A 206     9450   4740   9534    387   -715   1419       C  
ATOM   1580  O   ILE A 206     -55.380   6.724 -54.765  1.00 60.30           O  
ANISOU 1580  O   ILE A 206     9445   4177   9289    362   -786   1489       O  
ATOM   1581  CB  ILE A 206     -56.948   4.319 -56.311  1.00 68.59           C  
ANISOU 1581  CB  ILE A 206    10290   5492  10281    561  -1272   1640       C  
ATOM   1582  CG1 ILE A 206     -58.064   4.026 -55.309  1.00 76.53           C  
ANISOU 1582  CG1 ILE A 206    10809   6565  11703    753  -1230   1386       C  
ATOM   1583  CG2 ILE A 206     -56.873   3.230 -57.371  1.00 62.40           C  
ANISOU 1583  CG2 ILE A 206     9654   4859   9196    473  -1403   1790       C  
ATOM   1584  CD1 ILE A 206     -59.454   4.109 -55.903  1.00 84.43           C  
ANISOU 1584  CD1 ILE A 206    11661   7373  13044    999  -1648   1375       C  
ATOM   1585  N   SER A 207     -55.926   5.133 -53.267  1.00 63.06           N  
ANISOU 1585  N   SER A 207     9166   5009   9783    426   -483   1187       N  
ATOM   1586  CA  SER A 207     -55.947   6.090 -52.165  1.00 64.25           C  
ANISOU 1586  CA  SER A 207     9205   5050  10159    437   -294    990       C  
ATOM   1587  C   SER A 207     -54.554   6.652 -51.899  1.00 65.24           C  
ANISOU 1587  C   SER A 207     9555   5224  10009    196    -67   1018       C  
ATOM   1588  O   SER A 207     -54.368   7.875 -51.829  1.00 67.58           O  
ANISOU 1588  O   SER A 207    10023   5252  10403    171    -63   1002       O  
ATOM   1589  CB  SER A 207     -56.515   5.427 -50.911  1.00 58.31           C  
ANISOU 1589  CB  SER A 207     8071   4516   9569    465    -63    732       C  
ATOM   1590  OG  SER A 207     -56.582   6.344 -49.836  1.00 58.74           O  
ANISOU 1590  OG  SER A 207     8030   4463   9826    453    141    511       O  
ATOM   1591  N   SER A 208     -53.559   5.770 -51.762  1.00 62.50           N  
ANISOU 1591  N   SER A 208     9201   5209   9338     18    114   1045       N  
ATOM   1592  CA  SER A 208     -52.188   6.220 -51.534  1.00 59.56           C  
ANISOU 1592  CA  SER A 208     8977   4929   8726   -221    319   1038       C  
ATOM   1593  C   SER A 208     -51.712   7.135 -52.656  1.00 58.77           C  
ANISOU 1593  C   SER A 208     9258   4565   8506   -334    210   1211       C  
ATOM   1594  O   SER A 208     -51.050   8.152 -52.403  1.00 69.06           O  
ANISOU 1594  O   SER A 208    10715   5744   9781   -494    339   1164       O  
ATOM   1595  CB  SER A 208     -51.259   5.014 -51.390  1.00 57.30           C  
ANISOU 1595  CB  SER A 208     8591   5025   8157   -339    460   1041       C  
ATOM   1596  OG  SER A 208     -51.290   4.204 -52.552  1.00 46.28           O  
ANISOU 1596  OG  SER A 208     7301   3672   6612   -316    320   1207       O  
ATOM   1597  N   ILE A 209     -52.048   6.794 -53.905  1.00 56.54           N  
ANISOU 1597  N   ILE A 209     9171   4182   8128   -285    -23   1411       N  
ATOM   1598  CA  ILE A 209     -51.730   7.678 -55.024  1.00 58.46           C  
ANISOU 1598  CA  ILE A 209     9863   4125   8222   -412   -154   1599       C  
ATOM   1599  C   ILE A 209     -52.371   9.044 -54.819  1.00 62.10           C  
ANISOU 1599  C   ILE A 209    10464   4162   8968   -291   -296   1588       C  
ATOM   1600  O   ILE A 209     -51.751  10.085 -55.076  1.00 60.10           O  
ANISOU 1600  O   ILE A 209    10550   3672   8612   -475   -239   1645       O  
ATOM   1601  CB  ILE A 209     -52.175   7.047 -56.355  1.00 60.38           C  
ANISOU 1601  CB  ILE A 209    10315   4316   8309   -367   -428   1810       C  
ATOM   1602  CG1 ILE A 209     -51.435   5.738 -56.609  1.00 61.20           C  
ANISOU 1602  CG1 ILE A 209    10314   4807   8131   -503   -249   1798       C  
ATOM   1603  CG2 ILE A 209     -51.924   8.005 -57.501  1.00 63.69           C  
ANISOU 1603  CG2 ILE A 209    11281   4383   8535   -521   -587   2023       C  
ATOM   1604  CD1 ILE A 209     -51.957   4.990 -57.807  1.00 65.62           C  
ANISOU 1604  CD1 ILE A 209    11044   5346   8543   -462   -495   1964       C  
ATOM   1605  N   ARG A 210     -53.622   9.063 -54.351  1.00 58.57           N  
ANISOU 1605  N   ARG A 210     9755   3598   8903     11   -469   1493       N  
ATOM   1606  CA  ARG A 210     -54.297  10.332 -54.106  1.00 67.28           C  
ANISOU 1606  CA  ARG A 210    10936   4275  10351    178   -608   1439       C  
ATOM   1607  C   ARG A 210     -53.539  11.174 -53.083  1.00 67.46           C  
ANISOU 1607  C   ARG A 210    10959   4281  10391      2   -275   1256       C  
ATOM   1608  O   ARG A 210     -53.341  12.381 -53.288  1.00 64.94           O  
ANISOU 1608  O   ARG A 210    10967   3589  10116    -56   -315   1304       O  
ATOM   1609  CB  ARG A 210     -55.733  10.076 -53.652  1.00 72.72           C  
ANISOU 1609  CB  ARG A 210    11227   4913  11491    523   -782   1283       C  
ATOM   1610  CG  ARG A 210     -56.659  11.272 -53.753  1.00 80.49           C  
ANISOU 1610  CG  ARG A 210    12283   5400  12900    789  -1059   1254       C  
ATOM   1611  CD  ARG A 210     -58.042  10.821 -54.191  1.00 86.46           C  
ANISOU 1611  CD  ARG A 210    12779   6077  13995   1123  -1438   1244       C  
ATOM   1612  NE  ARG A 210     -58.038  10.353 -55.575  1.00 92.25           N  
ANISOU 1612  NE  ARG A 210    13823   6782  14447   1103  -1794   1554       N  
ATOM   1613  CZ  ARG A 210     -58.950   9.537 -56.095  1.00 96.10           C  
ANISOU 1613  CZ  ARG A 210    14091   7394  15031   1274  -2070   1572       C  
ATOM   1614  NH1 ARG A 210     -59.942   9.080 -55.343  1.00 96.08           N  
ANISOU 1614  NH1 ARG A 210    13552   7497  15456   1484  -2046   1305       N  
ATOM   1615  NH2 ARG A 210     -58.866   9.169 -57.367  1.00 97.61           N  
ANISOU 1615  NH2 ARG A 210    14569   7673  14845   1188  -2304   1808       N  
ATOM   1616  N   VAL A 211     -53.084  10.556 -51.986  1.00 65.17           N  
ANISOU 1616  N   VAL A 211    10344   4376  10041   -104     42   1051       N  
ATOM   1617  CA  VAL A 211     -52.333  11.345 -51.009  1.00 64.64           C  
ANISOU 1617  CA  VAL A 211    10286   4314   9960   -299    336    867       C  
ATOM   1618  C   VAL A 211     -51.019  11.833 -51.609  1.00 59.98           C  
ANISOU 1618  C   VAL A 211    10054   3706   9030   -627    444    990       C  
ATOM   1619  O   VAL A 211     -50.552  12.929 -51.278  1.00 61.99           O  
ANISOU 1619  O   VAL A 211    10493   3752   9307   -787    578    908       O  
ATOM   1620  CB  VAL A 211     -52.100  10.572 -49.690  1.00 63.61           C  
ANISOU 1620  CB  VAL A 211     9780   4597   9792   -363    609    634       C  
ATOM   1621  CG1 VAL A 211     -53.015   9.365 -49.578  1.00 54.89           C  
ANISOU 1621  CG1 VAL A 211     8374   3694   8787   -158    520    616       C  
ATOM   1622  CG2 VAL A 211     -50.632  10.180 -49.514  1.00 62.23           C  
ANISOU 1622  CG2 VAL A 211     9635   4765   9243   -666    815    636       C  
ATOM   1623  N   CYS A 212     -50.407  11.056 -52.510  1.00 63.28           N  
ANISOU 1623  N   CYS A 212    10579   4328   9136   -757    416   1160       N  
ATOM   1624  CA  CYS A 212     -49.194  11.540 -53.168  1.00 61.79           C  
ANISOU 1624  CA  CYS A 212    10728   4113   8637  -1103    554   1244       C  
ATOM   1625  C   CYS A 212     -49.485  12.766 -54.028  1.00 63.83           C  
ANISOU 1625  C   CYS A 212    11493   3839   8921  -1135    373   1419       C  
ATOM   1626  O   CYS A 212     -48.736  13.755 -53.995  1.00 65.96           O  
ANISOU 1626  O   CYS A 212    12037   3932   9094  -1407    542   1386       O  
ATOM   1627  CB  CYS A 212     -48.569  10.427 -54.009  1.00 62.63           C  
ANISOU 1627  CB  CYS A 212    10837   4528   8432  -1225    580   1355       C  
ATOM   1628  SG  CYS A 212     -47.884   9.053 -53.046  1.00 61.90           S  
ANISOU 1628  SG  CYS A 212    10232   5024   8264  -1235    798   1160       S  
ATOM   1629  N   CYS A 213     -50.580  12.726 -54.793  1.00 65.28           N  
ANISOU 1629  N   CYS A 213    11821   3745   9236   -865      8   1604       N  
ATOM   1630  CA  CYS A 213     -50.952  13.867 -55.622  1.00 69.65           C  
ANISOU 1630  CA  CYS A 213    12846   3793   9826   -836   -245   1787       C  
ATOM   1631  C   CYS A 213     -51.253  15.096 -54.778  1.00 74.84           C  
ANISOU 1631  C   CYS A 213    13525   4097  10815   -746   -203   1636       C  
ATOM   1632  O   CYS A 213     -50.978  16.222 -55.206  1.00 84.56           O  
ANISOU 1632  O   CYS A 213    15048   5089  11992   -859   -221   1696       O  
ATOM   1633  CB  CYS A 213     -52.162  13.523 -56.491  1.00 71.03           C  
ANISOU 1633  CB  CYS A 213    12987   3877  10126   -495   -676   1951       C  
ATOM   1634  SG  CYS A 213     -51.893  12.177 -57.659  1.00 79.30           S  
ANISOU 1634  SG  CYS A 213    14071   5296  10763   -611   -746   2118       S  
ATOM   1635  N   LEU A 214     -51.817  14.909 -53.584  1.00 76.32           N  
ANISOU 1635  N   LEU A 214    13275   4384  11339   -535   -111   1388       N  
ATOM   1636  CA  LEU A 214     -52.071  16.069 -52.739  1.00 78.84           C  
ANISOU 1636  CA  LEU A 214    13607   4375  11975   -470    -20   1196       C  
ATOM   1637  C   LEU A 214     -50.799  16.598 -52.086  1.00 82.19           C  
ANISOU 1637  C   LEU A 214    14118   4930  12179   -875    383   1041       C  
ATOM   1638  O   LEU A 214     -50.667  17.813 -51.903  1.00 86.70           O  
ANISOU 1638  O   LEU A 214    14979   5105  12857   -964    441    987       O  
ATOM   1639  CB  LEU A 214     -53.115  15.738 -51.672  1.00 80.36           C  
ANISOU 1639  CB  LEU A 214    13268   4673  12591   -145     -2    929       C  
ATOM   1640  CG  LEU A 214     -54.546  15.503 -52.169  1.00 84.42           C  
ANISOU 1640  CG  LEU A 214    13637   4971  13467    288   -408    996       C  
ATOM   1641  CD1 LEU A 214     -55.551  15.824 -51.070  1.00 85.39           C  
ANISOU 1641  CD1 LEU A 214    13346   4988  14110    565   -332    660       C  
ATOM   1642  CD2 LEU A 214     -54.843  16.315 -53.423  1.00 91.28           C  
ANISOU 1642  CD2 LEU A 214    14985   5364  14332    397   -796   1282       C  
ATOM   1643  N   VAL A 215     -49.848  15.720 -51.741  1.00 83.86           N  
ANISOU 1643  N   VAL A 215    14088   5674  12100  -1120    643    960       N  
ATOM   1644  CA  VAL A 215     -48.633  16.177 -51.064  1.00 89.60           C  
ANISOU 1644  CA  VAL A 215    14826   6571  12646  -1501    994    777       C  
ATOM   1645  C   VAL A 215     -47.533  16.617 -52.021  1.00 94.34           C  
ANISOU 1645  C   VAL A 215    15859   7088  12899  -1896   1094    923       C  
ATOM   1646  O   VAL A 215     -46.491  17.109 -51.561  1.00 91.82           O  
ANISOU 1646  O   VAL A 215    15568   6878  12443  -2251   1382    759       O  
ATOM   1647  CB  VAL A 215     -48.043  15.101 -50.128  1.00 89.93           C  
ANISOU 1647  CB  VAL A 215    14390   7217  12564  -1583   1206    585       C  
ATOM   1648  CG1 VAL A 215     -49.072  14.657 -49.097  1.00 87.59           C  
ANISOU 1648  CG1 VAL A 215    13710   7017  12554  -1274   1174    416       C  
ATOM   1649  CG2 VAL A 215     -47.512  13.922 -50.929  1.00 92.56           C  
ANISOU 1649  CG2 VAL A 215    14651   7902  12614  -1646   1168    741       C  
ATOM   1650  N   ILE A 216     -47.715  16.455 -53.334  1.00 98.76           N  
ANISOU 1650  N   ILE A 216    16737   7491  13296  -1873    872   1203       N  
ATOM   1651  CA  ILE A 216     -46.675  16.908 -54.252  1.00 99.40           C  
ANISOU 1651  CA  ILE A 216    17093   7652  13022  -2223    979   1280       C  
ATOM   1652  C   ILE A 216     -46.636  18.431 -54.358  1.00105.61           C  
ANISOU 1652  C   ILE A 216    18205   8056  13865  -2306    957   1278       C  
ATOM   1653  O   ILE A 216     -45.618  18.994 -54.778  1.00105.83           O  
ANISOU 1653  O   ILE A 216    18449   8146  13616  -2668   1154   1250       O  
ATOM   1654  CB  ILE A 216     -46.860  16.258 -55.638  1.00 95.47           C  
ANISOU 1654  CB  ILE A 216    16755   7231  12288  -2166    760   1528       C  
ATOM   1655  CG1 ILE A 216     -45.604  16.452 -56.491  1.00 99.06           C  
ANISOU 1655  CG1 ILE A 216    17436   7868  12332  -2590    988   1525       C  
ATOM   1656  CG2 ILE A 216     -48.076  16.830 -56.345  1.00 94.56           C  
ANISOU 1656  CG2 ILE A 216    16870   6713  12346  -1830    342   1739       C  
ATOM   1657  CD1 ILE A 216     -44.335  15.952 -55.833  1.00 97.80           C  
ANISOU 1657  CD1 ILE A 216    16986   8128  12046  -2923   1393   1277       C  
ATOM   1658  N   VAL A 217     -47.706  19.120 -53.961  1.00110.82           N  
ANISOU 1658  N   VAL A 217    18892   8318  14895  -1981    742   1280       N  
ATOM   1659  CA  VAL A 217     -47.788  20.570 -54.099  1.00117.27           C  
ANISOU 1659  CA  VAL A 217    20030   8717  15809  -2009    684   1297       C  
ATOM   1660  C   VAL A 217     -47.347  21.243 -52.804  1.00122.37           C  
ANISOU 1660  C   VAL A 217    20557   9337  16602  -2174    984    996       C  
ATOM   1661  O   VAL A 217     -47.580  22.441 -52.601  1.00126.78           O  
ANISOU 1661  O   VAL A 217    21312   9515  17344  -2138    948    949       O  
ATOM   1662  CB  VAL A 217     -49.215  21.005 -54.488  1.00117.66           C  
ANISOU 1662  CB  VAL A 217    20157   8326  16221  -1541    263   1453       C  
ATOM   1663  CG1 VAL A 217     -49.191  22.328 -55.248  1.00125.85           C  
ANISOU 1663  CG1 VAL A 217    21652   8959  17207  -1602    132   1599       C  
ATOM   1664  CG2 VAL A 217     -49.895  19.922 -55.309  1.00113.24           C  
ANISOU 1664  CG2 VAL A 217    19497   7918  15610  -1294    -22   1654       C  
ATOM   1665  N   LYS A 218     -46.696  20.484 -51.920  1.00122.64           N  
ANISOU 1665  N   LYS A 218    20266   9781  16550  -2362   1280    780       N  
ATOM   1666  CA  LYS A 218     -46.310  21.032 -50.624  1.00125.81           C  
ANISOU 1666  CA  LYS A 218    20515  10216  17070  -2526   1563    464       C  
ATOM   1667  C   LYS A 218     -45.171  22.038 -50.724  1.00131.50           C  
ANISOU 1667  C   LYS A 218    21469  10942  17555  -2946   1785    379       C  
ATOM   1668  O   LYS A 218     -44.969  22.812 -49.782  1.00133.22           O  
ANISOU 1668  O   LYS A 218    21654  11079  17886  -3065   1964    139       O  
ATOM   1669  CB  LYS A 218     -45.930  19.905 -49.664  1.00120.73           C  
ANISOU 1669  CB  LYS A 218    19449  10035  16388  -2619   1792    258       C  
ATOM   1670  CG  LYS A 218     -47.117  19.078 -49.212  1.00118.24           C  
ANISOU 1670  CG  LYS A 218    18814   9763  16349  -2183   1625    246       C  
ATOM   1671  CD  LYS A 218     -48.226  19.971 -48.682  1.00122.07           C  
ANISOU 1671  CD  LYS A 218    19362   9769  17250  -1893   1540    131       C  
ATOM   1672  CE  LYS A 218     -49.593  19.361 -48.942  1.00121.80           C  
ANISOU 1672  CE  LYS A 218    19125   9648  17506  -1400   1234    234       C  
ATOM   1673  NZ  LYS A 218     -49.710  17.990 -48.376  1.00115.97           N  
ANISOU 1673  NZ  LYS A 218    17878   9482  16702  -1301   1283    148       N  
ATOM   1674  N   ASP A 219     -44.431  22.041 -51.830  1.00133.84           N  
ANISOU 1674  N   ASP A 219    21996  11339  17518  -3185   1800    541       N  
ATOM   1675  CA  ASP A 219     -43.343  22.993 -52.052  1.00136.44           C  
ANISOU 1675  CA  ASP A 219    22572  11667  17603  -3602   2029    453       C  
ATOM   1676  C   ASP A 219     -42.296  22.914 -50.941  1.00136.47           C  
ANISOU 1676  C   ASP A 219    22250  12062  17542  -3934   2380    110       C  
ATOM   1677  O   ASP A 219     -42.155  21.887 -50.276  1.00133.88           O  
ANISOU 1677  O   ASP A 219    21514  12107  17246  -3910   2454    -19       O  
ATOM   1678  CB  ASP A 219     -43.895  24.420 -52.163  1.00140.02           C  
ANISOU 1678  CB  ASP A 219    23414  11562  18226  -3505   1896    520       C  
ATOM   1679  CG  ASP A 219     -42.905  25.389 -52.785  1.00146.01           C  
ANISOU 1679  CG  ASP A 219    24557  12244  18677  -3917   2077    520       C  
ATOM   1680  OD1 ASP A 219     -41.698  25.070 -52.842  1.00147.26           O  
ANISOU 1680  OD1 ASP A 219    24603  12811  18537  -4310   2371    371       O  
ATOM   1681  OD2 ASP A 219     -43.337  26.479 -53.215  1.00150.11           O  
ANISOU 1681  OD2 ASP A 219    25483  12283  19268  -3845   1926    653       O  
ATOM   1682  N   SER A 222     -42.436  17.908 -48.431  1.00 90.55           N  
ANISOU 1682  N   SER A 222    14697   7814  11894  -3501   2418   -229       N  
ATOM   1683  CA  SER A 222     -42.954  17.706 -47.082  1.00 85.92           C  
ANISOU 1683  CA  SER A 222    13792   7379  11474  -3295   2393   -420       C  
ATOM   1684  C   SER A 222     -43.670  16.365 -46.961  1.00 84.22           C  
ANISOU 1684  C   SER A 222    13254   7440  11306  -2907   2199   -317       C  
ATOM   1685  O   SER A 222     -44.847  16.246 -47.302  1.00 89.21           O  
ANISOU 1685  O   SER A 222    13970   7808  12119  -2570   2023   -163       O  
ATOM   1686  CB  SER A 222     -43.900  18.845 -46.697  1.00 85.08           C  
ANISOU 1686  CB  SER A 222    13953   6744  11628  -3169   2387   -472       C  
ATOM   1687  OG  SER A 222     -44.414  18.663 -45.390  1.00 79.13           O  
ANISOU 1687  OG  SER A 222    12910   6138  11018  -3014   2417   -694       O  
ATOM   1688  N   GLY A 223     -42.956  15.356 -46.468  1.00 81.14           N  
ANISOU 1688  N   GLY A 223    12495   7569  10767  -2956   2216   -413       N  
ATOM   1689  CA  GLY A 223     -43.539  14.037 -46.333  1.00 76.57           C  
ANISOU 1689  CA  GLY A 223    11646   7246  10201  -2629   2050   -318       C  
ATOM   1690  C   GLY A 223     -43.758  13.307 -47.636  1.00 72.07           C  
ANISOU 1690  C   GLY A 223    11152   6653   9576  -2479   1917    -57       C  
ATOM   1691  O   GLY A 223     -44.611  12.420 -47.702  1.00 70.29           O  
ANISOU 1691  O   GLY A 223    10805   6479   9422  -2170   1759     58       O  
ATOM   1692  N   MET A 224     -43.012  13.662 -48.685  1.00 72.52           N  
ANISOU 1692  N   MET A 224    11430   6632   9492  -2727   1998     25       N  
ATOM   1693  CA  MET A 224     -43.170  12.989 -49.970  1.00 72.46           C  
ANISOU 1693  CA  MET A 224    11546   6602   9384  -2637   1894    259       C  
ATOM   1694  C   MET A 224     -42.557  11.595 -49.941  1.00 69.47           C  
ANISOU 1694  C   MET A 224    10796   6709   8891  -2581   1888    220       C  
ATOM   1695  O   MET A 224     -43.088  10.664 -50.559  1.00 68.96           O  
ANISOU 1695  O   MET A 224    10707   6687   8809  -2355   1746    384       O  
ATOM   1696  CB  MET A 224     -42.537  13.829 -51.078  1.00 80.08           C  
ANISOU 1696  CB  MET A 224    12920   7320  10189  -2979   2025    338       C  
ATOM   1697  CG  MET A 224     -43.104  15.234 -51.191  1.00 91.41           C  
ANISOU 1697  CG  MET A 224    14797   8205  11730  -3032   2002    403       C  
ATOM   1698  SD  MET A 224     -41.915  16.415 -51.856  1.00102.97           S  
ANISOU 1698  SD  MET A 224    16670   9483  12971  -3591   2277    348       S  
ATOM   1699  CE  MET A 224     -41.452  15.608 -53.387  1.00102.93           C  
ANISOU 1699  CE  MET A 224    16767   9671  12671  -3670   2264    521       C  
ATOM   1700  N   LYS A 225     -41.441  11.434 -49.225  1.00 71.04           N  
ANISOU 1700  N   LYS A 225    10702   7264   9026  -2776   2019     -7       N  
ATOM   1701  CA  LYS A 225     -40.765  10.142 -49.178  1.00 72.93           C  
ANISOU 1701  CA  LYS A 225    10580   7938   9192  -2702   1987    -63       C  
ATOM   1702  C   LYS A 225     -41.648   9.071 -48.549  1.00 69.17           C  
ANISOU 1702  C   LYS A 225     9918   7575   8787  -2324   1782     16       C  
ATOM   1703  O   LYS A 225     -41.684   7.931 -49.026  1.00 66.98           O  
ANISOU 1703  O   LYS A 225     9523   7458   8470  -2152   1696    109       O  
ATOM   1704  CB  LYS A 225     -39.448  10.266 -48.413  1.00 77.24           C  
ANISOU 1704  CB  LYS A 225    10823   8823   9702  -2955   2104   -343       C  
ATOM   1705  CG  LYS A 225     -38.226  10.456 -49.298  1.00 82.95           C  
ANISOU 1705  CG  LYS A 225    11516   9670  10332  -3297   2320   -459       C  
ATOM   1706  CD  LYS A 225     -37.033  10.937 -48.489  1.00 90.53           C  
ANISOU 1706  CD  LYS A 225    12199  10895  11303  -3597   2437   -771       C  
ATOM   1707  CE  LYS A 225     -36.830  10.096 -47.236  1.00 93.80           C  
ANISOU 1707  CE  LYS A 225    12206  11664  11768  -3374   2220   -889       C  
ATOM   1708  NZ  LYS A 225     -35.787  10.681 -46.346  1.00 97.90           N  
ANISOU 1708  NZ  LYS A 225    12485  12417  12295  -3663   2272  -1192       N  
ATOM   1709  N   ASP A 226     -42.374   9.418 -47.484  1.00 67.48           N  
ANISOU 1709  N   ASP A 226     9698   7267   8674  -2217   1730    -38       N  
ATOM   1710  CA  ASP A 226     -43.181   8.422 -46.786  1.00 66.52           C  
ANISOU 1710  CA  ASP A 226     9420   7261   8594  -1925   1584      4       C  
ATOM   1711  C   ASP A 226     -44.472   8.112 -47.534  1.00 64.01           C  
ANISOU 1711  C   ASP A 226     9250   6690   8380  -1670   1472    210       C  
ATOM   1712  O   ASP A 226     -44.938   6.967 -47.518  1.00 61.66           O  
ANISOU 1712  O   ASP A 226     8829   6524   8073  -1459   1361    290       O  
ATOM   1713  CB  ASP A 226     -43.482   8.894 -45.364  1.00 71.11           C  
ANISOU 1713  CB  ASP A 226     9955   7846   9218  -1955   1615   -166       C  
ATOM   1714  CG  ASP A 226     -42.234   9.012 -44.517  1.00 78.10           C  
ANISOU 1714  CG  ASP A 226    10664   9033   9977  -2188   1656   -373       C  
ATOM   1715  OD1 ASP A 226     -41.400   8.084 -44.554  1.00 82.16           O  
ANISOU 1715  OD1 ASP A 226    10958   9864  10394  -2166   1568   -384       O  
ATOM   1716  OD2 ASP A 226     -42.078  10.038 -43.824  1.00 81.63           O  
ANISOU 1716  OD2 ASP A 226    11185   9394  10437  -2389   1763   -539       O  
ATOM   1717  N   ALA A 227     -45.068   9.113 -48.187  1.00 61.87           N  
ANISOU 1717  N   ALA A 227     9252   6042   8215  -1687   1475    293       N  
ATOM   1718  CA  ALA A 227     -46.235   8.850 -49.024  1.00 60.08           C  
ANISOU 1718  CA  ALA A 227     9157   5575   8096  -1446   1311    489       C  
ATOM   1719  C   ALA A 227     -45.859   7.959 -50.200  1.00 50.49           C  
ANISOU 1719  C   ALA A 227     7980   4486   6718  -1443   1251    646       C  
ATOM   1720  O   ALA A 227     -46.563   6.988 -50.518  1.00 48.88           O  
ANISOU 1720  O   ALA A 227     7706   4331   6537  -1227   1115    754       O  
ATOM   1721  CB  ALA A 227     -46.840  10.167 -49.512  1.00 61.54           C  
ANISOU 1721  CB  ALA A 227     9656   5299   8427  -1456   1271    552       C  
ATOM   1722  N   ALA A 228     -44.737   8.276 -50.854  1.00 51.84           N  
ANISOU 1722  N   ALA A 228     8262   4712   6722  -1712   1382    633       N  
ATOM   1723  CA  ALA A 228     -44.228   7.417 -51.916  1.00 59.02           C  
ANISOU 1723  CA  ALA A 228     9188   5773   7463  -1757   1393    721       C  
ATOM   1724  C   ALA A 228     -43.930   6.020 -51.390  1.00 57.04           C  
ANISOU 1724  C   ALA A 228     8582   5896   7195  -1601   1366    649       C  
ATOM   1725  O   ALA A 228     -44.155   5.025 -52.089  1.00 61.37           O  
ANISOU 1725  O   ALA A 228     9122   6511   7686  -1476   1293    751       O  
ATOM   1726  CB  ALA A 228     -42.978   8.039 -52.538  1.00 53.78           C  
ANISOU 1726  CB  ALA A 228     8657   5140   6638  -2128   1613    643       C  
ATOM   1727  N   PHE A 229     -43.432   5.925 -50.154  1.00 56.25           N  
ANISOU 1727  N   PHE A 229     8220   6021   7132  -1609   1405    476       N  
ATOM   1728  CA  PHE A 229     -43.190   4.617 -49.557  1.00 52.21           C  
ANISOU 1728  CA  PHE A 229     7425   5813   6599  -1440   1328    429       C  
ATOM   1729  C   PHE A 229     -44.487   3.837 -49.404  1.00 47.94           C  
ANISOU 1729  C   PHE A 229     6906   5186   6125  -1165   1176    561       C  
ATOM   1730  O   PHE A 229     -44.532   2.639 -49.694  1.00 48.13           O  
ANISOU 1730  O   PHE A 229     6845   5338   6104  -1020   1105    622       O  
ATOM   1731  CB  PHE A 229     -42.493   4.762 -48.203  1.00 57.61           C  
ANISOU 1731  CB  PHE A 229     7891   6716   7281  -1512   1342    237       C  
ATOM   1732  CG  PHE A 229     -42.261   3.450 -47.498  1.00 61.50           C  
ANISOU 1732  CG  PHE A 229     8156   7477   7736  -1327   1207    213       C  
ATOM   1733  CD1 PHE A 229     -43.199   2.945 -46.611  1.00 59.81           C  
ANISOU 1733  CD1 PHE A 229     7963   7234   7529  -1156   1100    264       C  
ATOM   1734  CD2 PHE A 229     -41.107   2.719 -47.730  1.00 65.38           C  
ANISOU 1734  CD2 PHE A 229     8424   8226   8192  -1331   1192    126       C  
ATOM   1735  CE1 PHE A 229     -42.990   1.741 -45.967  1.00 63.45           C  
ANISOU 1735  CE1 PHE A 229     8296   7894   7918  -1006    963    267       C  
ATOM   1736  CE2 PHE A 229     -40.892   1.513 -47.088  1.00 67.78           C  
ANISOU 1736  CE2 PHE A 229     8556   8725   8473  -1130   1023    120       C  
ATOM   1737  CZ  PHE A 229     -41.836   1.024 -46.206  1.00 67.15           C  
ANISOU 1737  CZ  PHE A 229     8569   8588   8357   -974    899    211       C  
ATOM   1738  N   GLY A 230     -45.549   4.494 -48.934  1.00 48.01           N  
ANISOU 1738  N   GLY A 230     7011   4972   6259  -1099   1142    577       N  
ATOM   1739  CA  GLY A 230     -46.827   3.809 -48.813  1.00 50.20           C  
ANISOU 1739  CA  GLY A 230     7272   5170   6631   -871   1028    659       C  
ATOM   1740  C   GLY A 230     -47.335   3.305 -50.150  1.00 53.23           C  
ANISOU 1740  C   GLY A 230     7777   5442   7005   -772    922    834       C  
ATOM   1741  O   GLY A 230     -47.665   2.120 -50.305  1.00 57.21           O  
ANISOU 1741  O   GLY A 230     8206   6057   7476   -638    850    891       O  
ATOM   1742  N   ARG A 231     -47.384   4.198 -51.143  1.00 55.40           N  
ANISOU 1742  N   ARG A 231     8285   5482   7283   -861    902    923       N  
ATOM   1743  CA  ARG A 231     -47.833   3.810 -52.476  1.00 51.85           C  
ANISOU 1743  CA  ARG A 231     8015   4911   6774   -807    774   1097       C  
ATOM   1744  C   ARG A 231     -47.029   2.628 -53.010  1.00 48.14           C  
ANISOU 1744  C   ARG A 231     7473   4697   6120   -844    834   1103       C  
ATOM   1745  O   ARG A 231     -47.598   1.607 -53.410  1.00 43.08           O  
ANISOU 1745  O   ARG A 231     6808   4096   5465   -704    732   1178       O  
ATOM   1746  CB  ARG A 231     -47.729   5.003 -53.425  1.00 53.71           C  
ANISOU 1746  CB  ARG A 231     8589   4856   6963   -962    752   1197       C  
ATOM   1747  CG  ARG A 231     -48.056   4.678 -54.869  1.00 54.57           C  
ANISOU 1747  CG  ARG A 231     8964   4838   6934   -967    608   1384       C  
ATOM   1748  CD  ARG A 231     -47.523   5.766 -55.778  1.00 55.30           C  
ANISOU 1748  CD  ARG A 231     9452   4692   6867  -1222    652   1473       C  
ATOM   1749  NE  ARG A 231     -46.079   5.919 -55.623  1.00 54.29           N  
ANISOU 1749  NE  ARG A 231     9268   4773   6585  -1507    951   1326       N  
ATOM   1750  CZ  ARG A 231     -45.393   6.989 -56.007  1.00 59.29           C  
ANISOU 1750  CZ  ARG A 231    10179   5247   7101  -1801   1092   1320       C  
ATOM   1751  NH1 ARG A 231     -46.019   8.017 -56.568  1.00 62.25           N  
ANISOU 1751  NH1 ARG A 231    10963   5213   7476  -1830    937   1486       N  
ATOM   1752  NH2 ARG A 231     -44.080   7.034 -55.823  1.00 62.27           N  
ANISOU 1752  NH2 ARG A 231    10426   5861   7373  -2068   1377   1139       N  
ATOM   1753  N   ASP A 232     -45.698   2.745 -53.004  1.00 50.97           N  
ANISOU 1753  N   ASP A 232     7774   5230   6362  -1036   1008    996       N  
ATOM   1754  CA  ASP A 232     -44.858   1.681 -53.549  1.00 53.21           C  
ANISOU 1754  CA  ASP A 232     7957   5741   6520  -1062   1088    955       C  
ATOM   1755  C   ASP A 232     -44.969   0.399 -52.732  1.00 55.61           C  
ANISOU 1755  C   ASP A 232     8004   6249   6876   -843   1016    910       C  
ATOM   1756  O   ASP A 232     -44.754  -0.695 -53.266  1.00 58.79           O  
ANISOU 1756  O   ASP A 232     8363   6757   7218   -770   1015    919       O  
ATOM   1757  CB  ASP A 232     -43.403   2.143 -53.621  1.00 56.39           C  
ANISOU 1757  CB  ASP A 232     8279   6299   6847  -1315   1302    791       C  
ATOM   1758  CG  ASP A 232     -43.226   3.369 -54.499  1.00 56.82           C  
ANISOU 1758  CG  ASP A 232     8660   6128   6801  -1593   1409    840       C  
ATOM   1759  OD1 ASP A 232     -44.137   3.659 -55.302  1.00 59.60           O  
ANISOU 1759  OD1 ASP A 232     9329   6211   7105  -1567   1284   1029       O  
ATOM   1760  OD2 ASP A 232     -42.177   4.040 -54.388  1.00 54.99           O  
ANISOU 1760  OD2 ASP A 232     8381   5978   6533  -1847   1603    688       O  
ATOM   1761  N   TYR A 233     -45.294   0.514 -51.444  1.00 52.93           N  
ANISOU 1761  N   TYR A 233     7533   5946   6632   -754    966    856       N  
ATOM   1762  CA  TYR A 233     -45.567  -0.671 -50.643  1.00 49.02           C  
ANISOU 1762  CA  TYR A 233     6891   5585   6148   -570    881    847       C  
ATOM   1763  C   TYR A 233     -46.800  -1.395 -51.161  1.00 48.95           C  
ANISOU 1763  C   TYR A 233     6983   5447   6169   -426    780    976       C  
ATOM   1764  O   TYR A 233     -46.798  -2.627 -51.293  1.00 49.42           O  
ANISOU 1764  O   TYR A 233     7002   5594   6182   -316    740   1002       O  
ATOM   1765  CB  TYR A 233     -45.743  -0.284 -49.173  1.00 48.18           C  
ANISOU 1765  CB  TYR A 233     6700   5518   6088   -567    870    761       C  
ATOM   1766  CG  TYR A 233     -46.367  -1.366 -48.317  1.00 49.16           C  
ANISOU 1766  CG  TYR A 233     6784   5699   6195   -418    788    782       C  
ATOM   1767  CD1 TYR A 233     -45.593  -2.383 -47.775  1.00 50.19           C  
ANISOU 1767  CD1 TYR A 233     6818   6018   6234   -345    721    752       C  
ATOM   1768  CD2 TYR A 233     -47.730  -1.364 -48.046  1.00 47.40           C  
ANISOU 1768  CD2 TYR A 233     6627   5326   6058   -359    775    819       C  
ATOM   1769  CE1 TYR A 233     -46.159  -3.372 -46.993  1.00 50.56           C  
ANISOU 1769  CE1 TYR A 233     6910   6077   6226   -240    645    792       C  
ATOM   1770  CE2 TYR A 233     -48.305  -2.346 -47.265  1.00 44.39           C  
ANISOU 1770  CE2 TYR A 233     6244   4987   5635   -283    746    823       C  
ATOM   1771  CZ  TYR A 233     -47.515  -3.350 -46.741  1.00 49.25           C  
ANISOU 1771  CZ  TYR A 233     6838   5766   6110   -236    682    826       C  
ATOM   1772  OH  TYR A 233     -48.083  -4.335 -45.962  1.00 45.56           O  
ANISOU 1772  OH  TYR A 233     6446   5302   5561   -190    652    851       O  
ATOM   1773  N   VAL A 234     -47.865  -0.648 -51.466  1.00 45.60           N  
ANISOU 1773  N   VAL A 234     6681   4802   5842   -420    722   1046       N  
ATOM   1774  CA  VAL A 234     -49.060  -1.296 -52.001  1.00 45.88           C  
ANISOU 1774  CA  VAL A 234     6771   4728   5931   -295    599   1142       C  
ATOM   1775  C   VAL A 234     -48.783  -1.869 -53.388  1.00 48.33           C  
ANISOU 1775  C   VAL A 234     7219   5036   6107   -325    567   1234       C  
ATOM   1776  O   VAL A 234     -49.255  -2.963 -53.732  1.00 48.83           O  
ANISOU 1776  O   VAL A 234     7282   5128   6143   -237    506   1274       O  
ATOM   1777  CB  VAL A 234     -50.244  -0.314 -52.011  1.00 46.92           C  
ANISOU 1777  CB  VAL A 234     6955   4620   6252   -253    504   1165       C  
ATOM   1778  CG1 VAL A 234     -51.498  -1.000 -52.530  1.00 40.01           C  
ANISOU 1778  CG1 VAL A 234     6075   3659   5468   -126    352   1229       C  
ATOM   1779  CG2 VAL A 234     -50.478   0.244 -50.610  1.00 45.46           C  
ANISOU 1779  CG2 VAL A 234     6637   4441   6195   -251    594   1027       C  
ATOM   1780  N   ILE A 235     -48.002  -1.152 -54.200  1.00 51.70           N  
ANISOU 1780  N   ILE A 235     7790   5423   6429   -485    635   1251       N  
ATOM   1781  CA  ILE A 235     -47.639  -1.659 -55.521  1.00 49.26           C  
ANISOU 1781  CA  ILE A 235     7647   5120   5949   -571    657   1307       C  
ATOM   1782  C   ILE A 235     -46.873  -2.968 -55.395  1.00 47.84           C  
ANISOU 1782  C   ILE A 235     7301   5164   5713   -513    759   1211       C  
ATOM   1783  O   ILE A 235     -47.074  -3.900 -56.183  1.00 46.85           O  
ANISOU 1783  O   ILE A 235     7255   5042   5504   -483    737   1245       O  
ATOM   1784  CB  ILE A 235     -46.829  -0.607 -56.299  1.00 50.01           C  
ANISOU 1784  CB  ILE A 235     7951   5137   5912   -816    773   1312       C  
ATOM   1785  CG1 ILE A 235     -47.632   0.684 -56.446  1.00 51.37           C  
ANISOU 1785  CG1 ILE A 235     8342   5023   6152   -843    628   1428       C  
ATOM   1786  CG2 ILE A 235     -46.434  -1.142 -57.669  1.00 51.81           C  
ANISOU 1786  CG2 ILE A 235     8386   5377   5923   -956    843   1342       C  
ATOM   1787  CD1 ILE A 235     -46.867   1.809 -57.109  1.00 50.93           C  
ANISOU 1787  CD1 ILE A 235     8561   4841   5949  -1116    747   1447       C  
ATOM   1788  N   GLN A 236     -45.980  -3.062 -54.406  1.00 48.37           N  
ANISOU 1788  N   GLN A 236     7142   5405   5830   -491    850   1083       N  
ATOM   1789  CA  GLN A 236     -45.200  -4.283 -54.241  1.00 51.22           C  
ANISOU 1789  CA  GLN A 236     7335   5948   6177   -392    899    986       C  
ATOM   1790  C   GLN A 236     -46.060  -5.422 -53.708  1.00 47.22           C  
ANISOU 1790  C   GLN A 236     6809   5421   5711   -193    770   1048       C  
ATOM   1791  O   GLN A 236     -45.874  -6.577 -54.101  1.00 43.46           O  
ANISOU 1791  O   GLN A 236     6329   4982   5201   -105    777   1031       O  
ATOM   1792  CB  GLN A 236     -44.002  -4.035 -53.324  1.00 60.57           C  
ANISOU 1792  CB  GLN A 236     8279   7319   7417   -410    966    830       C  
ATOM   1793  CG  GLN A 236     -42.665  -3.976 -54.053  1.00 71.20           C  
ANISOU 1793  CG  GLN A 236     9521   8799   8734   -550   1149    669       C  
ATOM   1794  CD  GLN A 236     -42.307  -5.286 -54.740  1.00 74.40           C  
ANISOU 1794  CD  GLN A 236     9875   9264   9130   -441   1195    607       C  
ATOM   1795  OE1 GLN A 236     -42.814  -6.348 -54.382  1.00 77.85           O  
ANISOU 1795  OE1 GLN A 236    10307   9676   9597   -228   1063    670       O  
ATOM   1796  NE2 GLN A 236     -41.428  -5.212 -55.735  1.00 72.46           N  
ANISOU 1796  NE2 GLN A 236     9610   9085   8838   -611   1411    465       N  
ATOM   1797  N   LYS A 237     -47.002  -5.122 -52.809  1.00 47.21           N  
ANISOU 1797  N   LYS A 237     6805   5349   5785   -140    680   1099       N  
ATOM   1798  CA  LYS A 237     -47.908  -6.163 -52.335  1.00 50.00           C  
ANISOU 1798  CA  LYS A 237     7172   5668   6160    -13    598   1145       C  
ATOM   1799  C   LYS A 237     -48.730  -6.733 -53.488  1.00 53.07           C  
ANISOU 1799  C   LYS A 237     7697   5948   6520     -7    548   1223       C  
ATOM   1800  O   LYS A 237     -48.869  -7.958 -53.624  1.00 53.46           O  
ANISOU 1800  O   LYS A 237     7775   6006   6530     69    534   1229       O  
ATOM   1801  CB  LYS A 237     -48.815  -5.614 -51.231  1.00 51.16           C  
ANISOU 1801  CB  LYS A 237     7287   5758   6396    -13    569   1140       C  
ATOM   1802  CG  LYS A 237     -49.802  -6.641 -50.698  1.00 58.39           C  
ANISOU 1802  CG  LYS A 237     8229   6635   7322     55    535   1160       C  
ATOM   1803  CD  LYS A 237     -50.573  -6.136 -49.485  1.00 65.36           C  
ANISOU 1803  CD  LYS A 237     9068   7486   8279     13    573   1100       C  
ATOM   1804  CE  LYS A 237     -49.708  -6.099 -48.235  1.00 70.22           C  
ANISOU 1804  CE  LYS A 237     9665   8221   8796    -10    602   1044       C  
ATOM   1805  NZ  LYS A 237     -50.496  -5.730 -47.020  1.00 70.98           N  
ANISOU 1805  NZ  LYS A 237     9768   8286   8916    -92    679    965       N  
ATOM   1806  N   LEU A 238     -49.270  -5.856 -54.341  1.00 48.65           N  
ANISOU 1806  N   LEU A 238     7249   5267   5970    -92    497   1286       N  
ATOM   1807  CA  LEU A 238     -49.996  -6.328 -55.518  1.00 47.84           C  
ANISOU 1807  CA  LEU A 238     7299   5069   5811   -108    404   1361       C  
ATOM   1808  C   LEU A 238     -49.088  -7.132 -56.442  1.00 50.43           C  
ANISOU 1808  C   LEU A 238     7714   5469   5978   -157    506   1327       C  
ATOM   1809  O   LEU A 238     -49.476  -8.200 -56.935  1.00 56.23           O  
ANISOU 1809  O   LEU A 238     8516   6188   6662   -123    478   1334       O  
ATOM   1810  CB  LEU A 238     -50.607  -5.144 -56.265  1.00 48.32           C  
ANISOU 1810  CB  LEU A 238     7504   4964   5891   -184    277   1449       C  
ATOM   1811  CG  LEU A 238     -51.904  -4.565 -55.701  1.00 48.89           C  
ANISOU 1811  CG  LEU A 238     7487   4912   6179    -96    127   1463       C  
ATOM   1812  CD1 LEU A 238     -52.206  -3.214 -56.331  1.00 50.89           C  
ANISOU 1812  CD1 LEU A 238     7892   4971   6475   -140    -14   1546       C  
ATOM   1813  CD2 LEU A 238     -53.055  -5.530 -55.934  1.00 47.36           C  
ANISOU 1813  CD2 LEU A 238     7254   4694   6047    -29      3   1469       C  
ATOM   1814  N   PHE A 239     -47.871  -6.635 -56.679  1.00 50.77           N  
ANISOU 1814  N   PHE A 239     7744   5592   5954   -254    651   1259       N  
ATOM   1815  CA  PHE A 239     -46.921  -7.327 -57.548  1.00 54.02           C  
ANISOU 1815  CA  PHE A 239     8197   6083   6247   -319    805   1167       C  
ATOM   1816  C   PHE A 239     -46.647  -8.740 -57.049  1.00 57.72           C  
ANISOU 1816  C   PHE A 239     8527   6628   6775   -140    826   1087       C  
ATOM   1817  O   PHE A 239     -46.658  -9.702 -57.827  1.00 60.84           O  
ANISOU 1817  O   PHE A 239     9018   7000   7097   -134    870   1054       O  
ATOM   1818  CB  PHE A 239     -45.623  -6.520 -57.628  1.00 57.95           C  
ANISOU 1818  CB  PHE A 239     8619   6681   6718   -463    990   1051       C  
ATOM   1819  CG  PHE A 239     -44.596  -7.099 -58.559  1.00 64.68           C  
ANISOU 1819  CG  PHE A 239     9478   7623   7474   -566   1206    898       C  
ATOM   1820  CD1 PHE A 239     -44.539  -6.694 -59.881  1.00 69.65           C  
ANISOU 1820  CD1 PHE A 239    10389   8178   7896   -816   1316    913       C  
ATOM   1821  CD2 PHE A 239     -43.676  -8.035 -58.111  1.00 67.45           C  
ANISOU 1821  CD2 PHE A 239     9567   8118   7942   -417   1298    725       C  
ATOM   1822  CE1 PHE A 239     -43.593  -7.218 -60.742  1.00 74.76           C  
ANISOU 1822  CE1 PHE A 239    11045   8913   8449   -949   1573    729       C  
ATOM   1823  CE2 PHE A 239     -42.729  -8.565 -58.967  1.00 72.16           C  
ANISOU 1823  CE2 PHE A 239    10123   8792   8501   -500   1526    532       C  
ATOM   1824  CZ  PHE A 239     -42.688  -8.157 -60.284  1.00 75.69           C  
ANISOU 1824  CZ  PHE A 239    10840   9184   8736   -783   1695    519       C  
ATOM   1825  N   ILE A 240     -46.402  -8.881 -55.744  1.00 53.37           N  
ANISOU 1825  N   ILE A 240     7789   6149   6342      0    783   1059       N  
ATOM   1826  CA  ILE A 240     -46.077 -10.180 -55.167  1.00 47.79           C  
ANISOU 1826  CA  ILE A 240     6999   5475   5684    184    760   1006       C  
ATOM   1827  C   ILE A 240     -47.278 -11.115 -55.237  1.00 47.43           C  
ANISOU 1827  C   ILE A 240     7107   5301   5612    236    670   1099       C  
ATOM   1828  O   ILE A 240     -47.146 -12.287 -55.615  1.00 48.90           O  
ANISOU 1828  O   ILE A 240     7355   5447   5778    313    696   1059       O  
ATOM   1829  CB  ILE A 240     -45.570  -9.999 -53.724  1.00 44.69           C  
ANISOU 1829  CB  ILE A 240     6434   5171   5374    290    688    978       C  
ATOM   1830  CG1 ILE A 240     -44.141  -9.446 -53.737  1.00 41.86           C  
ANISOU 1830  CG1 ILE A 240     5868   4969   5067    258    780    826       C  
ATOM   1831  CG2 ILE A 240     -45.653 -11.306 -52.945  1.00 45.75           C  
ANISOU 1831  CG2 ILE A 240     6594   5263   5527    479    583    999       C  
ATOM   1832  CD1 ILE A 240     -43.632  -9.018 -52.383  1.00 40.96           C  
ANISOU 1832  CD1 ILE A 240     5592   4959   5012    314    679    793       C  
ATOM   1833  N   ALA A 241     -48.468 -10.614 -54.889  1.00 44.55           N  
ANISOU 1833  N   ALA A 241     6792   4864   5269    186    578   1195       N  
ATOM   1834  CA  ALA A 241     -49.668 -11.441 -54.989  1.00 41.51           C  
ANISOU 1834  CA  ALA A 241     6517   4374   4880    193    509   1248       C  
ATOM   1835  C   ALA A 241     -49.872 -11.955 -56.409  1.00 47.15           C  
ANISOU 1835  C   ALA A 241     7382   5034   5500    121    519   1245       C  
ATOM   1836  O   ALA A 241     -50.195 -13.133 -56.611  1.00 54.32           O  
ANISOU 1836  O   ALA A 241     8380   5882   6377    152    523   1228       O  
ATOM   1837  CB  ALA A 241     -50.892 -10.652 -54.528  1.00 42.37           C  
ANISOU 1837  CB  ALA A 241     6591   4431   5078    137    426   1298       C  
ATOM   1838  N   ILE A 242     -49.682 -11.092 -57.409  1.00 47.31           N  
ANISOU 1838  N   ILE A 242     7473   5058   5446     -1    527   1260       N  
ATOM   1839  CA  ILE A 242     -49.864 -11.526 -58.791  1.00 45.02           C  
ANISOU 1839  CA  ILE A 242     7380   4715   5009   -112    531   1256       C  
ATOM   1840  C   ILE A 242     -48.780 -12.523 -59.188  1.00 45.00           C  
ANISOU 1840  C   ILE A 242     7391   4758   4947    -79    715   1124       C  
ATOM   1841  O   ILE A 242     -49.040 -13.472 -59.941  1.00 48.76           O  
ANISOU 1841  O   ILE A 242     8013   5176   5337   -115    740   1085       O  
ATOM   1842  CB  ILE A 242     -49.902 -10.309 -59.732  1.00 44.22           C  
ANISOU 1842  CB  ILE A 242     7427   4578   4797   -280    481   1323       C  
ATOM   1843  CG1 ILE A 242     -51.128  -9.451 -59.428  1.00 43.91           C  
ANISOU 1843  CG1 ILE A 242     7369   4447   4869   -263    253   1439       C  
ATOM   1844  CG2 ILE A 242     -49.923 -10.752 -61.191  1.00 43.81           C  
ANISOU 1844  CG2 ILE A 242     7639   4481   4524   -439    501   1312       C  
ATOM   1845  CD1 ILE A 242     -51.264  -8.234 -60.337  1.00 45.43           C  
ANISOU 1845  CD1 ILE A 242     7764   4540   4957   -400    134   1539       C  
ATOM   1846  N   GLU A 243     -47.554 -12.332 -58.691  1.00 44.79           N  
ANISOU 1846  N   GLU A 243     7195   4834   4990     -8    842   1027       N  
ATOM   1847  CA  GLU A 243     -46.501 -13.321 -58.910  1.00 49.85           C  
ANISOU 1847  CA  GLU A 243     7770   5511   5659     83   1000    861       C  
ATOM   1848  C   GLU A 243     -46.924 -14.690 -58.392  1.00 54.57           C  
ANISOU 1848  C   GLU A 243     8404   6010   6322    258    928    869       C  
ATOM   1849  O   GLU A 243     -46.757 -15.707 -59.077  1.00 59.48           O  
ANISOU 1849  O   GLU A 243     9126   6563   6911    276   1019    772       O  
ATOM   1850  CB  GLU A 243     -45.204 -12.879 -58.230  1.00 52.56           C  
ANISOU 1850  CB  GLU A 243     7850   5990   6129    168   1083    744       C  
ATOM   1851  CG  GLU A 243     -44.355 -11.925 -59.043  1.00 61.61           C  
ANISOU 1851  CG  GLU A 243     8970   7234   7205    -40   1275    634       C  
ATOM   1852  CD  GLU A 243     -43.717 -12.591 -60.245  1.00 69.69           C  
ANISOU 1852  CD  GLU A 243    10063   8263   8153   -135   1508    446       C  
ATOM   1853  OE1 GLU A 243     -43.101 -13.664 -60.073  1.00 74.36           O  
ANISOU 1853  OE1 GLU A 243    10507   8861   8885     56   1570    289       O  
ATOM   1854  OE2 GLU A 243     -43.834 -12.043 -61.362  1.00 71.38           O  
ANISOU 1854  OE2 GLU A 243    10503   8457   8162   -404   1627    449       O  
ATOM   1855  N   GLU A 244     -47.482 -14.731 -57.180  1.00 54.40           N  
ANISOU 1855  N   GLU A 244     8333   5959   6376    362    784    975       N  
ATOM   1856  CA  GLU A 244     -47.892 -16.008 -56.606  1.00 55.72           C  
ANISOU 1856  CA  GLU A 244     8594   6002   6573    490    725    997       C  
ATOM   1857  C   GLU A 244     -49.049 -16.616 -57.386  1.00 50.20           C  
ANISOU 1857  C   GLU A 244     8101   5190   5784    361    713   1031       C  
ATOM   1858  O   GLU A 244     -49.091 -17.835 -57.586  1.00 53.76           O  
ANISOU 1858  O   GLU A 244     8683   5521   6223    415    749    981       O  
ATOM   1859  CB  GLU A 244     -48.262 -15.832 -55.132  1.00 56.64           C  
ANISOU 1859  CB  GLU A 244     8667   6114   6739    559    605   1097       C  
ATOM   1860  CG  GLU A 244     -48.507 -17.139 -54.388  1.00 61.93           C  
ANISOU 1860  CG  GLU A 244     9490   6634   7407    674    549   1131       C  
ATOM   1861  CD  GLU A 244     -47.241 -17.952 -54.181  1.00 69.00           C  
ANISOU 1861  CD  GLU A 244    10350   7489   8378    907    529   1050       C  
ATOM   1862  OE1 GLU A 244     -46.139 -17.436 -54.461  1.00 72.85           O  
ANISOU 1862  OE1 GLU A 244    10626   8106   8946    978    570    941       O  
ATOM   1863  OE2 GLU A 244     -47.347 -19.113 -53.735  1.00 73.72           O  
ANISOU 1863  OE2 GLU A 244    11130   7911   8970   1019    468   1082       O  
ATOM   1864  N   ILE A 245     -49.995 -15.787 -57.835  1.00 47.14           N  
ANISOU 1864  N   ILE A 245     7742   4824   5343    195    642   1104       N  
ATOM   1865  CA  ILE A 245     -51.063 -16.287 -58.699  1.00 46.15           C  
ANISOU 1865  CA  ILE A 245     7783   4617   5136     58    590   1115       C  
ATOM   1866  C   ILE A 245     -50.474 -16.942 -59.940  1.00 46.29           C  
ANISOU 1866  C   ILE A 245     7952   4606   5029      0    711   1007       C  
ATOM   1867  O   ILE A 245     -50.908 -18.023 -60.355  1.00 49.12           O  
ANISOU 1867  O   ILE A 245     8463   4863   5338    -37    731    957       O  
ATOM   1868  CB  ILE A 245     -52.038 -15.154 -59.070  1.00 47.22           C  
ANISOU 1868  CB  ILE A 245     7897   4781   5265    -74    438   1201       C  
ATOM   1869  CG1 ILE A 245     -53.041 -14.918 -57.944  1.00 49.72           C  
ANISOU 1869  CG1 ILE A 245     8080   5084   5729    -47    346   1249       C  
ATOM   1870  CG2 ILE A 245     -52.778 -15.479 -60.358  1.00 46.54           C  
ANISOU 1870  CG2 ILE A 245     7994   4642   5048   -233    352   1193       C  
ATOM   1871  CD1 ILE A 245     -54.002 -13.781 -58.212  1.00 52.88           C  
ANISOU 1871  CD1 ILE A 245     8402   5489   6201   -121    176   1302       C  
ATOM   1872  N   ILE A 246     -49.469 -16.305 -60.545  1.00 45.21           N  
ANISOU 1872  N   ILE A 246     7788   4555   4835    -39    825    943       N  
ATOM   1873  CA  ILE A 246     -48.846 -16.867 -61.740  1.00 50.22           C  
ANISOU 1873  CA  ILE A 246     8568   5173   5341   -132   1001    796       C  
ATOM   1874  C   ILE A 246     -48.161 -18.187 -61.414  1.00 54.93           C  
ANISOU 1874  C   ILE A 246     9128   5691   6053     58   1129    653       C  
ATOM   1875  O   ILE A 246     -48.206 -19.137 -62.205  1.00 60.28           O  
ANISOU 1875  O   ILE A 246     9975   6274   6653      3   1231    539       O  
ATOM   1876  CB  ILE A 246     -47.867 -15.851 -62.360  1.00 51.81           C  
ANISOU 1876  CB  ILE A 246     8739   5486   5459   -254   1147    730       C  
ATOM   1877  CG1 ILE A 246     -48.630 -14.632 -62.878  1.00 46.87           C  
ANISOU 1877  CG1 ILE A 246     8257   4868   4684   -454    987    890       C  
ATOM   1878  CG2 ILE A 246     -47.062 -16.489 -63.486  1.00 48.37           C  
ANISOU 1878  CG2 ILE A 246     8426   5046   4906   -363   1406    517       C  
ATOM   1879  CD1 ILE A 246     -47.738 -13.520 -63.392  1.00 47.71           C  
ANISOU 1879  CD1 ILE A 246     8393   5051   4683   -616   1128    856       C  
ATOM   1880  N   ARG A 247     -47.527 -18.274 -60.242  1.00 55.11           N  
ANISOU 1880  N   ARG A 247     8948   5730   6260    288   1102    655       N  
ATOM   1881  CA  ARG A 247     -46.817 -19.496 -59.877  1.00 58.62           C  
ANISOU 1881  CA  ARG A 247     9366   6064   6842    517   1163    532       C  
ATOM   1882  C   ARG A 247     -47.785 -20.650 -59.643  1.00 59.16           C  
ANISOU 1882  C   ARG A 247     9659   5934   6884    536   1081    600       C  
ATOM   1883  O   ARG A 247     -47.566 -21.766 -60.127  1.00 59.79           O  
ANISOU 1883  O   ARG A 247     9872   5866   6979    591   1182    472       O  
ATOM   1884  CB  ARG A 247     -45.958 -19.255 -58.635  1.00 59.01           C  
ANISOU 1884  CB  ARG A 247     9174   6173   7074    757   1076    544       C  
ATOM   1885  CG  ARG A 247     -44.998 -20.394 -58.336  1.00 60.66           C  
ANISOU 1885  CG  ARG A 247     9320   6264   7465   1041   1095    397       C  
ATOM   1886  CD  ARG A 247     -44.331 -20.227 -56.981  1.00 61.64           C  
ANISOU 1886  CD  ARG A 247     9252   6424   7742   1283    909    451       C  
ATOM   1887  NE  ARG A 247     -45.285 -20.377 -55.886  1.00 62.82           N  
ANISOU 1887  NE  ARG A 247     9585   6474   7809   1284    712    680       N  
ATOM   1888  CZ  ARG A 247     -45.605 -21.542 -55.328  1.00 62.59           C  
ANISOU 1888  CZ  ARG A 247     9785   6212   7783   1415    607    750       C  
ATOM   1889  NH1 ARG A 247     -45.048 -22.665 -55.763  1.00 62.57           N  
ANISOU 1889  NH1 ARG A 247     9849   6032   7892   1598    650    615       N  
ATOM   1890  NH2 ARG A 247     -46.485 -21.584 -54.336  1.00 59.25           N  
ANISOU 1890  NH2 ARG A 247     9545   5715   7252   1347    478    940       N  
ATOM   1891  N   VAL A 248     -48.864 -20.399 -58.898  1.00 58.99           N  
ANISOU 1891  N   VAL A 248     9683   5898   6833    471    926    773       N  
ATOM   1892  CA  VAL A 248     -49.836 -21.449 -58.611  1.00 58.45           C  
ANISOU 1892  CA  VAL A 248     9825   5648   6734    432    878    822       C  
ATOM   1893  C   VAL A 248     -50.590 -21.847 -59.872  1.00 56.23           C  
ANISOU 1893  C   VAL A 248     9723   5324   6320    210    931    754       C  
ATOM   1894  O   VAL A 248     -50.948 -23.019 -60.046  1.00 47.77           O  
ANISOU 1894  O   VAL A 248     8852   4074   5223    186    975    699       O  
ATOM   1895  CB  VAL A 248     -50.792 -20.989 -57.495  1.00 54.64           C  
ANISOU 1895  CB  VAL A 248     9309   5189   6263    373    749    976       C  
ATOM   1896  CG1 VAL A 248     -51.812 -22.073 -57.180  1.00 55.70           C  
ANISOU 1896  CG1 VAL A 248     9665   5140   6359    276    744   1000       C  
ATOM   1897  CG2 VAL A 248     -50.005 -20.617 -56.247  1.00 53.21           C  
ANISOU 1897  CG2 VAL A 248     8998   5050   6168    566    687   1037       C  
ATOM   1898  N   LEU A 249     -50.838 -20.888 -60.770  1.00 45.97           N  
ANISOU 1898  N   LEU A 249     8387   4166   4913     33    912    760       N  
ATOM   1899  CA  LEU A 249     -51.491 -21.195 -62.038  1.00 47.66           C  
ANISOU 1899  CA  LEU A 249     8798   4351   4959   -194    919    698       C  
ATOM   1900  C   LEU A 249     -50.713 -22.230 -62.839  1.00 49.37           C  
ANISOU 1900  C   LEU A 249     9173   4461   5124   -177   1125    507       C  
ATOM   1901  O   LEU A 249     -51.312 -23.030 -63.565  1.00 50.73           O  
ANISOU 1901  O   LEU A 249     9561   4532   5182   -332   1149    432       O  
ATOM   1902  CB  LEU A 249     -51.664 -19.917 -62.865  1.00 51.84           C  
ANISOU 1902  CB  LEU A 249     9313   5028   5358   -364    834    754       C  
ATOM   1903  CG  LEU A 249     -52.963 -19.128 -62.696  1.00 52.48           C  
ANISOU 1903  CG  LEU A 249     9334   5155   5450   -471    582    897       C  
ATOM   1904  CD1 LEU A 249     -52.889 -17.794 -63.429  1.00 51.36           C  
ANISOU 1904  CD1 LEU A 249     9212   5110   5194   -582    477    973       C  
ATOM   1905  CD2 LEU A 249     -54.137 -19.943 -63.201  1.00 53.52           C  
ANISOU 1905  CD2 LEU A 249     9609   5210   5517   -634    479    861       C  
ATOM   1906  N   GLN A 250     -49.387 -22.237 -62.715  1.00 50.12           N  
ANISOU 1906  N   GLN A 250     9144   4576   5322      6   1281    396       N  
ATOM   1907  CA  GLN A 250     -48.528 -23.096 -63.516  1.00 61.57           C  
ANISOU 1907  CA  GLN A 250    10686   5936   6772     38   1516    159       C  
ATOM   1908  C   GLN A 250     -48.155 -24.398 -62.818  1.00 64.27           C  
ANISOU 1908  C   GLN A 250    11058   6053   7309    305   1548     84       C  
ATOM   1909  O   GLN A 250     -47.410 -25.199 -63.392  1.00 61.67           O  
ANISOU 1909  O   GLN A 250    10779   5610   7041    385   1744   -142       O  
ATOM   1910  CB  GLN A 250     -47.257 -22.337 -63.911  1.00 67.07           C  
ANISOU 1910  CB  GLN A 250    11193   6789   7500     62   1698     19       C  
ATOM   1911  CG  GLN A 250     -47.515 -21.141 -64.819  1.00 68.36           C  
ANISOU 1911  CG  GLN A 250    11438   7118   7419   -243   1703     74       C  
ATOM   1912  CD  GLN A 250     -46.259 -20.343 -65.111  1.00 74.37           C  
ANISOU 1912  CD  GLN A 250    12025   8029   8204   -268   1916    -68       C  
ATOM   1913  OE1 GLN A 250     -45.362 -20.250 -64.273  1.00 77.56           O  
ANISOU 1913  OE1 GLN A 250    12134   8482   8852    -27   1951   -129       O  
ATOM   1914  NE2 GLN A 250     -46.188 -19.764 -66.306  1.00 75.80           N  
ANISOU 1914  NE2 GLN A 250    12402   8281   8116   -584   2055   -130       N  
ATOM   1915  N   LEU A 251     -48.647 -24.632 -61.604  1.00 65.47           N  
ANISOU 1915  N   LEU A 251    11206   6116   7553    436   1366    259       N  
ATOM   1916  CA  LEU A 251     -48.384 -25.889 -60.919  1.00 64.30           C  
ANISOU 1916  CA  LEU A 251    11181   5702   7549    670   1353    230       C  
ATOM   1917  C   LEU A 251     -49.256 -26.991 -61.503  1.00 65.63           C  
ANISOU 1917  C   LEU A 251    11674   5657   7604    494   1416    173       C  
ATOM   1918  O   LEU A 251     -50.477 -26.838 -61.613  1.00 61.38           O  
ANISOU 1918  O   LEU A 251    11244   5158   6919    234   1338    276       O  
ATOM   1919  CB  LEU A 251     -48.637 -25.751 -59.419  1.00 61.12           C  
ANISOU 1919  CB  LEU A 251    10745   5262   7217    808   1147    445       C  
ATOM   1920  CG  LEU A 251     -47.567 -24.995 -58.630  1.00 65.55           C  
ANISOU 1920  CG  LEU A 251    11016   5963   7925   1050   1061    473       C  
ATOM   1921  CD1 LEU A 251     -47.869 -25.044 -57.139  1.00 67.40           C  
ANISOU 1921  CD1 LEU A 251    11314   6120   8175   1155    856    679       C  
ATOM   1922  CD2 LEU A 251     -46.188 -25.565 -58.921  1.00 67.86           C  
ANISOU 1922  CD2 LEU A 251    11184   6175   8422   1333   1151    255       C  
ATOM   1923  N   THR A 252     -48.624 -28.099 -61.886  1.00 73.38           N  
ANISOU 1923  N   THR A 252    12790   6411   8680    638   1557    -17       N  
ATOM   1924  CA  THR A 252     -49.322 -29.272 -62.400  1.00 80.08           C  
ANISOU 1924  CA  THR A 252    13975   7012   9441    486   1640   -101       C  
ATOM   1925  C   THR A 252     -49.031 -30.501 -61.545  1.00 84.58           C  
ANISOU 1925  C   THR A 252    14741   7218  10179    756   1596    -89       C  
ATOM   1926  O   THR A 252     -49.048 -31.629 -62.039  1.00 87.87           O  
ANISOU 1926  O   THR A 252    15416   7359  10610    751   1722   -244       O  
ATOM   1927  CB  THR A 252     -48.947 -29.536 -63.858  1.00 79.24           C  
ANISOU 1927  CB  THR A 252    13942   6919   9248    344   1884   -376       C  
ATOM   1928  OG1 THR A 252     -47.542 -29.808 -63.954  1.00 81.61           O  
ANISOU 1928  OG1 THR A 252    14081   7150   9775    647   2040   -590       O  
ATOM   1929  CG2 THR A 252     -49.286 -28.332 -64.725  1.00 75.77           C  
ANISOU 1929  CG2 THR A 252    13405   6799   8584     45   1889   -353       C  
ATOM   1930  N   THR A 253     -48.762 -30.292 -60.258  1.00 86.62           N  
ANISOU 1930  N   THR A 253    14917   7447  10547    985   1405     98       N  
ATOM   1931  CA  THR A 253     -48.331 -31.357 -59.366  1.00 95.18           C  
ANISOU 1931  CA  THR A 253    16215   8168  11782   1283   1300    144       C  
ATOM   1932  C   THR A 253     -49.167 -31.358 -58.094  1.00 94.24           C  
ANISOU 1932  C   THR A 253    16289   7971  11548   1194   1115    424       C  
ATOM   1933  O   THR A 253     -49.690 -30.323 -57.671  1.00 93.84           O  
ANISOU 1933  O   THR A 253    16065   8195  11396   1030   1045    565       O  
ATOM   1934  CB  THR A 253     -46.848 -31.211 -58.993  1.00101.96           C  
ANISOU 1934  CB  THR A 253    16796   9032  12913   1718   1217     59       C  
ATOM   1935  OG1 THR A 253     -46.616 -29.900 -58.459  1.00100.27           O  
ANISOU 1935  OG1 THR A 253    16251   9161  12687   1722   1100    183       O  
ATOM   1936  CG2 THR A 253     -45.963 -31.427 -60.212  1.00106.59           C  
ANISOU 1936  CG2 THR A 253    17213   9638  13649   1807   1462   -281       C  
ATOM   1937  N   THR A 254     -49.284 -32.538 -57.489  1.00 93.05           N  
ANISOU 1937  N   THR A 254    16526   7419  11411   1289   1054    489       N  
ATOM   1938  CA  THR A 254     -49.909 -32.654 -56.179  1.00 91.08           C  
ANISOU 1938  CA  THR A 254    16529   7042  11034   1208    899    743       C  
ATOM   1939  C   THR A 254     -49.025 -31.982 -55.135  1.00 91.32           C  
ANISOU 1939  C   THR A 254    16362   7181  11154   1511    663    883       C  
ATOM   1940  O   THR A 254     -47.828 -32.269 -55.042  1.00 94.32           O  
ANISOU 1940  O   THR A 254    16649   7441  11747   1911    539    815       O  
ATOM   1941  CB  THR A 254     -50.137 -34.124 -55.822  1.00 90.32           C  
ANISOU 1941  CB  THR A 254    16909   6501  10909   1218    881    772       C  
ATOM   1942  OG1 THR A 254     -50.972 -34.739 -56.813  1.00 70.17           O  
ANISOU 1942  OG1 THR A 254    14548   3846   8268    909   1108    621       O  
ATOM   1943  CG2 THR A 254     -50.803 -34.247 -54.459  1.00 87.12           C  
ANISOU 1943  CG2 THR A 254    16646   6133  10322   1035    737    989       C  
ATOM   1944  N   PHE A 255     -49.621 -31.079 -54.352  1.00 91.96           N  
ANISOU 1944  N   PHE A 255    16358   7494  11090   1318    599   1052       N  
ATOM   1945  CA  PHE A 255     -48.845 -30.273 -53.413  1.00 94.68           C  
ANISOU 1945  CA  PHE A 255    16487   8000  11486   1544    388   1167       C  
ATOM   1946  C   PHE A 255     -48.224 -31.129 -52.317  1.00 96.10           C  
ANISOU 1946  C   PHE A 255    16939   7884  11689   1808    127   1293       C  
ATOM   1947  O   PHE A 255     -47.064 -30.922 -51.941  1.00 96.85           O  
ANISOU 1947  O   PHE A 255    16852   7995  11953   2173    -89   1290       O  
ATOM   1948  CB  PHE A 255     -49.736 -29.190 -52.802  1.00 98.61           C  
ANISOU 1948  CB  PHE A 255    16872   8784  11813   1237    409   1293       C  
ATOM   1949  CG  PHE A 255     -48.991 -28.178 -51.978  1.00103.85           C  
ANISOU 1949  CG  PHE A 255    17273   9670  12514   1410    229   1376       C  
ATOM   1950  CD1 PHE A 255     -47.665 -27.878 -52.249  1.00106.42           C  
ANISOU 1950  CD1 PHE A 255    17284  10099  13051   1751    122   1272       C  
ATOM   1951  CD2 PHE A 255     -49.618 -27.529 -50.927  1.00104.70           C  
ANISOU 1951  CD2 PHE A 255    17438   9891  12453   1208    188   1525       C  
ATOM   1952  CE1 PHE A 255     -46.981 -26.947 -51.489  1.00107.03           C  
ANISOU 1952  CE1 PHE A 255    17112  10392  13163   1882    -49   1329       C  
ATOM   1953  CE2 PHE A 255     -48.940 -26.597 -50.164  1.00105.47           C  
ANISOU 1953  CE2 PHE A 255    17316  10190  12568   1341     26   1587       C  
ATOM   1954  CZ  PHE A 255     -47.620 -26.306 -50.446  1.00106.09           C  
ANISOU 1954  CZ  PHE A 255    17085  10374  12850   1677   -106   1495       C  
ATOM   1955  N   GLU A 256     -48.973 -32.103 -51.802  1.00 98.27           N  
ANISOU 1955  N   GLU A 256    17548   7982  11806   1587    129   1363       N  
ATOM   1956  CA  GLU A 256     -48.547 -32.868 -50.636  1.00102.77           C  
ANISOU 1956  CA  GLU A 256    18339   8371  12337   1724   -132   1491       C  
ATOM   1957  C   GLU A 256     -47.542 -33.957 -51.000  1.00106.97           C  
ANISOU 1957  C   GLU A 256    18939   8592  13111   2107   -265   1400       C  
ATOM   1958  O   GLU A 256     -47.440 -34.972 -50.304  1.00107.70           O  
ANISOU 1958  O   GLU A 256    19330   8430  13160   2162   -430   1490       O  
ATOM   1959  CB  GLU A 256     -49.765 -33.477 -49.934  1.00102.85           C  
ANISOU 1959  CB  GLU A 256    18716   8298  12065   1317    -39   1584       C  
ATOM   1960  CG  GLU A 256     -50.701 -32.456 -49.279  1.00100.07           C  
ANISOU 1960  CG  GLU A 256    18282   8234  11506    963     65   1653       C  
ATOM   1961  CD  GLU A 256     -51.553 -31.683 -50.278  1.00 96.23           C  
ANISOU 1961  CD  GLU A 256    17564   7960  11039    714    333   1541       C  
ATOM   1962  OE1 GLU A 256     -51.448 -31.946 -51.495  1.00 96.02           O  
ANISOU 1962  OE1 GLU A 256    17483   7860  11142    782    447   1415       O  
ATOM   1963  OE2 GLU A 256     -52.331 -30.809 -49.843  1.00 93.94           O  
ANISOU 1963  OE2 GLU A 256    17155   7900  10640    446    427   1568       O  
ATOM   1964  N   GLU A 257     -46.799 -33.755 -52.086  1.00109.68           N  
ANISOU 1964  N   GLU A 257    19011   8944  13717   2372   -179   1202       N  
ATOM   1965  CA  GLU A 257     -45.715 -34.638 -52.501  1.00114.92           C  
ANISOU 1965  CA  GLU A 257    19621   9347  14695   2783   -280   1044       C  
ATOM   1966  C   GLU A 257     -44.490 -33.822 -52.887  1.00120.49           C  
ANISOU 1966  C   GLU A 257    19854  10226  15699   3166   -341    876       C  
ATOM   1967  O   GLU A 257     -43.762 -34.160 -53.824  1.00122.36           O  
ANISOU 1967  O   GLU A 257    19907  10361  16223   3425   -221    606       O  
ATOM   1968  CB  GLU A 257     -46.149 -35.539 -53.656  1.00113.20           C  
ANISOU 1968  CB  GLU A 257    19591   8905  14517   2670      1    854       C  
ATOM   1969  CG  GLU A 257     -47.316 -36.457 -53.331  1.00112.51           C  
ANISOU 1969  CG  GLU A 257    19955   8634  14161   2300     73    976       C  
ATOM   1970  CD  GLU A 257     -47.671 -37.383 -54.479  1.00112.63           C  
ANISOU 1970  CD  GLU A 257    20150   8423  14222   2193    332    770       C  
ATOM   1971  OE1 GLU A 257     -46.784 -37.677 -55.308  1.00114.97           O  
ANISOU 1971  OE1 GLU A 257    20282   8596  14805   2498    392    538       O  
ATOM   1972  OE2 GLU A 257     -48.841 -37.814 -54.554  1.00111.43           O  
ANISOU 1972  OE2 GLU A 257    20286   8227  13826   1789    493    809       O  
ATOM   1973  N   GLU A 258     -44.247 -32.732 -52.165  1.00128.62           N  
ANISOU 1973  N   GLU A 258    20668  11533  16668   3190   -501    998       N  
ATOM   1974  CA  GLU A 258     -43.154 -31.824 -52.490  1.00131.33           C  
ANISOU 1974  CA  GLU A 258    20537  12095  17268   3511   -540    826       C  
ATOM   1975  C   GLU A 258     -42.526 -31.236 -51.230  1.00131.92           C  
ANISOU 1975  C   GLU A 258    20441  12336  17345   3661   -913    986       C  
ATOM   1976  O   GLU A 258     -43.145 -30.436 -50.529  1.00128.51           O  
ANISOU 1976  O   GLU A 258    20088  12100  16640   3395   -947   1185       O  
ATOM   1977  CB  GLU A 258     -43.655 -30.704 -53.404  1.00130.72           C  
ANISOU 1977  CB  GLU A 258    20148  12438  17082   3155   -191    713       C  
ATOM   1978  CG  GLU A 258     -42.606 -29.669 -53.764  1.00136.28           C  
ANISOU 1978  CG  GLU A 258    20249  13527  18006   3289   -158    507       C  
ATOM   1979  CD  GLU A 258     -43.135 -28.621 -54.724  1.00136.98           C  
ANISOU 1979  CD  GLU A 258    20104  13991  17953   2898    176    416       C  
ATOM   1980  OE1 GLU A 258     -44.235 -28.825 -55.280  1.00137.91           O  
ANISOU 1980  OE1 GLU A 258    20484  14058  17858   2577    372    464       O  
ATOM   1981  OE2 GLU A 258     -42.454 -27.594 -54.920  1.00137.17           O  
ANISOU 1981  OE2 GLU A 258    19696  14347  18076   2905    225    295       O  
ATOM   1982  N   ALA A 266     -38.059 -30.239 -34.386  1.00106.31           N  
ANISOU 1982  N   ALA A 266    18345  12815   9234   2227   1337    989       N  
ATOM   1983  CA  ALA A 266     -39.409 -30.743 -34.607  1.00105.00           C  
ANISOU 1983  CA  ALA A 266    18745  12286   8863   2020    851    662       C  
ATOM   1984  C   ALA A 266     -40.419 -29.600 -34.647  1.00102.67           C  
ANISOU 1984  C   ALA A 266    18202  11956   8853   1543    569    689       C  
ATOM   1985  O   ALA A 266     -40.046 -28.427 -34.646  1.00105.21           O  
ANISOU 1985  O   ALA A 266    18029  12495   9452   1420    760    926       O  
ATOM   1986  CB  ALA A 266     -39.783 -31.745 -33.525  1.00102.70           C  
ANISOU 1986  CB  ALA A 266    18508  11800   8712   1867    560    409       C  
ATOM   1987  N   SER A 267     -41.700 -29.954 -34.690  1.00 93.40           N  
ANISOU 1987  N   SER A 267    17366  10492   7630   1277     94    491       N  
ATOM   1988  CA  SER A 267     -42.786 -28.990 -34.673  1.00 80.45           C  
ANISOU 1988  CA  SER A 267    15494   8806   6268    859   -188    544       C  
ATOM   1989  C   SER A 267     -43.426 -28.959 -33.287  1.00 68.45           C  
ANISOU 1989  C   SER A 267    13548   7251   5210    507   -408    471       C  
ATOM   1990  O   SER A 267     -42.986 -29.634 -32.354  1.00 63.67           O  
ANISOU 1990  O   SER A 267    12818   6666   4706    561   -350    375       O  
ATOM   1991  CB  SER A 267     -43.817 -29.329 -35.752  1.00 75.63           C  
ANISOU 1991  CB  SER A 267    15472   7924   5342    806   -579    480       C  
ATOM   1992  OG  SER A 267     -44.396 -30.602 -35.516  1.00 72.40           O  
ANISOU 1992  OG  SER A 267    15361   7213   4934    737   -949    274       O  
ATOM   1993  N   ALA A 268     -44.484 -28.157 -33.152  1.00 62.04           N  
ANISOU 1993  N   ALA A 268    12517   6396   4661    187   -636    547       N  
ATOM   1994  CA  ALA A 268     -45.194 -28.090 -31.879  1.00 55.59           C  
ANISOU 1994  CA  ALA A 268    11335   5559   4228    -61   -793    530       C  
ATOM   1995  C   ALA A 268     -45.956 -29.380 -31.605  1.00 51.87           C  
ANISOU 1995  C   ALA A 268    11133   4876   3700   -147  -1140    455       C  
ATOM   1996  O   ALA A 268     -45.936 -29.894 -30.480  1.00 51.25           O  
ANISOU 1996  O   ALA A 268    10857   4814   3803   -179  -1138    405       O  
ATOM   1997  CB  ALA A 268     -46.141 -26.892 -31.863  1.00 50.30           C  
ANISOU 1997  CB  ALA A 268    10383   4902   3826   -289   -894    686       C  
ATOM   1998  N   ALA A 269     -46.636 -29.914 -32.621  1.00 58.78           N  
ANISOU 1998  N   ALA A 269    12483   5527   4324   -203  -1485    472       N  
ATOM   1999  CA  ALA A 269     -47.353 -31.174 -32.454  1.00 63.71           C  
ANISOU 1999  CA  ALA A 269    13411   5879   4915   -338  -1919    446       C  
ATOM   2000  C   ALA A 269     -46.400 -32.329 -32.174  1.00 64.70           C  
ANISOU 2000  C   ALA A 269    13850   5929   4806    -69  -1798    239       C  
ATOM   2001  O   ALA A 269     -46.752 -33.261 -31.442  1.00 66.37           O  
ANISOU 2001  O   ALA A 269    14075   5995   5146   -182  -2026    227       O  
ATOM   2002  CB  ALA A 269     -48.194 -31.465 -33.698  1.00 64.26           C  
ANISOU 2002  CB  ALA A 269    13988   5666   4763   -472  -2395    502       C  
ATOM   2003  N   SER A 270     -45.194 -32.286 -32.746  1.00 67.70           N  
ANISOU 2003  N   SER A 270    14453   6415   4854    310  -1422    129       N  
ATOM   2004  CA  SER A 270     -44.209 -33.326 -32.468  1.00 68.43           C  
ANISOU 2004  CA  SER A 270    14754   6470   4776    637  -1223    -22       C  
ATOM   2005  C   SER A 270     -43.596 -33.157 -31.085  1.00 67.45           C  
ANISOU 2005  C   SER A 270    14053   6601   4974    623   -943     -4       C  
ATOM   2006  O   SER A 270     -43.214 -34.150 -30.457  1.00 73.76           O  
ANISOU 2006  O   SER A 270    14946   7327   5750    744   -942    -97       O  
ATOM   2007  CB  SER A 270     -43.118 -33.323 -33.537  1.00 71.83           C  
ANISOU 2007  CB  SER A 270    15432   6973   4889   1101   -831    -51       C  
ATOM   2008  OG  SER A 270     -43.652 -33.669 -34.802  1.00 84.14           O  
ANISOU 2008  OG  SER A 270    17488   8232   6249   1156  -1085   -107       O  
ATOM   2009  N   LEU A 271     -43.482 -31.919 -30.602  1.00 64.55           N  
ANISOU 2009  N   LEU A 271    13107   6496   4923    483   -733    111       N  
ATOM   2010  CA  LEU A 271     -43.053 -31.705 -29.225  1.00 60.08           C  
ANISOU 2010  CA  LEU A 271    12032   6111   4685    423   -574    116       C  
ATOM   2011  C   LEU A 271     -44.085 -32.249 -28.248  1.00 56.54           C  
ANISOU 2011  C   LEU A 271    11491   5538   4454    187   -869    110       C  
ATOM   2012  O   LEU A 271     -43.740 -32.959 -27.297  1.00 57.14           O  
ANISOU 2012  O   LEU A 271    11479   5631   4602    245   -836     56       O  
ATOM   2013  CB  LEU A 271     -42.800 -30.219 -28.975  1.00 63.77           C  
ANISOU 2013  CB  LEU A 271    12031   6790   5409    312   -387    229       C  
ATOM   2014  CG  LEU A 271     -41.435 -29.684 -29.409  1.00 72.89           C  
ANISOU 2014  CG  LEU A 271    13033   8150   6512    523    -37    336       C  
ATOM   2015  CD1 LEU A 271     -41.405 -28.164 -29.334  1.00 73.70           C  
ANISOU 2015  CD1 LEU A 271    12759   8360   6883    332     17    474       C  
ATOM   2016  CD2 LEU A 271     -40.334 -30.288 -28.550  1.00 75.24           C  
ANISOU 2016  CD2 LEU A 271    13144   8569   6875    689    132    326       C  
ATOM   2017  N   ALA A 272     -45.362 -31.925 -28.469  1.00 55.17           N  
ANISOU 2017  N   ALA A 272    11299   5258   4403    -69  -1147    227       N  
ATOM   2018  CA  ALA A 272     -46.418 -32.464 -27.619  1.00 53.91           C  
ANISOU 2018  CA  ALA A 272    10996   5008   4479   -277  -1408    346       C  
ATOM   2019  C   ALA A 272     -46.437 -33.986 -27.666  1.00 56.33           C  
ANISOU 2019  C   ALA A 272    11698   5067   4640   -258  -1670    285       C  
ATOM   2020  O   ALA A 272     -46.543 -34.650 -26.625  1.00 54.17           O  
ANISOU 2020  O   ALA A 272    11264   4792   4524   -290  -1702    326       O  
ATOM   2021  CB  ALA A 272     -47.772 -31.898 -28.045  1.00 49.39           C  
ANISOU 2021  CB  ALA A 272    10319   4373   4076   -533  -1671    580       C  
ATOM   2022  N   HIS A 273     -46.324 -34.556 -28.869  1.00 55.20           N  
ANISOU 2022  N   HIS A 273    12130   4681   4162   -181  -1872    188       N  
ATOM   2023  CA  HIS A 273     -46.324 -36.008 -29.000  1.00 58.52           C  
ANISOU 2023  CA  HIS A 273    13067   4774   4396   -137  -2180    102       C  
ATOM   2024  C   HIS A 273     -45.129 -36.625 -28.286  1.00 61.25           C  
ANISOU 2024  C   HIS A 273    13397   5218   4656    176  -1845    -57       C  
ATOM   2025  O   HIS A 273     -45.245 -37.695 -27.681  1.00 60.19           O  
ANISOU 2025  O   HIS A 273    13386   4906   4578    145  -2036    -59       O  
ATOM   2026  CB  HIS A 273     -46.331 -36.401 -30.477  1.00 64.58           C  
ANISOU 2026  CB  HIS A 273    14544   5228   4765    -24  -2423    -14       C  
ATOM   2027  CG  HIS A 273     -46.582 -37.856 -30.712  1.00 67.62           C  
ANISOU 2027  CG  HIS A 273    15433   5151   5108    -31  -2811    -73       C  
ATOM   2028  ND1 HIS A 273     -45.565 -38.760 -30.931  1.00 68.85           N  
ANISOU 2028  ND1 HIS A 273    15979   5163   5019    392  -2599   -249       N  
ATOM   2029  CD2 HIS A 273     -47.734 -38.566 -30.759  1.00 70.15           C  
ANISOU 2029  CD2 HIS A 273    15932   5099   5623   -412  -3426     84       C  
ATOM   2030  CE1 HIS A 273     -46.081 -39.964 -31.108  1.00 73.05           C  
ANISOU 2030  CE1 HIS A 273    16973   5229   5554    294  -3072   -217       C  
ATOM   2031  NE2 HIS A 273     -47.395 -39.873 -31.007  1.00 73.70           N  
ANISOU 2031  NE2 HIS A 273    16935   5150   5919   -220  -3598    -11       N  
ATOM   2032  N   MET A 274     -43.973 -35.960 -28.338  1.00 54.30           N  
ANISOU 2032  N   MET A 274    12331   4622   3677    463  -1367   -135       N  
ATOM   2033  CA  MET A 274     -42.801 -36.460 -27.625  1.00 69.09           C  
ANISOU 2033  CA  MET A 274    14092   6633   5525    749  -1053   -212       C  
ATOM   2034  C   MET A 274     -43.012 -36.404 -26.115  1.00 61.63           C  
ANISOU 2034  C   MET A 274    12625   5842   4951    560  -1043   -138       C  
ATOM   2035  O   MET A 274     -42.645 -37.343 -25.395  1.00 58.70           O  
ANISOU 2035  O   MET A 274    12293   5420   4591    664  -1046   -174       O  
ATOM   2036  CB  MET A 274     -41.564 -35.662 -28.038  1.00 68.16           C  
ANISOU 2036  CB  MET A 274    13789   6807   5300   1043   -587   -192       C  
ATOM   2037  CG  MET A 274     -40.265 -36.142 -27.413  1.00 72.26           C  
ANISOU 2037  CG  MET A 274    14142   7498   5817   1356   -265   -186       C  
ATOM   2038  SD  MET A 274     -38.838 -35.191 -27.974  1.00 77.05           S  
ANISOU 2038  SD  MET A 274    14428   8466   6382   1662    247     -1       S  
ATOM   2039  CE  MET A 274     -38.701 -35.754 -29.669  1.00 83.96           C  
ANISOU 2039  CE  MET A 274    16070   9152   6680   2105    359    -39       C  
ATOM   2040  N   PHE A 275     -43.600 -35.311 -25.619  1.00 58.81           N  
ANISOU 2040  N   PHE A 275    11823   5661   4862    329  -1021    -29       N  
ATOM   2041  CA  PHE A 275     -43.976 -35.227 -24.211  1.00 59.42           C  
ANISOU 2041  CA  PHE A 275    11504   5859   5215    204  -1018     56       C  
ATOM   2042  C   PHE A 275     -44.856 -36.405 -23.810  1.00 59.59           C  
ANISOU 2042  C   PHE A 275    11662   5663   5314     65  -1330    165       C  
ATOM   2043  O   PHE A 275     -44.604 -37.073 -22.800  1.00 55.05           O  
ANISOU 2043  O   PHE A 275    10984   5122   4812    125  -1292    179       O  
ATOM   2044  CB  PHE A 275     -44.705 -33.907 -23.942  1.00 61.38           C  
ANISOU 2044  CB  PHE A 275    11406   6250   5667     38   -976    172       C  
ATOM   2045  CG  PHE A 275     -43.820 -32.809 -23.418  1.00 57.66           C  
ANISOU 2045  CG  PHE A 275    10655   5999   5253    132   -706    103       C  
ATOM   2046  CD1 PHE A 275     -43.112 -31.991 -24.287  1.00 57.49           C  
ANISOU 2046  CD1 PHE A 275    10638   6044   5160    183   -566     69       C  
ATOM   2047  CD2 PHE A 275     -43.710 -32.582 -22.056  1.00 51.86           C  
ANISOU 2047  CD2 PHE A 275     9681   5382   4641    161   -633    105       C  
ATOM   2048  CE1 PHE A 275     -42.303 -30.976 -23.803  1.00 55.78           C  
ANISOU 2048  CE1 PHE A 275    10158   5981   5055    201   -413     62       C  
ATOM   2049  CE2 PHE A 275     -42.902 -31.570 -21.568  1.00 48.40           C  
ANISOU 2049  CE2 PHE A 275     9067   5071   4254    203   -505     41       C  
ATOM   2050  CZ  PHE A 275     -42.199 -30.768 -22.441  1.00 51.59           C  
ANISOU 2050  CZ  PHE A 275     9442   5511   4647    192   -423     32       C  
ATOM   2051  N   HIS A 276     -45.891 -36.680 -24.606  1.00 61.71           N  
ANISOU 2051  N   HIS A 276    12164   5694   5589   -147  -1683    283       N  
ATOM   2052  CA  HIS A 276     -46.851 -37.716 -24.240  1.00 62.34           C  
ANISOU 2052  CA  HIS A 276    12306   5546   5835   -368  -2065    494       C  
ATOM   2053  C   HIS A 276     -46.230 -39.106 -24.322  1.00 63.50           C  
ANISOU 2053  C   HIS A 276    12921   5420   5788   -229  -2213    345       C  
ATOM   2054  O   HIS A 276     -46.519 -39.971 -23.487  1.00 58.81           O  
ANISOU 2054  O   HIS A 276    12250   4738   5359   -314  -2358    488       O  
ATOM   2055  CB  HIS A 276     -48.084 -37.616 -25.137  1.00 66.24           C  
ANISOU 2055  CB  HIS A 276    12921   5828   6420   -678  -2494    712       C  
ATOM   2056  CG  HIS A 276     -48.728 -36.264 -25.125  1.00 68.04           C  
ANISOU 2056  CG  HIS A 276    12709   6307   6835   -772  -2340    886       C  
ATOM   2057  ND1 HIS A 276     -49.722 -35.904 -26.009  1.00 72.04           N  
ANISOU 2057  ND1 HIS A 276    13257   6692   7424  -1017  -2663   1093       N  
ATOM   2058  CD2 HIS A 276     -48.520 -35.183 -24.334  1.00 65.67           C  
ANISOU 2058  CD2 HIS A 276    11969   6337   6644   -637  -1926    886       C  
ATOM   2059  CE1 HIS A 276     -50.098 -34.661 -25.765  1.00 70.46           C  
ANISOU 2059  CE1 HIS A 276    12625   6759   7387  -1002  -2405   1225       C  
ATOM   2060  NE2 HIS A 276     -49.384 -34.201 -24.753  1.00 67.80           N  
ANISOU 2060  NE2 HIS A 276    12031   6676   7054   -766  -1965   1086       N  
ATOM   2061  N   GLN A 277     -45.377 -39.337 -25.322  1.00 68.15           N  
ANISOU 2061  N   GLN A 277    14015   5869   6010     28  -2153     88       N  
ATOM   2062  CA  GLN A 277     -44.693 -40.620 -25.439  1.00 65.91           C  
ANISOU 2062  CA  GLN A 277    14250   5311   5483    271  -2232    -70       C  
ATOM   2063  C   GLN A 277     -43.741 -40.843 -24.272  1.00 59.86           C  
ANISOU 2063  C   GLN A 277    13141   4799   4803    496  -1862   -106       C  
ATOM   2064  O   GLN A 277     -43.620 -41.966 -23.765  1.00 65.92           O  
ANISOU 2064  O   GLN A 277    14097   5371   5579    550  -2001    -99       O  
ATOM   2065  CB  GLN A 277     -43.938 -40.688 -26.767  1.00 67.54           C  
ANISOU 2065  CB  GLN A 277    15075   5368   5220    622  -2134   -301       C  
ATOM   2066  CG  GLN A 277     -44.834 -40.797 -27.986  1.00 69.70           C  
ANISOU 2066  CG  GLN A 277    15844   5273   5367    438  -2590   -281       C  
ATOM   2067  CD  GLN A 277     -45.219 -42.229 -28.300  1.00 78.77           C  
ANISOU 2067  CD  GLN A 277    17564   5893   6472    406  -3069   -246       C  
ATOM   2068  OE1 GLN A 277     -44.356 -43.095 -28.445  1.00 83.97           O  
ANISOU 2068  OE1 GLN A 277    18579   6425   6900    807  -2912   -351       O  
ATOM   2069  NE2 GLN A 277     -46.518 -42.486 -28.403  1.00 82.33           N  
ANISOU 2069  NE2 GLN A 277    18087   6060   7136    -70  -3687    -25       N  
ATOM   2070  N   ALA A 278     -43.054 -39.786 -23.836  1.00 52.97           N  
ANISOU 2070  N   ALA A 278    11789   4333   4003    611  -1440   -127       N  
ATOM   2071  CA  ALA A 278     -42.168 -39.914 -22.685  1.00 51.51           C  
ANISOU 2071  CA  ALA A 278    11266   4389   3915    779  -1164   -133       C  
ATOM   2072  C   ALA A 278     -42.963 -40.153 -21.406  1.00 65.71           C  
ANISOU 2072  C   ALA A 278    12742   6231   5995    547  -1305     42       C  
ATOM   2073  O   ALA A 278     -42.538 -40.927 -20.539  1.00 50.57           O  
ANISOU 2073  O   ALA A 278    10780   4322   4111    656  -1270     61       O  
ATOM   2074  CB  ALA A 278     -41.291 -38.670 -22.558  1.00 49.58           C  
ANISOU 2074  CB  ALA A 278    10622   4510   3707    888   -799   -158       C  
ATOM   2075  N   GLN A 279     -44.125 -39.506 -21.278  1.00 62.20           N  
ANISOU 2075  N   GLN A 279    12059   5828   5745    267  -1438    216       N  
ATOM   2076  CA  GLN A 279     -44.980 -39.739 -20.118  1.00 61.45           C  
ANISOU 2076  CA  GLN A 279    11651   5799   5899    110  -1518    474       C  
ATOM   2077  C   GLN A 279     -45.492 -41.175 -20.088  1.00 64.19           C  
ANISOU 2077  C   GLN A 279    12258   5818   6315    -18  -1877    629       C  
ATOM   2078  O   GLN A 279     -45.493 -41.816 -19.032  1.00 59.20           O  
ANISOU 2078  O   GLN A 279    11468   5230   5795      8  -1856    770       O  
ATOM   2079  CB  GLN A 279     -46.146 -38.749 -20.120  1.00 59.57           C  
ANISOU 2079  CB  GLN A 279    11107   5678   5850    -94  -1546    700       C  
ATOM   2080  CG  GLN A 279     -45.734 -37.297 -19.894  1.00 59.32           C  
ANISOU 2080  CG  GLN A 279    10824   5934   5782     28  -1220    575       C  
ATOM   2081  CD  GLN A 279     -46.777 -36.304 -20.384  1.00 59.16           C  
ANISOU 2081  CD  GLN A 279    10647   5950   5883   -125  -1262    744       C  
ATOM   2082  OE1 GLN A 279     -47.884 -36.684 -20.768  1.00 57.89           O  
ANISOU 2082  OE1 GLN A 279    10473   5648   5876   -339  -1531   1017       O  
ATOM   2083  NE2 GLN A 279     -46.423 -35.025 -20.379  1.00 60.29           N  
ANISOU 2083  NE2 GLN A 279    10663   6262   5982    -32  -1035    618       N  
ATOM   2084  N   ASP A 280     -45.925 -41.699 -21.235  1.00 67.11           N  
ANISOU 2084  N   ASP A 280    13070   5822   6607   -162  -2251    616       N  
ATOM   2085  CA  ASP A 280     -46.452 -43.058 -21.267  1.00 66.41           C  
ANISOU 2085  CA  ASP A 280    13305   5325   6601   -339  -2710    778       C  
ATOM   2086  C   ASP A 280     -45.351 -44.088 -21.046  1.00 69.71           C  
ANISOU 2086  C   ASP A 280    14087   5591   6810    -34  -2628    552       C  
ATOM   2087  O   ASP A 280     -45.572 -45.106 -20.377  1.00 68.92           O  
ANISOU 2087  O   ASP A 280    14020   5311   6855   -116  -2833    727       O  
ATOM   2088  CB  ASP A 280     -47.173 -43.315 -22.589  1.00 71.12           C  
ANISOU 2088  CB  ASP A 280    14392   5504   7127   -580  -3226    799       C  
ATOM   2089  CG  ASP A 280     -48.584 -42.762 -22.597  1.00 78.14           C  
ANISOU 2089  CG  ASP A 280    14868   6451   8370   -989  -3488   1219       C  
ATOM   2090  OD1 ASP A 280     -48.904 -41.943 -21.711  1.00 78.75           O  
ANISOU 2090  OD1 ASP A 280    14307   6944   8671   -982  -3140   1430       O  
ATOM   2091  OD2 ASP A 280     -49.373 -43.144 -23.489  1.00 82.23           O  
ANISOU 2091  OD2 ASP A 280    15616   6685   8945  -1287  -3994   1290       O  
ATOM   2092  N   ALA A 281     -44.160 -43.850 -21.600  1.00 69.94           N  
ANISOU 2092  N   ALA A 281    14363   5695   6515    338  -2316    222       N  
ATOM   2093  CA  ALA A 281     -43.069 -44.794 -21.387  1.00 68.86           C  
ANISOU 2093  CA  ALA A 281    14526   5452   6187    698  -2179     61       C  
ATOM   2094  C   ALA A 281     -42.554 -44.745 -19.955  1.00 65.97           C  
ANISOU 2094  C   ALA A 281    13625   5441   6001    786  -1877    157       C  
ATOM   2095  O   ALA A 281     -42.108 -45.768 -19.425  1.00 69.86           O  
ANISOU 2095  O   ALA A 281    14267   5799   6478    938  -1907    169       O  
ATOM   2096  CB  ALA A 281     -41.931 -44.525 -22.369  1.00 60.30           C  
ANISOU 2096  CB  ALA A 281    13775   4409   4728   1126  -1867   -209       C  
ATOM   2097  N   LEU A 282     -42.601 -43.577 -19.313  1.00 63.15           N  
ANISOU 2097  N   LEU A 282    12705   5503   5785    711  -1614    220       N  
ATOM   2098  CA  LEU A 282     -42.180 -43.502 -17.917  1.00 59.78           C  
ANISOU 2098  CA  LEU A 282    11860   5377   5477    792  -1396    306       C  
ATOM   2099  C   LEU A 282     -43.223 -44.118 -16.992  1.00 58.43           C  
ANISOU 2099  C   LEU A 282    11528   5136   5536    566  -1607    613       C  
ATOM   2100  O   LEU A 282     -42.875 -44.796 -16.020  1.00 54.13           O  
ANISOU 2100  O   LEU A 282    10899   4640   5029    672  -1559    698       O  
ATOM   2101  CB  LEU A 282     -41.899 -42.052 -17.526  1.00 55.39           C  
ANISOU 2101  CB  LEU A 282    10884   5214   4949    804  -1115    259       C  
ATOM   2102  CG  LEU A 282     -40.539 -41.496 -17.956  1.00 55.12           C  
ANISOU 2102  CG  LEU A 282    10823   5350   4770   1052   -855     69       C  
ATOM   2103  CD1 LEU A 282     -40.403 -40.034 -17.556  1.00 49.94           C  
ANISOU 2103  CD1 LEU A 282     9796   4994   4187    976   -702     56       C  
ATOM   2104  CD2 LEU A 282     -39.418 -42.327 -17.354  1.00 56.79           C  
ANISOU 2104  CD2 LEU A 282    11038   5609   4933   1318   -746     59       C  
ATOM   2105  N   ALA A 283     -44.508 -43.891 -17.279  1.00 57.30           N  
ANISOU 2105  N   ALA A 283    11302   4899   5568    261  -1835    843       N  
ATOM   2106  CA  ALA A 283     -45.566 -44.452 -16.446  1.00 59.36           C  
ANISOU 2106  CA  ALA A 283    11323   5128   6102     45  -2014   1264       C  
ATOM   2107  C   ALA A 283     -45.579 -45.973 -16.504  1.00 68.20           C  
ANISOU 2107  C   ALA A 283    12801   5835   7276    -29  -2370   1363       C  
ATOM   2108  O   ALA A 283     -46.042 -46.625 -15.561  1.00 71.78           O  
ANISOU 2108  O   ALA A 283    13041   6298   7936   -120  -2444   1707       O  
ATOM   2109  CB  ALA A 283     -46.923 -43.891 -16.869  1.00 59.15           C  
ANISOU 2109  CB  ALA A 283    11087   5090   6299   -264  -2201   1576       C  
ATOM   2110  N   SER A 284     -45.082 -46.554 -17.595  1.00 70.15           N  
ANISOU 2110  N   SER A 284    13634   5701   7320     40  -2591   1084       N  
ATOM   2111  CA  SER A 284     -44.846 -47.990 -17.641  1.00 74.48           C  
ANISOU 2111  CA  SER A 284    14653   5807   7837     76  -2902   1087       C  
ATOM   2112  C   SER A 284     -43.563 -48.305 -16.882  1.00 81.52           C  
ANISOU 2112  C   SER A 284    15505   6898   8572    481  -2525    905       C  
ATOM   2113  O   SER A 284     -43.291 -47.701 -15.839  1.00 87.50           O  
ANISOU 2113  O   SER A 284    15751   8103   9392    572  -2176    977       O  
ATOM   2114  CB  SER A 284     -44.768 -48.484 -19.088  1.00 71.61           C  
ANISOU 2114  CB  SER A 284    15038   4942   7229     92  -3260    825       C  
ATOM   2115  OG  SER A 284     -43.665 -47.916 -19.772  1.00 65.30           O  
ANISOU 2115  OG  SER A 284    14470   4278   6063    502  -2887    440       O  
ATOM   2116  N   GLY A 285     -42.759 -49.232 -17.389  1.00 85.62           N  
ANISOU 2116  N   GLY A 285    16589   7076   8865    756  -2603    682       N  
ATOM   2117  CA  GLY A 285     -41.523 -49.561 -16.710  1.00 87.99           C  
ANISOU 2117  CA  GLY A 285    16813   7572   9046   1156  -2254    570       C  
ATOM   2118  C   GLY A 285     -40.287 -49.010 -17.391  1.00 92.46           C  
ANISOU 2118  C   GLY A 285    17488   8326   9316   1578  -1867    263       C  
ATOM   2119  O   GLY A 285     -39.180 -49.106 -16.853  1.00100.44           O  
ANISOU 2119  O   GLY A 285    18322   9575  10264   1910  -1550    226       O  
ATOM   2120  N   ASP A 286     -40.466 -48.410 -18.565  1.00 88.88           N  
ANISOU 2120  N   ASP A 286    17281   7790   8698   1565  -1891    104       N  
ATOM   2121  CA  ASP A 286     -39.335 -48.098 -19.428  1.00 84.94           C  
ANISOU 2121  CA  ASP A 286    16999   7386   7889   2015  -1544   -118       C  
ATOM   2122  C   ASP A 286     -38.522 -46.932 -18.878  1.00 78.30           C  
ANISOU 2122  C   ASP A 286    15479   7134   7137   2106  -1100    -88       C  
ATOM   2123  O   ASP A 286     -39.060 -45.853 -18.612  1.00 82.40           O  
ANISOU 2123  O   ASP A 286    15573   7918   7819   1803  -1084    -36       O  
ATOM   2124  CB  ASP A 286     -39.825 -47.779 -20.839  1.00 85.35           C  
ANISOU 2124  CB  ASP A 286    17538   7177   7714   1972  -1715   -266       C  
ATOM   2125  CG  ASP A 286     -38.742 -47.954 -21.883  1.00 90.59           C  
ANISOU 2125  CG  ASP A 286    18699   7764   7958   2552  -1414   -457       C  
ATOM   2126  OD1 ASP A 286     -37.552 -47.981 -21.508  1.00 91.12           O  
ANISOU 2126  OD1 ASP A 286    18512   8124   7986   2956   -983   -421       O  
ATOM   2127  OD2 ASP A 286     -39.081 -48.064 -23.081  1.00 99.02           O  
ANISOU 2127  OD2 ASP A 286    20355   8536   8732   2607  -1602   -581       O  
ATOM   2128  N   ILE A 287     -37.218 -47.157 -18.710  1.00 72.08           N  
ANISOU 2128  N   ILE A 287    14608   6527   6254   2531   -770    -90       N  
ATOM   2129  CA  ILE A 287     -36.264 -46.103 -18.381  1.00 67.50           C  
ANISOU 2129  CA  ILE A 287    13442   6446   5759   2630   -416    -20       C  
ATOM   2130  C   ILE A 287     -35.025 -46.280 -19.251  1.00 71.17           C  
ANISOU 2130  C   ILE A 287    14076   6966   5998   3170    -59     -9       C  
ATOM   2131  O   ILE A 287     -33.902 -45.982 -18.827  1.00 74.18           O  
ANISOU 2131  O   ILE A 287    14004   7701   6480   3382    222    159       O  
ATOM   2132  CB  ILE A 287     -35.890 -46.109 -16.887  1.00 63.22           C  
ANISOU 2132  CB  ILE A 287    12401   6180   5441   2546   -399    124       C  
ATOM   2133  CG1 ILE A 287     -35.345 -47.477 -16.473  1.00 62.97           C  
ANISOU 2133  CG1 ILE A 287    12601   5965   5361   2853   -403    186       C  
ATOM   2134  CG2 ILE A 287     -37.082 -45.715 -16.033  1.00 59.03           C  
ANISOU 2134  CG2 ILE A 287    11661   5679   5088   2101   -640    166       C  
ATOM   2135  CD1 ILE A 287     -34.693 -47.477 -15.109  1.00 62.97           C  
ANISOU 2135  CD1 ILE A 287    12117   6275   5534   2861   -348    349       C  
ATOM   2136  N   SER A 288     -35.223 -46.765 -20.473  1.00 74.29           N  
ANISOU 2136  N   SER A 288    15135   7012   6078   3415    -79   -145       N  
ATOM   2137  CA  SER A 288     -34.118 -47.012 -21.386  1.00 79.08           C  
ANISOU 2137  CA  SER A 288    16006   7651   6388   4046    323   -105       C  
ATOM   2138  C   SER A 288     -33.484 -45.694 -21.835  1.00 78.77           C  
ANISOU 2138  C   SER A 288    15448   8070   6411   4085    676     46       C  
ATOM   2139  O   SER A 288     -33.915 -44.598 -21.464  1.00 77.47           O  
ANISOU 2139  O   SER A 288    14796   8138   6500   3615    565     67       O  
ATOM   2140  CB  SER A 288     -34.598 -47.815 -22.590  1.00 81.00           C  
ANISOU 2140  CB  SER A 288    17230   7348   6196   4314    161   -322       C  
ATOM   2141  OG  SER A 288     -35.608 -47.109 -23.291  1.00 80.77           O  
ANISOU 2141  OG  SER A 288    17368   7203   6119   3931    -95   -450       O  
ATOM   2142  N   ARG A 289     -32.442 -45.814 -22.658  1.00 85.16           N  
ANISOU 2142  N   ARG A 289    16383   8996   6980   4691   1119    192       N  
ATOM   2143  CA  ARG A 289     -31.731 -44.633 -23.134  1.00 90.55           C  
ANISOU 2143  CA  ARG A 289    16532  10120   7751   4765   1480    441       C  
ATOM   2144  C   ARG A 289     -32.610 -43.790 -24.050  1.00 88.11           C  
ANISOU 2144  C   ARG A 289    16454   9715   7309   4487   1351    277       C  
ATOM   2145  O   ARG A 289     -32.530 -42.556 -24.033  1.00 88.69           O  
ANISOU 2145  O   ARG A 289    15968  10108   7621   4188   1412    416       O  
ATOM   2146  CB  ARG A 289     -30.449 -45.058 -23.849  1.00105.08           C  
ANISOU 2146  CB  ARG A 289    18458  12120   9349   5559   2042    726       C  
ATOM   2147  CG  ARG A 289     -29.369 -43.994 -23.899  1.00112.35           C  
ANISOU 2147  CG  ARG A 289    18531  13607  10550   5633   2433   1193       C  
ATOM   2148  CD  ARG A 289     -27.999 -44.636 -24.062  1.00123.82           C  
ANISOU 2148  CD  ARG A 289    19826  15289  11929   6394   2967   1614       C  
ATOM   2149  NE  ARG A 289     -26.917 -43.658 -24.018  1.00129.63           N  
ANISOU 2149  NE  ARG A 289    19628  16586  13039   6409   3288   2186       N  
ATOM   2150  CZ  ARG A 289     -26.399 -43.166 -22.897  1.00130.32           C  
ANISOU 2150  CZ  ARG A 289    18880  16978  13656   5989   3093   2460       C  
ATOM   2151  NH1 ARG A 289     -26.867 -43.556 -21.719  1.00126.01           N  
ANISOU 2151  NH1 ARG A 289    18336  16264  13279   5578   2644   2192       N  
ATOM   2152  NH2 ARG A 289     -25.414 -42.281 -22.954  1.00134.61           N  
ANISOU 2152  NH2 ARG A 289    18602  17982  14561   5974   3315   3036       N  
ATOM   2153  N   SER A 290     -33.463 -44.437 -24.847  1.00 86.23           N  
ANISOU 2153  N   SER A 290    17060   9004   6699   4561   1116     -6       N  
ATOM   2154  CA  SER A 290     -34.351 -43.703 -25.745  1.00 88.22           C  
ANISOU 2154  CA  SER A 290    17570   9138   6812   4292    939   -148       C  
ATOM   2155  C   SER A 290     -35.320 -42.827 -24.960  1.00 83.08           C  
ANISOU 2155  C   SER A 290    16401   8587   6577   3549    579   -192       C  
ATOM   2156  O   SER A 290     -35.447 -41.622 -25.221  1.00 84.93           O  
ANISOU 2156  O   SER A 290    16256   9068   6946   3309    650   -114       O  
ATOM   2157  CB  SER A 290     -35.116 -44.685 -26.632  1.00 93.50           C  
ANISOU 2157  CB  SER A 290    19061   9248   7215   4334    557   -313       C  
ATOM   2158  OG  SER A 290     -34.337 -45.836 -26.913  1.00101.55           O  
ANISOU 2158  OG  SER A 290    20478  10115   7992   4889    719   -220       O  
ATOM   2159  N   THR A 291     -36.012 -43.424 -23.986  1.00 79.68           N  
ANISOU 2159  N   THR A 291    15961   7966   6346   3217    213   -283       N  
ATOM   2160  CA  THR A 291     -36.990 -42.676 -23.205  1.00 77.48           C  
ANISOU 2160  CA  THR A 291    15245   7779   6414   2613    -76   -285       C  
ATOM   2161  C   THR A 291     -36.334 -41.526 -22.455  1.00 72.01           C  
ANISOU 2161  C   THR A 291    13779   7558   6024   2479    153   -122       C  
ATOM   2162  O   THR A 291     -36.859 -40.408 -22.445  1.00 71.20           O  
ANISOU 2162  O   THR A 291    13390   7587   6075   2147     83   -114       O  
ATOM   2163  CB  THR A 291     -37.714 -43.610 -22.236  1.00 77.44           C  
ANISOU 2163  CB  THR A 291    15330   7534   6561   2375   -428   -315       C  
ATOM   2164  OG1 THR A 291     -36.781 -44.129 -21.280  1.00 84.47           O  
ANISOU 2164  OG1 THR A 291    15949   8592   7554   2595   -245   -220       O  
ATOM   2165  CG2 THR A 291     -38.348 -44.763 -22.996  1.00 72.02           C  
ANISOU 2165  CG2 THR A 291    15455   6301   5608   2452   -765   -448       C  
ATOM   2166  N   LEU A 292     -35.177 -41.774 -21.836  1.00 72.42           N  
ANISOU 2166  N   LEU A 292    13511   7838   6167   2734    387     29       N  
ATOM   2167  CA  LEU A 292     -34.488 -40.704 -21.121  1.00 70.71           C  
ANISOU 2167  CA  LEU A 292    12607   8010   6248   2570    495    211       C  
ATOM   2168  C   LEU A 292     -34.010 -39.609 -22.067  1.00 71.06           C  
ANISOU 2168  C   LEU A 292    12447   8262   6292   2622    729    355       C  
ATOM   2169  O   LEU A 292     -33.996 -38.432 -21.688  1.00 70.89           O  
ANISOU 2169  O   LEU A 292    11988   8430   6516   2299    655    434       O  
ATOM   2170  CB  LEU A 292     -33.316 -41.269 -20.319  1.00 71.67           C  
ANISOU 2170  CB  LEU A 292    12426   8319   6487   2822    638    405       C  
ATOM   2171  CG  LEU A 292     -33.697 -42.210 -19.174  1.00 70.38           C  
ANISOU 2171  CG  LEU A 292    12354   8009   6377   2733    404    314       C  
ATOM   2172  CD1 LEU A 292     -32.507 -42.461 -18.258  1.00 72.78           C  
ANISOU 2172  CD1 LEU A 292    12235   8565   6854   2901    501    545       C  
ATOM   2173  CD2 LEU A 292     -34.880 -41.661 -18.388  1.00 64.41           C  
ANISOU 2173  CD2 LEU A 292    11516   7202   5755   2251     90    181       C  
ATOM   2174  N   ASP A 293     -33.621 -39.965 -23.293  1.00 71.36           N  
ANISOU 2174  N   ASP A 293    12835   8245   6032   3047   1008    406       N  
ATOM   2175  CA  ASP A 293     -33.271 -38.942 -24.274  1.00 76.96           C  
ANISOU 2175  CA  ASP A 293    13379   9149   6713   3111   1250    582       C  
ATOM   2176  C   ASP A 293     -34.475 -38.063 -24.593  1.00 71.58           C  
ANISOU 2176  C   ASP A 293    12805   8338   6054   2669    981    393       C  
ATOM   2177  O   ASP A 293     -34.366 -36.830 -24.634  1.00 71.56           O  
ANISOU 2177  O   ASP A 293    12386   8535   6268   2421   1002    528       O  
ATOM   2178  CB  ASP A 293     -32.720 -39.591 -25.545  1.00 84.73           C  
ANISOU 2178  CB  ASP A 293    14842  10078   7274   3746   1632    668       C  
ATOM   2179  CG  ASP A 293     -31.315 -40.137 -25.361  1.00 94.06           C  
ANISOU 2179  CG  ASP A 293    15740  11513   8487   4264   2036   1012       C  
ATOM   2180  OD1 ASP A 293     -30.590 -39.630 -24.479  1.00 96.47           O  
ANISOU 2180  OD1 ASP A 293    15316  12128   9209   4067   2042   1289       O  
ATOM   2181  OD2 ASP A 293     -30.935 -41.074 -26.098  1.00 98.32           O  
ANISOU 2181  OD2 ASP A 293    16812  11923   8624   4889   2329   1024       O  
ATOM   2182  N   ALA A 294     -35.639 -38.683 -24.812  1.00 68.26           N  
ANISOU 2182  N   ALA A 294    12929   7566   5440   2552    694    119       N  
ATOM   2183  CA  ALA A 294     -36.848 -37.900 -25.055  1.00 63.21           C  
ANISOU 2183  CA  ALA A 294    12339   6815   4862   2134    422      0       C  
ATOM   2184  C   ALA A 294     -37.180 -37.005 -23.863  1.00 65.30           C  
ANISOU 2184  C   ALA A 294    12060   7242   5509   1709    263     27       C  
ATOM   2185  O   ALA A 294     -37.566 -35.840 -24.037  1.00 65.51           O  
ANISOU 2185  O   ALA A 294    11876   7350   5664   1461    223     57       O  
ATOM   2186  CB  ALA A 294     -38.018 -38.830 -25.375  1.00 57.36           C  
ANISOU 2186  CB  ALA A 294    12210   5663   3923   2042     67   -205       C  
ATOM   2187  N   VAL A 295     -37.029 -37.531 -22.644  1.00 60.77           N  
ANISOU 2187  N   VAL A 295    11311   6695   5085   1661    172     16       N  
ATOM   2188  CA  VAL A 295     -37.280 -36.733 -21.445  1.00 58.75           C  
ANISOU 2188  CA  VAL A 295    10651   6569   5101   1349     29     28       C  
ATOM   2189  C   VAL A 295     -36.346 -35.532 -21.400  1.00 58.49           C  
ANISOU 2189  C   VAL A 295    10191   6785   5249   1295    148    187       C  
ATOM   2190  O   VAL A 295     -36.761 -34.414 -21.066  1.00 61.40           O  
ANISOU 2190  O   VAL A 295    10385   7181   5765   1025     20    170       O  
ATOM   2191  CB  VAL A 295     -37.141 -37.606 -20.183  1.00 60.99           C  
ANISOU 2191  CB  VAL A 295    10875   6849   5450   1379    -67     15       C  
ATOM   2192  CG1 VAL A 295     -37.222 -36.748 -18.931  1.00 59.28           C  
ANISOU 2192  CG1 VAL A 295    10326   6771   5428   1150   -194     28       C  
ATOM   2193  CG2 VAL A 295     -38.210 -38.686 -20.160  1.00 57.83           C  
ANISOU 2193  CG2 VAL A 295    10851   6173   4948   1340   -256    -78       C  
ATOM   2194  N   ARG A 296     -35.071 -35.738 -21.743  1.00 59.05           N  
ANISOU 2194  N   ARG A 296    10088   7025   5325   1561    384    390       N  
ATOM   2195  CA  ARG A 296     -34.122 -34.630 -21.742  1.00 62.41           C  
ANISOU 2195  CA  ARG A 296    10042   7680   5992   1466    448    649       C  
ATOM   2196  C   ARG A 296     -34.484 -33.593 -22.799  1.00 62.52           C  
ANISOU 2196  C   ARG A 296    10076   7689   5990   1355    514    693       C  
ATOM   2197  O   ARG A 296     -34.311 -32.387 -22.578  1.00 62.55           O  
ANISOU 2197  O   ARG A 296     9774   7758   6233   1082    391    805       O  
ATOM   2198  CB  ARG A 296     -32.701 -35.154 -21.947  1.00 64.85           C  
ANISOU 2198  CB  ARG A 296    10087   8207   6346   1814    725    976       C  
ATOM   2199  CG  ARG A 296     -32.147 -35.872 -20.720  1.00 65.29           C  
ANISOU 2199  CG  ARG A 296     9969   8317   6521   1849    604   1013       C  
ATOM   2200  CD  ARG A 296     -30.680 -36.244 -20.870  1.00 71.95           C  
ANISOU 2200  CD  ARG A 296    10429   9421   7487   2181    873   1436       C  
ATOM   2201  NE  ARG A 296     -30.060 -36.503 -19.572  1.00 78.89           N  
ANISOU 2201  NE  ARG A 296    10994  10390   8589   2076    649   1546       N  
ATOM   2202  CZ  ARG A 296     -30.047 -37.688 -18.968  1.00 84.08           C  
ANISOU 2202  CZ  ARG A 296    11837  10980   9128   2288    651   1440       C  
ATOM   2203  NH1 ARG A 296     -30.619 -38.737 -19.544  1.00 84.62           N  
ANISOU 2203  NH1 ARG A 296    12426  10852   8873   2599    834   1218       N  
ATOM   2204  NH2 ARG A 296     -29.461 -37.825 -17.786  1.00 86.19           N  
ANISOU 2204  NH2 ARG A 296    11806  11344   9598   2174    421   1566       N  
ATOM   2205  N   LYS A 297     -35.001 -34.038 -23.949  1.00 65.45           N  
ANISOU 2205  N   LYS A 297    10857   7944   6067   1558    663    604       N  
ATOM   2206  CA  LYS A 297     -35.504 -33.084 -24.934  1.00 65.48           C  
ANISOU 2206  CA  LYS A 297    10930   7924   6026   1439    690    626       C  
ATOM   2207  C   LYS A 297     -36.671 -32.279 -24.371  1.00 66.34           C  
ANISOU 2207  C   LYS A 297    11035   7893   6276   1033    378    438       C  
ATOM   2208  O   LYS A 297     -36.778 -31.070 -24.617  1.00 68.71           O  
ANISOU 2208  O   LYS A 297    11153   8228   6724    831    339    523       O  
ATOM   2209  CB  LYS A 297     -35.922 -33.807 -26.215  1.00 64.15           C  
ANISOU 2209  CB  LYS A 297    11314   7608   5453   1739    828    535       C  
ATOM   2210  CG  LYS A 297     -34.791 -34.523 -26.930  1.00 70.31           C  
ANISOU 2210  CG  LYS A 297    12198   8517   6000   2272   1222    742       C  
ATOM   2211  CD  LYS A 297     -35.206 -34.929 -28.335  1.00 73.67           C  
ANISOU 2211  CD  LYS A 297    13268   8771   5954   2588   1341    651       C  
ATOM   2212  CE  LYS A 297     -34.208 -35.895 -28.951  1.00 83.23           C  
ANISOU 2212  CE  LYS A 297    14766  10039   6818   3249   1748    799       C  
ATOM   2213  NZ  LYS A 297     -32.815 -35.371 -28.918  1.00 86.26           N  
ANISOU 2213  NZ  LYS A 297    14501  10841   7433   3477   2174   1282       N  
ATOM   2214  N   CYS A 298     -37.554 -32.930 -23.609  1.00 66.50           N  
ANISOU 2214  N   CYS A 298    11248   7758   6261    942    174    227       N  
ATOM   2215  CA  CYS A 298     -38.663 -32.205 -22.995  1.00 65.12           C  
ANISOU 2215  CA  CYS A 298    11044   7490   6210    651    -49    119       C  
ATOM   2216  C   CYS A 298     -38.160 -31.186 -21.979  1.00 65.79           C  
ANISOU 2216  C   CYS A 298    10802   7667   6530    489   -142    166       C  
ATOM   2217  O   CYS A 298     -38.721 -30.090 -21.857  1.00 71.24           O  
ANISOU 2217  O   CYS A 298    11456   8298   7315    308   -248    142       O  
ATOM   2218  CB  CYS A 298     -39.633 -33.187 -22.342  1.00 64.88           C  
ANISOU 2218  CB  CYS A 298    11217   7315   6117    627   -207     -4       C  
ATOM   2219  SG  CYS A 298     -40.488 -34.252 -23.523  1.00 65.81           S  
ANISOU 2219  SG  CYS A 298    11814   7199   5993    695   -297    -56       S  
ATOM   2220  N   ILE A 299     -37.100 -31.527 -21.242  1.00 59.54           N  
ANISOU 2220  N   ILE A 299     9812   6986   5824    560   -141    243       N  
ATOM   2221  CA  ILE A 299     -36.495 -30.564 -20.326  1.00 58.49           C  
ANISOU 2221  CA  ILE A 299     9430   6889   5904    378   -330    308       C  
ATOM   2222  C   ILE A 299     -35.931 -29.379 -21.101  1.00 67.39           C  
ANISOU 2222  C   ILE A 299    10340   8060   7205    241   -317    513       C  
ATOM   2223  O   ILE A 299     -36.079 -28.220 -20.689  1.00 72.63           O  
ANISOU 2223  O   ILE A 299    10974   8615   8008     15   -542    495       O  
ATOM   2224  CB  ILE A 299     -35.417 -31.251 -19.468  1.00 57.77           C  
ANISOU 2224  CB  ILE A 299     9150   6913   5886    465   -379    408       C  
ATOM   2225  CG1 ILE A 299     -36.046 -32.344 -18.598  1.00 55.56           C  
ANISOU 2225  CG1 ILE A 299     9093   6573   5446    578   -416    220       C  
ATOM   2226  CG2 ILE A 299     -34.686 -30.234 -18.606  1.00 59.74           C  
ANISOU 2226  CG2 ILE A 299     9178   7159   6363    233   -681    512       C  
ATOM   2227  CD1 ILE A 299     -35.040 -33.125 -17.773  1.00 54.23           C  
ANISOU 2227  CD1 ILE A 299     8764   6515   5328    690   -458    321       C  
ATOM   2228  N   SER A 300     -35.285 -29.650 -22.241  1.00 67.88           N  
ANISOU 2228  N   SER A 300    10285   8264   7243    408    -48    733       N  
ATOM   2229  CA  SER A 300     -34.762 -28.567 -23.070  1.00 65.19           C  
ANISOU 2229  CA  SER A 300     9700   7994   7075    298     12   1010       C  
ATOM   2230  C   SER A 300     -35.879 -27.658 -23.564  1.00 68.09           C  
ANISOU 2230  C   SER A 300    10282   8197   7394    135    -64    861       C  
ATOM   2231  O   SER A 300     -35.710 -26.434 -23.624  1.00 72.40           O  
ANISOU 2231  O   SER A 300    10669   8686   8153    -95   -210    993       O  
ATOM   2232  CB  SER A 300     -33.976 -29.135 -24.251  1.00 64.21           C  
ANISOU 2232  CB  SER A 300     9473   8079   6846    623    407   1300       C  
ATOM   2233  OG  SER A 300     -32.669 -29.516 -23.860  1.00 68.27           O  
ANISOU 2233  OG  SER A 300     9599   8797   7544    740    485   1622       O  
ATOM   2234  N   GLU A 301     -37.026 -28.235 -23.931  1.00 63.43           N  
ANISOU 2234  N   GLU A 301    10044   7507   6549    236     -3    625       N  
ATOM   2235  CA  GLU A 301     -38.160 -27.408 -24.331  1.00 61.75           C  
ANISOU 2235  CA  GLU A 301     9996   7150   6314     89    -90    525       C  
ATOM   2236  C   GLU A 301     -38.669 -26.576 -23.160  1.00 64.62           C  
ANISOU 2236  C   GLU A 301    10365   7368   6820   -101   -349    390       C  
ATOM   2237  O   GLU A 301     -39.019 -25.399 -23.327  1.00 73.56           O  
ANISOU 2237  O   GLU A 301    11500   8391   8059   -247   -446    417       O  
ATOM   2238  CB  GLU A 301     -39.275 -28.285 -24.905  1.00 61.88           C  
ANISOU 2238  CB  GLU A 301    10354   7084   6075    202    -49    371       C  
ATOM   2239  CG  GLU A 301     -40.605 -27.572 -25.126  1.00 66.63           C  
ANISOU 2239  CG  GLU A 301    11080   7548   6687     52   -174    307       C  
ATOM   2240  CD  GLU A 301     -40.588 -26.594 -26.296  1.00 67.84           C  
ANISOU 2240  CD  GLU A 301    11210   7711   6855     -6   -102    455       C  
ATOM   2241  OE1 GLU A 301     -39.530 -26.425 -26.941  1.00 67.35           O  
ANISOU 2241  OE1 GLU A 301    11016   7777   6797     73     66    637       O  
ATOM   2242  OE2 GLU A 301     -41.646 -25.994 -26.576  1.00 67.40           O  
ANISOU 2242  OE2 GLU A 301    11242   7551   6815   -112   -197    439       O  
ATOM   2243  N   GLY A 302     -38.701 -27.165 -21.963  1.00 60.02           N  
ANISOU 2243  N   GLY A 302     9831   6767   6208    -58   -455    252       N  
ATOM   2244  CA  GLY A 302     -39.117 -26.412 -20.790  1.00 55.22           C  
ANISOU 2244  CA  GLY A 302     9323   6011   5645   -142   -675    121       C  
ATOM   2245  C   GLY A 302     -38.224 -25.218 -20.514  1.00 57.52           C  
ANISOU 2245  C   GLY A 302     9499   6211   6145   -336   -908    222       C  
ATOM   2246  O   GLY A 302     -38.709 -24.123 -20.216  1.00 59.15           O  
ANISOU 2246  O   GLY A 302     9876   6217   6382   -420  -1076    146       O  
ATOM   2247  N   ARG A 303     -36.905 -25.407 -20.614  1.00 58.33           N  
ANISOU 2247  N   ARG A 303     9313   6439   6412   -406   -945    435       N  
ATOM   2248  CA  ARG A 303     -35.989 -24.294 -20.383  1.00 58.68           C  
ANISOU 2248  CA  ARG A 303     9190   6375   6731   -667  -1254    626       C  
ATOM   2249  C   ARG A 303     -36.057 -23.270 -21.510  1.00 58.58           C  
ANISOU 2249  C   ARG A 303     9076   6317   6866   -804  -1199    817       C  
ATOM   2250  O   ARG A 303     -35.915 -22.064 -21.262  1.00 58.83           O  
ANISOU 2250  O   ARG A 303     9158   6114   7080  -1039  -1518    868       O  
ATOM   2251  CB  ARG A 303     -34.564 -24.819 -20.206  1.00 62.83           C  
ANISOU 2251  CB  ARG A 303     9329   7090   7455   -710  -1306    922       C  
ATOM   2252  CG  ARG A 303     -34.422 -25.780 -19.034  1.00 65.94           C  
ANISOU 2252  CG  ARG A 303     9819   7517   7718   -590  -1403    756       C  
ATOM   2253  CD  ARG A 303     -33.009 -26.319 -18.885  1.00 73.81           C  
ANISOU 2253  CD  ARG A 303    10389   8719   8936   -611  -1446   1102       C  
ATOM   2254  NE  ARG A 303     -32.926 -27.275 -17.783  1.00 78.40           N  
ANISOU 2254  NE  ARG A 303    11082   9332   9375   -482  -1534    941       N  
ATOM   2255  CZ  ARG A 303     -31.835 -27.965 -17.463  1.00 83.53           C  
ANISOU 2255  CZ  ARG A 303    11403  10165  10170   -438  -1562   1202       C  
ATOM   2256  NH1 ARG A 303     -30.718 -27.810 -18.161  1.00 87.98           N  
ANISOU 2256  NH1 ARG A 303    11464  10923  11042   -491  -1482   1684       N  
ATOM   2257  NH2 ARG A 303     -31.862 -28.812 -16.443  1.00 82.56           N  
ANISOU 2257  NH2 ARG A 303    11425  10052   9893   -316  -1650   1037       N  
ATOM   2258  N   ARG A 304     -36.277 -23.730 -22.745  1.00 58.46           N  
ANISOU 2258  N   ARG A 304     8976   6486   6750   -650   -828    922       N  
ATOM   2259  CA  ARG A 304     -36.454 -22.808 -23.862  1.00 60.90           C  
ANISOU 2259  CA  ARG A 304     9226   6767   7147   -743   -743   1104       C  
ATOM   2260  C   ARG A 304     -37.650 -21.896 -23.631  1.00 63.82           C  
ANISOU 2260  C   ARG A 304     9919   6867   7462   -819   -904    864       C  
ATOM   2261  O   ARG A 304     -37.568 -20.683 -23.854  1.00 66.40           O  
ANISOU 2261  O   ARG A 304    10228   7021   7979  -1015  -1080    990       O  
ATOM   2262  CB  ARG A 304     -36.624 -23.585 -25.168  1.00 61.36           C  
ANISOU 2262  CB  ARG A 304     9283   7043   6989   -496   -333   1196       C  
ATOM   2263  CG  ARG A 304     -36.579 -22.717 -26.415  1.00 64.91           C  
ANISOU 2263  CG  ARG A 304     9630   7525   7508   -552   -202   1466       C  
ATOM   2264  CD  ARG A 304     -37.166 -23.436 -27.623  1.00 66.96           C  
ANISOU 2264  CD  ARG A 304    10117   7900   7423   -282    120   1426       C  
ATOM   2265  NE  ARG A 304     -38.609 -23.238 -27.730  1.00 65.11           N  
ANISOU 2265  NE  ARG A 304    10214   7485   7042   -326     12   1150       N  
ATOM   2266  CZ  ARG A 304     -39.178 -22.259 -28.428  1.00 65.89           C  
ANISOU 2266  CZ  ARG A 304    10361   7495   7180   -433    -16   1230       C  
ATOM   2267  NH1 ARG A 304     -38.425 -21.386 -29.087  1.00 64.86           N  
ANISOU 2267  NH1 ARG A 304     9990   7427   7225   -522     52   1566       N  
ATOM   2268  NH2 ARG A 304     -40.500 -22.151 -28.471  1.00 63.67           N  
ANISOU 2268  NH2 ARG A 304    10327   7072   6791   -451   -113   1034       N  
ATOM   2269  N   VAL A 305     -38.773 -22.463 -23.183  1.00 65.44           N  
ANISOU 2269  N   VAL A 305    10407   7030   7429   -649   -840    570       N  
ATOM   2270  CA  VAL A 305     -39.928 -21.633 -22.858  1.00 58.76           C  
ANISOU 2270  CA  VAL A 305     9838   5958   6530   -639   -940    403       C  
ATOM   2271  C   VAL A 305     -39.640 -20.762 -21.640  1.00 60.19           C  
ANISOU 2271  C   VAL A 305    10208   5871   6789   -728  -1286    292       C  
ATOM   2272  O   VAL A 305     -40.121 -19.624 -21.553  1.00 62.64           O  
ANISOU 2272  O   VAL A 305    10738   5925   7136   -764  -1433    248       O  
ATOM   2273  CB  VAL A 305     -41.174 -22.513 -22.649  1.00 55.84           C  
ANISOU 2273  CB  VAL A 305     9635   5649   5932   -425   -773    236       C  
ATOM   2274  CG1 VAL A 305     -42.370 -21.668 -22.239  1.00 56.28           C  
ANISOU 2274  CG1 VAL A 305     9922   5517   5946   -337   -814    148       C  
ATOM   2275  CG2 VAL A 305     -41.485 -23.295 -23.919  1.00 52.20           C  
ANISOU 2275  CG2 VAL A 305     9103   5356   5375   -378   -555    335       C  
ATOM   2276  N   ALA A 306     -38.844 -21.265 -20.691  1.00 60.71           N  
ANISOU 2276  N   ALA A 306    10249   5959   6861   -749  -1455    245       N  
ATOM   2277  CA  ALA A 306     -38.502 -20.470 -19.515  1.00 65.56           C  
ANISOU 2277  CA  ALA A 306    11140   6270   7499   -839  -1875    127       C  
ATOM   2278  C   ALA A 306     -37.747 -19.203 -19.902  1.00 65.71           C  
ANISOU 2278  C   ALA A 306    11087   6058   7822  -1163  -2211    338       C  
ATOM   2279  O   ALA A 306     -37.957 -18.139 -19.307  1.00 60.97           O  
ANISOU 2279  O   ALA A 306    10882   5074   7207  -1218  -2556    208       O  
ATOM   2280  CB  ALA A 306     -37.677 -21.305 -18.535  1.00 55.84           C  
ANISOU 2280  CB  ALA A 306     9853   5129   6236   -839  -2033     94       C  
ATOM   2281  N   ALA A 307     -36.866 -19.295 -20.901  1.00 65.18           N  
ANISOU 2281  N   ALA A 307    10542   6201   8022  -1353  -2115    698       N  
ATOM   2282  CA  ALA A 307     -36.120 -18.116 -21.326  1.00 68.63           C  
ANISOU 2282  CA  ALA A 307    10820   6445   8813  -1695  -2431   1009       C  
ATOM   2283  C   ALA A 307     -37.014 -17.052 -21.955  1.00 66.73           C  
ANISOU 2283  C   ALA A 307    10814   5978   8561  -1695  -2396    960       C  
ATOM   2284  O   ALA A 307     -36.594 -15.895 -22.064  1.00 67.46           O  
ANISOU 2284  O   ALA A 307    10934   5777   8922  -1980  -2758   1146       O  
ATOM   2285  CB  ALA A 307     -35.015 -18.516 -22.304  1.00 71.97           C  
ANISOU 2285  CB  ALA A 307    10619   7217   9511  -1814  -2225   1501       C  
ATOM   2286  N   LEU A 308     -38.234 -17.411 -22.360  1.00 67.16           N  
ANISOU 2286  N   LEU A 308    11030   6146   8341  -1404  -2010    754       N  
ATOM   2287  CA  LEU A 308     -39.168 -16.480 -22.981  1.00 68.47           C  
ANISOU 2287  CA  LEU A 308    11389   6136   8491  -1362  -1942    736       C  
ATOM   2288  C   LEU A 308     -40.383 -16.202 -22.102  1.00 70.19           C  
ANISOU 2288  C   LEU A 308    12116   6115   8439  -1079  -1961    387       C  
ATOM   2289  O   LEU A 308     -41.410 -15.732 -22.603  1.00 75.47           O  
ANISOU 2289  O   LEU A 308    12910   6728   9039   -933  -1785    371       O  
ATOM   2290  CB  LEU A 308     -39.621 -17.013 -24.342  1.00 64.87           C  
ANISOU 2290  CB  LEU A 308    10671   6009   7968  -1259  -1500    890       C  
ATOM   2291  CG  LEU A 308     -38.537 -17.211 -25.401  1.00 66.82           C  
ANISOU 2291  CG  LEU A 308    10466   6518   8405  -1411  -1360   1288       C  
ATOM   2292  CD1 LEU A 308     -39.116 -17.875 -26.643  1.00 62.86           C  
ANISOU 2292  CD1 LEU A 308     9894   6299   7691  -1213   -940   1349       C  
ATOM   2293  CD2 LEU A 308     -37.887 -15.883 -25.750  1.00 70.53           C  
ANISOU 2293  CD2 LEU A 308    10805   6769   9224  -1721  -1633   1609       C  
ATOM   2294  N   ALA A 309     -40.291 -16.481 -20.805  1.00 69.74           N  
ANISOU 2294  N   ALA A 309    12348   5934   8216   -961  -2149    152       N  
ATOM   2295  CA  ALA A 309     -41.435 -16.314 -19.922  1.00 68.27           C  
ANISOU 2295  CA  ALA A 309    12644   5576   7720   -585  -2075   -124       C  
ATOM   2296  C   ALA A 309     -41.758 -14.836 -19.722  1.00 68.34           C  
ANISOU 2296  C   ALA A 309    13125   5108   7733   -550  -2345   -196       C  
ATOM   2297  O   ALA A 309     -40.893 -13.964 -19.834  1.00 65.99           O  
ANISOU 2297  O   ALA A 309    12888   4512   7673   -879  -2769    -98       O  
ATOM   2298  CB  ALA A 309     -41.171 -16.983 -18.573  1.00 67.78           C  
ANISOU 2298  CB  ALA A 309    12818   5505   7433   -431  -2203   -335       C  
ATOM   2299  N   ALA A 310     -43.030 -14.563 -19.418  1.00 69.12           N  
ANISOU 2299  N   ALA A 310    13557   5123   7581   -132  -2103   -323       N  
ATOM   2300  CA  ALA A 310     -43.471 -13.185 -19.234  1.00 70.10           C  
ANISOU 2300  CA  ALA A 310    14205   4777   7654     15  -2293   -401       C  
ATOM   2301  C   ALA A 310     -42.925 -12.577 -17.948  1.00 73.51           C  
ANISOU 2301  C   ALA A 310    15318   4720   7894     79  -2790   -662       C  
ATOM   2302  O   ALA A 310     -42.630 -11.377 -17.910  1.00 76.74           O  
ANISOU 2302  O   ALA A 310    16132   4643   8385    -48  -3207   -694       O  
ATOM   2303  CB  ALA A 310     -44.998 -13.117 -19.244  1.00 67.89           C  
ANISOU 2303  CB  ALA A 310    14054   4585   7155    523  -1839   -395       C  
ATOM   2304  N   THR A 311     -42.790 -13.375 -16.890  1.00 75.23           N  
ANISOU 2304  N   THR A 311    15704   5038   7840    272  -2791   -839       N  
ATOM   2305  CA  THR A 311     -42.278 -12.900 -15.613  1.00 80.42           C  
ANISOU 2305  CA  THR A 311    16957   5357   8244    363  -3252  -1053       C  
ATOM   2306  C   THR A 311     -41.175 -13.828 -15.122  1.00 81.67           C  
ANISOU 2306  C   THR A 311    16893   5662   8475     63  -3520  -1061       C  
ATOM   2307  O   THR A 311     -41.076 -14.987 -15.533  1.00 78.99           O  
ANISOU 2307  O   THR A 311    16007   5757   8249    -28  -3204   -954       O  
ATOM   2308  CB  THR A 311     -43.382 -12.806 -14.546  1.00 78.12           C  
ANISOU 2308  CB  THR A 311    17178   5078   7424   1060  -2939  -1213       C  
ATOM   2309  OG1 THR A 311     -43.941 -14.105 -14.312  1.00 74.02           O  
ANISOU 2309  OG1 THR A 311    16452   4928   6746   1339  -2469  -1224       O  
ATOM   2310  CG2 THR A 311     -44.483 -11.854 -14.993  1.00 79.23           C  
ANISOU 2310  CG2 THR A 311    17531   5080   7492   1401  -2664  -1166       C  
ATOM   2311  N   ASP A 312     -40.340 -13.296 -14.226  1.00 84.49           N  
ANISOU 2311  N   ASP A 312    17546   5783   8771    -63  -4065  -1094       N  
ATOM   2312  CA  ASP A 312     -39.263 -14.088 -13.644  1.00 86.83           C  
ANISOU 2312  CA  ASP A 312    17659   6187   9144   -327  -4376  -1063       C  
ATOM   2313  C   ASP A 312     -39.784 -15.201 -12.744  1.00 85.45           C  
ANISOU 2313  C   ASP A 312    17605   6289   8575    112  -4012  -1232       C  
ATOM   2314  O   ASP A 312     -39.042 -16.148 -12.458  1.00 84.29           O  
ANISOU 2314  O   ASP A 312    17192   6334   8500    -78  -4122  -1202       O  
ATOM   2315  CB  ASP A 312     -38.313 -13.185 -12.858  1.00 98.36           C  
ANISOU 2315  CB  ASP A 312    19463   7274  10636   -544  -5092  -1010       C  
ATOM   2316  CG  ASP A 312     -37.490 -12.282 -13.755  1.00107.50           C  
ANISOU 2316  CG  ASP A 312    20324   8224  12299  -1105  -5531   -726       C  
ATOM   2317  OD1 ASP A 312     -36.276 -12.535 -13.902  1.00111.45           O  
ANISOU 2317  OD1 ASP A 312    20393   8761  13190  -1603  -5930   -458       O  
ATOM   2318  OD2 ASP A 312     -38.058 -11.323 -14.319  1.00111.78           O  
ANISOU 2318  OD2 ASP A 312    21021   8585  12865  -1039  -5464   -721       O  
ATOM   2319  N   GLU A 313     -41.036 -15.110 -12.294  1.00 86.67           N  
ANISOU 2319  N   GLU A 313    18118   6484   8329    702  -3573  -1354       N  
ATOM   2320  CA  GLU A 313     -41.592 -16.155 -11.443  1.00 85.91           C  
ANISOU 2320  CA  GLU A 313    18081   6675   7887   1135  -3188  -1425       C  
ATOM   2321  C   GLU A 313     -41.830 -17.436 -12.232  1.00 81.19           C  
ANISOU 2321  C   GLU A 313    16919   6488   7441   1039  -2764  -1366       C  
ATOM   2322  O   GLU A 313     -41.418 -18.522 -11.808  1.00 82.77           O  
ANISOU 2322  O   GLU A 313    16920   6938   7592   1000  -2736  -1371       O  
ATOM   2323  CB  GLU A 313     -42.884 -15.664 -10.791  1.00 95.73           C  
ANISOU 2323  CB  GLU A 313    19809   7867   8697   1808  -2813  -1462       C  
ATOM   2324  CG  GLU A 313     -42.695 -14.411  -9.957  1.00111.65           C  
ANISOU 2324  CG  GLU A 313    22505   9450  10466   1971  -3241  -1537       C  
ATOM   2325  CD  GLU A 313     -43.852 -14.151  -9.014  1.00120.55           C  
ANISOU 2325  CD  GLU A 313    24167  10569  11066   2726  -2860  -1543       C  
ATOM   2326  OE1 GLU A 313     -44.996 -14.520  -9.354  1.00119.64           O  
ANISOU 2326  OE1 GLU A 313    23851  10737  10871   3100  -2241  -1434       O  
ATOM   2327  OE2 GLU A 313     -43.612 -13.584  -7.926  1.00126.69           O  
ANISOU 2327  OE2 GLU A 313    25578  11050  11510   2961  -3188  -1615       O  
ATOM   2328  N   THR A 314     -42.491 -17.331 -13.388  1.00 79.53           N  
ANISOU 2328  N   THR A 314    16343   6424   7450    997  -2414  -1221       N  
ATOM   2329  CA  THR A 314     -42.678 -18.509 -14.229  1.00 76.99           C  
ANISOU 2329  CA  THR A 314    15276   6614   7361    857  -2001   -999       C  
ATOM   2330  C   THR A 314     -41.358 -18.991 -14.814  1.00 73.31           C  
ANISOU 2330  C   THR A 314    14321   6288   7247    335  -2254   -883       C  
ATOM   2331  O   THR A 314     -41.194 -20.190 -15.065  1.00 72.48           O  
ANISOU 2331  O   THR A 314    13773   6549   7218    277  -2022   -777       O  
ATOM   2332  CB  THR A 314     -43.680 -18.212 -15.345  1.00 75.65           C  
ANISOU 2332  CB  THR A 314    14832   6566   7347    916  -1631   -822       C  
ATOM   2333  OG1 THR A 314     -43.280 -17.028 -16.045  1.00 84.37           O  
ANISOU 2333  OG1 THR A 314    16020   7367   8670    645  -1914   -804       O  
ATOM   2334  CG2 THR A 314     -45.073 -18.010 -14.766  1.00 72.37           C  
ANISOU 2334  CG2 THR A 314    14733   6144   6621   1496  -1261   -811       C  
ATOM   2335  N   ARG A 315     -40.411 -18.079 -15.035  1.00 74.38           N  
ANISOU 2335  N   ARG A 315    14527   6124   7608    -27  -2727   -854       N  
ATOM   2336  CA  ARG A 315     -39.080 -18.472 -15.485  1.00 73.09           C  
ANISOU 2336  CA  ARG A 315    13865   6107   7799   -480  -2964   -645       C  
ATOM   2337  C   ARG A 315     -38.396 -19.355 -14.447  1.00 70.75           C  
ANISOU 2337  C   ARG A 315    13596   5909   7376   -463  -3147   -713       C  
ATOM   2338  O   ARG A 315     -37.987 -20.486 -14.740  1.00 68.62           O  
ANISOU 2338  O   ARG A 315    12838   6015   7219   -519  -2918   -570       O  
ATOM   2339  CB  ARG A 315     -38.252 -17.219 -15.773  1.00 78.42           C  
ANISOU 2339  CB  ARG A 315    14622   6400   8772   -879  -3500   -522       C  
ATOM   2340  CG  ARG A 315     -36.863 -17.463 -16.332  1.00 86.11           C  
ANISOU 2340  CG  ARG A 315    14986   7543  10188  -1345  -3726   -162       C  
ATOM   2341  CD  ARG A 315     -36.250 -16.138 -16.762  1.00100.54           C  
ANISOU 2341  CD  ARG A 315    16837   8995  12367  -1751  -4216     55       C  
ATOM   2342  NE  ARG A 315     -35.022 -16.298 -17.534  1.00109.77           N  
ANISOU 2342  NE  ARG A 315    17287  10398  14022  -2165  -4311    546       N  
ATOM   2343  CZ  ARG A 315     -34.455 -15.320 -18.234  1.00117.17           C  
ANISOU 2343  CZ  ARG A 315    18002  11152  15367  -2546  -4597    900       C  
ATOM   2344  NH1 ARG A 315     -35.012 -14.116 -18.264  1.00119.62           N  
ANISOU 2344  NH1 ARG A 315    18801  10999  15648  -2585  -4854    763       N  
ATOM   2345  NH2 ARG A 315     -33.336 -15.544 -18.910  1.00121.10           N  
ANISOU 2345  NH2 ARG A 315    17777  11930  16303  -2857  -4603   1436       N  
ATOM   2346  N   ALA A 316     -38.279 -18.852 -13.215  1.00 68.42           N  
ANISOU 2346  N   ALA A 316    13935   5253   6810   -350  -3574   -937       N  
ATOM   2347  CA  ALA A 316     -37.626 -19.616 -12.157  1.00 75.11           C  
ANISOU 2347  CA  ALA A 316    14873   6162   7506   -332  -3810  -1000       C  
ATOM   2348  C   ALA A 316     -38.401 -20.880 -11.808  1.00 72.19           C  
ANISOU 2348  C   ALA A 316    14391   6178   6860     69  -3255  -1062       C  
ATOM   2349  O   ALA A 316     -37.808 -21.862 -11.350  1.00 77.18           O  
ANISOU 2349  O   ALA A 316    14807   7025   7491     32  -3287  -1010       O  
ATOM   2350  CB  ALA A 316     -37.447 -18.741 -10.916  1.00 78.49           C  
ANISOU 2350  CB  ALA A 316    16043   6123   7658   -224  -4342  -1191       C  
ATOM   2351  N   LYS A 317     -39.721 -20.876 -12.013  1.00 72.09           N  
ANISOU 2351  N   LYS A 317    14492   6252   6648    442  -2765  -1121       N  
ATOM   2352  CA  LYS A 317     -40.519 -22.067 -11.736  1.00 71.99           C  
ANISOU 2352  CA  LYS A 317    14313   6595   6446    774  -2268  -1086       C  
ATOM   2353  C   LYS A 317     -40.279 -23.144 -12.788  1.00 67.41           C  
ANISOU 2353  C   LYS A 317    13029   6393   6188    539  -1991   -872       C  
ATOM   2354  O   LYS A 317     -40.074 -24.319 -12.456  1.00 62.87           O  
ANISOU 2354  O   LYS A 317    12248   6060   5579    588  -1868   -823       O  
ATOM   2355  CB  LYS A 317     -42.001 -21.695 -11.665  1.00 78.51           C  
ANISOU 2355  CB  LYS A 317    15400   7404   7025   1224  -1858  -1101       C  
ATOM   2356  CG  LYS A 317     -42.914 -22.830 -11.232  1.00 82.59           C  
ANISOU 2356  CG  LYS A 317    15760   8257   7364   1575  -1389   -978       C  
ATOM   2357  CD  LYS A 317     -44.317 -22.319 -10.938  1.00 88.86           C  
ANISOU 2357  CD  LYS A 317    16838   9023   7903   2085  -1013   -909       C  
ATOM   2358  CE  LYS A 317     -45.183 -23.403 -10.317  1.00 91.27           C  
ANISOU 2358  CE  LYS A 317    16984   9654   8041   2447   -585   -695       C  
ATOM   2359  NZ  LYS A 317     -44.602 -23.928  -9.051  1.00 93.65           N  
ANISOU 2359  NZ  LYS A 317    17608   9951   8024   2618   -735   -823       N  
ATOM   2360  N   LEU A 318     -40.303 -22.758 -14.067  1.00 66.27           N  
ANISOU 2360  N   LEU A 318    12572   6282   6327    315  -1895   -744       N  
ATOM   2361  CA  LEU A 318     -39.999 -23.707 -15.134  1.00 63.10           C  
ANISOU 2361  CA  LEU A 318    11627   6184   6163    140  -1661   -560       C  
ATOM   2362  C   LEU A 318     -38.590 -24.267 -14.984  1.00 61.66           C  
ANISOU 2362  C   LEU A 318    11184   6100   6143    -79  -1886   -467       C  
ATOM   2363  O   LEU A 318     -38.369 -25.471 -15.164  1.00 59.02           O  
ANISOU 2363  O   LEU A 318    10576   6018   5829    -34  -1682   -385       O  
ATOM   2364  CB  LEU A 318     -40.170 -23.037 -16.497  1.00 62.41           C  
ANISOU 2364  CB  LEU A 318    11337   6080   6294    -35  -1564   -433       C  
ATOM   2365  CG  LEU A 318     -41.606 -22.837 -16.984  1.00 62.42           C  
ANISOU 2365  CG  LEU A 318    11412   6097   6206    161  -1261   -423       C  
ATOM   2366  CD1 LEU A 318     -41.656 -21.852 -18.145  1.00 61.17           C  
ANISOU 2366  CD1 LEU A 318    11160   5840   6241    -22  -1276   -319       C  
ATOM   2367  CD2 LEU A 318     -42.206 -24.174 -17.389  1.00 59.94           C  
ANISOU 2367  CD2 LEU A 318    10853   6059   5864    250   -955   -329       C  
ATOM   2368  N   LEU A 319     -37.625 -23.408 -14.644  1.00 64.45           N  
ANISOU 2368  N   LEU A 319    11622   6236   6632   -317  -2338   -440       N  
ATOM   2369  CA  LEU A 319     -36.267 -23.891 -14.413  1.00 67.69           C  
ANISOU 2369  CA  LEU A 319    11726   6752   7243   -530  -2591   -263       C  
ATOM   2370  C   LEU A 319     -36.206 -24.817 -13.203  1.00 69.91           C  
ANISOU 2370  C   LEU A 319    12179   7107   7277   -333  -2641   -390       C  
ATOM   2371  O   LEU A 319     -35.445 -25.794 -13.200  1.00 70.01           O  
ANISOU 2371  O   LEU A 319    11843   7353   7406   -365  -2589   -233       O  
ATOM   2372  CB  LEU A 319     -35.314 -22.709 -14.244  1.00 69.78           C  
ANISOU 2372  CB  LEU A 319    12042   6721   7750   -885  -3168   -142       C  
ATOM   2373  CG  LEU A 319     -35.140 -21.837 -15.489  1.00 69.84           C  
ANISOU 2373  CG  LEU A 319    11773   6686   8078  -1130  -3138     89       C  
ATOM   2374  CD1 LEU A 319     -34.260 -20.634 -15.193  1.00 74.22           C  
ANISOU 2374  CD1 LEU A 319    12421   6880   8901  -1523  -3802    243       C  
ATOM   2375  CD2 LEU A 319     -34.566 -22.656 -16.636  1.00 68.11           C  
ANISOU 2375  CD2 LEU A 319    10912   6868   8097  -1161  -2742    420       C  
ATOM   2376  N   ALA A 320     -37.006 -24.535 -12.171  1.00 68.81           N  
ANISOU 2376  N   ALA A 320    12589   6781   6777    -77  -2707   -644       N  
ATOM   2377  CA  ALA A 320     -37.046 -25.412 -11.004  1.00 69.12           C  
ANISOU 2377  CA  ALA A 320    12821   6906   6535    158  -2710   -741       C  
ATOM   2378  C   ALA A 320     -37.555 -26.798 -11.380  1.00 62.38           C  
ANISOU 2378  C   ALA A 320    11628   6398   5676    336  -2206   -652       C  
ATOM   2379  O   ALA A 320     -36.975 -27.816 -10.982  1.00 64.25           O  
ANISOU 2379  O   ALA A 320    11683   6804   5925    353  -2211   -577       O  
ATOM   2380  CB  ALA A 320     -37.917 -24.794  -9.910  1.00 72.66           C  
ANISOU 2380  CB  ALA A 320    13966   7105   6536    499  -2781   -990       C  
ATOM   2381  N   ALA A 321     -38.644 -26.856 -12.152  1.00 58.21           N  
ANISOU 2381  N   ALA A 321    11030   5946   5143    455  -1814   -638       N  
ATOM   2382  CA  ALA A 321     -39.155 -28.146 -12.605  1.00 58.27           C  
ANISOU 2382  CA  ALA A 321    10760   6203   5176    560  -1438   -533       C  
ATOM   2383  C   ALA A 321     -38.135 -28.862 -13.481  1.00 63.39           C  
ANISOU 2383  C   ALA A 321    10996   7007   6082    369  -1414   -386       C  
ATOM   2384  O   ALA A 321     -37.984 -30.088 -13.399  1.00 67.56           O  
ANISOU 2384  O   ALA A 321    11385   7688   6597    459  -1275   -324       O  
ATOM   2385  CB  ALA A 321     -40.472 -27.956 -13.356  1.00 51.86           C  
ANISOU 2385  CB  ALA A 321     9941   5403   4359    653  -1133   -493       C  
ATOM   2386  N   ALA A 322     -37.414 -28.110 -14.317  1.00 64.15           N  
ANISOU 2386  N   ALA A 322    10907   7061   6407    143  -1530   -294       N  
ATOM   2387  CA  ALA A 322     -36.409 -28.716 -15.183  1.00 65.78           C  
ANISOU 2387  CA  ALA A 322    10718   7444   6831     52  -1434    -85       C  
ATOM   2388  C   ALA A 322     -35.296 -29.365 -14.369  1.00 69.53           C  
ANISOU 2388  C   ALA A 322    11043   8013   7360     49  -1621     17       C  
ATOM   2389  O   ALA A 322     -34.939 -30.527 -14.598  1.00 72.62           O  
ANISOU 2389  O   ALA A 322    11249   8580   7765    184  -1414    116       O  
ATOM   2390  CB  ALA A 322     -35.839 -27.667 -16.137  1.00 68.21           C  
ANISOU 2390  CB  ALA A 322    10824   7710   7384   -172  -1514     82       C  
ATOM   2391  N   ASP A 323     -34.735 -28.627 -13.406  1.00 75.47           N  
ANISOU 2391  N   ASP A 323    11918   8621   8137    -97  -2051     -1       N  
ATOM   2392  CA  ASP A 323     -33.648 -29.180 -12.603  1.00 78.27           C  
ANISOU 2392  CA  ASP A 323    12115   9058   8567   -136  -2305    138       C  
ATOM   2393  C   ASP A 323     -34.126 -30.311 -11.701  1.00 74.63           C  
ANISOU 2393  C   ASP A 323    11850   8676   7830    130  -2171     -6       C  
ATOM   2394  O   ASP A 323     -33.365 -31.251 -11.433  1.00 73.12           O  
ANISOU 2394  O   ASP A 323    11429   8644   7711    188  -2167    146       O  
ATOM   2395  CB  ASP A 323     -32.988 -28.077 -11.776  1.00 90.04           C  
ANISOU 2395  CB  ASP A 323    13773  10307  10131   -399  -2914    153       C  
ATOM   2396  CG  ASP A 323     -31.989 -27.268 -12.581  1.00 97.37           C  
ANISOU 2396  CG  ASP A 323    14289  11222  11484   -736  -3133    493       C  
ATOM   2397  OD1 ASP A 323     -31.379 -27.837 -13.513  1.00 97.43           O  
ANISOU 2397  OD1 ASP A 323    13780  11503  11735   -711  -2821    805       O  
ATOM   2398  OD2 ASP A 323     -31.813 -26.068 -12.282  1.00100.30           O  
ANISOU 2398  OD2 ASP A 323    14876  11296  11937  -1000  -3616    479       O  
ATOM   2399  N   GLU A 324     -35.370 -30.241 -11.222  1.00 71.18           N  
ANISOU 2399  N   GLU A 324    11807   8143   7096    314  -2043   -239       N  
ATOM   2400  CA  GLU A 324     -35.929 -31.360 -10.470  1.00 70.97           C  
ANISOU 2400  CA  GLU A 324    11909   8216   6840    571  -1858   -292       C  
ATOM   2401  C   GLU A 324     -35.993 -32.612 -11.335  1.00 69.01           C  
ANISOU 2401  C   GLU A 324    11369   8141   6710    649  -1504   -170       C  
ATOM   2402  O   GLU A 324     -35.612 -33.707 -10.898  1.00 68.05           O  
ANISOU 2402  O   GLU A 324    11164   8125   6568    762  -1465    -94       O  
ATOM   2403  CB  GLU A 324     -37.317 -31.000  -9.941  1.00 77.24           C  
ANISOU 2403  CB  GLU A 324    13094   8915   7338    785  -1712   -449       C  
ATOM   2404  CG  GLU A 324     -37.967 -32.103  -9.119  1.00 84.28           C  
ANISOU 2404  CG  GLU A 324    14081   9925   8015   1052  -1507   -414       C  
ATOM   2405  CD  GLU A 324     -39.343 -31.720  -8.606  1.00 89.09           C  
ANISOU 2405  CD  GLU A 324    15001  10493   8358   1318  -1298   -450       C  
ATOM   2406  OE1 GLU A 324     -40.124 -31.123  -9.376  1.00 87.07           O  
ANISOU 2406  OE1 GLU A 324    14720  10187   8174   1298  -1133   -445       O  
ATOM   2407  OE2 GLU A 324     -39.639 -32.011  -7.427  1.00 94.77           O  
ANISOU 2407  OE2 GLU A 324    15978  11245   8787   1582  -1278   -442       O  
ATOM   2408  N   LEU A 325     -36.463 -32.463 -12.578  1.00 66.25           N  
ANISOU 2408  N   LEU A 325    10921   7789   6463    603  -1275   -153       N  
ATOM   2409  CA  LEU A 325     -36.535 -33.610 -13.479  1.00 66.43           C  
ANISOU 2409  CA  LEU A 325    10806   7897   6538    697  -1001    -69       C  
ATOM   2410  C   LEU A 325     -35.147 -34.154 -13.796  1.00 68.20           C  
ANISOU 2410  C   LEU A 325    10747   8247   6919    724   -996    108       C  
ATOM   2411  O   LEU A 325     -34.957 -35.374 -13.874  1.00 69.47           O  
ANISOU 2411  O   LEU A 325    10886   8462   7047    898   -849    165       O  
ATOM   2412  CB  LEU A 325     -37.275 -33.226 -14.759  1.00 65.82           C  
ANISOU 2412  CB  LEU A 325    10751   7762   6495    640   -825    -88       C  
ATOM   2413  CG  LEU A 325     -38.775 -33.522 -14.742  1.00 66.45           C  
ANISOU 2413  CG  LEU A 325    11022   7768   6457    694   -714   -141       C  
ATOM   2414  CD1 LEU A 325     -39.501 -32.710 -15.801  1.00 69.80           C  
ANISOU 2414  CD1 LEU A 325    11472   8121   6926    591   -646   -151       C  
ATOM   2415  CD2 LEU A 325     -39.013 -35.011 -14.951  1.00 66.65           C  
ANISOU 2415  CD2 LEU A 325    11083   7789   6454    796   -614    -80       C  
ATOM   2416  N   ASP A 326     -34.163 -33.269 -13.977  1.00 69.67           N  
ANISOU 2416  N   ASP A 326    10701   8473   7297    566  -1161    247       N  
ATOM   2417  CA  ASP A 326     -32.795 -33.730 -14.193  1.00 73.36           C  
ANISOU 2417  CA  ASP A 326    10804   9109   7961    618  -1142    531       C  
ATOM   2418  C   ASP A 326     -32.283 -34.523 -12.996  1.00 69.84           C  
ANISOU 2418  C   ASP A 326    10337   8720   7479    703  -1309    573       C  
ATOM   2419  O   ASP A 326     -31.614 -35.551 -13.161  1.00 69.07           O  
ANISOU 2419  O   ASP A 326    10056   8754   7433    907  -1137    748       O  
ATOM   2420  CB  ASP A 326     -31.877 -32.543 -14.483  1.00 82.40           C  
ANISOU 2420  CB  ASP A 326    11639  10283   9386    370  -1360    772       C  
ATOM   2421  CG  ASP A 326     -31.539 -32.414 -15.955  1.00 90.18           C  
ANISOU 2421  CG  ASP A 326    12376  11386  10501    441  -1030    996       C  
ATOM   2422  OD1 ASP A 326     -31.406 -33.458 -16.629  1.00 93.19           O  
ANISOU 2422  OD1 ASP A 326    12737  11881  10789    748   -664   1066       O  
ATOM   2423  OD2 ASP A 326     -31.405 -31.269 -16.437  1.00 94.11           O  
ANISOU 2423  OD2 ASP A 326    12748  11842  11166    219  -1140   1110       O  
ATOM   2424  N   GLN A 327     -32.592 -34.063 -11.780  1.00 68.86           N  
ANISOU 2424  N   GLN A 327    10446   8488   7229    595  -1636    419       N  
ATOM   2425  CA  GLN A 327     -32.181 -34.800 -10.589  1.00 71.15           C  
ANISOU 2425  CA  GLN A 327    10772   8827   7434    687  -1815    451       C  
ATOM   2426  C   GLN A 327     -32.825 -36.182 -10.547  1.00 70.74           C  
ANISOU 2426  C   GLN A 327    10848   8812   7217    954  -1497    384       C  
ATOM   2427  O   GLN A 327     -32.153 -37.183 -10.260  1.00 71.21           O  
ANISOU 2427  O   GLN A 327    10760   8974   7322   1102  -1461    535       O  
ATOM   2428  CB  GLN A 327     -32.530 -34.003  -9.332  1.00 71.11           C  
ANISOU 2428  CB  GLN A 327    11133   8665   7221    587  -2205    266       C  
ATOM   2429  CG  GLN A 327     -32.024 -34.625  -8.043  1.00 77.26           C  
ANISOU 2429  CG  GLN A 327    11992   9487   7877    668  -2461    313       C  
ATOM   2430  CD  GLN A 327     -30.510 -34.628  -7.948  1.00 83.34           C  
ANISOU 2430  CD  GLN A 327    12350  10359   8956    502  -2783    634       C  
ATOM   2431  OE1 GLN A 327     -29.832 -33.835  -8.605  1.00 84.02           O  
ANISOU 2431  OE1 GLN A 327    12144  10441   9339    268  -2937    826       O  
ATOM   2432  NE2 GLN A 327     -29.970 -35.525  -7.129  1.00 85.01           N  
ANISOU 2432  NE2 GLN A 327    12494  10674   9129    620  -2891    757       N  
ATOM   2433  N   ILE A 328     -34.127 -36.257 -10.840  1.00 68.25           N  
ANISOU 2433  N   ILE A 328    10793   8399   6742   1008  -1294    204       N  
ATOM   2434  CA  ILE A 328     -34.799 -37.554 -10.894  1.00 67.36           C  
ANISOU 2434  CA  ILE A 328    10797   8268   6530   1193  -1064    195       C  
ATOM   2435  C   ILE A 328     -34.142 -38.452 -11.936  1.00 71.91           C  
ANISOU 2435  C   ILE A 328    11223   8876   7225   1331   -854    318       C  
ATOM   2436  O   ILE A 328     -34.007 -39.666 -11.735  1.00 79.65           O  
ANISOU 2436  O   ILE A 328    12250   9843   8169   1513   -774    380       O  
ATOM   2437  CB  ILE A 328     -36.303 -37.369 -11.171  1.00 64.66           C  
ANISOU 2437  CB  ILE A 328    10679   7814   6076   1169   -933     80       C  
ATOM   2438  CG1 ILE A 328     -36.977 -36.652  -9.999  1.00 66.30           C  
ANISOU 2438  CG1 ILE A 328    11084   8008   6098   1180  -1052      4       C  
ATOM   2439  CG2 ILE A 328     -36.974 -38.710 -11.420  1.00 64.36           C  
ANISOU 2439  CG2 ILE A 328    10734   7706   6014   1279   -778    139       C  
ATOM   2440  CD1 ILE A 328     -38.483 -36.565 -10.124  1.00 66.40           C  
ANISOU 2440  CD1 ILE A 328    11236   7964   6028   1219   -877      7       C  
ATOM   2441  N   LEU A 329     -33.711 -37.871 -13.059  1.00 72.23           N  
ANISOU 2441  N   LEU A 329    11118   8945   7380   1291   -748    374       N  
ATOM   2442  CA  LEU A 329     -33.047 -38.665 -14.089  1.00 73.69           C  
ANISOU 2442  CA  LEU A 329    11227   9167   7603   1528   -491    510       C  
ATOM   2443  C   LEU A 329     -31.719 -39.219 -13.590  1.00 78.41           C  
ANISOU 2443  C   LEU A 329    11533   9931   8327   1694   -503    763       C  
ATOM   2444  O   LEU A 329     -31.397 -40.390 -13.830  1.00 79.18           O  
ANISOU 2444  O   LEU A 329    11704  10012   8369   1994   -313    838       O  
ATOM   2445  CB  LEU A 329     -32.841 -37.826 -15.350  1.00 67.28           C  
ANISOU 2445  CB  LEU A 329    10310   8392   6861   1489   -342    573       C  
ATOM   2446  CG  LEU A 329     -33.858 -38.056 -16.470  1.00 64.08           C  
ANISOU 2446  CG  LEU A 329    10249   7813   6286   1544   -174    408       C  
ATOM   2447  CD1 LEU A 329     -35.280 -37.896 -15.957  1.00 60.53           C  
ANISOU 2447  CD1 LEU A 329    10038   7207   5753   1338   -339    200       C  
ATOM   2448  CD2 LEU A 329     -33.595 -37.113 -17.634  1.00 64.23           C  
ANISOU 2448  CD2 LEU A 329    10152   7896   6355   1510    -35    496       C  
ATOM   2449  N   LYS A 330     -30.933 -38.393 -12.895  1.00 82.96           N  
ANISOU 2449  N   LYS A 330    11799  10640   9080   1503   -765    918       N  
ATOM   2450  CA  LYS A 330     -29.680 -38.878 -12.325  1.00 88.03           C  
ANISOU 2450  CA  LYS A 330    12104  11454   9888   1617   -848   1224       C  
ATOM   2451  C   LYS A 330     -29.930 -40.005 -11.331  1.00 84.63           C  
ANISOU 2451  C   LYS A 330    11877  10971   9306   1766   -904   1136       C  
ATOM   2452  O   LYS A 330     -29.195 -41.001 -11.311  1.00 87.39           O  
ANISOU 2452  O   LYS A 330    12090  11404   9708   2042   -764   1341       O  
ATOM   2453  CB  LYS A 330     -28.929 -37.725 -11.660  1.00 98.45           C  
ANISOU 2453  CB  LYS A 330    13117  12857  11433   1290  -1270   1406       C  
ATOM   2454  CG  LYS A 330     -28.605 -36.582 -12.608  1.00107.64           C  
ANISOU 2454  CG  LYS A 330    14029  14064  12807   1106  -1253   1571       C  
ATOM   2455  CD  LYS A 330     -28.493 -35.259 -11.869  1.00115.54           C  
ANISOU 2455  CD  LYS A 330    15013  14961  13926    682  -1791   1555       C  
ATOM   2456  CE  LYS A 330     -28.430 -34.089 -12.840  1.00119.77           C  
ANISOU 2456  CE  LYS A 330    15381  15474  14651    472  -1779   1672       C  
ATOM   2457  NZ  LYS A 330     -28.483 -32.775 -12.141  1.00122.49           N  
ANISOU 2457  NZ  LYS A 330    15860  15613  15067     63  -2346   1589       N  
ATOM   2458  N   GLU A 331     -30.974 -39.872 -10.507  1.00 79.24           N  
ANISOU 2458  N   GLU A 331    11519  10158   8431   1626  -1074    872       N  
ATOM   2459  CA  GLU A 331     -31.308 -40.931  -9.558  1.00 73.86           C  
ANISOU 2459  CA  GLU A 331    11026   9434   7602   1765  -1106    834       C  
ATOM   2460  C   GLU A 331     -31.701 -42.218 -10.276  1.00 70.50           C  
ANISOU 2460  C   GLU A 331    10786   8885   7114   2023   -803    815       C  
ATOM   2461  O   GLU A 331     -31.298 -43.315  -9.867  1.00 70.01           O  
ANISOU 2461  O   GLU A 331    10731   8822   7047   2235   -767    931       O  
ATOM   2462  CB  GLU A 331     -32.430 -40.464  -8.631  1.00 74.39           C  
ANISOU 2462  CB  GLU A 331    11396   9413   7456   1626  -1268    624       C  
ATOM   2463  CG  GLU A 331     -32.017 -39.351  -7.678  1.00 83.39           C  
ANISOU 2463  CG  GLU A 331    12531  10595   8558   1440  -1648    606       C  
ATOM   2464  CD  GLU A 331     -33.168 -38.841  -6.831  1.00 89.17           C  
ANISOU 2464  CD  GLU A 331    13649  11232   8998   1425  -1724    401       C  
ATOM   2465  OE1 GLU A 331     -34.198 -38.428  -7.404  1.00 88.17           O  
ANISOU 2465  OE1 GLU A 331    13661  11022   8817   1397  -1538    272       O  
ATOM   2466  OE2 GLU A 331     -33.045 -38.859  -5.588  1.00 94.11           O  
ANISOU 2466  OE2 GLU A 331    14451  11876   9431   1480  -1957    401       O  
ATOM   2467  N   LEU A 332     -32.482 -42.106 -11.354  1.00 66.71           N  
ANISOU 2467  N   LEU A 332    10504   8262   6579   2005   -629    672       N  
ATOM   2468  CA  LEU A 332     -32.870 -43.292 -12.110  1.00 64.23           C  
ANISOU 2468  CA  LEU A 332    10481   7744   6178   2224   -442    635       C  
ATOM   2469  C   LEU A 332     -31.662 -43.964 -12.749  1.00 70.10           C  
ANISOU 2469  C   LEU A 332    11126   8545   6966   2584   -224    817       C  
ATOM   2470  O   LEU A 332     -31.565 -45.197 -12.768  1.00 70.09           O  
ANISOU 2470  O   LEU A 332    11349   8392   6891   2852   -144    848       O  
ATOM   2471  CB  LEU A 332     -33.901 -42.927 -13.176  1.00 58.86           C  
ANISOU 2471  CB  LEU A 332    10055   6888   5422   2104   -379    465       C  
ATOM   2472  CG  LEU A 332     -35.355 -42.866 -12.712  1.00 58.51           C  
ANISOU 2472  CG  LEU A 332    10195   6709   5326   1869   -522    363       C  
ATOM   2473  CD1 LEU A 332     -36.246 -42.368 -13.839  1.00 59.87           C  
ANISOU 2473  CD1 LEU A 332    10541   6739   5468   1730   -494    252       C  
ATOM   2474  CD2 LEU A 332     -35.814 -44.231 -12.222  1.00 57.74           C  
ANISOU 2474  CD2 LEU A 332    10312   6430   5198   1955   -587    428       C  
ATOM   2475  N   GLU A 333     -30.729 -43.170 -13.281  1.00 76.19           N  
ANISOU 2475  N   GLU A 333    11559   9526   7863   2621   -114    985       N  
ATOM   2476  CA  GLU A 333     -29.541 -43.754 -13.894  1.00 86.89           C  
ANISOU 2476  CA  GLU A 333    12752  10996   9268   3041    172   1259       C  
ATOM   2477  C   GLU A 333     -28.633 -44.406 -12.858  1.00 91.77           C  
ANISOU 2477  C   GLU A 333    13094  11760  10016   3185     88   1508       C  
ATOM   2478  O   GLU A 333     -28.004 -45.431 -13.147  1.00 94.71           O  
ANISOU 2478  O   GLU A 333    13524  12113  10350   3625    330   1673       O  
ATOM   2479  CB  GLU A 333     -28.788 -42.690 -14.692  1.00 90.49           C  
ANISOU 2479  CB  GLU A 333    12821  11684   9878   3029    323   1491       C  
ATOM   2480  CG  GLU A 333     -29.302 -42.537 -16.119  1.00 93.01           C  
ANISOU 2480  CG  GLU A 333    13473  11867  10001   3172    590   1352       C  
ATOM   2481  CD  GLU A 333     -28.916 -41.214 -16.753  1.00 95.94           C  
ANISOU 2481  CD  GLU A 333    13475  12444  10533   3003    653   1535       C  
ATOM   2482  OE1 GLU A 333     -28.606 -40.262 -16.007  1.00 97.75           O  
ANISOU 2482  OE1 GLU A 333    13293  12828  11022   2632    369   1659       O  
ATOM   2483  OE2 GLU A 333     -28.927 -41.127 -18.000  1.00 95.40           O  
ANISOU 2483  OE2 GLU A 333    13575  12356  10317   3244    959   1563       O  
ATOM   2484  N   GLU A 334     -28.561 -43.844 -11.648  1.00 95.24           N  
ANISOU 2484  N   GLU A 334    13291  12321  10575   2856   -263   1537       N  
ATOM   2485  CA  GLU A 334     -27.796 -44.502 -10.593  1.00100.21           C  
ANISOU 2485  CA  GLU A 334    13710  13068  11299   2967   -404   1762       C  
ATOM   2486  C   GLU A 334     -28.471 -45.793 -10.148  1.00 95.81           C  
ANISOU 2486  C   GLU A 334    13569  12281  10551   3140   -377   1600       C  
ATOM   2487  O   GLU A 334     -27.791 -46.769  -9.810  1.00102.78           O  
ANISOU 2487  O   GLU A 334    14385  13193  11474   3439   -307   1804       O  
ATOM   2488  CB  GLU A 334     -27.602 -43.559  -9.406  1.00109.28           C  
ANISOU 2488  CB  GLU A 334    14622  14350  12551   2575   -856   1804       C  
ATOM   2489  CG  GLU A 334     -26.719 -42.361  -9.708  1.00119.43           C  
ANISOU 2489  CG  GLU A 334    15440  15832  14108   2364  -1000   2070       C  
ATOM   2490  CD  GLU A 334     -26.252 -41.651  -8.454  1.00125.99           C  
ANISOU 2490  CD  GLU A 334    16083  16739  15047   2022  -1551   2179       C  
ATOM   2491  OE1 GLU A 334     -26.197 -42.299  -7.387  1.00129.08           O  
ANISOU 2491  OE1 GLU A 334    16578  17126  15340   2075  -1744   2178       O  
ATOM   2492  OE2 GLU A 334     -25.940 -40.444  -8.536  1.00131.28           O  
ANISOU 2492  OE2 GLU A 334    16548  17445  15890   1699  -1829   2272       O  
ATOM   2493  N   LEU A 335     -29.806 -45.819 -10.137  1.00 88.20           N  
ANISOU 2493  N   LEU A 335    13008  11089   9415   2951   -441   1291       N  
ATOM   2494  CA  LEU A 335     -30.518 -47.062  -9.850  1.00 84.85           C  
ANISOU 2494  CA  LEU A 335    12966  10410   8864   3073   -438   1205       C  
ATOM   2495  C   LEU A 335     -30.220 -48.117 -10.908  1.00 88.50           C  
ANISOU 2495  C   LEU A 335    13712  10655   9261   3482   -174   1229       C  
ATOM   2496  O   LEU A 335     -29.921 -49.273 -10.586  1.00 91.14           O  
ANISOU 2496  O   LEU A 335    14192  10864   9574   3753   -145   1331       O  
ATOM   2497  CB  LEU A 335     -32.022 -46.803  -9.770  1.00 77.28           C  
ANISOU 2497  CB  LEU A 335    12297   9269   7796   2774   -554    977       C  
ATOM   2498  CG  LEU A 335     -32.597 -46.359  -8.428  1.00 70.12           C  
ANISOU 2498  CG  LEU A 335    11324   8477   6843   2534   -773    972       C  
ATOM   2499  CD1 LEU A 335     -34.091 -46.105  -8.559  1.00 65.34           C  
ANISOU 2499  CD1 LEU A 335    10945   7719   6162   2317   -793    842       C  
ATOM   2500  CD2 LEU A 335     -32.314 -47.405  -7.361  1.00 61.16           C  
ANISOU 2500  CD2 LEU A 335    10199   7348   5690   2684   -854   1137       C  
ATOM   2501  N   GLN A 336     -30.303 -47.731 -12.183  1.00 92.73           N  
ANISOU 2501  N   GLN A 336    14390  11117   9725   3565     16   1133       N  
ATOM   2502  CA  GLN A 336     -30.064 -48.673 -13.270  1.00 94.78           C  
ANISOU 2502  CA  GLN A 336    15068  11123   9822   4022    267   1118       C  
ATOM   2503  C   GLN A 336     -28.625 -49.169 -13.277  1.00 94.17           C  
ANISOU 2503  C   GLN A 336    14727  11244   9811   4522    540   1442       C  
ATOM   2504  O   GLN A 336     -28.370 -50.324 -13.639  1.00 94.47           O  
ANISOU 2504  O   GLN A 336    15158  11036   9701   4983    701   1465       O  
ATOM   2505  CB  GLN A 336     -30.416 -48.019 -14.606  1.00103.61           C  
ANISOU 2505  CB  GLN A 336    16399  12164  10806   4024    414    968       C  
ATOM   2506  CG  GLN A 336     -30.375 -48.954 -15.801  1.00116.05           C  
ANISOU 2506  CG  GLN A 336    18604  13391  12097   4508    621    879       C  
ATOM   2507  CD  GLN A 336     -30.826 -48.271 -17.078  1.00122.70           C  
ANISOU 2507  CD  GLN A 336    19710  14148  12761   4482    717    720       C  
ATOM   2508  OE1 GLN A 336     -31.279 -47.126 -17.055  1.00123.34           O  
ANISOU 2508  OE1 GLN A 336    19489  14411  12964   4061    614    669       O  
ATOM   2509  NE2 GLN A 336     -30.705 -48.971 -18.200  1.00130.07           N  
ANISOU 2509  NE2 GLN A 336    21267  14784  13371   4965    906    637       N  
ATOM   2510  N   ALA A 337     -27.675 -48.320 -12.877  1.00 93.57           N  
ANISOU 2510  N   ALA A 337    13997  11587   9969   4447    566   1731       N  
ATOM   2511  CA  ALA A 337     -26.285 -48.758 -12.803  1.00 96.55           C  
ANISOU 2511  CA  ALA A 337    13993  12207  10484   4899    807   2156       C  
ATOM   2512  C   ALA A 337     -26.082 -49.810 -11.719  1.00 95.29           C  
ANISOU 2512  C   ALA A 337    13863  11980  10364   5014    657   2246       C  
ATOM   2513  O   ALA A 337     -25.232 -50.695 -11.869  1.00100.81           O  
ANISOU 2513  O   ALA A 337    14548  12691  11063   5549    917   2509       O  
ATOM   2514  CB  ALA A 337     -25.368 -47.560 -12.560  1.00 94.62           C  
ANISOU 2514  CB  ALA A 337    12990  12406  10556   4677    748   2516       C  
ATOM   2515  N   LYS A 338     -26.848 -49.733 -10.627  1.00 90.36           N  
ANISOU 2515  N   LYS A 338    13290  11290   9753   4568    273   2063       N  
ATOM   2516  CA  LYS A 338     -26.724 -50.706  -9.546  1.00 91.96           C  
ANISOU 2516  CA  LYS A 338    13529  11435   9978   4653    117   2164       C  
ATOM   2517  C   LYS A 338     -27.260 -52.079  -9.928  1.00 89.99           C  
ANISOU 2517  C   LYS A 338    13917  10739   9535   4971    221   2011       C  
ATOM   2518  O   LYS A 338     -26.951 -53.061  -9.246  1.00 89.93           O  
ANISOU 2518  O   LYS A 338    13962  10655   9553   5181    176   2159       O  
ATOM   2519  CB  LYS A 338     -27.462 -50.213  -8.301  1.00 89.99           C  
ANISOU 2519  CB  LYS A 338    13215  11243   9735   4142   -280   2034       C  
ATOM   2520  CG  LYS A 338     -26.809 -49.044  -7.593  1.00 93.13           C  
ANISOU 2520  CG  LYS A 338    13083  12006  10298   3848   -523   2203       C  
ATOM   2521  CD  LYS A 338     -27.656 -48.595  -6.412  1.00 95.16           C  
ANISOU 2521  CD  LYS A 338    13463  12257  10437   3451   -877   2021       C  
ATOM   2522  CE  LYS A 338     -26.894 -47.635  -5.516  1.00 98.64           C  
ANISOU 2522  CE  LYS A 338    13514  12976  10989   3207  -1231   2193       C  
ATOM   2523  NZ  LYS A 338     -25.685 -48.280  -4.932  1.00102.81           N  
ANISOU 2523  NZ  LYS A 338    13700  13678  11683   3425  -1318   2581       N  
ATOM   2524  N   GLY A 339     -28.049 -52.168 -10.993  1.00 88.46           N  
ANISOU 2524  N   GLY A 339    14238  10221   9153   4995    306   1733       N  
ATOM   2525  CA  GLY A 339     -28.752 -53.385 -11.330  1.00 83.80           C  
ANISOU 2525  CA  GLY A 339    14348   9109   8384   5165    245   1556       C  
ATOM   2526  C   GLY A 339     -30.186 -53.437 -10.856  1.00 79.48           C  
ANISOU 2526  C   GLY A 339    14048   8314   7837   4643   -117   1355       C  
ATOM   2527  O   GLY A 339     -30.799 -54.508 -10.913  1.00 79.68           O  
ANISOU 2527  O   GLY A 339    14591   7890   7794   4686   -278   1290       O  
ATOM   2528  N   LEU A 340     -30.742 -52.315 -10.398  1.00 76.58           N  
ANISOU 2528  N   LEU A 340    13333   8209   7555   4170   -255   1297       N  
ATOM   2529  CA  LEU A 340     -32.088 -52.266  -9.843  1.00 75.08           C  
ANISOU 2529  CA  LEU A 340    13263   7877   7387   3722   -532   1211       C  
ATOM   2530  C   LEU A 340     -33.094 -51.646 -10.807  1.00 67.20           C  
ANISOU 2530  C   LEU A 340    12495   6710   6328   3458   -586    999       C  
ATOM   2531  O   LEU A 340     -34.124 -51.123 -10.371  1.00 68.52           O  
ANISOU 2531  O   LEU A 340    12564   6922   6550   3068   -747    983       O  
ATOM   2532  CB  LEU A 340     -32.084 -51.502  -8.518  1.00 72.02           C  
ANISOU 2532  CB  LEU A 340    12403   7882   7081   3455   -640   1321       C  
ATOM   2533  CG  LEU A 340     -31.183 -52.063  -7.416  1.00 74.44           C  
ANISOU 2533  CG  LEU A 340    12475   8368   7441   3650   -670   1554       C  
ATOM   2534  CD1 LEU A 340     -31.292 -51.234  -6.141  1.00 75.47           C  
ANISOU 2534  CD1 LEU A 340    12282   8830   7562   3385   -839   1618       C  
ATOM   2535  CD2 LEU A 340     -31.516 -53.521  -7.141  1.00 74.92           C  
ANISOU 2535  CD2 LEU A 340    12883   8081   7501   3797   -745   1654       C  
ATOM   2536  N   GLY A 341     -32.819 -51.696 -12.112  1.00 68.68           N  
ANISOU 2536  N   GLY A 341    12998   6713   6382   3704   -438    866       N  
ATOM   2537  CA  GLY A 341     -33.729 -51.116 -13.086  1.00 67.18           C  
ANISOU 2537  CA  GLY A 341    13052   6356   6116   3466   -517    674       C  
ATOM   2538  C   GLY A 341     -35.095 -51.770 -13.112  1.00 78.65           C  
ANISOU 2538  C   GLY A 341    14903   7381   7599   3149   -871    644       C  
ATOM   2539  O   GLY A 341     -36.073 -51.135 -13.521  1.00 76.95           O  
ANISOU 2539  O   GLY A 341    14708   7118   7412   2806  -1012    574       O  
ATOM   2540  N   ASP A 342     -35.185 -53.025 -12.682  1.00 82.29           N  
ANISOU 2540  N   ASP A 342    15652   7524   8090   3242  -1042    748       N  
ATOM   2541  CA  ASP A 342     -36.442 -53.756 -12.641  1.00 85.20           C  
ANISOU 2541  CA  ASP A 342    16356   7455   8562   2902  -1444    826       C  
ATOM   2542  C   ASP A 342     -37.195 -53.574 -11.330  1.00 81.12           C  
ANISOU 2542  C   ASP A 342    15362   7183   8276   2534  -1549   1092       C  
ATOM   2543  O   ASP A 342     -38.369 -53.955 -11.249  1.00 80.78           O  
ANISOU 2543  O   ASP A 342    15426   6878   8391   2182  -1860   1267       O  
ATOM   2544  CB  ASP A 342     -36.186 -55.247 -12.862  1.00 96.56           C  
ANISOU 2544  CB  ASP A 342    18407   8355   9927   3183  -1621    838       C  
ATOM   2545  CG  ASP A 342     -35.547 -55.912 -11.655  1.00103.98           C  
ANISOU 2545  CG  ASP A 342    19086   9450  10972   3365  -1530   1053       C  
ATOM   2546  OD1 ASP A 342     -34.346 -55.669 -11.408  1.00106.26           O  
ANISOU 2546  OD1 ASP A 342    19092  10093  11189   3742  -1187   1052       O  
ATOM   2547  OD2 ASP A 342     -36.247 -56.671 -10.951  1.00106.99           O  
ANISOU 2547  OD2 ASP A 342    19447   9660  11544   3078  -1795   1246       O  
ATOM   2548  N   SER A 343     -36.553 -53.006 -10.312  1.00 76.28           N  
ANISOU 2548  N   SER A 343    14247   7059   7678   2622  -1316   1168       N  
ATOM   2549  CA  SER A 343     -37.136 -52.924  -8.983  1.00 73.29           C  
ANISOU 2549  CA  SER A 343    13511   6915   7421   2407  -1366   1428       C  
ATOM   2550  C   SER A 343     -38.383 -52.043  -8.979  1.00 68.44           C  
ANISOU 2550  C   SER A 343    12704   6416   6885   2039  -1424   1501       C  
ATOM   2551  O   SER A 343     -38.610 -51.229  -9.880  1.00 69.33           O  
ANISOU 2551  O   SER A 343    12852   6535   6956   1940  -1394   1313       O  
ATOM   2552  CB  SER A 343     -36.115 -52.374  -7.990  1.00 76.05           C  
ANISOU 2552  CB  SER A 343    13465   7734   7697   2601  -1158   1444       C  
ATOM   2553  OG  SER A 343     -35.752 -51.045  -8.328  1.00 73.69           O  
ANISOU 2553  OG  SER A 343    12936   7737   7325   2573  -1011   1257       O  
ATOM   2554  N   ARG A 344     -39.195 -52.212  -7.933  1.00 69.95           N  
ANISOU 2554  N   ARG A 344    12675   6717   7186   1874  -1476   1825       N  
ATOM   2555  CA  ARG A 344     -40.405 -51.406  -7.809  1.00 67.38           C  
ANISOU 2555  CA  ARG A 344    12115   6544   6940   1604  -1467   1992       C  
ATOM   2556  C   ARG A 344     -40.084 -49.953  -7.489  1.00 62.27           C  
ANISOU 2556  C   ARG A 344    11208   6334   6118   1689  -1214   1800       C  
ATOM   2557  O   ARG A 344     -40.866 -49.062  -7.834  1.00 63.57           O  
ANISOU 2557  O   ARG A 344    11265   6584   6305   1528  -1174   1799       O  
ATOM   2558  CB  ARG A 344     -41.329 -51.982  -6.737  1.00 69.62           C  
ANISOU 2558  CB  ARG A 344    12201   6874   7376   1488  -1517   2481       C  
ATOM   2559  CG  ARG A 344     -42.699 -51.317  -6.703  1.00 67.70           C  
ANISOU 2559  CG  ARG A 344    11696   6759   7267   1246  -1491   2780       C  
ATOM   2560  CD  ARG A 344     -43.252 -51.223  -5.293  1.00 71.53           C  
ANISOU 2560  CD  ARG A 344    11855   7596   7726   1350  -1277   3213       C  
ATOM   2561  NE  ARG A 344     -44.553 -50.562  -5.269  1.00 70.83           N  
ANISOU 2561  NE  ARG A 344    11480   7667   7766   1204  -1178   3567       N  
ATOM   2562  CZ  ARG A 344     -44.727 -49.253  -5.118  1.00 65.39           C  
ANISOU 2562  CZ  ARG A 344    10664   7304   6879   1343   -908   3430       C  
ATOM   2563  NH1 ARG A 344     -43.681 -48.453  -4.971  1.00 62.87           N  
ANISOU 2563  NH1 ARG A 344    10485   7158   6245   1567   -774   2943       N  
ATOM   2564  NH2 ARG A 344     -45.951 -48.745  -5.109  1.00 66.60           N  
ANISOU 2564  NH2 ARG A 344    10543   7592   7169   1258   -794   3821       N  
ATOM   2565  N   GLN A 345     -38.956 -49.687  -6.825  1.00 61.31           N  
ANISOU 2565  N   GLN A 345    10996   6464   5835   1926  -1088   1662       N  
ATOM   2566  CA  GLN A 345     -38.598 -48.298  -6.558  1.00 59.32           C  
ANISOU 2566  CA  GLN A 345    10572   6541   5426   1966   -956   1474       C  
ATOM   2567  C   GLN A 345     -38.148 -47.588  -7.829  1.00 56.65           C  
ANISOU 2567  C   GLN A 345    10284   6144   5096   1923   -931   1180       C  
ATOM   2568  O   GLN A 345     -38.329 -46.371  -7.956  1.00 59.29           O  
ANISOU 2568  O   GLN A 345    10515   6641   5370   1842   -869   1057       O  
ATOM   2569  CB  GLN A 345     -37.521 -48.221  -5.472  1.00 60.97           C  
ANISOU 2569  CB  GLN A 345    10684   6997   5485   2174   -940   1459       C  
ATOM   2570  CG  GLN A 345     -36.165 -48.794  -5.845  1.00 66.55           C  
ANISOU 2570  CG  GLN A 345    11405   7644   6235   2345   -970   1362       C  
ATOM   2571  CD  GLN A 345     -35.236 -48.900  -4.644  1.00 77.44           C  
ANISOU 2571  CD  GLN A 345    12658   9252   7514   2512  -1026   1455       C  
ATOM   2572  OE1 GLN A 345     -35.684 -48.913  -3.497  1.00 75.71           O  
ANISOU 2572  OE1 GLN A 345    12438   9163   7164   2531  -1052   1606       O  
ATOM   2573  NE2 GLN A 345     -33.936 -48.976  -4.905  1.00 85.89           N  
ANISOU 2573  NE2 GLN A 345    13615  10383   8637   2657  -1041   1409       N  
ATOM   2574  N   ALA A 346     -37.579 -48.329  -8.784  1.00 57.39           N  
ANISOU 2574  N   ALA A 346    10574   5991   5238   2013   -965   1084       N  
ATOM   2575  CA  ALA A 346     -37.258 -47.740 -10.078  1.00 59.40           C  
ANISOU 2575  CA  ALA A 346    10918   6182   5470   2016   -904    860       C  
ATOM   2576  C   ALA A 346     -38.525 -47.419 -10.861  1.00 59.42           C  
ANISOU 2576  C   ALA A 346    11044   6004   5527   1755   -996    851       C  
ATOM   2577  O   ALA A 346     -38.622 -46.356 -11.486  1.00 59.25           O  
ANISOU 2577  O   ALA A 346    10953   6083   5476   1670   -927    710       O  
ATOM   2578  CB  ALA A 346     -36.354 -48.679 -10.876  1.00 60.58           C  
ANISOU 2578  CB  ALA A 346    11326   6107   5584   2289   -867    792       C  
ATOM   2579  N   ARG A 347     -39.510 -48.321 -10.833  1.00 57.14           N  
ANISOU 2579  N   ARG A 347    10918   5441   5350   1603  -1188   1047       N  
ATOM   2580  CA  ARG A 347     -40.770 -48.057 -11.521  1.00 58.42           C  
ANISOU 2580  CA  ARG A 347    11141   5434   5621   1311  -1344   1132       C  
ATOM   2581  C   ARG A 347     -41.529 -46.911 -10.866  1.00 56.79           C  
ANISOU 2581  C   ARG A 347    10572   5559   5447   1189  -1208   1261       C  
ATOM   2582  O   ARG A 347     -42.137 -46.087 -11.560  1.00 54.22           O  
ANISOU 2582  O   ARG A 347    10209   5243   5149   1038  -1213   1215       O  
ATOM   2583  CB  ARG A 347     -41.633 -49.318 -11.551  1.00 66.86           C  
ANISOU 2583  CB  ARG A 347    12419   6116   6868   1125  -1660   1411       C  
ATOM   2584  CG  ARG A 347     -41.161 -50.373 -12.536  1.00 75.58           C  
ANISOU 2584  CG  ARG A 347    14072   6743   7901   1227  -1881   1240       C  
ATOM   2585  CD  ARG A 347     -42.183 -51.490 -12.675  1.00 81.68           C  
ANISOU 2585  CD  ARG A 347    15104   7043   8886    937  -2328   1532       C  
ATOM   2586  NE  ARG A 347     -42.380 -52.212 -11.422  1.00 86.67           N  
ANISOU 2586  NE  ARG A 347    15500   7743   9689    909  -2346   1888       N  
ATOM   2587  CZ  ARG A 347     -41.686 -53.288 -11.066  1.00 93.10           C  
ANISOU 2587  CZ  ARG A 347    16557   8350  10466   1117  -2400   1886       C  
ATOM   2588  NH1 ARG A 347     -40.748 -53.769 -11.870  1.00 95.64           N  
ANISOU 2588  NH1 ARG A 347    17377   8386  10576   1412  -2413   1551       N  
ATOM   2589  NH2 ARG A 347     -41.929 -53.885  -9.906  1.00 94.42           N  
ANISOU 2589  NH2 ARG A 347    16479   8604  10792   1076  -2410   2251       N  
ATOM   2590  N   ALA A 348     -41.512 -46.843  -9.534  1.00 55.43           N  
ANISOU 2590  N   ALA A 348    10176   5648   5235   1297  -1080   1431       N  
ATOM   2591  CA  ALA A 348     -42.204 -45.762  -8.840  1.00 54.61           C  
ANISOU 2591  CA  ALA A 348     9831   5840   5078   1297   -911   1550       C  
ATOM   2592  C   ALA A 348     -41.513 -44.427  -9.080  1.00 52.47           C  
ANISOU 2592  C   ALA A 348     9540   5752   4644   1375   -791   1211       C  
ATOM   2593  O   ALA A 348     -42.179 -43.395  -9.231  1.00 51.62           O  
ANISOU 2593  O   ALA A 348     9351   5744   4520   1318   -707   1211       O  
ATOM   2594  CB  ALA A 348     -42.288 -46.066  -7.344  1.00 56.08           C  
ANISOU 2594  CB  ALA A 348     9893   6240   5174   1472   -798   1806       C  
ATOM   2595  N   LEU A 349     -40.178 -44.428  -9.119  1.00 52.06           N  
ANISOU 2595  N   LEU A 349     9540   5739   4500   1504   -793    972       N  
ATOM   2596  CA  LEU A 349     -39.450 -43.202  -9.425  1.00 54.81           C  
ANISOU 2596  CA  LEU A 349     9835   6225   4764   1520   -744    721       C  
ATOM   2597  C   LEU A 349     -39.697 -42.763 -10.864  1.00 57.91           C  
ANISOU 2597  C   LEU A 349    10288   6479   5234   1382   -743    593       C  
ATOM   2598  O   LEU A 349     -39.826 -41.563 -11.142  1.00 64.42           O  
ANISOU 2598  O   LEU A 349    11050   7395   6033   1313   -698    485       O  
ATOM   2599  CB  LEU A 349     -37.958 -43.408  -9.165  1.00 58.73           C  
ANISOU 2599  CB  LEU A 349    10286   6808   5222   1668   -774    623       C  
ATOM   2600  CG  LEU A 349     -37.052 -42.178  -9.225  1.00 62.68           C  
ANISOU 2600  CG  LEU A 349    10662   7463   5689   1648   -801    468       C  
ATOM   2601  CD1 LEU A 349     -37.568 -41.089  -8.298  1.00 61.93           C  
ANISOU 2601  CD1 LEU A 349    10600   7484   5447   1615   -848    432       C  
ATOM   2602  CD2 LEU A 349     -35.627 -42.561  -8.861  1.00 64.45           C  
ANISOU 2602  CD2 LEU A 349    10755   7789   5944   1778   -868    510       C  
ATOM   2603  N   ALA A 350     -39.780 -43.721 -11.791  1.00 55.28           N  
ANISOU 2603  N   ALA A 350    10141   5894   4970   1356   -818    602       N  
ATOM   2604  CA  ALA A 350     -40.079 -43.385 -13.179  1.00 54.22           C  
ANISOU 2604  CA  ALA A 350    10151   5600   4852   1248   -847    489       C  
ATOM   2605  C   ALA A 350     -41.493 -42.837 -13.322  1.00 56.83           C  
ANISOU 2605  C   ALA A 350    10415   5906   5274   1020   -911    625       C  
ATOM   2606  O   ALA A 350     -41.723 -41.891 -14.083  1.00 64.40           O  
ANISOU 2606  O   ALA A 350    11356   6888   6225    931   -879    526       O  
ATOM   2607  CB  ALA A 350     -39.887 -44.610 -14.071  1.00 55.38           C  
ANISOU 2607  CB  ALA A 350    10650   5416   4974   1321   -965    458       C  
ATOM   2608  N   HIS A 351     -42.452 -43.421 -12.601  1.00 55.57           N  
ANISOU 2608  N   HIS A 351    10178   5713   5223    935   -989    913       N  
ATOM   2609  CA  HIS A 351     -43.820 -42.914 -12.635  1.00 54.79           C  
ANISOU 2609  CA  HIS A 351     9918   5643   5255    756  -1012   1164       C  
ATOM   2610  C   HIS A 351     -43.894 -41.505 -12.060  1.00 50.30           C  
ANISOU 2610  C   HIS A 351     9162   5369   4580    869   -779   1103       C  
ATOM   2611  O   HIS A 351     -44.601 -40.640 -12.596  1.00 52.95           O  
ANISOU 2611  O   HIS A 351     9426   5726   4967    775   -750   1138       O  
ATOM   2612  CB  HIS A 351     -44.743 -43.864 -11.871  1.00 55.60           C  
ANISOU 2612  CB  HIS A 351     9898   5698   5531    677  -1106   1598       C  
ATOM   2613  CG  HIS A 351     -46.200 -43.573 -12.055  1.00 61.02           C  
ANISOU 2613  CG  HIS A 351    10361   6390   6435    474  -1166   1992       C  
ATOM   2614  ND1 HIS A 351     -46.844 -42.549 -11.395  1.00 64.72           N  
ANISOU 2614  ND1 HIS A 351    10555   7161   6875    606   -892   2177       N  
ATOM   2615  CD2 HIS A 351     -47.140 -44.178 -12.819  1.00 62.10           C  
ANISOU 2615  CD2 HIS A 351    10512   6253   6830    162  -1493   2281       C  
ATOM   2616  CE1 HIS A 351     -48.116 -42.532 -11.749  1.00 65.28           C  
ANISOU 2616  CE1 HIS A 351    10404   7195   7205    406   -991   2604       C  
ATOM   2617  NE2 HIS A 351     -48.322 -43.511 -12.611  1.00 63.73           N  
ANISOU 2617  NE2 HIS A 351    10358   6647   7209     93  -1393   2687       N  
ATOM   2618  N   ALA A 352     -43.162 -41.252 -10.970  1.00 52.92           N  
ANISOU 2618  N   ALA A 352     9465   5894   4747   1081   -649   1012       N  
ATOM   2619  CA  ALA A 352     -43.082 -39.897 -10.435  1.00 55.74           C  
ANISOU 2619  CA  ALA A 352     9790   6443   4946   1209   -507    889       C  
ATOM   2620  C   ALA A 352     -42.481 -38.941 -11.458  1.00 53.55           C  
ANISOU 2620  C   ALA A 352     9561   6120   4668   1113   -542    600       C  
ATOM   2621  O   ALA A 352     -42.924 -37.792 -11.582  1.00 50.34           O  
ANISOU 2621  O   ALA A 352     9140   5759   4226   1110   -475    559       O  
ATOM   2622  CB  ALA A 352     -42.267 -39.886  -9.142  1.00 49.28           C  
ANISOU 2622  CB  ALA A 352     9031   5770   3921   1425   -478    815       C  
ATOM   2623  N   ALA A 353     -41.473 -39.401 -12.206  1.00 54.39           N  
ANISOU 2623  N   ALA A 353     9724   6135   4805   1071   -620    438       N  
ATOM   2624  CA  ALA A 353     -40.919 -38.578 -13.276  1.00 49.73           C  
ANISOU 2624  CA  ALA A 353     9144   5522   4231    997   -616    251       C  
ATOM   2625  C   ALA A 353     -41.964 -38.293 -14.345  1.00 52.04           C  
ANISOU 2625  C   ALA A 353     9476   5694   4603    840   -634    305       C  
ATOM   2626  O   ALA A 353     -42.005 -37.190 -14.903  1.00 52.97           O  
ANISOU 2626  O   ALA A 353     9564   5840   4723    779   -598    216       O  
ATOM   2627  CB  ALA A 353     -39.697 -39.258 -13.890  1.00 48.84           C  
ANISOU 2627  CB  ALA A 353     9074   5363   4118   1074   -621    162       C  
ATOM   2628  N   ALA A 354     -42.820 -39.272 -14.641  1.00 53.98           N  
ANISOU 2628  N   ALA A 354     9793   5783   4935    749   -740    481       N  
ATOM   2629  CA  ALA A 354     -43.886 -39.054 -15.614  1.00 53.83           C  
ANISOU 2629  CA  ALA A 354     9805   5632   5016    559   -843    591       C  
ATOM   2630  C   ALA A 354     -44.842 -37.970 -15.136  1.00 54.18           C  
ANISOU 2630  C   ALA A 354     9638   5833   5114    549   -728    749       C  
ATOM   2631  O   ALA A 354     -45.214 -37.066 -15.898  1.00 53.25           O  
ANISOU 2631  O   ALA A 354     9503   5706   5024    466   -720    715       O  
ATOM   2632  CB  ALA A 354     -44.636 -40.363 -15.872  1.00 52.57           C  
ANISOU 2632  CB  ALA A 354     9765   5231   4978    413  -1086    816       C  
ATOM   2633  N   VAL A 355     -45.246 -38.045 -13.865  1.00 55.16           N  
ANISOU 2633  N   VAL A 355     9627   6105   5227    687   -611    942       N  
ATOM   2634  CA  VAL A 355     -46.115 -37.016 -13.300  1.00 53.10           C  
ANISOU 2634  CA  VAL A 355     9225   6001   4949    808   -429   1110       C  
ATOM   2635  C   VAL A 355     -45.448 -35.648 -13.386  1.00 50.59           C  
ANISOU 2635  C   VAL A 355     9013   5729   4479    899   -348    792       C  
ATOM   2636  O   VAL A 355     -46.078 -34.655 -13.776  1.00 54.39           O  
ANISOU 2636  O   VAL A 355     9458   6219   4989    898   -281    833       O  
ATOM   2637  CB  VAL A 355     -46.493 -37.378 -11.851  1.00 55.69           C  
ANISOU 2637  CB  VAL A 355     9467   6493   5199   1046   -264   1367       C  
ATOM   2638  CG1 VAL A 355     -47.425 -36.332 -11.263  1.00 50.33           C  
ANISOU 2638  CG1 VAL A 355     8704   5976   4441   1290     -9   1575       C  
ATOM   2639  CG2 VAL A 355     -47.136 -38.753 -11.805  1.00 54.05           C  
ANISOU 2639  CG2 VAL A 355     9117   6214   5205    904   -386   1748       C  
ATOM   2640  N   LYS A 356     -44.158 -35.574 -13.040  1.00 49.81           N  
ANISOU 2640  N   LYS A 356     9033   5644   4249    959   -390    514       N  
ATOM   2641  CA  LYS A 356     -43.445 -34.303 -13.124  1.00 54.00           C  
ANISOU 2641  CA  LYS A 356     9653   6174   4692    976   -407    265       C  
ATOM   2642  C   LYS A 356     -43.352 -33.800 -14.559  1.00 59.15           C  
ANISOU 2642  C   LYS A 356    10272   6737   5464    781   -453    183       C  
ATOM   2643  O   LYS A 356     -43.312 -32.586 -14.789  1.00 62.78           O  
ANISOU 2643  O   LYS A 356    10768   7175   5912    765   -448     89       O  
ATOM   2644  CB  LYS A 356     -42.050 -34.441 -12.519  1.00 55.30           C  
ANISOU 2644  CB  LYS A 356     9878   6368   4766   1016   -517     84       C  
ATOM   2645  CG  LYS A 356     -42.059 -34.676 -11.020  1.00 60.16           C  
ANISOU 2645  CG  LYS A 356    10604   7064   5191   1235   -504    126       C  
ATOM   2646  CD  LYS A 356     -42.902 -33.626 -10.319  1.00 65.42           C  
ANISOU 2646  CD  LYS A 356    11445   7740   5674   1443   -399    150       C  
ATOM   2647  CE  LYS A 356     -43.050 -33.921  -8.839  1.00 69.13           C  
ANISOU 2647  CE  LYS A 356    12093   8298   5876   1745   -333    230       C  
ATOM   2648  NZ  LYS A 356     -43.989 -32.963  -8.197  1.00 72.70           N  
ANISOU 2648  NZ  LYS A 356    12775   8759   6088   2065   -149    296       N  
ATOM   2649  N   LEU A 357     -43.312 -34.708 -15.534  1.00 59.24           N  
ANISOU 2649  N   LEU A 357    10275   6671   5563    656   -513    219       N  
ATOM   2650  CA  LEU A 357     -43.281 -34.285 -16.929  1.00 56.06           C  
ANISOU 2650  CA  LEU A 357     9905   6185   5211    519   -544    161       C  
ATOM   2651  C   LEU A 357     -44.628 -33.713 -17.352  1.00 54.01           C  
ANISOU 2651  C   LEU A 357     9596   5890   5036    432   -545    327       C  
ATOM   2652  O   LEU A 357     -44.686 -32.725 -18.098  1.00 58.68           O  
ANISOU 2652  O   LEU A 357    10188   6461   5646    368   -531    273       O  
ATOM   2653  CB  LEU A 357     -42.877 -35.459 -17.819  1.00 61.17           C  
ANISOU 2653  CB  LEU A 357    10688   6715   5838    488   -620    138       C  
ATOM   2654  CG  LEU A 357     -42.297 -35.115 -19.190  1.00 65.31           C  
ANISOU 2654  CG  LEU A 357    11318   7188   6308    465   -597     36       C  
ATOM   2655  CD1 LEU A 357     -41.276 -33.996 -19.065  1.00 66.62           C  
ANISOU 2655  CD1 LEU A 357    11325   7496   6493    499   -489    -45       C  
ATOM   2656  CD2 LEU A 357     -41.663 -36.346 -19.806  1.00 63.53           C  
ANISOU 2656  CD2 LEU A 357    11324   6847   5968    583   -617    -11       C  
ATOM   2657  N   GLN A 358     -45.723 -34.312 -16.873  1.00 50.45           N  
ANISOU 2657  N   GLN A 358     9059   5444   4666    431   -561    590       N  
ATOM   2658  CA  GLN A 358     -47.037 -33.716 -17.095  1.00 55.55           C  
ANISOU 2658  CA  GLN A 358     9565   6107   5435    388   -535    852       C  
ATOM   2659  C   GLN A 358     -47.133 -32.330 -16.467  1.00 59.13           C  
ANISOU 2659  C   GLN A 358    10002   6661   5802    591   -337    796       C  
ATOM   2660  O   GLN A 358     -47.677 -31.400 -17.077  1.00 63.11           O  
ANISOU 2660  O   GLN A 358    10470   7145   6365    560   -310    849       O  
ATOM   2661  CB  GLN A 358     -48.132 -34.623 -16.540  1.00 59.88           C  
ANISOU 2661  CB  GLN A 358     9935   6683   6134    370   -569   1261       C  
ATOM   2662  CG  GLN A 358     -48.731 -35.566 -17.557  1.00 72.20           C  
ANISOU 2662  CG  GLN A 358    11510   8050   7873     71   -884   1457       C  
ATOM   2663  CD  GLN A 358     -50.066 -36.120 -17.109  1.00 84.01           C  
ANISOU 2663  CD  GLN A 358    12709   9584   9628    -13   -955   2013       C  
ATOM   2664  OE1 GLN A 358     -50.356 -36.183 -15.914  1.00 86.28           O  
ANISOU 2664  OE1 GLN A 358    12802  10057   9922    203   -723   2243       O  
ATOM   2665  NE2 GLN A 358     -50.894 -36.518 -18.069  1.00 89.45           N  
ANISOU 2665  NE2 GLN A 358    13359  10096  10533   -324  -1295   2279       N  
ATOM   2666  N   GLU A 359     -46.614 -32.171 -15.246  1.00 57.62           N  
ANISOU 2666  N   GLU A 359     9897   6547   5447    815   -229    685       N  
ATOM   2667  CA  GLU A 359     -46.671 -30.866 -14.592  1.00 58.66           C  
ANISOU 2667  CA  GLU A 359    10163   6694   5430   1046   -102    591       C  
ATOM   2668  C   GLU A 359     -45.811 -29.840 -15.323  1.00 56.41           C  
ANISOU 2668  C   GLU A 359     9998   6291   5143    908   -221    307       C  
ATOM   2669  O   GLU A 359     -46.173 -28.659 -15.398  1.00 61.42           O  
ANISOU 2669  O   GLU A 359    10725   6862   5749    996   -172    285       O  
ATOM   2670  CB  GLU A 359     -46.245 -30.992 -13.130  1.00 64.02           C  
ANISOU 2670  CB  GLU A 359    11015   7433   5875   1317    -39    515       C  
ATOM   2671  CG  GLU A 359     -47.234 -31.770 -12.277  1.00 74.20           C  
ANISOU 2671  CG  GLU A 359    12175   8872   7144   1537    157    882       C  
ATOM   2672  CD  GLU A 359     -46.741 -32.012 -10.858  1.00 78.57           C  
ANISOU 2672  CD  GLU A 359    12944   9493   7417   1821    214    806       C  
ATOM   2673  OE1 GLU A 359     -45.688 -31.456 -10.480  1.00 83.07           O  
ANISOU 2673  OE1 GLU A 359    13795   9967   7802   1844     56    459       O  
ATOM   2674  OE2 GLU A 359     -47.412 -32.764 -10.121  1.00 78.55           O  
ANISOU 2674  OE2 GLU A 359    12822   9634   7389   2008    389   1135       O  
ATOM   2675  N   LEU A 360     -44.671 -30.271 -15.869  1.00 52.93           N  
ANISOU 2675  N   LEU A 360     9546   5823   4743    718   -361    136       N  
ATOM   2676  CA  LEU A 360     -43.856 -29.367 -16.674  1.00 52.04           C  
ANISOU 2676  CA  LEU A 360     9458   5632   4683    569   -453    -19       C  
ATOM   2677  C   LEU A 360     -44.603 -28.929 -17.927  1.00 56.78           C  
ANISOU 2677  C   LEU A 360     9991   6190   5394    447   -421     86       C  
ATOM   2678  O   LEU A 360     -44.583 -27.745 -18.290  1.00 55.33           O  
ANISOU 2678  O   LEU A 360     9850   5931   5240    414   -435     42       O  
ATOM   2679  CB  LEU A 360     -42.530 -30.032 -17.042  1.00 47.55           C  
ANISOU 2679  CB  LEU A 360     8822   5098   4148    459   -534   -107       C  
ATOM   2680  CG  LEU A 360     -41.626 -29.245 -17.995  1.00 48.85           C  
ANISOU 2680  CG  LEU A 360     8920   5233   4409    310   -586   -146       C  
ATOM   2681  CD1 LEU A 360     -41.303 -27.868 -17.427  1.00 49.24           C  
ANISOU 2681  CD1 LEU A 360     9053   5179   4476    278   -724   -222       C  
ATOM   2682  CD2 LEU A 360     -40.351 -30.014 -18.288  1.00 47.73           C  
ANISOU 2682  CD2 LEU A 360     8659   5179   4299    296   -586   -131       C  
ATOM   2683  N   GLU A 361     -45.272 -29.871 -18.600  1.00 59.67           N  
ANISOU 2683  N   GLU A 361    10281   6571   5821    363   -428    238       N  
ATOM   2684  CA  GLU A 361     -46.097 -29.511 -19.750  1.00 60.25           C  
ANISOU 2684  CA  GLU A 361    10315   6591   5984    237   -460    371       C  
ATOM   2685  C   GLU A 361     -47.165 -28.493 -19.364  1.00 56.48           C  
ANISOU 2685  C   GLU A 361     9777   6126   5559    357   -359    529       C  
ATOM   2686  O   GLU A 361     -47.377 -27.496 -20.073  1.00 54.52           O  
ANISOU 2686  O   GLU A 361     9535   5822   5357    308   -358    536       O  
ATOM   2687  CB  GLU A 361     -46.735 -30.769 -20.340  1.00 64.68           C  
ANISOU 2687  CB  GLU A 361    10870   7108   6598    110   -592    536       C  
ATOM   2688  CG  GLU A 361     -47.668 -30.522 -21.510  1.00 70.24           C  
ANISOU 2688  CG  GLU A 361    11562   7734   7391    -53   -720    712       C  
ATOM   2689  CD  GLU A 361     -48.287 -31.803 -22.044  1.00 73.78           C  
ANISOU 2689  CD  GLU A 361    12084   8060   7890   -225   -980    883       C  
ATOM   2690  OE1 GLU A 361     -47.955 -32.889 -21.523  1.00 74.71           O  
ANISOU 2690  OE1 GLU A 361    12267   8144   7976   -202  -1032    853       O  
ATOM   2691  OE2 GLU A 361     -49.105 -31.723 -22.985  1.00 80.46           O  
ANISOU 2691  OE2 GLU A 361    12948   8810   8812   -398  -1181   1060       O  
ATOM   2692  N   GLN A 362     -47.832 -28.716 -18.229  1.00 54.30           N  
ANISOU 2692  N   GLN A 362     9448   5927   5258    564   -239    686       N  
ATOM   2693  CA  GLN A 362     -48.886 -27.800 -17.804  1.00 53.31           C  
ANISOU 2693  CA  GLN A 362     9278   5833   5145    794    -66    893       C  
ATOM   2694  C   GLN A 362     -48.328 -26.414 -17.507  1.00 54.78           C  
ANISOU 2694  C   GLN A 362     9715   5902   5195    942    -30    637       C  
ATOM   2695  O   GLN A 362     -48.958 -25.402 -17.836  1.00 56.94           O  
ANISOU 2695  O   GLN A 362    10008   6119   5508   1035     44    729       O  
ATOM   2696  CB  GLN A 362     -49.614 -28.359 -16.582  1.00 50.34           C  
ANISOU 2696  CB  GLN A 362     8811   5594   4722   1071    120   1160       C  
ATOM   2697  CG  GLN A 362     -50.861 -27.572 -16.199  1.00 56.89           C  
ANISOU 2697  CG  GLN A 362     9542   6504   5571   1396    379   1504       C  
ATOM   2698  CD  GLN A 362     -51.896 -27.540 -17.313  1.00 65.40           C  
ANISOU 2698  CD  GLN A 362    10306   7605   6938   1190    307   1868       C  
ATOM   2699  OE1 GLN A 362     -52.018 -28.485 -18.092  1.00 66.21           O  
ANISOU 2699  OE1 GLN A 362    10242   7689   7226    836     61   1991       O  
ATOM   2700  NE2 GLN A 362     -52.643 -26.446 -17.396  1.00 71.10           N  
ANISOU 2700  NE2 GLN A 362    10995   8336   7683   1423    487   2047       N  
ATOM   2701  N   GLU A 363     -47.145 -26.345 -16.890  1.00 53.21           N  
ANISOU 2701  N   GLU A 363     9722   5641   4856    950   -127    341       N  
ATOM   2702  CA  GLU A 363     -46.551 -25.042 -16.608  1.00 49.39           C  
ANISOU 2702  CA  GLU A 363     9521   4974   4273   1018   -217    115       C  
ATOM   2703  C   GLU A 363     -46.087 -24.351 -17.885  1.00 49.63           C  
ANISOU 2703  C   GLU A 363     9481   4907   4471    731   -347     61       C  
ATOM   2704  O   GLU A 363     -46.067 -23.116 -17.945  1.00 50.29           O  
ANISOU 2704  O   GLU A 363     9747   4812   4548    771   -405     -8       O  
ATOM   2705  CB  GLU A 363     -45.389 -25.190 -15.626  1.00 54.86           C  
ANISOU 2705  CB  GLU A 363    10425   5607   4813   1037   -385   -124       C  
ATOM   2706  CG  GLU A 363     -45.494 -24.299 -14.389  1.00 68.95           C  
ANISOU 2706  CG  GLU A 363    12653   7221   6324   1376   -409   -256       C  
ATOM   2707  CD  GLU A 363     -46.689 -24.638 -13.509  1.00 75.98           C  
ANISOU 2707  CD  GLU A 363    13606   8243   7019   1818    -88    -52       C  
ATOM   2708  OE1 GLU A 363     -47.819 -24.211 -13.832  1.00 79.47           O  
ANISOU 2708  OE1 GLU A 363    13964   8724   7508   2009    149    178       O  
ATOM   2709  OE2 GLU A 363     -46.499 -25.337 -12.491  1.00 77.91           O  
ANISOU 2709  OE2 GLU A 363    13954   8575   7075   1993    -56    -66       O  
ATOM   2710  N   ILE A 364     -45.706 -25.120 -18.907  1.00 49.42           N  
ANISOU 2710  N   ILE A 364     9238   4974   4565    475   -392    103       N  
ATOM   2711  CA  ILE A 364     -45.402 -24.526 -20.206  1.00 50.43           C  
ANISOU 2711  CA  ILE A 364     9296   5051   4813    261   -453    120       C  
ATOM   2712  C   ILE A 364     -46.654 -23.885 -20.792  1.00 50.50           C  
ANISOU 2712  C   ILE A 364     9269   5029   4888    310   -371    302       C  
ATOM   2713  O   ILE A 364     -46.628 -22.741 -21.272  1.00 45.37           O  
ANISOU 2713  O   ILE A 364     8684   4258   4298    271   -404    298       O  
ATOM   2714  CB  ILE A 364     -44.807 -25.582 -21.153  1.00 50.54           C  
ANISOU 2714  CB  ILE A 364     9183   5171   4850     90   -472    139       C  
ATOM   2715  CG1 ILE A 364     -43.380 -25.928 -20.725  1.00 54.28           C  
ANISOU 2715  CG1 ILE A 364     9639   5680   5306     55   -534     15       C  
ATOM   2716  CG2 ILE A 364     -44.838 -25.094 -22.590  1.00 50.93           C  
ANISOU 2716  CG2 ILE A 364     9193   5199   4958    -54   -476    224       C  
ATOM   2717  CD1 ILE A 364     -42.720 -26.973 -21.598  1.00 59.29           C  
ANISOU 2717  CD1 ILE A 364    10197   6416   5913      3   -487     48       C  
ATOM   2718  N   ARG A 365     -47.778 -24.608 -20.745  1.00 53.97           N  
ANISOU 2718  N   ARG A 365     9580   5572   5353    385   -288    518       N  
ATOM   2719  CA  ARG A 365     -49.038 -24.021 -21.192  1.00 56.62           C  
ANISOU 2719  CA  ARG A 365     9813   5906   5792    452   -216    780       C  
ATOM   2720  C   ARG A 365     -49.380 -22.768 -20.393  1.00 57.93           C  
ANISOU 2720  C   ARG A 365    10151   5968   5892    761    -79    763       C  
ATOM   2721  O   ARG A 365     -49.852 -21.771 -20.957  1.00 54.06           O  
ANISOU 2721  O   ARG A 365     9676   5390   5476    792    -56    856       O  
ATOM   2722  CB  ARG A 365     -50.163 -25.050 -21.088  1.00 61.25           C  
ANISOU 2722  CB  ARG A 365    10171   6628   6474    467   -191   1111       C  
ATOM   2723  CG  ARG A 365     -50.067 -26.163 -22.112  1.00 64.43           C  
ANISOU 2723  CG  ARG A 365    10513   7033   6933    154   -414   1152       C  
ATOM   2724  CD  ARG A 365     -51.411 -26.832 -22.323  1.00 71.30           C  
ANISOU 2724  CD  ARG A 365    11142   7959   7989     71   -515   1582       C  
ATOM   2725  NE  ARG A 365     -51.790 -27.668 -21.190  1.00 76.23           N  
ANISOU 2725  NE  ARG A 365    11627   8687   8652    205   -426   1770       N  
ATOM   2726  CZ  ARG A 365     -51.510 -28.964 -21.097  1.00 77.30           C  
ANISOU 2726  CZ  ARG A 365    11788   8798   8784     53   -590   1753       C  
ATOM   2727  NH1 ARG A 365     -50.847 -29.571 -22.073  1.00 75.71           N  
ANISOU 2727  NH1 ARG A 365    11800   8461   8506   -189   -836   1533       N  
ATOM   2728  NH2 ARG A 365     -51.893 -29.653 -20.031  1.00 76.95           N  
ANISOU 2728  NH2 ARG A 365    11590   8858   8791    185   -490   1976       N  
ATOM   2729  N   LYS A 366     -49.138 -22.794 -19.080  1.00 60.18           N  
ANISOU 2729  N   LYS A 366    10630   6233   6003   1025      2    639       N  
ATOM   2730  CA  LYS A 366     -49.426 -21.624 -18.255  1.00 59.84           C  
ANISOU 2730  CA  LYS A 366    10906   6027   5803   1397    112    580       C  
ATOM   2731  C   LYS A 366     -48.534 -20.448 -18.637  1.00 56.98           C  
ANISOU 2731  C   LYS A 366    10811   5392   5449   1241   -109    319       C  
ATOM   2732  O   LYS A 366     -48.982 -19.295 -18.633  1.00 55.59           O  
ANISOU 2732  O   LYS A 366    10855   5026   5241   1444    -67    337       O  
ATOM   2733  CB  LYS A 366     -49.261 -21.975 -16.775  1.00 60.50           C  
ANISOU 2733  CB  LYS A 366    11238   6124   5623   1725    203    477       C  
ATOM   2734  CG  LYS A 366     -49.859 -20.949 -15.822  1.00 69.23           C  
ANISOU 2734  CG  LYS A 366    12757   7078   6471   2267    392    479       C  
ATOM   2735  CD  LYS A 366     -50.111 -21.555 -14.445  1.00 73.15           C  
ANISOU 2735  CD  LYS A 366    13418   7694   6681   2688    600    535       C  
ATOM   2736  CE  LYS A 366     -51.044 -20.682 -13.615  1.00 79.10           C  
ANISOU 2736  CE  LYS A 366    14540   8370   7144   3369    930    675       C  
ATOM   2737  NZ  LYS A 366     -51.497 -21.361 -12.365  1.00 81.75           N  
ANISOU 2737  NZ  LYS A 366    14958   8905   7197   3853   1241    863       N  
ATOM   2738  N   ALA A 367     -47.274 -20.719 -18.981  1.00 56.92           N  
ANISOU 2738  N   ALA A 367    10767   5355   5504    894   -343    130       N  
ATOM   2739  CA  ALA A 367     -46.371 -19.645 -19.379  1.00 51.08           C  
ANISOU 2739  CA  ALA A 367    10191   4371   4847    686   -586    -12       C  
ATOM   2740  C   ALA A 367     -46.813 -19.018 -20.694  1.00 57.67           C  
ANISOU 2740  C   ALA A 367    10856   5192   5864    536   -549    159       C  
ATOM   2741  O   ALA A 367     -46.787 -17.788 -20.840  1.00 61.78           O  
ANISOU 2741  O   ALA A 367    11585   5460   6427    550   -651    134       O  
ATOM   2742  CB  ALA A 367     -44.940 -20.169 -19.483  1.00 50.09           C  
ANISOU 2742  CB  ALA A 367     9945   4289   4799    368   -799   -121       C  
ATOM   2743  N   LEU A 368     -47.228 -19.842 -21.660  1.00 53.65           N  
ANISOU 2743  N   LEU A 368    10021   4917   5447    394   -442    337       N  
ATOM   2744  CA  LEU A 368     -47.725 -19.285 -22.916  1.00 53.03           C  
ANISOU 2744  CA  LEU A 368     9815   4833   5500    271   -426    517       C  
ATOM   2745  C   LEU A 368     -48.994 -18.470 -22.695  1.00 52.35           C  
ANISOU 2745  C   LEU A 368     9806   4662   5422    561   -290    679       C  
ATOM   2746  O   LEU A 368     -49.141 -17.369 -23.245  1.00 54.91           O  
ANISOU 2746  O   LEU A 368    10212   4822   5828    549   -327    734       O  
ATOM   2747  CB  LEU A 368     -47.968 -20.400 -23.934  1.00 49.21           C  
ANISOU 2747  CB  LEU A 368     9082   4568   5047     88   -409    659       C  
ATOM   2748  CG  LEU A 368     -46.805 -20.679 -24.888  1.00 49.22           C  
ANISOU 2748  CG  LEU A 368     9031   4619   5053   -166   -490    600       C  
ATOM   2749  CD1 LEU A 368     -45.555 -21.088 -24.121  1.00 45.74           C  
ANISOU 2749  CD1 LEU A 368     8617   4188   4573   -194   -538    419       C  
ATOM   2750  CD2 LEU A 368     -47.192 -21.740 -25.909  1.00 48.95           C  
ANISOU 2750  CD2 LEU A 368     8916   4727   4957   -264   -498    714       C  
ATOM   2751  N   ALA A 369     -49.919 -18.989 -21.882  1.00 51.15           N  
ANISOU 2751  N   ALA A 369     9611   4629   5195    856   -108    809       N  
ATOM   2752  CA  ALA A 369     -51.122 -18.229 -21.561  1.00 53.75           C  
ANISOU 2752  CA  ALA A 369     9988   4913   5521   1236     97   1036       C  
ATOM   2753  C   ALA A 369     -50.787 -16.924 -20.851  1.00 66.28           C  
ANISOU 2753  C   ALA A 369    12058   6168   6958   1509     76    813       C  
ATOM   2754  O   ALA A 369     -51.515 -15.935 -20.993  1.00 72.87           O  
ANISOU 2754  O   ALA A 369    13009   6866   7812   1766    187    954       O  
ATOM   2755  CB  ALA A 369     -52.068 -19.071 -20.707  1.00 54.76           C  
ANISOU 2755  CB  ALA A 369     9944   5264   5598   1544    338   1291       C  
ATOM   2756  N   GLU A 370     -49.689 -16.897 -20.090  1.00 65.65           N  
ANISOU 2756  N   GLU A 370    12294   5922   6729   1458   -110    480       N  
ATOM   2757  CA  GLU A 370     -49.285 -15.666 -19.420  1.00 68.22           C  
ANISOU 2757  CA  GLU A 370    13181   5840   6901   1657   -267    244       C  
ATOM   2758  C   GLU A 370     -48.719 -14.660 -20.415  1.00 65.39           C  
ANISOU 2758  C   GLU A 370    12851   5239   6753   1315   -523    218       C  
ATOM   2759  O   GLU A 370     -49.036 -13.465 -20.348  1.00 66.70           O  
ANISOU 2759  O   GLU A 370    13378   5081   6885   1525   -566    200       O  
ATOM   2760  CB  GLU A 370     -48.266 -15.977 -18.324  1.00 73.77           C  
ANISOU 2760  CB  GLU A 370    14209   6417   7402   1641   -489    -62       C  
ATOM   2761  CG  GLU A 370     -48.239 -14.958 -17.198  1.00 81.47           C  
ANISOU 2761  CG  GLU A 370    15919   6969   8068   2049   -614   -292       C  
ATOM   2762  CD  GLU A 370     -47.085 -15.173 -16.239  1.00 85.31           C  
ANISOU 2762  CD  GLU A 370    16756   7275   8384   1924   -980   -593       C  
ATOM   2763  OE1 GLU A 370     -46.027 -15.666 -16.683  1.00 83.98           O  
ANISOU 2763  OE1 GLU A 370    16259   7205   8446   1411  -1237   -620       O  
ATOM   2764  OE2 GLU A 370     -47.235 -14.848 -15.042  1.00 92.06           O  
ANISOU 2764  OE2 GLU A 370    18234   7891   8855   2372  -1009   -775       O  
ATOM   2765  N   ARG A 371     -47.879 -15.125 -21.346  1.00 63.26           N  
ANISOU 2765  N   ARG A 371    13948   5401   4686    -30   -489    860       N  
ATOM   2766  CA  ARG A 371     -47.402 -14.250 -22.413  1.00 58.21           C  
ANISOU 2766  CA  ARG A 371    12737   4979   4401      0   -577    780       C  
ATOM   2767  C   ARG A 371     -48.566 -13.645 -23.184  1.00 54.67           C  
ANISOU 2767  C   ARG A 371    12004   4662   4105    -45    -96    699       C  
ATOM   2768  O   ARG A 371     -48.557 -12.449 -23.499  1.00 52.08           O  
ANISOU 2768  O   ARG A 371    11503   4420   3866    -70    -57    617       O  
ATOM   2769  CB  ARG A 371     -46.482 -15.020 -23.360  1.00 54.57           C  
ANISOU 2769  CB  ARG A 371    11820   4624   4291    129   -827    834       C  
ATOM   2770  CG  ARG A 371     -45.017 -15.025 -22.948  1.00 63.44           C  
ANISOU 2770  CG  ARG A 371    12924   5705   5474    199  -1387    910       C  
ATOM   2771  CD  ARG A 371     -44.356 -13.677 -23.203  1.00 59.00           C  
ANISOU 2771  CD  ARG A 371    12087   5261   5067    130  -1581    840       C  
ATOM   2772  NE  ARG A 371     -44.292 -13.357 -24.626  1.00 59.95           N  
ANISOU 2772  NE  ARG A 371    11614   5587   5576    176  -1376    781       N  
ATOM   2773  CZ  ARG A 371     -43.290 -13.702 -25.430  1.00 58.06           C  
ANISOU 2773  CZ  ARG A 371    10917   5440   5705    297  -1541    834       C  
ATOM   2774  NH1 ARG A 371     -42.256 -14.382 -24.949  1.00 58.75           N  
ANISOU 2774  NH1 ARG A 371    10996   5444   5884    405  -1938    961       N  
ATOM   2775  NH2 ARG A 371     -43.320 -13.368 -26.715  1.00 51.16           N  
ANISOU 2775  NH2 ARG A 371     9605   4722   5110    321  -1297    773       N  
ATOM   2776  N   VAL A 372     -49.583 -14.453 -23.490  1.00 53.11           N  
ANISOU 2776  N   VAL A 372    11757   4466   3957    -65    250    737       N  
ATOM   2777  CA  VAL A 372     -50.743 -13.923 -24.200  1.00 53.52           C  
ANISOU 2777  CA  VAL A 372    11501   4638   4196   -113    655    698       C  
ATOM   2778  C   VAL A 372     -51.493 -12.919 -23.330  1.00 57.59           C  
ANISOU 2778  C   VAL A 372    12316   5058   4509   -152    962    661       C  
ATOM   2779  O   VAL A 372     -51.909 -11.855 -23.806  1.00 58.12           O  
ANISOU 2779  O   VAL A 372    12134   5217   4732   -137   1131    604       O  
ATOM   2780  CB  VAL A 372     -51.654 -15.070 -24.664  1.00 54.23           C  
ANISOU 2780  CB  VAL A 372    11471   4733   4402   -171    900    768       C  
ATOM   2781  CG1 VAL A 372     -52.937 -14.523 -25.266  1.00 54.10           C  
ANISOU 2781  CG1 VAL A 372    11127   4828   4601   -238   1274    765       C  
ATOM   2782  CG2 VAL A 372     -50.916 -15.935 -25.664  1.00 53.79           C  
ANISOU 2782  CG2 VAL A 372    11152   4745   4543   -116    642    777       C  
ATOM   2783  N   ALA A 373     -51.669 -13.233 -22.043  1.00 55.36           N  
ANISOU 2783  N   ALA A 373    12618   4558   3858   -189   1058    696       N  
ATOM   2784  CA  ALA A 373     -52.366 -12.315 -21.147  1.00 61.19           C  
ANISOU 2784  CA  ALA A 373    13730   5152   4366   -209   1416    647       C  
ATOM   2785  C   ALA A 373     -51.649 -10.975 -21.037  1.00 65.63           C  
ANISOU 2785  C   ALA A 373    14392   5702   4843   -190   1190    543       C  
ATOM   2786  O   ALA A 373     -52.295  -9.941 -20.835  1.00 64.37           O  
ANISOU 2786  O   ALA A 373    14329   5481   4648   -169   1532    481       O  
ATOM   2787  CB  ALA A 373     -52.524 -12.943 -19.764  1.00 66.96           C  
ANISOU 2787  CB  ALA A 373    14956   5658   4829   -246   1472    612       C  
ATOM   2788  N   THR A 374     -50.322 -10.968 -21.172  1.00 65.58           N  
ANISOU 2788  N   THR A 374    14339   5739   4842   -196    627    528       N  
ATOM   2789  CA  THR A 374     -49.578  -9.720 -21.047  1.00 63.65           C  
ANISOU 2789  CA  THR A 374    14178   5467   4538   -230    364    435       C  
ATOM   2790  C   THR A 374     -49.553  -8.943 -22.358  1.00 56.83           C  
ANISOU 2790  C   THR A 374    12680   4824   4090   -190    400    386       C  
ATOM   2791  O   THR A 374     -49.814  -7.734 -22.380  1.00 54.70           O  
ANISOU 2791  O   THR A 374    12459   4513   3813   -197    557    305       O  
ATOM   2792  CB  THR A 374     -48.152 -10.004 -20.578  1.00 64.27           C  
ANISOU 2792  CB  THR A 374    14438   5489   4491   -281   -282    469       C  
ATOM   2793  OG1 THR A 374     -48.190 -10.659 -19.304  1.00 62.87           O  
ANISOU 2793  OG1 THR A 374    14887   5080   3922   -322   -349    507       O  
ATOM   2794  CG2 THR A 374     -47.365  -8.705 -20.455  1.00 63.98           C  
ANISOU 2794  CG2 THR A 374    14473   5416   4421   -374   -594    381       C  
ATOM   2795  N   ASP A 375     -49.242  -9.621 -23.464  1.00 56.06           N  
ANISOU 2795  N   ASP A 375    12040   4929   4331   -144    271    435       N  
ATOM   2796  CA  ASP A 375     -48.946  -8.911 -24.705  1.00 56.29           C  
ANISOU 2796  CA  ASP A 375    11543   5142   4701   -124    220    398       C  
ATOM   2797  C   ASP A 375     -50.200  -8.495 -25.470  1.00 53.26           C  
ANISOU 2797  C   ASP A 375    10881   4848   4507    -83    652    393       C  
ATOM   2798  O   ASP A 375     -50.170  -7.489 -26.187  1.00 55.87           O  
ANISOU 2798  O   ASP A 375    10966   5253   5009    -72    676    352       O  
ATOM   2799  CB  ASP A 375     -48.047  -9.774 -25.591  1.00 57.90           C  
ANISOU 2799  CB  ASP A 375    11347   5491   5162    -83    -61    450       C  
ATOM   2800  CG  ASP A 375     -46.743 -10.155 -24.906  1.00 66.63           C  
ANISOU 2800  CG  ASP A 375    12617   6519   6182    -93   -530    491       C  
ATOM   2801  OD1 ASP A 375     -46.382  -9.514 -23.895  1.00 73.05           O  
ANISOU 2801  OD1 ASP A 375    13820   7190   6747   -176   -732    465       O  
ATOM   2802  OD2 ASP A 375     -46.073 -11.096 -25.384  1.00 66.34           O  
ANISOU 2802  OD2 ASP A 375    12329   6544   6331    -14   -709    558       O  
ATOM   2803  N   PHE A 376     -51.301  -9.232 -25.337  1.00 53.19           N  
ANISOU 2803  N   PHE A 376    10893   4824   4492    -69    976    452       N  
ATOM   2804  CA  PHE A 376     -52.527  -8.934 -26.064  1.00 50.25           C  
ANISOU 2804  CA  PHE A 376    10186   4542   4363    -39   1331    487       C  
ATOM   2805  C   PHE A 376     -53.562  -8.217 -25.206  1.00 52.38           C  
ANISOU 2805  C   PHE A 376    10716   4663   4523      3   1764    486       C  
ATOM   2806  O   PHE A 376     -54.743  -8.195 -25.566  1.00 54.67           O  
ANISOU 2806  O   PHE A 376    10732   5002   5039     37   2105    559       O  
ATOM   2807  CB  PHE A 376     -53.131 -10.218 -26.637  1.00 46.37           C  
ANISOU 2807  CB  PHE A 376     9451   4138   4028    -81   1403    576       C  
ATOM   2808  CG  PHE A 376     -52.400 -10.759 -27.827  1.00 49.66           C  
ANISOU 2808  CG  PHE A 376     9550   4699   4621    -92   1104    573       C  
ATOM   2809  CD1 PHE A 376     -51.251 -11.518 -27.666  1.00 55.06           C  
ANISOU 2809  CD1 PHE A 376    10362   5351   5208    -78    804    562       C  
ATOM   2810  CD2 PHE A 376     -52.868 -10.522 -29.108  1.00 51.27           C  
ANISOU 2810  CD2 PHE A 376     9351   5046   5085   -103   1133    593       C  
ATOM   2811  CE1 PHE A 376     -50.578 -12.024 -28.766  1.00 55.98           C  
ANISOU 2811  CE1 PHE A 376    10206   5566   5496    -56    614    558       C  
ATOM   2812  CE2 PHE A 376     -52.201 -11.022 -30.210  1.00 53.83           C  
ANISOU 2812  CE2 PHE A 376     9474   5463   5518   -113    914    581       C  
ATOM   2813  CZ  PHE A 376     -51.055 -11.774 -30.039  1.00 55.51           C  
ANISOU 2813  CZ  PHE A 376     9815   5633   5644    -80    693    557       C  
ATOM   2814  N   VAL A 377     -53.147  -7.629 -24.082  1.00 51.75           N  
ANISOU 2814  N   VAL A 377    11168   4384   4110      0   1761    413       N  
ATOM   2815  CA  VAL A 377     -54.104  -6.973 -23.202  1.00 54.72           C  
ANISOU 2815  CA  VAL A 377    11888   4565   4338     61   2248    400       C  
ATOM   2816  C   VAL A 377     -54.653  -5.690 -23.817  1.00 61.73           C  
ANISOU 2816  C   VAL A 377    12502   5477   5476    173   2471    379       C  
ATOM   2817  O   VAL A 377     -55.750  -5.247 -23.450  1.00 56.80           O  
ANISOU 2817  O   VAL A 377    11927   4740   4912    280   2978    414       O  
ATOM   2818  CB  VAL A 377     -53.462  -6.697 -21.828  1.00 64.60           C  
ANISOU 2818  CB  VAL A 377    13907   5550   5088      6   2154    315       C  
ATOM   2819  CG1 VAL A 377     -52.440  -5.569 -21.923  1.00 68.46           C  
ANISOU 2819  CG1 VAL A 377    14515   5997   5499    -31   1787    204       C  
ATOM   2820  CG2 VAL A 377     -54.526  -6.377 -20.793  1.00 61.52           C  
ANISOU 2820  CG2 VAL A 377    13976   4914   4486     71   2755    310       C  
ATOM   2821  N   ASN A 378     -53.925  -5.089 -24.765  1.00 56.16           N  
ANISOU 2821  N   ASN A 378    11497   4901   4939    163   2130    340       N  
ATOM   2822  CA  ASN A 378     -54.316  -3.805 -25.344  1.00 55.65           C  
ANISOU 2822  CA  ASN A 378    11242   4826   5078    268   2286    325       C  
ATOM   2823  C   ASN A 378     -53.717  -3.735 -26.753  1.00 56.55           C  
ANISOU 2823  C   ASN A 378    10858   5165   5463    230   1926    346       C  
ATOM   2824  O   ASN A 378     -52.709  -3.071 -27.002  1.00 63.22           O  
ANISOU 2824  O   ASN A 378    11762   6000   6259    170   1635    273       O  
ATOM   2825  CB  ASN A 378     -53.852  -2.639 -24.473  1.00 60.27           C  
ANISOU 2825  CB  ASN A 378    12391   5150   5360    271   2313    199       C  
ATOM   2826  CG  ASN A 378     -54.405  -1.310 -24.934  1.00 65.94           C  
ANISOU 2826  CG  ASN A 378    12995   5790   6270    413   2563    192       C  
ATOM   2827  OD1 ASN A 378     -55.221  -1.251 -25.852  1.00 59.31           O  
ANISOU 2827  OD1 ASN A 378    11640   5093   5802    528   2723    301       O  
ATOM   2828  ND2 ASN A 378     -53.974  -0.232 -24.287  1.00 57.24           N  
ANISOU 2828  ND2 ASN A 378    12406   4433   4909    399   2573     71       N  
ATOM   2829  N   VAL A 379     -54.357  -4.441 -27.688  1.00 53.09           N  
ANISOU 2829  N   VAL A 379     9951   4915   5308    242   1956    453       N  
ATOM   2830  CA  VAL A 379     -53.805  -4.574 -29.033  1.00 52.27           C  
ANISOU 2830  CA  VAL A 379     9462   5001   5396    192   1641    474       C  
ATOM   2831  C   VAL A 379     -53.876  -3.248 -29.786  1.00 49.46           C  
ANISOU 2831  C   VAL A 379     8957   4639   5195    263   1651    476       C  
ATOM   2832  O   VAL A 379     -52.911  -2.846 -30.447  1.00 44.47           O  
ANISOU 2832  O   VAL A 379     8268   4057   4572    203   1390    434       O  
ATOM   2833  CB  VAL A 379     -54.529  -5.699 -29.795  1.00 54.54           C  
ANISOU 2833  CB  VAL A 379     9393   5445   5886    154   1650    582       C  
ATOM   2834  CG1 VAL A 379     -54.036  -5.771 -31.227  1.00 57.14           C  
ANISOU 2834  CG1 VAL A 379     9422   5928   6362    106   1372    597       C  
ATOM   2835  CG2 VAL A 379     -54.322  -7.030 -29.095  1.00 55.50           C  
ANISOU 2835  CG2 VAL A 379     9707   5542   5838     73   1616    579       C  
ATOM   2836  N   GLY A 380     -55.007  -2.547 -29.694  1.00 51.96           N  
ANISOU 2836  N   GLY A 380     9206   4879   5659    400   1972    542       N  
ATOM   2837  CA  GLY A 380     -55.224  -1.333 -30.456  1.00 56.58           C  
ANISOU 2837  CA  GLY A 380     9642   5437   6419    499   1990    577       C  
ATOM   2838  C   GLY A 380     -54.785  -0.038 -29.809  1.00 59.89           C  
ANISOU 2838  C   GLY A 380    10459   5627   6670    551   2082    472       C  
ATOM   2839  O   GLY A 380     -54.797   1.004 -30.470  1.00 60.79           O  
ANISOU 2839  O   GLY A 380    10500   5692   6905    618   2064    496       O  
ATOM   2840  N   GLY A 381     -54.397  -0.074 -28.536  1.00 61.20           N  
ANISOU 2840  N   GLY A 381    11097   5624   6533    507   2161    360       N  
ATOM   2841  CA  GLY A 381     -53.995   1.111 -27.812  1.00 60.23           C  
ANISOU 2841  CA  GLY A 381    11457   5235   6193    518   2233    244       C  
ATOM   2842  C   GLY A 381     -52.840   1.876 -28.435  1.00 59.57           C  
ANISOU 2842  C   GLY A 381    11386   5152   6096    382   1875    183       C  
ATOM   2843  O   GLY A 381     -52.963   3.061 -28.767  1.00 58.86           O  
ANISOU 2843  O   GLY A 381    11365   4924   6077    453   1965    178       O  
ATOM   2844  N   PRO A 382     -51.684   1.218 -28.592  1.00 56.95           N  
ANISOU 2844  N   PRO A 382    10983   4958   5695    189   1483    148       N  
ATOM   2845  CA  PRO A 382     -50.500   1.944 -29.087  1.00 57.18           C  
ANISOU 2845  CA  PRO A 382    11008   4975   5741     29   1172    101       C  
ATOM   2846  C   PRO A 382     -50.669   2.556 -30.469  1.00 56.74           C  
ANISOU 2846  C   PRO A 382    10598   5010   5949     82   1192    183       C  
ATOM   2847  O   PRO A 382     -50.180   3.670 -30.702  1.00 58.32           O  
ANISOU 2847  O   PRO A 382    10934   5075   6149     12   1132    148       O  
ATOM   2848  CB  PRO A 382     -49.407   0.867 -29.070  1.00 52.15           C  
ANISOU 2848  CB  PRO A 382    10227   4506   5081   -129    814     96       C  
ATOM   2849  CG  PRO A 382     -49.839  -0.078 -28.004  1.00 51.17           C  
ANISOU 2849  CG  PRO A 382    10339   4345   4757    -88    900     85       C  
ATOM   2850  CD  PRO A 382     -51.336  -0.131 -28.111  1.00 51.41           C  
ANISOU 2850  CD  PRO A 382    10281   4372   4882    108   1329    150       C  
ATOM   2851  N   ILE A 383     -51.340   1.869 -31.398  1.00 54.30           N  
ANISOU 2851  N   ILE A 383     9886   4903   5842    178   1253    295       N  
ATOM   2852  CA  ILE A 383     -51.504   2.446 -32.730  1.00 54.45           C  
ANISOU 2852  CA  ILE A 383     9644   4984   6059    215   1232    386       C  
ATOM   2853  C   ILE A 383     -52.482   3.614 -32.689  1.00 59.10           C  
ANISOU 2853  C   ILE A 383    10346   5382   6726    401   1488    435       C  
ATOM   2854  O   ILE A 383     -52.361   4.562 -33.477  1.00 55.99           O  
ANISOU 2854  O   ILE A 383     9939   4918   6415    413   1454    480       O  
ATOM   2855  CB  ILE A 383     -51.938   1.375 -33.751  1.00 48.92           C  
ANISOU 2855  CB  ILE A 383     8556   4523   5510    234   1168    493       C  
ATOM   2856  CG1 ILE A 383     -51.802   1.920 -35.177  1.00 52.80           C  
ANISOU 2856  CG1 ILE A 383     8877   5063   6120    216   1072    577       C  
ATOM   2857  CG2 ILE A 383     -53.368   0.929 -33.503  1.00 43.31           C  
ANISOU 2857  CG2 ILE A 383     7710   3835   4911    391   1380    584       C  
ATOM   2858  CD1 ILE A 383     -52.208   0.936 -36.256  1.00 54.44           C  
ANISOU 2858  CD1 ILE A 383     8807   5461   6416    204    975    674       C  
ATOM   2859  N   LYS A 384     -53.455   3.576 -31.774  1.00 64.78           N  
ANISOU 2859  N   LYS A 384    11195   5990   7429    563   1780    437       N  
ATOM   2860  CA  LYS A 384     -54.334   4.725 -31.592  1.00 70.45           C  
ANISOU 2860  CA  LYS A 384    12050   6477   8239    784   2084    480       C  
ATOM   2861  C   LYS A 384     -53.565   5.910 -31.026  1.00 69.13           C  
ANISOU 2861  C   LYS A 384    12386   6025   7857    708   2081    343       C  
ATOM   2862  O   LYS A 384     -53.770   7.053 -31.453  1.00 74.22           O  
ANISOU 2862  O   LYS A 384    13118   6493   8590    812   2169    382       O  
ATOM   2863  CB  LYS A 384     -55.503   4.354 -30.679  1.00 79.56           C  
ANISOU 2863  CB  LYS A 384    13227   7561   9442    977   2473    516       C  
ATOM   2864  CG  LYS A 384     -56.495   5.480 -30.460  1.00 89.09           C  
ANISOU 2864  CG  LYS A 384    14534   8512  10804   1266   2868    580       C  
ATOM   2865  CD  LYS A 384     -57.095   5.937 -31.778  1.00 95.38           C  
ANISOU 2865  CD  LYS A 384    14887   9398  11956   1407   2771    772       C  
ATOM   2866  CE  LYS A 384     -58.103   7.053 -31.569  1.00104.40           C  
ANISOU 2866  CE  LYS A 384    16085  10268  13312   1745   3165    866       C  
ATOM   2867  NZ  LYS A 384     -58.673   7.525 -32.861  1.00107.80           N  
ANISOU 2867  NZ  LYS A 384    16100  10769  14089   1890   3002   1082       N  
ATOM   2868  N   ALA A 385     -52.667   5.653 -30.071  1.00 68.54           N  
ANISOU 2868  N   ALA A 385    12666   5882   7495    511   1945    194       N  
ATOM   2869  CA  ALA A 385     -51.814   6.715 -29.550  1.00 67.04           C  
ANISOU 2869  CA  ALA A 385    12967   5419   7088    358   1844     61       C  
ATOM   2870  C   ALA A 385     -50.912   7.288 -30.636  1.00 62.10           C  
ANISOU 2870  C   ALA A 385    12155   4854   6585    187   1561     92       C  
ATOM   2871  O   ALA A 385     -50.634   8.493 -30.641  1.00 55.40           O  
ANISOU 2871  O   ALA A 385    11614   3750   5685    137   1578     48       O  
ATOM   2872  CB  ALA A 385     -50.980   6.189 -28.381  1.00 60.52           C  
ANISOU 2872  CB  ALA A 385    12513   4539   5945    141   1640    -75       C  
ATOM   2873  N   LEU A 386     -50.454   6.446 -31.568  1.00 59.23           N  
ANISOU 2873  N   LEU A 386    11331   4797   6376     93   1337    170       N  
ATOM   2874  CA  LEU A 386     -49.648   6.946 -32.677  1.00 57.66           C  
ANISOU 2874  CA  LEU A 386    10957   4652   6301    -58   1150    217       C  
ATOM   2875  C   LEU A 386     -50.478   7.810 -33.619  1.00 58.61           C  
ANISOU 2875  C   LEU A 386    11008   4686   6576    132   1327    338       C  
ATOM   2876  O   LEU A 386     -50.025   8.878 -34.050  1.00 64.06           O  
ANISOU 2876  O   LEU A 386    11862   5205   7273     43   1296    344       O  
ATOM   2877  CB  LEU A 386     -49.014   5.783 -33.437  1.00 55.43           C  
ANISOU 2877  CB  LEU A 386    10252   4683   6124   -168    947    268       C  
ATOM   2878  CG  LEU A 386     -48.242   6.167 -34.703  1.00 58.28           C  
ANISOU 2878  CG  LEU A 386    10416   5111   6617   -305    841    335       C  
ATOM   2879  CD1 LEU A 386     -47.017   7.006 -34.366  1.00 56.98           C  
ANISOU 2879  CD1 LEU A 386    10446   4787   6418   -570    685    260       C  
ATOM   2880  CD2 LEU A 386     -47.848   4.930 -35.487  1.00 57.14           C  
ANISOU 2880  CD2 LEU A 386     9898   5246   6565   -342    747    388       C  
ATOM   2881  N   GLU A 387     -51.696   7.367 -33.950  1.00 56.48           N  
ANISOU 2881  N   GLU A 387    10491   4520   6448    381   1490    454       N  
ATOM   2882  CA  GLU A 387     -52.551   8.166 -34.823  1.00 59.24           C  
ANISOU 2882  CA  GLU A 387    10751   4783   6977    586   1603    605       C  
ATOM   2883  C   GLU A 387     -52.889   9.510 -34.185  1.00 65.26           C  
ANISOU 2883  C   GLU A 387    11927   5174   7695    728   1837    565       C  
ATOM   2884  O   GLU A 387     -52.895  10.544 -34.864  1.00 68.52           O  
ANISOU 2884  O   GLU A 387    12444   5418   8172    774   1840    640       O  
ATOM   2885  CB  GLU A 387     -53.830   7.401 -35.165  1.00 60.44           C  
ANISOU 2885  CB  GLU A 387    10522   5110   7333    808   1689    754       C  
ATOM   2886  CG  GLU A 387     -54.685   8.086 -36.226  1.00 65.61           C  
ANISOU 2886  CG  GLU A 387    11004   5714   8209   1006   1691    956       C  
ATOM   2887  CD  GLU A 387     -56.097   7.533 -36.299  1.00 70.37           C  
ANISOU 2887  CD  GLU A 387    11232   6428   9079   1242   1790   1121       C  
ATOM   2888  OE1 GLU A 387     -56.708   7.306 -35.233  1.00 75.02           O  
ANISOU 2888  OE1 GLU A 387    11834   6956   9714   1378   2069   1081       O  
ATOM   2889  OE2 GLU A 387     -56.595   7.324 -37.424  1.00 70.81           O  
ANISOU 2889  OE2 GLU A 387    10991   6617   9296   1275   1585   1300       O  
ATOM   2890  N   ASP A 388     -53.172   9.516 -32.880  1.00 66.16           N  
ANISOU 2890  N   ASP A 388    12342   5123   7673    802   2056    447       N  
ATOM   2891  CA  ASP A 388     -53.426  10.779 -32.193  1.00 74.11           C  
ANISOU 2891  CA  ASP A 388    13850   5722   8584    931   2317    378       C  
ATOM   2892  C   ASP A 388     -52.175  11.645 -32.133  1.00 71.97           C  
ANISOU 2892  C   ASP A 388    13983   5248   8113    628   2104    253       C  
ATOM   2893  O   ASP A 388     -52.273  12.877 -32.178  1.00 75.57           O  
ANISOU 2893  O   ASP A 388    14787   5373   8553    700   2235    248       O  
ATOM   2894  CB  ASP A 388     -53.960  10.520 -30.784  1.00 83.81           C  
ANISOU 2894  CB  ASP A 388    15398   6797   9650   1055   2632    267       C  
ATOM   2895  CG  ASP A 388     -55.308   9.829 -30.791  1.00 91.35           C  
ANISOU 2895  CG  ASP A 388    15948   7897  10863   1364   2926    413       C  
ATOM   2896  OD1 ASP A 388     -56.014   9.916 -31.817  1.00 95.56           O  
ANISOU 2896  OD1 ASP A 388    16034   8550  11724   1546   2914    609       O  
ATOM   2897  OD2 ASP A 388     -55.664   9.202 -29.770  1.00 93.29           O  
ANISOU 2897  OD2 ASP A 388    16332   8127  10988   1407   3154    345       O  
ATOM   2898  N   ALA A 389     -50.996  11.025 -32.032  1.00 68.37           N  
ANISOU 2898  N   ALA A 389    13472   4971   7536    288   1776    165       N  
ATOM   2899  CA  ALA A 389     -49.756  11.794 -32.052  1.00 66.99           C  
ANISOU 2899  CA  ALA A 389    13570   4635   7248    -47   1535     78       C  
ATOM   2900  C   ALA A 389     -49.544  12.456 -33.406  1.00 62.28           C  
ANISOU 2900  C   ALA A 389    12780   4048   6837    -81   1481    211       C  
ATOM   2901  O   ALA A 389     -49.054  13.590 -33.481  1.00 61.87           O  
ANISOU 2901  O   ALA A 389    13068   3710   6730   -229   1460    179       O  
ATOM   2902  CB  ALA A 389     -48.572  10.893 -31.701  1.00 68.23           C  
ANISOU 2902  CB  ALA A 389    13587   5011   7327   -373   1186      0       C  
ATOM   2903  N   ALA A 390     -49.912  11.766 -34.488  1.00 63.66           N  
ANISOU 2903  N   ALA A 390    12467   4521   7201     34   1456    364       N  
ATOM   2904  CA  ALA A 390     -49.801  12.361 -35.814  1.00 56.59           C  
ANISOU 2904  CA  ALA A 390    11455   3615   6429     18   1418    508       C  
ATOM   2905  C   ALA A 390     -50.799  13.495 -36.009  1.00 75.29           C  
ANISOU 2905  C   ALA A 390    14066   5679   8861    310   1638    605       C  
ATOM   2906  O   ALA A 390     -50.527  14.434 -36.765  1.00 64.75           O  
ANISOU 2906  O   ALA A 390    12889   4165   7548    248   1619    684       O  
ATOM   2907  CB  ALA A 390     -50.001  11.293 -36.887  1.00 53.82           C  
ANISOU 2907  CB  ALA A 390    10619   3626   6205     63   1321    639       C  
ATOM   2908  N   LEU A 391     -51.949  13.429 -35.341  1.00 60.31           N  
ANISOU 2908  N   LEU A 391    12199   3701   7013    638   1873    615       N  
ATOM   2909  CA  LEU A 391     -52.998  14.428 -35.481  1.00 68.79           C  
ANISOU 2909  CA  LEU A 391    13434   4484   8218    990   2119    734       C  
ATOM   2910  C   LEU A 391     -52.807  15.628 -34.560  1.00 66.86           C  
ANISOU 2910  C   LEU A 391    13796   3807   7801    985   2312    585       C  
ATOM   2911  O   LEU A 391     -53.740  16.421 -34.399  1.00 69.98           O  
ANISOU 2911  O   LEU A 391    14267   4039   8285   1303   2559    639       O  
ATOM   2912  CB  LEU A 391     -54.366  13.792 -35.222  1.00 70.20           C  
ANISOU 2912  CB  LEU A 391    13282   4786   8605   1362   2328    840       C  
ATOM   2913  CG  LEU A 391     -54.866  12.811 -36.281  1.00 73.84           C  
ANISOU 2913  CG  LEU A 391    13152   5630   9275   1413   2124   1030       C  
ATOM   2914  CD1 LEU A 391     -56.155  12.144 -35.823  1.00 74.67           C  
ANISOU 2914  CD1 LEU A 391    12919   5844   9608   1715   2331   1122       C  
ATOM   2915  CD2 LEU A 391     -55.069  13.520 -37.610  1.00 62.39           C  
ANISOU 2915  CD2 LEU A 391    11637   4114   7953   1494   1971   1241       C  
ATOM   2916  N   ALA A 392     -51.632  15.777 -33.955  1.00 69.16           N  
ANISOU 2916  N   ALA A 392    14394   4038   7847    604   2148    392       N  
ATOM   2917  CA  ALA A 392     -51.386  16.905 -33.069  1.00 74.90           C  
ANISOU 2917  CA  ALA A 392    15616   4495   8347    522   2235    231       C  
ATOM   2918  C   ALA A 392     -51.378  18.204 -33.861  1.00 81.75           C  
ANISOU 2918  C   ALA A 392    16607   5175   9279    552   2247    319       C  
ATOM   2919  O   ALA A 392     -50.888  18.255 -34.993  1.00 82.99           O  
ANISOU 2919  O   ALA A 392    16568   5412   9552    406   2061    440       O  
ATOM   2920  CB  ALA A 392     -50.060  16.727 -32.333  1.00 75.25           C  
ANISOU 2920  CB  ALA A 392    15913   4534   8145     61   1953     42       C  
ATOM   2921  N   SER A 393     -51.931  19.257 -33.262  1.00 86.12           N  
ANISOU 2921  N   SER A 393    17517   5467   9737    743   2491    267       N  
ATOM   2922  CA  SER A 393     -51.976  20.543 -33.935  1.00 92.52           C  
ANISOU 2922  CA  SER A 393    18497   6061  10596    794   2519    348       C  
ATOM   2923  C   SER A 393     -50.555  21.063 -34.149  1.00 92.73           C  
ANISOU 2923  C   SER A 393    18747   6018  10470    299   2230    259       C  
ATOM   2924  O   SER A 393     -49.650  20.767 -33.361  1.00 94.36           O  
ANISOU 2924  O   SER A 393    19125   6245  10482    -47   2057     93       O  
ATOM   2925  CB  SER A 393     -52.789  21.551 -33.122  1.00 98.50           C  
ANISOU 2925  CB  SER A 393    19640   6527  11259   1082   2863    296       C  
ATOM   2926  OG  SER A 393     -51.994  22.173 -32.129  1.00 99.18           O  
ANISOU 2926  OG  SER A 393    20277   6411  10997    776   2824     86       O  
ATOM   2927  N   PRO A 394     -50.324  21.829 -35.219  1.00 93.07           N  
ANISOU 2927  N   PRO A 394    18773   5978  10612    243   2158    385       N  
ATOM   2928  CA  PRO A 394     -48.975  22.365 -35.463  1.00 94.15           C  
ANISOU 2928  CA  PRO A 394    19079   6043  10650   -242   1924    323       C  
ATOM   2929  C   PRO A 394     -48.487  23.317 -34.382  1.00100.37           C  
ANISOU 2929  C   PRO A 394    20406   6552  11180   -454   1923    133       C  
ATOM   2930  O   PRO A 394     -47.287  23.619 -34.351  1.00102.76           O  
ANISOU 2930  O   PRO A 394    20817   6813  11413   -911   1685     65       O  
ATOM   2931  CB  PRO A 394     -49.119  23.084 -36.811  1.00 97.80           C  
ANISOU 2931  CB  PRO A 394    19468   6437  11255   -163   1935    521       C  
ATOM   2932  CG  PRO A 394     -50.319  22.465 -37.448  1.00 97.52           C  
ANISOU 2932  CG  PRO A 394    19078   6555  11419    279   2037    708       C  
ATOM   2933  CD  PRO A 394     -51.247  22.128 -36.324  1.00 95.43           C  
ANISOU 2933  CD  PRO A 394    18851   6270  11139    597   2250    618       C  
ATOM   2934  N   SER A 395     -49.368  23.800 -33.503  1.00102.88           N  
ANISOU 2934  N   SER A 395    21059   6671  11358   -148   2188     59       N  
ATOM   2935  CA  SER A 395     -48.955  24.688 -32.424  1.00107.81           C  
ANISOU 2935  CA  SER A 395    22276   7013  11673   -346   2198   -118       C  
ATOM   2936  C   SER A 395     -48.253  23.951 -31.293  1.00107.58           C  
ANISOU 2936  C   SER A 395    22374   7084  11419   -655   1989   -287       C  
ATOM   2937  O   SER A 395     -47.504  24.577 -30.537  1.00113.59           O  
ANISOU 2937  O   SER A 395    23584   7654  11921   -985   1828   -418       O  
ATOM   2938  CB  SER A 395     -50.166  25.436 -31.862  1.00109.39           C  
ANISOU 2938  CB  SER A 395    22822   6957  11786    103   2609   -122       C  
ATOM   2939  OG  SER A 395     -50.830  26.165 -32.878  1.00107.11           O  
ANISOU 2939  OG  SER A 395    22422   6553  11723    402   2761     52       O  
ATOM   2940  N   ASP A 396     -48.480  22.645 -31.163  1.00103.48           N  
ANISOU 2940  N   ASP A 396    21487   6846  10984   -560   1962   -275       N  
ATOM   2941  CA  ASP A 396     -47.889  21.821 -30.114  1.00101.49           C  
ANISOU 2941  CA  ASP A 396    21331   6703  10527   -815   1746   -412       C  
ATOM   2942  C   ASP A 396     -46.368  21.831 -30.206  1.00103.49           C  
ANISOU 2942  C   ASP A 396    21537   7002  10781  -1379   1279   -455       C  
ATOM   2943  O   ASP A 396     -45.791  21.247 -31.131  1.00 98.75           O  
ANISOU 2943  O   ASP A 396    20450   6619  10452  -1541   1097   -358       O  
ATOM   2944  CB  ASP A 396     -48.418  20.389 -30.208  1.00 93.48           C  
ANISOU 2944  CB  ASP A 396    19863   5989   9664   -598   1804   -358       C  
ATOM   2945  CG  ASP A 396     -48.279  19.622 -28.905  1.00 92.32           C  
ANISOU 2945  CG  ASP A 396    19938   5894   9245   -695   1724   -490       C  
ATOM   2946  OD1 ASP A 396     -47.409  19.982 -28.082  1.00 94.42           O  
ANISOU 2946  OD1 ASP A 396    20600   6034   9241  -1052   1456   -607       O  
ATOM   2947  OD2 ASP A 396     -49.040  18.654 -28.699  1.00 92.14           O  
ANISOU 2947  OD2 ASP A 396    19703   6032   9275   -424   1913   -461       O  
ATOM   2948  N   PRO A 397     -45.684  22.468 -29.254  1.00108.42           N  
ANISOU 2948  N   PRO A 397    22648   7426  11121  -1697   1079   -581       N  
ATOM   2949  CA  PRO A 397     -44.224  22.607 -29.324  1.00107.29           C  
ANISOU 2949  CA  PRO A 397    22423   7305  11038  -2253    614   -598       C  
ATOM   2950  C   PRO A 397     -43.443  21.323 -29.097  1.00104.60           C  
ANISOU 2950  C   PRO A 397    21686   7252  10804  -2506    248   -600       C  
ATOM   2951  O   PRO A 397     -42.223  21.395 -28.935  1.00107.22           O  
ANISOU 2951  O   PRO A 397    21940   7601  11198  -2973   -169   -609       O  
ATOM   2952  CB  PRO A 397     -43.923  23.615 -28.196  1.00110.20           C  
ANISOU 2952  CB  PRO A 397    23493   7354  11023  -2466    510   -725       C  
ATOM   2953  CG  PRO A 397     -45.258  24.200 -27.788  1.00112.94           C  
ANISOU 2953  CG  PRO A 397    24292   7479  11141  -1990   1008   -758       C  
ATOM   2954  CD  PRO A 397     -46.246  23.119 -28.058  1.00110.56           C  
ANISOU 2954  CD  PRO A 397    23581   7424  11004  -1560   1285   -694       C  
ATOM   2955  N   ASN A 398     -44.087  20.157 -29.074  1.00100.79           N  
ANISOU 2955  N   ASN A 398    20934   6989  10373  -2221    377   -580       N  
ATOM   2956  CA  ASN A 398     -43.369  18.901 -28.874  1.00101.55           C  
ANISOU 2956  CA  ASN A 398    20664   7346  10576  -2438     33   -575       C  
ATOM   2957  C   ASN A 398     -44.097  17.756 -29.569  1.00 87.02           C  
ANISOU 2957  C   ASN A 398    18362   5756   8946  -2105    258   -487       C  
ATOM   2958  O   ASN A 398     -44.133  16.626 -29.069  1.00 84.05           O  
ANISOU 2958  O   ASN A 398    17861   5546   8528  -2068    151   -514       O  
ATOM   2959  CB  ASN A 398     -43.176  18.592 -27.388  1.00111.32           C  
ANISOU 2959  CB  ASN A 398    22321   8526  11450  -2558   -201   -694       C  
ATOM   2960  CG  ASN A 398     -44.464  18.712 -26.592  1.00111.35           C  
ANISOU 2960  CG  ASN A 398    22799   8389  11123  -2142    224   -760       C  
ATOM   2961  OD1 ASN A 398     -45.517  18.227 -27.015  1.00112.11           O  
ANISOU 2961  OD1 ASN A 398    22677   8584  11334  -1731    611   -711       O  
ATOM   2962  ND2 ASN A 398     -44.389  19.367 -25.441  1.00109.10           N  
ANISOU 2962  ND2 ASN A 398    23157   7860  10436  -2255    167   -850       N  
ATOM   2963  N   ARG A 399     -44.680  18.039 -30.735  1.00 84.87           N  
ANISOU 2963  N   ARG A 399    17854   5501   8891  -1865    548   -368       N  
ATOM   2964  CA  ARG A 399     -45.376  17.004 -31.490  1.00 83.05           C  
ANISOU 2964  CA  ARG A 399    17193   5499   8864  -1564    735   -255       C  
ATOM   2965  C   ARG A 399     -44.402  15.998 -32.094  1.00 79.92           C  
ANISOU 2965  C   ARG A 399    16311   5350   8707  -1850    465   -178       C  
ATOM   2966  O   ARG A 399     -44.752  14.825 -32.274  1.00 67.28           O  
ANISOU 2966  O   ARG A 399    14338   4037   7189  -1662    503   -127       O  
ATOM   2967  CB  ARG A 399     -46.234  17.649 -32.579  1.00 79.00           C  
ANISOU 2967  CB  ARG A 399    16589   4928   8498  -1247   1054   -117       C  
ATOM   2968  CG  ARG A 399     -45.447  18.505 -33.566  1.00 78.55           C  
ANISOU 2968  CG  ARG A 399    16459   4803   8583  -1511    962    -28       C  
ATOM   2969  CD  ARG A 399     -46.337  19.551 -34.220  1.00 75.71           C  
ANISOU 2969  CD  ARG A 399    16257   4267   8243  -1199   1242     64       C  
ATOM   2970  NE  ARG A 399     -47.476  18.955 -34.911  1.00 72.94           N  
ANISOU 2970  NE  ARG A 399    15622   4059   8035   -770   1454    210       N  
ATOM   2971  CZ  ARG A 399     -47.450  18.545 -36.174  1.00 70.59           C  
ANISOU 2971  CZ  ARG A 399    14967   3932   7922   -749   1438    388       C  
ATOM   2972  NH1 ARG A 399     -46.340  18.665 -36.888  1.00 74.65           N  
ANISOU 2972  NH1 ARG A 399    15358   4497   8507  -1118   1289    437       N  
ATOM   2973  NH2 ARG A 399     -48.534  18.015 -36.723  1.00 71.10           N  
ANISOU 2973  NH2 ARG A 399    14797   4117   8101   -369   1575    530       N  
ATOM   2974  N   GLN A 400     -43.178  16.435 -32.401  1.00 79.18           N  
ANISOU 2974  N   GLN A 400    16103   5240   8743  -2275    206   -155       N  
ATOM   2975  CA  GLN A 400     -42.186  15.530 -32.971  1.00 74.71           C  
ANISOU 2975  CA  GLN A 400    14962   4972   8453  -2525     -9    -61       C  
ATOM   2976  C   GLN A 400     -41.709  14.515 -31.941  1.00 75.42           C  
ANISOU 2976  C   GLN A 400    14926   5245   8485  -2631   -337   -141       C  
ATOM   2977  O   GLN A 400     -41.561  13.328 -32.254  1.00 73.93           O  
ANISOU 2977  O   GLN A 400    14200   5433   8455  -2518   -373    -70       O  
ATOM   2978  CB  GLN A 400     -41.005  16.329 -33.523  1.00 80.37           C  
ANISOU 2978  CB  GLN A 400    15590   5572   9375  -2978   -157      3       C  
ATOM   2979  CG  GLN A 400     -41.379  17.332 -34.604  1.00 82.88           C  
ANISOU 2979  CG  GLN A 400    15987   5766   9737  -2861    152    104       C  
ATOM   2980  CD  GLN A 400     -41.669  16.673 -35.939  1.00 84.74           C  
ANISOU 2980  CD  GLN A 400    15790   6256  10151  -2656    396    273       C  
ATOM   2981  OE1 GLN A 400     -41.190  15.574 -36.218  1.00 84.83           O  
ANISOU 2981  OE1 GLN A 400    15265   6634  10330  -2671    324    321       O  
ATOM   2982  NE2 GLN A 400     -42.457  17.343 -36.773  1.00 85.62           N  
ANISOU 2982  NE2 GLN A 400    16095   6225  10212  -2417    671    366       N  
ATOM   2983  N   ALA A 401     -41.462  14.961 -30.707  1.00 80.71           N  
ANISOU 2983  N   ALA A 401    16135   5629   8901  -2848   -589   -285       N  
ATOM   2984  CA  ALA A 401     -41.020  14.043 -29.663  1.00 89.68           C  
ANISOU 2984  CA  ALA A 401    17251   6890   9932  -2961   -953   -348       C  
ATOM   2985  C   ALA A 401     -42.120  13.050 -29.304  1.00 87.72           C  
ANISOU 2985  C   ALA A 401    17006   6811   9512  -2517   -708   -375       C  
ATOM   2986  O   ALA A 401     -41.871  11.842 -29.193  1.00 69.28           O  
ANISOU 2986  O   ALA A 401    14259   4794   7269  -2461   -863   -327       O  
ATOM   2987  CB  ALA A 401     -40.572  14.828 -28.429  1.00 79.54           C  
ANISOU 2987  CB  ALA A 401    16488   5385   8347  -3207  -1261   -464       C  
ATOM   2988  N   ASN A 402     -43.347  13.547 -29.117  1.00 84.21           N  
ANISOU 2988  N   ASN A 402    17013   6138   8844  -2195   -306   -438       N  
ATOM   2989  CA  ASN A 402     -44.479  12.664 -28.853  1.00 77.94           C  
ANISOU 2989  CA  ASN A 402    16170   5497   7948  -1777    -11   -438       C  
ATOM   2990  C   ASN A 402     -44.658  11.657 -29.980  1.00 73.03           C  
ANISOU 2990  C   ASN A 402    14790   5316   7641  -1576     91   -282       C  
ATOM   2991  O   ASN A 402     -44.855  10.460 -29.736  1.00 74.93           O  
ANISOU 2991  O   ASN A 402    14774   5815   7882  -1444     61   -263       O  
ATOM   2992  CB  ASN A 402     -45.755  13.487 -28.666  1.00 83.97           C  
ANISOU 2992  CB  ASN A 402    17375   5987   8541  -1433    458   -480       C  
ATOM   2993  CG  ASN A 402     -45.782  14.232 -27.347  1.00 93.22           C  
ANISOU 2993  CG  ASN A 402    19167   6935   9315  -1497    439   -609       C  
ATOM   2994  OD1 ASN A 402     -44.792  14.260 -26.616  1.00100.69           O  
ANISOU 2994  OD1 ASN A 402    20312   7846  10099  -1851     21   -670       O  
ATOM   2995  ND2 ASN A 402     -46.918  14.845 -27.037  1.00 94.31           N  
ANISOU 2995  ND2 ASN A 402    19611   6916   9306  -1155    890   -624       N  
ATOM   2996  N   PHE A 403     -44.584  12.125 -31.228  1.00 70.10           N  
ANISOU 2996  N   PHE A 403    14116   5006   7512  -1566    212   -171       N  
ATOM   2997  CA  PHE A 403     -44.764  11.225 -32.360  1.00 65.19           C  
ANISOU 2997  CA  PHE A 403    12880   4755   7133  -1395    313    -31       C  
ATOM   2998  C   PHE A 403     -43.667  10.169 -32.405  1.00 62.73           C  
ANISOU 2998  C   PHE A 403    12115   4741   6978  -1597     17     -1       C  
ATOM   2999  O   PHE A 403     -43.934   9.000 -32.702  1.00 62.45           O  
ANISOU 2999  O   PHE A 403    11718   4992   7019  -1418     64     52       O  
ATOM   3000  CB  PHE A 403     -44.797  12.015 -33.667  1.00 62.34           C  
ANISOU 3000  CB  PHE A 403    12395   4351   6941  -1386    477     85       C  
ATOM   3001  CG  PHE A 403     -45.036  11.159 -34.876  1.00 57.86           C  
ANISOU 3001  CG  PHE A 403    11319   4112   6553  -1223    583    222       C  
ATOM   3002  CD1 PHE A 403     -46.324  10.827 -35.258  1.00 58.85           C  
ANISOU 3002  CD1 PHE A 403    11380   4315   6667   -866    799    290       C  
ATOM   3003  CD2 PHE A 403     -43.975  10.673 -35.620  1.00 55.65           C  
ANISOU 3003  CD2 PHE A 403    10638   4046   6462  -1432    471    288       C  
ATOM   3004  CE1 PHE A 403     -46.550  10.035 -36.366  1.00 52.10           C  
ANISOU 3004  CE1 PHE A 403    10133   3731   5933   -756    845    409       C  
ATOM   3005  CE2 PHE A 403     -44.195   9.882 -36.727  1.00 53.75           C  
ANISOU 3005  CE2 PHE A 403    10037   4059   6326  -1287    593    396       C  
ATOM   3006  CZ  PHE A 403     -45.485   9.562 -37.100  1.00 51.75           C  
ANISOU 3006  CZ  PHE A 403     9788   3868   6006   -965    752    450       C  
ATOM   3007  N   ALA A 404     -42.425  10.563 -32.118  1.00 66.58           N  
ANISOU 3007  N   ALA A 404    12604   5148   7544  -1972   -295    -22       N  
ATOM   3008  CA  ALA A 404     -41.327   9.604 -32.111  1.00 65.48           C  
ANISOU 3008  CA  ALA A 404    11988   5270   7622  -2145   -585     32       C  
ATOM   3009  C   ALA A 404     -41.537   8.545 -31.037  1.00 65.94           C  
ANISOU 3009  C   ALA A 404    12126   5421   7506  -2032   -763    -27       C  
ATOM   3010  O   ALA A 404     -41.392   7.343 -31.294  1.00 69.18           O  
ANISOU 3010  O   ALA A 404    12119   6112   8055  -1904   -785     39       O  
ATOM   3011  CB  ALA A 404     -39.998  10.330 -31.901  1.00 64.97           C  
ANISOU 3011  CB  ALA A 404    11897   5072   7719  -2593   -922     41       C  
ATOM   3012  N   GLN A 405     -41.897   8.975 -29.824  1.00 70.18           N  
ANISOU 3012  N   GLN A 405    13261   5691   7711  -2073   -865   -150       N  
ATOM   3013  CA  GLN A 405     -42.075   8.026 -28.730  1.00 71.09           C  
ANISOU 3013  CA  GLN A 405    13556   5849   7606  -1994  -1032   -201       C  
ATOM   3014  C   GLN A 405     -43.226   7.066 -29.012  1.00 66.06           C  
ANISOU 3014  C   GLN A 405    12760   5407   6935  -1601   -671   -169       C  
ATOM   3015  O   GLN A 405     -43.092   5.849 -28.833  1.00 68.43           O  
ANISOU 3015  O   GLN A 405    12806   5922   7274  -1520   -782   -126       O  
ATOM   3016  CB  GLN A 405     -42.300   8.773 -27.416  1.00 76.69           C  
ANISOU 3016  CB  GLN A 405    15059   6178   7901  -2119  -1145   -349       C  
ATOM   3017  CG  GLN A 405     -42.417   7.851 -26.214  1.00 83.17           C  
ANISOU 3017  CG  GLN A 405    16176   6996   8429  -2078  -1335   -396       C  
ATOM   3018  CD  GLN A 405     -41.835   8.453 -24.954  1.00 91.90           C  
ANISOU 3018  CD  GLN A 405    17965   7763   9189  -2408  -1751   -507       C  
ATOM   3019  OE1 GLN A 405     -42.154   9.584 -24.585  1.00 96.19           O  
ANISOU 3019  OE1 GLN A 405    19119   7949   9480  -2491  -1623   -626       O  
ATOM   3020  NE2 GLN A 405     -40.966   7.701 -24.289  1.00 96.27           N  
ANISOU 3020  NE2 GLN A 405    18452   8403   9723  -2601  -2275   -463       N  
ATOM   3021  N   LYS A 406     -44.368   7.596 -29.461  1.00 66.63           N  
ANISOU 3021  N   LYS A 406    12965   5392   6958  -1359   -253   -175       N  
ATOM   3022  CA  LYS A 406     -45.498   6.731 -29.789  1.00 62.41           C  
ANISOU 3022  CA  LYS A 406    12226   5042   6447  -1024     61   -122       C  
ATOM   3023  C   LYS A 406     -45.167   5.797 -30.945  1.00 62.34           C  
ANISOU 3023  C   LYS A 406    11591   5370   6726   -980     33     -4       C  
ATOM   3024  O   LYS A 406     -45.649   4.658 -30.982  1.00 66.84           O  
ANISOU 3024  O   LYS A 406    11959   6130   7307   -812    106     33       O  
ATOM   3025  CB  LYS A 406     -46.731   7.570 -30.125  1.00 63.28           C  
ANISOU 3025  CB  LYS A 406    12524   4987   6532   -779    467   -113       C  
ATOM   3026  CG  LYS A 406     -47.201   8.486 -29.003  1.00 67.48           C  
ANISOU 3026  CG  LYS A 406    13731   5139   6770   -754    614   -236       C  
ATOM   3027  CD  LYS A 406     -47.691   7.700 -27.801  1.00 72.17           C  
ANISOU 3027  CD  LYS A 406    14621   5697   7104   -657    690   -302       C  
ATOM   3028  CE  LYS A 406     -48.218   8.627 -26.715  1.00 79.55           C  
ANISOU 3028  CE  LYS A 406    16306   6210   7708   -607    926   -431       C  
ATOM   3029  NZ  LYS A 406     -48.791   7.865 -25.569  1.00 83.56           N  
ANISOU 3029  NZ  LYS A 406    17155   6659   7934   -496   1091   -484       N  
ATOM   3030  N   ALA A 407     -44.343   6.253 -31.889  1.00 63.91           N  
ANISOU 3030  N   ALA A 407    11518   5620   7144  -1140    -44     54       N  
ATOM   3031  CA  ALA A 407     -43.955   5.404 -33.010  1.00 63.18           C  
ANISOU 3031  CA  ALA A 407    10908   5805   7294  -1102    -17    156       C  
ATOM   3032  C   ALA A 407     -43.098   4.235 -32.541  1.00 62.65           C  
ANISOU 3032  C   ALA A 407    10596   5903   7306  -1168   -276    165       C  
ATOM   3033  O   ALA A 407     -43.352   3.080 -32.906  1.00 61.41           O  
ANISOU 3033  O   ALA A 407    10191   5941   7201  -1005   -198    209       O  
ATOM   3034  CB  ALA A 407     -43.216   6.231 -34.062  1.00 60.60           C  
ANISOU 3034  CB  ALA A 407    10408   5452   7164  -1274     16    220       C  
ATOM   3035  N   LYS A 408     -42.075   4.514 -31.728  1.00 67.02           N  
ANISOU 3035  N   LYS A 408    11228   6361   7874  -1413   -613    136       N  
ATOM   3036  CA  LYS A 408     -41.220   3.436 -31.240  1.00 70.31           C  
ANISOU 3036  CA  LYS A 408    11395   6916   8402  -1459   -913    176       C  
ATOM   3037  C   LYS A 408     -42.003   2.473 -30.357  1.00 67.60           C  
ANISOU 3037  C   LYS A 408    11296   6589   7801  -1268   -915    135       C  
ATOM   3038  O   LYS A 408     -41.822   1.249 -30.442  1.00 66.54           O  
ANISOU 3038  O   LYS A 408    10898   6625   7761  -1148   -961    192       O  
ATOM   3039  CB  LYS A 408     -40.024   4.012 -30.483  1.00 81.29           C  
ANISOU 3039  CB  LYS A 408    12837   8180   9869  -1787  -1352    174       C  
ATOM   3040  CG  LYS A 408     -38.870   3.036 -30.341  1.00 90.42           C  
ANISOU 3040  CG  LYS A 408    13539   9503  11315  -1846  -1680    279       C  
ATOM   3041  CD  LYS A 408     -38.431   2.528 -31.706  1.00 95.73           C  
ANISOU 3041  CD  LYS A 408    13614  10393  12366  -1738  -1408    386       C  
ATOM   3042  CE  LYS A 408     -37.346   1.470 -31.590  1.00101.94           C  
ANISOU 3042  CE  LYS A 408    13918  11331  13484  -1719  -1658    504       C  
ATOM   3043  NZ  LYS A 408     -36.964   0.930 -32.925  1.00101.71           N  
ANISOU 3043  NZ  LYS A 408    13380  11475  13791  -1578  -1301    595       N  
ATOM   3044  N   GLU A 409     -42.891   3.007 -29.513  1.00 65.83           N  
ANISOU 3044  N   GLU A 409    11600   6163   7251  -1229   -821     41       N  
ATOM   3045  CA  GLU A 409     -43.736   2.143 -28.697  1.00 64.30           C  
ANISOU 3045  CA  GLU A 409    11664   5961   6804  -1052   -732     13       C  
ATOM   3046  C   GLU A 409     -44.626   1.262 -29.565  1.00 58.38           C  
ANISOU 3046  C   GLU A 409    10602   5415   6166   -801   -404     73       C  
ATOM   3047  O   GLU A 409     -44.849   0.089 -29.242  1.00 61.39           O  
ANISOU 3047  O   GLU A 409    10940   5891   6494   -695   -416    101       O  
ATOM   3048  CB  GLU A 409     -44.579   2.978 -27.733  1.00 68.38           C  
ANISOU 3048  CB  GLU A 409    12813   6195   6971  -1036   -573    -95       C  
ATOM   3049  CG  GLU A 409     -43.793   3.550 -26.565  1.00 76.90           C  
ANISOU 3049  CG  GLU A 409    14378   7032   7811  -1300   -957   -173       C  
ATOM   3050  CD  GLU A 409     -44.661   4.351 -25.613  1.00 77.68           C  
ANISOU 3050  CD  GLU A 409    15202   6801   7512  -1262   -724   -297       C  
ATOM   3051  OE1 GLU A 409     -45.836   4.609 -25.949  1.00 80.44           O  
ANISOU 3051  OE1 GLU A 409    15587   7119   7857  -1017   -240   -305       O  
ATOM   3052  OE2 GLU A 409     -44.167   4.721 -24.528  1.00 81.85           O  
ANISOU 3052  OE2 GLU A 409    16277   7085   7738  -1475  -1026   -377       O  
ATOM   3053  N   PHE A 410     -45.136   1.802 -30.678  1.00 52.26           N  
ANISOU 3053  N   PHE A 410     9637   4687   5532   -722   -141    104       N  
ATOM   3054  CA  PHE A 410     -45.940   0.977 -31.576  1.00 47.41           C  
ANISOU 3054  CA  PHE A 410     8740   4253   5019   -532     92    171       C  
ATOM   3055  C   PHE A 410     -45.102  -0.133 -32.200  1.00 50.20           C  
ANISOU 3055  C   PHE A 410     8716   4803   5556   -545    -38    229       C  
ATOM   3056  O   PHE A 410     -45.533  -1.292 -32.254  1.00 52.77           O  
ANISOU 3056  O   PHE A 410     8952   5234   5864   -426     20    256       O  
ATOM   3057  CB  PHE A 410     -46.584   1.821 -32.674  1.00 45.38           C  
ANISOU 3057  CB  PHE A 410     8392   3987   4862   -463    322    213       C  
ATOM   3058  CG  PHE A 410     -47.153   0.995 -33.797  1.00 46.17           C  
ANISOU 3058  CG  PHE A 410     8191   4274   5079   -340    452    296       C  
ATOM   3059  CD1 PHE A 410     -48.413   0.430 -33.689  1.00 46.21           C  
ANISOU 3059  CD1 PHE A 410     8202   4317   5040   -183    612    328       C  
ATOM   3060  CD2 PHE A 410     -46.416   0.754 -34.948  1.00 41.85           C  
ANISOU 3060  CD2 PHE A 410     7376   3844   4679   -401    420    345       C  
ATOM   3061  CE1 PHE A 410     -48.932  -0.345 -34.714  1.00 39.56           C  
ANISOU 3061  CE1 PHE A 410     7119   3624   4287   -118    665    404       C  
ATOM   3062  CE2 PHE A 410     -46.930  -0.019 -35.969  1.00 39.71           C  
ANISOU 3062  CE2 PHE A 410     6934   3703   4450   -312    519    406       C  
ATOM   3063  CZ  PHE A 410     -48.192  -0.568 -35.850  1.00 38.91           C  
ANISOU 3063  CZ  PHE A 410     6856   3636   4290   -186    604    434       C  
ATOM   3064  N   GLU A 411     -43.910   0.209 -32.695  1.00 48.38           N  
ANISOU 3064  N   GLU A 411     8259   4603   5520   -688   -181    256       N  
ATOM   3065  CA  GLU A 411     -43.055  -0.798 -33.320  1.00 53.76           C  
ANISOU 3065  CA  GLU A 411     8568   5442   6418   -665   -233    319       C  
ATOM   3066  C   GLU A 411     -42.742  -1.932 -32.349  1.00 51.68           C  
ANISOU 3066  C   GLU A 411     8328   5202   6106   -615   -453    326       C  
ATOM   3067  O   GLU A 411     -42.858  -3.115 -32.699  1.00 52.41           O  
ANISOU 3067  O   GLU A 411     8277   5394   6242   -476   -376    361       O  
ATOM   3068  CB  GLU A 411     -41.769  -0.148 -33.833  1.00 61.74           C  
ANISOU 3068  CB  GLU A 411     9314   6454   7690   -840   -323    362       C  
ATOM   3069  CG  GLU A 411     -41.977   0.767 -35.032  1.00 69.62           C  
ANISOU 3069  CG  GLU A 411    10273   7434   8744   -879    -66    384       C  
ATOM   3070  CD  GLU A 411     -42.041   0.011 -36.349  1.00 73.90           C  
ANISOU 3070  CD  GLU A 411    10595   8106   9376   -756    189    439       C  
ATOM   3071  OE1 GLU A 411     -41.119   0.181 -37.173  1.00 81.11           O  
ANISOU 3071  OE1 GLU A 411    11269   9047  10503   -837    296    495       O  
ATOM   3072  OE2 GLU A 411     -43.006  -0.755 -36.561  1.00 70.93           O  
ANISOU 3072  OE2 GLU A 411    10310   7786   8856   -594    293    429       O  
ATOM   3073  N   ALA A 412     -42.358  -1.587 -31.115  1.00 50.03           N  
ANISOU 3073  N   ALA A 412     8361   4870   5777   -734   -743    295       N  
ATOM   3074  CA  ALA A 412     -42.086  -2.622 -30.121  1.00 51.34           C  
ANISOU 3074  CA  ALA A 412     8627   5027   5852   -690   -994    319       C  
ATOM   3075  C   ALA A 412     -43.343  -3.412 -29.779  1.00 52.69           C  
ANISOU 3075  C   ALA A 412     9058   5190   5771   -524   -774    293       C  
ATOM   3076  O   ALA A 412     -43.271  -4.622 -29.524  1.00 58.84           O  
ANISOU 3076  O   ALA A 412     9805   6013   6541   -423   -842    339       O  
ATOM   3077  CB  ALA A 412     -41.486  -1.999 -28.860  1.00 51.78           C  
ANISOU 3077  CB  ALA A 412     8993   4917   5762   -886  -1389    293       C  
ATOM   3078  N   HIS A 413     -44.505  -2.753 -29.789  1.00 49.98           N  
ANISOU 3078  N   HIS A 413     8951   4780   5259   -490   -497    235       N  
ATOM   3079  CA  HIS A 413     -45.756  -3.441 -29.487  1.00 49.64           C  
ANISOU 3079  CA  HIS A 413     9089   4731   5042   -353   -250    232       C  
ATOM   3080  C   HIS A 413     -46.061  -4.515 -30.529  1.00 48.74           C  
ANISOU 3080  C   HIS A 413     8647   4780   5089   -241   -105    291       C  
ATOM   3081  O   HIS A 413     -46.204  -5.699 -30.200  1.00 51.59           O  
ANISOU 3081  O   HIS A 413     9047   5161   5393   -177   -125    322       O  
ATOM   3082  CB  HIS A 413     -46.896  -2.426 -29.398  1.00 47.87           C  
ANISOU 3082  CB  HIS A 413     9085   4401   4703   -316     43    187       C  
ATOM   3083  CG  HIS A 413     -48.239  -3.041 -29.153  1.00 50.53           C  
ANISOU 3083  CG  HIS A 413     9514   4737   4946   -185    341    210       C  
ATOM   3084  ND1 HIS A 413     -48.548  -3.721 -27.995  1.00 50.03           N  
ANISOU 3084  ND1 HIS A 413     9779   4577   4653   -171    365    202       N  
ATOM   3085  CD2 HIS A 413     -49.356  -3.073 -29.918  1.00 50.92           C  
ANISOU 3085  CD2 HIS A 413     9362   4863   5124    -81    618    260       C  
ATOM   3086  CE1 HIS A 413     -49.797  -4.146 -28.057  1.00 51.47           C  
ANISOU 3086  CE1 HIS A 413     9926   4780   4849    -69    690    244       C  
ATOM   3087  NE2 HIS A 413     -50.310  -3.767 -29.214  1.00 52.25           N  
ANISOU 3087  NE2 HIS A 413     9678   4990   5183    -16    821    284       N  
ATOM   3088  N   THR A 414     -46.159  -4.118 -31.800  1.00 47.01           N  
ANISOU 3088  N   THR A 414     8166   4653   5044   -229     35    308       N  
ATOM   3089  CA  THR A 414     -46.489  -5.090 -32.840  1.00 46.93           C  
ANISOU 3089  CA  THR A 414     7941   4760   5131   -151    162    352       C  
ATOM   3090  C   THR A 414     -45.404  -6.151 -32.990  1.00 46.69           C  
ANISOU 3090  C   THR A 414     7749   4778   5215   -120     21    379       C  
ATOM   3091  O   THR A 414     -45.719  -7.323 -33.250  1.00 47.54           O  
ANISOU 3091  O   THR A 414     7845   4913   5306    -45     86    401       O  
ATOM   3092  CB  THR A 414     -46.741  -4.378 -34.172  1.00 44.47           C  
ANISOU 3092  CB  THR A 414     7467   4502   4927   -163    306    371       C  
ATOM   3093  OG1 THR A 414     -47.041  -5.345 -35.185  1.00 47.02           O  
ANISOU 3093  OG1 THR A 414     7670   4907   5288   -116    396    405       O  
ATOM   3094  CG2 THR A 414     -45.528  -3.558 -34.599  1.00 43.52           C  
ANISOU 3094  CG2 THR A 414     7212   4376   4947   -252    226    368       C  
ATOM   3095  N   ALA A 415     -44.134  -5.778 -32.809  1.00 48.91           N  
ANISOU 3095  N   ALA A 415     7897   5049   5636   -178   -172    390       N  
ATOM   3096  CA  ALA A 415     -43.079  -6.786 -32.793  1.00 53.08           C  
ANISOU 3096  CA  ALA A 415     8233   5603   6331   -108   -312    444       C  
ATOM   3097  C   ALA A 415     -43.320  -7.807 -31.688  1.00 53.22           C  
ANISOU 3097  C   ALA A 415     8481   5556   6185    -40   -462    462       C  
ATOM   3098  O   ALA A 415     -43.121  -9.013 -31.889  1.00 50.36           O  
ANISOU 3098  O   ALA A 415     8055   5197   5883     81   -444    503       O  
ATOM   3099  CB  ALA A 415     -41.712  -6.123 -32.624  1.00 45.10           C  
ANISOU 3099  CB  ALA A 415     6990   4589   5555   -205   -539    483       C  
ATOM   3100  N   ARG A 416     -43.767  -7.344 -30.516  1.00 53.47           N  
ANISOU 3100  N   ARG A 416     8841   5494   5982   -114   -581    431       N  
ATOM   3101  CA  ARG A 416     -44.045  -8.265 -29.419  1.00 50.07           C  
ANISOU 3101  CA  ARG A 416     8712   4971   5339    -68   -696    456       C  
ATOM   3102  C   ARG A 416     -45.226  -9.172 -29.742  1.00 54.77           C  
ANISOU 3102  C   ARG A 416     9397   5580   5832     11   -406    455       C  
ATOM   3103  O   ARG A 416     -45.205 -10.367 -29.413  1.00 43.85           O  
ANISOU 3103  O   ARG A 416     8113   4151   4397     86   -453    502       O  
ATOM   3104  CB  ARG A 416     -44.304  -7.485 -28.132  1.00 48.10           C  
ANISOU 3104  CB  ARG A 416     8883   4584   4808   -179   -827    413       C  
ATOM   3105  CG  ARG A 416     -44.515  -8.360 -26.912  1.00 48.31           C  
ANISOU 3105  CG  ARG A 416     9313   4482   4560   -152   -952    448       C  
ATOM   3106  CD  ARG A 416     -43.267  -9.162 -26.583  1.00 55.56           C  
ANISOU 3106  CD  ARG A 416    10118   5386   5606   -109  -1361    547       C  
ATOM   3107  NE  ARG A 416     -43.367  -9.788 -25.270  1.00 63.77           N  
ANISOU 3107  NE  ARG A 416    11644   6260   6324   -114  -1563    592       N  
ATOM   3108  CZ  ARG A 416     -42.350 -10.356 -24.631  1.00 68.91           C  
ANISOU 3108  CZ  ARG A 416    12334   6843   7004    -91  -2014    698       C  
ATOM   3109  NH1 ARG A 416     -41.145 -10.380 -25.183  1.00 72.99           N  
ANISOU 3109  NH1 ARG A 416    12359   7455   7919    -50  -2283    775       N  
ATOM   3110  NH2 ARG A 416     -42.537 -10.893 -23.434  1.00 68.76           N  
ANISOU 3110  NH2 ARG A 416    12847   6648   6630   -105  -2190    744       N  
ATOM   3111  N   LEU A 417     -46.267  -8.626 -30.378  1.00 51.79           N  
ANISOU 3111  N   LEU A 417     8984   5252   5442    -15   -130    417       N  
ATOM   3112  CA  LEU A 417     -47.396  -9.458 -30.789  1.00 49.14           C  
ANISOU 3112  CA  LEU A 417     8667   4938   5067     16    100    436       C  
ATOM   3113  C   LEU A 417     -46.941 -10.574 -31.720  1.00 51.33           C  
ANISOU 3113  C   LEU A 417     8768   5257   5477     80     93    462       C  
ATOM   3114  O   LEU A 417     -47.300 -11.744 -31.530  1.00 55.20           O  
ANISOU 3114  O   LEU A 417     9385   5693   5897    108    127    491       O  
ATOM   3115  CB  LEU A 417     -48.468  -8.606 -31.468  1.00 45.41           C  
ANISOU 3115  CB  LEU A 417     8096   4521   4636    -18    325    423       C  
ATOM   3116  CG  LEU A 417     -49.204  -7.582 -30.608  1.00 49.34           C  
ANISOU 3116  CG  LEU A 417     8792   4940   5014    -37    450    401       C  
ATOM   3117  CD1 LEU A 417     -50.279  -6.889 -31.434  1.00 49.97           C  
ANISOU 3117  CD1 LEU A 417     8697   5076   5215    -24    660    426       C  
ATOM   3118  CD2 LEU A 417     -49.801  -8.243 -29.372  1.00 45.37           C  
ANISOU 3118  CD2 LEU A 417     8602   4326   4310    -34    542    418       C  
ATOM   3119  N   ALA A 418     -46.141 -10.231 -32.734  1.00 51.76           N  
ANISOU 3119  N   ALA A 418     8571   5381   5714    101     83    452       N  
ATOM   3120  CA  ALA A 418     -45.701 -11.249 -33.686  1.00 48.89           C  
ANISOU 3120  CA  ALA A 418     8100   5019   5457    182    150    465       C  
ATOM   3121  C   ALA A 418     -44.784 -12.273 -33.024  1.00 50.96           C  
ANISOU 3121  C   ALA A 418     8393   5198   5772    302     -9    512       C  
ATOM   3122  O   ALA A 418     -44.863 -13.471 -33.326  1.00 48.81           O  
ANISOU 3122  O   ALA A 418     8205   4854   5485    381     64    527       O  
ATOM   3123  CB  ALA A 418     -45.009 -10.589 -34.878  1.00 46.98           C  
ANISOU 3123  CB  ALA A 418     7623   4842   5385    183    241    451       C  
ATOM   3124  N   ASP A 419     -43.911 -11.822 -32.117  1.00 55.90           N  
ANISOU 3124  N   ASP A 419     8973   5810   6458    310   -255    547       N  
ATOM   3125  CA  ASP A 419     -43.049 -12.754 -31.395  1.00 60.90           C  
ANISOU 3125  CA  ASP A 419     9629   6354   7156    435   -480    626       C  
ATOM   3126  C   ASP A 419     -43.870 -13.729 -30.562  1.00 59.91           C  
ANISOU 3126  C   ASP A 419     9877   6113   6772    446   -489    646       C  
ATOM   3127  O   ASP A 419     -43.600 -14.936 -30.558  1.00 60.94           O  
ANISOU 3127  O   ASP A 419    10073   6147   6934    577   -506    699       O  
ATOM   3128  CB  ASP A 419     -42.066 -11.989 -30.508  1.00 70.19           C  
ANISOU 3128  CB  ASP A 419    10717   7530   8423    388   -829    675       C  
ATOM   3129  CG  ASP A 419     -40.906 -11.407 -31.291  1.00 80.69           C  
ANISOU 3129  CG  ASP A 419    11599   8944  10117    404   -848    705       C  
ATOM   3130  OD1 ASP A 419     -41.026 -11.280 -32.528  1.00 87.66           O  
ANISOU 3130  OD1 ASP A 419    12310   9890  11106    424   -536    663       O  
ATOM   3131  OD2 ASP A 419     -39.874 -11.077 -30.669  1.00 88.06           O  
ANISOU 3131  OD2 ASP A 419    12363   9867  11228    379  -1183    783       O  
ATOM   3132  N   THR A 420     -44.881 -13.223 -29.853  1.00 56.88           N  
ANISOU 3132  N   THR A 420     9757   5715   6139    316   -438    611       N  
ATOM   3133  CA  THR A 420     -45.728 -14.097 -29.048  1.00 53.71           C  
ANISOU 3133  CA  THR A 420     9717   5195   5494    298   -379    640       C  
ATOM   3134  C   THR A 420     -46.482 -15.090 -29.923  1.00 50.94           C  
ANISOU 3134  C   THR A 420     9356   4832   5167    303   -134    633       C  
ATOM   3135  O   THR A 420     -46.593 -16.274 -29.578  1.00 55.03           O  
ANISOU 3135  O   THR A 420    10089   5219   5599    348   -140    683       O  
ATOM   3136  CB  THR A 420     -46.695 -13.260 -28.212  1.00 55.41           C  
ANISOU 3136  CB  THR A 420    10188   5389   5475    168   -271    604       C  
ATOM   3137  OG1 THR A 420     -45.961 -12.573 -27.191  1.00 59.88           O  
ANISOU 3137  OG1 THR A 420    10930   5892   5929    143   -551    611       O  
ATOM   3138  CG2 THR A 420     -47.752 -14.141 -27.560  1.00 55.93           C  
ANISOU 3138  CG2 THR A 420    10586   5340   5325    126    -87    642       C  
ATOM   3139  N   ALA A 421     -46.998 -14.632 -31.067  1.00 48.41           N  
ANISOU 3139  N   ALA A 421     8826   4623   4947    242     54    577       N  
ATOM   3140  CA  ALA A 421     -47.621 -15.560 -32.006  1.00 45.30           C  
ANISOU 3140  CA  ALA A 421     8448   4198   4564    211    218    567       C  
ATOM   3141  C   ALA A 421     -46.642 -16.648 -32.432  1.00 44.63           C  
ANISOU 3141  C   ALA A 421     8377   4009   4572    368    171    584       C  
ATOM   3142  O   ALA A 421     -47.017 -17.822 -32.545  1.00 43.81           O  
ANISOU 3142  O   ALA A 421     8481   3772   4393    365    238    598       O  
ATOM   3143  CB  ALA A 421     -48.150 -14.802 -33.223  1.00 40.89           C  
ANISOU 3143  CB  ALA A 421     7687   3763   4085    122    346    519       C  
ATOM   3144  N   GLU A 422     -45.375 -16.282 -32.651  1.00 43.77           N  
ANISOU 3144  N   GLU A 422     8044   3935   4650    510     74    593       N  
ATOM   3145  CA  GLU A 422     -44.376 -17.279 -33.023  1.00 51.34           C  
ANISOU 3145  CA  GLU A 422     8968   4778   5761    713     77    628       C  
ATOM   3146  C   GLU A 422     -44.137 -18.275 -31.893  1.00 54.20           C  
ANISOU 3146  C   GLU A 422     9564   4979   6051    820   -105    718       C  
ATOM   3147  O   GLU A 422     -43.989 -19.479 -32.142  1.00 55.14           O  
ANISOU 3147  O   GLU A 422     9840   4929   6179    945    -31    742       O  
ATOM   3148  CB  GLU A 422     -43.069 -16.593 -33.419  1.00 55.08           C  
ANISOU 3148  CB  GLU A 422     9071   5334   6522    837     32    649       C  
ATOM   3149  CG  GLU A 422     -41.917 -17.556 -33.664  1.00 68.33           C  
ANISOU 3149  CG  GLU A 422    10635   6884   8441   1101     54    718       C  
ATOM   3150  CD  GLU A 422     -42.197 -18.526 -34.797  1.00 74.01           C  
ANISOU 3150  CD  GLU A 422    11541   7469   9109   1171    372    655       C  
ATOM   3151  OE1 GLU A 422     -42.749 -18.090 -35.830  1.00 76.42           O  
ANISOU 3151  OE1 GLU A 422    11879   7836   9320   1036    582    563       O  
ATOM   3152  OE2 GLU A 422     -41.871 -19.726 -34.651  1.00 73.17           O  
ANISOU 3152  OE2 GLU A 422    11595   7169   9036   1357    395    702       O  
ATOM   3153  N   LEU A 423     -44.095 -17.793 -30.647  1.00 52.98           N  
ANISOU 3153  N   LEU A 423     9497   4840   5795    771   -343    770       N  
ATOM   3154  CA  LEU A 423     -43.907 -18.690 -29.510  1.00 50.78           C  
ANISOU 3154  CA  LEU A 423     9519   4387   5389    854   -547    872       C  
ATOM   3155  C   LEU A 423     -45.062 -19.675 -29.398  1.00 50.16           C  
ANISOU 3155  C   LEU A 423     9813   4172   5074    757   -353    864       C  
ATOM   3156  O   LEU A 423     -44.852 -20.877 -29.208  1.00 53.81           O  
ANISOU 3156  O   LEU A 423    10494   4441   5511    877   -382    932       O  
ATOM   3157  CB  LEU A 423     -43.765 -17.886 -28.216  1.00 54.48           C  
ANISOU 3157  CB  LEU A 423    10118   4875   5706    770   -832    915       C  
ATOM   3158  CG  LEU A 423     -43.680 -18.719 -26.934  1.00 58.64           C  
ANISOU 3158  CG  LEU A 423    11067   5203   6012    819  -1068   1031       C  
ATOM   3159  CD1 LEU A 423     -42.429 -19.584 -26.936  1.00 62.03           C  
ANISOU 3159  CD1 LEU A 423    11361   5519   6688   1082  -1326   1159       C  
ATOM   3160  CD2 LEU A 423     -43.716 -17.836 -25.698  1.00 63.71           C  
ANISOU 3160  CD2 LEU A 423    11965   5837   6406    685  -1310   1046       C  
ATOM   3161  N   VAL A 424     -46.295 -19.177 -29.511  1.00 49.59           N  
ANISOU 3161  N   VAL A 424     9799   4185   4858    536   -153    797       N  
ATOM   3162  CA  VAL A 424     -47.462 -20.054 -29.459  1.00 50.80           C  
ANISOU 3162  CA  VAL A 424    10232   4223   4846    392     40    805       C  
ATOM   3163  C   VAL A 424     -47.409 -21.077 -30.586  1.00 53.44           C  
ANISOU 3163  C   VAL A 424    10576   4455   5273    437    157    774       C  
ATOM   3164  O   VAL A 424     -47.702 -22.262 -30.384  1.00 58.33           O  
ANISOU 3164  O   VAL A 424    11503   4870   5790    423    201    817       O  
ATOM   3165  CB  VAL A 424     -48.756 -19.219 -29.507  1.00 51.21           C  
ANISOU 3165  CB  VAL A 424    10215   4409   4833    165    237    761       C  
ATOM   3166  CG1 VAL A 424     -49.943 -20.091 -29.872  1.00 46.93           C  
ANISOU 3166  CG1 VAL A 424     9804   3785   4244    -18    437    773       C  
ATOM   3167  CG2 VAL A 424     -48.987 -18.537 -28.170  1.00 51.34           C  
ANISOU 3167  CG2 VAL A 424    10418   4420   4671    121    206    796       C  
ATOM   3168  N   ALA A 425     -47.019 -20.639 -31.785  1.00 55.05           N  
ANISOU 3168  N   ALA A 425    10507   4767   5644    483    225    698       N  
ATOM   3169  CA  ALA A 425     -46.934 -21.557 -32.914  1.00 48.19           C  
ANISOU 3169  CA  ALA A 425     9732   3765   4812    524    365    650       C  
ATOM   3170  C   ALA A 425     -45.851 -22.608 -32.706  1.00 52.84           C  
ANISOU 3170  C   ALA A 425    10456   4137   5483    803    314    709       C  
ATOM   3171  O   ALA A 425     -45.956 -23.720 -33.237  1.00 54.67           O  
ANISOU 3171  O   ALA A 425    10954   4152   5665    834    439    688       O  
ATOM   3172  CB  ALA A 425     -46.677 -20.776 -34.205  1.00 46.94           C  
ANISOU 3172  CB  ALA A 425     9313   3748   4773    522    472    563       C  
ATOM   3173  N   SER A 426     -44.811 -22.284 -31.937  1.00 53.08           N  
ANISOU 3173  N   SER A 426    10318   4201   5650   1007    113    793       N  
ATOM   3174  CA  SER A 426     -43.703 -23.211 -31.741  1.00 56.36           C  
ANISOU 3174  CA  SER A 426    10774   4417   6223   1318     31    886       C  
ATOM   3175  C   SER A 426     -43.865 -24.113 -30.524  1.00 60.42           C  
ANISOU 3175  C   SER A 426    11666   4726   6567   1353   -150   1004       C  
ATOM   3176  O   SER A 426     -43.215 -25.162 -30.466  1.00 64.37           O  
ANISOU 3176  O   SER A 426    12310   4990   7157   1601   -177   1085       O  
ATOM   3177  CB  SER A 426     -42.384 -22.444 -31.613  1.00 60.01           C  
ANISOU 3177  CB  SER A 426    10795   5010   6997   1525   -145    952       C  
ATOM   3178  OG  SER A 426     -41.971 -21.929 -32.865  1.00 69.95           O  
ANISOU 3178  OG  SER A 426    11747   6374   8456   1569     93    868       O  
ATOM   3179  N   SER A 427     -44.707 -23.740 -29.556  1.00 55.94           N  
ANISOU 3179  N   SER A 427    11290   4213   5751   1127   -243   1025       N  
ATOM   3180  CA  SER A 427     -44.780 -24.490 -28.307  1.00 58.28           C  
ANISOU 3180  CA  SER A 427    11992   4305   5848   1154   -417   1154       C  
ATOM   3181  C   SER A 427     -46.200 -24.656 -27.776  1.00 57.50           C  
ANISOU 3181  C   SER A 427    12247   4161   5438    845   -251   1139       C  
ATOM   3182  O   SER A 427     -46.364 -25.072 -26.623  1.00 74.73           O  
ANISOU 3182  O   SER A 427    14809   6188   7398    820   -360   1247       O  
ATOM   3183  CB  SER A 427     -43.919 -23.820 -27.229  1.00 59.74           C  
ANISOU 3183  CB  SER A 427    12094   4553   6053   1262   -796   1261       C  
ATOM   3184  OG  SER A 427     -42.571 -23.703 -27.650  1.00 66.12           O  
ANISOU 3184  OG  SER A 427    12503   5399   7221   1540   -969   1313       O  
ATOM   3185  N   GLY A 428     -47.223 -24.355 -28.565  1.00 61.12           N  
ANISOU 3185  N   GLY A 428    12595   4738   5888    608      8   1030       N  
ATOM   3186  CA  GLY A 428     -48.581 -24.422 -28.075  1.00 58.30           C  
ANISOU 3186  CA  GLY A 428    12460   4363   5330    312    189   1040       C  
ATOM   3187  C   GLY A 428     -49.291 -25.731 -28.289  1.00 61.73           C  
ANISOU 3187  C   GLY A 428    13224   4555   5675    171    345   1066       C  
ATOM   3188  O   GLY A 428     -50.489 -25.825 -28.005  1.00 66.68           O  
ANISOU 3188  O   GLY A 428    13966   5172   6199   -112    530   1086       O  
ATOM   3189  N   GLY A 429     -48.593 -26.754 -28.777  1.00 65.16           N  
ANISOU 3189  N   GLY A 429    13816   4773   6167    356    298   1073       N  
ATOM   3190  CA  GLY A 429     -49.233 -28.030 -29.024  1.00 66.75           C  
ANISOU 3190  CA  GLY A 429    14313   4763   6285    202    432   1055       C  
ATOM   3191  C   GLY A 429     -50.279 -28.014 -30.112  1.00 68.25           C  
ANISOU 3191  C   GLY A 429    14431   4992   6508   -109    604    966       C  
ATOM   3192  O   GLY A 429     -51.179 -28.856 -30.102  1.00 74.05           O  
ANISOU 3192  O   GLY A 429    15337   5632   7167   -365    699    951       O  
ATOM   3193  N   CYS A 430     -50.196 -27.075 -31.050  1.00 65.44           N  
ANISOU 3193  N   CYS A 430    13730   4851   6285   -110    609    879       N  
ATOM   3194  CA  CYS A 430     -51.151 -27.010 -32.145  1.00 63.80           C  
ANISOU 3194  CA  CYS A 430    13428   4707   6107   -409    693    796       C  
ATOM   3195  C   CYS A 430     -50.676 -27.862 -33.319  1.00 66.82           C  
ANISOU 3195  C   CYS A 430    14047   4867   6474   -336    720    702       C  
ATOM   3196  O   CYS A 430     -49.490 -28.171 -33.456  1.00 68.84           O  
ANISOU 3196  O   CYS A 430    14379   5002   6776      9    722    685       O  
ATOM   3197  CB  CYS A 430     -51.360 -25.562 -32.594  1.00 63.83           C  
ANISOU 3197  CB  CYS A 430    12964   5055   6233   -452    674    744       C  
ATOM   3198  SG  CYS A 430     -49.843 -24.687 -33.042  1.00 64.47           S  
ANISOU 3198  SG  CYS A 430    12764   5285   6445    -74    600    677       S  
ATOM   3199  N   SER A 431     -51.627 -28.247 -34.167  1.00 65.07           N  
ANISOU 3199  N   SER A 431    13953   4574   6198   -671    744    648       N  
ATOM   3200  CA  SER A 431     -51.292 -29.016 -35.355  1.00 66.00           C  
ANISOU 3200  CA  SER A 431    14395   4446   6234   -652    784    536       C  
ATOM   3201  C   SER A 431     -50.442 -28.181 -36.310  1.00 60.74           C  
ANISOU 3201  C   SER A 431    13495   3940   5642   -419    820    436       C  
ATOM   3202  O   SER A 431     -50.335 -26.957 -36.188  1.00 61.83           O  
ANISOU 3202  O   SER A 431    13195   4398   5900   -363    775    450       O  
ATOM   3203  CB  SER A 431     -52.557 -29.497 -36.067  1.00 69.62           C  
ANISOU 3203  CB  SER A 431    14991   4858   6603  -1114    719    490       C  
ATOM   3204  OG  SER A 431     -53.252 -28.413 -36.655  1.00 69.11           O  
ANISOU 3204  OG  SER A 431    14594   5047   6619  -1340    625    491       O  
ATOM   3205  N   ASP A 432     -49.827 -28.869 -37.276  1.00 60.33           N  
ANISOU 3205  N   ASP A 432    13784   3629   5508   -286    938    334       N  
ATOM   3206  CA  ASP A 432     -48.934 -28.201 -38.216  1.00 59.70           C  
ANISOU 3206  CA  ASP A 432    13547   3645   5490    -48   1056    245       C  
ATOM   3207  C   ASP A 432     -49.677 -27.198 -39.088  1.00 57.96           C  
ANISOU 3207  C   ASP A 432    13128   3674   5222   -336    965    191       C  
ATOM   3208  O   ASP A 432     -49.102 -26.178 -39.492  1.00 56.35           O  
ANISOU 3208  O   ASP A 432    12612   3684   5115   -180   1017    167       O  
ATOM   3209  CB  ASP A 432     -48.228 -29.239 -39.087  1.00 66.56           C  
ANISOU 3209  CB  ASP A 432    14914   4126   6251    145   1277    145       C  
ATOM   3210  CG  ASP A 432     -47.419 -30.227 -38.274  1.00 73.93           C  
ANISOU 3210  CG  ASP A 432    15927   4893   7272    483   1350    213       C  
ATOM   3211  OD1 ASP A 432     -46.701 -29.792 -37.349  1.00 69.97           O  
ANISOU 3211  OD1 ASP A 432    15124   4471   6990    771   1301    332       O  
ATOM   3212  OD2 ASP A 432     -47.506 -31.440 -38.554  1.00 89.08           O  
ANISOU 3212  OD2 ASP A 432    18220   6597   9031    454   1425    161       O  
ATOM   3213  N   ALA A 433     -50.948 -27.468 -39.392  1.00 59.70           N  
ANISOU 3213  N   ALA A 433    13512   3858   5314   -764    809    189       N  
ATOM   3214  CA  ALA A 433     -51.721 -26.554 -40.225  1.00 58.37           C  
ANISOU 3214  CA  ALA A 433    13152   3907   5119  -1040    657    171       C  
ATOM   3215  C   ALA A 433     -52.015 -25.256 -39.481  1.00 60.59           C  
ANISOU 3215  C   ALA A 433    12834   4574   5613  -1018    577    270       C  
ATOM   3216  O   ALA A 433     -51.771 -24.159 -40.002  1.00 60.39           O  
ANISOU 3216  O   ALA A 433    12545   4762   5638   -944    569    250       O  
ATOM   3217  CB  ALA A 433     -53.016 -27.230 -40.679  1.00 60.75           C  
ANISOU 3217  CB  ALA A 433    13736   4061   5287  -1520    452    177       C  
ATOM   3218  N   VAL A 434     -52.531 -25.365 -38.252  1.00 59.63           N  
ANISOU 3218  N   VAL A 434    12545   4515   5597  -1080    549    377       N  
ATOM   3219  CA  VAL A 434     -52.770 -24.185 -37.426  1.00 53.81           C  
ANISOU 3219  CA  VAL A 434    11327   4088   5031  -1030    529    461       C  
ATOM   3220  C   VAL A 434     -51.474 -23.426 -37.181  1.00 55.41           C  
ANISOU 3220  C   VAL A 434    11337   4410   5307   -651    610    431       C  
ATOM   3221  O   VAL A 434     -51.472 -22.189 -37.125  1.00 53.98           O  
ANISOU 3221  O   VAL A 434    10802   4478   5229   -609    584    447       O  
ATOM   3222  CB  VAL A 434     -53.449 -24.596 -36.103  1.00 55.21           C  
ANISOU 3222  CB  VAL A 434    11488   4237   5252  -1142    560    574       C  
ATOM   3223  CG1 VAL A 434     -53.802 -23.371 -35.274  1.00 50.70           C  
ANISOU 3223  CG1 VAL A 434    10498   3943   4822  -1104    589    650       C  
ATOM   3224  CG2 VAL A 434     -54.691 -25.437 -36.377  1.00 58.24           C  
ANISOU 3224  CG2 VAL A 434    12037   4479   5612  -1550    491    620       C  
ATOM   3225  N   ALA A 435     -50.353 -24.139 -37.044  1.00 50.80           N  
ANISOU 3225  N   ALA A 435    10963   3637   4700   -374    702    401       N  
ATOM   3226  CA  ALA A 435     -49.072 -23.469 -36.840  1.00 54.73           C  
ANISOU 3226  CA  ALA A 435    11220   4243   5333    -34    751    398       C  
ATOM   3227  C   ALA A 435     -48.670 -22.668 -38.072  1.00 56.46           C  
ANISOU 3227  C   ALA A 435    11304   4571   5579      2    825    318       C  
ATOM   3228  O   ALA A 435     -48.281 -21.496 -37.965  1.00 53.98           O  
ANISOU 3228  O   ALA A 435    10639   4481   5390     86    807    333       O  
ATOM   3229  CB  ALA A 435     -47.991 -24.492 -36.486  1.00 54.18           C  
ANISOU 3229  CB  ALA A 435    11363   3926   5296    269    824    415       C  
ATOM   3230  N   ALA A 436     -48.766 -23.282 -39.256  1.00 59.80           N  
ANISOU 3230  N   ALA A 436    12061   4807   5853    -79    916    231       N  
ATOM   3231  CA  ALA A 436     -48.438 -22.567 -40.486  1.00 50.79           C  
ANISOU 3231  CA  ALA A 436    10895   3730   4672    -70   1013    159       C  
ATOM   3232  C   ALA A 436     -49.338 -21.352 -40.677  1.00 51.24           C  
ANISOU 3232  C   ALA A 436    10674   4057   4740   -304    841    194       C  
ATOM   3233  O   ALA A 436     -48.871 -20.283 -41.089  1.00 53.00           O  
ANISOU 3233  O   ALA A 436    10668   4439   5032   -219    893    188       O  
ATOM   3234  CB  ALA A 436     -48.543 -23.506 -41.688  1.00 53.61           C  
ANISOU 3234  CB  ALA A 436    11793   3791   4783   -166   1124     55       C  
ATOM   3235  N   GLU A 437     -50.632 -21.495 -40.379  1.00 52.85           N  
ANISOU 3235  N   GLU A 437    10876   4299   4905   -595    651    248       N  
ATOM   3236  CA  GLU A 437     -51.550 -20.371 -40.529  1.00 57.59           C  
ANISOU 3236  CA  GLU A 437    11174   5136   5570   -783    492    309       C  
ATOM   3237  C   GLU A 437     -51.202 -19.245 -39.563  1.00 59.32           C  
ANISOU 3237  C   GLU A 437    10975   5583   5980   -607    524    364       C  
ATOM   3238  O   GLU A 437     -51.186 -18.068 -39.947  1.00 63.24           O  
ANISOU 3238  O   GLU A 437    11248   6246   6535   -592    501    375       O  
ATOM   3239  CB  GLU A 437     -52.989 -20.840 -40.320  1.00 66.74           C  
ANISOU 3239  CB  GLU A 437    12346   6278   6733  -1114    310    385       C  
ATOM   3240  CG  GLU A 437     -54.022 -19.733 -40.421  1.00 76.86           C  
ANISOU 3240  CG  GLU A 437    13257   7790   8155  -1279    150    482       C  
ATOM   3241  CD  GLU A 437     -55.442 -20.261 -40.395  1.00 87.23           C  
ANISOU 3241  CD  GLU A 437    14532   9076   9537  -1628    -35    580       C  
ATOM   3242  OE1 GLU A 437     -55.616 -21.497 -40.329  1.00 91.90           O  
ANISOU 3242  OE1 GLU A 437    15433   9456  10030  -1778    -46    558       O  
ATOM   3243  OE2 GLU A 437     -56.384 -19.441 -40.442  1.00 90.16           O  
ANISOU 3243  OE2 GLU A 437    14548   9621  10088  -1753   -167    692       O  
ATOM   3244  N   LEU A 438     -50.911 -19.588 -38.307  1.00 57.10           N  
ANISOU 3244  N   LEU A 438    10643   5283   5769   -483    565    399       N  
ATOM   3245  CA  LEU A 438     -50.503 -18.579 -37.336  1.00 55.13           C  
ANISOU 3245  CA  LEU A 438    10099   5203   5647   -333    570    438       C  
ATOM   3246  C   LEU A 438     -49.260 -17.836 -37.808  1.00 56.01           C  
ANISOU 3246  C   LEU A 438    10071   5378   5832   -128    630    392       C  
ATOM   3247  O   LEU A 438     -49.209 -16.600 -37.773  1.00 56.36           O  
ANISOU 3247  O   LEU A 438     9871   5586   5956   -118    608    405       O  
ATOM   3248  CB  LEU A 438     -50.253 -19.235 -35.979  1.00 57.95           C  
ANISOU 3248  CB  LEU A 438    10550   5470   5999   -236    572    484       C  
ATOM   3249  CG  LEU A 438     -51.145 -18.775 -34.829  1.00 59.30           C  
ANISOU 3249  CG  LEU A 438    10620   5729   6182   -339    567    558       C  
ATOM   3250  CD1 LEU A 438     -50.720 -19.443 -33.528  1.00 63.49           C  
ANISOU 3250  CD1 LEU A 438    11349   6134   6642   -231    561    604       C  
ATOM   3251  CD2 LEU A 438     -51.110 -17.263 -34.702  1.00 53.99           C  
ANISOU 3251  CD2 LEU A 438     9665   5252   5598   -294    560    558       C  
ATOM   3252  N   ARG A 439     -48.245 -18.578 -38.259  1.00 56.90           N  
ANISOU 3252  N   ARG A 439    10334   5342   5942     41    736    347       N  
ATOM   3253  CA  ARG A 439     -47.024 -17.934 -38.732  1.00 58.85           C  
ANISOU 3253  CA  ARG A 439    10403   5640   6318    230    846    324       C  
ATOM   3254  C   ARG A 439     -47.305 -17.026 -39.924  1.00 60.13           C  
ANISOU 3254  C   ARG A 439    10538   5891   6420    109    900    289       C  
ATOM   3255  O   ARG A 439     -46.713 -15.944 -40.044  1.00 56.11           O  
ANISOU 3255  O   ARG A 439     9784   5507   6028    170    939    300       O  
ATOM   3256  CB  ARG A 439     -45.977 -18.989 -39.090  1.00 59.69           C  
ANISOU 3256  CB  ARG A 439    10672   5539   6468    454   1018    297       C  
ATOM   3257  CG  ARG A 439     -45.524 -19.840 -37.912  1.00 58.92           C  
ANISOU 3257  CG  ARG A 439    10593   5335   6457    623    933    360       C  
ATOM   3258  CD  ARG A 439     -44.287 -20.648 -38.264  1.00 61.35           C  
ANISOU 3258  CD  ARG A 439    10945   5454   6912    922   1121    362       C  
ATOM   3259  NE  ARG A 439     -43.714 -21.316 -37.100  1.00 62.56           N  
ANISOU 3259  NE  ARG A 439    11059   5516   7195   1122    981    458       N  
ATOM   3260  CZ  ARG A 439     -43.863 -22.608 -36.830  1.00 65.58           C  
ANISOU 3260  CZ  ARG A 439    11780   5653   7485   1196    995    474       C  
ATOM   3261  NH1 ARG A 439     -44.567 -23.383 -37.646  1.00 64.74           N  
ANISOU 3261  NH1 ARG A 439    12077   5362   7157   1062   1144    386       N  
ATOM   3262  NH2 ARG A 439     -43.303 -23.127 -35.746  1.00 73.75           N  
ANISOU 3262  NH2 ARG A 439    12785   6601   8634   1388    830    586       N  
ATOM   3263  N   LYS A 440     -48.213 -17.444 -40.812  1.00 63.35           N  
ANISOU 3263  N   LYS A 440    11219   6217   6635    -86    873    259       N  
ATOM   3264  CA  LYS A 440     -48.577 -16.607 -41.950  1.00 60.50           C  
ANISOU 3264  CA  LYS A 440    10896   5919   6174   -219    862    248       C  
ATOM   3265  C   LYS A 440     -49.217 -15.304 -41.485  1.00 60.22           C  
ANISOU 3265  C   LYS A 440    10534   6100   6248   -298    712    321       C  
ATOM   3266  O   LYS A 440     -48.863 -14.218 -41.961  1.00 62.02           O  
ANISOU 3266  O   LYS A 440    10638   6416   6512   -270    757    330       O  
ATOM   3267  CB  LYS A 440     -49.517 -17.371 -42.885  1.00 63.90           C  
ANISOU 3267  CB  LYS A 440    11714   6203   6364   -453    762    220       C  
ATOM   3268  CG  LYS A 440     -49.713 -16.716 -44.244  1.00 70.04           C  
ANISOU 3268  CG  LYS A 440    12674   6973   6964   -577    739    208       C  
ATOM   3269  CD  LYS A 440     -50.484 -17.620 -45.198  1.00 79.32           C  
ANISOU 3269  CD  LYS A 440    14333   7950   7857   -824    600    171       C  
ATOM   3270  CE  LYS A 440     -51.974 -17.629 -44.890  1.00 85.06           C  
ANISOU 3270  CE  LYS A 440    14918   8767   8633  -1105    238    269       C  
ATOM   3271  NZ  LYS A 440     -52.622 -16.333 -45.240  1.00 87.07           N  
ANISOU 3271  NZ  LYS A 440    14916   9211   8957  -1194     40    372       N  
ATOM   3272  N   GLU A 441     -50.156 -15.392 -40.539  1.00 61.84           N  
ANISOU 3272  N   GLU A 441    10618   6367   6511   -389    574    378       N  
ATOM   3273  CA  GLU A 441     -50.803 -14.184 -40.036  1.00 61.78           C  
ANISOU 3273  CA  GLU A 441    10327   6526   6619   -427    492    447       C  
ATOM   3274  C   GLU A 441     -49.814 -13.273 -39.317  1.00 57.36           C  
ANISOU 3274  C   GLU A 441     9568   6047   6179   -252    567    435       C  
ATOM   3275  O   GLU A 441     -49.953 -12.043 -39.361  1.00 57.57           O  
ANISOU 3275  O   GLU A 441     9433   6172   6269   -255    550    463       O  
ATOM   3276  CB  GLU A 441     -51.963 -14.558 -39.115  1.00 62.87           C  
ANISOU 3276  CB  GLU A 441    10392   6684   6813   -540    420    515       C  
ATOM   3277  CG  GLU A 441     -53.019 -15.411 -39.796  1.00 67.68           C  
ANISOU 3277  CG  GLU A 441    11144   7217   7354   -772    294    550       C  
ATOM   3278  CD  GLU A 441     -54.214 -15.691 -38.909  1.00 73.78           C  
ANISOU 3278  CD  GLU A 441    11766   8017   8250   -906    266    645       C  
ATOM   3279  OE1 GLU A 441     -55.293 -16.011 -39.452  1.00 80.30           O  
ANISOU 3279  OE1 GLU A 441    12563   8832   9114  -1135    114    718       O  
ATOM   3280  OE2 GLU A 441     -54.075 -15.589 -37.673  1.00 75.29           O  
ANISOU 3280  OE2 GLU A 441    11877   8230   8500   -796    393    657       O  
ATOM   3281  N   ALA A 442     -48.806 -13.852 -38.661  1.00 54.14           N  
ANISOU 3281  N   ALA A 442     9179   5580   5813   -106    621    405       N  
ATOM   3282  CA  ALA A 442     -47.775 -13.038 -38.026  1.00 49.81           C  
ANISOU 3282  CA  ALA A 442     8437   5094   5395     21    624    405       C  
ATOM   3283  C   ALA A 442     -46.932 -12.309 -39.067  1.00 48.92           C  
ANISOU 3283  C   ALA A 442     8235   5007   5346     57    733    385       C  
ATOM   3284  O   ALA A 442     -46.670 -11.105 -38.937  1.00 49.59           O  
ANISOU 3284  O   ALA A 442     8154   5174   5513     44    714    400       O  
ATOM   3285  CB  ALA A 442     -46.896 -13.911 -37.130  1.00 49.35           C  
ANISOU 3285  CB  ALA A 442     8403   4954   5395    166    592    410       C  
ATOM   3286  N   ALA A 443     -46.492 -13.025 -40.107  1.00 48.57           N  
ANISOU 3286  N   ALA A 443     8342   4864   5249     96    880    350       N  
ATOM   3287  CA  ALA A 443     -45.703 -12.390 -41.160  1.00 48.77           C  
ANISOU 3287  CA  ALA A 443     8332   4887   5312    124   1061    338       C  
ATOM   3288  C   ALA A 443     -46.493 -11.281 -41.845  1.00 47.71           C  
ANISOU 3288  C   ALA A 443     8233   4823   5071    -29   1007    361       C  
ATOM   3289  O   ALA A 443     -45.938 -10.226 -42.184  1.00 45.39           O  
ANISOU 3289  O   ALA A 443     7818   4574   4855    -30   1087    380       O  
ATOM   3290  CB  ALA A 443     -45.244 -13.434 -42.177  1.00 51.89           C  
ANISOU 3290  CB  ALA A 443     8989   5115   5610    194   1287    288       C  
ATOM   3291  N   LYS A 444     -47.795 -11.500 -42.048  1.00 48.67           N  
ANISOU 3291  N   LYS A 444     8505   4945   5043   -164    855    379       N  
ATOM   3292  CA  LYS A 444     -48.649 -10.441 -42.573  1.00 49.14           C  
ANISOU 3292  CA  LYS A 444     8552   5068   5049   -281    744    437       C  
ATOM   3293  C   LYS A 444     -48.703  -9.254 -41.620  1.00 52.11           C  
ANISOU 3293  C   LYS A 444     8660   5550   5588   -241    690    476       C  
ATOM   3294  O   LYS A 444     -48.648  -8.096 -42.055  1.00 53.54           O  
ANISOU 3294  O   LYS A 444     8799   5757   5787   -261    702    512       O  
ATOM   3295  CB  LYS A 444     -50.052 -10.985 -42.842  1.00 57.14           C  
ANISOU 3295  CB  LYS A 444     9692   6066   5953   -434    545    480       C  
ATOM   3296  CG  LYS A 444     -51.138  -9.923 -42.822  1.00 67.61           C  
ANISOU 3296  CG  LYS A 444    10854   7485   7350   -504    376    583       C  
ATOM   3297  CD  LYS A 444     -52.425 -10.412 -43.464  1.00 74.51           C  
ANISOU 3297  CD  LYS A 444    11828   8335   8148   -686    142    658       C  
ATOM   3298  CE  LYS A 444     -53.511  -9.352 -43.365  1.00 77.98           C  
ANISOU 3298  CE  LYS A 444    12019   8865   8746   -707    -21    794       C  
ATOM   3299  NZ  LYS A 444     -54.690  -9.660 -44.220  1.00 82.76           N  
ANISOU 3299  NZ  LYS A 444    12684   9449   9314   -900   -321    905       N  
ATOM   3300  N   LEU A 445     -48.796  -9.521 -40.313  1.00 49.35           N  
ANISOU 3300  N   LEU A 445     8191   5231   5329   -190    640    469       N  
ATOM   3301  CA  LEU A 445     -48.856  -8.427 -39.347  1.00 46.60           C  
ANISOU 3301  CA  LEU A 445     7688   4936   5081   -160    605    488       C  
ATOM   3302  C   LEU A 445     -47.589  -7.580 -39.385  1.00 47.13           C  
ANISOU 3302  C   LEU A 445     7661   5005   5241   -121    665    465       C  
ATOM   3303  O   LEU A 445     -47.660  -6.345 -39.364  1.00 38.56           O  
ANISOU 3303  O   LEU A 445     6527   3930   4193   -149    658    486       O  
ATOM   3304  CB  LEU A 445     -49.093  -8.973 -37.941  1.00 43.03           C  
ANISOU 3304  CB  LEU A 445     7231   4476   4643   -123    562    479       C  
ATOM   3305  CG  LEU A 445     -49.251  -7.905 -36.856  1.00 46.47           C  
ANISOU 3305  CG  LEU A 445     7620   4919   5117   -100    548    483       C  
ATOM   3306  CD1 LEU A 445     -50.427  -6.998 -37.171  1.00 47.36           C  
ANISOU 3306  CD1 LEU A 445     7684   5052   5258   -125    580    543       C  
ATOM   3307  CD2 LEU A 445     -49.415  -8.544 -35.481  1.00 46.69           C  
ANISOU 3307  CD2 LEU A 445     7745   4904   5090    -72    528    473       C  
ATOM   3308  N   ARG A 446     -46.418  -8.221 -39.438  1.00 50.49           N  
ANISOU 3308  N   ARG A 446     8042   5404   5736    -59    731    434       N  
ATOM   3309  CA  ARG A 446     -45.176  -7.463 -39.571  1.00 53.88           C  
ANISOU 3309  CA  ARG A 446     8312   5839   6322    -50    797    438       C  
ATOM   3310  C   ARG A 446     -45.175  -6.645 -40.859  1.00 52.54           C  
ANISOU 3310  C   ARG A 446     8204   5655   6105   -120    940    460       C  
ATOM   3311  O   ARG A 446     -44.862  -5.441 -40.855  1.00 52.40           O  
ANISOU 3311  O   ARG A 446     8108   5641   6160   -182    945    483       O  
ATOM   3312  CB  ARG A 446     -43.975  -8.410 -39.539  1.00 56.59           C  
ANISOU 3312  CB  ARG A 446     8540   6150   6812     59    874    433       C  
ATOM   3313  CG  ARG A 446     -43.803  -9.188 -38.240  1.00 60.12           C  
ANISOU 3313  CG  ARG A 446     8948   6587   7309    138    692    436       C  
ATOM   3314  CD  ARG A 446     -42.522 -10.011 -38.273  1.00 64.55           C  
ANISOU 3314  CD  ARG A 446     9337   7103   8084    282    755    464       C  
ATOM   3315  NE  ARG A 446     -42.116 -10.468 -36.947  1.00 71.63           N  
ANISOU 3315  NE  ARG A 446    10163   7986   9065    350    504    500       N  
ATOM   3316  CZ  ARG A 446     -42.245 -11.717 -36.513  1.00 78.83           C  
ANISOU 3316  CZ  ARG A 446    11206   8822   9923    467    456    510       C  
ATOM   3317  NH1 ARG A 446     -42.769 -12.647 -37.301  1.00 81.54           N  
ANISOU 3317  NH1 ARG A 446    11752   9094  10136    514    650    473       N  
ATOM   3318  NH2 ARG A 446     -41.848 -12.037 -35.289  1.00 81.25           N  
ANISOU 3318  NH2 ARG A 446    11489   9101  10281    520    194    562       N  
ATOM   3319  N   ASP A 447     -45.548  -7.286 -41.973  1.00 49.85           N  
ANISOU 3319  N   ASP A 447     8063   5269   5609   -129   1046    456       N  
ATOM   3320  CA  ASP A 447     -45.502  -6.622 -43.271  1.00 55.88           C  
ANISOU 3320  CA  ASP A 447     8980   5987   6266   -200   1184    486       C  
ATOM   3321  C   ASP A 447     -46.374  -5.371 -43.289  1.00 53.16           C  
ANISOU 3321  C   ASP A 447     8658   5666   5876   -276   1041    544       C  
ATOM   3322  O   ASP A 447     -45.923  -4.297 -43.704  1.00 52.08           O  
ANISOU 3322  O   ASP A 447     8516   5500   5773   -324   1129    580       O  
ATOM   3323  CB  ASP A 447     -45.925  -7.595 -44.371  1.00 60.49           C  
ANISOU 3323  CB  ASP A 447     9884   6485   6615   -222   1255    466       C  
ATOM   3324  CG  ASP A 447     -45.849  -6.977 -45.752  1.00 63.54           C  
ANISOU 3324  CG  ASP A 447    10532   6789   6820   -304   1398    500       C  
ATOM   3325  OD1 ASP A 447     -44.721  -6.792 -46.259  1.00 63.22           O  
ANISOU 3325  OD1 ASP A 447    10485   6693   6843   -272   1698    493       O  
ATOM   3326  OD2 ASP A 447     -46.915  -6.680 -46.331  1.00 66.67           O  
ANISOU 3326  OD2 ASP A 447    11139   7169   7023   -402   1210    551       O  
ATOM   3327  N   ILE A 448     -47.626  -5.486 -42.837  1.00 51.81           N  
ANISOU 3327  N   ILE A 448     8500   5530   5654   -282    845    569       N  
ATOM   3328  CA  ILE A 448     -48.497  -4.314 -42.813  1.00 53.46           C  
ANISOU 3328  CA  ILE A 448     8697   5742   5872   -303    734    644       C  
ATOM   3329  C   ILE A 448     -48.033  -3.322 -41.755  1.00 54.69           C  
ANISOU 3329  C   ILE A 448     8703   5897   6177   -272    751    624       C  
ATOM   3330  O   ILE A 448     -48.276  -2.115 -41.875  1.00 60.14           O  
ANISOU 3330  O   ILE A 448     9423   6539   6887   -283    742    674       O  
ATOM   3331  CB  ILE A 448     -49.967  -4.726 -42.603  1.00 56.83           C  
ANISOU 3331  CB  ILE A 448     9108   6204   6281   -305    555    700       C  
ATOM   3332  CG1 ILE A 448     -50.893  -3.518 -42.770  1.00 57.25           C  
ANISOU 3332  CG1 ILE A 448     9126   6239   6387   -285    458    810       C  
ATOM   3333  CG2 ILE A 448     -50.166  -5.349 -41.231  1.00 59.78           C  
ANISOU 3333  CG2 ILE A 448     9344   6621   6750   -251    547    653       C  
ATOM   3334  CD1 ILE A 448     -50.676  -2.748 -44.063  1.00 58.08           C  
ANISOU 3334  CD1 ILE A 448     9421   6274   6373   -337    451    878       C  
ATOM   3335  N   SER A 449     -47.345  -3.799 -40.716  1.00 52.46           N  
ANISOU 3335  N   SER A 449     8306   5641   5986   -241    752    556       N  
ATOM   3336  CA  SER A 449     -46.806  -2.887 -39.714  1.00 48.65           C  
ANISOU 3336  CA  SER A 449     7751   5129   5605   -255    718    529       C  
ATOM   3337  C   SER A 449     -45.728  -1.986 -40.302  1.00 51.89           C  
ANISOU 3337  C   SER A 449     8121   5494   6100   -342    808    543       C  
ATOM   3338  O   SER A 449     -45.520  -0.869 -39.811  1.00 52.07           O  
ANISOU 3338  O   SER A 449     8157   5452   6175   -401    769    541       O  
ATOM   3339  CB  SER A 449     -46.254  -3.673 -38.525  1.00 51.30           C  
ANISOU 3339  CB  SER A 449     8011   5487   5993   -224    633    474       C  
ATOM   3340  OG  SER A 449     -47.279  -4.408 -37.878  1.00 59.29           O  
ANISOU 3340  OG  SER A 449     9093   6515   6918   -166    586    470       O  
ATOM   3341  N   THR A 450     -45.034  -2.442 -41.353  1.00 48.79           N  
ANISOU 3341  N   THR A 450     7710   5110   5718   -361    960    558       N  
ATOM   3342  CA  THR A 450     -44.031  -1.577 -41.974  1.00 48.87           C  
ANISOU 3342  CA  THR A 450     7672   5067   5829   -460   1110    591       C  
ATOM   3343  C   THR A 450     -44.632  -0.301 -42.564  1.00 51.89           C  
ANISOU 3343  C   THR A 450     8243   5365   6109   -523   1122    650       C  
ATOM   3344  O   THR A 450     -43.899   0.672 -42.776  1.00 48.59           O  
ANISOU 3344  O   THR A 450     7806   4875   5782   -634   1212    679       O  
ATOM   3345  CB  THR A 450     -43.268  -2.320 -43.074  1.00 55.89           C  
ANISOU 3345  CB  THR A 450     8558   5949   6727   -446   1364    603       C  
ATOM   3346  OG1 THR A 450     -44.131  -2.547 -44.197  1.00 57.39           O  
ANISOU 3346  OG1 THR A 450     9050   6100   6657   -437   1422    628       O  
ATOM   3347  CG2 THR A 450     -42.739  -3.651 -42.557  1.00 58.30           C  
ANISOU 3347  CG2 THR A 450     8698   6307   7145   -336   1365    559       C  
ATOM   3348  N   ALA A 451     -45.937  -0.272 -42.827  1.00 48.78           N  
ANISOU 3348  N   ALA A 451     8013   4965   5557   -458   1022    687       N  
ATOM   3349  CA  ALA A 451     -46.570   0.862 -43.487  1.00 47.53           C  
ANISOU 3349  CA  ALA A 451     8038   4710   5313   -479   1007    775       C  
ATOM   3350  C   ALA A 451     -47.278   1.809 -42.527  1.00 52.96           C  
ANISOU 3350  C   ALA A 451     8723   5336   6063   -421    893    782       C  
ATOM   3351  O   ALA A 451     -47.786   2.846 -42.966  1.00 51.26           O  
ANISOU 3351  O   ALA A 451     8653   5010   5812   -406    882    866       O  
ATOM   3352  CB  ALA A 451     -47.566   0.368 -44.541  1.00 42.24           C  
ANISOU 3352  CB  ALA A 451     7548   4047   4456   -444    934    849       C  
ATOM   3353  N   VAL A 452     -47.319   1.490 -41.234  1.00 55.88           N  
ANISOU 3353  N   VAL A 452     8979   5744   6506   -378    827    703       N  
ATOM   3354  CA  VAL A 452     -48.090   2.293 -40.291  1.00 51.61           C  
ANISOU 3354  CA  VAL A 452     8507   5114   5989   -298    783    699       C  
ATOM   3355  C   VAL A 452     -47.370   3.598 -39.966  1.00 51.88           C  
ANISOU 3355  C   VAL A 452     8659   4991   6063   -398    815    674       C  
ATOM   3356  O   VAL A 452     -47.961   4.682 -40.025  1.00 47.98           O  
ANISOU 3356  O   VAL A 452     8324   4349   5556   -343    844    724       O  
ATOM   3357  CB  VAL A 452     -48.389   1.472 -39.023  1.00 47.30           C  
ANISOU 3357  CB  VAL A 452     7895   4629   5449   -233    736    622       C  
ATOM   3358  CG1 VAL A 452     -48.878   2.371 -37.902  1.00 43.65           C  
ANISOU 3358  CG1 VAL A 452     7578   4026   4981   -170    765    588       C  
ATOM   3359  CG2 VAL A 452     -49.417   0.394 -39.331  1.00 47.48           C  
ANISOU 3359  CG2 VAL A 452     7830   4763   5448   -145    710    671       C  
ATOM   3360  N   VAL A 453     -46.083   3.515 -39.613  1.00 54.41           N  
ANISOU 3360  N   VAL A 453     8896   5323   6454   -552    795    609       N  
ATOM   3361  CA  VAL A 453     -45.338   4.732 -39.269  1.00 53.82           C  
ANISOU 3361  CA  VAL A 453     8930   5087   6434   -710    782    587       C  
ATOM   3362  C   VAL A 453     -45.205   5.678 -40.449  1.00 58.50           C  
ANISOU 3362  C   VAL A 453     9632   5571   7024   -782    907    680       C  
ATOM   3363  O   VAL A 453     -45.366   6.894 -40.255  1.00 60.26           O  
ANISOU 3363  O   VAL A 453    10072   5597   7228   -821    915    691       O  
ATOM   3364  CB  VAL A 453     -43.985   4.357 -38.636  1.00 51.62           C  
ANISOU 3364  CB  VAL A 453     8466   4859   6290   -882    673    527       C  
ATOM   3365  CG1 VAL A 453     -43.138   5.601 -38.421  1.00 50.34           C  
ANISOU 3365  CG1 VAL A 453     8391   4525   6213  -1114    627    521       C  
ATOM   3366  CG2 VAL A 453     -44.203   3.625 -37.314  1.00 47.91           C  
ANISOU 3366  CG2 VAL A 453     8007   4432   5763   -814    508    445       C  
ATOM   3367  N   PRO A 454     -44.909   5.232 -41.680  1.00 58.18           N  
ANISOU 3367  N   PRO A 454     9522   5611   6973   -807   1026    751       N  
ATOM   3368  CA  PRO A 454     -44.830   6.199 -42.789  1.00 54.62           C  
ANISOU 3368  CA  PRO A 454     9264   5022   6468   -884   1154    854       C  
ATOM   3369  C   PRO A 454     -46.112   6.983 -43.015  1.00 56.15           C  
ANISOU 3369  C   PRO A 454     9703   5083   6546   -728   1097    935       C  
ATOM   3370  O   PRO A 454     -46.053   8.200 -43.238  1.00 63.24           O  
ANISOU 3370  O   PRO A 454    10815   5780   7434   -788   1142    992       O  
ATOM   3371  CB  PRO A 454     -44.483   5.314 -43.993  1.00 57.96           C  
ANISOU 3371  CB  PRO A 454     9640   5553   6829   -896   1303    903       C  
ATOM   3372  CG  PRO A 454     -43.741   4.178 -43.403  1.00 57.02           C  
ANISOU 3372  CG  PRO A 454     9226   5592   6846   -904   1300    814       C  
ATOM   3373  CD  PRO A 454     -44.421   3.902 -42.095  1.00 56.16           C  
ANISOU 3373  CD  PRO A 454     9063   5530   6746   -793   1083    736       C  
ATOM   3374  N   ALA A 455     -47.273   6.326 -42.960  1.00 51.74           N  
ANISOU 3374  N   ALA A 455     9103   4620   5935   -530    997    960       N  
ATOM   3375  CA  ALA A 455     -48.533   7.031 -43.186  1.00 52.62           C  
ANISOU 3375  CA  ALA A 455     9361   4615   6016   -352    929   1073       C  
ATOM   3376  C   ALA A 455     -48.791   8.058 -42.091  1.00 51.91           C  
ANISOU 3376  C   ALA A 455     9381   4340   6003   -280    956   1027       C  
ATOM   3377  O   ALA A 455     -49.121   9.220 -42.370  1.00 60.78           O  
ANISOU 3377  O   ALA A 455    10723   5248   7123   -224    986   1113       O  
ATOM   3378  CB  ALA A 455     -49.684   6.030 -43.273  1.00 45.82           C  
ANISOU 3378  CB  ALA A 455     8349   3909   5153   -188    804   1121       C  
ATOM   3379  N   ALA A 456     -48.639   7.644 -40.831  1.00 49.70           N  
ANISOU 3379  N   ALA A 456     9010   4109   5764   -279    951    891       N  
ATOM   3380  CA  ALA A 456     -48.806   8.577 -39.722  1.00 52.36           C  
ANISOU 3380  CA  ALA A 456     9551   4231   6112   -234   1001    820       C  
ATOM   3381  C   ALA A 456     -47.809   9.722 -39.805  1.00 52.31           C  
ANISOU 3381  C   ALA A 456     9771   4012   6091   -451   1026    794       C  
ATOM   3382  O   ALA A 456     -48.106  10.834 -39.357  1.00 62.70           O  
ANISOU 3382  O   ALA A 456    11373   5062   7388   -400   1086    784       O  
ATOM   3383  CB  ALA A 456     -48.667   7.843 -38.389  1.00 51.46           C  
ANISOU 3383  CB  ALA A 456     9378   4195   5978   -243    972    677       C  
ATOM   3384  N   ARG A 457     -46.629   9.477 -40.376  1.00 49.93           N  
ANISOU 3384  N   ARG A 457     9351   3801   5819   -695   1009    790       N  
ATOM   3385  CA  ARG A 457     -45.659  10.549 -40.555  1.00 52.18           C  
ANISOU 3385  CA  ARG A 457     9805   3887   6134   -947   1045    793       C  
ATOM   3386  C   ARG A 457     -46.056  11.488 -41.688  1.00 57.10           C  
ANISOU 3386  C   ARG A 457    10658   4334   6704   -901   1148    942       C  
ATOM   3387  O   ARG A 457     -45.734  12.679 -41.636  1.00 56.02           O  
ANISOU 3387  O   ARG A 457    10792   3928   6564  -1028   1192    954       O  
ATOM   3388  CB  ARG A 457     -44.266   9.970 -40.810  1.00 53.58           C  
ANISOU 3388  CB  ARG A 457     9712   4219   6429  -1213   1039    770       C  
ATOM   3389  CG  ARG A 457     -43.131  10.928 -40.473  1.00 62.54           C  
ANISOU 3389  CG  ARG A 457    10927   5168   7668  -1538   1010    740       C  
ATOM   3390  CD  ARG A 457     -41.765  10.306 -40.718  1.00 66.47           C  
ANISOU 3390  CD  ARG A 457    11047   5833   8376  -1779   1019    751       C  
ATOM   3391  NE  ARG A 457     -41.514   9.151 -39.862  1.00 64.34           N  
ANISOU 3391  NE  ARG A 457    10496   5773   8179  -1728    850    667       N  
ATOM   3392  CZ  ARG A 457     -40.935   9.221 -38.667  1.00 66.31           C  
ANISOU 3392  CZ  ARG A 457    10713   5981   8501  -1888    601    580       C  
ATOM   3393  NH1 ARG A 457     -40.550  10.394 -38.180  1.00 66.46           N  
ANISOU 3393  NH1 ARG A 457    10975   5752   8527  -2132    493    550       N  
ATOM   3394  NH2 ARG A 457     -40.742   8.118 -37.956  1.00 65.94           N  
ANISOU 3394  NH2 ARG A 457    10441   6116   8499  -1819    436    529       N  
ATOM   3395  N   VAL A 458     -46.752  10.980 -42.710  1.00 54.94           N  
ANISOU 3395  N   VAL A 458    10324   4181   6371   -737   1158   1064       N  
ATOM   3396  CA  VAL A 458     -47.304  11.865 -43.729  1.00 58.71           C  
ANISOU 3396  CA  VAL A 458    11068   4470   6769   -654   1192   1232       C  
ATOM   3397  C   VAL A 458     -48.377  12.757 -43.125  1.00 62.99           C  
ANISOU 3397  C   VAL A 458    11804   4786   7342   -404   1168   1266       C  
ATOM   3398  O   VAL A 458     -48.445  13.957 -43.424  1.00 70.09           O  
ANISOU 3398  O   VAL A 458    13016   5398   8218   -399   1221   1350       O  
ATOM   3399  CB  VAL A 458     -47.854  11.061 -44.921  1.00 59.49           C  
ANISOU 3399  CB  VAL A 458    11103   4736   6765   -553   1134   1360       C  
ATOM   3400  CG1 VAL A 458     -48.528  11.998 -45.925  1.00 56.40           C  
ANISOU 3400  CG1 VAL A 458    11026   4129   6274   -448   1094   1561       C  
ATOM   3401  CG2 VAL A 458     -46.745  10.271 -45.593  1.00 59.18           C  
ANISOU 3401  CG2 VAL A 458    10955   4854   6676   -779   1249   1326       C  
ATOM   3402  N   VAL A 459     -49.233  12.193 -42.269  1.00 54.62           N  
ANISOU 3402  N   VAL A 459    10577   3828   6347   -182   1127   1209       N  
ATOM   3403  CA  VAL A 459     -50.240  13.023 -41.615  1.00 60.34           C  
ANISOU 3403  CA  VAL A 459    11469   4318   7138     89   1190   1239       C  
ATOM   3404  C   VAL A 459     -49.579  14.046 -40.699  1.00 61.78           C  
ANISOU 3404  C   VAL A 459    11985   4208   7282    -52   1292   1102       C  
ATOM   3405  O   VAL A 459     -49.979  15.216 -40.663  1.00 60.74           O  
ANISOU 3405  O   VAL A 459    12173   3749   7155     73   1383   1160       O  
ATOM   3406  CB  VAL A 459     -51.250  12.150 -40.852  1.00 55.28           C  
ANISOU 3406  CB  VAL A 459    10565   3845   6593    334   1194   1210       C  
ATOM   3407  CG1 VAL A 459     -52.127  13.015 -39.955  1.00 57.40           C  
ANISOU 3407  CG1 VAL A 459    11022   3839   6947    610   1364   1207       C  
ATOM   3408  CG2 VAL A 459     -52.104  11.378 -41.830  1.00 54.42           C  
ANISOU 3408  CG2 VAL A 459    10181   3949   6546    473   1049   1383       C  
ATOM   3409  N   LEU A 460     -48.547  13.626 -39.962  1.00 64.23           N  
ANISOU 3409  N   LEU A 460    12245   4608   7553   -323   1253    930       N  
ATOM   3410  CA  LEU A 460     -47.888  14.514 -39.009  1.00 66.54           C  
ANISOU 3410  CA  LEU A 460    12876   4618   7786   -515   1274    790       C  
ATOM   3411  C   LEU A 460     -47.359  15.773 -39.688  1.00 69.85           C  
ANISOU 3411  C   LEU A 460    13604   4745   8191   -694   1317    865       C  
ATOM   3412  O   LEU A 460     -47.425  16.868 -39.117  1.00 64.56           O  
ANISOU 3412  O   LEU A 460    13353   3712   7464   -704   1384    811       O  
ATOM   3413  CB  LEU A 460     -46.748  13.776 -38.309  1.00 58.15           C  
ANISOU 3413  CB  LEU A 460    11644   3733   6716   -822   1129    640       C  
ATOM   3414  CG  LEU A 460     -45.892  14.613 -37.356  1.00 60.79           C  
ANISOU 3414  CG  LEU A 460    12320   3793   6985  -1117   1045    500       C  
ATOM   3415  CD1 LEU A 460     -46.669  14.964 -36.093  1.00 62.11           C  
ANISOU 3415  CD1 LEU A 460    12873   3722   7005   -926   1118    376       C  
ATOM   3416  CD2 LEU A 460     -44.592  13.900 -37.022  1.00 60.36           C  
ANISOU 3416  CD2 LEU A 460    11986   3943   7004  -1462    830    427       C  
ATOM   3417  N   GLU A 461     -46.833  15.640 -40.906  1.00 69.92           N  
ANISOU 3417  N   GLU A 461    13466   4873   8226   -844   1308    989       N  
ATOM   3418  CA  GLU A 461     -46.225  16.756 -41.617  1.00 78.40           C  
ANISOU 3418  CA  GLU A 461    14830   5678   9281  -1063   1376   1077       C  
ATOM   3419  C   GLU A 461     -47.143  17.343 -42.686  1.00 77.86           C  
ANISOU 3419  C   GLU A 461    14887   5525   9169   -789   1418   1265       C  
ATOM   3420  O   GLU A 461     -46.673  18.070 -43.570  1.00 78.76           O  
ANISOU 3420  O   GLU A 461    15121   5560   9246   -938   1454   1347       O  
ATOM   3421  CB  GLU A 461     -44.894  16.318 -42.229  1.00 87.40           C  
ANISOU 3421  CB  GLU A 461    15724   7000  10485  -1439   1382   1086       C  
ATOM   3422  CG  GLU A 461     -43.794  16.123 -41.191  1.00 98.86           C  
ANISOU 3422  CG  GLU A 461    17031   8495  12035  -1763   1269    919       C  
ATOM   3423  CD  GLU A 461     -43.037  14.822 -41.367  1.00105.26           C  
ANISOU 3423  CD  GLU A 461    17339   9686  12970  -1876   1230    900       C  
ATOM   3424  OE1 GLU A 461     -42.936  14.341 -42.515  1.00110.53           O  
ANISOU 3424  OE1 GLU A 461    17842  10511  13644  -1847   1366   1016       O  
ATOM   3425  OE2 GLU A 461     -42.546  14.277 -40.354  1.00110.52           O  
ANISOU 3425  OE2 GLU A 461    17816  10468  13710  -1983   1065    772       O  
ATOM   3426  N   ASN A 462     -48.446  17.056 -42.614  1.00 76.76           N  
ANISOU 3426  N   ASN A 462    14700   5410   9056   -394   1398   1343       N  
ATOM   3427  CA  ASN A 462     -49.427  17.597 -43.558  1.00 71.49           C  
ANISOU 3427  CA  ASN A 462    14101   4669   8392   -109   1359   1545       C  
ATOM   3428  C   ASN A 462     -50.775  17.715 -42.860  1.00 67.57           C  
ANISOU 3428  C   ASN A 462    13570   4082   8020    317   1385   1577       C  
ATOM   3429  O   ASN A 462     -51.735  17.018 -43.204  1.00 69.01           O  
ANISOU 3429  O   ASN A 462    13528   4399   8292    579   1301   1725       O  
ATOM   3430  CB  ASN A 462     -49.531  16.711 -44.800  1.00 70.37           C  
ANISOU 3430  CB  ASN A 462    13790   4761   8187   -122   1252   1708       C  
ATOM   3431  CG  ASN A 462     -48.366  16.897 -45.749  1.00 71.05           C  
ANISOU 3431  CG  ASN A 462    13963   4880   8153   -471   1307   1720       C  
ATOM   3432  OD1 ASN A 462     -48.009  18.022 -46.094  1.00 74.06           O  
ANISOU 3432  OD1 ASN A 462    14577   5066   8498   -570   1361   1743       O  
ATOM   3433  ND2 ASN A 462     -47.762  15.792 -46.174  1.00 70.14           N  
ANISOU 3433  ND2 ASN A 462    13663   5002   7984   -650   1330   1705       N  
ATOM   3434  N   PRO A 463     -50.890  18.624 -41.885  1.00 74.95           N  
ANISOU 3434  N   PRO A 463    14727   4777   8972    395   1513   1448       N  
ATOM   3435  CA  PRO A 463     -52.114  18.660 -41.058  1.00 78.14           C  
ANISOU 3435  CA  PRO A 463    15075   5101   9513    803   1634   1451       C  
ATOM   3436  C   PRO A 463     -53.396  18.869 -41.851  1.00 82.18           C  
ANISOU 3436  C   PRO A 463    15425   5591  10210   1200   1573   1715       C  
ATOM   3437  O   PRO A 463     -54.352  18.100 -41.693  1.00 83.74           O  
ANISOU 3437  O   PRO A 463    15314   5921  10583   1477   1570   1815       O  
ATOM   3438  CB  PRO A 463     -51.846  19.827 -40.094  1.00 83.73           C  
ANISOU 3438  CB  PRO A 463    16162   5516  10136    762   1795   1269       C  
ATOM   3439  CG  PRO A 463     -50.367  20.043 -40.138  1.00 85.24           C  
ANISOU 3439  CG  PRO A 463    16528   5696  10165    272   1706   1136       C  
ATOM   3440  CD  PRO A 463     -49.954  19.702 -41.530  1.00 81.74           C  
ANISOU 3440  CD  PRO A 463    15913   5417   9728    117   1570   1307       C  
ATOM   3441  N   GLY A 464     -53.444  19.886 -42.706  1.00 84.36           N  
ANISOU 3441  N   GLY A 464    15884   5697  10471   1226   1502   1850       N  
ATOM   3442  CA  GLY A 464     -54.666  20.192 -43.426  1.00 86.85           C  
ANISOU 3442  CA  GLY A 464    16056   5957  10985   1604   1387   2122       C  
ATOM   3443  C   GLY A 464     -54.935  19.315 -44.632  1.00 84.06           C  
ANISOU 3443  C   GLY A 464    15466   5840  10631   1587   1091   2347       C  
ATOM   3444  O   GLY A 464     -55.543  19.767 -45.605  1.00 85.14           O  
ANISOU 3444  O   GLY A 464    15610   5907  10832   1743    887   2591       O  
ATOM   3445  N   ASN A 465     -54.500  18.058 -44.581  1.00 79.80           N  
ANISOU 3445  N   ASN A 465    14748   5569  10003   1392   1045   2273       N  
ATOM   3446  CA  ASN A 465     -54.655  17.126 -45.692  1.00 77.15           C  
ANISOU 3446  CA  ASN A 465    14257   5464   9593   1321    770   2449       C  
ATOM   3447  C   ASN A 465     -55.619  16.024 -45.268  1.00 73.70           C  
ANISOU 3447  C   ASN A 465    13358   5276   9369   1534    687   2493       C  
ATOM   3448  O   ASN A 465     -55.267  15.163 -44.455  1.00 72.91           O  
ANISOU 3448  O   ASN A 465    13047   5400   9257   1402    804   2275       O  
ATOM   3449  CB  ASN A 465     -53.306  16.547 -46.112  1.00 79.78           C  
ANISOU 3449  CB  ASN A 465    14710   5955   9646    879    791   2305       C  
ATOM   3450  CG  ASN A 465     -53.369  15.828 -47.445  1.00 84.20           C  
ANISOU 3450  CG  ASN A 465    15250   6701  10042    771    537   2467       C  
ATOM   3451  OD1 ASN A 465     -54.445  15.465 -47.920  1.00 87.94           O  
ANISOU 3451  OD1 ASN A 465    15561   7244  10610    994    275   2672       O  
ATOM   3452  ND2 ASN A 465     -52.209  15.616 -48.056  1.00 84.83           N  
ANISOU 3452  ND2 ASN A 465    15481   6866   9884    418    612   2372       N  
ATOM   3453  N   GLN A 466     -56.828  16.046 -45.832  1.00 73.20           N  
ANISOU 3453  N   GLN A 466    13077   5215   9521   1831    451   2768       N  
ATOM   3454  CA  GLN A 466     -57.824  15.044 -45.472  1.00 72.99           C  
ANISOU 3454  CA  GLN A 466    12510   5462   9763   1997    351   2819       C  
ATOM   3455  C   GLN A 466     -57.509  13.690 -46.095  1.00 72.86           C  
ANISOU 3455  C   GLN A 466    12317   5808   9559   1692     98   2771       C  
ATOM   3456  O   GLN A 466     -57.770  12.651 -45.477  1.00 70.42           O  
ANISOU 3456  O   GLN A 466    11647   5752   9357   1664    135   2664       O  
ATOM   3457  CB  GLN A 466     -59.217  15.515 -45.888  1.00 80.24           C  
ANISOU 3457  CB  GLN A 466    13185   6261  11041   2399    140   3160       C  
ATOM   3458  CG  GLN A 466     -60.359  14.670 -45.339  1.00 88.00           C  
ANISOU 3458  CG  GLN A 466    13547   7473  12418   2607    113   3239       C  
ATOM   3459  CD  GLN A 466     -60.629  14.921 -43.863  1.00 95.14           C  
ANISOU 3459  CD  GLN A 466    14338   8261  13551   2846    615   3080       C  
ATOM   3460  OE1 GLN A 466     -59.905  15.666 -43.203  1.00 99.66           O  
ANISOU 3460  OE1 GLN A 466    15331   8589  13946   2823    947   2880       O  
ATOM   3461  NE2 GLN A 466     -61.682  14.302 -43.341  1.00 95.90           N  
ANISOU 3461  NE2 GLN A 466    13893   8512  14034   3057    677   3174       N  
ATOM   3462  N   ALA A 467     -56.951  13.679 -47.309  1.00 69.22           N  
ANISOU 3462  N   ALA A 467    12156   5346   8799   1462   -126   2848       N  
ATOM   3463  CA  ALA A 467     -56.630  12.414 -47.964  1.00 74.84           C  
ANISOU 3463  CA  ALA A 467    12796   6348   9293   1182   -327   2795       C  
ATOM   3464  C   ALA A 467     -55.613  11.615 -47.159  1.00 68.59           C  
ANISOU 3464  C   ALA A 467    11931   5742   8388    946    -46   2478       C  
ATOM   3465  O   ALA A 467     -55.765  10.400 -46.984  1.00 60.90           O  
ANISOU 3465  O   ALA A 467    10680   5029   7428    862   -121   2398       O  
ATOM   3466  CB  ALA A 467     -56.112  12.672 -49.378  1.00 68.58           C  
ANISOU 3466  CB  ALA A 467    12460   5453   8145    981   -520   2919       C  
ATOM   3467  N   ALA A 468     -54.567  12.281 -46.662  1.00 67.72           N  
ANISOU 3467  N   ALA A 468    12071   5484   8177    828    248   2309       N  
ATOM   3468  CA  ALA A 468     -53.590  11.596 -45.822  1.00 61.92           C  
ANISOU 3468  CA  ALA A 468    11241   4906   7380    619    463   2035       C  
ATOM   3469  C   ALA A 468     -54.236  11.077 -44.546  1.00 59.21           C  
ANISOU 3469  C   ALA A 468    10561   4676   7260    790    555   1935       C  
ATOM   3470  O   ALA A 468     -53.889   9.994 -44.060  1.00 59.78           O  
ANISOU 3470  O   ALA A 468    10441   4974   7301    663    587   1780       O  
ATOM   3471  CB  ALA A 468     -52.428  12.533 -45.494  1.00 63.03           C  
ANISOU 3471  CB  ALA A 468    11689   4835   7423    445    698   1908       C  
ATOM   3472  N   LYS A 469     -55.186  11.835 -43.995  1.00 60.89           N  
ANISOU 3472  N   LYS A 469    10723   4710   7701   1094    629   2031       N  
ATOM   3473  CA  LYS A 469     -55.893  11.401 -42.794  1.00 65.94           C  
ANISOU 3473  CA  LYS A 469    11079   5420   8555   1280    789   1957       C  
ATOM   3474  C   LYS A 469     -56.684  10.125 -43.056  1.00 63.65           C  
ANISOU 3474  C   LYS A 469    10371   5424   8388   1293    590   2044       C  
ATOM   3475  O   LYS A 469     -56.601   9.157 -42.287  1.00 58.95           O  
ANISOU 3475  O   LYS A 469     9591   5011   7798   1217    686   1898       O  
ATOM   3476  CB  LYS A 469     -56.815  12.522 -42.314  1.00 72.08           C  
ANISOU 3476  CB  LYS A 469    11897   5910   9581   1643    960   2079       C  
ATOM   3477  CG  LYS A 469     -57.549  12.247 -41.015  1.00 76.45           C  
ANISOU 3477  CG  LYS A 469    12232   6465  10349   1864   1243   2006       C  
ATOM   3478  CD  LYS A 469     -58.458  13.419 -40.675  1.00 87.31           C  
ANISOU 3478  CD  LYS A 469    13672   7513  11990   2265   1466   2148       C  
ATOM   3479  CE  LYS A 469     -58.917  13.388 -39.228  1.00 90.07           C  
ANISOU 3479  CE  LYS A 469    14000   7761  12462   2464   1893   2016       C  
ATOM   3480  NZ  LYS A 469     -59.674  14.624 -38.876  1.00 96.37           N  
ANISOU 3480  NZ  LYS A 469    14949   8174  13494   2874   2194   2130       N  
ATOM   3481  N   ASP A 470     -57.454  10.105 -44.148  1.00 65.24           N  
ANISOU 3481  N   ASP A 470    10453   5657   8679   1368    280   2294       N  
ATOM   3482  CA  ASP A 470     -58.262   8.934 -44.469  1.00 65.13           C  
ANISOU 3482  CA  ASP A 470    10059   5893   8792   1340     27   2397       C  
ATOM   3483  C   ASP A 470     -57.384   7.732 -44.792  1.00 59.88           C  
ANISOU 3483  C   ASP A 470     9472   5448   7831   1006    -54   2226       C  
ATOM   3484  O   ASP A 470     -57.723   6.594 -44.443  1.00 57.54           O  
ANISOU 3484  O   ASP A 470     8905   5353   7605    939    -93   2176       O  
ATOM   3485  CB  ASP A 470     -59.197   9.244 -45.638  1.00 73.46           C  
ANISOU 3485  CB  ASP A 470    11031   6904   9977   1451   -374   2716       C  
ATOM   3486  CG  ASP A 470     -59.957  10.545 -45.449  1.00 85.19           C  
ANISOU 3486  CG  ASP A 470    12476   8126  11765   1817   -294   2913       C  
ATOM   3487  OD1 ASP A 470     -59.976  11.065 -44.313  1.00 91.06           O  
ANISOU 3487  OD1 ASP A 470    13203   8738  12659   2007    107   2799       O  
ATOM   3488  OD2 ASP A 470     -60.535  11.047 -46.436  1.00 87.90           O  
ANISOU 3488  OD2 ASP A 470    12845   8371  12184   1922   -636   3188       O  
ATOM   3489  N   TYR A 471     -56.246   7.963 -45.453  1.00 56.34           N  
ANISOU 3489  N   TYR A 471     9396   4944   7067    800    -46   2141       N  
ATOM   3490  CA  TYR A 471     -55.345   6.855 -45.744  1.00 54.62           C  
ANISOU 3490  CA  TYR A 471     9253   4901   6598    525    -50   1979       C  
ATOM   3491  C   TYR A 471     -54.730   6.296 -44.467  1.00 54.25           C  
ANISOU 3491  C   TYR A 471     9077   4953   6584    478    214   1741       C  
ATOM   3492  O   TYR A 471     -54.626   5.073 -44.306  1.00 51.26           O  
ANISOU 3492  O   TYR A 471     8557   4758   6162    368    183   1651       O  
ATOM   3493  CB  TYR A 471     -54.254   7.292 -46.720  1.00 53.91           C  
ANISOU 3493  CB  TYR A 471     9566   4707   6210    336    -18   1961       C  
ATOM   3494  CG  TYR A 471     -53.412   6.136 -47.210  1.00 57.12           C  
ANISOU 3494  CG  TYR A 471    10058   5266   6380     96      5   1831       C  
ATOM   3495  CD1 TYR A 471     -53.934   5.201 -48.093  1.00 58.24           C  
ANISOU 3495  CD1 TYR A 471    10234   5505   6388     15   -258   1913       C  
ATOM   3496  CD2 TYR A 471     -52.101   5.974 -46.783  1.00 53.88           C  
ANISOU 3496  CD2 TYR A 471     9696   4880   5896    -48    281   1636       C  
ATOM   3497  CE1 TYR A 471     -53.174   4.138 -48.540  1.00 66.36           C  
ANISOU 3497  CE1 TYR A 471    11399   6627   7187   -177   -187   1785       C  
ATOM   3498  CE2 TYR A 471     -51.332   4.917 -47.225  1.00 59.00           C  
ANISOU 3498  CE2 TYR A 471    10398   5644   6375   -217    349   1532       C  
ATOM   3499  CZ  TYR A 471     -51.874   3.999 -48.102  1.00 67.24           C  
ANISOU 3499  CZ  TYR A 471    11530   6759   7261   -268    144   1598       C  
ATOM   3500  OH  TYR A 471     -51.115   2.939 -48.547  1.00 71.69           O  
ANISOU 3500  OH  TYR A 471    12206   7392   7640   -412    259   1485       O  
ATOM   3501  N   LEU A 472     -54.322   7.176 -43.546  1.00 56.52           N  
ANISOU 3501  N   LEU A 472     9457   5091   6926    550    452   1644       N  
ATOM   3502  CA  LEU A 472     -53.808   6.714 -42.260  1.00 54.78           C  
ANISOU 3502  CA  LEU A 472     9168   4931   6714    506    647   1437       C  
ATOM   3503  C   LEU A 472     -54.854   5.901 -41.513  1.00 60.51           C  
ANISOU 3503  C   LEU A 472     9595   5780   7617    643    664   1456       C  
ATOM   3504  O   LEU A 472     -54.534   4.869 -40.910  1.00 59.17           O  
ANISOU 3504  O   LEU A 472     9332   5754   7395    544    705   1326       O  
ATOM   3505  CB  LEU A 472     -53.349   7.901 -41.413  1.00 53.04           C  
ANISOU 3505  CB  LEU A 472     9176   4478   6498    550    850   1346       C  
ATOM   3506  CG  LEU A 472     -52.991   7.604 -39.951  1.00 51.86           C  
ANISOU 3506  CG  LEU A 472     9040   4330   6334    527   1015   1153       C  
ATOM   3507  CD1 LEU A 472     -51.873   6.571 -39.854  1.00 50.14           C  
ANISOU 3507  CD1 LEU A 472     8765   4299   5988    285    949   1013       C  
ATOM   3508  CD2 LEU A 472     -52.612   8.877 -39.208  1.00 50.32           C  
ANISOU 3508  CD2 LEU A 472     9166   3849   6102    546   1174   1071       C  
ATOM   3509  N   ARG A 473     -56.114   6.346 -41.541  1.00 67.31           N  
ANISOU 3509  N   ARG A 473    10285   6573   8716    876    646   1634       N  
ATOM   3510  CA  ARG A 473     -57.168   5.578 -40.885  1.00 71.27           C  
ANISOU 3510  CA  ARG A 473    10448   7189   9442    991    699   1684       C  
ATOM   3511  C   ARG A 473     -57.350   4.217 -41.547  1.00 72.02           C  
ANISOU 3511  C   ARG A 473    10351   7516   9496    809    442   1720       C  
ATOM   3512  O   ARG A 473     -57.544   3.204 -40.862  1.00 76.30           O  
ANISOU 3512  O   ARG A 473    10730   8183  10076    756    518   1646       O  
ATOM   3513  CB  ARG A 473     -58.477   6.366 -40.897  1.00 77.65           C  
ANISOU 3513  CB  ARG A 473    11040   7873  10591   1292    735   1908       C  
ATOM   3514  CG  ARG A 473     -59.665   5.605 -40.334  1.00 83.40           C  
ANISOU 3514  CG  ARG A 473    11335   8718  11633   1407    811   2009       C  
ATOM   3515  CD  ARG A 473     -60.844   6.533 -40.108  1.00 93.62           C  
ANISOU 3515  CD  ARG A 473    12395   9848  13327   1760    968   2221       C  
ATOM   3516  NE  ARG A 473     -61.008   7.476 -41.211  1.00 99.09           N  
ANISOU 3516  NE  ARG A 473    13154  10418  14075   1862    698   2415       N  
ATOM   3517  CZ  ARG A 473     -61.953   8.410 -41.263  1.00103.99           C  
ANISOU 3517  CZ  ARG A 473    13594  10865  15054   2196    760   2640       C  
ATOM   3518  NH1 ARG A 473     -62.827   8.528 -40.273  1.00109.04           N  
ANISOU 3518  NH1 ARG A 473    13950  11433  16049   2470   1137   2693       N  
ATOM   3519  NH2 ARG A 473     -62.024   9.225 -42.307  1.00103.73           N  
ANISOU 3519  NH2 ARG A 473    13678  10707  15026   2272    469   2826       N  
ATOM   3520  N   THR A 474     -57.274   4.170 -42.879  1.00 67.25           N  
ANISOU 3520  N   THR A 474     9833   6940   8779    697    143   1830       N  
ATOM   3521  CA  THR A 474     -57.424   2.902 -43.587  1.00 64.38           C  
ANISOU 3521  CA  THR A 474     9392   6747   8322    500   -115   1852       C  
ATOM   3522  C   THR A 474     -56.314   1.925 -43.210  1.00 55.34           C  
ANISOU 3522  C   THR A 474     8387   5697   6943    315     19   1618       C  
ATOM   3523  O   THR A 474     -56.574   0.750 -42.915  1.00 55.59           O  
ANISOU 3523  O   THR A 474     8275   5853   6994    228    -14   1575       O  
ATOM   3524  CB  THR A 474     -57.435   3.144 -45.096  1.00 67.70           C  
ANISOU 3524  CB  THR A 474    10023   7124   8576    403   -443   1997       C  
ATOM   3525  OG1 THR A 474     -58.538   3.992 -45.440  1.00 72.40           O  
ANISOU 3525  OG1 THR A 474    10452   7628   9428    595   -633   2252       O  
ATOM   3526  CG2 THR A 474     -57.568   1.829 -45.834  1.00 68.18           C  
ANISOU 3526  CG2 THR A 474    10108   7314   8483    177   -709   1999       C  
ATOM   3527  N   VAL A 475     -55.064   2.396 -43.220  1.00 50.81           N  
ANISOU 3527  N   VAL A 475     8076   5053   6175    252    167   1483       N  
ATOM   3528  CA  VAL A 475     -53.946   1.545 -42.822  1.00 48.99           C  
ANISOU 3528  CA  VAL A 475     7923   4901   5790    113    291   1288       C  
ATOM   3529  C   VAL A 475     -54.115   1.094 -41.378  1.00 50.83           C  
ANISOU 3529  C   VAL A 475     8001   5179   6136    179    448   1188       C  
ATOM   3530  O   VAL A 475     -53.822  -0.059 -41.031  1.00 52.18           O  
ANISOU 3530  O   VAL A 475     8131   5450   6246     94    456   1095       O  
ATOM   3531  CB  VAL A 475     -52.610   2.281 -43.035  1.00 49.46           C  
ANISOU 3531  CB  VAL A 475     8211   4869   5713     34    421   1198       C  
ATOM   3532  CG1 VAL A 475     -51.449   1.427 -42.549  1.00 52.27           C  
ANISOU 3532  CG1 VAL A 475     8562   5305   5994    -79    534   1028       C  
ATOM   3533  CG2 VAL A 475     -52.432   2.635 -44.501  1.00 50.16           C  
ANISOU 3533  CG2 VAL A 475     8518   4896   5645    -49    316   1303       C  
ATOM   3534  N   LYS A 476     -54.609   1.989 -40.517  1.00 48.78           N  
ANISOU 3534  N   LYS A 476     7703   4812   6018    342    595   1209       N  
ATOM   3535  CA  LYS A 476     -54.871   1.622 -39.131  1.00 49.49           C  
ANISOU 3535  CA  LYS A 476     7728   4905   6172    410    783   1125       C  
ATOM   3536  C   LYS A 476     -55.868   0.474 -39.044  1.00 51.17           C  
ANISOU 3536  C   LYS A 476     7685   5247   6509    404    734   1201       C  
ATOM   3537  O   LYS A 476     -55.686  -0.457 -38.253  1.00 50.43           O  
ANISOU 3537  O   LYS A 476     7593   5212   6357    344    816   1106       O  
ATOM   3538  CB  LYS A 476     -55.385   2.833 -38.350  1.00 50.39           C  
ANISOU 3538  CB  LYS A 476     7905   4835   6405    609    996   1150       C  
ATOM   3539  CG  LYS A 476     -55.558   2.576 -36.859  1.00 49.84           C  
ANISOU 3539  CG  LYS A 476     7898   4713   6324    674   1247   1045       C  
ATOM   3540  CD  LYS A 476     -56.170   3.771 -36.137  1.00 54.75           C  
ANISOU 3540  CD  LYS A 476     8641   5109   7051    897   1520   1070       C  
ATOM   3541  CE  LYS A 476     -57.641   3.940 -36.483  1.00 58.20           C  
ANISOU 3541  CE  LYS A 476     8740   5548   7825   1115   1595   1287       C  
ATOM   3542  NZ  LYS A 476     -58.316   4.930 -35.595  1.00 60.93           N  
ANISOU 3542  NZ  LYS A 476     9193   5653   8305   1384   1968   1308       N  
ATOM   3543  N   GLU A 477     -56.927   0.520 -39.856  1.00 55.20           N  
ANISOU 3543  N   GLU A 477     7981   5791   7200    446    572   1390       N  
ATOM   3544  CA  GLU A 477     -57.919  -0.548 -39.815  1.00 58.41           C  
ANISOU 3544  CA  GLU A 477     8110   6313   7770    393    492   1485       C  
ATOM   3545  C   GLU A 477     -57.384  -1.845 -40.413  1.00 60.05           C  
ANISOU 3545  C   GLU A 477     8417   6629   7771    160    297   1409       C  
ATOM   3546  O   GLU A 477     -57.803  -2.932 -39.999  1.00 64.09           O  
ANISOU 3546  O   GLU A 477     8808   7210   8332     72    306   1402       O  
ATOM   3547  CB  GLU A 477     -59.195  -0.108 -40.529  1.00 62.22           C  
ANISOU 3547  CB  GLU A 477     8295   6796   8551    484    305   1736       C  
ATOM   3548  CG  GLU A 477     -59.879   1.072 -39.857  1.00 73.21           C  
ANISOU 3548  CG  GLU A 477     9546   8056  10216    769    562   1834       C  
ATOM   3549  CD  GLU A 477     -61.045   1.609 -40.662  1.00 81.23           C  
ANISOU 3549  CD  GLU A 477    10238   9056  11569    896    333   2116       C  
ATOM   3550  OE1 GLU A 477     -62.196   1.526 -40.181  1.00 88.59           O  
ANISOU 3550  OE1 GLU A 477    10764  10003  12892   1030    454   2275       O  
ATOM   3551  OE2 GLU A 477     -60.808   2.110 -41.782  1.00 82.90           O  
ANISOU 3551  OE2 GLU A 477    10599   9233  11668    860     32   2196       O  
ATOM   3552  N   LYS A 478     -56.468  -1.761 -41.382  1.00 56.83           N  
ANISOU 3552  N   LYS A 478     8254   6210   7130     60    158   1353       N  
ATOM   3553  CA  LYS A 478     -55.824  -2.979 -41.866  1.00 53.70           C  
ANISOU 3553  CA  LYS A 478     8014   5870   6519   -122     64   1254       C  
ATOM   3554  C   LYS A 478     -54.967  -3.614 -40.779  1.00 49.95           C  
ANISOU 3554  C   LYS A 478     7605   5410   5965   -121    274   1081       C  
ATOM   3555  O   LYS A 478     -55.014  -4.837 -40.575  1.00 51.28           O  
ANISOU 3555  O   LYS A 478     7775   5621   6088   -213    253   1037       O  
ATOM   3556  CB  LYS A 478     -54.983  -2.681 -43.107  1.00 58.90           C  
ANISOU 3556  CB  LYS A 478     8950   6481   6947   -203    -33   1234       C  
ATOM   3557  CG  LYS A 478     -55.807  -2.329 -44.329  1.00 63.44           C  
ANISOU 3557  CG  LYS A 478     9561   7027   7515   -251   -327   1414       C  
ATOM   3558  CD  LYS A 478     -56.760  -3.459 -44.672  1.00 67.74           C  
ANISOU 3558  CD  LYS A 478    10007   7631   8098   -398   -586   1494       C  
ATOM   3559  CE  LYS A 478     -57.866  -2.984 -45.595  1.00 74.51           C  
ANISOU 3559  CE  LYS A 478    10782   8466   9060   -427   -954   1726       C  
ATOM   3560  NZ  LYS A 478     -58.827  -4.077 -45.905  1.00 78.41           N  
ANISOU 3560  NZ  LYS A 478    11153   9013   9628   -621  -1264   1819       N  
ATOM   3561  N   TRP A 479     -54.188  -2.797 -40.064  1.00 45.56           N  
ANISOU 3561  N   TRP A 479     7127   4797   5387    -31    445    993       N  
ATOM   3562  CA  TRP A 479     -53.381  -3.328 -38.972  1.00 48.78           C  
ANISOU 3562  CA  TRP A 479     7607   5205   5723    -33    573    854       C  
ATOM   3563  C   TRP A 479     -54.261  -3.928 -37.882  1.00 51.60           C  
ANISOU 3563  C   TRP A 479     7866   5573   6167      5    674    873       C  
ATOM   3564  O   TRP A 479     -53.957  -5.003 -37.352  1.00 48.06           O  
ANISOU 3564  O   TRP A 479     7473   5147   5639    -51    689    807       O  
ATOM   3565  CB  TRP A 479     -52.480  -2.238 -38.393  1.00 47.22           C  
ANISOU 3565  CB  TRP A 479     7526   4923   5493     16    671    775       C  
ATOM   3566  CG  TRP A 479     -51.507  -2.757 -37.365  1.00 51.00           C  
ANISOU 3566  CG  TRP A 479     8095   5394   5888    -13    705    652       C  
ATOM   3567  CD1 TRP A 479     -50.199  -3.091 -37.570  1.00 55.56           C  
ANISOU 3567  CD1 TRP A 479     8706   5991   6412    -82    651    580       C  
ATOM   3568  CD2 TRP A 479     -51.772  -3.014 -35.978  1.00 47.65           C  
ANISOU 3568  CD2 TRP A 479     7745   4927   5435     32    792    607       C  
ATOM   3569  NE1 TRP A 479     -49.633  -3.535 -36.397  1.00 52.46           N  
ANISOU 3569  NE1 TRP A 479     8375   5578   5978    -82    633    507       N  
ATOM   3570  CE2 TRP A 479     -50.578  -3.497 -35.406  1.00 48.28           C  
ANISOU 3570  CE2 TRP A 479     7920   5002   5423    -23    714    515       C  
ATOM   3571  CE3 TRP A 479     -52.901  -2.879 -35.165  1.00 47.81           C  
ANISOU 3571  CE3 TRP A 479     7767   4897   5503    118    949    649       C  
ATOM   3572  CZ2 TRP A 479     -50.482  -3.844 -34.061  1.00 47.04           C  
ANISOU 3572  CZ2 TRP A 479     7923   4784   5167    -11    731    463       C  
ATOM   3573  CZ3 TRP A 479     -52.804  -3.228 -33.832  1.00 49.73           C  
ANISOU 3573  CZ3 TRP A 479     8191   5071   5634    130   1044    583       C  
ATOM   3574  CH2 TRP A 479     -51.604  -3.705 -33.293  1.00 47.51           C  
ANISOU 3574  CH2 TRP A 479     8065   4779   5207     57    907    490       C  
ATOM   3575  N   LEU A 480     -55.358  -3.249 -37.536  1.00 51.34           N  
ANISOU 3575  N   LEU A 480     7691   5505   6310    111    774    975       N  
ATOM   3576  CA  LEU A 480     -56.253  -3.771 -36.507  1.00 52.86           C  
ANISOU 3576  CA  LEU A 480     7780   5691   6612    149    953   1011       C  
ATOM   3577  C   LEU A 480     -56.912  -5.070 -36.952  1.00 56.55           C  
ANISOU 3577  C   LEU A 480     8089   6251   7146      6    824   1086       C  
ATOM   3578  O   LEU A 480     -57.122  -5.977 -36.139  1.00 60.98           O  
ANISOU 3578  O   LEU A 480     8671   6809   7689    -44    942   1062       O  
ATOM   3579  CB  LEU A 480     -57.313  -2.729 -36.148  1.00 54.03           C  
ANISOU 3579  CB  LEU A 480     7770   5765   6993    325   1146   1127       C  
ATOM   3580  CG  LEU A 480     -56.846  -1.538 -35.311  1.00 55.65           C  
ANISOU 3580  CG  LEU A 480     8219   5813   7111    469   1361   1035       C  
ATOM   3581  CD1 LEU A 480     -57.997  -0.569 -35.051  1.00 60.64           C  
ANISOU 3581  CD1 LEU A 480     8694   6339   8005    685   1600   1165       C  
ATOM   3582  CD2 LEU A 480     -56.234  -2.013 -34.003  1.00 51.60           C  
ANISOU 3582  CD2 LEU A 480     7990   5237   6377    432   1513    888       C  
ATOM   3583  N   GLU A 481     -57.250  -5.178 -38.238  1.00 58.96           N  
ANISOU 3583  N   GLU A 481     8285   6612   7505    -84    568   1180       N  
ATOM   3584  CA  GLU A 481     -57.848  -6.412 -38.738  1.00 62.15           C  
ANISOU 3584  CA  GLU A 481     8598   7072   7943   -270    391   1243       C  
ATOM   3585  C   GLU A 481     -56.864  -7.573 -38.646  1.00 54.01           C  
ANISOU 3585  C   GLU A 481     7836   6027   6657   -378    378   1091       C  
ATOM   3586  O   GLU A 481     -57.184  -8.630 -38.083  1.00 51.87           O  
ANISOU 3586  O   GLU A 481     7564   5749   6395   -469    432   1087       O  
ATOM   3587  CB  GLU A 481     -58.326  -6.217 -40.177  1.00 72.40           C  
ANISOU 3587  CB  GLU A 481     9825   8398   9285   -365     61   1369       C  
ATOM   3588  CG  GLU A 481     -58.730  -7.509 -40.871  1.00 83.28           C  
ANISOU 3588  CG  GLU A 481    11237   9796  10610   -614   -194   1403       C  
ATOM   3589  CD  GLU A 481     -57.831  -7.847 -42.047  1.00 89.89           C  
ANISOU 3589  CD  GLU A 481    12443  10589  11122   -725   -381   1307       C  
ATOM   3590  OE1 GLU A 481     -57.400  -6.913 -42.758  1.00 88.39           O  
ANISOU 3590  OE1 GLU A 481    12369  10378  10839   -653   -438   1317       O  
ATOM   3591  OE2 GLU A 481     -57.553  -9.048 -42.257  1.00 93.77           O  
ANISOU 3591  OE2 GLU A 481    13143  11042  11443   -881   -435   1224       O  
ATOM   3592  N   ALA A 482     -55.655  -7.390 -39.186  1.00 49.00           N  
ANISOU 3592  N   ALA A 482     7425   5373   5819   -361    333    981       N  
ATOM   3593  CA  ALA A 482     -54.662  -8.459 -39.135  1.00 44.68           C  
ANISOU 3593  CA  ALA A 482     7098   4795   5083   -413    346    855       C  
ATOM   3594  C   ALA A 482     -54.334  -8.840 -37.697  1.00 45.78           C  
ANISOU 3594  C   ALA A 482     7279   4906   5209   -342    518    789       C  
ATOM   3595  O   ALA A 482     -54.258 -10.030 -37.362  1.00 51.37           O  
ANISOU 3595  O   ALA A 482     8091   5579   5849   -406    523    759       O  
ATOM   3596  CB  ALA A 482     -53.396  -8.035 -39.878  1.00 41.39           C  
ANISOU 3596  CB  ALA A 482     6843   4357   4526   -373    341    771       C  
ATOM   3597  N   ALA A 483     -54.155  -7.841 -36.829  1.00 48.64           N  
ANISOU 3597  N   ALA A 483     7620   5253   5606   -220    649    770       N  
ATOM   3598  CA  ALA A 483     -53.779  -8.110 -35.446  1.00 49.31           C  
ANISOU 3598  CA  ALA A 483     7839   5282   5613   -166    777    708       C  
ATOM   3599  C   ALA A 483     -54.901  -8.808 -34.688  1.00 51.97           C  
ANISOU 3599  C   ALA A 483     8136   5597   6014   -210    913    779       C  
ATOM   3600  O   ALA A 483     -54.642  -9.678 -33.848  1.00 51.74           O  
ANISOU 3600  O   ALA A 483     8281   5510   5869   -231    965    743       O  
ATOM   3601  CB  ALA A 483     -53.387  -6.806 -34.752  1.00 47.34           C  
ANISOU 3601  CB  ALA A 483     7657   4983   5347    -60    867    665       C  
ATOM   3602  N   GLU A 484     -56.155  -8.446 -34.973  1.00 57.21           N  
ANISOU 3602  N   GLU A 484     8558   6296   6885   -225    973    901       N  
ATOM   3603  CA  GLU A 484     -57.276  -9.080 -34.286  1.00 63.68           C  
ANISOU 3603  CA  GLU A 484     9269   7094   7832   -284   1149    995       C  
ATOM   3604  C   GLU A 484     -57.477 -10.517 -34.753  1.00 64.21           C  
ANISOU 3604  C   GLU A 484     9347   7171   7879   -481   1001   1019       C  
ATOM   3605  O   GLU A 484     -57.782 -11.400 -33.941  1.00 67.60           O  
ANISOU 3605  O   GLU A 484     9868   7540   8278   -552   1143   1036       O  
ATOM   3606  CB  GLU A 484     -58.552  -8.263 -34.488  1.00 74.30           C  
ANISOU 3606  CB  GLU A 484    10267   8473   9490   -229   1256   1149       C  
ATOM   3607  CG  GLU A 484     -58.700  -7.072 -33.542  1.00 87.45           C  
ANISOU 3607  CG  GLU A 484    11980  10054  11193    -22   1565   1139       C  
ATOM   3608  CD  GLU A 484     -59.140  -7.472 -32.138  1.00 99.52           C  
ANISOU 3608  CD  GLU A 484    13648  11483  12684      2   1935   1141       C  
ATOM   3609  OE1 GLU A 484     -59.162  -8.684 -31.829  1.00107.34           O  
ANISOU 3609  OE1 GLU A 484    14726  12469  13590   -145   1931   1140       O  
ATOM   3610  OE2 GLU A 484     -59.471  -6.569 -31.340  1.00104.26           O  
ANISOU 3610  OE2 GLU A 484    14319  11978  13317    169   2256   1144       O  
ATOM   3611  N   SER A 485     -57.317 -10.780 -36.053  1.00 60.70           N  
ANISOU 3611  N   SER A 485     8873   6770   7419   -582    730   1021       N  
ATOM   3612  CA  SER A 485     -57.436 -12.158 -36.524  1.00 56.94           C  
ANISOU 3612  CA  SER A 485     8506   6255   6875   -781    586   1021       C  
ATOM   3613  C   SER A 485     -56.305 -13.025 -35.979  1.00 54.79           C  
ANISOU 3613  C   SER A 485     8567   5890   6361   -736    637    891       C  
ATOM   3614  O   SER A 485     -56.541 -14.157 -35.525  1.00 53.72           O  
ANISOU 3614  O   SER A 485     8559   5671   6181   -845    679    903       O  
ATOM   3615  CB  SER A 485     -57.457 -12.194 -38.050  1.00 54.74           C  
ANISOU 3615  CB  SER A 485     8234   6000   6565   -899    291   1036       C  
ATOM   3616  OG  SER A 485     -56.211 -11.784 -38.578  1.00 57.78           O  
ANISOU 3616  OG  SER A 485     8824   6375   6756   -780    261    916       O  
ATOM   3617  N   MET A 486     -55.071 -12.510 -36.010  1.00 52.83           N  
ANISOU 3617  N   MET A 486     8447   5644   5983   -579    625    787       N  
ATOM   3618  CA  MET A 486     -53.962 -13.232 -35.394  1.00 52.68           C  
ANISOU 3618  CA  MET A 486     8676   5539   5800   -498    648    697       C  
ATOM   3619  C   MET A 486     -54.236 -13.491 -33.918  1.00 51.95           C  
ANISOU 3619  C   MET A 486     8685   5383   5669   -471    804    724       C  
ATOM   3620  O   MET A 486     -53.907 -14.563 -33.394  1.00 51.78           O  
ANISOU 3620  O   MET A 486     8883   5257   5533   -485    806    711       O  
ATOM   3621  CB  MET A 486     -52.659 -12.452 -35.567  1.00 49.84           C  
ANISOU 3621  CB  MET A 486     8336   5208   5395   -346    608    616       C  
ATOM   3622  CG  MET A 486     -51.410 -13.280 -35.308  1.00 50.70           C  
ANISOU 3622  CG  MET A 486     8620   5234   5409   -254    569    552       C  
ATOM   3623  SD  MET A 486     -49.921 -12.277 -35.162  1.00 52.25           S  
ANISOU 3623  SD  MET A 486     8740   5469   5642   -102    520    496       S  
ATOM   3624  CE  MET A 486     -50.195 -11.517 -33.562  1.00 47.21           C  
ANISOU 3624  CE  MET A 486     8168   4816   4954    -79    538    511       C  
ATOM   3625  N   GLY A 487     -54.853 -12.522 -33.237  1.00 47.65           N  
ANISOU 3625  N   GLY A 487     8032   4872   5201   -425    959    766       N  
ATOM   3626  CA  GLY A 487     -55.232 -12.732 -31.850  1.00 42.34           C  
ANISOU 3626  CA  GLY A 487     7525   4109   4452   -412   1170    795       C  
ATOM   3627  C   GLY A 487     -56.270 -13.825 -31.686  1.00 50.47           C  
ANISOU 3627  C   GLY A 487     8535   5088   5553   -579   1285    890       C  
ATOM   3628  O   GLY A 487     -56.244 -14.575 -30.708  1.00 54.27           O  
ANISOU 3628  O   GLY A 487     9279   5450   5891   -604   1404    902       O  
ATOM   3629  N   ARG A 488     -57.202 -13.929 -32.638  1.00 51.24           N  
ANISOU 3629  N   ARG A 488     8337   5260   5870   -718   1226    972       N  
ATOM   3630  CA  ARG A 488     -58.178 -15.015 -32.595  1.00 56.97           C  
ANISOU 3630  CA  ARG A 488     9011   5933   6702   -936   1285   1074       C  
ATOM   3631  C   ARG A 488     -57.501 -16.371 -32.742  1.00 57.67           C  
ANISOU 3631  C   ARG A 488     9427   5900   6587  -1023   1141   1011       C  
ATOM   3632  O   ARG A 488     -57.863 -17.332 -32.052  1.00 60.50           O  
ANISOU 3632  O   ARG A 488     9956   6136   6896  -1140   1269   1061       O  
ATOM   3633  CB  ARG A 488     -59.234 -14.834 -33.685  1.00 65.05           C  
ANISOU 3633  CB  ARG A 488     9643   7058   8016  -1097   1143   1187       C  
ATOM   3634  CG  ARG A 488     -60.476 -14.084 -33.241  1.00 76.75           C  
ANISOU 3634  CG  ARG A 488    10739   8600   9823  -1084   1389   1339       C  
ATOM   3635  CD  ARG A 488     -61.627 -14.327 -34.207  1.00 86.68           C  
ANISOU 3635  CD  ARG A 488    11592   9931  11413  -1315   1184   1500       C  
ATOM   3636  NE  ARG A 488     -61.245 -14.064 -35.592  1.00 90.43           N  
ANISOU 3636  NE  ARG A 488    12060  10470  11829  -1347    778   1460       N  
ATOM   3637  CZ  ARG A 488     -61.359 -12.881 -36.187  1.00 93.77           C  
ANISOU 3637  CZ  ARG A 488    12260  10989  12381  -1209    672   1503       C  
ATOM   3638  NH1 ARG A 488     -61.847 -11.846 -35.518  1.00 93.98           N  
ANISOU 3638  NH1 ARG A 488    12031  11051  12626  -1011    948   1582       N  
ATOM   3639  NH2 ARG A 488     -60.985 -12.732 -37.451  1.00 96.41           N  
ANISOU 3639  NH2 ARG A 488    12676  11352  12604  -1262    316   1470       N  
ATOM   3640  N   SER A 489     -56.521 -16.477 -33.643  1.00 55.56           N  
ANISOU 3640  N   SER A 489     9268   5637   6204   -960    911    910       N  
ATOM   3641  CA  SER A 489     -55.804 -17.742 -33.781  1.00 55.62           C  
ANISOU 3641  CA  SER A 489     9603   5494   6034   -984    818    849       C  
ATOM   3642  C   SER A 489     -55.029 -18.075 -32.510  1.00 52.39           C  
ANISOU 3642  C   SER A 489     9475   4977   5455   -828    916    826       C  
ATOM   3643  O   SER A 489     -55.059 -19.221 -32.029  1.00 46.59           O  
ANISOU 3643  O   SER A 489     9007   4078   4617   -896    952    854       O  
ATOM   3644  CB  SER A 489     -54.864 -17.687 -34.985  1.00 57.11           C  
ANISOU 3644  CB  SER A 489     9851   5695   6153   -904    636    749       C  
ATOM   3645  OG  SER A 489     -55.588 -17.459 -36.180  1.00 61.62           O  
ANISOU 3645  OG  SER A 489    10266   6332   6816  -1074    500    778       O  
ATOM   3646  N   VAL A 490     -54.337 -17.080 -31.948  1.00 50.78           N  
ANISOU 3646  N   VAL A 490     9248   4841   5207   -635    930    786       N  
ATOM   3647  CA  VAL A 490     -53.577 -17.297 -30.718  1.00 51.02           C  
ANISOU 3647  CA  VAL A 490     9571   4762   5055   -504    943    778       C  
ATOM   3648  C   VAL A 490     -54.496 -17.780 -29.601  1.00 55.67           C  
ANISOU 3648  C   VAL A 490    10351   5238   5563   -618   1169    867       C  
ATOM   3649  O   VAL A 490     -54.188 -18.749 -28.894  1.00 58.31           O  
ANISOU 3649  O   VAL A 490    11023   5404   5728   -614   1162    897       O  
ATOM   3650  CB  VAL A 490     -52.823 -16.017 -30.325  1.00 45.37           C  
ANISOU 3650  CB  VAL A 490     8798   4129   4310   -343    886    725       C  
ATOM   3651  CG1 VAL A 490     -52.356 -16.097 -28.891  1.00 44.70           C  
ANISOU 3651  CG1 VAL A 490     9053   3919   4011   -268    882    741       C  
ATOM   3652  CG2 VAL A 490     -51.638 -15.805 -31.253  1.00 43.54           C  
ANISOU 3652  CG2 VAL A 490     8439   3960   4144   -226    680    654       C  
ATOM   3653  N   ASP A 491     -55.648 -17.120 -29.435  1.00 56.53           N  
ANISOU 3653  N   ASP A 491    10248   5421   5810   -710   1399    926       N  
ATOM   3654  CA  ASP A 491     -56.611 -17.569 -28.434  1.00 63.11           C  
ANISOU 3654  CA  ASP A 491    11228   6142   6611   -831   1705   1026       C  
ATOM   3655  C   ASP A 491     -57.138 -18.962 -28.750  1.00 60.95           C  
ANISOU 3655  C   ASP A 491    11015   5760   6382  -1048   1700   1095       C  
ATOM   3656  O   ASP A 491     -57.475 -19.720 -27.834  1.00 58.12           O  
ANISOU 3656  O   ASP A 491    10946   5239   5900  -1138   1894   1168       O  
ATOM   3657  CB  ASP A 491     -57.769 -16.577 -28.328  1.00 70.35           C  
ANISOU 3657  CB  ASP A 491    11816   7157   7756   -860   1996   1095       C  
ATOM   3658  CG  ASP A 491     -57.326 -15.208 -27.847  1.00 76.96           C  
ANISOU 3658  CG  ASP A 491    12700   8035   8508   -655   2057   1024       C  
ATOM   3659  OD1 ASP A 491     -56.220 -15.107 -27.274  1.00 83.34           O  
ANISOU 3659  OD1 ASP A 491    13852   8769   9043   -536   1903    940       O  
ATOM   3660  OD2 ASP A 491     -58.085 -14.235 -28.036  1.00 78.59           O  
ANISOU 3660  OD2 ASP A 491    12600   8326   8933   -617   2241   1062       O  
ATOM   3661  N   GLY A 492     -57.213 -19.319 -30.033  1.00 59.50           N  
ANISOU 3661  N   GLY A 492    10625   5639   6345  -1154   1484   1074       N  
ATOM   3662  CA  GLY A 492     -57.659 -20.656 -30.389  1.00 61.28           C  
ANISOU 3662  CA  GLY A 492    10975   5724   6585  -1390   1441   1123       C  
ATOM   3663  C   GLY A 492     -56.678 -21.734 -29.968  1.00 62.87           C  
ANISOU 3663  C   GLY A 492    11656   5712   6521  -1299   1352   1081       C  
ATOM   3664  O   GLY A 492     -57.081 -22.821 -29.543  1.00 54.92           O  
ANISOU 3664  O   GLY A 492    10907   4515   5447  -1464   1447   1151       O  
ATOM   3665  N   VAL A 493     -55.379 -21.454 -30.078  1.00 60.31           N  
ANISOU 3665  N   VAL A 493    11440   5402   6072  -1035   1171    984       N  
ATOM   3666  CA  VAL A 493     -54.383 -22.449 -29.686  1.00 55.78           C  
ANISOU 3666  CA  VAL A 493    11269   4619   5304   -897   1062    971       C  
ATOM   3667  C   VAL A 493     -54.230 -22.507 -28.170  1.00 62.45           C  
ANISOU 3667  C   VAL A 493    12433   5349   5947   -820   1166   1043       C  
ATOM   3668  O   VAL A 493     -54.137 -23.594 -27.587  1.00 68.73           O  
ANISOU 3668  O   VAL A 493    13614   5914   6586   -846   1182   1107       O  
ATOM   3669  CB  VAL A 493     -53.039 -22.154 -30.374  1.00 53.94           C  
ANISOU 3669  CB  VAL A 493    10970   4440   5083   -639    843    871       C  
ATOM   3670  CG1 VAL A 493     -51.962 -23.096 -29.858  1.00 59.30           C  
ANISOU 3670  CG1 VAL A 493    12001   4905   5627   -438    726    890       C  
ATOM   3671  CG2 VAL A 493     -53.180 -22.269 -31.879  1.00 58.31           C  
ANISOU 3671  CG2 VAL A 493    11358   5042   5755   -729    776    800       C  
ATOM   3672  N   ILE A 494     -54.212 -21.345 -27.513  1.00 63.46           N  
ANISOU 3672  N   ILE A 494    12468   5602   6042   -731   1235   1035       N  
ATOM   3673  CA  ILE A 494     -53.879 -21.275 -26.095  1.00 58.12           C  
ANISOU 3673  CA  ILE A 494    12186   4796   5100   -642   1278   1083       C  
ATOM   3674  C   ILE A 494     -54.900 -22.032 -25.256  1.00 61.28           C  
ANISOU 3674  C   ILE A 494    12838   5042   5403   -831   1573   1173       C  
ATOM   3675  O   ILE A 494     -56.101 -22.045 -25.558  1.00 57.50           O  
ANISOU 3675  O   ILE A 494    12129   4610   5107  -1046   1843   1226       O  
ATOM   3676  CB  ILE A 494     -53.767 -19.800 -25.668  1.00 54.28           C  
ANISOU 3676  CB  ILE A 494    11579   4454   4590   -546   1315   1032       C  
ATOM   3677  CG1 ILE A 494     -52.368 -19.269 -25.978  1.00 56.16           C  
ANISOU 3677  CG1 ILE A 494    11728   4773   4838   -335    952    953       C  
ATOM   3678  CG2 ILE A 494     -54.110 -19.607 -24.198  1.00 59.09           C  
ANISOU 3678  CG2 ILE A 494    12622   4916   4915   -569   1534   1089       C  
ATOM   3679  CD1 ILE A 494     -51.267 -20.086 -25.352  1.00 59.60           C  
ANISOU 3679  CD1 ILE A 494    12521   5031   5094   -197    672   1000       C  
ATOM   3680  N   ASP A 495     -54.410 -22.693 -24.204  1.00 59.02           N  
ANISOU 3680  N   ASP A 495     9573   7129   5724   1003   -219    203       N  
ATOM   3681  CA  ASP A 495     -55.282 -23.327 -23.221  1.00 61.06           C  
ANISOU 3681  CA  ASP A 495    10075   7164   5960   1006   -172    224       C  
ATOM   3682  C   ASP A 495     -56.091 -22.263 -22.494  1.00 58.22           C  
ANISOU 3682  C   ASP A 495     9949   6689   5484    968    -34    356       C  
ATOM   3683  O   ASP A 495     -55.531 -21.415 -21.791  1.00 60.86           O  
ANISOU 3683  O   ASP A 495    10458   6918   5749    930    -97    420       O  
ATOM   3684  CB  ASP A 495     -54.450 -24.143 -22.231  1.00 68.66           C  
ANISOU 3684  CB  ASP A 495    11209   7923   6954   1024   -362    196       C  
ATOM   3685  CG  ASP A 495     -55.289 -25.111 -21.409  1.00 75.21           C  
ANISOU 3685  CG  ASP A 495    12257   8538   7781   1033   -305    211       C  
ATOM   3686  OD1 ASP A 495     -56.529 -24.954 -21.362  1.00 77.66           O  
ANISOU 3686  OD1 ASP A 495    12626   8829   8053   1007   -108    255       O  
ATOM   3687  OD2 ASP A 495     -54.702 -26.031 -20.802  1.00 81.26           O  
ANISOU 3687  OD2 ASP A 495    13131   9151   8594   1070   -455    188       O  
ATOM   3688  N   SER A 496     -57.413 -22.315 -22.656  1.00 58.20           N  
ANISOU 3688  N   SER A 496     9940   6702   5471    977    154    381       N  
ATOM   3689  CA  SER A 496     -58.254 -21.214 -22.201  1.00 57.90           C  
ANISOU 3689  CA  SER A 496    10060   6594   5347    964    319    497       C  
ATOM   3690  C   SER A 496     -58.389 -21.194 -20.684  1.00 57.18           C  
ANISOU 3690  C   SER A 496    10340   6223   5163    935    332    549       C  
ATOM   3691  O   SER A 496     -58.454 -20.117 -20.081  1.00 55.58           O  
ANISOU 3691  O   SER A 496    10328   5921   4868    916    390    623       O  
ATOM   3692  CB  SER A 496     -59.624 -21.300 -22.862  1.00 63.49           C  
ANISOU 3692  CB  SER A 496    10608   7424   6091    995    508    502       C  
ATOM   3693  OG  SER A 496     -59.509 -21.117 -24.264  1.00 71.07           O  
ANISOU 3693  OG  SER A 496    11253   8664   7084   1027    492    469       O  
ATOM   3694  N   LEU A 497     -58.443 -22.370 -20.050  1.00 59.87           N  
ANISOU 3694  N   LEU A 497    10803   6426   5520    934    287    512       N  
ATOM   3695  CA  LEU A 497     -58.543 -22.418 -18.594  1.00 51.60           C  
ANISOU 3695  CA  LEU A 497    10133   5125   4348    911    298    575       C  
ATOM   3696  C   LEU A 497     -57.345 -21.746 -17.937  1.00 52.14           C  
ANISOU 3696  C   LEU A 497    10377   5118   4316    889    100    590       C  
ATOM   3697  O   LEU A 497     -57.493 -21.028 -16.940  1.00 52.90           O  
ANISOU 3697  O   LEU A 497    10768   5066   4264    862    145    644       O  
ATOM   3698  CB  LEU A 497     -58.672 -23.868 -18.126  1.00 62.32           C  
ANISOU 3698  CB  LEU A 497    11581   6349   5749    916    265    553       C  
ATOM   3699  CG  LEU A 497     -58.643 -24.120 -16.615  1.00 60.88           C  
ANISOU 3699  CG  LEU A 497    11810   5910   5412    901    249    634       C  
ATOM   3700  CD1 LEU A 497     -59.682 -23.270 -15.894  1.00 57.90           C  
ANISOU 3700  CD1 LEU A 497    11657   5445   4897    873    495    710       C  
ATOM   3701  CD2 LEU A 497     -58.864 -25.594 -16.321  1.00 54.80           C  
ANISOU 3701  CD2 LEU A 497    11101   5005   4715    908    246    635       C  
ATOM   3702  N   GLU A 498     -56.148 -21.961 -18.488  1.00 52.01           N  
ANISOU 3702  N   GLU A 498    10173   5207   4381    898   -119    528       N  
ATOM   3703  CA  GLU A 498     -54.969 -21.283 -17.961  1.00 61.76           C  
ANISOU 3703  CA  GLU A 498    11516   6396   5555    863   -322    527       C  
ATOM   3704  C   GLU A 498     -55.067 -19.775 -18.156  1.00 57.55           C  
ANISOU 3704  C   GLU A 498    10986   5901   4979    811   -223    565       C  
ATOM   3705  O   GLU A 498     -54.665 -19.003 -17.277  1.00 58.53           O  
ANISOU 3705  O   GLU A 498    11350   5894   4994    760   -294    579       O  
ATOM   3706  CB  GLU A 498     -53.702 -21.831 -18.619  1.00 62.39           C  
ANISOU 3706  CB  GLU A 498    11334   6603   5770    886   -550    447       C  
ATOM   3707  CG  GLU A 498     -53.341 -23.246 -18.201  1.00 62.79           C  
ANISOU 3707  CG  GLU A 498    11433   6556   5866    950   -702    413       C  
ATOM   3708  CD  GLU A 498     -53.011 -23.365 -16.722  1.00 69.51           C  
ANISOU 3708  CD  GLU A 498    12657   7187   6565    947   -853    471       C  
ATOM   3709  OE1 GLU A 498     -52.766 -22.330 -16.068  1.00 76.25           O  
ANISOU 3709  OE1 GLU A 498    13695   7989   7287    887   -896    499       O  
ATOM   3710  OE2 GLU A 498     -52.996 -24.502 -16.208  1.00 69.66           O  
ANISOU 3710  OE2 GLU A 498    12799   7081   6590   1006   -932    489       O  
ATOM   3711  N   PHE A 499     -55.602 -19.335 -19.302  1.00 51.41           N  
ANISOU 3711  N   PHE A 499     9955   5295   4283    827    -65    582       N  
ATOM   3712  CA  PHE A 499     -55.811 -17.905 -19.511  1.00 56.77           C  
ANISOU 3712  CA  PHE A 499    10650   5983   4936    794     54    644       C  
ATOM   3713  C   PHE A 499     -56.766 -17.337 -18.469  1.00 55.86           C  
ANISOU 3713  C   PHE A 499    10861   5667   4697    793    222    695       C  
ATOM   3714  O   PHE A 499     -56.551 -16.234 -17.955  1.00 52.74           O  
ANISOU 3714  O   PHE A 499    10646   5154   4239    747    234    715       O  
ATOM   3715  CB  PHE A 499     -56.340 -17.642 -20.925  1.00 50.43           C  
ANISOU 3715  CB  PHE A 499     9532   5407   4223    836    196    678       C  
ATOM   3716  CG  PHE A 499     -56.421 -16.178 -21.286  1.00 50.64           C  
ANISOU 3716  CG  PHE A 499     9551   5444   4248    815    303    767       C  
ATOM   3717  CD1 PHE A 499     -57.536 -15.423 -20.949  1.00 50.86           C  
ANISOU 3717  CD1 PHE A 499     9731   5365   4230    851    509    843       C  
ATOM   3718  CD2 PHE A 499     -55.384 -15.561 -21.969  1.00 50.89           C  
ANISOU 3718  CD2 PHE A 499     9417   5579   4340    762    213    780       C  
ATOM   3719  CE1 PHE A 499     -57.610 -14.081 -21.275  1.00 56.99           C  
ANISOU 3719  CE1 PHE A 499    10512   6118   5024    846    610    934       C  
ATOM   3720  CE2 PHE A 499     -55.452 -14.215 -22.303  1.00 55.79           C  
ANISOU 3720  CE2 PHE A 499    10046   6179   4974    736    323    880       C  
ATOM   3721  CZ  PHE A 499     -56.567 -13.476 -21.957  1.00 51.59           C  
ANISOU 3721  CZ  PHE A 499     9682   5520   4400    785    515    959       C  
ATOM   3722  N   MET A 500     -57.822 -18.084 -18.137  1.00 57.26           N  
ANISOU 3722  N   MET A 500    11116   5794   4845    838    366    707       N  
ATOM   3723  CA  MET A 500     -58.783 -17.603 -17.151  1.00 60.73           C  
ANISOU 3723  CA  MET A 500    11853   6055   5168    844    562    751       C  
ATOM   3724  C   MET A 500     -58.188 -17.579 -15.750  1.00 61.96           C  
ANISOU 3724  C   MET A 500    12386   6005   5153    796    437    728       C  
ATOM   3725  O   MET A 500     -58.519 -16.691 -14.956  1.00 64.60           O  
ANISOU 3725  O   MET A 500    12987   6193   5366    780    548    738       O  
ATOM   3726  CB  MET A 500     -60.047 -18.462 -17.180  1.00 58.87           C  
ANISOU 3726  CB  MET A 500    11573   5830   4966    888    760    769       C  
ATOM   3727  CG  MET A 500     -60.791 -18.422 -18.506  1.00 60.05           C  
ANISOU 3727  CG  MET A 500    11360   6193   5261    938    881    781       C  
ATOM   3728  SD  MET A 500     -61.088 -16.737 -19.087  1.00 61.47           S  
ANISOU 3728  SD  MET A 500    11464   6430   5461    979   1009    859       S  
ATOM   3729  CE  MET A 500     -61.885 -17.051 -20.662  1.00 57.70           C  
ANISOU 3729  CE  MET A 500    10554   6247   5124   1050   1085    875       C  
ATOM   3730  N   LYS A 501     -57.312 -18.534 -15.425  1.00 58.82           N  
ANISOU 3730  N   LYS A 501    12021   5592   4736    783    203    693       N  
ATOM   3731  CA  LYS A 501     -56.657 -18.515 -14.120  1.00 58.74           C  
ANISOU 3731  CA  LYS A 501    12364   5413   4543    746     37    677       C  
ATOM   3732  C   LYS A 501     -55.685 -17.345 -14.014  1.00 57.71           C  
ANISOU 3732  C   LYS A 501    12270   5270   4389    677   -120    628       C  
ATOM   3733  O   LYS A 501     -55.750 -16.554 -13.065  1.00 63.87           O  
ANISOU 3733  O   LYS A 501    13361   5900   5006    636    -94    609       O  
ATOM   3734  CB  LYS A 501     -55.929 -19.838 -13.871  1.00 59.10           C  
ANISOU 3734  CB  LYS A 501    12409   5451   4597    771   -197    667       C  
ATOM   3735  CG  LYS A 501     -56.837 -21.004 -13.499  1.00 62.32           C  
ANISOU 3735  CG  LYS A 501    12928   5775   4977    814    -52    723       C  
ATOM   3736  CD  LYS A 501     -56.031 -22.281 -13.286  1.00 57.61           C  
ANISOU 3736  CD  LYS A 501    12333   5142   4412    853   -298    724       C  
ATOM   3737  CE  LYS A 501     -56.909 -23.415 -12.775  1.00 67.68           C  
ANISOU 3737  CE  LYS A 501    13775   6284   5655    878   -146    797       C  
ATOM   3738  NZ  LYS A 501     -56.158 -24.698 -12.677  1.00 69.17           N  
ANISOU 3738  NZ  LYS A 501    13950   6417   5915    932   -374    809       N  
ATOM   3739  N   VAL A 502     -54.773 -17.222 -14.983  1.00 58.83           N  
ANISOU 3739  N   VAL A 502    12094   5564   4696    655   -274    597       N  
ATOM   3740  CA  VAL A 502     -53.793 -16.140 -14.956  1.00 62.30           C  
ANISOU 3740  CA  VAL A 502    12526   5990   5154    565   -421    551       C  
ATOM   3741  C   VAL A 502     -54.492 -14.786 -14.945  1.00 64.75           C  
ANISOU 3741  C   VAL A 502    12951   6211   5439    535   -192    576       C  
ATOM   3742  O   VAL A 502     -54.141 -13.895 -14.158  1.00 58.52           O  
ANISOU 3742  O   VAL A 502    12406   5275   4554    460   -248    525       O  
ATOM   3743  CB  VAL A 502     -52.824 -16.277 -16.146  1.00 59.11           C  
ANISOU 3743  CB  VAL A 502    11719   5787   4955    549   -559    529       C  
ATOM   3744  CG1 VAL A 502     -51.863 -15.104 -16.190  1.00 57.09           C  
ANISOU 3744  CG1 VAL A 502    11427   5514   4752    433   -674    490       C  
ATOM   3745  CG2 VAL A 502     -52.057 -17.588 -16.054  1.00 61.23           C  
ANISOU 3745  CG2 VAL A 502    11891   6113   5262    595   -797    488       C  
ATOM   3746  N   SER A 503     -55.503 -14.618 -15.801  1.00 61.31           N  
ANISOU 3746  N   SER A 503    12344   5858   5092    600     63    647       N  
ATOM   3747  CA  SER A 503     -56.261 -13.371 -15.826  1.00 60.32           C  
ANISOU 3747  CA  SER A 503    12315   5637   4965    605    295    688       C  
ATOM   3748  C   SER A 503     -57.015 -13.140 -14.522  1.00 59.90           C  
ANISOU 3748  C   SER A 503    12663   5371   4724    620    431    662       C  
ATOM   3749  O   SER A 503     -57.157 -11.992 -14.089  1.00 62.67           O  
ANISOU 3749  O   SER A 503    13209   5569   5033    591    527    639       O  
ATOM   3750  CB  SER A 503     -57.237 -13.372 -17.003  1.00 58.30           C  
ANISOU 3750  CB  SER A 503    11778   5537   4835    697    514    779       C  
ATOM   3751  OG  SER A 503     -56.550 -13.459 -18.238  1.00 59.96           O  
ANISOU 3751  OG  SER A 503    11642   5954   5186    684    413    801       O  
ATOM   3752  N   GLU A 504     -57.500 -14.206 -13.884  1.00 58.37           N  
ANISOU 3752  N   GLU A 504    12605   5155   4417    663    457    665       N  
ATOM   3753  CA  GLU A 504     -58.183 -14.048 -12.605  1.00 61.99           C  
ANISOU 3753  CA  GLU A 504    13461   5424   4669    673    603    644       C  
ATOM   3754  C   GLU A 504     -57.223 -13.545 -11.535  1.00 66.38           C  
ANISOU 3754  C   GLU A 504    14337   5837   5046    584    388    550       C  
ATOM   3755  O   GLU A 504     -57.563 -12.648 -10.754  1.00 68.64           O  
ANISOU 3755  O   GLU A 504    14921   5960   5200    567    513    497       O  
ATOM   3756  CB  GLU A 504     -58.817 -15.375 -12.183  1.00 68.39           C  
ANISOU 3756  CB  GLU A 504    14342   6242   5401    722    673    686       C  
ATOM   3757  CG  GLU A 504     -59.748 -15.288 -10.978  1.00 77.99           C  
ANISOU 3757  CG  GLU A 504    15937   7288   6406    743    905    690       C  
ATOM   3758  CD  GLU A 504     -60.261 -16.650 -10.538  1.00 86.04           C  
ANISOU 3758  CD  GLU A 504    17035   8299   7357    768    968    750       C  
ATOM   3759  OE1 GLU A 504     -59.743 -17.671 -11.039  1.00 87.23           O  
ANISOU 3759  OE1 GLU A 504    16989   8546   7609    767    782    772       O  
ATOM   3760  OE2 GLU A 504     -61.180 -16.703  -9.691  1.00 91.56           O  
ANISOU 3760  OE2 GLU A 504    17995   8887   7909    787   1217    774       O  
ATOM   3761  N   ALA A 505     -56.009 -14.100 -11.496  1.00 67.00           N  
ANISOU 3761  N   ALA A 505    14351   5979   5126    532     58    514       N  
ATOM   3762  CA  ALA A 505     -55.031 -13.674 -10.498  1.00 67.18           C  
ANISOU 3762  CA  ALA A 505    14647   5893   4984    442   -195    413       C  
ATOM   3763  C   ALA A 505     -54.573 -12.242 -10.752  1.00 66.05           C  
ANISOU 3763  C   ALA A 505    14474   5687   4934    348   -206    339       C  
ATOM   3764  O   ALA A 505     -54.561 -11.410  -9.835  1.00 68.56           O  
ANISOU 3764  O   ALA A 505    15119   5836   5093    290   -197    245       O  
ATOM   3765  CB  ALA A 505     -53.839 -14.630 -10.492  1.00 63.44           C  
ANISOU 3765  CB  ALA A 505    14051   5521   4533    426   -557    399       C  
ATOM   3766  N   ARG A 506     -54.192 -11.935 -11.996  1.00 62.83           N  
ANISOU 3766  N   ARG A 506    13687   5405   4780    327   -217    379       N  
ATOM   3767  CA  ARG A 506     -53.737 -10.587 -12.322  1.00 66.01           C  
ANISOU 3767  CA  ARG A 506    14046   5732   5303    227   -210    335       C  
ATOM   3768  C   ARG A 506     -54.833  -9.558 -12.069  1.00 65.49           C  
ANISOU 3768  C   ARG A 506    14195   5490   5197    266    107    342       C  
ATOM   3769  O   ARG A 506     -54.565  -8.473 -11.539  1.00 65.89           O  
ANISOU 3769  O   ARG A 506    14459   5359   5216    177    101    247       O  
ATOM   3770  CB  ARG A 506     -53.265 -10.530 -13.776  1.00 67.65           C  
ANISOU 3770  CB  ARG A 506    13808   6123   5773    213   -227    412       C  
ATOM   3771  CG  ARG A 506     -51.954 -11.263 -14.022  1.00 75.64           C  
ANISOU 3771  CG  ARG A 506    14592   7286   6862    154   -548    370       C  
ATOM   3772  CD  ARG A 506     -51.726 -11.555 -15.499  1.00 79.42           C  
ANISOU 3772  CD  ARG A 506    14629   7988   7558    184   -507    455       C  
ATOM   3773  NE  ARG A 506     -50.632 -10.773 -16.067  1.00 82.05           N  
ANISOU 3773  NE  ARG A 506    14754   8360   8062     51   -618    432       N  
ATOM   3774  CZ  ARG A 506     -50.784  -9.843 -17.006  1.00 84.64           C  
ANISOU 3774  CZ  ARG A 506    14920   8706   8532     18   -435    517       C  
ATOM   3775  NH1 ARG A 506     -51.990  -9.579 -17.494  1.00 81.80           N  
ANISOU 3775  NH1 ARG A 506    14574   8343   8162    127   -155    627       N  
ATOM   3776  NH2 ARG A 506     -49.729  -9.183 -17.463  1.00 88.32           N  
ANISOU 3776  NH2 ARG A 506    15204   9197   9158   -122   -532    501       N  
ATOM   3777  N   ILE A 507     -56.075  -9.887 -12.429  1.00 62.66           N  
ANISOU 3777  N   ILE A 507    13777   5176   4855    399    386    443       N  
ATOM   3778  CA  ILE A 507     -57.187  -8.978 -12.169  1.00 63.48           C  
ANISOU 3778  CA  ILE A 507    14065   5118   4937    466    701    453       C  
ATOM   3779  C   ILE A 507     -57.406  -8.817 -10.669  1.00 70.74           C  
ANISOU 3779  C   ILE A 507    15447   5840   5588    446    732    331       C  
ATOM   3780  O   ILE A 507     -57.742  -7.727 -10.196  1.00 72.49           O  
ANISOU 3780  O   ILE A 507    15903   5866   5776    439    887    258       O  
ATOM   3781  CB  ILE A 507     -58.458  -9.467 -12.888  1.00 70.74           C  
ANISOU 3781  CB  ILE A 507    14775   6159   5945    615    969    582       C  
ATOM   3782  CG1 ILE A 507     -58.361  -9.180 -14.388  1.00 66.37           C  
ANISOU 3782  CG1 ILE A 507    13815   5768   5633    642    985    695       C  
ATOM   3783  CG2 ILE A 507     -59.700  -8.803 -12.314  1.00 73.80           C  
ANISOU 3783  CG2 ILE A 507    15390   6378   6271    709   1297    577       C  
ATOM   3784  CD1 ILE A 507     -59.504  -9.752 -15.193  1.00 58.79           C  
ANISOU 3784  CD1 ILE A 507    12604   4973   4760    779   1184    807       C  
ATOM   3785  N   GLN A 508     -57.206  -9.889  -9.895  1.00 74.73           N  
ANISOU 3785  N   GLN A 508    16111   6390   5894    443    589    306       N  
ATOM   3786  CA  GLN A 508     -57.319  -9.778  -8.442  1.00 73.40           C  
ANISOU 3786  CA  GLN A 508    16409   6058   5422    419    594    195       C  
ATOM   3787  C   GLN A 508     -56.281  -8.813  -7.883  1.00 70.71           C  
ANISOU 3787  C   GLN A 508    16266   5586   5016    280    365     34       C  
ATOM   3788  O   GLN A 508     -56.603  -7.940  -7.068  1.00 72.95           O  
ANISOU 3788  O   GLN A 508    16886   5678   5153    260    493    -85       O  
ATOM   3789  CB  GLN A 508     -57.174 -11.152  -7.788  1.00 77.77           C  
ANISOU 3789  CB  GLN A 508    17084   6691   5774    440    448    231       C  
ATOM   3790  CG  GLN A 508     -58.437 -11.993  -7.792  1.00 79.93           C  
ANISOU 3790  CG  GLN A 508    17346   7003   6020    555    745    346       C  
ATOM   3791  CD  GLN A 508     -58.249 -13.315  -7.076  1.00 83.42           C  
ANISOU 3791  CD  GLN A 508    17953   7481   6262    565    605    395       C  
ATOM   3792  OE1 GLN A 508     -57.338 -13.468  -6.262  1.00 87.74           O  
ANISOU 3792  OE1 GLN A 508    18738   7992   6606    507    319    331       O  
ATOM   3793  NE2 GLN A 508     -59.108 -14.282  -7.380  1.00 81.90           N  
ANISOU 3793  NE2 GLN A 508    17630   7354   6135    638    797    511       N  
ATOM   3794  N   ALA A 509     -55.025  -8.954  -8.314  1.00 70.36           N  
ANISOU 3794  N   ALA A 509    16005   5641   5088    179     29     13       N  
ATOM   3795  CA  ALA A 509     -53.972  -8.072  -7.816  1.00 72.69           C  
ANISOU 3795  CA  ALA A 509    16444   5823   5352     22   -216   -152       C  
ATOM   3796  C   ALA A 509     -54.211  -6.624  -8.232  1.00 75.98           C  
ANISOU 3796  C   ALA A 509    16851   6069   5950    -28    -15   -197       C  
ATOM   3797  O   ALA A 509     -54.042  -5.702  -7.424  1.00 81.11           O  
ANISOU 3797  O   ALA A 509    17813   6517   6489   -116    -30   -364       O  
ATOM   3798  CB  ALA A 509     -52.608  -8.552  -8.310  1.00 72.22           C  
ANISOU 3798  CB  ALA A 509    16083   5925   5433    -71   -593   -153       C  
ATOM   3799  N   ASP A 510     -54.608  -6.403  -9.488  1.00 72.49           N  
ANISOU 3799  N   ASP A 510    16065   5697   5782     32    173    -50       N  
ATOM   3800  CA  ASP A 510     -54.797  -5.037  -9.969  1.00 78.25           C  
ANISOU 3800  CA  ASP A 510    16771   6254   6707     -2    358    -56       C  
ATOM   3801  C   ASP A 510     -56.020  -4.384  -9.336  1.00 75.93           C  
ANISOU 3801  C   ASP A 510    16795   5751   6305    106    695    -97       C  
ATOM   3802  O   ASP A 510     -56.010  -3.181  -9.054  1.00 75.54           O  
ANISOU 3802  O   ASP A 510    16936   5461   6305     48    786   -203       O  
ATOM   3803  CB  ASP A 510     -54.902  -5.025 -11.493  1.00 78.17           C  
ANISOU 3803  CB  ASP A 510    16320   6397   6984     50    458    137       C  
ATOM   3804  CG  ASP A 510     -53.574  -5.314 -12.170  1.00 84.13           C  
ANISOU 3804  CG  ASP A 510    16763   7315   7887    -82    162    150       C  
ATOM   3805  OD1 ASP A 510     -52.526  -5.140 -11.513  1.00 87.40           O  
ANISOU 3805  OD1 ASP A 510    17292   7668   8250   -239   -109      0       O  
ATOM   3806  OD2 ASP A 510     -53.578  -5.707 -13.356  1.00 85.61           O  
ANISOU 3806  OD2 ASP A 510    16585   7701   8241    -29    201    301       O  
ATOM   3807  N   VAL A 511     -57.083  -5.157  -9.107  1.00 75.44           N  
ANISOU 3807  N   VAL A 511    16787   5765   6112    261    897    -23       N  
ATOM   3808  CA  VAL A 511     -58.258  -4.617  -8.428  1.00 78.50           C  
ANISOU 3808  CA  VAL A 511    17468   5969   6388    372   1234    -73       C  
ATOM   3809  C   VAL A 511     -57.937  -4.312  -6.970  1.00 85.32           C  
ANISOU 3809  C   VAL A 511    18812   6656   6950    284   1148   -295       C  
ATOM   3810  O   VAL A 511     -58.387  -3.299  -6.422  1.00 92.26           O  
ANISOU 3810  O   VAL A 511    19968   7301   7788    300   1350   -420       O  
ATOM   3811  CB  VAL A 511     -59.448  -5.585  -8.561  1.00 79.07           C  
ANISOU 3811  CB  VAL A 511    17442   6185   6415    540   1473     63       C  
ATOM   3812  CG1 VAL A 511     -60.541  -5.230  -7.560  1.00 80.94           C  
ANISOU 3812  CG1 VAL A 511    18033   6249   6471    638   1798    -21       C  
ATOM   3813  CG2 VAL A 511     -59.998  -5.549  -9.977  1.00 76.41           C  
ANISOU 3813  CG2 VAL A 511    16674   5981   6376    645   1618    251       C  
ATOM   3814  N   LYS A 512     -57.151  -5.175  -6.319  1.00 85.35           N  
ANISOU 3814  N   LYS A 512    18928   6769   6730    200    842   -352       N  
ATOM   3815  CA  LYS A 512     -56.702  -4.880  -4.962  1.00 89.18           C  
ANISOU 3815  CA  LYS A 512    19867   7116   6900    104    696   -569       C  
ATOM   3816  C   LYS A 512     -55.907  -3.580  -4.922  1.00 92.20           C  
ANISOU 3816  C   LYS A 512    20326   7305   7402    -53    564   -747       C  
ATOM   3817  O   LYS A 512     -56.144  -2.717  -4.068  1.00 94.03           O  
ANISOU 3817  O   LYS A 512    20931   7313   7484    -82    678   -938       O  
ATOM   3818  CB  LYS A 512     -55.868  -6.041  -4.414  1.00 86.95           C  
ANISOU 3818  CB  LYS A 512    19639   7006   6392     48    332   -569       C  
ATOM   3819  CG  LYS A 512     -54.743  -5.609  -3.480  1.00 91.42           C  
ANISOU 3819  CG  LYS A 512    20484   7493   6758   -118    -23   -790       C  
ATOM   3820  CD  LYS A 512     -54.355  -6.702  -2.498  1.00 94.46           C  
ANISOU 3820  CD  LYS A 512    21108   7999   6783   -110   -283   -797       C  
ATOM   3821  CE  LYS A 512     -55.389  -6.837  -1.390  1.00 97.35           C  
ANISOU 3821  CE  LYS A 512    21882   8286   6822    -12     -3   -815       C  
ATOM   3822  NZ  LYS A 512     -54.935  -7.752  -0.305  1.00100.29           N  
ANISOU 3822  NZ  LYS A 512    22378   8769   6958    -17   -267   -771       N  
ATOM   3823  N   GLU A 513     -54.965  -3.417  -5.854  1.00 92.20           N  
ANISOU 3823  N   GLU A 513    19972   7378   7680   -163    342   -693       N  
ATOM   3824  CA  GLU A 513     -54.165  -2.197  -5.884  1.00 94.69           C  
ANISOU 3824  CA  GLU A 513    20326   7500   8152   -340    221   -850       C  
ATOM   3825  C   GLU A 513     -55.033  -0.977  -6.167  1.00 97.61           C  
ANISOU 3825  C   GLU A 513    20779   7612   8697   -274    596   -856       C  
ATOM   3826  O   GLU A 513     -54.799   0.102  -5.612  1.00 98.58           O  
ANISOU 3826  O   GLU A 513    21167   7473   8815   -383    603  -1059       O  
ATOM   3827  CB  GLU A 513     -53.053  -2.328  -6.925  1.00 95.25           C  
ANISOU 3827  CB  GLU A 513    19959   7720   8510   -464    -41   -758       C  
ATOM   3828  CG  GLU A 513     -52.061  -1.175  -6.935  1.00101.25           C  
ANISOU 3828  CG  GLU A 513    20726   8294   9448   -689   -207   -920       C  
ATOM   3829  CD  GLU A 513     -51.452  -0.914  -5.571  1.00105.51           C  
ANISOU 3829  CD  GLU A 513    21661   8715   9715   -833   -465  -1208       C  
ATOM   3830  OE1 GLU A 513     -51.474   0.254  -5.126  1.00110.77           O  
ANISOU 3830  OE1 GLU A 513    22582   9099  10405   -934   -382  -1396       O  
ATOM   3831  OE2 GLU A 513     -50.959  -1.876  -4.943  1.00101.71           O  
ANISOU 3831  OE2 GLU A 513    21241   8415   8989   -840   -755  -1248       O  
ATOM   3832  N   ALA A 514     -56.053  -1.133  -7.016  1.00 97.18           N  
ANISOU 3832  N   ALA A 514    20501   7621   8802    -90    904   -641       N  
ATOM   3833  CA  ALA A 514     -56.933  -0.013  -7.332  1.00 95.29           C  
ANISOU 3833  CA  ALA A 514    20314   7143   8747     11   1260   -617       C  
ATOM   3834  C   ALA A 514     -57.788   0.376  -6.132  1.00 97.79           C  
ANISOU 3834  C   ALA A 514    21085   7253   8816     98   1502   -798       C  
ATOM   3835  O   ALA A 514     -58.042   1.565  -5.905  1.00102.10           O  
ANISOU 3835  O   ALA A 514    21835   7503   9454     97   1682   -921       O  
ATOM   3836  CB  ALA A 514     -57.814  -0.355  -8.533  1.00 88.94           C  
ANISOU 3836  CB  ALA A 514    19137   6498   8157    200   1493   -340       C  
ATOM   3837  N   LYS A 515     -58.251  -0.609  -5.358  1.00 95.43           N  
ANISOU 3837  N   LYS A 515    20958   7096   8206    177   1529   -814       N  
ATOM   3838  CA  LYS A 515     -58.973  -0.298  -4.128  1.00 96.92           C  
ANISOU 3838  CA  LYS A 515    21606   7111   8109    243   1755  -1000       C  
ATOM   3839  C   LYS A 515     -58.058   0.384  -3.119  1.00 99.23           C  
ANISOU 3839  C   LYS A 515    22261   7229   8212     50   1517  -1290       C  
ATOM   3840  O   LYS A 515     -58.483   1.301  -2.404  1.00103.02           O  
ANISOU 3840  O   LYS A 515    22928   7557   8658     62   1698  -1413       O  
ATOM   3841  CB  LYS A 515     -59.580  -1.569  -3.533  1.00100.19           C  
ANISOU 3841  CB  LYS A 515    22117   7729   8221    345   1825   -929       C  
ATOM   3842  CG  LYS A 515     -60.703  -2.175  -4.362  1.00 98.96           C  
ANISOU 3842  CG  LYS A 515    21634   7724   8242    538   2116   -681       C  
ATOM   3843  CD  LYS A 515     -61.365  -3.342  -3.638  1.00 98.60           C  
ANISOU 3843  CD  LYS A 515    21735   7827   7901    618   2233   -632       C  
ATOM   3844  CE  LYS A 515     -60.400  -4.503  -3.438  1.00 97.01           C  
ANISOU 3844  CE  LYS A 515    21509   7830   7520    504   1842   -589       C  
ATOM   3845  NZ  LYS A 515     -61.064  -5.680  -2.808  1.00 95.04           N  
ANISOU 3845  NZ  LYS A 515    21360   7713   7038    578   1962   -491       N  
ATOM   3846  N   ARG A 516     -56.797  -0.050  -3.051  1.00 97.10           N  
ANISOU 3846  N   ARG A 516    21939   7079   7874   -132   1083  -1344       N  
ATOM   3847  CA  ARG A 516     -55.829   0.603  -2.174  1.00100.38           C  
ANISOU 3847  CA  ARG A 516    22587   7389   8165   -335    799  -1597       C  
ATOM   3848  C   ARG A 516     -55.625   2.060  -2.572  1.00100.01           C  
ANISOU 3848  C   ARG A 516    22509   7057   8435   -432    889  -1705       C  
ATOM   3849  O   ARG A 516     -55.606   2.954  -1.718  1.00105.92           O  
ANISOU 3849  O   ARG A 516    23468   7662   9113   -500    921  -1899       O  
ATOM   3850  CB  ARG A 516     -54.503  -0.155  -2.207  1.00 98.68           C  
ANISOU 3850  CB  ARG A 516    22276   7349   7869   -501    307  -1630       C  
ATOM   3851  CG  ARG A 516     -53.361   0.568  -1.518  1.00102.47           C  
ANISOU 3851  CG  ARG A 516    22875   7747   8312   -735    -35  -1878       C  
ATOM   3852  CD  ARG A 516     -52.020  -0.051  -1.871  1.00 97.56           C  
ANISOU 3852  CD  ARG A 516    22032   7294   7743   -896   -509  -1881       C  
ATOM   3853  NE  ARG A 516     -50.911   0.731  -1.336  1.00108.45           N  
ANISOU 3853  NE  ARG A 516    23486   8575   9146  -1140   -836  -2135       N  
ATOM   3854  CZ  ARG A 516     -50.354   1.761  -1.964  1.00108.80           C  
ANISOU 3854  CZ  ARG A 516    23400   8405   9533  -1320   -862  -2231       C  
ATOM   3855  NH1 ARG A 516     -50.802   2.134  -3.155  1.00104.12           N  
ANISOU 3855  NH1 ARG A 516    22497   7749   9315  -1251   -569  -2015       N  
ATOM   3856  NH2 ARG A 516     -49.349   2.419  -1.401  1.00111.89           N  
ANISOU 3856  NH2 ARG A 516    23821   8738   9953  -1549  -1165  -2465       N  
ATOM   3857  N   ILE A 517     -55.469   2.318  -3.873  1.00 98.45           N  
ANISOU 3857  N   ILE A 517    21991   6804   8610   -439    933  -1547       N  
ATOM   3858  CA  ILE A 517     -55.293   3.686  -4.350  1.00102.44           C  
ANISOU 3858  CA  ILE A 517    22474   7002   9448   -527   1042  -1609       C  
ATOM   3859  C   ILE A 517     -56.571   4.494  -4.153  1.00105.56           C  
ANISOU 3859  C   ILE A 517    22973   7232   9903   -331   1483  -1590       C  
ATOM   3860  O   ILE A 517     -56.524   5.720  -3.995  1.00107.53           O  
ANISOU 3860  O   ILE A 517    23295   7238  10323   -395   1577  -1710       O  
ATOM   3861  CB  ILE A 517     -54.840   3.670  -5.824  1.00103.11           C  
ANISOU 3861  CB  ILE A 517    22049   7205   9924   -563    984  -1339       C  
ATOM   3862  CG1 ILE A 517     -53.506   2.934  -5.959  1.00105.26           C  
ANISOU 3862  CG1 ILE A 517    22092   7727  10176   -760    538  -1344       C  
ATOM   3863  CG2 ILE A 517     -54.708   5.080  -6.379  1.00104.86           C  
ANISOU 3863  CG2 ILE A 517    22247   7091  10502   -646   1128  -1354       C  
ATOM   3864  CD1 ILE A 517     -53.048   2.748  -7.389  1.00102.71           C  
ANISOU 3864  CD1 ILE A 517    21263   7572  10190   -787    490  -1080       C  
ATOM   3865  N   ALA A 518     -57.727   3.829  -4.136  1.00103.91           N  
ANISOU 3865  N   ALA A 518    22752   7157   9571    -93   1757  -1445       N  
ATOM   3866  CA  ALA A 518     -58.990   4.541  -3.976  1.00103.66           C  
ANISOU 3866  CA  ALA A 518    22769   7002   9617    108   2177  -1415       C  
ATOM   3867  C   ALA A 518     -59.232   4.947  -2.527  1.00109.11           C  
ANISOU 3867  C   ALA A 518    23795   7635  10025     84   2236  -1652       C  
ATOM   3868  O   ALA A 518     -59.706   6.058  -2.266  1.00111.44           O  
ANISOU 3868  O   ALA A 518    24180   7715  10446    131   2461  -1749       O  
ATOM   3869  CB  ALA A 518     -60.145   3.681  -4.487  1.00102.41           C  
ANISOU 3869  CB  ALA A 518    22441   7015   9456    358   2447  -1182       C  
ATOM   3870  N   LEU A 519     -58.919   4.068  -1.574  1.00116.21           N  
ANISOU 3870  N   LEU A 519    24881   8725  10550     18   2036  -1737       N  
ATOM   3871  CA  LEU A 519     -59.147   4.395  -0.169  1.00127.19           C  
ANISOU 3871  CA  LEU A 519    26593  10080  11652     -1   2087  -1941       C  
ATOM   3872  C   LEU A 519     -58.121   5.405   0.334  1.00142.51           C  
ANISOU 3872  C   LEU A 519    28683  11842  13622   -224   1836  -2212       C  
ATOM   3873  O   LEU A 519     -58.476   6.512   0.759  1.00144.69           O  
ANISOU 3873  O   LEU A 519    29097  11900  13978   -212   2028  -2370       O  
ATOM   3874  CB  LEU A 519     -59.123   3.123   0.678  1.00119.23           C  
ANISOU 3874  CB  LEU A 519    25721   9333  10247      5   1945  -1905       C  
ATOM   3875  CG  LEU A 519     -60.328   2.198   0.490  1.00103.56           C  
ANISOU 3875  CG  LEU A 519    23642   7499   8208    221   2258  -1675       C  
ATOM   3876  CD1 LEU A 519     -60.302   1.069   1.507  1.00104.18           C  
ANISOU 3876  CD1 LEU A 519    23892   7785   7905    209   2134  -1647       C  
ATOM   3877  CD2 LEU A 519     -61.629   2.983   0.586  1.00105.26           C  
ANISOU 3877  CD2 LEU A 519    23878   7564   8551    400   2728  -1671       C  
ATOM   3878  N   ALA A 520     -56.842   5.039   0.304  1.00151.70           N  
ANISOU 3878  N   ALA A 520    29809  13095  14735   -432   1401  -2280       N  
ATOM   3879  CA  ALA A 520     -55.775   5.974   0.632  1.00160.67           C  
ANISOU 3879  CA  ALA A 520    31022  14068  15958   -670   1133  -2535       C  
ATOM   3880  C   ALA A 520     -55.534   6.885  -0.564  1.00162.27           C  
ANISOU 3880  C   ALA A 520    30990  14034  16630   -731   1210  -2477       C  
ATOM   3881  O   ALA A 520     -55.240   6.410  -1.664  1.00161.82           O  
ANISOU 3881  O   ALA A 520    30670  14042  16772   -739   1137  -2277       O  
ATOM   3882  CB  ALA A 520     -54.500   5.225   1.011  1.00160.89           C  
ANISOU 3882  CB  ALA A 520    31049  14296  15787   -865    631  -2619       C  
ATOM   3883  N   GLU A 521     -55.655   8.193  -0.351  1.00167.72           N  
ANISOU 3883  N   GLU A 521    31776  14442  17506   -774   1362  -2642       N  
ATOM   3884  CA  GLU A 521     -55.673   9.140  -1.461  1.00165.42           C  
ANISOU 3884  CA  GLU A 521    31277  13897  17679   -784   1523  -2538       C  
ATOM   3885  C   GLU A 521     -54.302   9.305  -2.101  1.00158.87           C  
ANISOU 3885  C   GLU A 521    30263  13013  17087  -1061   1176  -2564       C  
ATOM   3886  O   GLU A 521     -53.523  10.183  -1.716  1.00161.07           O  
ANISOU 3886  O   GLU A 521    30616  13105  17479  -1281   1011  -2801       O  
ATOM   3887  CB  GLU A 521     -56.215  10.492  -1.000  1.00171.84           C  
ANISOU 3887  CB  GLU A 521    32253  14407  18632   -741   1788  -2709       C  
ATOM   3888  CG  GLU A 521     -57.684  10.444  -0.628  1.00175.24           C  
ANISOU 3888  CG  GLU A 521    32792  14860  18932   -446   2196  -2637       C  
ATOM   3889  CD  GLU A 521     -58.495   9.602  -1.598  1.00175.51           C  
ANISOU 3889  CD  GLU A 521    32582  15069  19036   -221   2396  -2294       C  
ATOM   3890  OE1 GLU A 521     -58.457   9.880  -2.815  1.00175.56           O  
ANISOU 3890  OE1 GLU A 521    32321  14989  19393   -190   2456  -2086       O  
ATOM   3891  OE2 GLU A 521     -59.162   8.651  -1.139  1.00175.99           O  
ANISOU 3891  OE2 GLU A 521    32710  15357  18802    -80   2489  -2227       O  
ATOM   3892  N   GLU A 522     -54.004   8.459  -3.083  1.00147.52           N  
ANISOU 3892  N   GLU A 522    28575  11738  15739  -1057   1069  -2328       N  
ATOM   3893  CA  GLU A 522     -52.870   8.644  -3.969  1.00140.09           C  
ANISOU 3893  CA  GLU A 522    27395  10729  15102  -1291    829  -2280       C  
ATOM   3894  C   GLU A 522     -53.360   9.311  -5.253  1.00135.56           C  
ANISOU 3894  C   GLU A 522    26596   9965  14945  -1189   1138  -2011       C  
ATOM   3895  O   GLU A 522     -54.514   9.743  -5.352  1.00134.61           O  
ANISOU 3895  O   GLU A 522    26511   9751  14881   -948   1500  -1908       O  
ATOM   3896  CB  GLU A 522     -52.176   7.307  -4.233  1.00134.55           C  
ANISOU 3896  CB  GLU A 522    26556  10326  14241  -1357    504  -2194       C  
ATOM   3897  CG  GLU A 522     -51.406   6.761  -3.039  1.00136.03           C  
ANISOU 3897  CG  GLU A 522    26916  10699  14071  -1499    114  -2446       C  
ATOM   3898  CD  GLU A 522     -50.728   5.436  -3.334  1.00133.03           C  
ANISOU 3898  CD  GLU A 522    26376  10612  13557  -1540   -216  -2348       C  
ATOM   3899  OE1 GLU A 522     -51.195   4.719  -4.244  1.00128.80           O  
ANISOU 3899  OE1 GLU A 522    25586  10244  13110  -1373    -74  -2057       O  
ATOM   3900  OE2 GLU A 522     -49.727   5.115  -2.659  1.00134.98           O  
ANISOU 3900  OE2 GLU A 522    26651  10998  13638  -1716   -623  -2529       O  
ATOM   3901  N   ASP A 523     -52.486   9.396  -6.253  1.00131.43           N  
ANISOU 3901  N   ASP A 523    25823   9398  14716  -1369    994  -1881       N  
ATOM   3902  CA  ASP A 523     -52.827  10.108  -7.477  1.00127.68           C  
ANISOU 3902  CA  ASP A 523    25127   8747  14639  -1295   1265  -1602       C  
ATOM   3903  C   ASP A 523     -53.965   9.405  -8.210  1.00120.12           C  
ANISOU 3903  C   ASP A 523    24029   7970  13642   -968   1529  -1286       C  
ATOM   3904  O   ASP A 523     -53.939   8.186  -8.401  1.00114.22           O  
ANISOU 3904  O   ASP A 523    23150   7542  12708   -906   1400  -1176       O  
ATOM   3905  CB  ASP A 523     -51.600  10.221  -8.382  1.00124.98           C  
ANISOU 3905  CB  ASP A 523    24539   8358  14589  -1575   1056  -1506       C  
ATOM   3906  CG  ASP A 523     -51.715  11.357  -9.385  1.00123.07           C  
ANISOU 3906  CG  ASP A 523    24130   7855  14776  -1579   1310  -1287       C  
ATOM   3907  OD1 ASP A 523     -52.840  11.633  -9.853  1.00120.70           O  
ANISOU 3907  OD1 ASP A 523    23787   7523  14550  -1290   1638  -1068       O  
ATOM   3908  OD2 ASP A 523     -50.678  11.977  -9.701  1.00124.09           O  
ANISOU 3908  OD2 ASP A 523    24157   7819  15173  -1872   1176  -1328       O  
ATOM   3909  N   SER A 524     -54.970  10.185  -8.617  1.00121.35           N  
ANISOU 3909  N   SER A 524    24142   7980  13987   -750   1879  -1132       N  
ATOM   3910  CA  SER A 524     -56.099   9.631  -9.358  1.00119.49           C  
ANISOU 3910  CA  SER A 524    23729   7921  13750   -435   2129   -831       C  
ATOM   3911  C   SER A 524     -55.690   9.097 -10.724  1.00119.36           C  
ANISOU 3911  C   SER A 524    23383   8059  13910   -454   2062   -507       C  
ATOM   3912  O   SER A 524     -56.396   8.246 -11.277  1.00120.72           O  
ANISOU 3912  O   SER A 524    23324   8541  14002   -235   2145   -283       O  
ATOM   3913  CB  SER A 524     -57.196  10.684  -9.518  1.00117.90           C  
ANISOU 3913  CB  SER A 524    23526   7526  13744   -205   2484   -743       C  
ATOM   3914  OG  SER A 524     -58.270  10.436  -8.628  1.00116.72           O  
ANISOU 3914  OG  SER A 524    23560   7442  13348      8   2669   -864       O  
ATOM   3915  N   MET A 525     -54.577   9.583 -11.279  1.00122.87           N  
ANISOU 3915  N   MET A 525    23670   8424  14590   -711   1899   -469       N  
ATOM   3916  CA  MET A 525     -54.070   9.028 -12.530  1.00124.43           C  
ANISOU 3916  CA  MET A 525    23418   8944  14917   -745   1797   -168       C  
ATOM   3917  C   MET A 525     -53.762   7.544 -12.380  1.00120.10           C  
ANISOU 3917  C   MET A 525    22680   8858  14093   -744   1541   -187       C  
ATOM   3918  O   MET A 525     -54.043   6.746 -13.284  1.00116.32           O  
ANISOU 3918  O   MET A 525    21879   8712  13606   -602   1564     68       O  
ATOM   3919  CB  MET A 525     -52.828   9.797 -12.978  1.00132.35           C  
ANISOU 3919  CB  MET A 525    24309   9774  16205  -1061   1665   -170       C  
ATOM   3920  CG  MET A 525     -53.044  11.295 -13.119  1.00144.61           C  
ANISOU 3920  CG  MET A 525    26063  10821  18060  -1090   1913   -150       C  
ATOM   3921  SD  MET A 525     -54.169  11.722 -14.461  1.00148.77           S  
ANISOU 3921  SD  MET A 525    26371  11357  18797   -757   2272    306       S  
ATOM   3922  CE  MET A 525     -53.184  11.270 -15.887  1.00146.83           C  
ANISOU 3922  CE  MET A 525    25671  11421  18697   -915   2141    628       C  
ATOM   3923  N   LYS A 526     -53.186   7.155 -11.239  1.00121.69           N  
ANISOU 3923  N   LYS A 526    23091   9081  14065   -896   1290   -492       N  
ATOM   3924  CA  LYS A 526     -52.998   5.740 -10.942  1.00115.72           C  
ANISOU 3924  CA  LYS A 526    22218   8721  13028   -862   1061   -515       C  
ATOM   3925  C   LYS A 526     -54.327   4.998 -10.902  1.00110.01           C  
ANISOU 3925  C   LYS A 526    21523   8163  12114   -552   1281   -393       C  
ATOM   3926  O   LYS A 526     -54.400   3.831 -11.306  1.00108.91           O  
ANISOU 3926  O   LYS A 526    21135   8379  11868   -462   1192   -255       O  
ATOM   3927  CB  LYS A 526     -52.264   5.579  -9.610  1.00116.50           C  
ANISOU 3927  CB  LYS A 526    22605   8772  12889  -1053    767   -863       C  
ATOM   3928  CG  LYS A 526     -50.750   5.608  -9.714  1.00116.34           C  
ANISOU 3928  CG  LYS A 526    22396   8814  12996  -1360    411   -961       C  
ATOM   3929  CD  LYS A 526     -50.216   4.278 -10.220  1.00113.65           C  
ANISOU 3929  CD  LYS A 526    21688   8911  12584  -1340    179   -819       C  
ATOM   3930  CE  LYS A 526     -48.700   4.226 -10.150  1.00115.94           C  
ANISOU 3930  CE  LYS A 526    21793   9281  12977  -1632   -197   -955       C  
ATOM   3931  NZ  LYS A 526     -48.179   2.889 -10.546  1.00113.37           N  
ANISOU 3931  NZ  LYS A 526    21129   9369  12576  -1589   -426   -842       N  
ATOM   3932  N   LEU A 527     -55.387   5.658 -10.430  1.00108.35           N  
ANISOU 3932  N   LEU A 527    21599   7691  11879   -387   1577   -449       N  
ATOM   3933  CA  LEU A 527     -56.674   4.985 -10.301  1.00103.59           C  
ANISOU 3933  CA  LEU A 527    21019   7233  11106   -105   1801   -357       C  
ATOM   3934  C   LEU A 527     -57.331   4.767 -11.659  1.00101.61           C  
ANISOU 3934  C   LEU A 527    20386   7170  11051     89   1973    -13       C  
ATOM   3935  O   LEU A 527     -57.879   3.691 -11.918  1.00102.27           O  
ANISOU 3935  O   LEU A 527    20286   7564  11010    235   1986    109       O  
ATOM   3936  CB  LEU A 527     -57.601   5.780  -9.383  1.00100.09           C  
ANISOU 3936  CB  LEU A 527    20979   6459  10591     21   2083   -533       C  
ATOM   3937  CG  LEU A 527     -58.937   5.088  -9.107  1.00 95.04           C  
ANISOU 3937  CG  LEU A 527    20374   5964   9773    296   2333   -468       C  
ATOM   3938  CD1 LEU A 527     -58.750   3.887  -8.189  1.00 92.10           C  
ANISOU 3938  CD1 LEU A 527    20130   5834   9030    246   2147   -604       C  
ATOM   3939  CD2 LEU A 527     -59.939   6.063  -8.528  1.00 97.92           C  
ANISOU 3939  CD2 LEU A 527    20998   6037  10171    456   2672   -575       C  
ATOM   3940  N   ILE A 528     -57.306   5.775 -12.534  1.00101.47           N  
ANISOU 3940  N   ILE A 528    20254   6965  11333     95   2104    149       N  
ATOM   3941  CA  ILE A 528     -57.893   5.590 -13.860  1.00 97.85           C  
ANISOU 3941  CA  ILE A 528    19439   6707  11032    281   2241    485       C  
ATOM   3942  C   ILE A 528     -57.046   4.635 -14.689  1.00 92.01           C  
ANISOU 3942  C   ILE A 528    18332   6348  10278    168   1991    616       C  
ATOM   3943  O   ILE A 528     -57.576   3.834 -15.469  1.00 92.92           O  
ANISOU 3943  O   ILE A 528    18167   6775  10364    327   2027    812       O  
ATOM   3944  CB  ILE A 528     -58.082   6.941 -14.576  1.00102.68           C  
ANISOU 3944  CB  ILE A 528    20050   7008  11954    330   2448    652       C  
ATOM   3945  CG1 ILE A 528     -56.839   7.817 -14.423  1.00109.22           C  
ANISOU 3945  CG1 ILE A 528    20995   7563  12940     26   2306    527       C  
ATOM   3946  CG2 ILE A 528     -59.325   7.643 -14.067  1.00103.90           C  
ANISOU 3946  CG2 ILE A 528    20458   6877  12142    570   2763    610       C  
ATOM   3947  CD1 ILE A 528     -56.980   9.195 -15.037  1.00115.73           C  
ANISOU 3947  CD1 ILE A 528    21867   8021  14085     53   2520    686       C  
ATOM   3948  N   ALA A 529     -55.721   4.702 -14.540  1.00 91.01           N  
ANISOU 3948  N   ALA A 529    18191   6205  10182   -108   1734    496       N  
ATOM   3949  CA  ALA A 529     -54.852   3.785 -15.269  1.00 86.39           C  
ANISOU 3949  CA  ALA A 529    17255   5977   9592   -214   1501    592       C  
ATOM   3950  C   ALA A 529     -55.107   2.343 -14.848  1.00 80.06           C  
ANISOU 3950  C   ALA A 529    16403   5491   8527   -123   1372    529       C  
ATOM   3951  O   ALA A 529     -55.354   1.469 -15.690  1.00 74.93           O  
ANISOU 3951  O   ALA A 529    15451   5159   7861    -11   1368    703       O  
ATOM   3952  CB  ALA A 529     -53.388   4.164 -15.048  1.00 85.62           C  
ANISOU 3952  CB  ALA A 529    17155   5784   9594   -529   1251    444       C  
ATOM   3953  N   LYS A 530     -55.066   2.080 -13.539  1.00 78.94           N  
ANISOU 3953  N   LYS A 530    16569   5257   8166   -172   1271    280       N  
ATOM   3954  CA  LYS A 530     -55.273   0.721 -13.050  1.00 76.48           C  
ANISOU 3954  CA  LYS A 530    16249   5209   7600    -97   1151    229       C  
ATOM   3955  C   LYS A 530     -56.688   0.238 -13.347  1.00 75.82           C  
ANISOU 3955  C   LYS A 530    16105   5241   7463    170   1416    378       C  
ATOM   3956  O   LYS A 530     -56.894  -0.927 -13.709  1.00 72.17           O  
ANISOU 3956  O   LYS A 530    15429   5074   6919    251   1358    467       O  
ATOM   3957  CB  LYS A 530     -54.978   0.662 -11.552  1.00 78.48           C  
ANISOU 3957  CB  LYS A 530    16894   5319   7608   -198   1007    -52       C  
ATOM   3958  CG  LYS A 530     -54.521  -0.702 -11.057  1.00 78.89           C  
ANISOU 3958  CG  LYS A 530    16914   5635   7427   -224    740   -114       C  
ATOM   3959  CD  LYS A 530     -53.376  -1.234 -11.907  1.00 77.53           C  
ANISOU 3959  CD  LYS A 530    16361   5700   7398   -347    474    -33       C  
ATOM   3960  CE  LYS A 530     -52.308  -1.900 -11.055  1.00 79.58           C  
ANISOU 3960  CE  LYS A 530    16702   6046   7488   -492    103   -211       C  
ATOM   3961  NZ  LYS A 530     -51.570  -0.911 -10.223  1.00 83.83           N  
ANISOU 3961  NZ  LYS A 530    17503   6329   8018   -697    -44   -441       N  
ATOM   3962  N   ALA A 531     -57.676   1.128 -13.219  1.00 79.73           N  
ANISOU 3962  N   ALA A 531    16769   5500   8025    309   1710    402       N  
ATOM   3963  CA  ALA A 531     -59.062   0.749 -13.475  1.00 79.55           C  
ANISOU 3963  CA  ALA A 531    16666   5580   7980    565   1969    533       C  
ATOM   3964  C   ALA A 531     -59.278   0.388 -14.940  1.00 77.17           C  
ANISOU 3964  C   ALA A 531    15935   5547   7838    665   1990    801       C  
ATOM   3965  O   ALA A 531     -59.921  -0.623 -15.253  1.00 70.53           O  
ANISOU 3965  O   ALA A 531    14905   4969   6923    791   2020    883       O  
ATOM   3966  CB  ALA A 531     -60.000   1.882 -13.055  1.00 77.46           C  
ANISOU 3966  CB  ALA A 531    16653   4988   7790    701   2277    496       C  
ATOM   3967  N   SER A 532     -58.750   1.205 -15.857  1.00 73.30           N  
ANISOU 3967  N   SER A 532    15294   4996   7562    605   1980    937       N  
ATOM   3968  CA  SER A 532     -58.904   0.899 -17.275  1.00 72.72           C  
ANISOU 3968  CA  SER A 532    14833   5194   7603    698   1994   1192       C  
ATOM   3969  C   SER A 532     -58.120  -0.348 -17.661  1.00 69.08           C  
ANISOU 3969  C   SER A 532    14121   5077   7047    594   1743   1183       C  
ATOM   3970  O   SER A 532     -58.559  -1.108 -18.532  1.00 67.09           O  
ANISOU 3970  O   SER A 532    13583   5121   6788    712   1756   1324       O  
ATOM   3971  CB  SER A 532     -58.478   2.096 -18.131  1.00 75.21           C  
ANISOU 3971  CB  SER A 532    15078   5349   8150    649   2057   1357       C  
ATOM   3972  OG  SER A 532     -57.109   2.410 -17.952  1.00 78.17           O  
ANISOU 3972  OG  SER A 532    15499   5627   8577    380   1862   1251       O  
ATOM   3973  N   SER A 533     -56.968  -0.579 -17.025  1.00 70.79           N  
ANISOU 3973  N   SER A 533    14436   5263   7199    382   1506   1009       N  
ATOM   3974  CA  SER A 533     -56.260  -1.840 -17.221  1.00 67.39           C  
ANISOU 3974  CA  SER A 533    13793   5136   6677    309   1266    975       C  
ATOM   3975  C   SER A 533     -57.124  -3.025 -16.801  1.00 68.30           C  
ANISOU 3975  C   SER A 533    13925   5414   6614    453   1295    940       C  
ATOM   3976  O   SER A 533     -57.174  -4.048 -17.498  1.00 63.56           O  
ANISOU 3976  O   SER A 533    13050   5102   5996    508   1230   1016       O  
ATOM   3977  CB  SER A 533     -54.946  -1.831 -16.441  1.00 72.49           C  
ANISOU 3977  CB  SER A 533    14568   5693   7284     77    998    780       C  
ATOM   3978  OG  SER A 533     -54.396  -3.134 -16.358  1.00 75.62           O  
ANISOU 3978  OG  SER A 533    14819   6346   7567     46    769    722       O  
ATOM   3979  N   VAL A 534     -57.816  -2.901 -15.666  1.00 67.99           N  
ANISOU 3979  N   VAL A 534    14209   5183   6441    509   1409    819       N  
ATOM   3980  CA  VAL A 534     -58.724  -3.958 -15.229  1.00 65.45           C  
ANISOU 3980  CA  VAL A 534    13918   4988   5963    637   1485    801       C  
ATOM   3981  C   VAL A 534     -59.836  -4.163 -16.250  1.00 64.11           C  
ANISOU 3981  C   VAL A 534    13470   4991   5899    828   1686    986       C  
ATOM   3982  O   VAL A 534     -60.206  -5.300 -16.570  1.00 62.31           O  
ANISOU 3982  O   VAL A 534    13051   5001   5622    890   1658   1023       O  
ATOM   3983  CB  VAL A 534     -59.286  -3.634 -13.833  1.00 67.37           C  
ANISOU 3983  CB  VAL A 534    14576   4981   6040    661   1616    645       C  
ATOM   3984  CG1 VAL A 534     -60.437  -4.564 -13.491  1.00 66.45           C  
ANISOU 3984  CG1 VAL A 534    14472   4974   5802    808   1783    666       C  
ATOM   3985  CG2 VAL A 534     -58.187  -3.737 -12.791  1.00 72.27           C  
ANISOU 3985  CG2 VAL A 534    15459   5504   6497    476   1359    450       C  
ATOM   3986  N   ALA A 535     -60.381  -3.067 -16.786  1.00 65.23           N  
ANISOU 3986  N   ALA A 535    13581   5010   6194    925   1880   1103       N  
ATOM   3987  CA  ALA A 535     -61.426  -3.181 -17.800  1.00 64.36           C  
ANISOU 3987  CA  ALA A 535    13191   5078   6184   1118   2043   1288       C  
ATOM   3988  C   ALA A 535     -60.920  -3.909 -19.042  1.00 62.40           C  
ANISOU 3988  C   ALA A 535    12574   5160   5977   1090   1879   1403       C  
ATOM   3989  O   ALA A 535     -61.640  -4.728 -19.629  1.00 61.03           O  
ANISOU 3989  O   ALA A 535    12164   5233   5792   1204   1914   1471       O  
ATOM   3990  CB  ALA A 535     -61.951  -1.794 -18.168  1.00 66.33           C  
ANISOU 3990  CB  ALA A 535    13485   5118   6599   1232   2248   1411       C  
ATOM   3991  N   ARG A 536     -59.680  -3.629 -19.454  1.00 62.50           N  
ANISOU 3991  N   ARG A 536    12523   5185   6038    933   1707   1413       N  
ATOM   3992  CA  ARG A 536     -59.130  -4.294 -20.632  1.00 60.95           C  
ANISOU 3992  CA  ARG A 536    11984   5304   5870    905   1571   1507       C  
ATOM   3993  C   ARG A 536     -58.892  -5.777 -20.372  1.00 61.91           C  
ANISOU 3993  C   ARG A 536    12019   5632   5871    868   1406   1385       C  
ATOM   3994  O   ARG A 536     -59.155  -6.614 -21.245  1.00 64.06           O  
ANISOU 3994  O   ARG A 536    12014   6186   6140    937   1380   1444       O  
ATOM   3995  CB  ARG A 536     -57.836  -3.606 -21.072  1.00 62.26           C  
ANISOU 3995  CB  ARG A 536    12104   5420   6132    735   1456   1542       C  
ATOM   3996  CG  ARG A 536     -58.037  -2.190 -21.596  1.00 69.30           C  
ANISOU 3996  CG  ARG A 536    13034   6126   7170    773   1625   1711       C  
ATOM   3997  CD  ARG A 536     -56.790  -1.663 -22.295  1.00 74.79           C  
ANISOU 3997  CD  ARG A 536    13606   6836   7975    600   1533   1786       C  
ATOM   3998  NE  ARG A 536     -55.662  -1.504 -21.380  1.00 77.00           N  
ANISOU 3998  NE  ARG A 536    14055   6933   8267    374   1369   1593       N  
ATOM   3999  CZ  ARG A 536     -55.359  -0.370 -20.756  1.00 77.03           C  
ANISOU 3999  CZ  ARG A 536    14308   6591   8368    264   1414   1538       C  
ATOM   4000  NH1 ARG A 536     -56.101   0.713 -20.946  1.00 76.13           N  
ANISOU 4000  NH1 ARG A 536    14315   6253   8358    372   1636   1671       N  
ATOM   4001  NH2 ARG A 536     -54.312  -0.316 -19.944  1.00 75.80           N  
ANISOU 4001  NH2 ARG A 536    14279   6308   8213     51   1229   1342       N  
ATOM   4002  N   GLN A 537     -58.399  -6.126 -19.181  1.00 59.39           N  
ANISOU 4002  N   GLN A 537    11943   5173   5448    763   1289   1213       N  
ATOM   4003  CA  GLN A 537     -58.208  -7.538 -18.858  1.00 57.97           C  
ANISOU 4003  CA  GLN A 537    11713   5152   5160    743   1138   1115       C  
ATOM   4004  C   GLN A 537     -59.540  -8.279 -18.817  1.00 57.11           C  
ANISOU 4004  C   GLN A 537    11564   5131   5003    893   1300   1140       C  
ATOM   4005  O   GLN A 537     -59.650  -9.410 -19.311  1.00 60.51           O  
ANISOU 4005  O   GLN A 537    11782   5785   5426    923   1233   1140       O  
ATOM   4006  CB  GLN A 537     -57.467  -7.674 -17.529  1.00 58.93           C  
ANISOU 4006  CB  GLN A 537    12138   5092   5160    618    977    948       C  
ATOM   4007  CG  GLN A 537     -56.063  -7.095 -17.545  1.00 59.95           C  
ANISOU 4007  CG  GLN A 537    12262   5161   5354    446    776    895       C  
ATOM   4008  CD  GLN A 537     -55.373  -7.191 -16.201  1.00 61.29           C  
ANISOU 4008  CD  GLN A 537    12734   5164   5388    329    589    721       C  
ATOM   4009  OE1 GLN A 537     -55.281  -8.268 -15.609  1.00 61.04           O  
ANISOU 4009  OE1 GLN A 537    12767   5201   5224    343    459    652       O  
ATOM   4010  NE2 GLN A 537     -54.884  -6.059 -15.707  1.00 77.51           N  
ANISOU 4010  NE2 GLN A 537    14987   6993   7473    214    567    648       N  
ATOM   4011  N   ALA A 538     -60.570  -7.650 -18.245  1.00 59.25           N  
ANISOU 4011  N   ALA A 538    12026   5226   5261    987   1524   1153       N  
ATOM   4012  CA  ALA A 538     -61.889  -8.270 -18.207  1.00 57.76           C  
ANISOU 4012  CA  ALA A 538    11771   5119   5058   1123   1703   1179       C  
ATOM   4013  C   ALA A 538     -62.449  -8.467 -19.611  1.00 60.65           C  
ANISOU 4013  C   ALA A 538    11755   5750   5541   1231   1745   1314       C  
ATOM   4014  O   ALA A 538     -63.008  -9.527 -19.921  1.00 55.76           O  
ANISOU 4014  O   ALA A 538    10952   5320   4916   1275   1746   1303       O  
ATOM   4015  CB  ALA A 538     -62.842  -7.426 -17.363  1.00 59.52           C  
ANISOU 4015  CB  ALA A 538    12252   5099   5265   1212   1957   1165       C  
ATOM   4016  N   ASN A 539     -62.310  -7.457 -20.478  1.00 57.38           N  
ANISOU 4016  N   ASN A 539    11225   5349   5228   1272   1776   1443       N  
ATOM   4017  CA  ASN A 539     -62.800  -7.610 -21.845  1.00 59.84           C  
ANISOU 4017  CA  ASN A 539    11187   5935   5612   1381   1794   1580       C  
ATOM   4018  C   ASN A 539     -62.011  -8.665 -22.609  1.00 57.08           C  
ANISOU 4018  C   ASN A 539    10599   5859   5228   1299   1588   1542       C  
ATOM   4019  O   ASN A 539     -62.567  -9.339 -23.485  1.00 54.99           O  
ANISOU 4019  O   ASN A 539    10065   5856   4975   1377   1583   1576       O  
ATOM   4020  CB  ASN A 539     -62.766  -6.269 -22.575  1.00 66.47           C  
ANISOU 4020  CB  ASN A 539    11991   6714   6551   1446   1872   1753       C  
ATOM   4021  CG  ASN A 539     -64.142  -5.642 -22.690  1.00 78.09           C  
ANISOU 4021  CG  ASN A 539    13435   8135   8102   1649   2091   1864       C  
ATOM   4022  OD1 ASN A 539     -64.930  -6.008 -23.562  1.00 88.10           O  
ANISOU 4022  OD1 ASN A 539    14428   9650   9395   1777   2115   1954       O  
ATOM   4023  ND2 ASN A 539     -64.442  -4.698 -21.805  1.00 77.45           N  
ANISOU 4023  ND2 ASN A 539    13629   7735   8062   1684   2247   1844       N  
ATOM   4024  N   ARG A 540     -60.723  -8.826 -22.298  1.00 59.82           N  
ANISOU 4024  N   ARG A 540    11032   6154   5541   1146   1414   1458       N  
ATOM   4025  CA AARG A 540     -59.969  -9.930 -22.879  0.89 58.02           C  
ANISOU 4025  CA AARG A 540    10592   6163   5291   1080   1229   1392       C  
ATOM   4026  CA BARG A 540     -59.962  -9.932 -22.870  0.11 57.66           C  
ANISOU 4026  CA BARG A 540    10548   6116   5245   1079   1228   1391       C  
ATOM   4027  C   ARG A 540     -60.511 -11.272 -22.402  1.00 56.28           C  
ANISOU 4027  C   ARG A 540    10365   5999   5018   1101   1207   1278       C  
ATOM   4028  O   ARG A 540     -60.564 -12.240 -23.174  1.00 57.02           O  
ANISOU 4028  O   ARG A 540    10212   6332   5121   1122   1138   1248       O  
ATOM   4029  CB AARG A 540     -58.485  -9.785 -22.542  0.89 60.05           C  
ANISOU 4029  CB AARG A 540    10934   6335   5547    921   1049   1322       C  
ATOM   4030  CB BARG A 540     -58.484  -9.800 -22.504  0.11 59.33           C  
ANISOU 4030  CB BARG A 540    10850   6239   5454    920   1047   1318       C  
ATOM   4031  CG AARG A 540     -57.759  -8.802 -23.450  0.89 55.63           C  
ANISOU 4031  CG AARG A 540    10249   5823   5065    873   1046   1441       C  
ATOM   4032  CG BARG A 540     -57.636  -9.104 -23.557  0.11 55.90           C  
ANISOU 4032  CG BARG A 540    10232   5915   5091    866   1010   1420       C  
ATOM   4033  CD AARG A 540     -57.682  -9.357 -24.859  0.89 56.51           C  
ANISOU 4033  CD AARG A 540    10016   6274   5180    923   1019   1506       C  
ATOM   4034  CD BARG A 540     -57.064 -10.099 -24.557  0.11 58.78           C  
ANISOU 4034  CD BARG A 540    10290   6591   5452    856    888   1390       C  
ATOM   4035  NE AARG A 540     -56.852 -10.558 -24.903  0.89 56.14           N  
ANISOU 4035  NE AARG A 540     9842   6376   5113    854    838   1364       N  
ATOM   4036  NE BARG A 540     -58.086 -10.697 -25.410  0.11 52.64           N  
ANISOU 4036  NE BARG A 540     9307   6049   4643    992    967   1434       N  
ATOM   4037  CZ AARG A 540     -57.021 -11.558 -25.761  0.89 52.59           C  
ANISOU 4037  CZ AARG A 540     9143   6201   4638    913    801   1329       C  
ATOM   4038  CZ BARG A 540     -57.842 -11.634 -26.320  0.11 54.89           C  
ANISOU 4038  CZ BARG A 540     9332   6616   4909   1007    886   1385       C  
ATOM   4039  NH1AARG A 540     -58.004 -11.519 -26.650  0.89 54.66           N  
ANISOU 4039  NH1AARG A 540     9249   6644   4875   1033    915   1423       N  
ATOM   4040  NH1BARG A 540     -56.607 -12.083 -26.495  0.11 54.34           N  
ANISOU 4040  NH1BARG A 540     9167   6622   4856    910    741   1301       N  
ATOM   4041  NH2AARG A 540     -56.210 -12.606 -25.723  0.89 51.48           N  
ANISOU 4041  NH2AARG A 540     8908   6152   4501    858    642   1191       N  
ATOM   4042  NH2BARG A 540     -58.830 -12.124 -27.055  0.11 51.60           N  
ANISOU 4042  NH2BARG A 540     8741   6406   4460   1121    949   1407       N  
ATOM   4043  N   VAL A 541     -60.926 -11.349 -21.134  1.00 54.77           N  
ANISOU 4043  N   VAL A 541    10454   5586   4769   1092   1276   1210       N  
ATOM   4044  CA  VAL A 541     -61.589 -12.558 -20.651  1.00 57.50           C  
ANISOU 4044  CA  VAL A 541    10813   5958   5075   1112   1303   1132       C  
ATOM   4045  C   VAL A 541     -62.866 -12.804 -21.445  1.00 60.11           C  
ANISOU 4045  C   VAL A 541    10894   6467   5477   1230   1453   1191       C  
ATOM   4046  O   VAL A 541     -63.186 -13.946 -21.803  1.00 59.76           O  
ANISOU 4046  O   VAL A 541    10673   6579   5454   1233   1415   1134       O  
ATOM   4047  CB  VAL A 541     -61.870 -12.446 -19.141  1.00 55.16           C  
ANISOU 4047  CB  VAL A 541    10890   5390   4679   1086   1390   1073       C  
ATOM   4048  CG1 VAL A 541     -62.819 -13.543 -18.689  1.00 53.50           C  
ANISOU 4048  CG1 VAL A 541    10690   5193   4444   1117   1496   1034       C  
ATOM   4049  CG2 VAL A 541     -60.571 -12.497 -18.356  1.00 53.91           C  
ANISOU 4049  CG2 VAL A 541    10953   5101   4430    963   1180    990       C  
ATOM   4050  N   ILE A 542     -63.600 -11.731 -21.752  1.00 61.83           N  
ANISOU 4050  N   ILE A 542    11084   6661   5748   1332   1614   1302       N  
ATOM   4051  CA  ILE A 542     -64.813 -11.853 -22.558  1.00 64.31           C  
ANISOU 4051  CA  ILE A 542    11133   7165   6138   1460   1733   1369       C  
ATOM   4052  C   ILE A 542     -64.487 -12.432 -23.929  1.00 66.33           C  
ANISOU 4052  C   ILE A 542    11057   7739   6408   1462   1583   1379       C  
ATOM   4053  O   ILE A 542     -65.159 -13.353 -24.409  1.00 67.08           O  
ANISOU 4053  O   ILE A 542    10932   8022   6531   1491   1578   1327       O  
ATOM   4054  CB  ILE A 542     -65.515 -10.488 -22.685  1.00 64.46           C  
ANISOU 4054  CB  ILE A 542    11181   7090   6219   1590   1907   1506       C  
ATOM   4055  CG1 ILE A 542     -65.879  -9.935 -21.307  1.00 67.50           C  
ANISOU 4055  CG1 ILE A 542    11905   7158   6584   1595   2078   1464       C  
ATOM   4056  CG2 ILE A 542     -66.754 -10.608 -23.561  1.00 63.64           C  
ANISOU 4056  CG2 ILE A 542    10770   7210   6199   1738   1996   1582       C  
ATOM   4057  CD1 ILE A 542     -66.936 -10.730 -20.599  1.00 71.37           C  
ANISOU 4057  CD1 ILE A 542    12416   7628   7075   1623   2229   1389       C  
ATOM   4058  N   GLN A 543     -63.451 -11.898 -24.582  1.00 63.26           N  
ANISOU 4058  N   GLN A 543    10625   7413   5999   1423   1468   1437       N  
ATOM   4059  CA  GLN A 543     -63.116 -12.344 -25.932  1.00 64.95           C  
ANISOU 4059  CA  GLN A 543    10536   7943   6198   1434   1351   1451       C  
ATOM   4060  C   GLN A 543     -62.675 -13.803 -25.942  1.00 63.99           C  
ANISOU 4060  C   GLN A 543    10325   7931   6059   1352   1212   1280       C  
ATOM   4061  O   GLN A 543     -63.133 -14.596 -26.775  1.00 65.35           O  
ANISOU 4061  O   GLN A 543    10248   8347   6235   1388   1177   1227       O  
ATOM   4062  CB  GLN A 543     -62.027 -11.453 -26.527  1.00 64.29           C  
ANISOU 4062  CB  GLN A 543    10449   7880   6097   1392   1289   1554       C  
ATOM   4063  CG  GLN A 543     -62.430 -10.004 -26.700  1.00 69.38           C  
ANISOU 4063  CG  GLN A 543    11167   8415   6779   1480   1425   1745       C  
ATOM   4064  CD  GLN A 543     -61.305  -9.161 -27.260  1.00 72.89           C  
ANISOU 4064  CD  GLN A 543    11615   8855   7223   1409   1378   1853       C  
ATOM   4065  OE1 GLN A 543     -60.372  -9.681 -27.876  1.00 70.72           O  
ANISOU 4065  OE1 GLN A 543    11199   8763   6910   1326   1256   1806       O  
ATOM   4066  NE2 GLN A 543     -61.381  -7.852 -27.044  1.00 75.64           N  
ANISOU 4066  NE2 GLN A 543    12126   8985   7629   1438   1491   1993       N  
ATOM   4067  N   VAL A 544     -61.777 -14.176 -25.027  1.00 59.46           N  
ANISOU 4067  N   VAL A 544     9951   7176   5467   1244   1122   1186       N  
ATOM   4068  CA  VAL A 544     -61.328 -15.564 -24.971  1.00 58.08           C  
ANISOU 4068  CA  VAL A 544     9709   7065   5293   1184    989   1035       C  
ATOM   4069  C   VAL A 544     -62.504 -16.490 -24.683  1.00 54.94           C  
ANISOU 4069  C   VAL A 544     9276   6668   4930   1215   1077    967       C  
ATOM   4070  O   VAL A 544     -62.608 -17.582 -25.256  1.00 54.98           O  
ANISOU 4070  O   VAL A 544     9089   6832   4968   1206   1010    862       O  
ATOM   4071  CB  VAL A 544     -60.201 -15.722 -23.935  1.00 60.27           C  
ANISOU 4071  CB  VAL A 544    10226   7130   5544   1084    864    969       C  
ATOM   4072  CG1 VAL A 544     -59.835 -17.188 -23.766  1.00 58.40           C  
ANISOU 4072  CG1 VAL A 544     9946   6919   5326   1048    736    830       C  
ATOM   4073  CG2 VAL A 544     -58.987 -14.918 -24.367  1.00 49.88           C  
ANISOU 4073  CG2 VAL A 544     8873   5849   4228   1031    767   1015       C  
ATOM   4074  N   ALA A 545     -63.424 -16.058 -23.816  1.00 55.74           N  
ANISOU 4074  N   ALA A 545     9554   6589   5037   1247   1243   1017       N  
ATOM   4075  CA  ALA A 545     -64.635 -16.840 -23.591  1.00 59.87           C  
ANISOU 4075  CA  ALA A 545    10011   7121   5617   1269   1363    968       C  
ATOM   4076  C   ALA A 545     -65.465 -16.964 -24.863  1.00 61.22           C  
ANISOU 4076  C   ALA A 545     9830   7582   5849   1346   1382    977       C  
ATOM   4077  O   ALA A 545     -66.091 -18.003 -25.098  1.00 63.74           O  
ANISOU 4077  O   ALA A 545     9987   7999   6232   1325   1385    877       O  
ATOM   4078  CB  ALA A 545     -65.467 -16.218 -22.469  1.00 51.65           C  
ANISOU 4078  CB  ALA A 545     9209   5847   4568   1300   1571   1026       C  
ATOM   4079  N   LYS A 546     -65.476 -15.921 -25.696  1.00 59.19           N  
ANISOU 4079  N   LYS A 546     9456   7464   5572   1431   1386   1097       N  
ATOM   4080  CA  LYS A 546     -66.201 -15.982 -26.962  1.00 62.13           C  
ANISOU 4080  CA  LYS A 546     9498   8142   5964   1518   1371   1119       C  
ATOM   4081  C   LYS A 546     -65.584 -17.017 -27.896  1.00 59.28           C  
ANISOU 4081  C   LYS A 546     8933   8018   5572   1462   1198    986       C  
ATOM   4082  O   LYS A 546     -66.295 -17.821 -28.513  1.00 56.94           O  
ANISOU 4082  O   LYS A 546     8405   7917   5315   1471   1173    886       O  
ATOM   4083  CB  LYS A 546     -66.220 -14.598 -27.614  1.00 67.71           C  
ANISOU 4083  CB  LYS A 546    10168   8923   6635   1629   1405   1309       C  
ATOM   4084  CG  LYS A 546     -66.522 -14.590 -29.106  1.00 74.04           C  
ANISOU 4084  CG  LYS A 546    10653  10086   7393   1715   1324   1354       C  
ATOM   4085  CD  LYS A 546     -67.968 -14.954 -29.399  1.00 79.75           C  
ANISOU 4085  CD  LYS A 546    11149  10962   8190   1800   1378   1327       C  
ATOM   4086  CE  LYS A 546     -68.301 -14.709 -30.864  1.00 84.50           C  
ANISOU 4086  CE  LYS A 546    11463  11929   8716   1910   1283   1403       C  
ATOM   4087  NZ  LYS A 546     -69.685 -15.135 -31.214  1.00 87.02           N  
ANISOU 4087  NZ  LYS A 546    11518  12432   9113   1985   1295   1352       N  
ATOM   4088  N   VAL A 547     -64.252 -17.015 -28.008  1.00 60.29           N  
ANISOU 4088  N   VAL A 547     9135   8132   5640   1401   1081    967       N  
ATOM   4089  CA  VAL A 547     -63.578 -18.011 -28.837  1.00 63.32           C  
ANISOU 4089  CA  VAL A 547     9337   8721   5999   1356    935    821       C  
ATOM   4090  C   VAL A 547     -63.850 -19.418 -28.314  1.00 63.24           C  
ANISOU 4090  C   VAL A 547     9334   8620   6073   1287    909    640       C  
ATOM   4091  O   VAL A 547     -64.123 -20.341 -29.091  1.00 64.23           O  
ANISOU 4091  O   VAL A 547     9241   8940   6222   1280    848    499       O  
ATOM   4092  CB  VAL A 547     -62.068 -17.714 -28.909  1.00 64.62           C  
ANISOU 4092  CB  VAL A 547     9581   8859   6114   1304    835    836       C  
ATOM   4093  CG1 VAL A 547     -61.301 -18.940 -29.391  1.00 59.58           C  
ANISOU 4093  CG1 VAL A 547     8808   8345   5485   1255    700    648       C  
ATOM   4094  CG2 VAL A 547     -61.808 -16.531 -29.828  1.00 68.04           C  
ANISOU 4094  CG2 VAL A 547     9927   9458   6466   1361    858   1002       C  
ATOM   4095  N   GLU A 548     -63.794 -19.603 -26.993  1.00 62.65           N  
ANISOU 4095  N   GLU A 548     9521   8243   6039   1233    959    639       N  
ATOM   4096  CA  GLU A 548     -64.016 -20.933 -26.433  1.00 63.60           C  
ANISOU 4096  CA  GLU A 548     9682   8241   6241   1165    948    499       C  
ATOM   4097  C   GLU A 548     -65.451 -21.397 -26.648  1.00 60.57           C  
ANISOU 4097  C   GLU A 548     9131   7937   5947   1173   1061    452       C  
ATOM   4098  O   GLU A 548     -65.694 -22.585 -26.893  1.00 59.63           O  
ANISOU 4098  O   GLU A 548     8890   7856   5913   1118   1022    299       O  
ATOM   4099  CB  GLU A 548     -63.669 -20.947 -24.947  1.00 72.76           C  
ANISOU 4099  CB  GLU A 548    11187   9069   7389   1114    982    540       C  
ATOM   4100  CG  GLU A 548     -62.553 -21.910 -24.602  1.00 81.89           C  
ANISOU 4100  CG  GLU A 548    12438  10119   8558   1058    823    440       C  
ATOM   4101  CD  GLU A 548     -62.875 -23.345 -24.964  1.00 86.35           C  
ANISOU 4101  CD  GLU A 548    12854  10723   9231   1024    791    285       C  
ATOM   4102  OE1 GLU A 548     -63.661 -23.982 -24.231  1.00 87.77           O  
ANISOU 4102  OE1 GLU A 548    13139  10734   9474    981    897    273       O  
ATOM   4103  OE2 GLU A 548     -62.345 -23.833 -25.985  1.00 87.41           O  
ANISOU 4103  OE2 GLU A 548    12769  11052   9391   1037    673    170       O  
ATOM   4104  N   ALA A 549     -66.414 -20.480 -26.555  1.00 60.80           N  
ANISOU 4104  N   ALA A 549     9140   7982   5978   1240   1202    574       N  
ATOM   4105  CA  ALA A 549     -67.805 -20.848 -26.790  1.00 68.09           C  
ANISOU 4105  CA  ALA A 549     9859   9006   7007   1252   1306    532       C  
ATOM   4106  C   ALA A 549     -68.042 -21.204 -28.253  1.00 75.80           C  
ANISOU 4106  C   ALA A 549    10485  10332   7981   1282   1183    435       C  
ATOM   4107  O   ALA A 549     -68.749 -22.174 -28.556  1.00 74.72           O  
ANISOU 4107  O   ALA A 549    10161  10282   7948   1227   1176    288       O  
ATOM   4108  CB  ALA A 549     -68.730 -19.712 -26.354  1.00 64.80           C  
ANISOU 4108  CB  ALA A 549     9490   8527   6605   1343   1486    689       C  
ATOM   4109  N   ASP A 550     -67.454 -20.434 -29.176  1.00 83.06           N  
ANISOU 4109  N   ASP A 550    11322  11459   8778   1360   1087    512       N  
ATOM   4110  CA  ASP A 550     -67.614 -20.730 -30.597  1.00 88.37           C  
ANISOU 4110  CA  ASP A 550    11689  12492   9397   1397    964    424       C  
ATOM   4111  C   ASP A 550     -67.063 -22.102 -30.960  1.00 90.91           C  
ANISOU 4111  C   ASP A 550    11931  12865   9746   1300    844    187       C  
ATOM   4112  O   ASP A 550     -67.626 -22.785 -31.823  1.00 99.02           O  
ANISOU 4112  O   ASP A 550    12708  14124  10792   1287    775     32       O  
ATOM   4113  CB  ASP A 550     -66.922 -19.657 -31.436  1.00 92.27           C  
ANISOU 4113  CB  ASP A 550    12159  13169   9729   1489    904    574       C  
ATOM   4114  CG  ASP A 550     -67.639 -18.328 -31.389  1.00 97.45           C  
ANISOU 4114  CG  ASP A 550    12830  13825  10372   1612   1009    802       C  
ATOM   4115  OD1 ASP A 550     -68.557 -18.172 -30.551  1.00 99.51           O  
ANISOU 4115  OD1 ASP A 550    13150  13911  10749   1628   1142    841       O  
ATOM   4116  OD2 ASP A 550     -67.282 -17.437 -32.187  1.00 99.45           O  
ANISOU 4116  OD2 ASP A 550    13038  14244  10503   1698    971    948       O  
ATOM   4117  N   ASN A 551     -65.979 -22.523 -30.312  1.00 83.93           N  
ANISOU 4117  N   ASN A 551    11253  11765   8870   1236    810    145       N  
ATOM   4118  CA  ASN A 551     -65.307 -23.770 -30.651  1.00 80.42           C  
ANISOU 4118  CA  ASN A 551    10749  11343   8465   1169    696    -71       C  
ATOM   4119  C   ASN A 551     -66.053 -25.009 -30.168  1.00 80.28           C  
ANISOU 4119  C   ASN A 551    10713  11172   8619   1075    735   -231       C  
ATOM   4120  O   ASN A 551     -65.649 -26.126 -30.510  1.00 81.62           O  
ANISOU 4120  O   ASN A 551    10815  11346   8850   1022    648   -431       O  
ATOM   4121  CB  ASN A 551     -63.887 -23.758 -30.074  1.00 79.04           C  
ANISOU 4121  CB  ASN A 551    10788  10980   8262   1150    636    -44       C  
ATOM   4122  CG  ASN A 551     -63.043 -24.916 -30.567  1.00 82.57           C  
ANISOU 4122  CG  ASN A 551    11150  11475   8748   1118    514   -258       C  
ATOM   4123  OD1 ASN A 551     -62.687 -24.984 -31.744  1.00 84.67           O  
ANISOU 4123  OD1 ASN A 551    11214  12025   8931   1153    441   -352       O  
ATOM   4124  ND2 ASN A 551     -62.716 -25.837 -29.664  1.00 82.57           N  
ANISOU 4124  ND2 ASN A 551    11311  11193   8869   1062    496   -332       N  
ATOM   4125  N   SER A 552     -67.128 -24.852 -29.403  1.00 78.98           N  
ANISOU 4125  N   SER A 552    10601  10863   8545   1052    878   -152       N  
ATOM   4126  CA  SER A 552     -67.864 -25.980 -28.853  1.00 80.27           C  
ANISOU 4126  CA  SER A 552    10762  10851   8888    943    951   -276       C  
ATOM   4127  C   SER A 552     -69.236 -26.090 -29.503  1.00 81.75           C  
ANISOU 4127  C   SER A 552    10649  11251   9162    930    994   -351       C  
ATOM   4128  O   SER A 552     -69.908 -25.080 -29.734  1.00 81.92           O  
ANISOU 4128  O   SER A 552    10569  11425   9132   1018   1047   -218       O  
ATOM   4129  CB  SER A 552     -68.024 -25.846 -27.336  1.00 81.88           C  
ANISOU 4129  CB  SER A 552    11272  10700   9137    905   1109   -135       C  
ATOM   4130  OG  SER A 552     -68.795 -26.914 -26.812  1.00 83.34           O  
ANISOU 4130  OG  SER A 552    11455  10713   9497    790   1210   -230       O  
ATOM   4131  N   GLU A 553     -69.644 -27.324 -29.796  1.00 89.14           N  
ANISOU 4131  N   GLU A 553    11436  12189  10245    821    962   -570       N  
ATOM   4132  CA  GLU A 553     -70.988 -27.615 -30.275  1.00 95.22           C  
ANISOU 4132  CA  GLU A 553    11912  13125  11143    771    997   -675       C  
ATOM   4133  C   GLU A 553     -71.903 -28.103 -29.161  1.00 93.12           C  
ANISOU 4133  C   GLU A 553    11722  12574  11086    656   1199   -650       C  
ATOM   4134  O   GLU A 553     -72.987 -28.621 -29.444  1.00 96.10           O  
ANISOU 4134  O   GLU A 553    11848  13035  11629    569   1239   -775       O  
ATOM   4135  CB  GLU A 553     -70.940 -28.644 -31.406  1.00104.69           C  
ANISOU 4135  CB  GLU A 553    12868  14530  12380    706    833   -963       C  
ATOM   4136  CG  GLU A 553     -70.103 -28.210 -32.599  1.00112.73           C  
ANISOU 4136  CG  GLU A 553    13792  15869  13172    816    655  -1002       C  
ATOM   4137  CD  GLU A 553     -70.706 -28.631 -33.927  1.00119.82           C  
ANISOU 4137  CD  GLU A 553    14351  17133  14045    800    515  -1229       C  
ATOM   4138  OE1 GLU A 553     -71.624 -29.478 -33.925  1.00123.70           O  
ANISOU 4138  OE1 GLU A 553    14678  17593  14730    676    531  -1409       O  
ATOM   4139  OE2 GLU A 553     -70.265 -28.108 -34.972  1.00120.33           O  
ANISOU 4139  OE2 GLU A 553    14313  17519  13887    905    389  -1228       O  
ATOM   4140  N   ASN A 554     -71.486 -27.953 -27.904  1.00 83.54           N  
ANISOU 4140  N   ASN A 554    10847  11035   9860    647   1329   -494       N  
ATOM   4141  CA  ASN A 554     -72.272 -28.336 -26.738  1.00 76.62           C  
ANISOU 4141  CA  ASN A 554    10100   9874   9139    544   1555   -434       C  
ATOM   4142  C   ASN A 554     -73.175 -27.176 -26.339  1.00 73.83           C  
ANISOU 4142  C   ASN A 554     9713   9573   8765    628   1729   -256       C  
ATOM   4143  O   ASN A 554     -72.702 -26.195 -25.752  1.00 73.41           O  
ANISOU 4143  O   ASN A 554     9900   9431   8560    729   1779    -75       O  
ATOM   4144  CB  ASN A 554     -71.348 -28.737 -25.586  1.00 72.74           C  
ANISOU 4144  CB  ASN A 554    10011   9022   8603    508   1597   -349       C  
ATOM   4145  CG  ASN A 554     -72.102 -29.280 -24.388  1.00 70.80           C  
ANISOU 4145  CG  ASN A 554     9929   8475   8495    389   1840   -285       C  
ATOM   4146  OD1 ASN A 554     -73.295 -29.574 -24.466  1.00 72.59           O  
ANISOU 4146  OD1 ASN A 554     9937   8744   8900    302   1981   -342       O  
ATOM   4147  ND2 ASN A 554     -71.402 -29.425 -23.270  1.00 68.76           N  
ANISOU 4147  ND2 ASN A 554    10055   7918   8153    382   1890   -163       N  
ATOM   4148  N   PRO A 555     -74.477 -27.253 -26.630  1.00 73.46           N  
ANISOU 4148  N   PRO A 555     9364   9663   8882    590   1824   -312       N  
ATOM   4149  CA  PRO A 555     -75.338 -26.071 -26.441  1.00 76.42           C  
ANISOU 4149  CA  PRO A 555     9651  10136   9250    710   1968   -153       C  
ATOM   4150  C   PRO A 555     -75.461 -25.623 -24.995  1.00 82.91           C  
ANISOU 4150  C   PRO A 555    10801  10646  10055    715   2231     23       C  
ATOM   4151  O   PRO A 555     -75.516 -24.415 -24.732  1.00 86.43           O  
ANISOU 4151  O   PRO A 555    11338  11107  10396    859   2307    183       O  
ATOM   4152  CB  PRO A 555     -76.690 -26.532 -27.008  1.00 75.76           C  
ANISOU 4152  CB  PRO A 555     9148  10246   9393    638   2002   -288       C  
ATOM   4153  CG  PRO A 555     -76.371 -27.711 -27.877  1.00 75.85           C  
ANISOU 4153  CG  PRO A 555     8998  10359   9462    514   1798   -533       C  
ATOM   4154  CD  PRO A 555     -75.213 -28.384 -27.215  1.00 75.11           C  
ANISOU 4154  CD  PRO A 555     9273   9960   9306    442   1788   -537       C  
ATOM   4155  N   GLU A 556     -75.515 -26.561 -24.046  1.00 84.66           N  
ANISOU 4155  N   GLU A 556    11217  10579  10369    563   2378     -2       N  
ATOM   4156  CA  GLU A 556     -75.662 -26.182 -22.644  1.00 85.36           C  
ANISOU 4156  CA  GLU A 556    11640  10385  10407    563   2641    160       C  
ATOM   4157  C   GLU A 556     -74.430 -25.440 -22.140  1.00 78.33           C  
ANISOU 4157  C   GLU A 556    11132   9371   9261    666   2555    286       C  
ATOM   4158  O   GLU A 556     -74.550 -24.426 -21.440  1.00 77.00           O  
ANISOU 4158  O   GLU A 556    11151   9119   8986    760   2704    424       O  
ATOM   4159  CB  GLU A 556     -75.932 -27.422 -21.791  1.00 94.63           C  
ANISOU 4159  CB  GLU A 556    12957  11283  11717    372   2808    121       C  
ATOM   4160  CG  GLU A 556     -77.046 -28.315 -22.321  1.00104.79           C  
ANISOU 4160  CG  GLU A 556    13857  12666  13291    227   2873    -35       C  
ATOM   4161  CD  GLU A 556     -78.407 -27.641 -22.303  1.00112.64           C  
ANISOU 4161  CD  GLU A 556    14568  13806  14424    268   3086      4       C  
ATOM   4162  OE1 GLU A 556     -78.606 -26.713 -21.490  1.00116.99           O  
ANISOU 4162  OE1 GLU A 556    15308  14268  14875    372   3288    165       O  
ATOM   4163  OE2 GLU A 556     -79.278 -28.040 -23.105  1.00117.18           O  
ANISOU 4163  OE2 GLU A 556    14722  14586  15215    201   3048   -140       O  
ATOM   4164  N   PHE A 557     -73.238 -25.927 -22.492  1.00 73.94           N  
ANISOU 4164  N   PHE A 557    10681   8799   8613    648   2317    225       N  
ATOM   4165  CA  PHE A 557     -72.012 -25.248 -22.086  1.00 71.47           C  
ANISOU 4165  CA  PHE A 557    10686   8391   8080    732   2207    326       C  
ATOM   4166  C   PHE A 557     -71.900 -23.873 -22.736  1.00 73.60           C  
ANISOU 4166  C   PHE A 557    10848   8871   8244    886   2139    403       C  
ATOM   4167  O   PHE A 557     -71.442 -22.916 -22.099  1.00 77.18           O  
ANISOU 4167  O   PHE A 557    11562   9210   8553    960   2181    527       O  
ATOM   4168  CB  PHE A 557     -70.800 -26.116 -22.425  1.00 68.96           C  
ANISOU 4168  CB  PHE A 557    10437   8037   7726    686   1966    230       C  
ATOM   4169  CG  PHE A 557     -69.493 -25.378 -22.388  1.00 69.35           C  
ANISOU 4169  CG  PHE A 557    10686   8082   7581    776   1796    301       C  
ATOM   4170  CD1 PHE A 557     -68.986 -24.894 -21.194  1.00 69.94           C  
ANISOU 4170  CD1 PHE A 557    11140   7923   7511    792   1856    428       C  
ATOM   4171  CD2 PHE A 557     -68.764 -25.176 -23.549  1.00 66.57           C  
ANISOU 4171  CD2 PHE A 557    10139   7967   7186    836   1578    232       C  
ATOM   4172  CE1 PHE A 557     -67.781 -24.211 -21.161  1.00 67.41           C  
ANISOU 4172  CE1 PHE A 557    10978   7600   7035    856   1687    477       C  
ATOM   4173  CE2 PHE A 557     -67.558 -24.500 -23.522  1.00 62.54           C  
ANISOU 4173  CE2 PHE A 557     9786   7451   6523    900   1437    296       C  
ATOM   4174  CZ  PHE A 557     -67.066 -24.017 -22.327  1.00 60.83           C  
ANISOU 4174  CZ  PHE A 557     9926   6995   6193    904   1485    414       C  
ATOM   4175  N   VAL A 558     -72.320 -23.753 -23.997  1.00 72.58           N  
ANISOU 4175  N   VAL A 558    10348   9046   8183    935   2032    333       N  
ATOM   4176  CA  VAL A 558     -72.302 -22.454 -24.666  1.00 72.33           C  
ANISOU 4176  CA  VAL A 558    10208   9214   8059   1091   1978    435       C  
ATOM   4177  C   VAL A 558     -73.280 -21.498 -23.995  1.00 72.42           C  
ANISOU 4177  C   VAL A 558    10259   9146   8110   1177   2222    565       C  
ATOM   4178  O   VAL A 558     -73.019 -20.293 -23.886  1.00 72.15           O  
ANISOU 4178  O   VAL A 558    10350   9091   7973   1300   2245    697       O  
ATOM   4179  CB  VAL A 558     -72.606 -22.621 -26.169  1.00 73.54           C  
ANISOU 4179  CB  VAL A 558     9960   9727   8253   1129   1805    337       C  
ATOM   4180  CG1 VAL A 558     -72.730 -21.264 -26.850  1.00 74.27           C  
ANISOU 4180  CG1 VAL A 558     9942  10022   8256   1303   1768    479       C  
ATOM   4181  CG2 VAL A 558     -71.523 -23.450 -26.842  1.00 71.96           C  
ANISOU 4181  CG2 VAL A 558     9748   9604   7992   1064   1579    199       C  
ATOM   4182  N   ALA A 559     -74.414 -22.019 -23.525  1.00 71.87           N  
ANISOU 4182  N   ALA A 559    10084   9019   8206   1112   2422    526       N  
ATOM   4183  CA  ALA A 559     -75.390 -21.175 -22.843  1.00 73.52           C  
ANISOU 4183  CA  ALA A 559    10314   9149   8472   1199   2687    634       C  
ATOM   4184  C   ALA A 559     -74.859 -20.696 -21.497  1.00 73.39           C  
ANISOU 4184  C   ALA A 559    10759   8818   8307   1200   2842    731       C  
ATOM   4185  O   ALA A 559     -74.961 -19.508 -21.165  1.00 75.98           O  
ANISOU 4185  O   ALA A 559    11208   9090   8571   1331   2948    838       O  
ATOM   4186  CB  ALA A 559     -76.707 -21.932 -22.670  1.00 76.34           C  
ANISOU 4186  CB  ALA A 559    10420   9528   9059   1107   2878    556       C  
ATOM   4187  N   LYS A 560     -74.289 -21.609 -20.704  1.00 72.06           N  
ANISOU 4187  N   LYS A 560    10862   8437   8080   1060   2849    692       N  
ATOM   4188  CA  LYS A 560     -73.727 -21.222 -19.412  1.00 71.47           C  
ANISOU 4188  CA  LYS A 560    11245   8083   7828   1055   2961    775       C  
ATOM   4189  C   LYS A 560     -72.600 -20.210 -19.586  1.00 65.70           C  
ANISOU 4189  C   LYS A 560    10692   7352   6919   1150   2776    833       C  
ATOM   4190  O   LYS A 560     -72.555 -19.183 -18.895  1.00 69.46           O  
ANISOU 4190  O   LYS A 560    11407   7695   7291   1227   2897    912       O  
ATOM   4191  CB  LYS A 560     -73.224 -22.459 -18.665  1.00 74.09           C  
ANISOU 4191  CB  LYS A 560    11821   8212   8118    900   2945    737       C  
ATOM   4192  CG  LYS A 560     -74.315 -23.424 -18.228  1.00 77.32           C  
ANISOU 4192  CG  LYS A 560    12138   8544   8697    780   3186    704       C  
ATOM   4193  CD  LYS A 560     -73.711 -24.689 -17.629  1.00 80.92           C  
ANISOU 4193  CD  LYS A 560    12835   8791   9118    636   3135    685       C  
ATOM   4194  CE  LYS A 560     -74.784 -25.628 -17.097  1.00 86.64           C  
ANISOU 4194  CE  LYS A 560    13506   9398  10015    496   3410    677       C  
ATOM   4195  NZ  LYS A 560     -74.208 -26.907 -16.589  1.00 87.71           N  
ANISOU 4195  NZ  LYS A 560    13873   9312  10139    362   3355    676       N  
ATOM   4196  N   LEU A 561     -71.679 -20.485 -20.513  1.00 63.07           N  
ANISOU 4196  N   LEU A 561    10241   7162   6559   1139   2494    785       N  
ATOM   4197  CA  LEU A 561     -70.575 -19.564 -20.754  1.00 60.99           C  
ANISOU 4197  CA  LEU A 561    10110   6910   6152   1207   2323    840       C  
ATOM   4198  C   LEU A 561     -71.072 -18.220 -21.268  1.00 65.23           C  
ANISOU 4198  C   LEU A 561    10514   7558   6710   1356   2392    934       C  
ATOM   4199  O   LEU A 561     -70.485 -17.178 -20.953  1.00 71.07           O  
ANISOU 4199  O   LEU A 561    11469   8189   7345   1413   2384   1010       O  
ATOM   4200  CB  LEU A 561     -69.585 -20.181 -21.741  1.00 58.40           C  
ANISOU 4200  CB  LEU A 561     9631   6745   5814   1167   2040    763       C  
ATOM   4201  CG  LEU A 561     -68.293 -19.397 -21.959  1.00 60.08           C  
ANISOU 4201  CG  LEU A 561     9974   6960   5893   1203   1860    811       C  
ATOM   4202  CD1 LEU A 561     -67.635 -19.096 -20.621  1.00 53.30           C  
ANISOU 4202  CD1 LEU A 561     9533   5815   4903   1164   1892    851       C  
ATOM   4203  CD2 LEU A 561     -67.347 -20.165 -22.870  1.00 52.23           C  
ANISOU 4203  CD2 LEU A 561     8820   6125   4900   1159   1616    717       C  
ATOM   4204  N   SER A 562     -72.150 -18.220 -22.055  1.00 65.23           N  
ANISOU 4204  N   SER A 562    10162   7767   6857   1421   2453    931       N  
ATOM   4205  CA  SER A 562     -72.730 -16.960 -22.503  1.00 66.00           C  
ANISOU 4205  CA  SER A 562    10128   7956   6991   1589   2528   1042       C  
ATOM   4206  C   SER A 562     -73.322 -16.185 -21.335  1.00 71.61           C  
ANISOU 4206  C   SER A 562    11079   8425   7704   1652   2807   1105       C  
ATOM   4207  O   SER A 562     -73.209 -14.956 -21.278  1.00 74.66           O  
ANISOU 4207  O   SER A 562    11576   8739   8054   1774   2855   1202       O  
ATOM   4208  CB  SER A 562     -73.792 -17.217 -23.572  1.00 63.53           C  
ANISOU 4208  CB  SER A 562     9368   7937   6834   1652   2507   1018       C  
ATOM   4209  OG  SER A 562     -73.218 -17.805 -24.723  1.00 64.07           O  
ANISOU 4209  OG  SER A 562     9230   8247   6866   1610   2248    950       O  
ATOM   4210  N   SER A 563     -73.953 -16.884 -20.389  1.00 70.95           N  
ANISOU 4210  N   SER A 563    11090   8203   7666   1567   3009   1049       N  
ATOM   4211  CA  SER A 563     -74.482 -16.203 -19.213  1.00 71.03           C  
ANISOU 4211  CA  SER A 563    11357   7983   7650   1621   3300   1092       C  
ATOM   4212  C   SER A 563     -73.361 -15.597 -18.377  1.00 72.57           C  
ANISOU 4212  C   SER A 563    12002   7942   7631   1599   3254   1113       C  
ATOM   4213  O   SER A 563     -73.474 -14.457 -17.908  1.00 77.82           O  
ANISOU 4213  O   SER A 563    12845   8468   8256   1705   3392   1163       O  
ATOM   4214  CB  SER A 563     -75.320 -17.168 -18.375  1.00 69.85           C  
ANISOU 4214  CB  SER A 563    11227   7741   7570   1514   3538   1035       C  
ATOM   4215  OG  SER A 563     -76.509 -17.531 -19.057  1.00 67.95           O  
ANISOU 4215  OG  SER A 563    10553   7706   7561   1541   3619   1009       O  
ATOM   4216  N   ALA A 564     -72.263 -16.335 -18.192  1.00 68.61           N  
ANISOU 4216  N   ALA A 564    11679   7389   7002   1467   3052   1066       N  
ATOM   4217  CA  ALA A 564     -71.150 -15.809 -17.405  1.00 65.07           C  
ANISOU 4217  CA  ALA A 564    11635   6736   6354   1434   2969   1072       C  
ATOM   4218  C   ALA A 564     -70.490 -14.622 -18.101  1.00 65.72           C  
ANISOU 4218  C   ALA A 564    11684   6864   6423   1522   2825   1128       C  
ATOM   4219  O   ALA A 564     -70.202 -13.600 -17.467  1.00 67.21           O  
ANISOU 4219  O   ALA A 564    12145   6868   6523   1562   2894   1150       O  
ATOM   4220  CB  ALA A 564     -70.129 -16.913 -17.135  1.00 58.04           C  
ANISOU 4220  CB  ALA A 564    10892   5803   5358   1290   2758   1016       C  
ATOM   4221  N   SER A 565     -70.244 -14.737 -19.409  1.00 66.62           N  
ANISOU 4221  N   SER A 565    11476   7217   6618   1546   2632   1150       N  
ATOM   4222  CA  SER A 565     -69.580 -13.654 -20.128  1.00 68.30           C  
ANISOU 4222  CA  SER A 565    11657   7477   6817   1617   2505   1228       C  
ATOM   4223  C   SER A 565     -70.462 -12.413 -20.198  1.00 69.56           C  
ANISOU 4223  C   SER A 565    11777   7590   7063   1783   2705   1325       C  
ATOM   4224  O   SER A 565     -69.978 -11.289 -20.023  1.00 66.25           O  
ANISOU 4224  O   SER A 565    11546   7020   6604   1828   2713   1381       O  
ATOM   4225  CB  SER A 565     -69.187 -14.114 -21.532  1.00 71.31           C  
ANISOU 4225  CB  SER A 565    11705   8149   7242   1611   2281   1234       C  
ATOM   4226  OG  SER A 565     -70.328 -14.299 -22.349  1.00 74.93           O  
ANISOU 4226  OG  SER A 565    11812   8827   7829   1703   2346   1257       O  
ATOM   4227  N   GLU A 566     -71.761 -12.594 -20.447  1.00 74.62           N  
ANISOU 4227  N   GLU A 566    12164   8345   7841   1876   2866   1341       N  
ATOM   4228  CA  GLU A 566     -72.670 -11.454 -20.482  1.00 81.10           C  
ANISOU 4228  CA  GLU A 566    12925   9116   8771   2062   3064   1434       C  
ATOM   4229  C   GLU A 566     -72.786 -10.798 -19.111  1.00 78.17           C  
ANISOU 4229  C   GLU A 566    12938   8425   8339   2076   3301   1402       C  
ATOM   4230  O   GLU A 566     -72.761  -9.565 -19.001  1.00 79.68           O  
ANISOU 4230  O   GLU A 566    13261   8464   8549   2191   3384   1466       O  
ATOM   4231  CB  GLU A 566     -74.041 -11.897 -20.991  1.00 93.41           C  
ANISOU 4231  CB  GLU A 566    14100  10884  10506   2152   3175   1440       C  
ATOM   4232  CG  GLU A 566     -74.074 -12.203 -22.482  1.00103.30           C  
ANISOU 4232  CG  GLU A 566    14960  12474  11815   2190   2946   1484       C  
ATOM   4233  CD  GLU A 566     -75.230 -13.107 -22.869  1.00111.61           C  
ANISOU 4233  CD  GLU A 566    15643  13746  13017   2191   2991   1420       C  
ATOM   4234  OE1 GLU A 566     -75.791 -13.774 -21.975  1.00114.79           O  
ANISOU 4234  OE1 GLU A 566    16107  14037  13472   2106   3177   1330       O  
ATOM   4235  OE2 GLU A 566     -75.575 -13.152 -24.069  1.00114.20           O  
ANISOU 4235  OE2 GLU A 566    15620  14363  13406   2269   2841   1459       O  
ATOM   4236  N   SER A 567     -72.902 -11.608 -18.055  1.00 75.01           N  
ANISOU 4236  N   SER A 567    12736   7908   7855   1959   3415   1301       N  
ATOM   4237  CA  SER A 567     -72.980 -11.058 -16.705  1.00 72.78           C  
ANISOU 4237  CA  SER A 567    12850   7338   7465   1963   3641   1253       C  
ATOM   4238  C   SER A 567     -71.709 -10.300 -16.343  1.00 71.00           C  
ANISOU 4238  C   SER A 567    12968   6927   7081   1908   3488   1238       C  
ATOM   4239  O   SER A 567     -71.765  -9.275 -15.655  1.00 77.09           O  
ANISOU 4239  O   SER A 567    14004   7474   7812   1975   3644   1220       O  
ATOM   4240  CB  SER A 567     -73.242 -12.178 -15.698  1.00 72.43           C  
ANISOU 4240  CB  SER A 567    12967   7229   7325   1833   3768   1170       C  
ATOM   4241  OG  SER A 567     -73.289 -11.674 -14.374  1.00 75.34           O  
ANISOU 4241  OG  SER A 567    13745   7337   7542   1834   3986   1117       O  
ATOM   4242  N   LEU A 568     -70.552 -10.789 -16.793  1.00 61.78           N  
ANISOU 4242  N   LEU A 568    11794   5845   5835   1784   3188   1229       N  
ATOM   4243  CA  LEU A 568     -69.308 -10.071 -16.539  1.00 67.90           C  
ANISOU 4243  CA  LEU A 568    12840   6465   6492   1717   3022   1210       C  
ATOM   4244  C   LEU A 568     -69.256  -8.767 -17.324  1.00 71.14           C  
ANISOU 4244  C   LEU A 568    13149   6859   7022   1836   3019   1311       C  
ATOM   4245  O   LEU A 568     -68.830  -7.734 -16.796  1.00 62.98           O  
ANISOU 4245  O   LEU A 568    12390   5593   5946   1839   3060   1292       O  
ATOM   4246  CB  LEU A 568     -68.109 -10.954 -16.887  1.00 63.94           C  
ANISOU 4246  CB  LEU A 568    12304   6080   5910   1567   2710   1178       C  
ATOM   4247  CG  LEU A 568     -66.733 -10.283 -16.850  1.00 64.21           C  
ANISOU 4247  CG  LEU A 568    12522   6011   5865   1483   2498   1162       C  
ATOM   4248  CD1 LEU A 568     -66.443  -9.722 -15.468  1.00 60.53           C  
ANISOU 4248  CD1 LEU A 568    12499   5258   5242   1433   2575   1071       C  
ATOM   4249  CD2 LEU A 568     -65.644 -11.257 -17.274  1.00 65.31           C  
ANISOU 4249  CD2 LEU A 568    12558   6297   5959   1358   2206   1130       C  
ATOM   4250  N   ALA A 569     -69.691  -8.798 -18.587  1.00 72.93           N  
ANISOU 4250  N   ALA A 569    12993   7323   7393   1932   2969   1420       N  
ATOM   4251  CA  ALA A 569     -69.648  -7.605 -19.424  1.00 74.70           C  
ANISOU 4251  CA  ALA A 569    13113   7544   7724   2055   2959   1555       C  
ATOM   4252  C   ALA A 569     -70.594  -6.525 -18.918  1.00 82.73           C  
ANISOU 4252  C   ALA A 569    14242   8351   8840   2228   3239   1588       C  
ATOM   4253  O   ALA A 569     -70.309  -5.332 -19.077  1.00 86.15           O  
ANISOU 4253  O   ALA A 569    14785   8618   9328   2298   3262   1664       O  
ATOM   4254  CB  ALA A 569     -69.981  -7.966 -20.871  1.00 72.92           C  
ANISOU 4254  CB  ALA A 569    12460   7651   7595   2132   2838   1667       C  
ATOM   4255  N   LYS A 570     -71.712  -6.914 -18.302  1.00 86.03           N  
ANISOU 4255  N   LYS A 570    14632   8758   9296   2298   3468   1532       N  
ATOM   4256  CA  LYS A 570     -72.636  -5.917 -17.771  1.00 90.63           C  
ANISOU 4256  CA  LYS A 570    15313   9139   9983   2477   3761   1546       C  
ATOM   4257  C   LYS A 570     -72.104  -5.206 -16.532  1.00 87.37           C  
ANISOU 4257  C   LYS A 570    15376   8379   9443   2416   3871   1428       C  
ATOM   4258  O   LYS A 570     -72.770  -4.290 -16.039  1.00 92.11           O  
ANISOU 4258  O   LYS A 570    16102   8772  10122   2565   4123   1416       O  
ATOM   4259  CB  LYS A 570     -73.986  -6.565 -17.454  1.00 99.54           C  
ANISOU 4259  CB  LYS A 570    16251  10370  11201   2559   3996   1510       C  
ATOM   4260  CG  LYS A 570     -74.746  -7.033 -18.686  1.00109.10           C  
ANISOU 4260  CG  LYS A 570    16965  11909  12578   2659   3916   1616       C  
ATOM   4261  CD  LYS A 570     -76.215  -7.274 -18.379  1.00114.25           C  
ANISOU 4261  CD  LYS A 570    17404  12618  13388   2784   4195   1593       C  
ATOM   4262  CE  LYS A 570     -76.991  -7.608 -19.645  1.00118.37           C  
ANISOU 4262  CE  LYS A 570    17414  13475  14088   2896   4087   1692       C  
ATOM   4263  NZ  LYS A 570     -78.461  -7.640 -19.408  1.00121.94           N  
ANISOU 4263  NZ  LYS A 570    17613  13979  14741   3044   4360   1681       N  
ATOM   4264  N   SER A 571     -70.930  -5.586 -16.027  1.00 79.15           N  
ANISOU 4264  N   SER A 571    14595   7270   8210   2210   3682   1333       N  
ATOM   4265  CA  SER A 571     -70.367  -4.982 -14.828  1.00 77.22           C  
ANISOU 4265  CA  SER A 571    14807   6719   7812   2132   3744   1197       C  
ATOM   4266  C   SER A 571     -69.147  -4.115 -15.096  1.00 74.26           C  
ANISOU 4266  C   SER A 571    14581   6206   7430   2045   3538   1207       C  
ATOM   4267  O   SER A 571     -68.692  -3.421 -14.181  1.00 74.84           O  
ANISOU 4267  O   SER A 571    15023   6006   7405   1985   3582   1084       O  
ATOM   4268  CB  SER A 571     -69.981  -6.070 -13.817  1.00 73.84           C  
ANISOU 4268  CB  SER A 571    14612   6295   7148   1960   3691   1064       C  
ATOM   4269  OG  SER A 571     -68.852  -6.793 -14.271  1.00 72.25           O  
ANISOU 4269  OG  SER A 571    14340   6239   6872   1798   3359   1074       O  
ATOM   4270  N   ILE A 572     -68.604  -4.134 -16.314  1.00 73.28           N  
ANISOU 4270  N   ILE A 572    14181   6262   7402   2026   3323   1340       N  
ATOM   4271  CA  ILE A 572     -67.352  -3.433 -16.582  1.00 71.85           C  
ANISOU 4271  CA  ILE A 572    14116   5967   7217   1906   3125   1353       C  
ATOM   4272  C   ILE A 572     -67.578  -1.925 -16.629  1.00 74.43           C  
ANISOU 4272  C   ILE A 572    14568   6019   7691   2026   3287   1410       C  
ATOM   4273  O   ILE A 572     -66.909  -1.163 -15.921  1.00 74.88           O  
ANISOU 4273  O   ILE A 572    14951   5795   7705   1928   3280   1299       O  
ATOM   4274  CB  ILE A 572     -66.719  -3.954 -17.883  1.00 69.85           C  
ANISOU 4274  CB  ILE A 572    13527   6004   7010   1849   2878   1481       C  
ATOM   4275  CG1 ILE A 572     -66.533  -5.471 -17.804  1.00 65.39           C  
ANISOU 4275  CG1 ILE A 572    12848   5677   6321   1743   2733   1406       C  
ATOM   4276  CG2 ILE A 572     -65.391  -3.257 -18.148  1.00 65.30           C  
ANISOU 4276  CG2 ILE A 572    13051   5317   6443   1706   2695   1496       C  
ATOM   4277  CD1 ILE A 572     -66.059  -6.101 -19.094  1.00 61.27           C  
ANISOU 4277  CD1 ILE A 572    11977   5463   5839   1709   2521   1504       C  
ATOM   4278  N   SER A 573     -68.518  -1.474 -17.464  1.00 73.66           N  
ANISOU 4278  N   SER A 573    14217   5992   7778   2241   3424   1581       N  
ATOM   4279  CA  SER A 573     -68.762  -0.038 -17.607  1.00 80.67           C  
ANISOU 4279  CA  SER A 573    15207   6606   8837   2383   3579   1667       C  
ATOM   4280  C   SER A 573     -69.118   0.645 -16.291  1.00 84.13           C  
ANISOU 4280  C   SER A 573    16027   6689   9249   2420   3818   1485       C  
ATOM   4281  O   SER A 573     -68.514   1.690 -15.983  1.00 84.75           O  
ANISOU 4281  O   SER A 573    16373   6458   9372   2366   3829   1436       O  
ATOM   4282  CB  SER A 573     -69.844   0.200 -18.667  1.00 83.58           C  
ANISOU 4282  CB  SER A 573    15222   7140   9396   2642   3680   1888       C  
ATOM   4283  OG  SER A 573     -69.422  -0.251 -19.941  1.00 83.71           O  
ANISOU 4283  OG  SER A 573    14924   7466   9416   2606   3454   2055       O  
ATOM   4284  N   PRO A 574     -70.061   0.141 -15.478  1.00 85.38           N  
ANISOU 4284  N   PRO A 574    16238   6864   9340   2502   4026   1372       N  
ATOM   4285  CA  PRO A 574     -70.346   0.828 -14.206  1.00 88.83           C  
ANISOU 4285  CA  PRO A 574    17067   6962   9721   2535   4270   1181       C  
ATOM   4286  C   PRO A 574     -69.121   0.984 -13.325  1.00 88.07           C  
ANISOU 4286  C   PRO A 574    17370   6668   9425   2290   4115    986       C  
ATOM   4287  O   PRO A 574     -68.986   1.999 -12.631  1.00 92.34           O  
ANISOU 4287  O   PRO A 574    18239   6871   9974   2296   4239    854       O  
ATOM   4288  CB  PRO A 574     -71.407  -0.071 -13.554  1.00 90.56           C  
ANISOU 4288  CB  PRO A 574    17234   7320   9853   2610   4482   1103       C  
ATOM   4289  CG  PRO A 574     -72.046  -0.782 -14.684  1.00 87.84           C  
ANISOU 4289  CG  PRO A 574    16408   7320   9646   2712   4422   1293       C  
ATOM   4290  CD  PRO A 574     -70.946  -1.023 -15.670  1.00 83.62           C  
ANISOU 4290  CD  PRO A 574    15724   6951   9099   2567   4076   1405       C  
ATOM   4291  N   MET A 575     -68.214   0.007 -13.344  1.00 83.37           N  
ANISOU 4291  N   MET A 575    16747   6272   8657   2079   3836    955       N  
ATOM   4292  CA  MET A 575     -66.988   0.123 -12.563  1.00 82.21           C  
ANISOU 4292  CA  MET A 575    16938   5969   8328   1845   3640    777       C  
ATOM   4293  C   MET A 575     -66.147   1.302 -13.036  1.00 84.95           C  
ANISOU 4293  C   MET A 575    17346   6099   8833   1777   3534    811       C  
ATOM   4294  O   MET A 575     -65.626   2.073 -12.219  1.00 80.09           O  
ANISOU 4294  O   MET A 575    17084   5187   8161   1676   3539    632       O  
ATOM   4295  CB  MET A 575     -66.197  -1.183 -12.649  1.00 79.36           C  
ANISOU 4295  CB  MET A 575    16470   5885   7797   1665   3347    771       C  
ATOM   4296  CG  MET A 575     -65.027  -1.289 -11.687  1.00 85.63           C  
ANISOU 4296  CG  MET A 575    17603   6565   8368   1439   3129    576       C  
ATOM   4297  SD  MET A 575     -63.488  -0.612 -12.335  1.00 94.38           S  
ANISOU 4297  SD  MET A 575    18664   7604   9590   1243   2813    594       S  
ATOM   4298  CE  MET A 575     -63.341  -1.503 -13.883  1.00 90.14           C  
ANISOU 4298  CE  MET A 575    17605   7454   9189   1266   2650    836       C  
ATOM   4299  N   VAL A 576     -66.020   1.469 -14.354  1.00 76.73           N  
ANISOU 4299  N   VAL A 576    15969   5196   7987   1825   3444   1039       N  
ATOM   4300  CA  VAL A 576     -65.212   2.558 -14.889  1.00 79.96           C  
ANISOU 4300  CA  VAL A 576    16416   5405   8562   1748   3359   1108       C  
ATOM   4301  C   VAL A 576     -65.853   3.906 -14.582  1.00 82.98           C  
ANISOU 4301  C   VAL A 576    17009   5407   9112   1907   3634   1090       C  
ATOM   4302  O   VAL A 576     -65.165   4.858 -14.189  1.00 83.33           O  
ANISOU 4302  O   VAL A 576    17322   5129   9210   1786   3615    980       O  
ATOM   4303  CB  VAL A 576     -64.989   2.364 -16.400  1.00 81.87           C  
ANISOU 4303  CB  VAL A 576    16254   5912   8942   1776   3225   1378       C  
ATOM   4304  CG1 VAL A 576     -64.276   3.569 -16.993  1.00 77.71           C  
ANISOU 4304  CG1 VAL A 576    15767   5155   8605   1713   3194   1489       C  
ATOM   4305  CG2 VAL A 576     -64.192   1.097 -16.659  1.00 73.09           C  
ANISOU 4305  CG2 VAL A 576    14964   5132   7674   1602   2949   1357       C  
ATOM   4306  N   ILE A 577     -67.175   4.014 -14.746  1.00 82.05           N  
ANISOU 4306  N   ILE A 577    16766   5311   9099   2180   3892   1185       N  
ATOM   4307  CA  ILE A 577     -67.810   5.301 -14.475  1.00 95.17           C  
ANISOU 4307  CA  ILE A 577    18589   6628  10942   2352   4154   1164       C  
ATOM   4308  C   ILE A 577     -67.761   5.623 -12.985  1.00 93.50           C  
ANISOU 4308  C   ILE A 577    18775   6186  10566   2256   4263    840       C  
ATOM   4309  O   ILE A 577     -67.697   6.798 -12.601  1.00 92.86           O  
ANISOU 4309  O   ILE A 577    18857   5840  10586   2244   4351    738       O  
ATOM   4310  CB  ILE A 577     -69.251   5.340 -15.024  1.00 95.50           C  
ANISOU 4310  CB  ILE A 577    18350   6784  11152   2680   4389   1344       C  
ATOM   4311  CG1 ILE A 577     -70.214   4.562 -14.127  1.00 97.18           C  
ANISOU 4311  CG1 ILE A 577    18623   7074  11225   2784   4597   1195       C  
ATOM   4312  CG2 ILE A 577     -69.294   4.800 -16.446  1.00 93.47           C  
ANISOU 4312  CG2 ILE A 577    17675   6860  10979   2748   4229   1640       C  
ATOM   4313  CD1 ILE A 577     -71.670   4.750 -14.500  1.00 98.52           C  
ANISOU 4313  CD1 ILE A 577    18536   7300  11596   3113   4864   1331       C  
ATOM   4314  N   GLU A 578     -67.764   4.602 -12.120  1.00 89.41           N  
ANISOU 4314  N   GLU A 578    18426   5766   9781   2180   4251    675       N  
ATOM   4315  CA  GLU A 578     -67.583   4.863 -10.695  1.00 93.21           C  
ANISOU 4315  CA  GLU A 578    19299   6073  10044   2059   4312    371       C  
ATOM   4316  C   GLU A 578     -66.157   5.311 -10.399  1.00 96.55           C  
ANISOU 4316  C   GLU A 578    19948   6339  10398   1776   4036    227       C  
ATOM   4317  O   GLU A 578     -65.939   6.178  -9.544  1.00 96.08           O  
ANISOU 4317  O   GLU A 578    20160   6053  10294   1691   4079     17       O  
ATOM   4318  CB  GLU A 578     -67.940   3.627  -9.867  1.00 93.52           C  
ANISOU 4318  CB  GLU A 578    19459   6280   9793   2046   4363    257       C  
ATOM   4319  CG  GLU A 578     -69.417   3.244  -9.883  1.00 97.36           C  
ANISOU 4319  CG  GLU A 578    19759   6891  10341   2301   4684    339       C  
ATOM   4320  CD  GLU A 578     -70.327   4.316  -9.314  1.00108.19           C  
ANISOU 4320  CD  GLU A 578    21206   8088  11814   2450   4990    258       C  
ATOM   4321  OE1 GLU A 578     -69.860   5.144  -8.501  1.00112.84           O  
ANISOU 4321  OE1 GLU A 578    22093   8464  12318   2329   4977     67       O  
ATOM   4322  OE2 GLU A 578     -71.521   4.327  -9.683  1.00112.18           O  
ANISOU 4322  OE2 GLU A 578    21457   8670  12496   2691   5237    382       O  
ATOM   4323  N   ALA A 579     -65.173   4.736 -11.097  1.00 97.90           N  
ANISOU 4323  N   ALA A 579    19997   6630  10570   1623   3749    334       N  
ATOM   4324  CA  ALA A 579     -63.793   5.187 -10.936  1.00103.89           C  
ANISOU 4324  CA  ALA A 579    20917   7240  11315   1350   3484    213       C  
ATOM   4325  C   ALA A 579     -63.651   6.656 -11.323  1.00 90.21           C  
ANISOU 4325  C   ALA A 579    19161   5253   9860   1347   3555    249       C  
ATOM   4326  O   ALA A 579     -63.052   7.451 -10.587  1.00 92.94           O  
ANISOU 4326  O   ALA A 579    19765   5360  10187   1183   3501     29       O  
ATOM   4327  CB  ALA A 579     -62.852   4.313 -11.764  1.00 84.23           C  
ANISOU 4327  CB  ALA A 579    18128   5063   8811   1190   3161    358       C  
ATOM   4328  N   LYS A 580     -64.207   7.035 -12.479  1.00 89.80           N  
ANISOU 4328  N   LYS A 580    18801   5252  10069   1528   3669    528       N  
ATOM   4329  CA  LYS A 580     -64.199   8.442 -12.874  1.00103.96           C  
ANISOU 4329  CA  LYS A 580    20569   6791  12139   1557   3763    592       C  
ATOM   4330  C   LYS A 580     -64.929   9.303 -11.850  1.00 96.42           C  
ANISOU 4330  C   LYS A 580    19859   5592  11185   1657   4003    380       C  
ATOM   4331  O   LYS A 580     -64.516  10.435 -11.570  1.00 99.58           O  
ANISOU 4331  O   LYS A 580    20416   5700  11718   1559   4012    266       O  
ATOM   4332  CB  LYS A 580     -64.825   8.603 -14.260  1.00100.50           C  
ANISOU 4332  CB  LYS A 580    19756   6492  11936   1775   3846    945       C  
ATOM   4333  CG  LYS A 580     -64.076   7.872 -15.364  1.00 96.02           C  
ANISOU 4333  CG  LYS A 580    18930   6181  11372   1673   3618   1170       C  
ATOM   4334  CD  LYS A 580     -64.851   7.886 -16.673  1.00 96.83           C  
ANISOU 4334  CD  LYS A 580    18662   6490  11639   1916   3697   1509       C  
ATOM   4335  CE  LYS A 580     -64.100   7.134 -17.764  1.00 96.51           C  
ANISOU 4335  CE  LYS A 580    18363   6742  11566   1808   3477   1722       C  
ATOM   4336  NZ  LYS A 580     -64.895   7.025 -19.018  1.00 96.29           N  
ANISOU 4336  NZ  LYS A 580    17974   6973  11639   2048   3530   2037       N  
ATOM   4337  N   ALA A 581     -66.011   8.778 -11.270  1.00105.45           N  
ANISOU 4337  N   ALA A 581    21033   6846  12186   1845   4207    321       N  
ATOM   4338  CA  ALA A 581     -66.675   9.487 -10.183  1.00 99.92           C  
ANISOU 4338  CA  ALA A 581    20579   5943  11442   1923   4441    100       C  
ATOM   4339  C   ALA A 581     -65.747   9.674  -8.989  1.00101.70           C  
ANISOU 4339  C   ALA A 581    21181   6014  11444   1654   4295   -225       C  
ATOM   4340  O   ALA A 581     -65.874  10.662  -8.256  1.00112.10           O  
ANISOU 4340  O   ALA A 581    22715   7081  12798   1644   4414   -415       O  
ATOM   4341  CB  ALA A 581     -67.943   8.743  -9.764  1.00 99.39           C  
ANISOU 4341  CB  ALA A 581    20460   6059  11246   2143   4686    103       C  
ATOM   4342  N   VAL A 582     -64.809   8.748  -8.777  1.00 99.30           N  
ANISOU 4342  N   VAL A 582    20957   5859  10912   1440   4024   -298       N  
ATOM   4343  CA  VAL A 582     -63.824   8.942  -7.717  1.00101.20           C  
ANISOU 4343  CA  VAL A 582    21531   5973  10947   1175   3828   -597       C  
ATOM   4344  C   VAL A 582     -62.840  10.039  -8.102  1.00116.81           C  
ANISOU 4344  C   VAL A 582    23520   7691  13172    990   3678   -629       C  
ATOM   4345  O   VAL A 582     -62.450  10.860  -7.262  1.00106.68           O  
ANISOU 4345  O   VAL A 582    22493   6178  11864    856   3653   -882       O  
ATOM   4346  CB  VAL A 582     -63.098   7.626  -7.385  1.00 98.37           C  
ANISOU 4346  CB  VAL A 582    21244   5851  10281   1011   3558   -657       C  
ATOM   4347  CG1 VAL A 582     -62.074   7.855  -6.283  1.00100.74           C  
ANISOU 4347  CG1 VAL A 582    21872   6041  10362    745   3323   -963       C  
ATOM   4348  CG2 VAL A 582     -64.090   6.560  -6.963  1.00105.36           C  
ANISOU 4348  CG2 VAL A 582    22130   6969  10934   1182   3728   -622       C  
ATOM   4349  N   VAL A 583     -62.423  10.085  -9.372  1.00109.97           N  
ANISOU 4349  N   VAL A 583    22372   6858  12554    973   3581   -371       N  
ATOM   4350  CA  VAL A 583     -61.527  11.166  -9.775  1.00111.54           C  
ANISOU 4350  CA  VAL A 583    22567   6797  13017    790   3473   -375       C  
ATOM   4351  C   VAL A 583     -62.228  12.516  -9.712  1.00115.19           C  
ANISOU 4351  C   VAL A 583    23078   6966  13723    937   3731   -388       C  
ATOM   4352  O   VAL A 583     -61.562  13.553  -9.606  1.00115.13           O  
ANISOU 4352  O   VAL A 583    23177   6670  13898    771   3674   -496       O  
ATOM   4353  CB  VAL A 583     -60.936  10.927 -11.180  1.00110.91           C  
ANISOU 4353  CB  VAL A 583    22167   6832  13140    737   3336    -65       C  
ATOM   4354  CG1 VAL A 583     -60.851   9.449 -11.474  1.00107.05           C  
ANISOU 4354  CG1 VAL A 583    21541   6693  12440    749   3197     40       C  
ATOM   4355  CG2 VAL A 583     -61.729  11.663 -12.257  1.00113.33           C  
ANISOU 4355  CG2 VAL A 583    22222   7085  13753    974   3553    238       C  
ATOM   4356  N   THR A 584     -63.563  12.535  -9.759  1.00116.32           N  
ANISOU 4356  N   THR A 584    23140   7165  13890   1244   4013   -286       N  
ATOM   4357  CA  THR A 584     -64.284  13.795  -9.619  1.00117.04           C  
ANISOU 4357  CA  THR A 584    23289   6971  14209   1404   4261   -313       C  
ATOM   4358  C   THR A 584     -64.283  14.267  -8.170  1.00126.22           C  
ANISOU 4358  C   THR A 584    24818   7940  15201   1317   4322   -690       C  
ATOM   4359  O   THR A 584     -63.980  15.432  -7.886  1.00128.23           O  
ANISOU 4359  O   THR A 584    25220   7870  15633   1234   4346   -832       O  
ATOM   4360  CB  THR A 584     -65.715  13.644 -10.136  1.00114.25           C  
ANISOU 4360  CB  THR A 584    22709   6753  13948   1764   4531    -86       C  
ATOM   4361  OG1 THR A 584     -65.691  13.041 -11.436  1.00110.64           O  
ANISOU 4361  OG1 THR A 584    21912   6536  13591   1836   4439    249       O  
ATOM   4362  CG2 THR A 584     -66.389  15.003 -10.232  1.00119.01           C  
ANISOU 4362  CG2 THR A 584    23320   7051  14848   1943   4759    -57       C  
ATOM   4363  N   SER A 585     -64.623  13.373  -7.237  1.00132.57           N  
ANISOU 4363  N   SER A 585    25774   8941  15655   1331   4347   -851       N  
ATOM   4364  CA  SER A 585     -64.636  13.663  -5.804  1.00141.05           C  
ANISOU 4364  CA  SER A 585    27202   9896  16496   1249   4394  -1201       C  
ATOM   4365  C   SER A 585     -63.734  12.652  -5.104  1.00130.86           C  
ANISOU 4365  C   SER A 585    26081   8804  14834   1007   4107  -1367       C  
ATOM   4366  O   SER A 585     -64.210  11.625  -4.596  1.00143.16           O  
ANISOU 4366  O   SER A 585    27687  10612  16095   1077   4153  -1375       O  
ATOM   4367  CB  SER A 585     -66.053  13.617  -5.235  1.00119.08           C  
ANISOU 4367  CB  SER A 585    24456   7159  13630   1524   4741  -1223       C  
ATOM   4368  OG  SER A 585     -66.881  14.597  -5.835  1.00125.25           O  
ANISOU 4368  OG  SER A 585    25083   7745  14763   1758   4988  -1082       O  
ATOM   4369  N   PRO A 586     -62.422  12.906  -5.059  1.00139.46           N  
ANISOU 4369  N   PRO A 586    27255   9789  15942    717   3802  -1496       N  
ATOM   4370  CA  PRO A 586     -61.504  11.944  -4.428  1.00137.27           C  
ANISOU 4370  CA  PRO A 586    27120   9711  15325    491   3488  -1647       C  
ATOM   4371  C   PRO A 586     -61.677  11.819  -2.924  1.00139.07           C  
ANISOU 4371  C   PRO A 586    27689   9967  15183    454   3503  -1945       C  
ATOM   4372  O   PRO A 586     -61.164  10.854  -2.343  1.00143.11           O  
ANISOU 4372  O   PRO A 586    28314  10699  15362    330   3276  -2027       O  
ATOM   4373  CB  PRO A 586     -60.114  12.500  -4.775  1.00140.04           C  
ANISOU 4373  CB  PRO A 586    27451   9893  15863    196   3186  -1723       C  
ATOM   4374  CG  PRO A 586     -60.341  13.442  -5.920  1.00140.96           C  
ANISOU 4374  CG  PRO A 586    27337   9796  16423    290   3346  -1496       C  
ATOM   4375  CD  PRO A 586     -61.701  14.021  -5.693  1.00142.93           C  
ANISOU 4375  CD  PRO A 586    27626   9940  16742    583   3719  -1475       C  
ATOM   4376  N   GLN A 587     -62.377  12.748  -2.277  1.00136.72           N  
ANISOU 4376  N   GLN A 587    27557   9460  14929    562   3758  -2101       N  
ATOM   4377  CA  GLN A 587     -62.522  12.715  -0.829  1.00134.00           C  
ANISOU 4377  CA  GLN A 587    27546   9134  14233    521   3781  -2390       C  
ATOM   4378  C   GLN A 587     -63.774  11.982  -0.369  1.00127.47           C  
ANISOU 4378  C   GLN A 587    26744   8509  13180    757   4073  -2304       C  
ATOM   4379  O   GLN A 587     -63.832  11.551   0.788  1.00129.75           O  
ANISOU 4379  O   GLN A 587    27287   8911  13102    711   4053  -2478       O  
ATOM   4380  CB  GLN A 587     -62.536  14.142  -0.271  1.00140.10           C  
ANISOU 4380  CB  GLN A 587    28511   9556  15165    489   3892  -2649       C  
ATOM   4381  CG  GLN A 587     -61.457  15.046  -0.854  1.00140.60           C  
ANISOU 4381  CG  GLN A 587    28508   9359  15553    274   3673  -2705       C  
ATOM   4382  CD  GLN A 587     -60.055  14.503  -0.642  1.00137.14           C  
ANISOU 4382  CD  GLN A 587    28120   9045  14943    -39   3235  -2826       C  
ATOM   4383  OE1 GLN A 587     -59.537  13.748  -1.466  1.00131.71           O  
ANISOU 4383  OE1 GLN A 587    27217   8531  14296   -105   3050  -2617       O  
ATOM   4384  NE2 GLN A 587     -59.433  14.890   0.466  1.00140.34           N  
ANISOU 4384  NE2 GLN A 587    28800   9365  15158   -230   3059  -3174       N  
ATOM   4385  N   ASN A 588     -64.769  11.829  -1.240  1.00121.97           N  
ANISOU 4385  N   ASN A 588    25780   7865  12699   1003   4337  -2035       N  
ATOM   4386  CA  ASN A 588     -66.009  11.162  -0.865  1.00121.48           C  
ANISOU 4386  CA  ASN A 588    25697   7984  12477   1222   4635  -1947       C  
ATOM   4387  C   ASN A 588     -65.746   9.684  -0.598  1.00122.64           C  
ANISOU 4387  C   ASN A 588    25862   8456  12279   1142   4459  -1875       C  
ATOM   4388  O   ASN A 588     -65.316   8.949  -1.494  1.00114.06           O  
ANISOU 4388  O   ASN A 588    24560   7524  11255   1105   4278  -1682       O  
ATOM   4389  CB  ASN A 588     -67.050  11.333  -1.970  1.00119.89           C  
ANISOU 4389  CB  ASN A 588    25156   7776  12622   1494   4911  -1671       C  
ATOM   4390  CG  ASN A 588     -68.454  10.966  -1.518  1.00120.74           C  
ANISOU 4390  CG  ASN A 588    25231   7998  12647   1731   5274  -1621       C  
ATOM   4391  OD1 ASN A 588     -68.639  10.269  -0.521  1.00121.35           O  
ANISOU 4391  OD1 ASN A 588    25500   8224  12384   1685   5307  -1727       O  
ATOM   4392  ND2 ASN A 588     -69.452  11.436  -2.256  1.00121.04           N  
ANISOU 4392  ND2 ASN A 588    25011   7970  13009   1984   5543  -1448       N  
ATOM   4393  N   LYS A 589     -66.007   9.248   0.638  1.00124.93           N  
ANISOU 4393  N   LYS A 589    26412   8845  12210   1118   4515  -2024       N  
ATOM   4394  CA  LYS A 589     -65.835   7.839   0.978  1.00117.57           C  
ANISOU 4394  CA  LYS A 589    25513   8208  10951   1055   4367  -1939       C  
ATOM   4395  C   LYS A 589     -66.925   6.976   0.353  1.00114.48           C  
ANISOU 4395  C   LYS A 589    24847   8003  10645   1264   4620  -1668       C  
ATOM   4396  O   LYS A 589     -66.685   5.803   0.040  1.00121.35           O  
ANISOU 4396  O   LYS A 589    25610   9099  11396   1224   4465  -1518       O  
ATOM   4397  CB  LYS A 589     -65.829   7.661   2.497  1.00121.15           C  
ANISOU 4397  CB  LYS A 589    26324   8705  11004    975   4362  -2153       C  
ATOM   4398  CG  LYS A 589     -64.973   8.669   3.251  1.00125.34           C  
ANISOU 4398  CG  LYS A 589    27134   9033  11456    800   4175  -2467       C  
ATOM   4399  CD  LYS A 589     -63.497   8.521   2.919  1.00124.33           C  
ANISOU 4399  CD  LYS A 589    26995   8929  11315    558   3708  -2516       C  
ATOM   4400  CE  LYS A 589     -62.658   9.520   3.703  1.00128.28           C  
ANISOU 4400  CE  LYS A 589    27755   9233  11754    370   3514  -2848       C  
ATOM   4401  NZ  LYS A 589     -61.206   9.405   3.393  1.00127.11           N  
ANISOU 4401  NZ  LYS A 589    27565   9107  11622    120   3052  -2909       N  
ATOM   4402  N   ASP A 590     -68.120   7.539   0.161  1.00121.09           N  
ANISOU 4402  N   ASP A 590    25556   8748  11704   1488   4999  -1609       N  
ATOM   4403  CA  ASP A 590     -69.226   6.781  -0.417  1.00119.95           C  
ANISOU 4403  CA  ASP A 590    25122   8780  11673   1690   5248  -1368       C  
ATOM   4404  C   ASP A 590     -68.927   6.375  -1.857  1.00114.14           C  
ANISOU 4404  C   ASP A 590    24050   8141  11179   1722   5098  -1136       C  
ATOM   4405  O   ASP A 590     -69.129   5.216  -2.241  1.00105.83           O  
ANISOU 4405  O   ASP A 590    22826   7320  10063   1748   5068   -970       O  
ATOM   4406  CB  ASP A 590     -70.511   7.607  -0.337  1.00125.27           C  
ANISOU 4406  CB  ASP A 590    25708   9318  12570   1925   5660  -1373       C  
ATOM   4407  CG  ASP A 590     -71.679   6.946  -1.040  1.00127.84           C  
ANISOU 4407  CG  ASP A 590    25678   9817  13079   2141   5909  -1128       C  
ATOM   4408  OD1 ASP A 590     -71.772   5.700  -1.010  1.00127.04           O  
ANISOU 4408  OD1 ASP A 590    25507   9954  12810   2101   5861  -1016       O  
ATOM   4409  OD2 ASP A 590     -72.507   7.677  -1.623  1.00130.90           O  
ANISOU 4409  OD2 ASP A 590    25845  10099  13791   2353   6145  -1048       O  
ATOM   4410  N   ILE A 591     -68.448   7.321  -2.669  1.00116.53           N  
ANISOU 4410  N   ILE A 591    24249   8260  11768   1718   5004  -1118       N  
ATOM   4411  CA  ILE A 591     -68.081   7.007  -4.048  1.00113.73           C  
ANISOU 4411  CA  ILE A 591    23582   7987  11642   1738   4845   -894       C  
ATOM   4412  C   ILE A 591     -66.975   5.958  -4.076  1.00112.41           C  
ANISOU 4412  C   ILE A 591    23471   7995  11245   1525   4486   -896       C  
ATOM   4413  O   ILE A 591     -66.952   5.076  -4.946  1.00109.68           O  
ANISOU 4413  O   ILE A 591    22881   7834  10958   1564   4402   -704       O  
ATOM   4414  CB  ILE A 591     -67.672   8.290  -4.796  1.00112.79           C  
ANISOU 4414  CB  ILE A 591    23378   7614  11862   1740   4797   -874       C  
ATOM   4415  CG1 ILE A 591     -68.808   9.316  -4.760  1.00114.27           C  
ANISOU 4415  CG1 ILE A 591    23507   7623  12288   1975   5150   -866       C  
ATOM   4416  CG2 ILE A 591     -67.303   7.982  -6.235  1.00108.35           C  
ANISOU 4416  CG2 ILE A 591    22486   7148  11534   1761   4638   -615       C  
ATOM   4417  CD1 ILE A 591     -70.035   8.902  -5.547  1.00110.72           C  
ANISOU 4417  CD1 ILE A 591    22707   7332  12028   2252   5392   -615       C  
ATOM   4418  N   GLN A 592     -66.047   6.030  -3.117  1.00118.03           N  
ANISOU 4418  N   GLN A 592    24499   8653  11695   1305   4259  -1117       N  
ATOM   4419  CA  GLN A 592     -65.020   5.000  -2.998  1.00117.07           C  
ANISOU 4419  CA  GLN A 592    24444   8706  11332   1113   3906  -1131       C  
ATOM   4420  C   GLN A 592     -65.641   3.634  -2.735  1.00114.16           C  
ANISOU 4420  C   GLN A 592    24036   8600  10742   1190   3989  -1017       C  
ATOM   4421  O   GLN A 592     -65.216   2.629  -3.318  1.00115.91           O  
ANISOU 4421  O   GLN A 592    24113   8998  10930   1149   3796   -894       O  
ATOM   4422  CB  GLN A 592     -64.035   5.363  -1.887  1.00124.73           C  
ANISOU 4422  CB  GLN A 592    25757   9584  12050    886   3656  -1398       C  
ATOM   4423  CG  GLN A 592     -63.209   6.608  -2.159  1.00130.97           C  
ANISOU 4423  CG  GLN A 592    26577  10117  13067    753   3513  -1529       C  
ATOM   4424  CD  GLN A 592     -62.334   6.993  -0.982  1.00138.44           C  
ANISOU 4424  CD  GLN A 592    27854  10979  13766    536   3279  -1821       C  
ATOM   4425  OE1 GLN A 592     -62.417   6.395   0.092  1.00141.15           O  
ANISOU 4425  OE1 GLN A 592    28421  11456  13755    507   3243  -1919       O  
ATOM   4426  NE2 GLN A 592     -61.486   7.997  -1.178  1.00142.40           N  
ANISOU 4426  NE2 GLN A 592    28379  11262  14467    378   3114  -1956       N  
ATOM   4427  N   ARG A 593     -66.649   3.576  -1.859  1.00111.14           N  
ANISOU 4427  N   ARG A 593    23770   8234  10224   1296   4280  -1054       N  
ATOM   4428  CA  ARG A 593     -67.326   2.309  -1.600  1.00105.29           C  
ANISOU 4428  CA  ARG A 593    22967   7720   9317   1359   4392   -928       C  
ATOM   4429  C   ARG A 593     -68.012   1.783  -2.854  1.00101.06           C  
ANISOU 4429  C   ARG A 593    22038   7311   9049   1527   4530   -695       C  
ATOM   4430  O   ARG A 593     -67.932   0.585  -3.160  1.00 99.76           O  
ANISOU 4430  O   ARG A 593    21750   7351   8803   1506   4426   -575       O  
ATOM   4431  CB  ARG A 593     -68.338   2.470  -0.466  1.00105.51           C  
ANISOU 4431  CB  ARG A 593    23167   7715   9207   1440   4712  -1006       C  
ATOM   4432  CG  ARG A 593     -67.718   2.649   0.906  1.00107.26           C  
ANISOU 4432  CG  ARG A 593    23789   7879   9086   1278   4564  -1222       C  
ATOM   4433  CD  ARG A 593     -68.778   2.565   1.993  1.00115.49           C  
ANISOU 4433  CD  ARG A 593    24979   8926   9974   1364   4894  -1268       C  
ATOM   4434  NE  ARG A 593     -69.735   3.666   1.916  1.00117.98           N  
ANISOU 4434  NE  ARG A 593    25230   9071  10528   1534   5253  -1323       N  
ATOM   4435  CZ  ARG A 593     -69.672   4.763   2.663  1.00122.12           C  
ANISOU 4435  CZ  ARG A 593    26002   9397  11000   1516   5326  -1549       C  
ATOM   4436  NH1 ARG A 593     -68.696   4.907   3.549  1.00119.44           N  
ANISOU 4436  NH1 ARG A 593    25992   9021  10370   1329   5060  -1746       N  
ATOM   4437  NH2 ARG A 593     -70.585   5.716   2.528  1.00124.72           N  
ANISOU 4437  NH2 ARG A 593    26243   9570  11577   1691   5657  -1585       N  
ATOM   4438  N   LYS A 594     -68.693   2.664  -3.593  1.00100.43           N  
ANISOU 4438  N   LYS A 594    21748   7115   9298   1702   4754   -627       N  
ATOM   4439  CA  LYS A 594     -69.336   2.253  -4.839  1.00 97.13           C  
ANISOU 4439  CA  LYS A 594    20935   6821   9151   1877   4862   -403       C  
ATOM   4440  C   LYS A 594     -68.320   1.661  -5.809  1.00 93.46           C  
ANISOU 4440  C   LYS A 594    20333   6449   8727   1778   4530   -310       C  
ATOM   4441  O   LYS A 594     -68.538   0.582  -6.376  1.00 94.61           O  
ANISOU 4441  O   LYS A 594    20270   6799   8879   1825   4507   -176       O  
ATOM   4442  CB  LYS A 594     -70.054   3.443  -5.478  1.00101.09           C  
ANISOU 4442  CB  LYS A 594    21245   7160  10005   2075   5089   -338       C  
ATOM   4443  CG  LYS A 594     -71.142   4.062  -4.619  1.00106.72           C  
ANISOU 4443  CG  LYS A 594    22050   7771  10727   2203   5439   -427       C  
ATOM   4444  CD  LYS A 594     -71.687   5.329  -5.263  1.00108.66           C  
ANISOU 4444  CD  LYS A 594    22125   7831  11332   2394   5612   -370       C  
ATOM   4445  CE  LYS A 594     -72.737   5.993  -4.385  1.00116.02           C  
ANISOU 4445  CE  LYS A 594    23153   8643  12285   2526   5957   -481       C  
ATOM   4446  NZ  LYS A 594     -73.154   7.321  -4.919  1.00120.47           N  
ANISOU 4446  NZ  LYS A 594    23594   8987  13192   2704   6097   -447       N  
ATOM   4447  N   PHE A 595     -67.196   2.356  -6.005  1.00 94.32           N  
ANISOU 4447  N   PHE A 595    20547   6407   8882   1631   4270   -385       N  
ATOM   4448  CA  PHE A 595     -66.173   1.863  -6.922  1.00 93.18           C  
ANISOU 4448  CA  PHE A 595    20262   6334   8808   1520   3946   -291       C  
ATOM   4449  C   PHE A 595     -65.614   0.521  -6.464  1.00 93.09           C  
ANISOU 4449  C   PHE A 595    20319   6557   8496   1375   3710   -318       C  
ATOM   4450  O   PHE A 595     -65.432  -0.393  -7.278  1.00 91.34           O  
ANISOU 4450  O   PHE A 595    19749   6610   8346   1352   3537   -133       O  
ATOM   4451  CB  PHE A 595     -65.050   2.890  -7.060  1.00 95.61           C  
ANISOU 4451  CB  PHE A 595    20669   6437   9222   1350   3716   -379       C  
ATOM   4452  CG  PHE A 595     -63.753   2.302  -7.535  1.00 95.60           C  
ANISOU 4452  CG  PHE A 595    20569   6564   9192   1142   3314   -339       C  
ATOM   4453  CD1 PHE A 595     -63.614   1.863  -8.841  1.00 91.78           C  
ANISOU 4453  CD1 PHE A 595    19635   6317   8922   1164   3191    -80       C  
ATOM   4454  CD2 PHE A 595     -62.675   2.183  -6.675  1.00 98.23           C  
ANISOU 4454  CD2 PHE A 595    21192   6852   9280    916   3037   -550       C  
ATOM   4455  CE1 PHE A 595     -62.423   1.314  -9.279  1.00 89.72           C  
ANISOU 4455  CE1 PHE A 595    19212   6234   8644    969   2826    -38       C  
ATOM   4456  CE2 PHE A 595     -61.481   1.637  -7.108  1.00 96.46           C  
ANISOU 4456  CE2 PHE A 595    20788   6808   9055    725   2650   -499       C  
ATOM   4457  CZ  PHE A 595     -61.355   1.202  -8.411  1.00 91.77           C  
ANISOU 4457  CZ  PHE A 595    19740   6439   8689    753   2558   -245       C  
ATOM   4458  N   CYS A 596     -65.332   0.384  -5.165  1.00 91.88           N  
ANISOU 4458  N   CYS A 596    20539   6362   8011   1261   3665   -514       N  
ATOM   4459  CA  CYS A 596     -64.798  -0.876  -4.658  1.00 89.31           C  
ANISOU 4459  CA  CYS A 596    20320   6232   7382   1141   3440   -531       C  
ATOM   4460  C   CYS A 596     -65.774  -2.023  -4.891  1.00 87.56           C  
ANISOU 4460  C   CYS A 596    19884   6238   7146   1270   3634   -363       C  
ATOM   4461  O   CYS A 596     -65.371  -3.116  -5.310  1.00 86.76           O  
ANISOU 4461  O   CYS A 596    19564   6377   7024   1199   3405   -232       O  
ATOM   4462  CB  CYS A 596     -64.463  -0.745  -3.172  1.00 93.08           C  
ANISOU 4462  CB  CYS A 596    21164   6667   7534   1008   3352   -704       C  
ATOM   4463  SG  CYS A 596     -63.083   0.370  -2.806  1.00 97.38           S  
ANISOU 4463  SG  CYS A 596    21938   7010   8053    794   3023   -930       S  
ATOM   4464  N   SER A 597     -67.066  -1.790  -4.641  1.00 88.80           N  
ANISOU 4464  N   SER A 597    19989   6372   7380   1430   4015   -322       N  
ATOM   4465  CA  SER A 597     -68.061  -2.831  -4.881  1.00 87.16           C  
ANISOU 4465  CA  SER A 597    19540   6369   7207   1537   4216   -169       C  
ATOM   4466  C   SER A 597     -68.155  -3.179  -6.362  1.00 87.45           C  
ANISOU 4466  C   SER A 597    19097   6584   7546   1606   4133     29       C  
ATOM   4467  O   SER A 597     -68.335  -4.349  -6.722  1.00 87.01           O  
ANISOU 4467  O   SER A 597    18802   6768   7491   1586   4068    157       O  
ATOM   4468  CB  SER A 597     -69.422  -2.391  -4.345  1.00 90.07           C  
ANISOU 4468  CB  SER A 597    19881   6675   7666   1679   4618   -160       C  
ATOM   4469  OG  SER A 597     -69.352  -2.092  -2.961  1.00 94.82           O  
ANISOU 4469  OG  SER A 597    20834   7166   8026   1586   4646   -300       O  
ATOM   4470  N   SER A 598     -68.031  -2.177  -7.238  1.00 81.69           N  
ANISOU 4470  N   SER A 598    18182   5759   7099   1670   4104     81       N  
ATOM   4471  CA  SER A 598     -68.103  -2.437  -8.675  1.00 86.53           C  
ANISOU 4471  CA  SER A 598    18301   6577   7999   1724   3987    300       C  
ATOM   4472  C   SER A 598     -66.917  -3.273  -9.148  1.00 76.21           C  
ANISOU 4472  C   SER A 598    16863   5465   6630   1539   3579    356       C  
ATOM   4473  O   SER A 598     -67.082  -4.237  -9.910  1.00 88.67           O  
ANISOU 4473  O   SER A 598    18102   7301   8288   1548   3494    497       O  
ATOM   4474  CB  SER A 598     -68.171  -1.115  -9.440  1.00 84.37           C  
ANISOU 4474  CB  SER A 598    17913   6135   8010   1834   4048    360       C  
ATOM   4475  OG  SER A 598     -69.319  -0.368  -9.078  1.00 82.48           O  
ANISOU 4475  OG  SER A 598    17753   5716   7867   2038   4432    319       O  
ATOM   4476  N   ALA A 599     -65.708  -2.918  -8.703  1.00 76.79           N  
ANISOU 4476  N   ALA A 599    17190   5415   6571   1370   3323    230       N  
ATOM   4477  CA  ALA A 599     -64.528  -3.697  -9.065  1.00 79.67           C  
ANISOU 4477  CA  ALA A 599    17434   5956   6882   1201   2937    265       C  
ATOM   4478  C   ALA A 599     -64.622  -5.122  -8.528  1.00 75.41           C  
ANISOU 4478  C   ALA A 599    16934   5596   6122   1160   2878    272       C  
ATOM   4479  O   ALA A 599     -64.290  -6.085  -9.234  1.00 71.20           O  
ANISOU 4479  O   ALA A 599    16113   5288   5650   1122   2687    384       O  
ATOM   4480  CB  ALA A 599     -63.268  -3.001  -8.551  1.00 76.03           C  
ANISOU 4480  CB  ALA A 599    17247   5318   6324   1025   2686    105       C  
ATOM   4481  N   ASP A 600     -65.082  -5.277  -7.281  1.00 75.78           N  
ANISOU 4481  N   ASP A 600    17347   5536   5908   1171   3054    156       N  
ATOM   4482  CA  ASP A 600     -65.331  -6.616  -6.756  1.00 84.23           C  
ANISOU 4482  CA  ASP A 600    18471   6751   6780   1148   3057    195       C  
ATOM   4483  C   ASP A 600     -66.338  -7.373  -7.614  1.00 79.50           C  
ANISOU 4483  C   ASP A 600    17468   6345   6391   1257   3235    365       C  
ATOM   4484  O   ASP A 600     -66.213  -8.593  -7.788  1.00 71.83           O  
ANISOU 4484  O   ASP A 600    16360   5544   5386   1207   3109    445       O  
ATOM   4485  CB  ASP A 600     -65.817  -6.534  -5.307  1.00 87.46           C  
ANISOU 4485  CB  ASP A 600    19349   7010   6872   1160   3289     60       C  
ATOM   4486  CG  ASP A 600     -64.740  -6.043  -4.353  1.00 87.65           C  
ANISOU 4486  CG  ASP A 600    19798   6886   6621   1028   3050   -126       C  
ATOM   4487  OD1 ASP A 600     -63.542  -6.287  -4.626  1.00 87.12           O  
ANISOU 4487  OD1 ASP A 600    19665   6888   6550    900   2655   -127       O  
ATOM   4488  OD2 ASP A 600     -65.088  -5.422  -3.325  1.00 91.54           O  
ANISOU 4488  OD2 ASP A 600    20551   7222   7010   1028   3194   -234       O  
ATOM   4489  N   LYS A 601     -67.331  -6.672  -8.169  1.00 76.55           N  
ANISOU 4489  N   LYS A 601    16894   5943   6249   1408   3513    416       N  
ATOM   4490  CA  LYS A 601     -68.279  -7.329  -9.062  1.00 77.51           C  
ANISOU 4490  CA  LYS A 601    16594   6266   6589   1509   3648    564       C  
ATOM   4491  C   LYS A 601     -67.584  -7.819 -10.327  1.00 76.47           C  
ANISOU 4491  C   LYS A 601    16086   6344   6624   1455   3335    676       C  
ATOM   4492  O   LYS A 601     -67.883  -8.912 -10.829  1.00 75.16           O  
ANISOU 4492  O   LYS A 601    15656   6380   6521   1446   3298    758       O  
ATOM   4493  CB  LYS A 601     -69.426  -6.379  -9.410  1.00 83.79           C  
ANISOU 4493  CB  LYS A 601    17241   6990   7604   1700   3977    597       C  
ATOM   4494  CG  LYS A 601     -70.717  -7.088  -9.776  1.00 90.22           C  
ANISOU 4494  CG  LYS A 601    17735   7975   8569   1809   4222    694       C  
ATOM   4495  CD  LYS A 601     -71.334  -7.754  -8.557  1.00 98.34           C  
ANISOU 4495  CD  LYS A 601    19028   8953   9383   1779   4479    623       C  
ATOM   4496  CE  LYS A 601     -72.047  -9.044  -8.928  1.00103.88           C  
ANISOU 4496  CE  LYS A 601    19418   9871  10180   1761   4547    722       C  
ATOM   4497  NZ  LYS A 601     -73.066  -8.845  -9.995  1.00106.20           N  
ANISOU 4497  NZ  LYS A 601    19236  10309  10805   1912   4684    818       N  
ATOM   4498  N   VAL A 602     -66.646  -7.025 -10.853  1.00 74.57           N  
ANISOU 4498  N   VAL A 602    15820   6054   6458   1410   3118    672       N  
ATOM   4499  CA  VAL A 602     -65.845  -7.479 -11.989  1.00 70.12           C  
ANISOU 4499  CA  VAL A 602    14934   5692   6018   1345   2822    763       C  
ATOM   4500  C   VAL A 602     -65.103  -8.765 -11.637  1.00 68.26           C  
ANISOU 4500  C   VAL A 602    14750   5567   5618   1213   2581    731       C  
ATOM   4501  O   VAL A 602     -65.173  -9.767 -12.366  1.00 64.82           O  
ANISOU 4501  O   VAL A 602    14018   5342   5268   1210   2492    808       O  
ATOM   4502  CB  VAL A 602     -64.873  -6.374 -12.439  1.00 70.94           C  
ANISOU 4502  CB  VAL A 602    15053   5692   6208   1290   2652    756       C  
ATOM   4503  CG1 VAL A 602     -63.909  -6.914 -13.485  1.00 69.27           C  
ANISOU 4503  CG1 VAL A 602    14542   5693   6083   1202   2349    832       C  
ATOM   4504  CG2 VAL A 602     -65.643  -5.174 -12.978  1.00 69.32           C  
ANISOU 4504  CG2 VAL A 602    14751   5382   6206   1444   2884    830       C  
ATOM   4505  N   VAL A 603     -64.382  -8.756 -10.509  1.00 70.28           N  
ANISOU 4505  N   VAL A 603    15389   5678   5636   1109   2465    613       N  
ATOM   4506  CA  VAL A 603     -63.648  -9.946 -10.077  1.00 72.75           C  
ANISOU 4506  CA  VAL A 603    15786   6073   5783   1004   2223    595       C  
ATOM   4507  C   VAL A 603     -64.574 -11.155 -10.005  1.00 72.20           C  
ANISOU 4507  C   VAL A 603    15617   6111   5702   1051   2387    668       C  
ATOM   4508  O   VAL A 603     -64.229 -12.253 -10.465  1.00 68.82           O  
ANISOU 4508  O   VAL A 603    14995   5833   5319   1011   2213    721       O  
ATOM   4509  CB  VAL A 603     -62.953  -9.686  -8.725  1.00 71.34           C  
ANISOU 4509  CB  VAL A 603    16077   5716   5312    912   2110    459       C  
ATOM   4510  CG1 VAL A 603     -62.475 -10.997  -8.109  1.00 73.55           C  
ANISOU 4510  CG1 VAL A 603    16487   6066   5393    845   1918    470       C  
ATOM   4511  CG2 VAL A 603     -61.788  -8.727  -8.901  1.00 68.34           C  
ANISOU 4511  CG2 VAL A 603    15734   5257   4974    817   1859    376       C  
ATOM   4512  N   GLU A 604     -65.774 -10.966  -9.451  1.00 75.82           N  
ANISOU 4512  N   GLU A 604    16196   6489   6125   1134   2740    666       N  
ATOM   4513  CA  GLU A 604     -66.714 -12.075  -9.332  1.00 77.01           C  
ANISOU 4513  CA  GLU A 604    16251   6725   6285   1159   2931    732       C  
ATOM   4514  C   GLU A 604     -67.145 -12.590 -10.703  1.00 73.54           C  
ANISOU 4514  C   GLU A 604    15309   6500   6132   1204   2910    827       C  
ATOM   4515  O   GLU A 604     -67.281 -13.805 -10.902  1.00 74.12           O  
ANISOU 4515  O   GLU A 604    15239   6683   6239   1161   2865    870       O  
ATOM   4516  CB  GLU A 604     -67.926 -11.644  -8.507  1.00 86.51           C  
ANISOU 4516  CB  GLU A 604    17647   7804   7420   1241   3341    703       C  
ATOM   4517  CG  GLU A 604     -68.717 -12.801  -7.923  1.00 96.39           C  
ANISOU 4517  CG  GLU A 604    18854   9087   8682   1212   3487    723       C  
ATOM   4518  CD  GLU A 604     -70.119 -12.890  -8.487  1.00105.14           C  
ANISOU 4518  CD  GLU A 604    19653  10285  10011   1311   3826    792       C  
ATOM   4519  OE1 GLU A 604     -70.544 -11.942  -9.180  1.00108.60           O  
ANISOU 4519  OE1 GLU A 604    19935  10745  10585   1429   3962    814       O  
ATOM   4520  OE2 GLU A 604     -70.796 -13.909  -8.235  1.00109.65           O  
ANISOU 4520  OE2 GLU A 604    20128  10903  10633   1271   3953    828       O  
ATOM   4521  N   GLY A 605     -67.359 -11.687 -11.665  1.00 71.05           N  
ANISOU 4521  N   GLY A 605    14733   6243   6021   1289   2938    859       N  
ATOM   4522  CA  GLY A 605     -67.717 -12.130 -13.005  1.00 64.75           C  
ANISOU 4522  CA  GLY A 605    13468   5674   5459   1335   2888    942       C  
ATOM   4523  C   GLY A 605     -66.619 -12.947 -13.663  1.00 63.27           C  
ANISOU 4523  C   GLY A 605    13128   5630   5283   1238   2546    947       C  
ATOM   4524  O   GLY A 605     -66.883 -13.998 -14.266  1.00 62.66           O  
ANISOU 4524  O   GLY A 605    12790   5716   5303   1223   2503    973       O  
ATOM   4525  N   VAL A 606     -65.372 -12.479 -13.556  1.00 62.35           N  
ANISOU 4525  N   VAL A 606    13160   5449   5081   1169   2303    909       N  
ATOM   4526  CA  VAL A 606     -64.248 -13.250 -14.085  1.00 59.79           C  
ANISOU 4526  CA  VAL A 606    12699   5251   4767   1083   1984    901       C  
ATOM   4527  C   VAL A 606     -64.194 -14.623 -13.430  1.00 64.18           C  
ANISOU 4527  C   VAL A 606    13372   5798   5215   1024   1929    881       C  
ATOM   4528  O   VAL A 606     -63.998 -15.646 -14.103  1.00 61.68           O  
ANISOU 4528  O   VAL A 606    12814   5627   4993   1004   1800    893       O  
ATOM   4529  CB  VAL A 606     -62.928 -12.480 -13.895  1.00 61.02           C  
ANISOU 4529  CB  VAL A 606    13014   5318   4851   1006   1750    851       C  
ATOM   4530  CG1 VAL A 606     -61.739 -13.367 -14.234  1.00 57.40           C  
ANISOU 4530  CG1 VAL A 606    12439   4976   4394    923   1429    829       C  
ATOM   4531  CG2 VAL A 606     -62.922 -11.227 -14.757  1.00 60.38           C  
ANISOU 4531  CG2 VAL A 606    12769   5252   4919   1054   1796    899       C  
ATOM   4532  N   ALA A 607     -64.382 -14.671 -12.108  1.00 69.07           N  
ANISOU 4532  N   ALA A 607    14376   6236   5629   1000   2036    850       N  
ATOM   4533  CA  ALA A 607     -64.433 -15.954 -11.418  1.00 60.71           C  
ANISOU 4533  CA  ALA A 607    13465   5144   4456    953   2020    864       C  
ATOM   4534  C   ALA A 607     -65.546 -16.840 -11.962  1.00 66.76           C  
ANISOU 4534  C   ALA A 607    13958   6016   5393    981   2219    916       C  
ATOM   4535  O   ALA A 607     -65.387 -18.063 -12.028  1.00 59.87           O  
ANISOU 4535  O   ALA A 607    13024   5176   4547    935   2123    934       O  
ATOM   4536  CB  ALA A 607     -64.613 -15.737  -9.915  1.00 64.88           C  
ANISOU 4536  CB  ALA A 607    14471   5473   4709    934   2156    839       C  
ATOM   4537  N   ALA A 608     -66.672 -16.245 -12.364  1.00 62.30           N  
ANISOU 4537  N   ALA A 608    13213   5496   4961   1057   2487    935       N  
ATOM   4538  CA  ALA A 608     -67.770 -17.036 -12.913  1.00 60.35           C  
ANISOU 4538  CA  ALA A 608    12667   5364   4898   1073   2666    968       C  
ATOM   4539  C   ALA A 608     -67.381 -17.666 -14.245  1.00 63.92           C  
ANISOU 4539  C   ALA A 608    12726   6026   5535   1061   2439    961       C  
ATOM   4540  O   ALA A 608     -67.606 -18.865 -14.466  1.00 64.93           O  
ANISOU 4540  O   ALA A 608    12717   6206   5746   1008   2421    954       O  
ATOM   4541  CB  ALA A 608     -69.017 -16.167 -13.070  1.00 62.34           C  
ANISOU 4541  CB  ALA A 608    12787   5634   5263   1176   2977    986       C  
ATOM   4542  N   VAL A 609     -66.793 -16.874 -15.146  1.00 57.15           N  
ANISOU 4542  N   VAL A 609    11692   5282   4741   1104   2276    959       N  
ATOM   4543  CA  VAL A 609     -66.359 -17.421 -16.432  1.00 55.51           C  
ANISOU 4543  CA  VAL A 609    11126   5291   4674   1096   2068    943       C  
ATOM   4544  C   VAL A 609     -65.331 -18.529 -16.218  1.00 60.09           C  
ANISOU 4544  C   VAL A 609    11793   5842   5197   1010   1828    899       C  
ATOM   4545  O   VAL A 609     -65.410 -19.612 -16.822  1.00 54.40           O  
ANISOU 4545  O   VAL A 609    10854   5228   4589    984   1761    865       O  
ATOM   4546  CB  VAL A 609     -65.805 -16.301 -17.331  1.00 54.73           C  
ANISOU 4546  CB  VAL A 609    10878   5300   4618   1150   1952    970       C  
ATOM   4547  CG1 VAL A 609     -65.433 -16.852 -18.701  1.00 53.28           C  
ANISOU 4547  CG1 VAL A 609    10325   5368   4553   1150   1769    953       C  
ATOM   4548  CG2 VAL A 609     -66.820 -15.171 -17.451  1.00 55.59           C  
ANISOU 4548  CG2 VAL A 609    10936   5399   4789   1258   2189   1031       C  
ATOM   4549  N   ARG A 610     -64.352 -18.272 -15.343  1.00 60.91           N  
ANISOU 4549  N   ARG A 610    12218   5795   5132    972   1689    891       N  
ATOM   4550  CA  ARG A 610     -63.363 -19.287 -15.002  1.00 61.32           C  
ANISOU 4550  CA  ARG A 610    12377   5798   5123    914   1452    863       C  
ATOM   4551  C   ARG A 610     -64.020 -20.537 -14.435  1.00 68.83           C  
ANISOU 4551  C   ARG A 610    13420   6658   6074    882   1571    882       C  
ATOM   4552  O   ARG A 610     -63.525 -21.648 -14.651  1.00 71.68           O  
ANISOU 4552  O   ARG A 610    13708   7031   6496    855   1411    861       O  
ATOM   4553  CB  ARG A 610     -62.353 -18.715 -14.004  1.00 60.25           C  
ANISOU 4553  CB  ARG A 610    12593   5512   4787    883   1295    854       C  
ATOM   4554  CG  ARG A 610     -61.135 -19.591 -13.755  1.00 64.32           C  
ANISOU 4554  CG  ARG A 610    13181   6003   5255    847    989    830       C  
ATOM   4555  CD  ARG A 610     -61.279 -20.458 -12.505  1.00 70.44           C  
ANISOU 4555  CD  ARG A 610    14304   6598   5863    826   1015    872       C  
ATOM   4556  NE  ARG A 610     -61.461 -19.661 -11.294  1.00 79.77           N  
ANISOU 4556  NE  ARG A 610    15882   7623   6802    814   1121    885       N  
ATOM   4557  CZ  ARG A 610     -62.583 -19.628 -10.581  1.00 84.95           C  
ANISOU 4557  CZ  ARG A 610    16738   8178   7362    819   1429    926       C  
ATOM   4558  NH1 ARG A 610     -63.626 -20.359 -10.951  1.00 88.94           N  
ANISOU 4558  NH1 ARG A 610    17064   8716   8012    824   1653    966       N  
ATOM   4559  NH2 ARG A 610     -62.661 -18.872  -9.494  1.00 83.31           N  
ANISOU 4559  NH2 ARG A 610    16903   7836   6916    812   1519    915       N  
ATOM   4560  N   SER A 611     -65.133 -20.381 -13.715  1.00 69.30           N  
ANISOU 4560  N   SER A 611    13635   6615   6079    884   1867    923       N  
ATOM   4561  CA  SER A 611     -65.812 -21.541 -13.149  1.00 65.99           C  
ANISOU 4561  CA  SER A 611    13309   6094   5670    835   2019    958       C  
ATOM   4562  C   SER A 611     -66.516 -22.352 -14.228  1.00 65.67           C  
ANISOU 4562  C   SER A 611    12864   6200   5888    819   2076    923       C  
ATOM   4563  O   SER A 611     -66.535 -23.587 -14.166  1.00 68.78           O  
ANISOU 4563  O   SER A 611    13247   6534   6353    761   2049    920       O  
ATOM   4564  CB  SER A 611     -66.811 -21.104 -12.079  1.00 65.66           C  
ANISOU 4564  CB  SER A 611    13536   5914   5498    836   2352   1008       C  
ATOM   4565  OG  SER A 611     -67.647 -22.189 -11.710  1.00 67.08           O  
ANISOU 4565  OG  SER A 611    13732   6018   5736    777   2555   1051       O  
ATOM   4566  N   VAL A 612     -67.113 -21.681 -15.215  1.00 57.24           N  
ANISOU 4566  N   VAL A 612    11469   5316   4963    870   2151    893       N  
ATOM   4567  CA  VAL A 612     -67.768 -22.408 -16.301  1.00 58.91           C  
ANISOU 4567  CA  VAL A 612    11281   5697   5404    853   2172    838       C  
ATOM   4568  C   VAL A 612     -66.738 -23.196 -17.103  1.00 55.58           C  
ANISOU 4568  C   VAL A 612    10703   5367   5047    833   1875    764       C  
ATOM   4569  O   VAL A 612     -66.896 -24.403 -17.346  1.00 57.43           O  
ANISOU 4569  O   VAL A 612    10826   5588   5406    773   1852    710       O  
ATOM   4570  CB  VAL A 612     -68.565 -21.443 -17.196  1.00 60.82           C  
ANISOU 4570  CB  VAL A 612    11216   6138   5755    935   2279    835       C  
ATOM   4571  CG1 VAL A 612     -69.125 -22.182 -18.400  1.00 61.87           C  
ANISOU 4571  CG1 VAL A 612    10927   6484   6099    917   2241    757       C  
ATOM   4572  CG2 VAL A 612     -69.686 -20.793 -16.401  1.00 63.30           C  
ANISOU 4572  CG2 VAL A 612    11652   6353   6047    968   2602    894       C  
ATOM   4573  N   ILE A 613     -65.654 -22.528 -17.509  1.00 54.35           N  
ANISOU 4573  N   ILE A 613    10538   5291   4820    878   1655    754       N  
ATOM   4574  CA  ILE A 613     -64.614 -23.222 -18.264  1.00 58.18           C  
ANISOU 4574  CA  ILE A 613    10868   5872   5367    871   1389    676       C  
ATOM   4575  C   ILE A 613     -63.999 -24.337 -17.425  1.00 65.59           C  
ANISOU 4575  C   ILE A 613    12048   6607   6267    825   1284    678       C  
ATOM   4576  O   ILE A 613     -63.703 -25.428 -17.931  1.00 66.50           O  
ANISOU 4576  O   ILE A 613    12017   6743   6506    807   1169    602       O  
ATOM   4577  CB  ILE A 613     -63.554 -22.219 -18.754  1.00 55.35           C  
ANISOU 4577  CB  ILE A 613    10465   5626   4940    917   1205    679       C  
ATOM   4578  CG1 ILE A 613     -64.152 -21.319 -19.841  1.00 53.53           C  
ANISOU 4578  CG1 ILE A 613     9945   5619   4776    973   1289    690       C  
ATOM   4579  CG2 ILE A 613     -62.313 -22.946 -19.258  1.00 51.83           C  
ANISOU 4579  CG2 ILE A 613     9918   5240   4537    911    938    602       C  
ATOM   4580  CD1 ILE A 613     -63.146 -20.428 -20.524  1.00 50.77           C  
ANISOU 4580  CD1 ILE A 613     9506   5396   4389   1004   1128    703       C  
ATOM   4581  N   GLU A 614     -63.827 -24.092 -16.125  1.00 67.65           N  
ANISOU 4581  N   GLU A 614    12693   6661   6348    814   1323    763       N  
ATOM   4582  CA  GLU A 614     -63.228 -25.088 -15.244  1.00 65.28           C  
ANISOU 4582  CA  GLU A 614    12663   6162   5980    789   1210    798       C  
ATOM   4583  C   GLU A 614     -64.113 -26.322 -15.121  1.00 65.98           C  
ANISOU 4583  C   GLU A 614    12727   6144   6196    731   1377    806       C  
ATOM   4584  O   GLU A 614     -63.619 -27.455 -15.151  1.00 62.33           O  
ANISOU 4584  O   GLU A 614    12273   5592   5817    719   1242    787       O  
ATOM   4585  CB  GLU A 614     -62.970 -24.470 -13.870  1.00 70.08           C  
ANISOU 4585  CB  GLU A 614    13703   6596   6327    790   1229    889       C  
ATOM   4586  CG  GLU A 614     -61.792 -25.058 -13.116  1.00 75.42           C  
ANISOU 4586  CG  GLU A 614    14642   7136   6880    801    965    923       C  
ATOM   4587  CD  GLU A 614     -61.511 -24.322 -11.817  1.00 79.13           C  
ANISOU 4587  CD  GLU A 614    15534   7472   7060    801    955    990       C  
ATOM   4588  OE1 GLU A 614     -62.479 -23.937 -11.126  1.00 81.14           O  
ANISOU 4588  OE1 GLU A 614    15989   7645   7196    778   1234   1041       O  
ATOM   4589  OE2 GLU A 614     -60.322 -24.119 -11.494  1.00 83.44           O  
ANISOU 4589  OE2 GLU A 614    16202   8004   7497    823    669    978       O  
ATOM   4590  N   ASP A 615     -65.425 -26.121 -14.991  1.00 68.94           N  
ANISOU 4590  N   ASP A 615    13061   6519   6613    693   1678    833       N  
ATOM   4591  CA  ASP A 615     -66.354 -27.238 -14.880  1.00 72.93           C  
ANISOU 4591  CA  ASP A 615    13519   6922   7269    611   1868    838       C  
ATOM   4592  C   ASP A 615     -66.570 -27.960 -16.201  1.00 73.17           C  
ANISOU 4592  C   ASP A 615    13131   7109   7562    585   1798    700       C  
ATOM   4593  O   ASP A 615     -67.039 -29.103 -16.193  1.00 78.45           O  
ANISOU 4593  O   ASP A 615    13756   7665   8388    504   1880    675       O  
ATOM   4594  CB  ASP A 615     -67.698 -26.756 -14.329  1.00 78.88           C  
ANISOU 4594  CB  ASP A 615    14325   7642   8002    575   2226    899       C  
ATOM   4595  CG  ASP A 615     -67.598 -26.269 -12.896  1.00 83.69           C  
ANISOU 4595  CG  ASP A 615    15396   8066   8336    585   2340   1022       C  
ATOM   4596  OD1 ASP A 615     -66.612 -26.626 -12.216  1.00 87.55           O  
ANISOU 4596  OD1 ASP A 615    16187   8416   8662    596   2149   1077       O  
ATOM   4597  OD2 ASP A 615     -68.504 -25.534 -12.447  1.00 86.75           O  
ANISOU 4597  OD2 ASP A 615    15845   8452   8665    590   2616   1058       O  
ATOM   4598  N   ASN A 616     -66.246 -27.331 -17.330  1.00 70.95           N  
ANISOU 4598  N   ASN A 616    12552   7078   7326    644   1656    608       N  
ATOM   4599  CA  ASN A 616     -66.279 -28.040 -18.604  1.00 70.00           C  
ANISOU 4599  CA  ASN A 616    12063   7124   7410    628   1551    457       C  
ATOM   4600  C   ASN A 616     -64.948 -28.700 -18.951  1.00 67.88           C  
ANISOU 4600  C   ASN A 616    11795   6838   7159    664   1268    385       C  
ATOM   4601  O   ASN A 616     -64.837 -29.314 -20.018  1.00 64.50           O  
ANISOU 4601  O   ASN A 616    11080   6544   6882    660   1170    237       O  
ATOM   4602  CB  ASN A 616     -66.691 -27.086 -19.730  1.00 72.99           C  
ANISOU 4602  CB  ASN A 616    12108   7807   7818    680   1556    399       C  
ATOM   4603  CG  ASN A 616     -67.152 -27.816 -20.983  1.00 71.67           C  
ANISOU 4603  CG  ASN A 616    11553   7831   7846    645   1515    235       C  
ATOM   4604  OD1 ASN A 616     -66.416 -27.915 -21.967  1.00 68.85           O  
ANISOU 4604  OD1 ASN A 616    11008   7649   7503    687   1316    130       O  
ATOM   4605  ND2 ASN A 616     -68.375 -28.334 -20.950  1.00 71.54           N  
ANISOU 4605  ND2 ASN A 616    11413   7789   7981    561   1708    202       N  
ATOM   4606  N   TRP A 617     -63.947 -28.608 -18.079  1.00 69.24           N  
ANISOU 4606  N   TRP A 617    12274   6853   7182    704   1134    474       N  
ATOM   4607  CA  TRP A 617     -62.621 -29.113 -18.409  1.00 72.11           C  
ANISOU 4607  CA  TRP A 617    12608   7218   7572    761    855    409       C  
ATOM   4608  C   TRP A 617     -62.585 -30.636 -18.358  1.00 77.38           C  
ANISOU 4608  C   TRP A 617    13292   7702   8409    730    824    355       C  
ATOM   4609  O   TRP A 617     -63.167 -31.263 -17.469  1.00 79.92           O  
ANISOU 4609  O   TRP A 617    13843   7786   8738    671    969    449       O  
ATOM   4610  CB  TRP A 617     -61.579 -28.534 -17.454  1.00 73.85           C  
ANISOU 4610  CB  TRP A 617    13135   7333   7591    813    700    518       C  
ATOM   4611  CG  TRP A 617     -60.161 -28.824 -17.852  1.00 76.93           C  
ANISOU 4611  CG  TRP A 617    13441   7770   8017    884    406    449       C  
ATOM   4612  CD1 TRP A 617     -59.401 -28.122 -18.743  1.00 78.85           C  
ANISOU 4612  CD1 TRP A 617    13449   8243   8268    927    267    372       C  
ATOM   4613  CD2 TRP A 617     -59.330 -29.887 -17.366  1.00 79.11           C  
ANISOU 4613  CD2 TRP A 617    13861   7858   8340    928    225    461       C  
ATOM   4614  NE1 TRP A 617     -58.151 -28.684 -18.845  1.00 80.18           N  
ANISOU 4614  NE1 TRP A 617    13583   8389   8493    990     21    320       N  
ATOM   4615  CE2 TRP A 617     -58.082 -29.768 -18.009  1.00 78.69           C  
ANISOU 4615  CE2 TRP A 617    13621   7944   8334   1002    -20    372       C  
ATOM   4616  CE3 TRP A 617     -59.521 -30.926 -16.450  1.00 85.14           C  
ANISOU 4616  CE3 TRP A 617    14892   8342   9114    917    255    550       C  
ATOM   4617  CZ2 TRP A 617     -57.030 -30.648 -17.767  1.00 82.20           C  
ANISOU 4617  CZ2 TRP A 617    14118   8263   8850   1080   -246    357       C  
ATOM   4618  CZ3 TRP A 617     -58.475 -31.801 -16.211  1.00 90.37           C  
ANISOU 4618  CZ3 TRP A 617    15631   8867   9837    998     21    553       C  
ATOM   4619  CH2 TRP A 617     -57.245 -31.656 -16.867  1.00 89.01           C  
ANISOU 4619  CH2 TRP A 617    15249   8845   9726   1086   -232    451       C  
ATOM   4620  N   VAL A 618     -61.889 -31.226 -19.325  1.00 83.54           N  
ANISOU 4620  N   VAL A 618    13832   8582   9328    772    648    204       N  
ATOM   4621  CA  VAL A 618     -61.722 -32.674 -19.427  1.00 88.15           C  
ANISOU 4621  CA  VAL A 618    14403   8985  10104    761    595    121       C  
ATOM   4622  C   VAL A 618     -60.238 -32.955 -19.633  1.00 90.82           C  
ANISOU 4622  C   VAL A 618    14725   9326  10456    876    316     69       C  
ATOM   4623  O   VAL A 618     -59.576 -32.222 -20.384  1.00 92.58           O  
ANISOU 4623  O   VAL A 618    14747   9798  10631    933    197     -5       O  
ATOM   4624  CB  VAL A 618     -62.577 -33.252 -20.569  1.00 88.79           C  
ANISOU 4624  CB  VAL A 618    14146   9198  10393    689    696    -71       C  
ATOM   4625  CG1 VAL A 618     -62.187 -34.691 -20.877  1.00 92.87           C  
ANISOU 4625  CG1 VAL A 618    14616   9543  11129    692    605   -206       C  
ATOM   4626  CG2 VAL A 618     -64.056 -33.166 -20.222  1.00 90.32           C  
ANISOU 4626  CG2 VAL A 618    14355   9345  10618    569    971    -13       C  
ATOM   4627  N   PRO A 619     -59.667 -33.964 -18.977  1.00 87.61           N  
ANISOU 4627  N   PRO A 619    14520   8650  10119    919    211    117       N  
ATOM   4628  CA  PRO A 619     -58.264 -34.315 -19.225  1.00 92.03           C  
ANISOU 4628  CA  PRO A 619    15019   9214  10734   1047    -57     51       C  
ATOM   4629  C   PRO A 619     -58.022 -34.567 -20.701  1.00 96.95           C  
ANISOU 4629  C   PRO A 619    15246  10070  11522   1073   -102   -193       C  
ATOM   4630  O   PRO A 619     -58.764 -35.331 -21.339  1.00 93.14           O  
ANISOU 4630  O   PRO A 619    14610   9570  11208   1010     14   -334       O  
ATOM   4631  CB  PRO A 619     -58.062 -35.596 -18.396  1.00 91.67           C  
ANISOU 4631  CB  PRO A 619    15229   8806  10795   1082   -106    135       C  
ATOM   4632  CG  PRO A 619     -59.449 -36.063 -18.037  1.00 89.87           C  
ANISOU 4632  CG  PRO A 619    15117   8410  10621    944    167    191       C  
ATOM   4633  CD  PRO A 619     -60.268 -34.818 -17.941  1.00 87.57           C  
ANISOU 4633  CD  PRO A 619    14815   8313  10144    862    339    252       C  
ATOM   4634  N   PRO A 620     -57.003 -33.924 -21.286  1.00104.92           N  
ANISOU 4634  N   PRO A 620    16077  11307  12481   1155   -262   -257       N  
ATOM   4635  CA  PRO A 620     -56.784 -34.033 -22.737  1.00106.08           C  
ANISOU 4635  CA  PRO A 620    15851  11719  12733   1179   -280   -486       C  
ATOM   4636  C   PRO A 620     -56.567 -35.464 -23.201  1.00110.01           C  
ANISOU 4636  C   PRO A 620    16251  12076  13472   1225   -324   -668       C  
ATOM   4637  O   PRO A 620     -57.459 -36.079 -23.794  1.00113.85           O  
ANISOU 4637  O   PRO A 620    16617  12564  14078   1148   -194   -809       O  
ATOM   4638  CB  PRO A 620     -55.531 -33.176 -22.965  1.00103.01           C  
ANISOU 4638  CB  PRO A 620    15362  11527  12252   1263   -448   -473       C  
ATOM   4639  CG  PRO A 620     -55.489 -32.239 -21.803  1.00102.55           C  
ANISOU 4639  CG  PRO A 620    15584  11379  12002   1237   -469   -250       C  
ATOM   4640  CD  PRO A 620     -56.040 -33.013 -20.645  1.00105.50           C  
ANISOU 4640  CD  PRO A 620    16282  11417  12387   1213   -421   -126       C  
ATOM   4641  N   ARG A 621     -55.384 -35.999 -22.934  1.00105.83           N  
ANISOU 4641  N   ARG A 621    15763  11419  13029   1352   -512   -675       N  
ATOM   4642  CA  ARG A 621     -55.039 -37.355 -23.327  1.00100.21           C  
ANISOU 4642  CA  ARG A 621    14971  10538  12565   1427   -565   -848       C  
ATOM   4643  C   ARG A 621     -55.650 -38.351 -22.349  1.00 99.87           C  
ANISOU 4643  C   ARG A 621    15225  10091  12630   1389   -503   -731       C  
ATOM   4644  O   ARG A 621     -56.164 -37.971 -21.294  1.00100.63           O  
ANISOU 4644  O   ARG A 621    15600  10052  12583   1323   -438   -503       O  
ATOM   4645  CB  ARG A 621     -53.520 -37.491 -23.383  1.00 95.10           C  
ANISOU 4645  CB  ARG A 621    14240   9911  11982   1599   -789   -886       C  
ATOM   4646  CG  ARG A 621     -52.781 -36.231 -22.975  1.00 91.69           C  
ANISOU 4646  CG  ARG A 621    13833   9657  11350   1623   -905   -734       C  
ATOM   4647  CD  ARG A 621     -51.283 -36.450 -22.929  1.00 92.87           C  
ANISOU 4647  CD  ARG A 621    13885   9803  11597   1788  -1137   -767       C  
ATOM   4648  NE  ARG A 621     -50.890 -37.409 -21.901  1.00 96.12           N  
ANISOU 4648  NE  ARG A 621    14546   9856  12120   1895  -1282   -653       N  
ATOM   4649  CZ  ARG A 621     -50.584 -38.680 -22.140  1.00 98.87           C  
ANISOU 4649  CZ  ARG A 621    14845  10004  12717   2010  -1326   -776       C  
ATOM   4650  NH1 ARG A 621     -50.624 -39.155 -23.378  1.00100.79           N  
ANISOU 4650  NH1 ARG A 621    14798  10380  13117   2025  -1233  -1046       N  
ATOM   4651  NH2 ARG A 621     -50.237 -39.478 -21.139  1.00101.04           N  
ANISOU 4651  NH2 ARG A 621    15374   9940  13077   2118  -1464   -629       N  
ATOM   4652  N   PRO A 622     -55.635 -39.642 -22.680  1.00101.33           N  
ANISOU 4652  N   PRO A 622    15366  10066  13070   1423   -501   -885       N  
ATOM   4653  CA  PRO A 622     -56.038 -40.644 -21.701  1.00104.19           C  
ANISOU 4653  CA  PRO A 622    16032  10001  13555   1401   -454   -745       C  
ATOM   4654  C   PRO A 622     -55.161 -40.562 -20.463  1.00104.78           C  
ANISOU 4654  C   PRO A 622    16406   9881  13525   1529   -634   -483       C  
ATOM   4655  O   PRO A 622     -54.001 -40.118 -20.534  1.00103.95           O  
ANISOU 4655  O   PRO A 622    16210   9922  13363   1668   -840   -486       O  
ATOM   4656  CB  PRO A 622     -55.841 -41.971 -22.448  1.00105.43           C  
ANISOU 4656  CB  PRO A 622    16043   9990  14026   1456   -467   -996       C  
ATOM   4657  CG  PRO A 622     -55.007 -41.638 -23.651  1.00102.72           C  
ANISOU 4657  CG  PRO A 622    15350   9988  13692   1557   -570  -1244       C  
ATOM   4658  CD  PRO A 622     -55.391 -40.243 -24.002  1.00100.31           C  
ANISOU 4658  CD  PRO A 622    14917  10074  13122   1463   -507  -1205       C  
ATOM   4659  N   PRO A 623     -55.683 -40.975 -19.306  1.00107.56           N  
ANISOU 4659  N   PRO A 623    17115   9912  13842   1481   -564   -250       N  
ATOM   4660  CA  PRO A 623     -54.918 -40.819 -18.060  1.00106.79           C  
ANISOU 4660  CA  PRO A 623    17336   9655  13585   1597   -747     18       C  
ATOM   4661  C   PRO A 623     -53.724 -41.755 -17.969  1.00105.50           C  
ANISOU 4661  C   PRO A 623    17182   9290  13614   1811   -990      3       C  
ATOM   4662  O   PRO A 623     -53.461 -42.535 -18.889  1.00106.12           O  
ANISOU 4662  O   PRO A 623    17020   9338  13961   1873  -1000   -228       O  
ATOM   4663  CB  PRO A 623     -55.958 -41.132 -16.977  1.00110.75           C  
ANISOU 4663  CB  PRO A 623    18209   9868  14002   1474   -553    252       C  
ATOM   4664  CG  PRO A 623     -56.909 -42.065 -17.648  1.00112.27           C  
ANISOU 4664  CG  PRO A 623    18275   9919  14465   1350   -335     89       C  
ATOM   4665  CD  PRO A 623     -56.995 -41.602 -19.077  1.00108.92           C  
ANISOU 4665  CD  PRO A 623    17416   9860  14110   1311   -310   -218       C  
ATOM   4666  N   LEU A 624     -52.997 -41.680 -16.860  1.00104.67           N  
ANISOU 4666  N   LEU A 624    17352   9048  13369   1932  -1192    243       N  
ATOM   4667  CA  LEU A 624     -51.842 -42.527 -16.614  1.00103.82           C  
ANISOU 4667  CA  LEU A 624    17277   8737  13432   2162  -1453    276       C  
ATOM   4668  C   LEU A 624     -52.247 -43.780 -15.855  1.00107.48           C  
ANISOU 4668  C   LEU A 624    18073   8734  14029   2189  -1394    452       C  
ATOM   4669  O   LEU A 624     -53.295 -43.817 -15.204  1.00110.25           O  
ANISOU 4669  O   LEU A 624    18702   8929  14260   2031  -1183    620       O  
ATOM   4670  CB  LEU A 624     -50.789 -41.767 -15.806  1.00 98.16           C  
ANISOU 4670  CB  LEU A 624    16670   8138  12490   2287  -1743    445       C  
ATOM   4671  CG  LEU A 624     -50.051 -40.576 -16.416  1.00 90.56           C  
ANISOU 4671  CG  LEU A 624    15392   7590  11427   2294  -1865    302       C  
ATOM   4672  CD1 LEU A 624     -49.586 -40.889 -17.830  1.00 87.65           C  
ANISOU 4672  CD1 LEU A 624    14578   7392  11333   2359  -1852     -7       C  
ATOM   4673  CD2 LEU A 624     -50.916 -39.330 -16.377  1.00 88.90           C  
ANISOU 4673  CD2 LEU A 624    15221   7614  10944   2086  -1676    332       C  
ATOM   4674  N   PRO A 625     -51.440 -44.829 -15.924  1.00108.63           N  
ANISOU 4674  N   PRO A 625    18198   8638  14437   2392  -1563    425       N  
ATOM   4675  CA  PRO A 625     -51.586 -45.952 -14.997  1.00112.46           C  
ANISOU 4675  CA  PRO A 625    19059   8651  15020   2463  -1569    667       C  
ATOM   4676  C   PRO A 625     -50.985 -45.587 -13.642  1.00111.51           C  
ANISOU 4676  C   PRO A 625    19291   8473  14606   2582  -1806   1005       C  
ATOM   4677  O   PRO A 625     -50.520 -44.470 -13.421  1.00107.87           O  
ANISOU 4677  O   PRO A 625    18780   8326  13881   2587  -1954   1030       O  
ATOM   4678  CB  PRO A 625     -50.806 -47.075 -15.681  1.00114.97           C  
ANISOU 4678  CB  PRO A 625    19176   8773  15735   2669  -1691    482       C  
ATOM   4679  CG  PRO A 625     -49.776 -46.364 -16.491  1.00110.26           C  
ANISOU 4679  CG  PRO A 625    18179   8571  15143   2787  -1880    256       C  
ATOM   4680  CD  PRO A 625     -50.435 -45.100 -16.968  1.00105.80           C  
ANISOU 4680  CD  PRO A 625    17451   8415  14332   2561  -1715    150       C  
ATOM   4681  N   GLU A 626     -51.000 -46.557 -12.729  1.00114.10           N  
ANISOU 4681  N   GLU A 626    19988   8384  14979   2677  -1846   1269       N  
ATOM   4682  CA  GLU A 626     -50.424 -46.347 -11.405  1.00114.76           C  
ANISOU 4682  CA  GLU A 626    20421   8412  14769   2800  -2086   1600       C  
ATOM   4683  C   GLU A 626     -49.574 -47.503 -10.906  1.00119.35           C  
ANISOU 4683  C   GLU A 626    21033   8772  15544   3009  -2281   1740       C  
ATOM   4684  O   GLU A 626     -48.828 -47.311  -9.941  1.00123.27           O  
ANISOU 4684  O   GLU A 626    21652   9367  15820   3117  -2526   1946       O  
ATOM   4685  CB  GLU A 626     -51.531 -46.065 -10.378  1.00116.00           C  
ANISOU 4685  CB  GLU A 626    20910   8560  14606   2561  -1819   1842       C  
ATOM   4686  N   LEU A 627     -49.650 -48.682 -11.515  1.00119.68           N  
ANISOU 4686  N   LEU A 627    20967   8517  15990   3071  -2184   1628       N  
ATOM   4687  CA  LEU A 627     -48.870 -49.830 -11.066  1.00123.90           C  
ANISOU 4687  CA  LEU A 627    21528   8809  16739   3281  -2345   1771       C  
ATOM   4688  C   LEU A 627     -47.389 -49.644 -11.376  1.00123.88           C  
ANISOU 4688  C   LEU A 627    21255   8982  16833   3569  -2728   1660       C  
ATOM   4689  O   LEU A 627     -46.603 -50.587 -11.277  1.00128.17           O  
ANISOU 4689  O   LEU A 627    21730   9343  17627   3786  -2878   1707       O  
ATOM   4690  CB  LEU A 627     -49.390 -51.107 -11.711  1.00125.23           C  
ANISOU 4690  CB  LEU A 627    21639   8602  17342   3254  -2113   1647       C  
ATOM   4691  N   LEU A 647     -56.563 -64.875 -40.567  1.00106.67           N  
ANISOU 4691  N   LEU A 647    18829   8789  12913  -2917    -92   2236       N  
ATOM   4692  CA  LEU A 647     -56.247 -63.990 -41.683  1.00101.54           C  
ANISOU 4692  CA  LEU A 647    17973   8273  12335  -2685   -186   2024       C  
ATOM   4693  C   LEU A 647     -55.990 -64.772 -42.965  1.00102.71           C  
ANISOU 4693  C   LEU A 647    18259   8103  12663  -2464   -418   1865       C  
ATOM   4694  O   LEU A 647     -55.459 -65.882 -42.925  1.00103.86           O  
ANISOU 4694  O   LEU A 647    18694   7960  12810  -2309   -574   1953       O  
ATOM   4695  CB  LEU A 647     -55.028 -63.124 -41.358  1.00 95.48           C  
ANISOU 4695  CB  LEU A 647    17173   7748  11357  -2340   -245   2107       C  
ATOM   4696  CG  LEU A 647     -55.192 -62.047 -40.287  1.00 94.87           C  
ANISOU 4696  CG  LEU A 647    16903   8046  11099  -2488    -46   2198       C  
ATOM   4697  CD1 LEU A 647     -53.908 -61.246 -40.146  1.00 90.27           C  
ANISOU 4697  CD1 LEU A 647    16280   7664  10356  -2116   -152   2246       C  
ATOM   4698  CD2 LEU A 647     -56.363 -61.136 -40.619  1.00 96.27           C  
ANISOU 4698  CD2 LEU A 647    16754   8441  11384  -2792    139   2014       C  
ATOM   4699  N   PRO A 648     -56.367 -64.194 -44.105  1.00103.66           N  
ANISOU 4699  N   PRO A 648    18185   8276  12925  -2430   -455   1616       N  
ATOM   4700  CA  PRO A 648     -56.023 -64.812 -45.389  1.00105.57           C  
ANISOU 4700  CA  PRO A 648    18552   8258  13301  -2148   -688   1433       C  
ATOM   4701  C   PRO A 648     -54.515 -64.841 -45.591  1.00108.31           C  
ANISOU 4701  C   PRO A 648    19050   8602  13499  -1651   -856   1496       C  
ATOM   4702  O   PRO A 648     -53.758 -64.127 -44.929  1.00117.78           O  
ANISOU 4702  O   PRO A 648    20196  10037  14519  -1516   -801   1636       O  
ATOM   4703  CB  PRO A 648     -56.712 -63.907 -46.418  1.00102.17           C  
ANISOU 4703  CB  PRO A 648    17864   7965  12993  -2199   -675   1155       C  
ATOM   4704  CG  PRO A 648     -56.899 -62.604 -45.712  1.00 99.84           C  
ANISOU 4704  CG  PRO A 648    17327   8039  12570  -2357   -472   1222       C  
ATOM   4705  CD  PRO A 648     -57.143 -62.955 -44.276  1.00100.53           C  
ANISOU 4705  CD  PRO A 648    17457   8176  12562  -2632   -300   1467       C  
ATOM   4706  N   ALA A 649     -54.082 -65.690 -46.528  1.00104.92           N  
ANISOU 4706  N   ALA A 649    18792   7913  13158  -1369  -1068   1365       N  
ATOM   4707  CA  ALA A 649     -52.652 -65.868 -46.766  1.00101.32           C  
ANISOU 4707  CA  ALA A 649    18463   7445  12588   -880  -1232   1387       C  
ATOM   4708  C   ALA A 649     -51.973 -64.561 -47.154  1.00 97.56           C  
ANISOU 4708  C   ALA A 649    17779   7284  12003   -631  -1178   1329       C  
ATOM   4709  O   ALA A 649     -50.813 -64.330 -46.791  1.00101.86           O  
ANISOU 4709  O   ALA A 649    18337   7949  12417   -333  -1221   1429       O  
ATOM   4710  CB  ALA A 649     -52.431 -66.924 -47.849  1.00101.44           C  
ANISOU 4710  CB  ALA A 649    18654   7167  12723   -620  -1452   1196       C  
ATOM   4711  N   GLU A 650     -52.679 -63.693 -47.880  1.00 89.93           N  
ANISOU 4711  N   GLU A 650    16623   6450  11098   -748  -1094   1162       N  
ATOM   4712  CA  GLU A 650     -52.102 -62.422 -48.306  1.00 86.62           C  
ANISOU 4712  CA  GLU A 650    15959   6376  10577   -524  -1018   1094       C  
ATOM   4713  C   GLU A 650     -51.808 -61.524 -47.108  1.00 78.40           C  
ANISOU 4713  C   GLU A 650    14751   5642   9396   -644   -862   1300       C  
ATOM   4714  O   GLU A 650     -50.673 -61.068 -46.911  1.00 76.29           O  
ANISOU 4714  O   GLU A 650    14395   5577   9016   -357   -868   1364       O  
ATOM   4715  CB  GLU A 650     -53.056 -61.734 -49.285  1.00 88.43           C  
ANISOU 4715  CB  GLU A 650    15939   6766  10894   -632   -961    839       C  
ATOM   4716  CG  GLU A 650     -52.380 -61.042 -50.451  1.00 88.68           C  
ANISOU 4716  CG  GLU A 650    15807   7034  10853   -249   -972    658       C  
ATOM   4717  CD  GLU A 650     -53.371 -60.601 -51.512  1.00 91.59           C  
ANISOU 4717  CD  GLU A 650    16039   7464  11295   -316   -985    396       C  
ATOM   4718  OE1 GLU A 650     -54.589 -60.789 -51.308  1.00 94.06           O  
ANISOU 4718  OE1 GLU A 650    16328   7663  11747   -664   -990    332       O  
ATOM   4719  OE2 GLU A 650     -52.930 -60.069 -52.552  1.00 90.33           O  
ANISOU 4719  OE2 GLU A 650    15801   7471  11051    -20   -992    247       O  
ATOM   4720  N   MET A 651     -52.829 -61.267 -46.286  1.00 76.47           N  
ANISOU 4720  N   MET A 651    14448   5445   9164  -1071   -721   1387       N  
ATOM   4721  CA  MET A 651     -52.646 -60.406 -45.125  1.00 74.66           C  
ANISOU 4721  CA  MET A 651    14071   5509   8785  -1192   -577   1560       C  
ATOM   4722  C   MET A 651     -51.771 -61.063 -44.066  1.00 73.44           C  
ANISOU 4722  C   MET A 651    14152   5252   8501  -1077   -651   1799       C  
ATOM   4723  O   MET A 651     -51.138 -60.362 -43.269  1.00 69.80           O  
ANISOU 4723  O   MET A 651    13600   5030   7892  -1002   -608   1921       O  
ATOM   4724  CB  MET A 651     -54.004 -60.027 -44.537  1.00 74.80           C  
ANISOU 4724  CB  MET A 651    13953   5625   8842  -1663   -393   1556       C  
ATOM   4725  CG  MET A 651     -54.950 -59.372 -45.533  1.00 74.20           C  
ANISOU 4725  CG  MET A 651    13580   5699   8912  -1751   -352   1270       C  
ATOM   4726  SD  MET A 651     -54.336 -57.806 -46.184  1.00 71.38           S  
ANISOU 4726  SD  MET A 651    12870   5773   8477  -1444   -326   1128       S  
ATOM   4727  CE  MET A 651     -53.705 -58.296 -47.788  1.00 72.74           C  
ANISOU 4727  CE  MET A 651    13151   5777   8711  -1043   -504    947       C  
ATOM   4728  N   GLN A 652     -51.727 -62.397 -44.035  1.00 75.01           N  
ANISOU 4728  N   GLN A 652    14600   5142   8758  -1040   -775   1832       N  
ATOM   4729  CA  GLN A 652     -50.835 -63.087 -43.106  1.00 77.42           C  
ANISOU 4729  CA  GLN A 652    15103   5369   8944   -865   -883   2012       C  
ATOM   4730  C   GLN A 652     -49.379 -62.899 -43.512  1.00 74.38           C  
ANISOU 4730  C   GLN A 652    14711   5042   8506   -374  -1048   1974       C  
ATOM   4731  O   GLN A 652     -48.521 -62.593 -42.672  1.00 73.83           O  
ANISOU 4731  O   GLN A 652    14628   5122   8301   -216  -1089   2098       O  
ATOM   4732  CB  GLN A 652     -51.193 -64.573 -43.040  1.00 80.91           C  
ANISOU 4732  CB  GLN A 652    15834   5440   9469   -953   -984   2048       C  
ATOM   4733  CG  GLN A 652     -50.123 -65.449 -42.402  1.00 88.43           C  
ANISOU 4733  CG  GLN A 652    17048   6233  10317   -669  -1174   2181       C  
ATOM   4734  CD  GLN A 652     -49.934 -65.177 -40.921  1.00 91.40           C  
ANISOU 4734  CD  GLN A 652    17464   6768  10495   -777  -1099   2404       C  
ATOM   4735  OE1 GLN A 652     -50.814 -64.625 -40.259  1.00 89.50           O  
ANISOU 4735  OE1 GLN A 652    17107   6698  10202  -1135   -882   2479       O  
ATOM   4736  NE2 GLN A 652     -48.780 -65.568 -40.392  1.00 94.84           N  
ANISOU 4736  NE2 GLN A 652    18063   7154  10817   -447  -1290   2488       N  
ATOM   4737  N   GLU A 653     -49.082 -63.078 -44.803  1.00 69.46           N  
ANISOU 4737  N   GLU A 653    14089   4313   7989   -115  -1146   1784       N  
ATOM   4738  CA  GLU A 653     -47.731 -62.815 -45.287  1.00 70.69           C  
ANISOU 4738  CA  GLU A 653    14189   4563   8106    358  -1261   1717       C  
ATOM   4739  C   GLU A 653     -47.351 -61.356 -45.070  1.00 73.01           C  
ANISOU 4739  C   GLU A 653    14138   5284   8318    373  -1113   1726       C  
ATOM   4740  O   GLU A 653     -46.203 -61.051 -44.726  1.00 78.20           O  
ANISOU 4740  O   GLU A 653    14681   6120   8912    655  -1174   1751       O  
ATOM   4741  CB  GLU A 653     -47.617 -63.185 -46.764  1.00 72.12           C  
ANISOU 4741  CB  GLU A 653    14402   4603   8398    616  -1342   1480       C  
ATOM   4742  CG  GLU A 653     -46.246 -62.910 -47.360  1.00 78.30           C  
ANISOU 4742  CG  GLU A 653    15008   5592   9151   1101  -1396   1350       C  
ATOM   4743  CD  GLU A 653     -46.206 -63.131 -48.858  1.00 86.51           C  
ANISOU 4743  CD  GLU A 653    16006   6604  10262   1335  -1411   1084       C  
ATOM   4744  OE1 GLU A 653     -47.171 -63.711 -49.400  1.00 91.83           O  
ANISOU 4744  OE1 GLU A 653    16866   7008  11018   1171  -1457   1002       O  
ATOM   4745  OE2 GLU A 653     -45.211 -62.722 -49.493  1.00 87.55           O  
ANISOU 4745  OE2 GLU A 653    15915   6989  10362   1677  -1371    948       O  
ATOM   4746  N   ALA A 654     -48.306 -60.440 -45.259  1.00 71.26           N  
ANISOU 4746  N   ALA A 654    13678   5277   8121     70   -920   1664       N  
ATOM   4747  CA  ALA A 654     -48.027 -59.034 -44.985  1.00 71.24           C  
ANISOU 4747  CA  ALA A 654    13312   5701   8054     47   -777   1654       C  
ATOM   4748  C   ALA A 654     -47.776 -58.787 -43.502  1.00 75.11           C  
ANISOU 4748  C   ALA A 654    13844   6286   8410    -62   -775   1866       C  
ATOM   4749  O   ALA A 654     -46.969 -57.919 -43.149  1.00 77.20           O  
ANISOU 4749  O   ALA A 654    13873   6842   8617     78   -759   1870       O  
ATOM   4750  CB  ALA A 654     -49.177 -58.164 -45.488  1.00 69.73           C  
ANISOU 4750  CB  ALA A 654    12900   5677   7917   -233   -610   1529       C  
ATOM   4751  N   GLU A 655     -48.454 -59.530 -42.623  1.00 77.96           N  
ANISOU 4751  N   GLU A 655    14510   6401   8711   -318   -790   2040       N  
ATOM   4752  CA  GLU A 655     -48.175 -59.433 -41.193  1.00 82.84           C  
ANISOU 4752  CA  GLU A 655    15204   7109   9163   -385   -800   2235       C  
ATOM   4753  C   GLU A 655     -46.753 -59.881 -40.886  1.00 84.79           C  
ANISOU 4753  C   GLU A 655    15562   7303   9352     29  -1025   2286       C  
ATOM   4754  O   GLU A 655     -46.019 -59.205 -40.152  1.00 85.91           O  
ANISOU 4754  O   GLU A 655    15602   7660   9378    152  -1070   2353       O  
ATOM   4755  CB  GLU A 655     -49.181 -60.273 -40.403  1.00 89.36           C  
ANISOU 4755  CB  GLU A 655    16208   7778   9967   -720   -724   2335       C  
ATOM   4756  CG  GLU A 655     -50.495 -59.574 -40.107  1.00 91.09           C  
ANISOU 4756  CG  GLU A 655    16254   8174  10184  -1146   -481   2314       C  
ATOM   4757  CD  GLU A 655     -50.440 -58.738 -38.843  1.00 89.76           C  
ANISOU 4757  CD  GLU A 655    15974   8302   9828  -1246   -383   2421       C  
ATOM   4758  OE1 GLU A 655     -49.776 -59.163 -37.874  1.00 87.84           O  
ANISOU 4758  OE1 GLU A 655    15901   8031   9444  -1117   -482   2564       O  
ATOM   4759  OE2 GLU A 655     -51.058 -57.653 -38.820  1.00 89.25           O  
ANISOU 4759  OE2 GLU A 655    15663   8495   9752  -1439   -223   2347       O  
ATOM   4760  N   GLU A 656     -46.347 -61.027 -41.441  1.00 88.33           N  
ANISOU 4760  N   GLU A 656    16210   7464   9885    261  -1191   2233       N  
ATOM   4761  CA  GLU A 656     -44.984 -61.500 -41.224  1.00 90.75           C  
ANISOU 4761  CA  GLU A 656    16603   7720  10160    695  -1429   2238       C  
ATOM   4762  C   GLU A 656     -43.962 -60.513 -41.774  1.00 87.94           C  
ANISOU 4762  C   GLU A 656    15911   7663   9840   1003  -1437   2105       C  
ATOM   4763  O   GLU A 656     -42.894 -60.322 -41.181  1.00 90.31           O  
ANISOU 4763  O   GLU A 656    16124   8103  10088   1269  -1577   2118       O  
ATOM   4764  CB  GLU A 656     -44.792 -62.877 -41.855  1.00 96.78           C  
ANISOU 4764  CB  GLU A 656    17606   8142  11026    895  -1598   2154       C  
ATOM   4765  CG  GLU A 656     -45.515 -63.994 -41.126  1.00104.47           C  
ANISOU 4765  CG  GLU A 656    18884   8844  11966    639  -1621   2282       C  
ATOM   4766  CD  GLU A 656     -45.019 -65.363 -41.538  1.00110.43           C  
ANISOU 4766  CD  GLU A 656    19900   9267  12793    912  -1853   2211       C  
ATOM   4767  OE1 GLU A 656     -44.040 -65.429 -42.311  1.00110.94           O  
ANISOU 4767  OE1 GLU A 656    19885   9344  12924   1331  -1999   2049       O  
ATOM   4768  OE2 GLU A 656     -45.604 -66.371 -41.088  1.00115.33           O  
ANISOU 4768  OE2 GLU A 656    20801   9618  13402    712  -1883   2310       O  
ATOM   4769  N   MET A 657     -44.270 -59.874 -42.905  1.00 84.19           N  
ANISOU 4769  N   MET A 657    15137   7368   9481    951  -1260   1920       N  
ATOM   4770  CA  MET A 657     -43.358 -58.877 -43.458  1.00 80.14           C  
ANISOU 4770  CA  MET A 657    14194   7228   9027   1165  -1185   1757       C  
ATOM   4771  C   MET A 657     -43.249 -57.664 -42.543  1.00 70.78           C  
ANISOU 4771  C   MET A 657    12753   6372   7769   1004  -1097   1827       C  
ATOM   4772  O   MET A 657     -42.146 -57.178 -42.268  1.00 68.85           O  
ANISOU 4772  O   MET A 657    12273   6351   7537   1229  -1162   1778       O  
ATOM   4773  CB  MET A 657     -43.816 -58.450 -44.853  1.00 81.87           C  
ANISOU 4773  CB  MET A 657    14225   7539   9342   1117  -1008   1574       C  
ATOM   4774  CG  MET A 657     -43.615 -59.492 -45.937  1.00 90.48           C  
ANISOU 4774  CG  MET A 657    15488   8384  10506   1379  -1103   1435       C  
ATOM   4775  SD  MET A 657     -43.744 -58.772 -47.586  1.00 96.12           S  
ANISOU 4775  SD  MET A 657    15935   9311  11275   1434   -899   1200       S  
ATOM   4776  CE  MET A 657     -45.287 -57.876 -47.452  1.00 90.70           C  
ANISOU 4776  CE  MET A 657    15194   8697  10573    948   -732   1254       C  
ATOM   4777  N   LEU A 658     -44.386 -57.160 -42.059  1.00 64.86           N  
ANISOU 4777  N   LEU A 658    12028   5661   6954    621   -956   1917       N  
ATOM   4778  CA  LEU A 658     -44.386 -55.942 -41.259  1.00 63.20           C  
ANISOU 4778  CA  LEU A 658    11574   5765   6675    466   -870   1952       C  
ATOM   4779  C   LEU A 658     -43.892 -56.163 -39.837  1.00 67.92           C  
ANISOU 4779  C   LEU A 658    12338   6349   7119    525  -1031   2113       C  
ATOM   4780  O   LEU A 658     -43.560 -55.188 -39.155  1.00 68.21           O  
ANISOU 4780  O   LEU A 658    12157   6658   7103    497  -1020   2109       O  
ATOM   4781  CB  LEU A 658     -45.787 -55.329 -41.233  1.00 58.88           C  
ANISOU 4781  CB  LEU A 658    10983   5280   6108     68   -673   1957       C  
ATOM   4782  CG  LEU A 658     -46.218 -54.675 -42.548  1.00 59.71           C  
ANISOU 4782  CG  LEU A 658    10854   5494   6341     23   -528   1774       C  
ATOM   4783  CD1 LEU A 658     -47.595 -54.043 -42.417  1.00 57.78           C  
ANISOU 4783  CD1 LEU A 658    10547   5323   6083   -336   -376   1752       C  
ATOM   4784  CD2 LEU A 658     -45.190 -53.645 -42.992  1.00 56.44           C  
ANISOU 4784  CD2 LEU A 658    10100   5365   5982    216   -494   1666       C  
ATOM   4785  N   ARG A 659     -43.840 -57.410 -39.369  1.00 70.95           N  
ANISOU 4785  N   ARG A 659    13130   6408   7420    613  -1199   2251       N  
ATOM   4786  CA  ARG A 659     -43.256 -57.704 -38.069  1.00 74.24           C  
ANISOU 4786  CA  ARG A 659    13764   6784   7661    736  -1397   2406       C  
ATOM   4787  C   ARG A 659     -41.834 -58.239 -38.166  1.00 76.61           C  
ANISOU 4787  C   ARG A 659    14058   7033   8017   1212  -1671   2330       C  
ATOM   4788  O   ARG A 659     -41.154 -58.336 -37.139  1.00 79.17           O  
ANISOU 4788  O   ARG A 659    14497   7373   8210   1389  -1883   2410       O  
ATOM   4789  CB  ARG A 659     -44.140 -58.694 -37.302  1.00 78.57           C  
ANISOU 4789  CB  ARG A 659    14729   7049   8076    494  -1385   2594       C  
ATOM   4790  CG  ARG A 659     -45.522 -58.132 -37.014  1.00 75.52           C  
ANISOU 4790  CG  ARG A 659    14265   6784   7643     27  -1102   2630       C  
ATOM   4791  CD  ARG A 659     -46.307 -58.978 -36.038  1.00 74.81           C  
ANISOU 4791  CD  ARG A 659    14432   6549   7441   -222  -1033   2765       C  
ATOM   4792  NE  ARG A 659     -47.591 -58.359 -35.725  1.00 71.17           N  
ANISOU 4792  NE  ARG A 659    13845   6253   6942   -637   -757   2769       N  
ATOM   4793  CZ  ARG A 659     -47.761 -57.419 -34.800  1.00 70.25           C  
ANISOU 4793  CZ  ARG A 659    13606   6420   6668   -755   -664   2801       C  
ATOM   4794  NH1 ARG A 659     -46.726 -56.987 -34.091  1.00 67.65           N  
ANISOU 4794  NH1 ARG A 659    13273   6230   6201   -503   -838   2839       N  
ATOM   4795  NH2 ARG A 659     -48.967 -56.911 -34.584  1.00 66.38           N  
ANISOU 4795  NH2 ARG A 659    12987   6076   6158  -1111   -414   2771       N  
ATOM   4796  N   ALA A 660     -41.375 -58.585 -39.364  1.00 73.87           N  
ANISOU 4796  N   ALA A 660    13578   6638   7852   1440  -1681   2158       N  
ATOM   4797  CA  ALA A 660     -39.979 -58.910 -39.597  1.00 74.63           C  
ANISOU 4797  CA  ALA A 660    13541   6777   8040   1907  -1900   2015       C  
ATOM   4798  C   ALA A 660     -39.164 -57.624 -39.642  1.00 73.68           C  
ANISOU 4798  C   ALA A 660    12886   7096   8012   1977  -1823   1858       C  
ATOM   4799  O   ALA A 660     -39.718 -56.528 -39.744  1.00 64.75           O  
ANISOU 4799  O   ALA A 660    11511   6198   6893   1680  -1593   1847       O  
ATOM   4800  CB  ALA A 660     -39.841 -59.698 -40.898  1.00 70.38           C  
ANISOU 4800  CB  ALA A 660    13038   6057   7648   2112  -1899   1866       C  
ATOM   4801  N   PRO A 661     -37.837 -57.722 -39.546  1.00 70.04           N  
ANISOU 4801  N   PRO A 661    12228   6751   7632   2367  -2025   1722       N  
ATOM   4802  CA  PRO A 661     -37.005 -56.519 -39.660  1.00 68.79           C  
ANISOU 4802  CA  PRO A 661    11527   7004   7604   2411  -1940   1552       C  
ATOM   4803  C   PRO A 661     -37.249 -55.781 -40.968  1.00 78.49           C  
ANISOU 4803  C   PRO A 661    12431   8417   8974   2252  -1613   1422       C  
ATOM   4804  O   PRO A 661     -37.660 -56.364 -41.975  1.00 65.67           O  
ANISOU 4804  O   PRO A 661    10937   6631   7382   2270  -1510   1385       O  
ATOM   4805  CB  PRO A 661     -35.578 -57.070 -39.584  1.00 72.42           C  
ANISOU 4805  CB  PRO A 661    11849   7501   8168   2897  -2216   1386       C  
ATOM   4806  CG  PRO A 661     -35.716 -58.299 -38.754  1.00 85.85           C  
ANISOU 4806  CG  PRO A 661    14094   8827   9699   3067  -2529   1548       C  
ATOM   4807  CD  PRO A 661     -37.049 -58.892 -39.114  1.00 81.02           C  
ANISOU 4807  CD  PRO A 661    13898   7899   8989   2773  -2375   1725       C  
ATOM   4808  N   LEU A 662     -36.995 -54.476 -40.935  1.00 73.15           N  
ANISOU 4808  N   LEU A 662    11356   8066   8370   2096  -1464   1352       N  
ATOM   4809  CA  LEU A 662     -37.284 -53.626 -42.078  1.00 66.76           C  
ANISOU 4809  CA  LEU A 662    10284   7424   7656   1907  -1152   1264       C  
ATOM   4810  C   LEU A 662     -36.392 -53.992 -43.261  1.00 69.48           C  
ANISOU 4810  C   LEU A 662    10421   7838   8141   2194  -1077   1073       C  
ATOM   4811  O   LEU A 662     -35.222 -54.343 -43.076  1.00 73.35           O  
ANISOU 4811  O   LEU A 662    10730   8415   8725   2518  -1237    946       O  
ATOM   4812  CB  LEU A 662     -37.078 -52.156 -41.713  1.00 65.50           C  
ANISOU 4812  CB  LEU A 662     9765   7568   7554   1697  -1042   1232       C  
ATOM   4813  CG  LEU A 662     -38.194 -51.475 -40.923  1.00 62.54           C  
ANISOU 4813  CG  LEU A 662     9533   7182   7045   1349  -1001   1376       C  
ATOM   4814  CD1 LEU A 662     -37.725 -50.135 -40.387  1.00 56.63           C  
ANISOU 4814  CD1 LEU A 662     8437   6714   6367   1229   -983   1314       C  
ATOM   4815  CD2 LEU A 662     -39.416 -51.301 -41.809  1.00 54.77           C  
ANISOU 4815  CD2 LEU A 662     8679   6104   6027   1096   -770   1413       C  
ATOM   4816  N   PRO A 663     -36.913 -53.926 -44.482  1.00 74.12           N  
ANISOU 4816  N   PRO A 663    11026   8400   8735   2103   -844   1030       N  
ATOM   4817  CA  PRO A 663     -36.059 -54.066 -45.663  1.00 79.47           C  
ANISOU 4817  CA  PRO A 663    11469   9209   9517   2346   -708    837       C  
ATOM   4818  C   PRO A 663     -35.090 -52.902 -45.751  1.00 86.47           C  
ANISOU 4818  C   PRO A 663    11858  10461  10536   2307   -551    727       C  
ATOM   4819  O   PRO A 663     -35.272 -51.884 -45.065  1.00 90.84           O  
ANISOU 4819  O   PRO A 663    12278  11138  11098   2049   -528    804       O  
ATOM   4820  CB  PRO A 663     -37.060 -54.047 -46.831  1.00 77.56           C  
ANISOU 4820  CB  PRO A 663    11409   8860   9202   2185   -491    847       C  
ATOM   4821  CG  PRO A 663     -38.397 -54.325 -46.215  1.00 75.34           C  
ANISOU 4821  CG  PRO A 663    11498   8318   8809   1934   -588   1024       C  
ATOM   4822  CD  PRO A 663     -38.329 -53.749 -44.839  1.00 72.85           C  
ANISOU 4822  CD  PRO A 663    11109   8094   8476   1788   -702   1138       C  
ATOM   4823  N   PRO A 664     -34.037 -53.017 -46.561  1.00 88.47           N  
ANISOU 4823  N   PRO A 664    11818  10895  10902   2551   -438    535       N  
ATOM   4824  CA  PRO A 664     -33.149 -51.868 -46.772  1.00 92.75           C  
ANISOU 4824  CA  PRO A 664    11869  11784  11588   2452   -230    429       C  
ATOM   4825  C   PRO A 664     -33.929 -50.660 -47.274  1.00 89.49           C  
ANISOU 4825  C   PRO A 664    11452  11434  11118   2052     52    538       C  
ATOM   4826  O   PRO A 664     -34.809 -50.777 -48.130  1.00 85.17           O  
ANISOU 4826  O   PRO A 664    11167  10752  10444   1961    194    594       O  
ATOM   4827  CB  PRO A 664     -32.154 -52.378 -47.819  1.00 94.28           C  
ANISOU 4827  CB  PRO A 664    11830  12126  11865   2764    -87    209       C  
ATOM   4828  CG  PRO A 664     -32.129 -53.853 -47.609  1.00 94.09           C  
ANISOU 4828  CG  PRO A 664    12101  11852  11797   3135   -383    162       C  
ATOM   4829  CD  PRO A 664     -33.533 -54.233 -47.221  1.00 90.69           C  
ANISOU 4829  CD  PRO A 664    12186  11075  11195   2942   -512    386       C  
ATOM   4830  N   LYS A 665     -33.596 -49.491 -46.719  1.00 94.03           N  
ANISOU 4830  N   LYS A 665    11736  12199  11794   1828     99    553       N  
ATOM   4831  CA  LYS A 665     -34.386 -48.288 -46.969  1.00 97.72           C  
ANISOU 4831  CA  LYS A 665    12239  12683  12208   1451    294    666       C  
ATOM   4832  C   LYS A 665     -34.419 -47.928 -48.450  1.00103.73           C  
ANISOU 4832  C   LYS A 665    12980  13508  12923   1385    638    635       C  
ATOM   4833  O   LYS A 665     -35.444 -47.457 -48.957  1.00102.64           O  
ANISOU 4833  O   LYS A 665    13083  13259  12656   1177    751    737       O  
ATOM   4834  CB  LYS A 665     -33.834 -47.125 -46.144  1.00 98.17           C  
ANISOU 4834  CB  LYS A 665    11962  12928  12409   1257    267    652       C  
ATOM   4835  CG  LYS A 665     -32.376 -47.292 -45.742  1.00103.96           C  
ANISOU 4835  CG  LYS A 665    12279  13873  13347   1477    171    476       C  
ATOM   4836  CD  LYS A 665     -31.802 -46.001 -45.180  1.00107.61           C  
ANISOU 4836  CD  LYS A 665    12369  14532  13984   1240    194    432       C  
ATOM   4837  CE  LYS A 665     -32.632 -45.474 -44.021  1.00105.70           C  
ANISOU 4837  CE  LYS A 665    12324  14179  13657   1049    -23    558       C  
ATOM   4838  NZ  LYS A 665     -32.092 -44.189 -43.492  1.00104.66           N  
ANISOU 4838  NZ  LYS A 665    11848  14215  13704    821    -23    495       N  
ATOM   4839  N   ASP A 666     -33.312 -48.151 -49.162  1.00112.97           N  
ANISOU 4839  N   ASP A 666    13873  14867  14185   1576    805    481       N  
ATOM   4840  CA  ASP A 666     -33.239 -47.763 -50.566  1.00118.97           C  
ANISOU 4840  CA  ASP A 666    14616  15719  14869   1513   1166    455       C  
ATOM   4841  C   ASP A 666     -34.133 -48.610 -51.461  1.00120.11           C  
ANISOU 4841  C   ASP A 666    15179  15652  14805   1649   1182    475       C  
ATOM   4842  O   ASP A 666     -34.485 -48.166 -52.559  1.00123.18           O  
ANISOU 4842  O   ASP A 666    15691  16052  15059   1546   1437    502       O  
ATOM   4843  CB  ASP A 666     -31.795 -47.856 -51.062  1.00130.00           C  
ANISOU 4843  CB  ASP A 666    15581  17400  16411   1691   1364    262       C  
ATOM   4844  CG  ASP A 666     -30.834 -47.050 -50.217  1.00135.84           C  
ANISOU 4844  CG  ASP A 666    15856  18360  17398   1560   1337    200       C  
ATOM   4845  OD1 ASP A 666     -30.409 -47.556 -49.156  1.00138.24           O  
ANISOU 4845  OD1 ASP A 666    16035  18666  17825   1744   1020    125       O  
ATOM   4846  OD2 ASP A 666     -30.498 -45.915 -50.616  1.00137.16           O  
ANISOU 4846  OD2 ASP A 666    15798  18682  17633   1273   1619    223       O  
ATOM   4847  N   GLN A 667     -34.514 -49.807 -51.021  1.00111.02           N  
ANISOU 4847  N   GLN A 667    14270  14293  13618   1873    903    463       N  
ATOM   4848  CA  GLN A 667     -35.160 -50.771 -51.902  1.00103.19           C  
ANISOU 4848  CA  GLN A 667    13631  13103  12472   2051    894    429       C  
ATOM   4849  C   GLN A 667     -36.675 -50.820 -51.764  1.00 92.59           C  
ANISOU 4849  C   GLN A 667    12690  11486  11004   1856    767    569       C  
ATOM   4850  O   GLN A 667     -37.357 -51.162 -52.736  1.00 92.13           O  
ANISOU 4850  O   GLN A 667    12897  11299  10810   1897    832    543       O  
ATOM   4851  CB  GLN A 667     -34.587 -52.171 -51.654  1.00103.07           C  
ANISOU 4851  CB  GLN A 667    13652  12998  12512   2444    668    299       C  
ATOM   4852  CG  GLN A 667     -33.067 -52.229 -51.735  1.00102.46           C  
ANISOU 4852  CG  GLN A 667    13135  13209  12585   2688    756    109       C  
ATOM   4853  CD  GLN A 667     -32.519 -53.629 -51.541  1.00 99.00           C  
ANISOU 4853  CD  GLN A 667    12758  12662  12198   3126    497    -44       C  
ATOM   4854  OE1 GLN A 667     -33.260 -54.611 -51.591  1.00 96.46           O  
ANISOU 4854  OE1 GLN A 667    12842  12032  11778   3250    299    -11       O  
ATOM   4855  NE2 GLN A 667     -31.213 -53.727 -51.316  1.00 99.64           N  
ANISOU 4855  NE2 GLN A 667    12428  12985  12445   3364    483   -229       N  
ATOM   4856  N   ASN A 668     -37.227 -50.491 -50.597  1.00 81.12           N  
ANISOU 4856  N   ASN A 668    11277   9953   9591   1651    588    696       N  
ATOM   4857  CA  ASN A 668     -38.664 -50.624 -50.343  1.00 73.63           C  
ANISOU 4857  CA  ASN A 668    10666   8763   8546   1467    465    804       C  
ATOM   4858  C   ASN A 668     -39.186 -49.403 -49.599  1.00 70.97           C  
ANISOU 4858  C   ASN A 668    10243   8498   8224   1139    476    916       C  
ATOM   4859  O   ASN A 668     -39.522 -49.476 -48.412  1.00 74.08           O  
ANISOU 4859  O   ASN A 668    10678   8830   8639   1045    295    996       O  
ATOM   4860  CB  ASN A 668     -38.954 -51.902 -49.552  1.00 72.37           C  
ANISOU 4860  CB  ASN A 668    10741   8364   8391   1603    187    835       C  
ATOM   4861  CG  ASN A 668     -38.736 -53.159 -50.369  1.00 68.44           C  
ANISOU 4861  CG  ASN A 668    10421   7716   7867   1915    138    717       C  
ATOM   4862  OD1 ASN A 668     -37.609 -53.633 -50.511  1.00 60.19           O  
ANISOU 4862  OD1 ASN A 668     9213   6771   6886   2206    124    601       O  
ATOM   4863  ND2 ASN A 668     -39.819 -53.711 -50.905  1.00 65.07           N  
ANISOU 4863  ND2 ASN A 668    10316   7049   7357   1867     95    719       N  
ATOM   4864  N   PRO A 669     -39.292 -48.255 -50.280  1.00 65.41           N  
ANISOU 4864  N   PRO A 669     9449   7912   7491    966    685    922       N  
ATOM   4865  CA  PRO A 669     -39.875 -47.074 -49.616  1.00 58.56           C  
ANISOU 4865  CA  PRO A 669     8531   7081   6637    671    670   1008       C  
ATOM   4866  C   PRO A 669     -41.333 -47.264 -49.232  1.00 55.22           C  
ANISOU 4866  C   PRO A 669     8380   6466   6134    532    528   1060       C  
ATOM   4867  O   PRO A 669     -41.746 -46.869 -48.129  1.00 59.44           O  
ANISOU 4867  O   PRO A 669     8884   7008   6692    372    412   1119       O  
ATOM   4868  CB  PRO A 669     -39.706 -45.963 -50.665  1.00 61.02           C  
ANISOU 4868  CB  PRO A 669     8773   7501   6913    555    921   1002       C  
ATOM   4869  CG  PRO A 669     -38.671 -46.470 -51.621  1.00 64.69           C  
ANISOU 4869  CG  PRO A 669     9135   8072   7373    777   1101    916       C  
ATOM   4870  CD  PRO A 669     -38.846 -47.953 -51.651  1.00 66.34           C  
ANISOU 4870  CD  PRO A 669     9526   8132   7547   1036    944    855       C  
ATOM   4871  N   ILE A 670     -42.126 -47.860 -50.126  1.00 48.20           N  
ANISOU 4871  N   ILE A 670     7743   5418   5153    590    537   1021       N  
ATOM   4872  CA  ILE A 670     -43.531 -48.121 -49.829  1.00 48.23           C  
ANISOU 4872  CA  ILE A 670     7968   5246   5112    451    409   1037       C  
ATOM   4873  C   ILE A 670     -43.657 -48.995 -48.589  1.00 54.86           C  
ANISOU 4873  C   ILE A 670     8867   5989   5988    444    233   1101       C  
ATOM   4874  O   ILE A 670     -44.506 -48.752 -47.722  1.00 55.66           O  
ANISOU 4874  O   ILE A 670     9009   6060   6078    244    159   1152       O  
ATOM   4875  CB  ILE A 670     -44.218 -48.764 -51.047  1.00 48.79           C  
ANISOU 4875  CB  ILE A 670     8282   5155   5100    551    420    950       C  
ATOM   4876  CG1 ILE A 670     -44.119 -47.844 -52.267  1.00 56.08           C  
ANISOU 4876  CG1 ILE A 670     9203   6168   5935    562    593    906       C  
ATOM   4877  CG2 ILE A 670     -45.669 -49.079 -50.739  1.00 49.72           C  
ANISOU 4877  CG2 ILE A 670     8580   5098   5211    391    286    936       C  
ATOM   4878  CD1 ILE A 670     -44.700 -48.444 -53.533  1.00 58.76           C  
ANISOU 4878  CD1 ILE A 670     9796   6367   6164    704    589    800       C  
ATOM   4879  N   HIS A 671     -42.804 -50.019 -48.479  1.00 56.79           N  
ANISOU 4879  N   HIS A 671     9130   6185   6262    673    164   1095       N  
ATOM   4880  CA  HIS A 671     -42.843 -50.898 -47.316  1.00 54.76           C  
ANISOU 4880  CA  HIS A 671     8991   5804   6013    692    -19   1177       C  
ATOM   4881  C   HIS A 671     -42.495 -50.141 -46.043  1.00 55.71           C  
ANISOU 4881  C   HIS A 671     8934   6085   6149    575    -70   1254       C  
ATOM   4882  O   HIS A 671     -43.076 -50.397 -44.985  1.00 58.54           O  
ANISOU 4882  O   HIS A 671     9423   6364   6455    449   -180   1346       O  
ATOM   4883  CB  HIS A 671     -41.888 -52.076 -47.515  1.00 54.81           C  
ANISOU 4883  CB  HIS A 671     9057   5719   6050   1012   -113   1135       C  
ATOM   4884  CG  HIS A 671     -41.996 -53.129 -46.457  1.00 62.74           C  
ANISOU 4884  CG  HIS A 671    10282   6521   7034   1056   -326   1232       C  
ATOM   4885  ND1 HIS A 671     -41.551 -52.938 -45.166  1.00 66.49           N  
ANISOU 4885  ND1 HIS A 671    10689   7074   7499   1036   -443   1324       N  
ATOM   4886  CD2 HIS A 671     -42.493 -54.387 -46.500  1.00 68.23           C  
ANISOU 4886  CD2 HIS A 671    11300   6918   7707   1117   -453   1257       C  
ATOM   4887  CE1 HIS A 671     -41.773 -54.032 -44.460  1.00 69.66           C  
ANISOU 4887  CE1 HIS A 671    11386   7235   7847   1085   -622   1420       C  
ATOM   4888  NE2 HIS A 671     -42.344 -54.927 -45.246  1.00 71.81           N  
ANISOU 4888  NE2 HIS A 671    11897   7265   8123   1121   -627   1386       N  
ATOM   4889  N   HIS A 672     -41.547 -49.206 -46.121  1.00 59.08           N  
ANISOU 4889  N   HIS A 672     9068   6738   6642    605     13   1212       N  
ATOM   4890  CA  HIS A 672     -41.208 -48.410 -44.946  1.00 60.73           C  
ANISOU 4890  CA  HIS A 672     9098   7100   6878    497    -58   1255       C  
ATOM   4891  C   HIS A 672     -42.379 -47.538 -44.509  1.00 61.83           C  
ANISOU 4891  C   HIS A 672     9287   7249   6957    210    -32   1294       C  
ATOM   4892  O   HIS A 672     -42.681 -47.455 -43.312  1.00 64.49           O  
ANISOU 4892  O   HIS A 672     9661   7602   7240    113   -143   1354       O  
ATOM   4893  CB  HIS A 672     -39.975 -47.554 -45.227  1.00 60.90           C  
ANISOU 4893  CB  HIS A 672     8772   7348   7019    556     36   1179       C  
ATOM   4894  CG  HIS A 672     -38.682 -48.295 -45.087  1.00 63.71           C  
ANISOU 4894  CG  HIS A 672     8987   7762   7458    841    -54   1117       C  
ATOM   4895  ND1 HIS A 672     -37.832 -48.111 -44.018  1.00 62.91           N  
ANISOU 4895  ND1 HIS A 672     8689   7785   7429    910   -214   1099       N  
ATOM   4896  CD2 HIS A 672     -38.095 -49.225 -45.877  1.00 65.19           C  
ANISOU 4896  CD2 HIS A 672     9193   7905   7671   1102    -28   1041       C  
ATOM   4897  CE1 HIS A 672     -36.775 -48.891 -44.158  1.00 63.55           C  
ANISOU 4897  CE1 HIS A 672     8659   7898   7588   1206   -290   1010       C  
ATOM   4898  NE2 HIS A 672     -36.911 -49.578 -45.277  1.00 65.48           N  
ANISOU 4898  NE2 HIS A 672     9030   8045   7806   1329   -172    972       N  
ATOM   4899  N   ALA A 673     -43.056 -46.884 -45.459  1.00 59.54           N  
ANISOU 4899  N   ALA A 673     9010   6953   6659     91    103   1248       N  
ATOM   4900  CA  ALA A 673     -44.209 -46.060 -45.098  1.00 58.44           C  
ANISOU 4900  CA  ALA A 673     8906   6823   6475   -146    106   1247       C  
ATOM   4901  C   ALA A 673     -45.321 -46.910 -44.490  1.00 57.58           C  
ANISOU 4901  C   ALA A 673     9017   6570   6289   -236     26   1287       C  
ATOM   4902  O   ALA A 673     -45.912 -46.552 -43.459  1.00 63.15           O  
ANISOU 4902  O   ALA A 673     9720   7329   6945   -395    -19   1313       O  
ATOM   4903  CB  ALA A 673     -44.716 -45.299 -46.324  1.00 55.55           C  
ANISOU 4903  CB  ALA A 673     8554   6447   6106   -206    229   1178       C  
ATOM   4904  N   ALA A 674     -45.610 -48.054 -45.117  1.00 55.40           N  
ANISOU 4904  N   ALA A 674     8936   6110   6002   -146     17   1285       N  
ATOM   4905  CA  ALA A 674     -46.596 -48.977 -44.566  1.00 56.38           C  
ANISOU 4905  CA  ALA A 674     9277   6067   6077   -260    -45   1333       C  
ATOM   4906  C   ALA A 674     -46.194 -49.473 -43.183  1.00 59.24           C  
ANISOU 4906  C   ALA A 674     9706   6427   6376   -257   -147   1458       C  
ATOM   4907  O   ALA A 674     -47.062 -49.741 -42.345  1.00 62.56           O  
ANISOU 4907  O   ALA A 674    10254   6795   6721   -442   -158   1520       O  
ATOM   4908  CB  ALA A 674     -46.804 -50.156 -45.518  1.00 53.64           C  
ANISOU 4908  CB  ALA A 674     9134   5495   5753   -143    -64   1298       C  
ATOM   4909  N   ALA A 675     -44.891 -49.600 -42.923  1.00 60.17           N  
ANISOU 4909  N   ALA A 675     9739   6608   6514    -46   -223   1488       N  
ATOM   4910  CA  ALA A 675     -44.422 -50.022 -41.608  1.00 60.19           C  
ANISOU 4910  CA  ALA A 675     9823   6609   6435      3   -363   1597       C  
ATOM   4911  C   ALA A 675     -44.574 -48.924 -40.568  1.00 57.29           C  
ANISOU 4911  C   ALA A 675     9313   6448   6008   -153   -366   1606       C  
ATOM   4912  O   ALA A 675     -44.861 -49.222 -39.404  1.00 47.75           O  
ANISOU 4912  O   ALA A 675     8258   5220   4664   -227   -439   1705       O  
ATOM   4913  CB  ALA A 675     -42.960 -50.463 -41.685  1.00 49.40           C  
ANISOU 4913  CB  ALA A 675     8375   5263   5131    315   -479   1580       C  
ATOM   4914  N   SER A 676     -44.397 -47.660 -40.961  1.00 54.55           N  
ANISOU 4914  N   SER A 676     8701   6283   5742   -207   -290   1506       N  
ATOM   4915  CA  SER A 676     -44.666 -46.568 -40.032  1.00 55.44           C  
ANISOU 4915  CA  SER A 676     8690   6569   5805   -359   -305   1485       C  
ATOM   4916  C   SER A 676     -46.144 -46.507 -39.678  1.00 51.48           C  
ANISOU 4916  C   SER A 676     8320   6037   5203   -595   -232   1489       C  
ATOM   4917  O   SER A 676     -46.501 -46.259 -38.521  1.00 48.96           O  
ANISOU 4917  O   SER A 676     8035   5807   4760   -698   -266   1520       O  
ATOM   4918  CB  SER A 676     -44.201 -45.238 -40.625  1.00 59.07           C  
ANISOU 4918  CB  SER A 676     8872   7180   6391   -380   -244   1376       C  
ATOM   4919  OG  SER A 676     -45.000 -44.868 -41.735  1.00 63.90           O  
ANISOU 4919  OG  SER A 676     9500   7737   7043   -476   -114   1315       O  
ATOM   4920  N   VAL A 677     -47.022 -46.737 -40.657  1.00 53.56           N  
ANISOU 4920  N   VAL A 677     8648   6189   5515   -674   -132   1440       N  
ATOM   4921  CA  VAL A 677     -48.454 -46.742 -40.361  1.00 49.79           C  
ANISOU 4921  CA  VAL A 677     8249   5693   4975   -900    -61   1408       C  
ATOM   4922  C   VAL A 677     -48.811 -47.925 -39.467  1.00 55.13           C  
ANISOU 4922  C   VAL A 677     9172   6247   5527   -977    -73   1545       C  
ATOM   4923  O   VAL A 677     -49.472 -47.767 -38.429  1.00 57.20           O  
ANISOU 4923  O   VAL A 677     9472   6597   5666  -1147    -33   1572       O  
ATOM   4924  CB  VAL A 677     -49.272 -46.752 -41.663  1.00 47.01           C  
ANISOU 4924  CB  VAL A 677     7900   5242   4719   -943     10   1296       C  
ATOM   4925  CG1 VAL A 677     -50.710 -47.112 -41.375  1.00 44.43           C  
ANISOU 4925  CG1 VAL A 677     7650   4868   4362  -1166     72   1252       C  
ATOM   4926  CG2 VAL A 677     -49.192 -45.401 -42.334  1.00 43.59           C  
ANISOU 4926  CG2 VAL A 677     7274   4932   4355   -922     29   1174       C  
ATOM   4927  N   PHE A 678     -48.383 -49.129 -39.860  1.00 57.18           N  
ANISOU 4927  N   PHE A 678     9623   6294   5809   -852   -124   1632       N  
ATOM   4928  CA  PHE A 678     -48.664 -50.323 -39.070  1.00 60.85           C  
ANISOU 4928  CA  PHE A 678    10383   6581   6155   -924   -150   1788       C  
ATOM   4929  C   PHE A 678     -48.148 -50.176 -37.646  1.00 62.14           C  
ANISOU 4929  C   PHE A 678    10613   6857   6141   -900   -227   1905       C  
ATOM   4930  O   PHE A 678     -48.797 -50.619 -36.693  1.00 63.51           O  
ANISOU 4930  O   PHE A 678    10990   6990   6151  -1077   -179   2018       O  
ATOM   4931  CB  PHE A 678     -48.045 -51.551 -39.740  1.00 61.59           C  
ANISOU 4931  CB  PHE A 678    10673   6415   6312   -725   -245   1846       C  
ATOM   4932  CG  PHE A 678     -48.272 -52.834 -38.991  1.00 61.74           C  
ANISOU 4932  CG  PHE A 678    11054   6188   6215   -789   -297   2023       C  
ATOM   4933  CD1 PHE A 678     -49.422 -53.577 -39.199  1.00 61.53           C  
ANISOU 4933  CD1 PHE A 678    11206   5960   6211  -1030   -204   2044       C  
ATOM   4934  CD2 PHE A 678     -47.335 -53.300 -38.084  1.00 61.34           C  
ANISOU 4934  CD2 PHE A 678    11178   6091   6037   -610   -452   2166       C  
ATOM   4935  CE1 PHE A 678     -49.635 -54.758 -38.510  1.00 61.63           C  
ANISOU 4935  CE1 PHE A 678    11586   5713   6119  -1125   -238   2229       C  
ATOM   4936  CE2 PHE A 678     -47.543 -54.478 -37.394  1.00 63.13           C  
ANISOU 4936  CE2 PHE A 678    11799   6054   6132   -667   -511   2353       C  
ATOM   4937  CZ  PHE A 678     -48.695 -55.208 -37.609  1.00 63.75           C  
ANISOU 4937  CZ  PHE A 678    12075   5916   6232   -941   -391   2397       C  
ATOM   4938  N   ARG A 679     -46.983 -49.550 -37.481  1.00 63.16           N  
ANISOU 4938  N   ARG A 679    10574   7131   6292   -689   -345   1873       N  
ATOM   4939  CA  ARG A 679     -46.431 -49.365 -36.146  1.00 65.86           C  
ANISOU 4939  CA  ARG A 679    10972   7587   6466   -629   -463   1953       C  
ATOM   4940  C   ARG A 679     -47.192 -48.302 -35.369  1.00 63.15           C  
ANISOU 4940  C   ARG A 679    10510   7469   6016   -836   -372   1890       C  
ATOM   4941  O   ARG A 679     -47.326 -48.410 -34.146  1.00 64.99           O  
ANISOU 4941  O   ARG A 679    10905   7758   6029   -888   -403   1982       O  
ATOM   4942  CB  ARG A 679     -44.952 -49.002 -36.243  1.00 70.76           C  
ANISOU 4942  CB  ARG A 679    11399   8303   7183   -344   -632   1896       C  
ATOM   4943  CG  ARG A 679     -44.176 -49.234 -34.968  1.00 82.04           C  
ANISOU 4943  CG  ARG A 679    12957   9771   8445   -189   -836   1983       C  
ATOM   4944  CD  ARG A 679     -42.694 -49.386 -35.259  1.00 91.12           C  
ANISOU 4944  CD  ARG A 679    13955  10935   9733    135  -1027   1921       C  
ATOM   4945  NE  ARG A 679     -42.418 -50.493 -36.175  1.00 96.55           N  
ANISOU 4945  NE  ARG A 679    14766  11398  10520    290  -1040   1949       N  
ATOM   4946  CZ  ARG A 679     -42.113 -50.344 -37.462  1.00 95.40           C  
ANISOU 4946  CZ  ARG A 679    14403  11263  10583    357   -944   1832       C  
ATOM   4947  NH1 ARG A 679     -42.040 -49.130 -37.990  1.00 95.13           N  
ANISOU 4947  NH1 ARG A 679    14035  11432  10678    263   -822   1703       N  
ATOM   4948  NH2 ARG A 679     -41.880 -51.408 -38.220  1.00 95.26           N  
ANISOU 4948  NH2 ARG A 679    14526  11040  10627    522   -971   1843       N  
ATOM   4949  N   GLU A 680     -47.696 -47.272 -36.054  1.00 56.97           N  
ANISOU 4949  N   GLU A 680     9467   6811   5367   -936   -270   1727       N  
ATOM   4950  CA  GLU A 680     -48.522 -46.280 -35.374  1.00 58.18           C  
ANISOU 4950  CA  GLU A 680     9506   7167   5431  -1115   -193   1632       C  
ATOM   4951  C   GLU A 680     -49.806 -46.906 -34.846  1.00 60.85           C  
ANISOU 4951  C   GLU A 680    10032   7464   5623  -1358    -37   1691       C  
ATOM   4952  O   GLU A 680     -50.219 -46.636 -33.712  1.00 60.93           O  
ANISOU 4952  O   GLU A 680    10094   7622   5436  -1465      7   1706       O  
ATOM   4953  CB  GLU A 680     -48.840 -45.118 -36.318  1.00 57.06           C  
ANISOU 4953  CB  GLU A 680     9091   7118   5471  -1151   -142   1444       C  
ATOM   4954  CG  GLU A 680     -49.711 -44.030 -35.703  1.00 56.47           C  
ANISOU 4954  CG  GLU A 680     8882   7242   5330  -1299    -88   1303       C  
ATOM   4955  CD  GLU A 680     -48.996 -43.252 -34.616  1.00 61.91           C  
ANISOU 4955  CD  GLU A 680     9500   8107   5915  -1218   -214   1282       C  
ATOM   4956  OE1 GLU A 680     -47.749 -43.183 -34.653  1.00 63.42           O  
ANISOU 4956  OE1 GLU A 680     9639   8285   6172  -1045   -354   1320       O  
ATOM   4957  OE2 GLU A 680     -49.682 -42.711 -33.722  1.00 67.27           O  
ANISOU 4957  OE2 GLU A 680    10161   8948   6452  -1322   -177   1204       O  
ATOM   4958  N   ALA A 681     -50.447 -47.755 -35.649  1.00 60.42           N  
ANISOU 4958  N   ALA A 681    10078   7217   5664  -1456     55   1714       N  
ATOM   4959  CA  ALA A 681     -51.692 -48.383 -35.224  1.00 61.80           C  
ANISOU 4959  CA  ALA A 681    10396   7343   5744  -1730    225   1756       C  
ATOM   4960  C   ALA A 681     -51.480 -49.593 -34.321  1.00 65.87           C  
ANISOU 4960  C   ALA A 681    11282   7690   6055  -1768    217   2001       C  
ATOM   4961  O   ALA A 681     -52.432 -50.022 -33.659  1.00 65.98           O  
ANISOU 4961  O   ALA A 681    11437   7700   5933  -2030    386   2068       O  
ATOM   4962  CB  ALA A 681     -52.514 -48.796 -36.447  1.00 60.69           C  
ANISOU 4962  CB  ALA A 681    10205   7048   5806  -1836    305   1656       C  
ATOM   4963  N   ASP A 682     -50.264 -50.141 -34.261  1.00 66.61           N  
ANISOU 4963  N   ASP A 682    11540   7646   6121  -1514     27   2132       N  
ATOM   4964  CA  ASP A 682     -50.040 -51.391 -33.542  1.00 68.77           C  
ANISOU 4964  CA  ASP A 682    12226   7693   6211  -1512    -23   2372       C  
ATOM   4965  C   ASP A 682     -50.027 -51.199 -32.032  1.00 72.65           C  
ANISOU 4965  C   ASP A 682    12840   8344   6421  -1542    -15   2459       C  
ATOM   4966  O   ASP A 682     -50.326 -52.143 -31.292  1.00 75.44           O  
ANISOU 4966  O   ASP A 682    13427   8571   6664  -1606     38   2585       O  
ATOM   4967  CB  ASP A 682     -48.728 -52.035 -33.998  1.00 67.60           C  
ANISOU 4967  CB  ASP A 682    12187   7353   6144  -1174   -263   2436       C  
ATOM   4968  CG  ASP A 682     -48.568 -53.459 -33.493  1.00 71.74           C  
ANISOU 4968  CG  ASP A 682    13080   7598   6580  -1120   -337   2616       C  
ATOM   4969  OD1 ASP A 682     -49.587 -54.176 -33.394  1.00 69.14           O  
ANISOU 4969  OD1 ASP A 682    12858   7144   6269  -1363   -171   2649       O  
ATOM   4970  OD2 ASP A 682     -47.424 -53.862 -33.194  1.00 77.79           O  
ANISOU 4970  OD2 ASP A 682    13990   8279   7288   -823   -570   2692       O  
ATOM   4971  N   GLN A 683     -49.689 -49.998 -31.556  1.00 71.00           N  
ANISOU 4971  N   GLN A 683    12439   8415   6123  -1473    -71   2361       N  
ATOM   4972  CA  GLN A 683     -49.658 -49.744 -30.121  1.00 71.33           C  
ANISOU 4972  CA  GLN A 683    12622   8623   5856  -1482    -82   2429       C  
ATOM   4973  C   GLN A 683     -51.047 -49.712 -29.496  1.00 77.35           C  
ANISOU 4973  C   GLN A 683    13367   9510   6514  -1790    210   2392       C  
ATOM   4974  O   GLN A 683     -51.152 -49.665 -28.264  1.00 78.33           O  
ANISOU 4974  O   GLN A 683    13618   9760   6382  -1799    247   2446       O  
ATOM   4975  CB  GLN A 683     -48.921 -48.434 -29.836  1.00 63.61           C  
ANISOU 4975  CB  GLN A 683    11371   7915   4885  -1295   -242   2264       C  
ATOM   4976  CG  GLN A 683     -49.388 -47.254 -30.667  1.00 59.58           C  
ANISOU 4976  CG  GLN A 683    10437   7577   4623  -1371   -151   2012       C  
ATOM   4977  CD  GLN A 683     -48.573 -46.000 -30.408  1.00 64.12           C  
ANISOU 4977  CD  GLN A 683    10750   8365   5246  -1189   -328   1850       C  
ATOM   4978  OE1 GLN A 683     -48.080 -45.785 -29.301  1.00 68.03           O  
ANISOU 4978  OE1 GLN A 683    11348   8977   5524  -1083   -460   1878       O  
ATOM   4979  NE2 GLN A 683     -48.423 -45.168 -31.433  1.00 66.39           N  
ANISOU 4979  NE2 GLN A 683    10718   8691   5815  -1154   -341   1679       N  
ATOM   4980  N   TRP A 684     -52.105 -49.745 -30.304  1.00 76.40           N  
ANISOU 4980  N   TRP A 684    13091   9362   6575  -2031    411   2293       N  
ATOM   4981  CA  TRP A 684     -53.476 -49.794 -29.819  1.00 78.77           C  
ANISOU 4981  CA  TRP A 684    13338   9777   6814  -2339    696   2235       C  
ATOM   4982  C   TRP A 684     -54.055 -51.187 -30.033  1.00 85.61           C  
ANISOU 4982  C   TRP A 684    14386  10361   7783  -2496    809   2352       C  
ATOM   4983  O   TRP A 684     -53.807 -51.821 -31.064  1.00 86.14           O  
ANISOU 4983  O   TRP A 684    14490  10176   8062  -2439    717   2373       O  
ATOM   4984  CB  TRP A 684     -54.352 -48.765 -30.536  1.00 69.50           C  
ANISOU 4984  CB  TRP A 684    11827   8806   5774  -2517    828   1995       C  
ATOM   4985  CG  TRP A 684     -53.795 -47.384 -30.525  1.00 67.41           C  
ANISOU 4985  CG  TRP A 684    11307   8782   5523  -2316    679   1819       C  
ATOM   4986  CD1 TRP A 684     -53.018 -46.808 -31.485  1.00 62.56           C  
ANISOU 4986  CD1 TRP A 684    10490   8126   5153  -2084    482   1711       C  
ATOM   4987  CD2 TRP A 684     -53.976 -46.394 -29.506  1.00 71.60           C  
ANISOU 4987  CD2 TRP A 684    11733   9623   5849  -2313    712   1702       C  
ATOM   4988  NE1 TRP A 684     -52.700 -45.522 -31.127  1.00 63.76           N  
ANISOU 4988  NE1 TRP A 684    10423   8517   5285  -1958    384   1546       N  
ATOM   4989  CE2 TRP A 684     -53.276 -45.243 -29.915  1.00 68.31           C  
ANISOU 4989  CE2 TRP A 684    11054   9309   5591  -2079    504   1525       C  
ATOM   4990  CE3 TRP A 684     -54.661 -46.370 -28.288  1.00 77.83           C  
ANISOU 4990  CE3 TRP A 684    12635  10612   6326  -2488    905   1725       C  
ATOM   4991  CZ2 TRP A 684     -53.241 -44.080 -29.150  1.00 65.76           C  
ANISOU 4991  CZ2 TRP A 684    10582   9257   5146  -2006    450   1359       C  
ATOM   4992  CZ3 TRP A 684     -54.625 -45.214 -27.528  1.00 76.84           C  
ANISOU 4992  CZ3 TRP A 684    12354  10785   6054  -2391    862   1550       C  
ATOM   4993  CH2 TRP A 684     -53.919 -44.085 -27.962  1.00 70.98           C  
ANISOU 4993  CH2 TRP A 684    11355  10116   5498  -2147    619   1363       C  
ATOM   4994  N   ASP A 685     -54.832 -51.656 -29.059  1.00 90.93           N  
ANISOU 4994  N   ASP A 685    15177  11074   8296  -2698   1011   2423       N  
ATOM   4995  CA  ASP A 685     -55.558 -52.906 -29.221  1.00 97.76           C  
ANISOU 4995  CA  ASP A 685    16192  11691   9262  -2915   1149   2518       C  
ATOM   4996  C   ASP A 685     -56.766 -52.691 -30.125  1.00 95.12           C  
ANISOU 4996  C   ASP A 685    15569  11405   9167  -3196   1336   2314       C  
ATOM   4997  O   ASP A 685     -57.324 -51.592 -30.203  1.00 91.59           O  
ANISOU 4997  O   ASP A 685    14826  11245   8727  -3285   1440   2109       O  
ATOM   4998  CB  ASP A 685     -56.003 -53.460 -27.867  1.00109.85           C  
ANISOU 4998  CB  ASP A 685    17948  13254  10535  -3061   1321   2672       C  
ATOM   4999  CG  ASP A 685     -57.099 -52.630 -27.228  1.00115.48           C  
ANISOU 4999  CG  ASP A 685    18431  14315  11133  -3302   1603   2519       C  
ATOM   5000  OD1 ASP A 685     -57.075 -51.391 -27.378  1.00115.80           O  
ANISOU 5000  OD1 ASP A 685    18203  14627  11167  -3232   1580   2325       O  
ATOM   5001  OD2 ASP A 685     -57.987 -53.219 -26.577  1.00119.79           O  
ANISOU 5001  OD2 ASP A 685    19059  14862  11592  -3562   1849   2586       O  
ATOM   5002  N   GLU A 686     -57.174 -53.758 -30.810  1.00 95.12           N  
ANISOU 5002  N   GLU A 686    15659  11119   9363  -3330   1362   2355       N  
ATOM   5003  CA  GLU A 686     -58.188 -53.636 -31.851  1.00 92.56           C  
ANISOU 5003  CA  GLU A 686    15071  10795   9302  -3556   1474   2146       C  
ATOM   5004  C   GLU A 686     -59.617 -53.735 -31.335  1.00 91.97           C  
ANISOU 5004  C   GLU A 686    14842  10870   9231  -3933   1784   2049       C  
ATOM   5005  O   GLU A 686     -60.521 -53.158 -31.949  1.00 89.50           O  
ANISOU 5005  O   GLU A 686    14202  10712   9090  -4108   1895   1799       O  
ATOM   5006  CB  GLU A 686     -57.975 -54.703 -32.927  1.00 94.92           C  
ANISOU 5006  CB  GLU A 686    15520  10714   9831  -3517   1334   2196       C  
ATOM   5007  CG  GLU A 686     -56.860 -54.389 -33.905  1.00 94.81           C  
ANISOU 5007  CG  GLU A 686    15515  10600   9910  -3187   1069   2177       C  
ATOM   5008  CD  GLU A 686     -57.101 -55.012 -35.264  1.00 99.84           C  
ANISOU 5008  CD  GLU A 686    16152  10965  10820  -3215    991   2090       C  
ATOM   5009  OE1 GLU A 686     -58.226 -55.503 -35.500  1.00100.93           O  
ANISOU 5009  OE1 GLU A 686    16219  11029  11101  -3513   1139   2002       O  
ATOM   5010  OE2 GLU A 686     -56.171 -55.010 -36.097  1.00104.05           O  
ANISOU 5010  OE2 GLU A 686    16748  11362  11425  -2939    783   2096       O  
ATOM   5011  N   LYS A 687     -59.850 -54.453 -30.237  1.00 97.12           N  
ANISOU 5011  N   LYS A 687    15715  11486   9702  -4061   1928   2228       N  
ATOM   5012  CA  LYS A 687     -61.217 -54.699 -29.794  1.00 96.74           C  
ANISOU 5012  CA  LYS A 687    15523  11554   9679  -4439   2243   2147       C  
ATOM   5013  C   LYS A 687     -61.905 -53.394 -29.410  1.00 89.62           C  
ANISOU 5013  C   LYS A 687    14257  11093   8702  -4524   2420   1898       C  
ATOM   5014  O   LYS A 687     -61.354 -52.577 -28.665  1.00 82.30           O  
ANISOU 5014  O   LYS A 687    13351  10388   7531  -4341   2381   1916       O  
ATOM   5015  CB  LYS A 687     -61.234 -55.684 -28.622  1.00 99.35           C  
ANISOU 5015  CB  LYS A 687    16202  11759   9787  -4547   2368   2420       C  
ATOM   5016  CG  LYS A 687     -60.436 -55.252 -27.403  1.00 98.09           C  
ANISOU 5016  CG  LYS A 687    16248  11756   9265  -4330   2322   2575       C  
ATOM   5017  CD  LYS A 687     -60.736 -56.150 -26.216  1.00102.44           C  
ANISOU 5017  CD  LYS A 687    17114  12227   9583  -4503   2508   2816       C  
ATOM   5018  CE  LYS A 687     -62.226 -56.171 -25.914  1.00107.01           C  
ANISOU 5018  CE  LYS A 687    17458  12990  10210  -4916   2886   2692       C  
ATOM   5019  NZ  LYS A 687     -62.563 -57.141 -24.838  1.00114.79           N  
ANISOU 5019  NZ  LYS A 687    18770  13864  10982  -5124   3091   2950       N  
ATOM   5020  N   GLY A 688     -63.113 -53.198 -29.935  1.00 91.22           N  
ANISOU 5020  N   GLY A 688    14111  11423   9125  -4791   2597   1639       N  
ATOM   5021  CA  GLY A 688     -63.843 -51.967 -29.711  1.00 91.75           C  
ANISOU 5021  CA  GLY A 688    13784  11911   9165  -4861   2749   1343       C  
ATOM   5022  C   GLY A 688     -63.369 -50.794 -30.534  1.00 89.70           C  
ANISOU 5022  C   GLY A 688    13310  11784   8987  -4638   2548   1145       C  
ATOM   5023  O   GLY A 688     -63.724 -49.652 -30.225  1.00 88.95           O  
ANISOU 5023  O   GLY A 688    12936  12048   8813  -4623   2626    917       O  
ATOM   5024  N   ASN A 689     -62.578 -51.036 -31.581  1.00 85.87           N  
ANISOU 5024  N   ASN A 689    12952  11022   8655  -4461   2293   1220       N  
ATOM   5025  CA  ASN A 689     -62.011 -49.950 -32.379  1.00 83.50           C  
ANISOU 5025  CA  ASN A 689    12498  10815   8413  -4247   2098   1077       C  
ATOM   5026  C   ASN A 689     -61.801 -50.476 -33.797  1.00 85.89           C  
ANISOU 5026  C   ASN A 689    12843  10796   8996  -4204   1919   1067       C  
ATOM   5027  O   ASN A 689     -60.794 -51.134 -34.074  1.00 86.12           O  
ANISOU 5027  O   ASN A 689    13178  10535   9008  -4007   1732   1295       O  
ATOM   5028  CB  ASN A 689     -60.709 -49.449 -31.770  1.00 79.77           C  
ANISOU 5028  CB  ASN A 689    12242  10387   7681  -3940   1927   1261       C  
ATOM   5029  CG  ASN A 689     -60.226 -48.158 -32.400  1.00 78.86           C  
ANISOU 5029  CG  ASN A 689    11887  10422   7654  -3655   1713   1060       C  
ATOM   5030  OD1 ASN A 689     -60.611 -47.812 -33.517  1.00 80.95           O  
ANISOU 5030  OD1 ASN A 689    11901  10653   8203  -3586   1608    831       O  
ATOM   5031  ND2 ASN A 689     -59.372 -47.438 -31.683  1.00 77.81           N  
ANISOU 5031  ND2 ASN A 689    11821  10437   7307  -3432   1603   1122       N  
ATOM   5032  N   ASP A 690     -62.746 -50.171 -34.685  1.00 94.59           N  
ANISOU 5032  N   ASP A 690    13597  11960  10384  -4281   1917    748       N  
ATOM   5033  CA  ASP A 690     -62.641 -50.600 -36.073  1.00102.33           C  
ANISOU 5033  CA  ASP A 690    14579  12656  11645  -4157   1701    671       C  
ATOM   5034  C   ASP A 690     -61.653 -49.762 -36.875  1.00 98.14           C  
ANISOU 5034  C   ASP A 690    14025  12115  11149  -3720   1404    621       C  
ATOM   5035  O   ASP A 690     -61.138 -50.242 -37.892  1.00100.10           O  
ANISOU 5035  O   ASP A 690    14407  12095  11531  -3555   1220    664       O  
ATOM   5036  CB  ASP A 690     -64.019 -50.559 -36.739  1.00112.93           C  
ANISOU 5036  CB  ASP A 690    15558  14074  13279  -4363   1766    319       C  
ATOM   5037  CG  ASP A 690     -65.041 -51.417 -36.014  1.00126.11           C  
ANISOU 5037  CG  ASP A 690    17205  15753  14956  -4849   2094    348       C  
ATOM   5038  OD1 ASP A 690     -64.649 -52.454 -35.439  1.00131.80           O  
ANISOU 5038  OD1 ASP A 690    18271  16256  15552  -4893   2145    656       O  
ATOM   5039  OD2 ASP A 690     -66.237 -51.053 -36.015  1.00129.79           O  
ANISOU 5039  OD2 ASP A 690    17276  16459  15579  -5050   2237     29       O  
ATOM   5040  N   LEU A 691     -61.375 -48.529 -36.441  1.00 86.23           N  
ANISOU 5040  N   LEU A 691    12357  10886   9522  -3538   1363    529       N  
ATOM   5041  CA  LEU A 691     -60.435 -47.677 -37.163  1.00 79.48           C  
ANISOU 5041  CA  LEU A 691    11479  10017   8703  -3167   1108    493       C  
ATOM   5042  C   LEU A 691     -59.044 -48.297 -37.184  1.00 80.38           C  
ANISOU 5042  C   LEU A 691    11926   9901   8714  -2986    990    801       C  
ATOM   5043  O   LEU A 691     -58.385 -48.344 -38.231  1.00 82.01           O  
ANISOU 5043  O   LEU A 691    12185   9936   9038  -2761    813    806       O  
ATOM   5044  CB  LEU A 691     -60.402 -46.284 -36.529  1.00 76.05           C  
ANISOU 5044  CB  LEU A 691    10840   9900   8154  -3047   1093    350       C  
ATOM   5045  CG  LEU A 691     -59.648 -45.165 -37.259  1.00 70.05           C  
ANISOU 5045  CG  LEU A 691    10001   9154   7458  -2717    854    260       C  
ATOM   5046  CD1 LEU A 691     -60.339 -43.837 -37.033  1.00 67.30           C  
ANISOU 5046  CD1 LEU A 691     9361   9083   7128  -2672    834    -35       C  
ATOM   5047  CD2 LEU A 691     -58.197 -45.073 -36.809  1.00 68.36           C  
ANISOU 5047  CD2 LEU A 691     9993   8894   7088  -2533    759    511       C  
ATOM   5048  N   ILE A 692     -58.582 -48.783 -36.030  1.00 78.60           N  
ANISOU 5048  N   ILE A 692    11932   9676   8255  -3066   1083   1050       N  
ATOM   5049  CA  ILE A 692     -57.279 -49.438 -35.957  1.00 76.95           C  
ANISOU 5049  CA  ILE A 692    12038   9251   7948  -2876    948   1323       C  
ATOM   5050  C   ILE A 692     -57.250 -50.667 -36.858  1.00 76.85           C  
ANISOU 5050  C   ILE A 692    12220   8888   8093  -2899    893   1404       C  
ATOM   5051  O   ILE A 692     -56.231 -50.967 -37.494  1.00 73.88           O  
ANISOU 5051  O   ILE A 692    11975   8332   7762  -2641    716   1491       O  
ATOM   5052  CB  ILE A 692     -56.948 -49.790 -34.494  1.00 76.63           C  
ANISOU 5052  CB  ILE A 692    12246   9264   7604  -2966   1044   1562       C  
ATOM   5053  CG1 ILE A 692     -56.855 -48.515 -33.653  1.00 72.06           C  
ANISOU 5053  CG1 ILE A 692    11482   9033   6866  -2888   1055   1455       C  
ATOM   5054  CG2 ILE A 692     -55.655 -50.583 -34.403  1.00 78.34           C  
ANISOU 5054  CG2 ILE A 692    12803   9235   7730  -2753    871   1827       C  
ATOM   5055  CD1 ILE A 692     -55.854 -47.506 -34.185  1.00 67.12           C  
ANISOU 5055  CD1 ILE A 692    10704   8473   6327  -2557    823   1364       C  
ATOM   5056  N   SER A 693     -58.372 -51.385 -36.941  1.00 80.86           N  
ANISOU 5056  N   SER A 693    12727   9297   8697  -3209   1045   1352       N  
ATOM   5057  CA  SER A 693     -58.445 -52.560 -37.804  1.00 83.39           C  
ANISOU 5057  CA  SER A 693    13232   9265   9188  -3249    977   1396       C  
ATOM   5058  C   SER A 693     -58.292 -52.172 -39.270  1.00 81.00           C  
ANISOU 5058  C   SER A 693    12764   8910   9102  -2999    790   1183       C  
ATOM   5059  O   SER A 693     -57.486 -52.764 -40.002  1.00 81.66           O  
ANISOU 5059  O   SER A 693    13036   8754   9236  -2783    633   1264       O  
ATOM   5060  CB  SER A 693     -59.769 -53.290 -37.577  1.00 90.11           C  
ANISOU 5060  CB  SER A 693    14064  10044  10131  -3675   1187   1344       C  
ATOM   5061  OG  SER A 693     -60.038 -53.434 -36.193  1.00 96.17           O  
ANISOU 5061  OG  SER A 693    14899  10953  10686  -3861   1387   1485       O  
ATOM   5062  N   LEU A 694     -59.062 -51.174 -39.715  1.00 82.55           N  
ANISOU 5062  N   LEU A 694    12624   9331   9412  -3009    799    901       N  
ATOM   5063  CA  LEU A 694     -58.963 -50.718 -41.099  1.00 80.70           C  
ANISOU 5063  CA  LEU A 694    12269   9053   9340  -2765    619    704       C  
ATOM   5064  C   LEU A 694     -57.557 -50.232 -41.420  1.00 77.93           C  
ANISOU 5064  C   LEU A 694    12007   8704   8900  -2416    479    820       C  
ATOM   5065  O   LEU A 694     -57.036 -50.487 -42.513  1.00 79.14           O  
ANISOU 5065  O   LEU A 694    12245   8692   9131  -2204    348    798       O  
ATOM   5066  CB  LEU A 694     -59.977 -49.605 -41.367  1.00 81.94           C  
ANISOU 5066  CB  LEU A 694    12077   9460   9596  -2803    627    391       C  
ATOM   5067  CG  LEU A 694     -61.455 -49.876 -41.079  1.00 88.01           C  
ANISOU 5067  CG  LEU A 694    12645  10306  10490  -3141    773    195       C  
ATOM   5068  CD1 LEU A 694     -62.315 -48.738 -41.607  1.00 86.20           C  
ANISOU 5068  CD1 LEU A 694    12071  10298  10384  -3064    694   -160       C  
ATOM   5069  CD2 LEU A 694     -61.895 -51.208 -41.668  1.00 92.66           C  
ANISOU 5069  CD2 LEU A 694    13372  10588  11245  -3309    763    198       C  
ATOM   5070  N   VAL A 695     -56.925 -49.533 -40.476  1.00 76.93           N  
ANISOU 5070  N   VAL A 695    11851   8770   8607  -2358    510    930       N  
ATOM   5071  CA  VAL A 695     -55.607 -48.966 -40.741  1.00 71.86           C  
ANISOU 5071  CA  VAL A 695    11231   8159   7912  -2057    388   1009       C  
ATOM   5072  C   VAL A 695     -54.550 -50.063 -40.814  1.00 69.25           C  
ANISOU 5072  C   VAL A 695    11174   7594   7543  -1916    316   1225       C  
ATOM   5073  O   VAL A 695     -53.671 -50.036 -41.683  1.00 68.36           O  
ANISOU 5073  O   VAL A 695    11084   7408   7483  -1665    211   1224       O  
ATOM   5074  CB  VAL A 695     -55.262 -47.908 -39.681  1.00 68.50           C  
ANISOU 5074  CB  VAL A 695    10684   7999   7344  -2041    414   1033       C  
ATOM   5075  CG1 VAL A 695     -53.830 -47.485 -39.831  1.00 66.99           C  
ANISOU 5075  CG1 VAL A 695    10515   7820   7119  -1773    294   1131       C  
ATOM   5076  CG2 VAL A 695     -56.180 -46.705 -39.822  1.00 67.56           C  
ANISOU 5076  CG2 VAL A 695    10291   8094   7285  -2099    434    780       C  
ATOM   5077  N   LYS A 696     -54.613 -51.042 -39.908  1.00 72.16           N  
ANISOU 5077  N   LYS A 696    11764   7841   7811  -2066    373   1407       N  
ATOM   5078  CA  LYS A 696     -53.675 -52.160 -39.966  1.00 69.66           C  
ANISOU 5078  CA  LYS A 696    11740   7265   7464  -1911    270   1596       C  
ATOM   5079  C   LYS A 696     -53.832 -52.935 -41.268  1.00 65.19           C  
ANISOU 5079  C   LYS A 696    11255   6443   7071  -1837    196   1506       C  
ATOM   5080  O   LYS A 696     -52.842 -53.257 -41.938  1.00 63.60           O  
ANISOU 5080  O   LYS A 696    11139   6127   6898  -1556     73   1532       O  
ATOM   5081  CB  LYS A 696     -53.875 -53.081 -38.763  1.00 74.77           C  
ANISOU 5081  CB  LYS A 696    12667   7786   7955  -2113    340   1815       C  
ATOM   5082  CG  LYS A 696     -52.937 -52.808 -37.600  1.00 76.86           C  
ANISOU 5082  CG  LYS A 696    13029   8175   8000  -1987    289   1988       C  
ATOM   5083  CD  LYS A 696     -53.190 -53.782 -36.462  1.00 82.75           C  
ANISOU 5083  CD  LYS A 696    14074   8788   8580  -2155    352   2193       C  
ATOM   5084  CE  LYS A 696     -52.154 -53.637 -35.365  1.00 88.17           C  
ANISOU 5084  CE  LYS A 696    14867   9577   9058  -1945    241   2335       C  
ATOM   5085  NZ  LYS A 696     -52.416 -54.558 -34.221  1.00 95.26           N  
ANISOU 5085  NZ  LYS A 696    16006  10381   9808  -2050    296   2491       N  
ATOM   5086  N   GLN A 697     -55.078 -53.239 -41.644  1.00 66.86           N  
ANISOU 5086  N   GLN A 697    11423   6576   7403  -2079    267   1374       N  
ATOM   5087  CA  GLN A 697     -55.322 -53.918 -42.914  1.00 67.40           C  
ANISOU 5087  CA  GLN A 697    11560   6409   7639  -2006    173   1247       C  
ATOM   5088  C   GLN A 697     -54.761 -53.116 -44.083  1.00 66.49           C  
ANISOU 5088  C   GLN A 697    11296   6399   7569  -1701     77   1096       C  
ATOM   5089  O   GLN A 697     -54.147 -53.680 -44.999  1.00 66.66           O  
ANISOU 5089  O   GLN A 697    11450   6247   7633  -1472    -30   1080       O  
ATOM   5090  CB  GLN A 697     -56.822 -54.158 -43.092  1.00 69.23           C  
ANISOU 5090  CB  GLN A 697    11692   6596   8016  -2328    253   1077       C  
ATOM   5091  CG  GLN A 697     -57.198 -54.981 -44.315  1.00 74.90           C  
ANISOU 5091  CG  GLN A 697    12503   7040   8915  -2286    132    928       C  
ATOM   5092  CD  GLN A 697     -57.112 -56.479 -44.075  1.00 82.57           C  
ANISOU 5092  CD  GLN A 697    13813   7642   9918  -2399    102   1090       C  
ATOM   5093  OE1 GLN A 697     -56.341 -56.948 -43.235  1.00 83.92           O  
ANISOU 5093  OE1 GLN A 697    14216   7724   9947  -2363    110   1343       O  
ATOM   5094  NE2 GLN A 697     -57.914 -57.239 -44.811  1.00 85.96           N  
ANISOU 5094  NE2 GLN A 697    14289   7834  10537  -2531     41    935       N  
ATOM   5095  N   MET A 698     -54.946 -51.793 -44.058  1.00 65.44           N  
ANISOU 5095  N   MET A 698    10908   6545   7413  -1692    118    986       N  
ATOM   5096  CA  MET A 698     -54.424 -50.949 -45.127  1.00 65.29           C  
ANISOU 5096  CA  MET A 698    10780   6616   7410  -1435     49    871       C  
ATOM   5097  C   MET A 698     -52.902 -50.994 -45.174  1.00 62.04           C  
ANISOU 5097  C   MET A 698    10446   6206   6922  -1168     11   1020       C  
ATOM   5098  O   MET A 698     -52.305 -50.976 -46.257  1.00 58.86           O  
ANISOU 5098  O   MET A 698    10069   5756   6538   -938    -37    963       O  
ATOM   5099  CB  MET A 698     -54.917 -49.514 -44.945  1.00 68.41           C  
ANISOU 5099  CB  MET A 698    10924   7277   7791  -1493     87    744       C  
ATOM   5100  CG  MET A 698     -54.633 -48.603 -46.126  1.00 72.56           C  
ANISOU 5100  CG  MET A 698    11379   7859   8332  -1277     19    618       C  
ATOM   5101  SD  MET A 698     -55.363 -46.967 -45.923  1.00 77.95           S  
ANISOU 5101  SD  MET A 698    11816   8789   9012  -1343     18    450       S  
ATOM   5102  CE  MET A 698     -57.028 -47.404 -45.425  1.00 77.03           C  
ANISOU 5102  CE  MET A 698    11591   8683   8994  -1632     51    279       C  
ATOM   5103  N   ALA A 699     -52.256 -51.054 -44.007  1.00 61.30           N  
ANISOU 5103  N   ALA A 699    10382   6176   6732  -1186     31   1195       N  
ATOM   5104  CA  ALA A 699     -50.801 -51.173 -43.973  1.00 59.51           C  
ANISOU 5104  CA  ALA A 699    10196   5956   6458   -927    -28   1308       C  
ATOM   5105  C   ALA A 699     -50.346 -52.493 -44.585  1.00 58.72           C  
ANISOU 5105  C   ALA A 699    10327   5588   6398   -758   -112   1343       C  
ATOM   5106  O   ALA A 699     -49.408 -52.523 -45.392  1.00 57.96           O  
ANISOU 5106  O   ALA A 699    10210   5490   6322   -493   -150   1306       O  
ATOM   5107  CB  ALA A 699     -50.296 -51.040 -42.537  1.00 56.35           C  
ANISOU 5107  CB  ALA A 699     9804   5666   5942   -971    -33   1466       C  
ATOM   5108  N   ARG A 700     -51.002 -53.596 -44.209  1.00 57.80           N  
ANISOU 5108  N   ARG A 700    10432   5236   6292   -915   -135   1408       N  
ATOM   5109  CA  ARG A 700     -50.683 -54.892 -44.804  1.00 57.89           C  
ANISOU 5109  CA  ARG A 700    10694   4945   6356   -762   -243   1421       C  
ATOM   5110  C   ARG A 700     -50.803 -54.839 -46.323  1.00 56.52           C  
ANISOU 5110  C   ARG A 700    10473   4730   6272   -605   -267   1222       C  
ATOM   5111  O   ARG A 700     -49.883 -55.238 -47.052  1.00 54.43           O  
ANISOU 5111  O   ARG A 700    10273   4398   6010   -308   -335   1189       O  
ATOM   5112  CB  ARG A 700     -51.606 -55.971 -44.232  1.00 60.08           C  
ANISOU 5112  CB  ARG A 700    11219   4953   6656  -1032   -246   1506       C  
ATOM   5113  CG  ARG A 700     -51.567 -56.117 -42.718  1.00 59.80           C  
ANISOU 5113  CG  ARG A 700    11303   4935   6482  -1203   -205   1725       C  
ATOM   5114  CD  ARG A 700     -52.535 -57.197 -42.252  1.00 63.54           C  
ANISOU 5114  CD  ARG A 700    12043   5123   6977  -1516   -169   1819       C  
ATOM   5115  NE  ARG A 700     -52.650 -57.252 -40.797  1.00 70.14           N  
ANISOU 5115  NE  ARG A 700    13012   6000   7638  -1721    -85   2034       N  
ATOM   5116  CZ  ARG A 700     -53.726 -56.878 -40.112  1.00 73.07           C  
ANISOU 5116  CZ  ARG A 700    13262   6523   7976  -2072    103   2025       C  
ATOM   5117  NH1 ARG A 700     -54.798 -56.424 -40.746  1.00 72.26           N  
ANISOU 5117  NH1 ARG A 700    12927   6508   8019  -2275    204   1819       N  
ATOM   5118  NH2 ARG A 700     -53.734 -56.966 -38.789  1.00 75.93           N  
ANISOU 5118  NH2 ARG A 700    13676   7000   8175  -2169    180   2169       N  
ATOM   5119  N   LYS A 701     -51.936 -54.329 -46.816  1.00 58.02           N  
ANISOU 5119  N   LYS A 701    10549   4974   6524   -784   -219   1069       N  
ATOM   5120  CA  LYS A 701     -52.147 -54.230 -48.256  1.00 54.64           C  
ANISOU 5120  CA  LYS A 701    10108   4505   6146   -631   -264    871       C  
ATOM   5121  C   LYS A 701     -51.073 -53.378 -48.922  1.00 51.40           C  
ANISOU 5121  C   LYS A 701     9577   4293   5658   -354   -226    850       C  
ATOM   5122  O   LYS A 701     -50.592 -53.716 -50.011  1.00 55.27           O  
ANISOU 5122  O   LYS A 701    10154   4711   6136   -110   -262    762       O  
ATOM   5123  CB  LYS A 701     -53.537 -53.661 -48.537  1.00 55.37           C  
ANISOU 5123  CB  LYS A 701    10069   4657   6310   -855   -247    698       C  
ATOM   5124  CG  LYS A 701     -54.681 -54.562 -48.085  1.00 58.31           C  
ANISOU 5124  CG  LYS A 701    10527   4830   6797  -1155   -263    671       C  
ATOM   5125  CD  LYS A 701     -56.026 -53.877 -48.277  1.00 59.90           C  
ANISOU 5125  CD  LYS A 701    10520   5152   7088  -1365   -244    464       C  
ATOM   5126  CE  LYS A 701     -57.180 -54.804 -47.935  1.00 63.26           C  
ANISOU 5126  CE  LYS A 701    10988   5386   7663  -1689   -240    404       C  
ATOM   5127  NZ  LYS A 701     -57.208 -56.002 -48.816  1.00 66.30           N  
ANISOU 5127  NZ  LYS A 701    11602   5440   8150  -1601   -383    325       N  
ATOM   5128  N   MET A 702     -50.672 -52.278 -48.280  1.00 50.68           N  
ANISOU 5128  N   MET A 702     9290   4453   5512   -398   -143    925       N  
ATOM   5129  CA  MET A 702     -49.661 -51.408 -48.877  1.00 53.18           C  
ANISOU 5129  CA  MET A 702     9478   4954   5775   -191    -80    914       C  
ATOM   5130  C   MET A 702     -48.303 -52.098 -48.938  1.00 55.79           C  
ANISOU 5130  C   MET A 702     9859   5249   6090     68    -97    986       C  
ATOM   5131  O   MET A 702     -47.545 -51.907 -49.900  1.00 55.29           O  
ANISOU 5131  O   MET A 702     9759   5252   5996    286    -43    923       O  
ATOM   5132  CB  MET A 702     -49.569 -50.096 -48.098  1.00 53.03           C  
ANISOU 5132  CB  MET A 702     9242   5179   5729   -321    -11    967       C  
ATOM   5133  CG  MET A 702     -48.638 -49.067 -48.722  1.00 57.52           C  
ANISOU 5133  CG  MET A 702     9669   5923   6261   -177     71    955       C  
ATOM   5134  SD  MET A 702     -49.246 -48.371 -50.280  1.00 61.27           S  
ANISOU 5134  SD  MET A 702    10198   6389   6693   -118    101    799       S  
ATOM   5135  CE  MET A 702     -50.621 -47.377 -49.701  1.00 54.32           C  
ANISOU 5135  CE  MET A 702     9221   5577   5839   -373     54    723       C  
ATOM   5136  N   ALA A 703     -47.978 -52.905 -47.921  1.00 53.01           N  
ANISOU 5136  N   ALA A 703     9599   4797   5746     58   -171   1111       N  
ATOM   5137  CA  ALA A 703     -46.758 -53.705 -47.976  1.00 54.75           C  
ANISOU 5137  CA  ALA A 703     9885   4951   5967    343   -237   1146       C  
ATOM   5138  C   ALA A 703     -46.813 -54.708 -49.123  1.00 56.99           C  
ANISOU 5138  C   ALA A 703    10362   5016   6274    536   -297   1025       C  
ATOM   5139  O   ALA A 703     -45.816 -54.912 -49.835  1.00 60.73           O  
ANISOU 5139  O   ALA A 703    10803   5536   6737    827   -284    955       O  
ATOM   5140  CB  ALA A 703     -46.537 -54.424 -46.645  1.00 57.61           C  
ANISOU 5140  CB  ALA A 703    10377   5200   6311    302   -348   1305       C  
ATOM   5141  N   MET A 704     -47.973 -55.343 -49.322  1.00 58.40           N  
ANISOU 5141  N   MET A 704    10731   4965   6494    375   -362    978       N  
ATOM   5142  CA  MET A 704     -48.127 -56.233 -50.468  1.00 62.62           C  
ANISOU 5142  CA  MET A 704    11454   5282   7055    552   -442    830       C  
ATOM   5143  C   MET A 704     -47.913 -55.484 -51.777  1.00 63.92           C  
ANISOU 5143  C   MET A 704    11510   5621   7155    720   -344    678       C  
ATOM   5144  O   MET A 704     -47.282 -56.009 -52.705  1.00 63.56           O  
ANISOU 5144  O   MET A 704    11551   5525   7074   1010   -362    571       O  
ATOM   5145  CB  MET A 704     -49.503 -56.897 -50.447  1.00 69.37           C  
ANISOU 5145  CB  MET A 704    12488   5878   7994    300   -528    782       C  
ATOM   5146  CG  MET A 704     -49.741 -57.772 -49.232  1.00 76.53           C  
ANISOU 5146  CG  MET A 704    13570   6566   8943    112   -601    951       C  
ATOM   5147  SD  MET A 704     -48.368 -58.900 -48.934  1.00 87.12           S  
ANISOU 5147  SD  MET A 704    15124   7718  10260    455   -745   1048       S  
ATOM   5148  CE  MET A 704     -48.410 -59.908 -50.414  1.00 90.30           C  
ANISOU 5148  CE  MET A 704    15733   7853  10725    719   -875    821       C  
ATOM   5149  N   MET A 705     -48.423 -54.250 -51.870  1.00 59.13           N  
ANISOU 5149  N   MET A 705    10736   5215   6514    553   -241    664       N  
ATOM   5150  CA  MET A 705     -48.181 -53.446 -53.065  1.00 59.80           C  
ANISOU 5150  CA  MET A 705    10762   5456   6502    700   -140    557       C  
ATOM   5151  C   MET A 705     -46.691 -53.221 -53.272  1.00 58.24           C  
ANISOU 5151  C   MET A 705    10440   5440   6247    939    -15    599       C  
ATOM   5152  O   MET A 705     -46.183 -53.364 -54.389  1.00 57.97           O  
ANISOU 5152  O   MET A 705    10463   5435   6129   1177     49    494       O  
ATOM   5153  CB  MET A 705     -48.907 -52.102 -52.985  1.00 62.49           C  
ANISOU 5153  CB  MET A 705    10964   5961   6818    486    -75    556       C  
ATOM   5154  CG  MET A 705     -48.459 -51.150 -54.098  1.00 66.22           C  
ANISOU 5154  CG  MET A 705    11405   6594   7161    631     49    501       C  
ATOM   5155  SD  MET A 705     -49.248 -49.530 -54.156  1.00 66.02           S  
ANISOU 5155  SD  MET A 705    11280   6714   7091    435     87    491       S  
ATOM   5156  CE  MET A 705     -50.946 -50.000 -54.440  1.00 60.06           C  
ANISOU 5156  CE  MET A 705    10661   5762   6398    325   -112    310       C  
ATOM   5157  N   SER A 706     -45.974 -52.861 -52.204  1.00 58.25           N  
ANISOU 5157  N   SER A 706    10260   5582   6292    880     23    734       N  
ATOM   5158  CA  SER A 706     -44.526 -52.706 -52.306  1.00 64.25           C  
ANISOU 5158  CA  SER A 706    10848   6524   7041   1096    127    747       C  
ATOM   5159  C   SER A 706     -43.886 -53.952 -52.904  1.00 70.04           C  
ANISOU 5159  C   SER A 706    11715   7125   7771   1417     62    647       C  
ATOM   5160  O   SER A 706     -43.092 -53.870 -53.854  1.00 71.45           O  
ANISOU 5160  O   SER A 706    11828   7434   7887   1642    193    549       O  
ATOM   5161  CB  SER A 706     -43.935 -52.405 -50.928  1.00 68.40           C  
ANISOU 5161  CB  SER A 706    11189   7163   7637   1007     96    881       C  
ATOM   5162  OG  SER A 706     -42.518 -52.413 -50.968  1.00 73.84           O  
ANISOU 5162  OG  SER A 706    11684   8017   8354   1232    159    859       O  
ATOM   5163  N   LYS A 707     -44.247 -55.124 -52.371  1.00 71.26           N  
ANISOU 5163  N   LYS A 707    12076   7012   7987   1437   -134    665       N  
ATOM   5164  CA  LYS A 707     -43.706 -56.375 -52.897  1.00 71.54           C  
ANISOU 5164  CA  LYS A 707    12278   6873   8032   1757   -242    554       C  
ATOM   5165  C   LYS A 707     -44.043 -56.554 -54.373  1.00 69.32           C  
ANISOU 5165  C   LYS A 707    12132   6542   7663   1905   -195    372       C  
ATOM   5166  O   LYS A 707     -43.223 -57.062 -55.148  1.00 68.11           O  
ANISOU 5166  O   LYS A 707    11996   6420   7464   2231   -166    239       O  
ATOM   5167  CB  LYS A 707     -44.229 -57.555 -52.077  1.00 72.83           C  
ANISOU 5167  CB  LYS A 707    12704   6694   8272   1697   -475    625       C  
ATOM   5168  CG  LYS A 707     -43.838 -58.922 -52.619  1.00 77.62           C  
ANISOU 5168  CG  LYS A 707    13547   7044   8903   2020   -637    500       C  
ATOM   5169  CD  LYS A 707     -44.233 -60.027 -51.654  1.00 78.80           C  
ANISOU 5169  CD  LYS A 707    13978   6833   9127   1935   -866    615       C  
ATOM   5170  CE  LYS A 707     -43.996 -61.401 -52.256  1.00 88.56           C  
ANISOU 5170  CE  LYS A 707    15499   7749  10399   2242  -1061    475       C  
ATOM   5171  NZ  LYS A 707     -44.871 -61.644 -53.437  1.00 90.15           N  
ANISOU 5171  NZ  LYS A 707    15846   7812  10595   2218  -1066    298       N  
ATOM   5172  N   TYR A 708     -45.238 -56.129 -54.788  1.00 68.46           N  
ANISOU 5172  N   TYR A 708    12118   6372   7521   1691   -194    343       N  
ATOM   5173  CA  TYR A 708     -45.656 -56.343 -56.170  1.00 68.65           C  
ANISOU 5173  CA  TYR A 708    12315   6325   7444   1843   -197    157       C  
ATOM   5174  C   TYR A 708     -44.980 -55.382 -57.143  1.00 66.81           C  
ANISOU 5174  C   TYR A 708    11956   6383   7046   1981     41    110       C  
ATOM   5175  O   TYR A 708     -44.711 -55.760 -58.288  1.00 63.44           O  
ANISOU 5175  O   TYR A 708    11658   5950   6494   2245     77    -47       O  
ATOM   5176  CB  TYR A 708     -47.176 -56.234 -56.277  1.00 70.04           C  
ANISOU 5176  CB  TYR A 708    12622   6335   7653   1586   -312    113       C  
ATOM   5177  CG  TYR A 708     -47.900 -57.299 -55.486  1.00 75.01           C  
ANISOU 5177  CG  TYR A 708    13406   6651   8442   1427   -516    142       C  
ATOM   5178  CD1 TYR A 708     -47.326 -58.550 -55.279  1.00 75.08           C  
ANISOU 5178  CD1 TYR A 708    13574   6440   8512   1619   -646    134       C  
ATOM   5179  CD2 TYR A 708     -49.151 -57.053 -54.933  1.00 74.58           C  
ANISOU 5179  CD2 TYR A 708    13342   6517   8478   1081   -573    174       C  
ATOM   5180  CE1 TYR A 708     -47.979 -59.526 -54.553  1.00 72.16           C  
ANISOU 5180  CE1 TYR A 708    13392   5748   8278   1447   -823    187       C  
ATOM   5181  CE2 TYR A 708     -49.811 -58.024 -54.203  1.00 72.70           C  
ANISOU 5181  CE2 TYR A 708    13246   5994   8382    891   -716    215       C  
ATOM   5182  CZ  TYR A 708     -49.220 -59.257 -54.018  1.00 73.35           C  
ANISOU 5182  CZ  TYR A 708    13527   5831   8511   1062   -838    237       C  
ATOM   5183  OH  TYR A 708     -49.877 -60.224 -53.296  1.00 78.03           O  
ANISOU 5183  OH  TYR A 708    14307   6105   9235    847   -973    303       O  
ATOM   5184  N   THR A 709     -44.699 -54.146 -56.724  1.00 67.74           N  
ANISOU 5184  N   THR A 709    11843   6745   7149   1803    209    241       N  
ATOM   5185  CA  THR A 709     -43.936 -53.254 -57.592  1.00 74.96           C  
ANISOU 5185  CA  THR A 709    12647   7921   7914   1905    464    224       C  
ATOM   5186  C   THR A 709     -42.468 -53.651 -57.636  1.00 87.05           C  
ANISOU 5186  C   THR A 709    14002   9614   9459   2161    593    190       C  
ATOM   5187  O   THR A 709     -41.788 -53.383 -58.633  1.00 88.09           O  
ANISOU 5187  O   THR A 709    14102   9923   9446   2333    808    112       O  
ATOM   5188  CB  THR A 709     -44.064 -51.796 -57.140  1.00 67.88           C  
ANISOU 5188  CB  THR A 709    11570   7205   7018   1623    593    368       C  
ATOM   5189  OG1 THR A 709     -43.251 -51.575 -55.981  1.00 73.35           O  
ANISOU 5189  OG1 THR A 709    11992   8028   7852   1541    626    486       O  
ATOM   5190  CG2 THR A 709     -45.505 -51.454 -56.815  1.00 58.81           C  
ANISOU 5190  CG2 THR A 709    10535   5908   5902   1375    431    385       C  
ATOM   5191  N   ARG A 710     -41.962 -54.287 -56.575  1.00103.07           N  
ANISOU 5191  N   ARG A 710    15919  11594  11650   2200    466    237       N  
ATOM   5192  CA  ARG A 710     -40.568 -54.719 -56.587  1.00114.62           C  
ANISOU 5192  CA  ARG A 710    17187  13211  13151   2483    545    164       C  
ATOM   5193  C   ARG A 710     -40.318 -55.857 -57.571  1.00122.27           C  
ANISOU 5193  C   ARG A 710    18347  14067  14041   2849    495    -41       C  
ATOM   5194  O   ARG A 710     -39.164 -56.087 -57.949  1.00126.38           O  
ANISOU 5194  O   ARG A 710    18694  14774  14548   3124    625   -158       O  
ATOM   5195  CB  ARG A 710     -40.131 -55.146 -55.185  1.00118.58           C  
ANISOU 5195  CB  ARG A 710    17565  13661  13830   2470    364    254       C  
ATOM   5196  CG  ARG A 710     -38.625 -55.074 -54.963  1.00126.15           C  
ANISOU 5196  CG  ARG A 710    18187  14880  14865   2681    468    196       C  
ATOM   5197  CD  ARG A 710     -38.097 -56.276 -54.190  1.00132.17           C  
ANISOU 5197  CD  ARG A 710    18994  15479  15744   2938    199    152       C  
ATOM   5198  NE  ARG A 710     -38.770 -56.457 -52.907  1.00133.26           N  
ANISOU 5198  NE  ARG A 710    19274  15404  15953   2724    -36    328       N  
ATOM   5199  CZ  ARG A 710     -39.660 -57.413 -52.659  1.00134.56           C  
ANISOU 5199  CZ  ARG A 710    19798  15214  16117   2697   -261    368       C  
ATOM   5200  NH1 ARG A 710     -39.984 -58.284 -53.605  1.00134.17           N  
ANISOU 5200  NH1 ARG A 710    19997  14962  16019   2884   -320    228       N  
ATOM   5201  NH2 ARG A 710     -40.223 -57.502 -51.462  1.00136.18           N  
ANISOU 5201  NH2 ARG A 710    20117  15261  16363   2474   -422    543       N  
ATOM   5202  N   GLY A 711     -41.362 -56.566 -57.994  1.00127.23           N  
ANISOU 5202  N   GLY A 711    19309  14403  14629   2863    308   -111       N  
ATOM   5203  CA  GLY A 711     -41.201 -57.695 -58.891  1.00132.77           C  
ANISOU 5203  CA  GLY A 711    20225  14957  15264   3215    215   -326       C  
ATOM   5204  C   GLY A 711     -40.675 -57.326 -60.264  1.00135.72           C  
ANISOU 5204  C   GLY A 711    20581  15570  15417   3433    478   -474       C  
ATOM   5205  O   GLY A 711     -41.338 -56.606 -61.017  1.00136.58           O  
ANISOU 5205  O   GLY A 711    20809  15723  15361   3306    586   -465       O  
ATOM   5206  N   GLU A 712     -39.480 -57.819 -60.602  1.00141.73           N  
ANISOU 5206  N   GLU A 712    21201  16489  16160   3775    581   -620       N  
ATOM   5207  CA  GLU A 712     -38.846 -57.551 -61.898  1.00140.90           C  
ANISOU 5207  CA  GLU A 712    21064  16647  15824   4004    878   -775       C  
ATOM   5208  C   GLU A 712     -38.137 -58.825 -62.354  1.00136.11           C  
ANISOU 5208  C   GLU A 712    20516  15987  15214   4471    781  -1036       C  
ATOM   5209  O   GLU A 712     -36.978 -59.061 -62.003  1.00136.86           O  
ANISOU 5209  O   GLU A 712    20319  16268  15414   4673    854  -1109       O  
ATOM   5210  CB  GLU A 712     -37.882 -56.373 -61.813  1.00143.72           C  
ANISOU 5210  CB  GLU A 712    21037  17407  16162   3870   1247   -671       C  
ATOM   5211  CG  GLU A 712     -38.548 -55.007 -61.716  1.00147.00           C  
ANISOU 5211  CG  GLU A 712    21451  17888  16515   3459   1383   -452       C  
ATOM   5212  CD  GLU A 712     -39.061 -54.497 -63.054  1.00150.52           C  
ANISOU 5212  CD  GLU A 712    22165  18374  16651   3468   1560   -490       C  
ATOM   5213  OE1 GLU A 712     -39.120 -55.286 -64.022  1.00153.42           O  
ANISOU 5213  OE1 GLU A 712    22768  18675  16849   3776   1527   -689       O  
ATOM   5214  OE2 GLU A 712     -39.400 -53.298 -63.139  1.00150.07           O  
ANISOU 5214  OE2 GLU A 712    22106  18406  16509   3182   1714   -326       O  
ATOM   5215  N   SER A 713     -38.841 -59.637 -63.137  1.00121.31           N  
ANISOU 5215  N   SER A 713    19010  13854  13227   4654    596  -1203       N  
ATOM   5216  CA  SER A 713     -38.263 -60.840 -63.727  1.00116.74           C  
ANISOU 5216  CA  SER A 713    18542  13201  12614   5126    490  -1487       C  
ATOM   5217  C   SER A 713     -39.156 -61.362 -64.849  1.00113.54           C  
ANISOU 5217  C   SER A 713    18553  12573  12015   5270    355  -1669       C  
ATOM   5218  O   SER A 713     -40.335 -61.015 -64.928  1.00107.58           O  
ANISOU 5218  O   SER A 713    18011  11636  11228   4995    241  -1573       O  
ATOM   5219  CB  SER A 713     -38.057 -61.928 -62.669  1.00113.80           C  
ANISOU 5219  CB  SER A 713    18187  12538  12514   5249    139  -1498       C  
ATOM   5220  OG  SER A 713     -37.349 -63.030 -63.210  1.00114.39           O  
ANISOU 5220  OG  SER A 713    18333  12562  12566   5744     37  -1791       O  
ATOM   5221  N   ARG A 717     -48.629 -62.968 -62.926  1.00114.75           N  
ANISOU 5221  N   ARG A 717    19988  10496  13117   3218  -1481  -1459       N  
ATOM   5222  CA  ARG A 717     -47.562 -61.982 -62.808  1.00110.25           C  
ANISOU 5222  CA  ARG A 717    19252  10262  12376   3355  -1170  -1327       C  
ATOM   5223  C   ARG A 717     -47.875 -60.963 -61.715  1.00103.55           C  
ANISOU 5223  C   ARG A 717    18146   9572  11624   2947  -1034  -1053       C  
ATOM   5224  O   ARG A 717     -48.955 -60.983 -61.123  1.00103.66           O  
ANISOU 5224  O   ARG A 717    18167   9410  11810   2610  -1168  -1003       O  
ATOM   5225  CB  ARG A 717     -47.336 -61.279 -64.141  1.00110.34           C  
ANISOU 5225  CB  ARG A 717    19311  10540  12074   3603  -1006  -1470       C  
ATOM   5226  N   SER A 718     -46.919 -60.072 -61.453  1.00 96.63           N  
ANISOU 5226  N   SER A 718    17031   9039  10645   2975   -760   -895       N  
ATOM   5227  CA  SER A 718     -47.071 -59.067 -60.409  1.00 90.34           C  
ANISOU 5227  CA  SER A 718    15987   8411   9927   2627   -631   -650       C  
ATOM   5228  C   SER A 718     -47.956 -57.900 -60.826  1.00 79.43           C  
ANISOU 5228  C   SER A 718    14568   7165   8446   2425   -567   -647       C  
ATOM   5229  O   SER A 718     -48.339 -57.096 -59.967  1.00 74.25           O  
ANISOU 5229  O   SER A 718    13735   6604   7875   2118   -509   -481       O  
ATOM   5230  CB  SER A 718     -45.696 -58.539 -59.991  1.00 93.66           C  
ANISOU 5230  CB  SER A 718    16154   9135  10298   2733   -388   -509       C  
ATOM   5231  OG  SER A 718     -44.816 -59.604 -59.673  1.00 98.38           O  
ANISOU 5231  OG  SER A 718    16780   9623  10978   2983   -473   -547       O  
ATOM   5232  N   LYS A 719     -48.295 -57.792 -62.111  1.00 77.58           N  
ANISOU 5232  N   LYS A 719    14517   6935   8023   2612   -595   -838       N  
ATOM   5233  CA  LYS A 719     -49.065 -56.648 -62.587  1.00 74.46           C  
ANISOU 5233  CA  LYS A 719    14126   6662   7503   2478   -560   -844       C  
ATOM   5234  C   LYS A 719     -50.500 -56.694 -62.075  1.00 74.22           C  
ANISOU 5234  C   LYS A 719    14091   6435   7676   2173   -792   -889       C  
ATOM   5235  O   LYS A 719     -51.004 -55.710 -61.517  1.00 74.24           O  
ANISOU 5235  O   LYS A 719    13930   6556   7723   1914   -741   -776       O  
ATOM   5236  CB  LYS A 719     -49.031 -56.607 -64.114  1.00 75.24           C  
ANISOU 5236  CB  LYS A 719    14474   6800   7313   2795   -555  -1044       C  
ATOM   5237  CG  LYS A 719     -47.624 -56.672 -64.677  1.00 76.19           C  
ANISOU 5237  CG  LYS A 719    14590   7131   7228   3101   -296  -1034       C  
ATOM   5238  CD  LYS A 719     -47.609 -57.204 -66.095  1.00 82.68           C  
ANISOU 5238  CD  LYS A 719    15716   7905   7794   3468   -356  -1288       C  
ATOM   5239  CE  LYS A 719     -46.188 -57.507 -66.543  1.00 90.21           C  
ANISOU 5239  CE  LYS A 719    16629   9063   8584   3785    -97  -1316       C  
ATOM   5240  NZ  LYS A 719     -45.318 -56.302 -66.468  1.00 93.54           N  
ANISOU 5240  NZ  LYS A 719    16838   9836   8866   3690    286  -1105       N  
ATOM   5241  N   ALA A 720     -51.175 -57.832 -62.256  1.00 77.33           N  
ANISOU 5241  N   ALA A 720    14650   6525   8206   2197  -1048  -1072       N  
ATOM   5242  CA  ALA A 720     -52.549 -57.958 -61.781  1.00 74.76           C  
ANISOU 5242  CA  ALA A 720    14285   6017   8105   1882  -1251  -1142       C  
ATOM   5243  C   ALA A 720     -52.623 -57.815 -60.268  1.00 70.82           C  
ANISOU 5243  C   ALA A 720    13560   5539   7811   1529  -1164   -906       C  
ATOM   5244  O   ALA A 720     -53.561 -57.206 -59.739  1.00 69.66           O  
ANISOU 5244  O   ALA A 720    13260   5436   7772   1235  -1186   -889       O  
ATOM   5245  CB  ALA A 720     -53.141 -59.295 -62.221  1.00 73.52           C  
ANISOU 5245  CB  ALA A 720    14343   5507   8085   1951  -1530  -1378       C  
ATOM   5246  N   ASP A 721     -51.641 -58.371 -59.553  1.00 69.55           N  
ANISOU 5246  N   ASP A 721    13380   5354   7694   1575  -1075   -739       N  
ATOM   5247  CA  ASP A 721     -51.600 -58.210 -58.104  1.00 68.17           C  
ANISOU 5247  CA  ASP A 721    13026   5214   7661   1277   -990   -502       C  
ATOM   5248  C   ASP A 721     -51.395 -56.750 -57.722  1.00 64.44           C  
ANISOU 5248  C   ASP A 721    12313   5079   7093   1161   -789   -356       C  
ATOM   5249  O   ASP A 721     -51.950 -56.276 -56.723  1.00 62.65           O  
ANISOU 5249  O   ASP A 721    11924   4907   6971    854   -756   -242       O  
ATOM   5250  CB  ASP A 721     -50.498 -59.090 -57.512  1.00 71.91           C  
ANISOU 5250  CB  ASP A 721    13563   5591   8168   1421   -975   -373       C  
ATOM   5251  CG  ASP A 721     -50.749 -60.572 -57.739  1.00 79.64           C  
ANISOU 5251  CG  ASP A 721    14811   6180   9268   1506  -1203   -502       C  
ATOM   5252  OD1 ASP A 721     -51.930 -60.966 -57.816  1.00 82.53           O  
ANISOU 5252  OD1 ASP A 721    15259   6325   9774   1286  -1356   -617       O  
ATOM   5253  OD2 ASP A 721     -49.768 -61.339 -57.846  1.00 82.43           O  
ANISOU 5253  OD2 ASP A 721    15285   6443   9591   1794  -1239   -506       O  
ATOM   5254  N   LEU A 722     -50.611 -56.014 -58.514  1.00 66.47           N  
ANISOU 5254  N   LEU A 722    12552   5558   7146   1397   -644   -362       N  
ATOM   5255  CA  LEU A 722     -50.402 -54.596 -58.240  1.00 61.39           C  
ANISOU 5255  CA  LEU A 722    11711   5199   6418   1283   -464   -229       C  
ATOM   5256  C   LEU A 722     -51.690 -53.803 -58.431  1.00 59.03           C  
ANISOU 5256  C   LEU A 722    11388   4910   6130   1098   -557   -325       C  
ATOM   5257  O   LEU A 722     -52.073 -53.003 -57.568  1.00 59.41           O  
ANISOU 5257  O   LEU A 722    11250   5071   6251    851   -511   -224       O  
ATOM   5258  CB  LEU A 722     -49.287 -54.049 -59.134  1.00 63.36           C  
ANISOU 5258  CB  LEU A 722    11975   5655   6445   1553   -271   -216       C  
ATOM   5259  CG  LEU A 722     -49.080 -52.531 -59.136  1.00 65.22           C  
ANISOU 5259  CG  LEU A 722    12068   6143   6568   1450    -89    -98       C  
ATOM   5260  CD1 LEU A 722     -48.921 -51.989 -57.720  1.00 60.34           C  
ANISOU 5260  CD1 LEU A 722    11195   5632   6100   1185    -26     91       C  
ATOM   5261  CD2 LEU A 722     -47.879 -52.157 -59.993  1.00 65.99           C  
ANISOU 5261  CD2 LEU A 722    12185   6431   6459   1686    143    -71       C  
ATOM   5262  N   ILE A 723     -52.375 -54.016 -59.555  1.00 60.76           N  
ANISOU 5262  N   ILE A 723    11795   5015   6277   1239   -710   -546       N  
ATOM   5263  CA  ILE A 723     -53.594 -53.261 -59.837  1.00 61.34           C  
ANISOU 5263  CA  ILE A 723    11847   5100   6359   1119   -840   -680       C  
ATOM   5264  C   ILE A 723     -54.680 -53.600 -58.822  1.00 62.29           C  
ANISOU 5264  C   ILE A 723    11809   5111   6748    789   -958   -716       C  
ATOM   5265  O   ILE A 723     -55.289 -52.708 -58.211  1.00 64.75           O  
ANISOU 5265  O   ILE A 723    11933   5549   7121    579   -939   -688       O  
ATOM   5266  CB  ILE A 723     -54.064 -53.532 -61.278  1.00 59.86           C  
ANISOU 5266  CB  ILE A 723    11917   4798   6030   1377  -1019   -935       C  
ATOM   5267  CG1 ILE A 723     -53.001 -53.069 -62.276  1.00 62.12           C  
ANISOU 5267  CG1 ILE A 723    12369   5231   6003   1681   -848   -881       C  
ATOM   5268  CG2 ILE A 723     -55.398 -52.857 -61.539  1.00 54.91           C  
ANISOU 5268  CG2 ILE A 723    11260   4160   5442   1277  -1215  -1115       C  
ATOM   5269  CD1 ILE A 723     -53.337 -53.382 -63.719  1.00 64.69           C  
ANISOU 5269  CD1 ILE A 723    12997   5455   6126   1978  -1009  -1123       C  
ATOM   5270  N   ARG A 724     -54.934 -54.897 -58.628  1.00 59.93           N  
ANISOU 5270  N   ARG A 724    11588   4572   6611    734  -1073   -783       N  
ATOM   5271  CA  ARG A 724     -55.942 -55.330 -57.666  1.00 60.15           C  
ANISOU 5271  CA  ARG A 724    11480   4481   6891    384  -1145   -804       C  
ATOM   5272  C   ARG A 724     -55.622 -54.824 -56.266  1.00 58.10           C  
ANISOU 5272  C   ARG A 724    11016   4384   6675    142   -956   -549       C  
ATOM   5273  O   ARG A 724     -56.519 -54.386 -55.535  1.00 61.17           O  
ANISOU 5273  O   ARG A 724    11214   4845   7183   -139   -947   -568       O  
ATOM   5274  CB  ARG A 724     -56.043 -56.856 -57.676  1.00 63.84           C  
ANISOU 5274  CB  ARG A 724    12120   4628   7508    365  -1275   -869       C  
ATOM   5275  CG  ARG A 724     -56.944 -57.434 -56.604  1.00 65.57           C  
ANISOU 5275  CG  ARG A 724    12232   4700   7982    -38  -1298   -841       C  
ATOM   5276  CD  ARG A 724     -56.947 -58.952 -56.663  1.00 70.39           C  
ANISOU 5276  CD  ARG A 724    13069   4944   8733    -53  -1432   -883       C  
ATOM   5277  NE  ARG A 724     -55.596 -59.500 -56.583  1.00 70.02           N  
ANISOU 5277  NE  ARG A 724    13204   4834   8565    201  -1374   -707       N  
ATOM   5278  CZ  ARG A 724     -54.953 -59.735 -55.444  1.00 69.62           C  
ANISOU 5278  CZ  ARG A 724    13149   4778   8523     92  -1251   -439       C  
ATOM   5279  NH1 ARG A 724     -55.538 -59.467 -54.283  1.00 73.83           N  
ANISOU 5279  NH1 ARG A 724    13530   5370   9153   -281  -1148   -299       N  
ATOM   5280  NH2 ARG A 724     -53.725 -60.236 -55.463  1.00 62.72           N  
ANISOU 5280  NH2 ARG A 724    12425   3854   7552    372  -1238   -329       N  
ATOM   5281  N   MET A 725     -54.345 -54.868 -55.879  1.00 56.55           N  
ANISOU 5281  N   MET A 725    10845   4262   6380    264   -810   -334       N  
ATOM   5282  CA  MET A 725     -53.958 -54.376 -54.562  1.00 58.89           C  
ANISOU 5282  CA  MET A 725    10964   4716   6696     72   -657   -104       C  
ATOM   5283  C   MET A 725     -54.220 -52.879 -54.436  1.00 59.60           C  
ANISOU 5283  C   MET A 725    10858   5071   6719     -4   -576    -99       C  
ATOM   5284  O   MET A 725     -54.677 -52.408 -53.387  1.00 57.80           O  
ANISOU 5284  O   MET A 725    10454   4946   6561   -255   -521    -28       O  
ATOM   5285  CB  MET A 725     -52.488 -54.691 -54.297  1.00 66.34           C  
ANISOU 5285  CB  MET A 725    11958   5695   7555    268   -556     79       C  
ATOM   5286  CG  MET A 725     -52.051 -54.395 -52.877  1.00 72.54           C  
ANISOU 5286  CG  MET A 725    12598   6601   8364     92   -448    303       C  
ATOM   5287  SD  MET A 725     -53.118 -55.210 -51.674  1.00 78.17           S  
ANISOU 5287  SD  MET A 725    13342   7121   9237   -280   -503    361       S  
ATOM   5288  CE  MET A 725     -52.826 -56.930 -52.069  1.00 79.44           C  
ANISOU 5288  CE  MET A 725    13815   6903   9467   -133   -651    336       C  
ATOM   5289  N   ALA A 726     -53.945 -52.117 -55.498  1.00 58.64           N  
ANISOU 5289  N   ALA A 726    10787   5049   6446    216   -570   -174       N  
ATOM   5290  CA  ALA A 726     -54.239 -50.687 -55.475  1.00 53.51           C  
ANISOU 5290  CA  ALA A 726    10004   4598   5730    160   -529   -178       C  
ATOM   5291  C   ALA A 726     -55.728 -50.433 -55.301  1.00 53.80           C  
ANISOU 5291  C   ALA A 726     9935   4613   5895    -32   -671   -367       C  
ATOM   5292  O   ALA A 726     -56.128 -49.553 -54.528  1.00 53.38           O  
ANISOU 5292  O   ALA A 726     9691   4710   5883   -203   -631   -341       O  
ATOM   5293  CB  ALA A 726     -53.732 -50.022 -56.752  1.00 48.97           C  
ANISOU 5293  CB  ALA A 726     9577   4083   4946    427   -504   -219       C  
ATOM   5294  N   LYS A 727     -56.566 -51.194 -56.009  1.00 57.05           N  
ANISOU 5294  N   LYS A 727    10448   4844   6383      1   -848   -585       N  
ATOM   5295  CA  LYS A 727     -58.007 -51.011 -55.867  1.00 60.02           C  
ANISOU 5295  CA  LYS A 727    10675   5211   6917   -183   -993   -808       C  
ATOM   5296  C   LYS A 727     -58.476 -51.373 -54.460  1.00 63.42           C  
ANISOU 5296  C   LYS A 727    10899   5665   7533   -533   -897   -730       C  
ATOM   5297  O   LYS A 727     -59.344 -50.696 -53.891  1.00 65.66           O  
ANISOU 5297  O   LYS A 727    10959   6086   7904   -716   -900   -826       O  
ATOM   5298  CB  LYS A 727     -58.747 -51.836 -56.921  1.00 59.62           C  
ANISOU 5298  CB  LYS A 727    10766   4952   6933    -77  -1219  -1078       C  
ATOM   5299  CG  LYS A 727     -58.441 -51.411 -58.349  1.00 63.25           C  
ANISOU 5299  CG  LYS A 727    11460   5403   7168    279  -1328  -1183       C  
ATOM   5300  CD  LYS A 727     -59.526 -51.864 -59.316  1.00 70.57           C  
ANISOU 5300  CD  LYS A 727    12470   6173   8170    371  -1617  -1524       C  
ATOM   5301  CE  LYS A 727     -59.021 -52.937 -60.267  1.00 72.26           C  
ANISOU 5301  CE  LYS A 727    12969   6187   8298    608  -1697  -1586       C  
ATOM   5302  NZ  LYS A 727     -60.091 -53.381 -61.204  1.00 75.33           N  
ANISOU 5302  NZ  LYS A 727    13441   6416   8767    704  -2012  -1945       N  
ATOM   5303  N   GLU A 728     -57.901 -52.428 -53.876  1.00 62.71           N  
ANISOU 5303  N   GLU A 728    10898   5444   7486   -617   -811   -557       N  
ATOM   5304  CA  GLU A 728     -58.264 -52.801 -52.511  1.00 66.68           C  
ANISOU 5304  CA  GLU A 728    11267   5956   8113   -951   -698   -440       C  
ATOM   5305  C   GLU A 728     -57.858 -51.720 -51.516  1.00 65.40           C  
ANISOU 5305  C   GLU A 728    10934   6056   7858  -1025   -541   -272       C  
ATOM   5306  O   GLU A 728     -58.614 -51.406 -50.586  1.00 66.40           O  
ANISOU 5306  O   GLU A 728    10866   6302   8061  -1286   -472   -295       O  
ATOM   5307  CB  GLU A 728     -57.628 -54.144 -52.149  1.00 71.23           C  
ANISOU 5307  CB  GLU A 728    12048   6298   8718   -980   -669   -270       C  
ATOM   5308  CG  GLU A 728     -58.463 -55.346 -52.572  1.00 80.34           C  
ANISOU 5308  CG  GLU A 728    13310   7161  10054  -1099   -808   -439       C  
ATOM   5309  CD  GLU A 728     -57.670 -56.640 -52.605  1.00 88.07           C  
ANISOU 5309  CD  GLU A 728    14574   7857  11033  -1002   -844   -305       C  
ATOM   5310  OE1 GLU A 728     -57.920 -57.465 -53.509  1.00 95.07           O  
ANISOU 5310  OE1 GLU A 728    15622   8501  11998   -898  -1012   -478       O  
ATOM   5311  OE2 GLU A 728     -56.796 -56.831 -51.734  1.00 88.02           O  
ANISOU 5311  OE2 GLU A 728    14636   7862  10945  -1006   -732    -45       O  
ATOM   5312  N   ILE A 729     -56.673 -51.131 -51.698  1.00 61.25           N  
ANISOU 5312  N   ILE A 729    10468   5633   7171   -803   -479   -121       N  
ATOM   5313  CA  ILE A 729     -56.253 -50.031 -50.834  1.00 57.99           C  
ANISOU 5313  CA  ILE A 729     9895   5457   6683   -859   -361     12       C  
ATOM   5314  C   ILE A 729     -57.182 -48.837 -51.004  1.00 60.81           C  
ANISOU 5314  C   ILE A 729    10082   5968   7057   -900   -420   -176       C  
ATOM   5315  O   ILE A 729     -57.486 -48.124 -50.040  1.00 63.23           O  
ANISOU 5315  O   ILE A 729    10204   6446   7376  -1058   -353   -157       O  
ATOM   5316  CB  ILE A 729     -54.787 -49.654 -51.119  1.00 54.63           C  
ANISOU 5316  CB  ILE A 729     9546   5097   6115   -623   -289    181       C  
ATOM   5317  CG1 ILE A 729     -53.859 -50.807 -50.747  1.00 51.89           C  
ANISOU 5317  CG1 ILE A 729     9330   4622   5765   -567   -250    350       C  
ATOM   5318  CG2 ILE A 729     -54.390 -48.400 -50.350  1.00 55.76           C  
ANISOU 5318  CG2 ILE A 729     9517   5469   6200   -678   -199    280       C  
ATOM   5319  CD1 ILE A 729     -52.406 -50.537 -51.050  1.00 52.98           C  
ANISOU 5319  CD1 ILE A 729     9493   4842   5794   -328   -176    475       C  
ATOM   5320  N   ALA A 730     -57.655 -48.602 -52.231  1.00 63.02           N  
ANISOU 5320  N   ALA A 730    10435   6184   7326   -734   -566   -375       N  
ATOM   5321  CA  ALA A 730     -58.575 -47.494 -52.466  1.00 64.44           C  
ANISOU 5321  CA  ALA A 730    10482   6479   7522   -728   -674   -580       C  
ATOM   5322  C   ALA A 730     -59.892 -47.709 -51.730  1.00 63.57           C  
ANISOU 5322  C   ALA A 730    10137   6418   7597   -992   -700   -763       C  
ATOM   5323  O   ALA A 730     -60.418 -46.789 -51.091  1.00 61.42           O  
ANISOU 5323  O   ALA A 730     9660   6327   7350  -1084   -686   -842       O  
ATOM   5324  CB  ALA A 730     -58.815 -47.320 -53.966  1.00 67.30           C  
ANISOU 5324  CB  ALA A 730    11024   6736   7811   -470   -856   -759       C  
ATOM   5325  N   LEU A 731     -60.440 -48.925 -51.808  1.00 66.93           N  
ANISOU 5325  N   LEU A 731    10585   6684   8162  -1124   -732   -846       N  
ATOM   5326  CA  LEU A 731     -61.685 -49.216 -51.101  1.00 74.02           C  
ANISOU 5326  CA  LEU A 731    11239   7632   9254  -1423   -714  -1019       C  
ATOM   5327  C   LEU A 731     -61.498 -49.107 -49.590  1.00 75.40           C  
ANISOU 5327  C   LEU A 731    11280   7962   9406  -1674   -486   -821       C  
ATOM   5328  O   LEU A 731     -62.367 -48.575 -48.881  1.00 77.17           O  
ANISOU 5328  O   LEU A 731    11243   8374   9705  -1855   -432   -959       O  
ATOM   5329  CB  LEU A 731     -62.187 -50.606 -51.490  1.00 80.56           C  
ANISOU 5329  CB  LEU A 731    12147   8217  10244  -1544   -780  -1118       C  
ATOM   5330  CG  LEU A 731     -63.569 -51.022 -50.985  1.00 89.17           C  
ANISOU 5330  CG  LEU A 731    12973   9331  11577  -1879   -766  -1344       C  
ATOM   5331  CD1 LEU A 731     -64.617 -49.998 -51.387  1.00 89.69           C  
ANISOU 5331  CD1 LEU A 731    12775   9578  11725  -1805   -924  -1691       C  
ATOM   5332  CD2 LEU A 731     -63.932 -52.400 -51.518  1.00 93.72           C  
ANISOU 5332  CD2 LEU A 731    13673   9614  12322  -1983   -860  -1436       C  
ATOM   5333  N   ASN A 732     -60.363 -49.597 -49.083  1.00 73.47           N  
ANISOU 5333  N   ASN A 732    11214   7653   9049  -1665   -361   -515       N  
ATOM   5334  CA  ASN A 732     -60.060 -49.436 -47.664  1.00 73.43           C  
ANISOU 5334  CA  ASN A 732    11132   7795   8972  -1852   -173   -313       C  
ATOM   5335  C   ASN A 732     -60.001 -47.965 -47.274  1.00 69.33           C  
ANISOU 5335  C   ASN A 732    10437   7539   8367  -1779   -159   -355       C  
ATOM   5336  O   ASN A 732     -60.474 -47.583 -46.198  1.00 68.40           O  
ANISOU 5336  O   ASN A 732    10138   7605   8244  -1971    -45   -370       O  
ATOM   5337  CB  ASN A 732     -58.743 -50.133 -47.325  1.00 74.21           C  
ANISOU 5337  CB  ASN A 732    11471   7772   8956  -1774   -105     -4       C  
ATOM   5338  CG  ASN A 732     -58.951 -51.479 -46.663  1.00 82.18           C  
ANISOU 5338  CG  ASN A 732    12609   8595  10022  -2014    -24    121       C  
ATOM   5339  OD1 ASN A 732     -60.015 -52.087 -46.785  1.00 86.08           O  
ANISOU 5339  OD1 ASN A 732    13047   8988  10670  -2229    -31    -33       O  
ATOM   5340  ND2 ASN A 732     -57.934 -51.950 -45.951  1.00 85.09           N  
ANISOU 5340  ND2 ASN A 732    13154   8905  10272  -1984     41    395       N  
ATOM   5341  N   ALA A 733     -59.425 -47.125 -48.138  1.00 69.56           N  
ANISOU 5341  N   ALA A 733    10532   7580   8318  -1506   -268   -375       N  
ATOM   5342  CA  ALA A 733     -59.396 -45.692 -47.865  1.00 73.36           C  
ANISOU 5342  CA  ALA A 733    10878   8261   8733  -1432   -288   -427       C  
ATOM   5343  C   ALA A 733     -60.795 -45.091 -47.873  1.00 77.94           C  
ANISOU 5343  C   ALA A 733    11228   8961   9427  -1503   -378   -743       C  
ATOM   5344  O   ALA A 733     -61.075 -44.169 -47.097  1.00 79.93           O  
ANISOU 5344  O   ALA A 733    11302   9409   9658  -1554   -347   -807       O  
ATOM   5345  CB  ALA A 733     -58.507 -44.981 -48.884  1.00 69.65           C  
ANISOU 5345  CB  ALA A 733    10569   7738   8158  -1154   -374   -369       C  
ATOM   5346  N   GLN A 734     -61.682 -45.596 -48.734  1.00 83.34           N  
ANISOU 5346  N   GLN A 734    11898   9532  10236  -1490   -509   -970       N  
ATOM   5347  CA  GLN A 734     -63.073 -45.153 -48.705  1.00 89.41           C  
ANISOU 5347  CA  GLN A 734    12398  10424  11148  -1562   -607  -1313       C  
ATOM   5348  C   GLN A 734     -63.709 -45.454 -47.354  1.00 90.37           C  
ANISOU 5348  C   GLN A 734    12271  10719  11347  -1889   -403  -1332       C  
ATOM   5349  O   GLN A 734     -64.293 -44.568 -46.715  1.00 96.83           O  
ANISOU 5349  O   GLN A 734    12850  11764  12178  -1928   -383  -1493       O  
ATOM   5350  CB  GLN A 734     -63.869 -45.821 -49.827  1.00 97.96           C  
ANISOU 5350  CB  GLN A 734    13503  11342  12374  -1507   -795  -1561       C  
ATOM   5351  CG  GLN A 734     -63.397 -45.487 -51.232  1.00103.58           C  
ANISOU 5351  CG  GLN A 734    14480  11900  12976  -1166  -1007  -1582       C  
ATOM   5352  CD  GLN A 734     -64.264 -46.132 -52.300  1.00111.24           C  
ANISOU 5352  CD  GLN A 734    15469  12718  14079  -1094  -1227  -1867       C  
ATOM   5353  OE1 GLN A 734     -65.274 -46.769 -51.996  1.00115.47           O  
ANISOU 5353  OE1 GLN A 734    15776  13269  14828  -1317  -1230  -2076       O  
ATOM   5354  NE2 GLN A 734     -63.871 -45.971 -53.558  1.00111.91           N  
ANISOU 5354  NE2 GLN A 734    15829  12659  14034   -792  -1407  -1885       N  
ATOM   5355  N   GLU A 735     -63.600 -46.707 -46.900  1.00 87.95           N  
ANISOU 5355  N   GLU A 735    12038  10301  11076  -2122   -244  -1169       N  
ATOM   5356  CA  GLU A 735     -64.191 -47.073 -45.615  1.00 83.92           C  
ANISOU 5356  CA  GLU A 735    11342   9941  10603  -2464    -12  -1152       C  
ATOM   5357  C   GLU A 735     -63.577 -46.271 -44.472  1.00 79.42           C  
ANISOU 5357  C   GLU A 735    10748   9583   9846  -2464    127   -977       C  
ATOM   5358  O   GLU A 735     -64.285 -45.850 -43.546  1.00 79.37           O  
ANISOU 5358  O   GLU A 735    10499   9817   9842  -2633    257  -1102       O  
ATOM   5359  CB  GLU A 735     -64.030 -48.574 -45.376  1.00 81.93           C  
ANISOU 5359  CB  GLU A 735    11269   9469  10391  -2700    118   -952       C  
ATOM   5360  CG  GLU A 735     -64.900 -49.431 -46.281  1.00 83.05           C  
ANISOU 5360  CG  GLU A 735    11371   9421  10764  -2788      0  -1181       C  
ATOM   5361  CD  GLU A 735     -64.542 -50.902 -46.217  1.00 84.26           C  
ANISOU 5361  CD  GLU A 735    11785   9280  10949  -2963     76   -960       C  
ATOM   5362  OE1 GLU A 735     -63.390 -51.220 -45.858  1.00 80.28           O  
ANISOU 5362  OE1 GLU A 735    11557   8675  10271  -2881    138   -632       O  
ATOM   5363  OE2 GLU A 735     -65.415 -51.741 -46.527  1.00 89.73           O  
ANISOU 5363  OE2 GLU A 735    12405   9833  11856  -3178     55  -1130       O  
ATOM   5364  N   LEU A 736     -62.263 -46.039 -44.526  1.00 78.10           N  
ANISOU 5364  N   LEU A 736    10813   9343   9518  -2270     99   -713       N  
ATOM   5365  CA  LEU A 736     -61.609 -45.224 -43.507  1.00 79.12           C  
ANISOU 5365  CA  LEU A 736    10922   9659   9482  -2243    185   -570       C  
ATOM   5366  C   LEU A 736     -62.166 -43.807 -43.495  1.00 81.31           C  
ANISOU 5366  C   LEU A 736    10975  10146   9775  -2127     85   -829       C  
ATOM   5367  O   LEU A 736     -62.374 -43.222 -42.425  1.00 82.77           O  
ANISOU 5367  O   LEU A 736    11009  10555   9886  -2214    187   -866       O  
ATOM   5368  CB  LEU A 736     -60.099 -45.199 -43.740  1.00 75.68           C  
ANISOU 5368  CB  LEU A 736    10734   9101   8919  -2041    141   -289       C  
ATOM   5369  CG  LEU A 736     -59.308 -44.266 -42.820  1.00 74.67           C  
ANISOU 5369  CG  LEU A 736    10582   9146   8645  -1979    177   -166       C  
ATOM   5370  CD1 LEU A 736     -59.292 -44.802 -41.395  1.00 76.27           C  
ANISOU 5370  CD1 LEU A 736    10791   9453   8733  -2196    360    -14       C  
ATOM   5371  CD2 LEU A 736     -57.893 -44.050 -43.337  1.00 73.46           C  
ANISOU 5371  CD2 LEU A 736    10603   8883   8425  -1757    102     30       C  
ATOM   5372  N   LEU A 737     -62.414 -43.236 -44.676  1.00 85.99           N  
ANISOU 5372  N   LEU A 737    11568  10659  10447  -1910   -129  -1017       N  
ATOM   5373  CA  LEU A 737     -62.988 -41.896 -44.730  1.00 90.88           C  
ANISOU 5373  CA  LEU A 737    12010  11434  11088  -1770   -269  -1279       C  
ATOM   5374  C   LEU A 737     -64.399 -41.883 -44.158  1.00 97.24           C  
ANISOU 5374  C   LEU A 737    12482  12447  12018  -1945   -212  -1594       C  
ATOM   5375  O   LEU A 737     -64.788 -40.928 -43.474  1.00105.64           O  
ANISOU 5375  O   LEU A 737    13353  13729  13056  -1920   -212  -1758       O  
ATOM   5376  CB  LEU A 737     -62.977 -41.374 -46.167  1.00 93.41           C  
ANISOU 5376  CB  LEU A 737    12463  11589  11441  -1494   -526  -1398       C  
ATOM   5377  CG  LEU A 737     -63.094 -39.858 -46.363  1.00 98.33           C  
ANISOU 5377  CG  LEU A 737    13052  12278  12030  -1275   -714  -1560       C  
ATOM   5378  CD1 LEU A 737     -62.425 -39.457 -47.660  1.00100.88           C  
ANISOU 5378  CD1 LEU A 737    13668  12382  12280  -1023   -889  -1472       C  
ATOM   5379  CD2 LEU A 737     -64.545 -39.389 -46.356  1.00100.59           C  
ANISOU 5379  CD2 LEU A 737    13055  12708  12457  -1252   -851  -1976       C  
ATOM   5380  N   LYS A 738     -65.180 -42.935 -44.419  1.00 99.43           N  
ANISOU 5380  N   LYS A 738    12671  12664  12443  -2127   -159  -1701       N  
ATOM   5381  CA  LYS A 738     -66.526 -43.002 -43.857  1.00101.58           C  
ANISOU 5381  CA  LYS A 738    12582  13155  12860  -2337    -63  -2013       C  
ATOM   5382  C   LYS A 738     -66.486 -43.048 -42.333  1.00 99.94           C  
ANISOU 5382  C   LYS A 738    12272  13177  12524  -2583    236  -1885       C  
ATOM   5383  O   LYS A 738     -67.147 -42.248 -41.658  1.00101.94           O  
ANISOU 5383  O   LYS A 738    12253  13705  12774  -2594    282  -2121       O  
ATOM   5384  CB  LYS A 738     -67.273 -44.214 -44.415  1.00104.10           C  
ANISOU 5384  CB  LYS A 738    12838  13336  13380  -2532    -48  -2126       C  
ATOM   5385  CG  LYS A 738     -67.869 -43.995 -45.797  1.00106.17           C  
ANISOU 5385  CG  LYS A 738    13057  13476  13806  -2298   -370  -2435       C  
ATOM   5386  CD  LYS A 738     -68.710 -45.185 -46.234  1.00110.57           C  
ANISOU 5386  CD  LYS A 738    13499  13917  14595  -2520   -362  -2599       C  
ATOM   5387  CE  LYS A 738     -69.405 -44.915 -47.560  1.00111.61           C  
ANISOU 5387  CE  LYS A 738    13563  13956  14886  -2265   -719  -2962       C  
ATOM   5388  NZ  LYS A 738     -70.223 -46.077 -48.005  1.00114.74           N  
ANISOU 5388  NZ  LYS A 738    13832  14229  15535  -2484   -741  -3154       N  
ATOM   5389  N   LEU A 739     -65.702 -43.973 -41.772  1.00 96.36           N  
ANISOU 5389  N   LEU A 739    12055  12613  11946  -2757    429  -1521       N  
ATOM   5390  CA  LEU A 739     -65.667 -44.127 -40.320  1.00 95.25           C  
ANISOU 5390  CA  LEU A 739    11877  12671  11643  -2993    712  -1378       C  
ATOM   5391  C   LEU A 739     -65.100 -42.884 -39.643  1.00 91.42           C  
ANISOU 5391  C   LEU A 739    11381  12377  10976  -2800    670  -1361       C  
ATOM   5392  O   LEU A 739     -65.693 -42.350 -38.696  1.00 96.69           O  
ANISOU 5392  O   LEU A 739    11826  13332  11578  -2889    805  -1524       O  
ATOM   5393  CB  LEU A 739     -64.852 -45.364 -39.943  1.00 98.46           C  
ANISOU 5393  CB  LEU A 739    12608  12867  11934  -3163    864   -978       C  
ATOM   5394  CG  LEU A 739     -64.703 -45.620 -38.442  1.00102.50           C  
ANISOU 5394  CG  LEU A 739    13178  13544  12223  -3392   1144   -775       C  
ATOM   5395  CD1 LEU A 739     -66.069 -45.725 -37.782  1.00107.99           C  
ANISOU 5395  CD1 LEU A 739    13554  14491  12985  -3704   1388  -1021       C  
ATOM   5396  CD2 LEU A 739     -63.887 -46.877 -38.194  1.00101.91           C  
ANISOU 5396  CD2 LEU A 739    13475  13205  12041  -3514   1232   -384       C  
ATOM   5397  N   ALA A 740     -63.944 -42.408 -40.115  1.00 88.73           N  
ANISOU 5397  N   ALA A 740    11272  11884  10557  -2541    490  -1178       N  
ATOM   5398  CA  ALA A 740     -63.343 -41.219 -39.519  1.00 86.29           C  
ANISOU 5398  CA  ALA A 740    10963  11720  10105  -2369    424  -1165       C  
ATOM   5399  C   ALA A 740     -64.243 -40.001 -39.672  1.00 87.08           C  
ANISOU 5399  C   ALA A 740    10791  11999  10295  -2226    281  -1554       C  
ATOM   5400  O   ALA A 740     -64.221 -39.102 -38.824  1.00 88.87           O  
ANISOU 5400  O   ALA A 740    10921  12430  10416  -2170    292  -1642       O  
ATOM   5401  CB  ALA A 740     -61.971 -40.958 -40.138  1.00 79.26           C  
ANISOU 5401  CB  ALA A 740    10339  10617   9161  -2147    263   -920       C  
ATOM   5402  N   ARG A 741     -65.043 -39.954 -40.740  1.00 91.03           N  
ANISOU 5402  N   ARG A 741    11178  12421  10989  -2142    121  -1810       N  
ATOM   5403  CA  ARG A 741     -66.035 -38.891 -40.862  1.00 95.37           C  
ANISOU 5403  CA  ARG A 741    11453  13141  11640  -1995    -36  -2221       C  
ATOM   5404  C   ARG A 741     -67.130 -39.043 -39.814  1.00 96.38           C  
ANISOU 5404  C   ARG A 741    11236  13594  11790  -2220    195  -2462       C  
ATOM   5405  O   ARG A 741     -67.620 -38.045 -39.271  1.00 99.57           O  
ANISOU 5405  O   ARG A 741    11426  14232  12173  -2113    152  -2732       O  
ATOM   5406  CB  ARG A 741     -66.626 -38.883 -42.271  1.00102.82           C  
ANISOU 5406  CB  ARG A 741    12379  13914  12774  -1831   -292  -2444       C  
ATOM   5407  CG  ARG A 741     -67.700 -37.831 -42.484  1.00112.68           C  
ANISOU 5407  CG  ARG A 741    13353  15315  14144  -1637   -507  -2900       C  
ATOM   5408  CD  ARG A 741     -67.844 -37.475 -43.953  1.00118.46           C  
ANISOU 5408  CD  ARG A 741    14224  15810  14975  -1354   -855  -3037       C  
ATOM   5409  NE  ARG A 741     -68.893 -36.484 -44.170  1.00125.60           N  
ANISOU 5409  NE  ARG A 741    14885  16840  15997  -1132  -1107  -3493       N  
ATOM   5410  CZ  ARG A 741     -69.049 -35.799 -45.297  1.00128.59           C  
ANISOU 5410  CZ  ARG A 741    15421  17024  16414   -803  -1448  -3606       C  
ATOM   5411  NH1 ARG A 741     -68.218 -35.992 -46.311  1.00127.87           N  
ANISOU 5411  NH1 ARG A 741    15704  16641  16239   -703  -1578  -3381       N  
ATOM   5412  NH2 ARG A 741     -70.033 -34.917 -45.408  1.00131.35           N  
ANISOU 5412  NH2 ARG A 741    15588  17452  16868   -546  -1606  -3841       N  
ATOM   5413  N   GLN A 742     -67.523 -40.284 -39.510  1.00 93.54           N  
ANISOU 5413  N   GLN A 742    10824  13250  11468  -2540    451  -2374       N  
ATOM   5414  CA  GLN A 742     -68.468 -40.505 -38.419  1.00 93.59           C  
ANISOU 5414  CA  GLN A 742    10525  13575  11459  -2812    745  -2549       C  
ATOM   5415  C   GLN A 742     -67.887 -40.064 -37.082  1.00 91.48           C  
ANISOU 5415  C   GLN A 742    10340  13508  10912  -2840    922  -2383       C  
ATOM   5416  O   GLN A 742     -68.628 -39.613 -36.201  1.00 93.49           O  
ANISOU 5416  O   GLN A 742    10319  14092  11111  -2912   1080  -2628       O  
ATOM   5417  CB  GLN A 742     -68.873 -41.977 -38.353  1.00 95.83           C  
ANISOU 5417  CB  GLN A 742    10808  13778  11823  -3189   1002  -2422       C  
ATOM   5418  CG  GLN A 742     -69.599 -42.487 -39.584  1.00 97.76           C  
ANISOU 5418  CG  GLN A 742    10927  13854  12365  -3196    835  -2644       C  
ATOM   5419  CD  GLN A 742     -69.949 -43.959 -39.479  1.00100.59           C  
ANISOU 5419  CD  GLN A 742    11309  14096  12817  -3595   1082  -2506       C  
ATOM   5420  OE1 GLN A 742     -69.882 -44.548 -38.399  1.00102.70           O  
ANISOU 5420  OE1 GLN A 742    11633  14457  12932  -3900   1415  -2292       O  
ATOM   5421  NE2 GLN A 742     -70.320 -44.562 -40.602  1.00100.92           N  
ANISOU 5421  NE2 GLN A 742    11335  13911  13098  -3594    909  -2627       N  
ATOM   5422  N   ILE A 743     -66.570 -40.193 -36.909  1.00 86.14           N  
ANISOU 5422  N   ILE A 743    10025  12649  10054  -2772    891  -1991       N  
ATOM   5423  CA  ILE A 743     -65.935 -39.724 -35.682  1.00 81.10           C  
ANISOU 5423  CA  ILE A 743     9485  12182   9146  -2756    998  -1847       C  
ATOM   5424  C   ILE A 743     -65.912 -38.201 -35.640  1.00 83.25           C  
ANISOU 5424  C   ILE A 743     9637  12582   9412  -2453    765  -2106       C  
ATOM   5425  O   ILE A 743     -66.193 -37.590 -34.601  1.00 87.68           O  
ANISOU 5425  O   ILE A 743    10059  13427   9827  -2449    865  -2258       O  
ATOM   5426  CB  ILE A 743     -64.522 -40.321 -35.559  1.00 73.54           C  
ANISOU 5426  CB  ILE A 743     8925  10987   8030  -2749    992  -1387       C  
ATOM   5427  CG1 ILE A 743     -64.614 -41.818 -35.262  1.00 75.86           C  
ANISOU 5427  CG1 ILE A 743     9363  11183   8276  -3066   1250  -1135       C  
ATOM   5428  CG2 ILE A 743     -63.717 -39.598 -34.488  1.00 70.22           C  
ANISOU 5428  CG2 ILE A 743     8612  10708   7360  -2639    984  -1280       C  
ATOM   5429  CD1 ILE A 743     -63.479 -42.622 -35.837  1.00 73.74           C  
ANISOU 5429  CD1 ILE A 743     9441  10573   8003  -3013   1151   -777       C  
ATOM   5430  N   ALA A 744     -65.585 -37.563 -36.766  1.00 82.43           N  
ANISOU 5430  N   ALA A 744     9607  12260   9453  -2193    450  -2163       N  
ATOM   5431  CA  ALA A 744     -65.552 -36.105 -36.804  1.00 81.35           C  
ANISOU 5431  CA  ALA A 744     9405  12181   9325  -1907    199  -2396       C  
ATOM   5432  C   ALA A 744     -66.935 -35.504 -36.597  1.00 87.88           C  
ANISOU 5432  C   ALA A 744     9853  13282  10255  -1858    186  -2878       C  
ATOM   5433  O   ALA A 744     -67.059 -34.421 -36.016  1.00 93.96           O  
ANISOU 5433  O   ALA A 744    10521  14220  10960  -1690     89  -3096       O  
ATOM   5434  CB  ALA A 744     -64.959 -35.627 -38.130  1.00 76.69           C  
ANISOU 5434  CB  ALA A 744     9015  11269   8854  -1669   -113  -2332       C  
ATOM   5435  N   ASN A 745     -67.985 -36.190 -37.054  1.00 87.88           N  
ANISOU 5435  N   ASN A 745     9624  13335  10431  -1997    270  -3074       N  
ATOM   5436  CA  ASN A 745     -69.329 -35.630 -36.950  1.00 91.87           C  
ANISOU 5436  CA  ASN A 745     9718  14114  11076  -1930    237  -3580       C  
ATOM   5437  C   ASN A 745     -69.793 -35.557 -35.500  1.00 93.19           C  
ANISOU 5437  C   ASN A 745     9655  14678  11075  -2096    553  -3708       C  
ATOM   5438  O   ASN A 745     -70.402 -34.563 -35.087  1.00 94.81           O  
ANISOU 5438  O   ASN A 745     9610  15127  11285  -1913    469  -4087       O  
ATOM   5439  CB  ASN A 745     -70.304 -36.457 -37.787  1.00 99.79           C  
ANISOU 5439  CB  ASN A 745    10507  15079  12331  -2062    252  -3768       C  
ATOM   5440  CG  ASN A 745     -71.645 -35.771 -37.966  1.00107.41           C  
ANISOU 5440  CG  ASN A 745    11033  16281  13496  -1910    112  -4342       C  
ATOM   5441  OD1 ASN A 745     -72.560 -35.951 -37.163  1.00112.50           O  
ANISOU 5441  OD1 ASN A 745    11305  17275  14166  -2099    376  -4602       O  
ATOM   5442  ND2 ASN A 745     -71.766 -34.979 -39.025  1.00107.92           N  
ANISOU 5442  ND2 ASN A 745    11146  16161  13697  -1560   -305  -4549       N  
ATOM   5443  N   ALA A 746     -69.514 -36.593 -34.712  1.00 91.35           N  
ANISOU 5443  N   ALA A 746     9525  14509  10675  -2427    912  -3400       N  
ATOM   5444  CA  ALA A 746     -69.941 -36.647 -33.320  1.00 92.62           C  
ANISOU 5444  CA  ALA A 746     9519  15047  10624  -2618   1260  -3478       C  
ATOM   5445  C   ALA A 746     -68.981 -35.935 -32.373  1.00 87.36           C  
ANISOU 5445  C   ALA A 746     9089  14442   9661  -2468   1227  -3311       C  
ATOM   5446  O   ALA A 746     -69.139 -36.046 -31.152  1.00 88.52           O  
ANISOU 5446  O   ALA A 746     9192  14881   9560  -2618   1520  -3304       O  
ATOM   5447  CB  ALA A 746     -70.117 -38.103 -32.881  1.00 94.19           C  
ANISOU 5447  CB  ALA A 746     9772  15264  10753  -3056   1664  -3210       C  
ATOM   5448  N   CYS A 747     -67.999 -35.214 -32.905  1.00 83.51           N  
ANISOU 5448  N   CYS A 747     8851  13690   9187  -2188    883  -3183       N  
ATOM   5449  CA  CYS A 747     -67.044 -34.479 -32.089  1.00 81.81           C  
ANISOU 5449  CA  CYS A 747     8844  13504   8737  -2036    798  -3054       C  
ATOM   5450  C   CYS A 747     -67.564 -33.075 -31.812  1.00 83.31           C  
ANISOU 5450  C   CYS A 747     8813  13892   8949  -1754    600  -3495       C  
ATOM   5451  O   CYS A 747     -68.065 -32.396 -32.712  1.00 84.93           O  
ANISOU 5451  O   CYS A 747     8881  14002   9389  -1540    325  -3780       O  
ATOM   5452  CB  CYS A 747     -65.686 -34.406 -32.787  1.00 79.95           C  
ANISOU 5452  CB  CYS A 747     8966  12883   8529  -1907    545  -2702       C  
ATOM   5453  SG  CYS A 747     -64.417 -33.493 -31.880  1.00 83.14           S  
ANISOU 5453  SG  CYS A 747     9603  13284   8703  -1729    393  -2557       S  
ATOM   5454  N   MET A 748     -67.450 -32.649 -30.554  1.00 82.69           N  
ANISOU 5454  N   MET A 748     8725  14083   8612  -1735    721  -3560       N  
ATOM   5455  CA  MET A 748     -67.929 -31.343 -30.123  1.00 83.26           C  
ANISOU 5455  CA  MET A 748     8597  14366   8673  -1461    547  -3996       C  
ATOM   5456  C   MET A 748     -66.803 -30.330 -29.962  1.00 82.75           C  
ANISOU 5456  C   MET A 748     8802  14108   8531  -1210    224  -3900       C  
ATOM   5457  O   MET A 748     -67.019 -29.264 -29.377  1.00 87.23           O  
ANISOU 5457  O   MET A 748     9270  14839   9033   -989     83  -4220       O  
ATOM   5458  CB  MET A 748     -68.710 -31.477 -28.816  1.00 86.74           C  
ANISOU 5458  CB  MET A 748     8804  15280   8874  -1591    907  -4215       C  
ATOM   5459  CG  MET A 748     -69.492 -32.774 -28.697  1.00 91.62           C  
ANISOU 5459  CG  MET A 748     9254  16069   9487  -1971   1339  -4141       C  
ATOM   5460  SD  MET A 748     -70.682 -32.752 -27.343  1.00101.29           S  
ANISOU 5460  SD  MET A 748    10107  17896  10481  -2115   1782  -4513       S  
ATOM   5461  CE  MET A 748     -71.972 -31.733 -28.052  1.00102.24           C  
ANISOU 5461  CE  MET A 748     9708  18182  10956  -1826   1537  -5196       C  
ATOM   5462  N   ASP A 749     -65.612 -30.640 -30.462  1.00 81.04           N  
ANISOU 5462  N   ASP A 749     8908  13549   8334  -1243    105  -3486       N  
ATOM   5463  CA  ASP A 749     -64.456 -29.749 -30.399  1.00 80.25           C  
ANISOU 5463  CA  ASP A 749     9050  13237   8205  -1053   -192  -3370       C  
ATOM   5464  C   ASP A 749     -64.115 -29.361 -31.834  1.00 82.35           C  
ANISOU 5464  C   ASP A 749     9432  13112   8746   -925   -493  -3305       C  
ATOM   5465  O   ASP A 749     -63.499 -30.141 -32.565  1.00 82.74           O  
ANISOU 5465  O   ASP A 749     9651  12925   8861  -1048   -453  -2966       O  
ATOM   5466  CB  ASP A 749     -63.284 -30.430 -29.699  1.00 78.08           C  
ANISOU 5466  CB  ASP A 749     9038  12922   7708  -1199    -63  -2954       C  
ATOM   5467  CG  ASP A 749     -62.202 -29.453 -29.282  1.00 78.65           C  
ANISOU 5467  CG  ASP A 749     9283  12879   7721  -1019   -337  -2920       C  
ATOM   5468  OD1 ASP A 749     -62.154 -28.336 -29.840  1.00 81.89           O  
ANISOU 5468  OD1 ASP A 749     9682  13120   8314   -814   -646  -3116       O  
ATOM   5469  OD2 ASP A 749     -61.397 -29.805 -28.395  1.00 76.42           O  
ANISOU 5469  OD2 ASP A 749     9161  12661   7213  -1084   -259  -2701       O  
ATOM   5470  N   LYS A 750     -64.512 -28.148 -32.231  1.00 85.39           N  
ANISOU 5470  N   LYS A 750     9749  13424   9272   -666   -797  -3634       N  
ATOM   5471  CA  LYS A 750     -64.366 -27.741 -33.626  1.00 85.31           C  
ANISOU 5471  CA  LYS A 750     9872  13048   9496   -535  -1074  -3595       C  
ATOM   5472  C   LYS A 750     -62.903 -27.661 -34.042  1.00 84.92           C  
ANISOU 5472  C   LYS A 750    10145  12668   9453   -569  -1190  -3201       C  
ATOM   5473  O   LYS A 750     -62.588 -27.785 -35.231  1.00 81.90           O  
ANISOU 5473  O   LYS A 750     9919  11992   9210   -558  -1296  -3030       O  
ATOM   5474  CB  LYS A 750     -65.066 -26.402 -33.863  1.00 86.82           C  
ANISOU 5474  CB  LYS A 750    10003  13098   9885   -206  -1316  -3812       C  
ATOM   5475  CG  LYS A 750     -66.578 -26.465 -33.747  1.00 90.48           C  
ANISOU 5475  CG  LYS A 750    10111  13833  10433   -124  -1222  -4181       C  
ATOM   5476  CD  LYS A 750     -67.214 -25.105 -34.004  1.00 92.13           C  
ANISOU 5476  CD  LYS A 750    10277  13897  10831    230  -1488  -4387       C  
ATOM   5477  CE  LYS A 750     -68.727 -25.159 -33.860  1.00 94.63           C  
ANISOU 5477  CE  LYS A 750    10180  14525  11249    335  -1407  -4802       C  
ATOM   5478  NZ  LYS A 750     -69.364 -23.823 -34.025  1.00 95.67           N  
ANISOU 5478  NZ  LYS A 750    10251  14546  11553    708  -1678  -5029       N  
ATOM   5479  N   ARG A 751     -61.997 -27.447 -33.086  1.00 85.72           N  
ANISOU 5479  N   ARG A 751    10341  12823   9405   -603  -1172  -3066       N  
ATOM   5480  CA  ARG A 751     -60.572 -27.447 -33.403  1.00 82.82           C  
ANISOU 5480  CA  ARG A 751    10224  12180   9065   -658  -1253  -2704       C  
ATOM   5481  C   ARG A 751     -60.116 -28.827 -33.866  1.00 79.67           C  
ANISOU 5481  C   ARG A 751     9907  11714   8651   -859  -1022  -2335       C  
ATOM   5482  O   ARG A 751     -59.542 -28.972 -34.953  1.00 79.01           O  
ANISOU 5482  O   ARG A 751     9973  11351   8697   -869  -1089  -2125       O  
ATOM   5483  CB  ARG A 751     -59.771 -26.978 -32.186  1.00 82.28           C  
ANISOU 5483  CB  ARG A 751    10199  12218   8845   -643  -1300  -2687       C  
ATOM   5484  CG  ARG A 751     -59.407 -25.500 -32.222  1.00 83.73           C  
ANISOU 5484  CG  ARG A 751    10461  12217   9137   -461  -1641  -2870       C  
ATOM   5485  CD  ARG A 751     -59.633 -24.819 -30.879  1.00 90.40           C  
ANISOU 5485  CD  ARG A 751    11223  13266   9858   -343  -1667  -3079       C  
ATOM   5486  NE  ARG A 751     -58.862 -25.429 -29.798  1.00 93.93           N  
ANISOU 5486  NE  ARG A 751    11696  13942  10050   -461  -1556  -2969       N  
ATOM   5487  CZ  ARG A 751     -58.974 -25.087 -28.518  1.00 98.90           C  
ANISOU 5487  CZ  ARG A 751    12280  14799  10498   -380  -1537  -3121       C  
ATOM   5488  NH1 ARG A 751     -59.829 -24.139 -28.158  1.00101.19           N  
ANISOU 5488  NH1 ARG A 751    12468  15119  10859   -186  -1603  -3388       N  
ATOM   5489  NH2 ARG A 751     -58.235 -25.691 -27.596  1.00 99.71           N  
ANISOU 5489  NH2 ARG A 751    12455  15078  10353   -472  -1446  -2974       N  
ATOM   5490  N   ALA A 752     -60.379 -29.857 -33.059  1.00 79.26           N  
ANISOU 5490  N   ALA A 752     9778  11907   8429  -1017   -743  -2256       N  
ATOM   5491  CA  ALA A 752     -60.007 -31.215 -33.441  1.00 77.06           C  
ANISOU 5491  CA  ALA A 752     9596  11548   8135  -1198   -538  -1923       C  
ATOM   5492  C   ALA A 752     -60.855 -31.714 -34.605  1.00 77.82           C  
ANISOU 5492  C   ALA A 752     9628  11543   8399  -1227   -504  -1985       C  
ATOM   5493  O   ALA A 752     -60.364 -32.450 -35.469  1.00 77.62           O  
ANISOU 5493  O   ALA A 752     9738  11306   8448  -1289   -472  -1733       O  
ATOM   5494  CB  ALA A 752     -60.138 -32.149 -32.239  1.00 76.87           C  
ANISOU 5494  CB  ALA A 752     9553  11785   7871  -1365   -261  -1824       C  
ATOM   5495  N   LYS A 753     -62.134 -31.327 -34.634  1.00 78.32           N  
ANISOU 5495  N   LYS A 753     9472  11763   8522  -1164   -522  -2345       N  
ATOM   5496  CA  LYS A 753     -63.006 -31.649 -35.761  1.00 79.22           C  
ANISOU 5496  CA  LYS A 753     9501  11783   8816  -1150   -556  -2474       C  
ATOM   5497  C   LYS A 753     -62.393 -31.176 -37.075  1.00 76.28           C  
ANISOU 5497  C   LYS A 753     9343  11055   8585  -1003   -809  -2359       C  
ATOM   5498  O   LYS A 753     -62.219 -31.958 -38.019  1.00 76.59           O  
ANISOU 5498  O   LYS A 753     9491  10915   8695  -1062   -771  -2174       O  
ATOM   5499  CB  LYS A 753     -64.374 -31.002 -35.534  1.00 82.42           C  
ANISOU 5499  CB  LYS A 753     9613  12420   9283  -1037   -615  -2945       C  
ATOM   5500  CG  LYS A 753     -65.532 -31.588 -36.318  1.00 85.32           C  
ANISOU 5500  CG  LYS A 753     9786  12817   9816  -1077   -577  -3147       C  
ATOM   5501  CD  LYS A 753     -66.771 -30.718 -36.134  1.00 89.33           C  
ANISOU 5501  CD  LYS A 753     9986  13544  10409   -897   -705  -3661       C  
ATOM   5502  CE  LYS A 753     -68.046 -31.432 -36.550  1.00 92.81           C  
ANISOU 5502  CE  LYS A 753    10126  14131  11007   -993   -596  -3918       C  
ATOM   5503  NZ  LYS A 753     -68.455 -32.470 -35.563  1.00 95.40           N  
ANISOU 5503  NZ  LYS A 753    10258  14761  11227  -1319   -173  -3868       N  
ATOM   5504  N   THR A 754     -62.050 -29.887 -37.141  1.00 77.16           N  
ANISOU 5504  N   THR A 754     9537  11054   8727   -814  -1065  -2466       N  
ATOM   5505  CA  THR A 754     -61.379 -29.340 -38.315  1.00 76.64           C  
ANISOU 5505  CA  THR A 754     9718  10641   8762   -700  -1281  -2325       C  
ATOM   5506  C   THR A 754     -60.060 -30.054 -38.580  1.00 74.70           C  
ANISOU 5506  C   THR A 754     9666  10239   8478   -838  -1151  -1901       C  
ATOM   5507  O   THR A 754     -59.725 -30.345 -39.734  1.00 75.18           O  
ANISOU 5507  O   THR A 754     9892  10071   8603   -824  -1181  -1736       O  
ATOM   5508  CB  THR A 754     -61.151 -27.838 -38.130  1.00 77.40           C  
ANISOU 5508  CB  THR A 754     9889  10633   8886   -520  -1555  -2487       C  
ATOM   5509  OG1 THR A 754     -62.408 -27.151 -38.172  1.00 80.34           O  
ANISOU 5509  OG1 THR A 754    10110  11089   9327   -330  -1720  -2886       O  
ATOM   5510  CG2 THR A 754     -60.241 -27.288 -39.217  1.00 77.15           C  
ANISOU 5510  CG2 THR A 754    10155  10230   8929   -466  -1723  -2267       C  
ATOM   5511  N   ASN A 755     -59.302 -30.352 -37.520  1.00 73.70           N  
ANISOU 5511  N   ASN A 755     9524  10243   8236   -953  -1016  -1739       N  
ATOM   5512  CA  ASN A 755     -58.025 -31.039 -37.692  1.00 70.40           C  
ANISOU 5512  CA  ASN A 755     9257   9700   7793  -1056   -913  -1372       C  
ATOM   5513  C   ASN A 755     -58.201 -32.368 -38.417  1.00 70.48           C  
ANISOU 5513  C   ASN A 755     9308   9653   7819  -1151   -745  -1208       C  
ATOM   5514  O   ASN A 755     -57.386 -32.728 -39.276  1.00 71.15           O  
ANISOU 5514  O   ASN A 755     9547   9538   7949  -1153   -737   -978       O  
ATOM   5515  CB  ASN A 755     -57.361 -31.253 -36.332  1.00 73.01           C  
ANISOU 5515  CB  ASN A 755     9550  10213   7978  -1137   -817  -1272       C  
ATOM   5516  CG  ASN A 755     -55.997 -31.907 -36.445  1.00 75.14           C  
ANISOU 5516  CG  ASN A 755     9948  10365   8237  -1206   -751   -932       C  
ATOM   5517  OD1 ASN A 755     -55.280 -31.706 -37.424  1.00 74.01           O  
ANISOU 5517  OD1 ASN A 755     9912  10000   8208  -1177   -817   -795       O  
ATOM   5518  ND2 ASN A 755     -55.633 -32.697 -35.441  1.00 77.88           N  
ANISOU 5518  ND2 ASN A 755    10291  10865   8434  -1289   -619   -801       N  
ATOM   5519  N   LEU A 756     -59.265 -33.107 -38.095  1.00 67.26           N  
ANISOU 5519  N   LEU A 756     8758   9418   7381  -1236   -606  -1339       N  
ATOM   5520  CA  LEU A 756     -59.491 -34.397 -38.739  1.00 65.78           C  
ANISOU 5520  CA  LEU A 756     8610   9157   7227  -1342   -463  -1206       C  
ATOM   5521  C   LEU A 756     -60.057 -34.236 -40.147  1.00 67.94           C  
ANISOU 5521  C   LEU A 756     8926   9249   7640  -1227   -606  -1329       C  
ATOM   5522  O   LEU A 756     -59.689 -34.992 -41.058  1.00 68.12           O  
ANISOU 5522  O   LEU A 756     9090   9095   7699  -1240   -574  -1153       O  
ATOM   5523  CB  LEU A 756     -60.426 -35.252 -37.881  1.00 64.05           C  
ANISOU 5523  CB  LEU A 756     8227   9171   6939  -1516   -248  -1296       C  
ATOM   5524  CG  LEU A 756     -60.786 -36.640 -38.413  1.00 62.89           C  
ANISOU 5524  CG  LEU A 756     8112   8941   6842  -1665    -96  -1184       C  
ATOM   5525  CD1 LEU A 756     -59.537 -37.492 -38.609  1.00 60.75           C  
ANISOU 5525  CD1 LEU A 756     8075   8489   6519  -1700    -38   -815       C  
ATOM   5526  CD2 LEU A 756     -61.769 -37.330 -37.479  1.00 64.24           C  
ANISOU 5526  CD2 LEU A 756     8110   9347   6951  -1878    135  -1290       C  
ATOM   5527  N   LEU A 757     -60.946 -33.258 -40.348  1.00 68.38           N  
ANISOU 5527  N   LEU A 757     8877   9342   7764  -1089   -785  -1645       N  
ATOM   5528  CA  LEU A 757     -61.554 -33.088 -41.665  1.00 69.39           C  
ANISOU 5528  CA  LEU A 757     9066   9296   8003   -947   -961  -1787       C  
ATOM   5529  C   LEU A 757     -60.540 -32.598 -42.693  1.00 73.41           C  
ANISOU 5529  C   LEU A 757     9869   9516   8508   -831  -1092  -1573       C  
ATOM   5530  O   LEU A 757     -60.596 -32.998 -43.864  1.00 75.16           O  
ANISOU 5530  O   LEU A 757    10237   9561   8760   -769  -1142  -1522       O  
ATOM   5531  CB  LEU A 757     -62.742 -32.132 -41.580  1.00 68.36           C  
ANISOU 5531  CB  LEU A 757     8756   9274   7945   -792  -1155  -2200       C  
ATOM   5532  CG  LEU A 757     -63.988 -32.733 -40.928  1.00 70.38           C  
ANISOU 5532  CG  LEU A 757     8683   9815   8244   -905  -1012  -2471       C  
ATOM   5533  CD1 LEU A 757     -65.195 -31.837 -41.139  1.00 71.95           C  
ANISOU 5533  CD1 LEU A 757     8688  10098   8551   -700  -1246  -2922       C  
ATOM   5534  CD2 LEU A 757     -64.251 -34.129 -41.469  1.00 71.56           C  
ANISOU 5534  CD2 LEU A 757     8822   9919   8449  -1069   -855  -2362       C  
ATOM   5535  N   GLN A 758     -59.607 -31.734 -42.279  1.00 75.27           N  
ANISOU 5535  N   GLN A 758    10194   9702   8702   -810  -1142  -1456       N  
ATOM   5536  CA  GLN A 758     -58.556 -31.286 -43.190  1.00 75.75           C  
ANISOU 5536  CA  GLN A 758    10518   9503   8761   -754  -1210  -1230       C  
ATOM   5537  C   GLN A 758     -57.771 -32.466 -43.747  1.00 73.74           C  
ANISOU 5537  C   GLN A 758    10367   9173   8477   -846  -1022   -939       C  
ATOM   5538  O   GLN A 758     -57.359 -32.455 -44.913  1.00 71.85           O  
ANISOU 5538  O   GLN A 758    10337   8730   8231   -777  -1054   -816       O  
ATOM   5539  CB  GLN A 758     -57.615 -30.317 -42.476  1.00 80.76           C  
ANISOU 5539  CB  GLN A 758    11179  10122   9385   -778  -1256  -1148       C  
ATOM   5540  CG  GLN A 758     -58.209 -28.950 -42.193  1.00 90.63           C  
ANISOU 5540  CG  GLN A 758    12413  11351  10672   -643  -1498  -1421       C  
ATOM   5541  CD  GLN A 758     -57.223 -28.024 -41.508  1.00 96.76           C  
ANISOU 5541  CD  GLN A 758    13227  12082  11457   -683  -1558  -1342       C  
ATOM   5542  OE1 GLN A 758     -56.102 -28.421 -41.187  1.00101.42           O  
ANISOU 5542  OE1 GLN A 758    13818  12687  12031   -814  -1416  -1096       O  
ATOM   5543  NE2 GLN A 758     -57.635 -26.782 -41.282  1.00102.00           N  
ANISOU 5543  NE2 GLN A 758    13914  12682  12159   -558  -1794  -1572       N  
ATOM   5544  N   LEU A 759     -57.554 -33.495 -42.926  1.00 69.61           N  
ANISOU 5544  N   LEU A 759     9723   8806   7918   -989   -830   -830       N  
ATOM   5545  CA  LEU A 759     -56.844 -34.682 -43.388  1.00 62.86           C  
ANISOU 5545  CA  LEU A 759     8966   7876   7042  -1052   -674   -580       C  
ATOM   5546  C   LEU A 759     -57.746 -35.582 -44.223  1.00 58.84           C  
ANISOU 5546  C   LEU A 759     8479   7310   6566  -1035   -665   -671       C  
ATOM   5547  O   LEU A 759     -57.293 -36.164 -45.216  1.00 56.72           O  
ANISOU 5547  O   LEU A 759     8373   6886   6290   -990   -636   -533       O  
ATOM   5548  CB  LEU A 759     -56.276 -35.449 -42.194  1.00 60.78           C  
ANISOU 5548  CB  LEU A 759     8613   7763   6717  -1188   -511   -428       C  
ATOM   5549  CG  LEU A 759     -55.330 -34.658 -41.289  1.00 59.89           C  
ANISOU 5549  CG  LEU A 759     8463   7719   6572  -1199   -541   -354       C  
ATOM   5550  CD1 LEU A 759     -54.979 -35.466 -40.052  1.00 58.11           C  
ANISOU 5550  CD1 LEU A 759     8171   7654   6252  -1304   -414   -241       C  
ATOM   5551  CD2 LEU A 759     -54.075 -34.254 -42.046  1.00 59.02           C  
ANISOU 5551  CD2 LEU A 759     8479   7441   6507  -1151   -564   -170       C  
ATOM   5552  N   LEU A 760     -59.022 -35.704 -43.846  1.00 61.26           N  
ANISOU 5552  N   LEU A 760     8610   7749   6917  -1070   -691   -924       N  
ATOM   5553  CA  LEU A 760     -59.925 -36.564 -44.603  1.00 65.44           C  
ANISOU 5553  CA  LEU A 760     9125   8227   7513  -1073   -701  -1047       C  
ATOM   5554  C   LEU A 760     -60.249 -36.020 -45.990  1.00 70.47           C  
ANISOU 5554  C   LEU A 760     9919   8678   8179   -868   -916  -1168       C  
ATOM   5555  O   LEU A 760     -60.593 -36.805 -46.880  1.00 69.08           O  
ANISOU 5555  O   LEU A 760     9818   8395   8034   -836   -939  -1196       O  
ATOM   5556  CB  LEU A 760     -61.232 -36.775 -43.835  1.00 68.34           C  
ANISOU 5556  CB  LEU A 760     9217   8805   7945  -1183   -661  -1319       C  
ATOM   5557  CG  LEU A 760     -61.225 -37.685 -42.608  1.00 71.28           C  
ANISOU 5557  CG  LEU A 760     9467   9347   8268  -1422   -413  -1210       C  
ATOM   5558  CD1 LEU A 760     -62.645 -38.134 -42.299  1.00 75.22           C  
ANISOU 5558  CD1 LEU A 760     9712  10008   8861  -1555   -346  -1487       C  
ATOM   5559  CD2 LEU A 760     -60.311 -38.885 -42.810  1.00 71.13           C  
ANISOU 5559  CD2 LEU A 760     9638   9182   8206  -1506   -280   -890       C  
ATOM   5560  N   ASP A 761     -60.147 -34.705 -46.202  1.00 76.73           N  
ANISOU 5560  N   ASP A 761    10794   9410   8952   -723  -1088  -1240       N  
ATOM   5561  CA  ASP A 761     -60.637 -34.123 -47.448  1.00 80.12           C  
ANISOU 5561  CA  ASP A 761    11401   9659   9382   -511  -1325  -1384       C  
ATOM   5562  C   ASP A 761     -59.747 -34.428 -48.646  1.00 76.02           C  
ANISOU 5562  C   ASP A 761    11195   8920   8771   -441  -1296  -1138       C  
ATOM   5563  O   ASP A 761     -60.222 -34.343 -49.783  1.00 74.07           O  
ANISOU 5563  O   ASP A 761    11126   8525   8493   -271  -1466  -1244       O  
ATOM   5564  CB  ASP A 761     -60.803 -32.610 -47.297  1.00 89.90           C  
ANISOU 5564  CB  ASP A 761    12681  10861  10617   -373  -1535  -1527       C  
ATOM   5565  CG  ASP A 761     -62.077 -32.237 -46.559  1.00 98.74           C  
ANISOU 5565  CG  ASP A 761    13508  12177  11831   -335  -1653  -1901       C  
ATOM   5566  OD1 ASP A 761     -63.059 -33.004 -46.649  1.00102.16           O  
ANISOU 5566  OD1 ASP A 761    13752  12717  12345   -360  -1645  -2105       O  
ATOM   5567  OD2 ASP A 761     -62.097 -31.181 -45.891  1.00101.89           O  
ANISOU 5567  OD2 ASP A 761    13853  12627  12233   -282  -1750  -2008       O  
ATOM   5568  N   ARG A 762     -58.479 -34.779 -48.436  1.00 73.27           N  
ANISOU 5568  N   ARG A 762    10915   8557   8368   -548  -1093   -833       N  
ATOM   5569  CA  ARG A 762     -57.583 -35.057 -49.551  1.00 72.44           C  
ANISOU 5569  CA  ARG A 762    11078   8279   8167   -481  -1029   -614       C  
ATOM   5570  C   ARG A 762     -57.387 -36.548 -49.812  1.00 70.06           C  
ANISOU 5570  C   ARG A 762    10772   7983   7866   -532   -879   -518       C  
ATOM   5571  O   ARG A 762     -56.706 -36.906 -50.777  1.00 66.29           O  
ANISOU 5571  O   ARG A 762    10504   7382   7301   -454   -818   -370       O  
ATOM   5572  CB  ARG A 762     -56.225 -34.377 -49.325  1.00 71.69           C  
ANISOU 5572  CB  ARG A 762    11061   8150   8028   -543   -914   -364       C  
ATOM   5573  CG  ARG A 762     -55.471 -34.802 -48.075  1.00 75.07           C  
ANISOU 5573  CG  ARG A 762    11276   8743   8506   -711   -740   -230       C  
ATOM   5574  CD  ARG A 762     -54.184 -33.990 -47.937  1.00 79.28           C  
ANISOU 5574  CD  ARG A 762    11859   9235   9029   -762   -672    -36       C  
ATOM   5575  NE  ARG A 762     -53.282 -34.515 -46.915  1.00 81.32           N  
ANISOU 5575  NE  ARG A 762    11941   9635   9324   -884   -524    104       N  
ATOM   5576  CZ  ARG A 762     -53.159 -34.012 -45.690  1.00 84.96           C  
ANISOU 5576  CZ  ARG A 762    12233  10221   9826   -965   -556     63       C  
ATOM   5577  NH1 ARG A 762     -53.881 -32.960 -45.323  1.00 87.30           N  
ANISOU 5577  NH1 ARG A 762    12500  10524  10145   -940   -719   -122       N  
ATOM   5578  NH2 ARG A 762     -52.308 -34.559 -44.831  1.00 83.61           N  
ANISOU 5578  NH2 ARG A 762    11935  10166   9666  -1045   -447    191       N  
ATOM   5579  N   ILE A 763     -57.985 -37.422 -48.996  1.00 68.06           N  
ANISOU 5579  N   ILE A 763    10300   7859   7699   -661   -816   -605       N  
ATOM   5580  CA  ILE A 763     -57.822 -38.865 -49.201  1.00 65.04           C  
ANISOU 5580  CA  ILE A 763     9942   7441   7330   -718   -696   -514       C  
ATOM   5581  C   ILE A 763     -58.393 -39.342 -50.535  1.00 63.91           C  
ANISOU 5581  C   ILE A 763     9964   7146   7174   -573   -822   -641       C  
ATOM   5582  O   ILE A 763     -57.704 -40.101 -51.238  1.00 57.98           O  
ANISOU 5582  O   ILE A 763     9383   6287   6359   -514   -745   -497       O  
ATOM   5583  CB  ILE A 763     -58.402 -39.636 -48.004  1.00 62.83           C  
ANISOU 5583  CB  ILE A 763     9429   7308   7137   -919   -597   -568       C  
ATOM   5584  CG1 ILE A 763     -57.584 -39.356 -46.741  1.00 62.85           C  
ANISOU 5584  CG1 ILE A 763     9336   7444   7101  -1034   -465   -395       C  
ATOM   5585  CG2 ILE A 763     -58.432 -41.131 -48.291  1.00 59.27           C  
ANISOU 5585  CG2 ILE A 763     9036   6765   6719   -982   -516   -507       C  
ATOM   5586  CD1 ILE A 763     -58.015 -40.166 -45.543  1.00 61.81           C  
ANISOU 5586  CD1 ILE A 763     9044   7446   6995  -1234   -338   -394       C  
ATOM   5587  N   PRO A 764     -59.615 -38.961 -50.943  1.00 67.01           N  
ANISOU 5587  N   PRO A 764    10313   7526   7621   -487  -1030   -928       N  
ATOM   5588  CA  PRO A 764     -60.165 -39.544 -52.183  1.00 69.32           C  
ANISOU 5588  CA  PRO A 764    10762   7675   7903   -340  -1176  -1069       C  
ATOM   5589  C   PRO A 764     -59.309 -39.294 -53.414  1.00 70.03           C  
ANISOU 5589  C   PRO A 764    11202   7600   7807   -143  -1193   -911       C  
ATOM   5590  O   PRO A 764     -59.098 -40.218 -54.213  1.00 78.66           O  
ANISOU 5590  O   PRO A 764    12447   8590   8849    -70  -1173   -878       O  
ATOM   5591  CB  PRO A 764     -61.544 -38.875 -52.301  1.00 70.40           C  
ANISOU 5591  CB  PRO A 764    10768   7851   8130   -251  -1432  -1424       C  
ATOM   5592  CG  PRO A 764     -61.446 -37.643 -51.475  1.00 66.67           C  
ANISOU 5592  CG  PRO A 764    10194   7487   7652   -272  -1439  -1421       C  
ATOM   5593  CD  PRO A 764     -60.570 -38.020 -50.331  1.00 64.37           C  
ANISOU 5593  CD  PRO A 764     9780   7313   7364   -492  -1166  -1171       C  
ATOM   5594  N   THR A 765     -58.802 -38.071 -53.592  1.00 66.67           N  
ANISOU 5594  N   THR A 765    10919   7141   7272    -62  -1220   -814       N  
ATOM   5595  CA  THR A 765     -57.933 -37.801 -54.732  1.00 63.41           C  
ANISOU 5595  CA  THR A 765    10849   6584   6661     87  -1181   -635       C  
ATOM   5596  C   THR A 765     -56.641 -38.602 -54.640  1.00 55.26           C  
ANISOU 5596  C   THR A 765     9829   5580   5588      2   -901   -366       C  
ATOM   5597  O   THR A 765     -56.112 -39.057 -55.662  1.00 56.01           O  
ANISOU 5597  O   THR A 765    10155   5584   5544    125   -839   -281       O  
ATOM   5598  CB  THR A 765     -57.630 -36.306 -54.829  1.00 64.55           C  
ANISOU 5598  CB  THR A 765    11145   6668   6713    138  -1244   -564       C  
ATOM   5599  OG1 THR A 765     -57.286 -35.798 -53.535  1.00 65.11           O  
ANISOU 5599  OG1 THR A 765    10968   6870   6902    -44  -1147   -496       O  
ATOM   5600  CG2 THR A 765     -58.837 -35.558 -55.364  1.00 68.36           C  
ANISOU 5600  CG2 THR A 765    11741   7057   7177    327  -1575   -837       C  
ATOM   5601  N   ILE A 766     -56.120 -38.789 -53.425  1.00 52.39           N  
ANISOU 5601  N   ILE A 766     9223   5350   5335   -186   -742   -248       N  
ATOM   5602  CA  ILE A 766     -54.936 -39.627 -53.248  1.00 54.55           C  
ANISOU 5602  CA  ILE A 766     9477   5657   5595   -242   -515    -29       C  
ATOM   5603  C   ILE A 766     -55.209 -41.044 -53.729  1.00 53.79           C  
ANISOU 5603  C   ILE A 766     9433   5494   5512   -185   -519    -91       C  
ATOM   5604  O   ILE A 766     -54.379 -41.647 -54.416  1.00 53.12           O  
ANISOU 5604  O   ILE A 766     9492   5356   5335    -86   -407     23       O  
ATOM   5605  CB  ILE A 766     -54.475 -39.625 -51.779  1.00 54.50           C  
ANISOU 5605  CB  ILE A 766     9210   5797   5699   -429   -403     73       C  
ATOM   5606  CG1 ILE A 766     -54.010 -38.240 -51.342  1.00 54.04           C  
ANISOU 5606  CG1 ILE A 766     9112   5787   5632   -480   -399    140       C  
ATOM   5607  CG2 ILE A 766     -53.339 -40.605 -51.595  1.00 55.40           C  
ANISOU 5607  CG2 ILE A 766     9303   5936   5811   -447   -221    261       C  
ATOM   5608  CD1 ILE A 766     -53.764 -38.150 -49.846  1.00 52.91           C  
ANISOU 5608  CD1 ILE A 766     8718   5798   5587   -642   -345    182       C  
ATOM   5609  N   SER A 767     -56.370 -41.601 -53.374  1.00 55.90           N  
ANISOU 5609  N   SER A 767     9575   5762   5902   -251   -643   -288       N  
ATOM   5610  CA  SER A 767     -56.658 -42.985 -53.743  1.00 57.24           C  
ANISOU 5610  CA  SER A 767     9790   5840   6120   -234   -659   -354       C  
ATOM   5611  C   SER A 767     -56.918 -43.119 -55.239  1.00 58.59           C  
ANISOU 5611  C   SER A 767    10223   5868   6171     -4   -796   -475       C  
ATOM   5612  O   SER A 767     -56.504 -44.108 -55.862  1.00 58.69           O  
ANISOU 5612  O   SER A 767    10376   5787   6135     90   -756   -444       O  
ATOM   5613  CB  SER A 767     -57.846 -43.508 -52.936  1.00 62.72           C  
ANISOU 5613  CB  SER A 767    10262   6573   6995   -415   -732   -533       C  
ATOM   5614  OG  SER A 767     -59.014 -42.750 -53.190  1.00 67.39           O  
ANISOU 5614  OG  SER A 767    10784   7188   7632   -374   -929   -792       O  
ATOM   5615  N   THR A 768     -57.604 -42.138 -55.832  1.00 58.69           N  
ANISOU 5615  N   THR A 768    10327   5855   6119    112   -978   -627       N  
ATOM   5616  CA  THR A 768     -57.812 -42.143 -57.278  1.00 57.38           C  
ANISOU 5616  CA  THR A 768    10463   5551   5787    361  -1127   -732       C  
ATOM   5617  C   THR A 768     -56.479 -42.093 -58.017  1.00 56.97           C  
ANISOU 5617  C   THR A 768    10664   5469   5515    481   -931   -492       C  
ATOM   5618  O   THR A 768     -56.207 -42.916 -58.907  1.00 59.12           O  
ANISOU 5618  O   THR A 768    11126   5659   5678    631   -917   -509       O  
ATOM   5619  CB  THR A 768     -58.699 -40.962 -57.676  1.00 54.22           C  
ANISOU 5619  CB  THR A 768    10143   5121   5338    480  -1374   -914       C  
ATOM   5620  OG1 THR A 768     -59.938 -41.030 -56.958  1.00 55.83           O  
ANISOU 5620  OG1 THR A 768    10053   5392   5766    371  -1537  -1173       O  
ATOM   5621  CG2 THR A 768     -58.982 -40.978 -59.171  1.00 49.95           C  
ANISOU 5621  CG2 THR A 768     9956   4428   4593    762  -1565  -1034       C  
ATOM   5622  N   GLN A 769     -55.625 -41.135 -57.644  1.00 54.93           N  
ANISOU 5622  N   GLN A 769    10392   5282   5195    409   -769   -284       N  
ATOM   5623  CA  GLN A 769     -54.283 -41.079 -58.211  1.00 57.87           C  
ANISOU 5623  CA  GLN A 769    10928   5664   5394    470   -529    -55       C  
ATOM   5624  C   GLN A 769     -53.516 -42.367 -57.953  1.00 58.55           C  
ANISOU 5624  C   GLN A 769    10905   5794   5545    448   -357     26       C  
ATOM   5625  O   GLN A 769     -52.696 -42.774 -58.779  1.00 61.04           O  
ANISOU 5625  O   GLN A 769    11389   6097   5706    586   -215    105       O  
ATOM   5626  CB  GLN A 769     -53.520 -39.883 -57.641  1.00 56.25           C  
ANISOU 5626  CB  GLN A 769    10651   5534   5187    334   -385    138       C  
ATOM   5627  CG  GLN A 769     -54.116 -38.536 -58.007  1.00 61.41           C  
ANISOU 5627  CG  GLN A 769    11485   6100   5748    381   -554     85       C  
ATOM   5628  CD  GLN A 769     -53.325 -37.374 -57.436  1.00 66.51           C  
ANISOU 5628  CD  GLN A 769    12072   6786   6414    226   -419    273       C  
ATOM   5629  OE1 GLN A 769     -52.201 -37.545 -56.962  1.00 72.76           O  
ANISOU 5629  OE1 GLN A 769    12707   7680   7258    101   -177    451       O  
ATOM   5630  NE2 GLN A 769     -53.911 -36.183 -57.476  1.00 67.26           N  
ANISOU 5630  NE2 GLN A 769    12287   6789   6479    243   -601    214       N  
ATOM   5631  N   LEU A 770     -53.776 -43.027 -56.823  1.00 54.92           N  
ANISOU 5631  N   LEU A 770    10185   5383   5297    289   -370      2       N  
ATOM   5632  CA  LEU A 770     -53.099 -44.284 -56.522  1.00 52.17           C  
ANISOU 5632  CA  LEU A 770     9770   5039   5013    285   -251     76       C  
ATOM   5633  C   LEU A 770     -53.477 -45.358 -57.531  1.00 51.37           C  
ANISOU 5633  C   LEU A 770     9867   4796   4854    464   -355    -73       C  
ATOM   5634  O   LEU A 770     -52.610 -46.059 -58.063  1.00 56.09           O  
ANISOU 5634  O   LEU A 770    10572   5376   5365    604   -239    -11       O  
ATOM   5635  CB  LEU A 770     -53.433 -44.741 -55.100  1.00 53.06           C  
ANISOU 5635  CB  LEU A 770     9627   5201   5334     71   -265     88       C  
ATOM   5636  CG  LEU A 770     -52.842 -46.091 -54.681  1.00 52.68           C  
ANISOU 5636  CG  LEU A 770     9548   5112   5358     66   -190    165       C  
ATOM   5637  CD1 LEU A 770     -51.325 -46.015 -54.574  1.00 53.93           C  
ANISOU 5637  CD1 LEU A 770     9669   5366   5456    136      5    358       C  
ATOM   5638  CD2 LEU A 770     -53.449 -46.565 -53.372  1.00 49.67           C  
ANISOU 5638  CD2 LEU A 770     8989   4741   5144   -157   -228    164       C  
ATOM   5639  N   LYS A 771     -54.776 -45.502 -57.808  1.00 44.23           N  
ANISOU 5639  N   LYS A 771     9000   3797   4009    471   -588   -297       N  
ATOM   5640  CA  LYS A 771     -55.202 -46.508 -58.776  1.00 45.96           C  
ANISOU 5640  CA  LYS A 771     9408   3866   4189    640   -727   -473       C  
ATOM   5641  C   LYS A 771     -54.662 -46.199 -60.166  1.00 52.60           C  
ANISOU 5641  C   LYS A 771    10561   4679   4744    911   -695   -464       C  
ATOM   5642  O   LYS A 771     -54.175 -47.098 -60.865  1.00 56.87           O  
ANISOU 5642  O   LYS A 771    11261   5156   5192   1082   -657   -489       O  
ATOM   5643  CB  LYS A 771     -56.727 -46.608 -58.797  1.00 52.35           C  
ANISOU 5643  CB  LYS A 771    10154   4595   5140    584   -999   -747       C  
ATOM   5644  CG  LYS A 771     -57.319 -47.151 -57.508  1.00 58.85           C  
ANISOU 5644  CG  LYS A 771    10687   5439   6234    300   -996   -772       C  
ATOM   5645  CD  LYS A 771     -58.813 -47.376 -57.637  1.00 63.31           C  
ANISOU 5645  CD  LYS A 771    11156   5934   6963    237  -1243  -1079       C  
ATOM   5646  CE  LYS A 771     -59.548 -46.075 -57.895  1.00 60.54           C  
ANISOU 5646  CE  LYS A 771    10774   5664   6563    308  -1400  -1227       C  
ATOM   5647  NZ  LYS A 771     -61.014 -46.298 -58.016  1.00 61.04           N  
ANISOU 5647  NZ  LYS A 771    10692   5686   6816    263  -1657  -1571       N  
ATOM   5648  N   ILE A 772     -54.722 -44.930 -60.580  1.00 49.33           N  
ANISOU 5648  N   ILE A 772    10264   4306   4173    959   -705   -427       N  
ATOM   5649  CA  ILE A 772     -54.217 -44.569 -61.904  1.00 50.91           C  
ANISOU 5649  CA  ILE A 772    10809   4478   4057   1197   -648   -391       C  
ATOM   5650  C   ILE A 772     -52.722 -44.857 -62.004  1.00 49.61           C  
ANISOU 5650  C   ILE A 772    10647   4413   3788   1226   -317   -176       C  
ATOM   5651  O   ILE A 772     -52.252 -45.482 -62.964  1.00 51.46           O  
ANISOU 5651  O   ILE A 772    11093   4624   3838   1437   -248   -209       O  
ATOM   5652  CB  ILE A 772     -54.533 -43.095 -62.216  1.00 52.76           C  
ANISOU 5652  CB  ILE A 772    11195   4707   4144   1212   -717   -354       C  
ATOM   5653  CG1 ILE A 772     -56.046 -42.880 -62.292  1.00 59.79           C  
ANISOU 5653  CG1 ILE A 772    12092   5501   5126   1258  -1086   -629       C  
ATOM   5654  CG2 ILE A 772     -53.862 -42.671 -63.513  1.00 51.74           C  
ANISOU 5654  CG2 ILE A 772    11456   4551   3651   1419   -592   -253       C  
ATOM   5655  CD1 ILE A 772     -56.451 -41.442 -62.533  1.00 64.64           C  
ANISOU 5655  CD1 ILE A 772    12866   6080   5613   1304  -1216   -623       C  
ATOM   5656  N   LEU A 773     -51.953 -44.416 -61.006  1.00 48.08           N  
ANISOU 5656  N   LEU A 773    10203   4347   3720   1028   -118     20       N  
ATOM   5657  CA  LEU A 773     -50.501 -44.541 -61.075  1.00 48.72           C  
ANISOU 5657  CA  LEU A 773    10233   4551   3726   1049    194    202       C  
ATOM   5658  C   LEU A 773     -50.051 -45.989 -60.954  1.00 69.11           C  
ANISOU 5658  C   LEU A 773    12736   7125   6399   1148    226    148       C  
ATOM   5659  O   LEU A 773     -49.041 -46.374 -61.556  1.00 73.61           O  
ANISOU 5659  O   LEU A 773    13369   7765   6835   1300    427    193       O  
ATOM   5660  CB  LEU A 773     -49.851 -43.684 -59.989  1.00 47.20           C  
ANISOU 5660  CB  LEU A 773     9771   4488   3674    814    347    388       C  
ATOM   5661  CG  LEU A 773     -50.019 -42.169 -60.159  1.00 53.23           C  
ANISOU 5661  CG  LEU A 773    10640   5247   4338    722    354    472       C  
ATOM   5662  CD1 LEU A 773     -49.504 -41.418 -58.935  1.00 52.84           C  
ANISOU 5662  CD1 LEU A 773    10296   5304   4476    480    448    612       C  
ATOM   5663  CD2 LEU A 773     -49.332 -41.685 -61.421  1.00 49.68           C  
ANISOU 5663  CD2 LEU A 773    10484   4801   3590    846    552    569       C  
ATOM   5664  N   ALA A 774     -50.773 -46.803 -60.179  1.00 61.05           N  
ANISOU 5664  N   ALA A 774    11583   6014   5601   1061     39     48       N  
ATOM   5665  CA  ALA A 774     -50.468 -48.227 -60.126  1.00 54.54           C  
ANISOU 5665  CA  ALA A 774    10751   5114   4858   1166     20    -14       C  
ATOM   5666  C   ALA A 774     -50.793 -48.907 -61.449  1.00 51.20           C  
ANISOU 5666  C   ALA A 774    10625   4566   4263   1430    -91   -202       C  
ATOM   5667  O   ALA A 774     -50.065 -49.807 -61.885  1.00 52.79           O  
ANISOU 5667  O   ALA A 774    10899   4753   4405   1621    -15   -234       O  
ATOM   5668  CB  ALA A 774     -51.233 -48.887 -58.983  1.00 55.01           C  
ANISOU 5668  CB  ALA A 774    10642   5077   5182    969   -144    -55       C  
ATOM   5669  N   THR A 775     -51.886 -48.496 -62.102  1.00 51.59           N  
ANISOU 5669  N   THR A 775    10850   4524   4229   1470   -295   -354       N  
ATOM   5670  CA  THR A 775     -52.190 -49.042 -63.422  1.00 60.73           C  
ANISOU 5670  CA  THR A 775    12318   5569   5188   1747   -425   -549       C  
ATOM   5671  C   THR A 775     -51.119 -48.657 -64.435  1.00 61.13           C  
ANISOU 5671  C   THR A 775    12575   5741   4909   1961   -172   -453       C  
ATOM   5672  O   THR A 775     -50.772 -49.454 -65.316  1.00 63.97           O  
ANISOU 5672  O   THR A 775    13131   6065   5110   2215   -158   -566       O  
ATOM   5673  CB  THR A 775     -53.568 -48.569 -63.887  1.00 63.35           C  
ANISOU 5673  CB  THR A 775    12784   5792   5495   1763   -723   -744       C  
ATOM   5674  OG1 THR A 775     -54.557 -48.964 -62.930  1.00 64.39           O  
ANISOU 5674  OG1 THR A 775    12679   5840   5948   1540   -917   -850       O  
ATOM   5675  CG2 THR A 775     -53.915 -49.176 -65.240  1.00 57.01           C  
ANISOU 5675  CG2 THR A 775    12317   4865   4482   2069   -900   -972       C  
ATOM   5676  N   VAL A 776     -50.573 -47.444 -64.320  1.00 59.01           N  
ANISOU 5676  N   VAL A 776    12269   5617   4536   1851     41   -252       N  
ATOM   5677  CA  VAL A 776     -49.503 -47.024 -65.221  1.00 59.65           C  
ANISOU 5677  CA  VAL A 776    12522   5831   4312   1995    341   -135       C  
ATOM   5678  C   VAL A 776     -48.226 -47.805 -64.936  1.00 61.64           C  
ANISOU 5678  C   VAL A 776    12571   6216   4635   2045    597    -72       C  
ATOM   5679  O   VAL A 776     -47.523 -48.232 -65.862  1.00 64.70           O  
ANISOU 5679  O   VAL A 776    13114   6673   4795   2278    766   -118       O  
ATOM   5680  CB  VAL A 776     -49.280 -45.503 -65.111  1.00 57.17           C  
ANISOU 5680  CB  VAL A 776    12218   5601   3903   1817    496     71       C  
ATOM   5681  CG1 VAL A 776     -48.076 -45.074 -65.938  1.00 59.27           C  
ANISOU 5681  CG1 VAL A 776    12622   6017   3879   1896    872    220       C  
ATOM   5682  CG2 VAL A 776     -50.519 -44.760 -65.562  1.00 56.80           C  
ANISOU 5682  CG2 VAL A 776    12429   5408   3745   1846    211    -23       C  
ATOM   5683  N   LYS A 777     -47.909 -48.012 -63.655  1.00 60.44           N  
ANISOU 5683  N   LYS A 777    12074   6107   4785   1852    617     17       N  
ATOM   5684  CA  LYS A 777     -46.703 -48.752 -63.292  1.00 64.45           C  
ANISOU 5684  CA  LYS A 777    12371   6734   5385   1922    810     58       C  
ATOM   5685  C   LYS A 777     -46.784 -50.204 -63.745  1.00 63.08           C  
ANISOU 5685  C   LYS A 777    12326   6431   5209   2184    668   -142       C  
ATOM   5686  O   LYS A 777     -45.785 -50.778 -64.195  1.00 65.09           O  
ANISOU 5686  O   LYS A 777    12569   6788   5372   2397    844   -181       O  
ATOM   5687  CB  LYS A 777     -46.481 -48.672 -61.780  1.00 67.39           C  
ANISOU 5687  CB  LYS A 777    12394   7148   6065   1678    794    183       C  
ATOM   5688  CG  LYS A 777     -45.418 -49.618 -61.242  1.00 70.24           C  
ANISOU 5688  CG  LYS A 777    12543   7579   6565   1779    883    188       C  
ATOM   5689  CD  LYS A 777     -44.042 -49.296 -61.798  1.00 74.88           C  
ANISOU 5689  CD  LYS A 777    13030   8405   7017   1895   1222    241       C  
ATOM   5690  CE  LYS A 777     -43.001 -50.272 -61.272  1.00 78.86           C  
ANISOU 5690  CE  LYS A 777    13304   8984   7676   2043   1267    201       C  
ATOM   5691  NZ  LYS A 777     -41.642 -49.971 -61.798  1.00 82.89           N  
ANISOU 5691  NZ  LYS A 777    13647   9762   8083   2152   1615    215       N  
ATOM   5692  N   ALA A 778     -47.967 -50.814 -63.639  1.00 60.08           N  
ANISOU 5692  N   ALA A 778    12060   5826   4943   2170    346   -288       N  
ATOM   5693  CA  ALA A 778     -48.115 -52.214 -64.024  1.00 59.33           C  
ANISOU 5693  CA  ALA A 778    12103   5559   4879   2392    173   -487       C  
ATOM   5694  C   ALA A 778     -47.890 -52.421 -65.517  1.00 74.57           C  
ANISOU 5694  C   ALA A 778    14341   7511   6481   2722    228   -641       C  
ATOM   5695  O   ALA A 778     -47.406 -53.481 -65.930  1.00 74.47           O  
ANISOU 5695  O   ALA A 778    14407   7452   6436   2975    216   -780       O  
ATOM   5696  CB  ALA A 778     -49.497 -52.726 -63.621  1.00 58.33           C  
ANISOU 5696  CB  ALA A 778    12021   5182   4959   2255   -171   -617       C  
ATOM   5697  N   THR A 779     -48.232 -51.432 -66.340  1.00 77.39           N  
ANISOU 5697  N   THR A 779    14901   7929   6573   2742    276   -625       N  
ATOM   5698  CA  THR A 779     -48.086 -51.540 -67.784  1.00 77.66           C  
ANISOU 5698  CA  THR A 779    15281   7989   6237   3056    329   -760       C  
ATOM   5699  C   THR A 779     -46.708 -51.115 -68.275  1.00 80.17           C  
ANISOU 5699  C   THR A 779    15573   8577   6310   3158    762   -629       C  
ATOM   5700  O   THR A 779     -46.487 -51.057 -69.488  1.00 84.16           O  
ANISOU 5700  O   THR A 779    16379   9149   6451   3401    880   -707       O  
ATOM   5701  CB  THR A 779     -49.162 -50.711 -68.487  1.00 78.07           C  
ANISOU 5701  CB  THR A 779    15624   7954   6087   3058    143   -813       C  
ATOM   5702  OG1 THR A 779     -49.035 -49.335 -68.103  1.00 77.75           O  
ANISOU 5702  OG1 THR A 779    15495   8032   6016   2819    313   -575       O  
ATOM   5703  CG2 THR A 779     -50.543 -51.212 -68.103  1.00 78.29           C  
ANISOU 5703  CG2 THR A 779    15641   7737   6370   2977   -285  -1003       C  
ATOM   5704  N   SER A 780     -45.783 -50.819 -67.367  1.00 83.27           N  
ANISOU 5704  N   SER A 780    15612   9135   6890   2975   1003   -444       N  
ATOM   5705  CA  SER A 780     -44.431 -50.426 -67.735  1.00 89.66           C  
ANISOU 5705  CA  SER A 780    16314  10224   7529   3029   1433   -337       C  
ATOM   5706  C   SER A 780     -43.353 -51.329 -67.159  1.00 92.94           C  
ANISOU 5706  C   SER A 780    16408  10753   8151   3132   1549   -384       C  
ATOM   5707  O   SER A 780     -42.327 -51.528 -67.812  1.00 94.74           O  
ANISOU 5707  O   SER A 780    16606  11188   8203   3333   1843   -437       O  
ATOM   5708  CB  SER A 780     -44.154 -48.980 -67.294  1.00 88.30           C  
ANISOU 5708  CB  SER A 780    15996  10185   7368   2709   1656    -74       C  
ATOM   5709  OG  SER A 780     -44.274 -48.846 -65.890  1.00 86.09           O  
ANISOU 5709  OG  SER A 780    15381   9867   7461   2446   1533     26       O  
ATOM   5710  N   MET A 781     -43.549 -51.875 -65.961  1.00 95.79           N  
ANISOU 5710  N   MET A 781    16537  10991   8867   3012   1329   -372       N  
ATOM   5711  CA  MET A 781     -42.561 -52.780 -65.394  1.00102.09           C  
ANISOU 5711  CA  MET A 781    17071  11860   9857   3149   1378   -428       C  
ATOM   5712  C   MET A 781     -42.557 -54.100 -66.155  1.00110.98           C  
ANISOU 5712  C   MET A 781    18415  12863  10888   3527   1237   -688       C  
ATOM   5713  O   MET A 781     -43.569 -54.521 -66.722  1.00114.51           O  
ANISOU 5713  O   MET A 781    19177  13084  11246   3617    981   -826       O  
ATOM   5714  CB  MET A 781     -42.837 -53.025 -63.911  1.00 97.84           C  
ANISOU 5714  CB  MET A 781    16304  11191   9682   2928   1156   -331       C  
ATOM   5715  CG  MET A 781     -44.048 -53.898 -63.625  1.00 96.42           C  
ANISOU 5715  CG  MET A 781    16323  10676   9638   2915    764   -435       C  
ATOM   5716  SD  MET A 781     -44.217 -54.257 -61.865  1.00 93.40           S  
ANISOU 5716  SD  MET A 781    15695  10162   9630   2660    568   -298       S  
ATOM   5717  CE  MET A 781     -45.673 -55.298 -61.870  1.00 93.49           C  
ANISOU 5717  CE  MET A 781    15991   9781   9750   2636    175   -446       C  
ATOM   5718  N   GLY A 782     -41.399 -54.752 -66.167  1.00119.64           N  
ANISOU 5718  N   GLY A 782    19329  14111  12018   3764   1389   -780       N  
ATOM   5719  CA  GLY A 782     -41.239 -55.979 -66.920  1.00123.49           C  
ANISOU 5719  CA  GLY A 782    20011  14504  12404   4164   1277  -1049       C  
ATOM   5720  C   GLY A 782     -40.968 -55.725 -68.388  1.00129.78           C  
ANISOU 5720  C   GLY A 782    21038  15484  12789   4402   1533  -1170       C  
ATOM   5721  O   GLY A 782     -41.757 -56.121 -69.251  1.00132.95           O  
ANISOU 5721  O   GLY A 782    21811  15710  12994   4574   1342  -1332       O  
ATOM   5722  N   GLY A 783     -39.856 -55.056 -68.681  1.00134.09           N  
ANISOU 5722  N   GLY A 783    21367  16386  13194   4405   1969  -1097       N  
ATOM   5723  CA  GLY A 783     -39.472 -54.760 -70.044  1.00138.16           C  
ANISOU 5723  CA  GLY A 783    22092  17118  13284   4607   2289  -1183       C  
ATOM   5724  C   GLY A 783     -39.995 -53.418 -70.527  1.00131.93           C  
ANISOU 5724  C   GLY A 783    21515  16375  12237   4341   2455   -969       C  
ATOM   5725  O   GLY A 783     -40.796 -52.743 -69.876  1.00125.94           O  
ANISOU 5725  O   GLY A 783    20766  15457  11630   4027   2274   -789       O  
ATOM   5726  N   GLY A 784     -39.518 -53.028 -71.707  1.00134.58           N  
ANISOU 5726  N   GLY A 784    21978  16928  12229   4428   2768   -970       N  
ATOM   5727  CA  GLY A 784     -39.956 -51.795 -72.330  1.00133.01           C  
ANISOU 5727  CA  GLY A 784    21988  16740  11808   4170   2879   -748       C  
ATOM   5728  C   GLY A 784     -39.058 -50.610 -72.042  1.00133.77           C  
ANISOU 5728  C   GLY A 784    21819  17104  11904   3857   3335   -502       C  
ATOM   5729  O   GLY A 784     -37.829 -50.736 -72.037  1.00138.91           O  
ANISOU 5729  O   GLY A 784    22138  18051  12590   3898   3696   -540       O  
ATOM   5730  N   ASP A 785     -39.664 -49.452 -71.802  1.00127.40           N  
ANISOU 5730  N   ASP A 785    21132  16188  11088   3535   3302   -264       N  
ATOM   5731  CA  ASP A 785     -38.912 -48.234 -71.546  1.00123.86           C  
ANISOU 5731  CA  ASP A 785    20455  15935  10670   3183   3687    -12       C  
ATOM   5732  C   ASP A 785     -38.394 -48.212 -70.113  1.00112.32           C  
ANISOU 5732  C   ASP A 785    18570  14556   9552   3036   3761     42       C  
ATOM   5733  O   ASP A 785     -39.043 -48.706 -69.186  1.00108.78           O  
ANISOU 5733  O   ASP A 785    18018  13898   9416   3020   3351     -6       O  
ATOM   5734  CB  ASP A 785     -39.785 -47.005 -71.806  1.00127.95           C  
ANISOU 5734  CB  ASP A 785    21265  16262  11090   2909   3559    208       C  
ATOM   5735  CG  ASP A 785     -38.972 -45.736 -71.995  1.00134.80           C  
ANISOU 5735  CG  ASP A 785    21991  17308  11920   2562   3958    450       C  
ATOM   5736  OD1 ASP A 785     -37.758 -45.747 -71.702  1.00138.20           O  
ANISOU 5736  OD1 ASP A 785    22031  18022  12457   2476   4335    460       O  
ATOM   5737  OD2 ASP A 785     -39.553 -44.721 -72.436  1.00136.05           O  
ANISOU 5737  OD2 ASP A 785    22421  17313  11959   2378   3878    614       O  
ATOM   5738  N   ALA A 786     -37.207 -47.631 -69.939  1.00112.70           N  
ANISOU 5738  N   ALA A 786    18257  14892   9672   2849   4194    148       N  
ATOM   5739  CA  ALA A 786     -36.615 -47.468 -68.617  1.00106.18           C  
ANISOU 5739  CA  ALA A 786    16894  14145   9305   2621   4171    210       C  
ATOM   5740  C   ALA A 786     -37.005 -46.143 -67.974  1.00103.10           C  
ANISOU 5740  C   ALA A 786    16489  13644   9038   2191   4141    479       C  
ATOM   5741  O   ALA A 786     -37.254 -46.091 -66.764  1.00 97.14           O  
ANISOU 5741  O   ALA A 786    15485  12784   8641   2035   3867    520       O  
ATOM   5742  CB  ALA A 786     -35.091 -47.578 -68.704  1.00102.35           C  
ANISOU 5742  CB  ALA A 786    15956  14042   8891   2653   4622    131       C  
ATOM   5743  N   ARG A 787     -37.057 -45.068 -68.765  1.00104.23           N  
ANISOU 5743  N   ARG A 787    16925  13801   8876   2007   4416    662       N  
ATOM   5744  CA  ARG A 787     -37.510 -43.780 -68.249  1.00103.72           C  
ANISOU 5744  CA  ARG A 787    16921  13585   8903   1626   4351    906       C  
ATOM   5745  C   ARG A 787     -38.953 -43.858 -67.771  1.00 99.67           C  
ANISOU 5745  C   ARG A 787    16661  12742   8467   1655   3817    892       C  
ATOM   5746  O   ARG A 787     -39.291 -43.341 -66.698  1.00102.44           O  
ANISOU 5746  O   ARG A 787    16821  12986   9115   1416   3607    983       O  
ATOM   5747  CB  ARG A 787     -37.357 -42.707 -69.328  1.00112.69           C  
ANISOU 5747  CB  ARG A 787    18260  14729   9830   1407   4531   1059       C  
ATOM   5748  CG  ARG A 787     -38.089 -41.405 -69.040  1.00117.20           C  
ANISOU 5748  CG  ARG A 787    19013  15058  10459   1092   4335   1270       C  
ATOM   5749  CD  ARG A 787     -37.925 -40.421 -70.190  1.00126.13           C  
ANISOU 5749  CD  ARG A 787    20398  16177  11347    931   4505   1412       C  
ATOM   5750  NE  ARG A 787     -38.592 -40.872 -71.411  1.00131.62           N  
ANISOU 5750  NE  ARG A 787    21538  16769  11704   1227   4360   1314       N  
ATOM   5751  CZ  ARG A 787     -39.705 -40.332 -71.901  1.00133.08           C  
ANISOU 5751  CZ  ARG A 787    22152  16671  11741   1265   4045   1360       C  
ATOM   5752  NH1 ARG A 787     -40.279 -39.310 -71.281  1.00132.10           N  
ANISOU 5752  NH1 ARG A 787    22076  16344  11771   1031   3843   1496       N  
ATOM   5753  NH2 ARG A 787     -40.240 -40.809 -73.016  1.00134.63           N  
ANISOU 5753  NH2 ARG A 787    22723  16788  11641   1554   3919   1249       N  
ATOM   5754  N   ALA A 788     -39.818 -44.508 -68.554  1.00 95.54           N  
ANISOU 5754  N   ALA A 788    16548  12066   7685   1949   3591    756       N  
ATOM   5755  CA  ALA A 788     -41.219 -44.637 -68.169  1.00 91.22           C  
ANISOU 5755  CA  ALA A 788    16210  11224   7224   1979   3090    703       C  
ATOM   5756  C   ALA A 788     -41.366 -45.428 -66.876  1.00 84.26           C  
ANISOU 5756  C   ALA A 788    14945  10294   6775   1965   2801    602       C  
ATOM   5757  O   ALA A 788     -42.187 -45.083 -66.018  1.00 81.74           O  
ANISOU 5757  O   ALA A 788    14580   9810   6669   1792   2506    649       O  
ATOM   5758  CB  ALA A 788     -42.014 -45.297 -69.295  1.00 88.14           C  
ANISOU 5758  CB  ALA A 788    16269  10698   6522   2308   2889    529       C  
ATOM   5759  N   ASP A 789     -40.575 -46.492 -66.715  1.00 83.93           N  
ANISOU 5759  N   ASP A 789    14641  10393   6856   2155   2880    459       N  
ATOM   5760  CA  ASP A 789     -40.643 -47.275 -65.485  1.00 86.71           C  
ANISOU 5760  CA  ASP A 789    14676  10682   7589   2152   2609    385       C  
ATOM   5761  C   ASP A 789     -40.088 -46.493 -64.301  1.00 83.29           C  
ANISOU 5761  C   ASP A 789    13842  10351   7452   1837   2689    546       C  
ATOM   5762  O   ASP A 789     -40.585 -46.625 -63.176  1.00 80.28           O  
ANISOU 5762  O   ASP A 789    13314   9849   7338   1720   2407    563       O  
ATOM   5763  CB  ASP A 789     -39.891 -48.594 -65.658  1.00 93.78           C  
ANISOU 5763  CB  ASP A 789    15431  11679   8523   2472   2649    184       C  
ATOM   5764  CG  ASP A 789     -39.979 -49.479 -64.427  1.00 94.25           C  
ANISOU 5764  CG  ASP A 789    15242  11628   8941   2494   2344    119       C  
ATOM   5765  OD1 ASP A 789     -41.002 -50.178 -64.267  1.00 89.78           O  
ANISOU 5765  OD1 ASP A 789    14882  10805   8424   2569   1994     33       O  
ATOM   5766  OD2 ASP A 789     -39.026 -49.475 -63.618  1.00 97.42           O  
ANISOU 5766  OD2 ASP A 789    15250  12192   9571   2430   2451    153       O  
ATOM   5767  N   ALA A 790     -39.059 -45.674 -64.532  1.00 84.48           N  
ANISOU 5767  N   ALA A 790    13814  10727   7557   1686   3078    658       N  
ATOM   5768  CA  ALA A 790     -38.492 -44.874 -63.452  1.00 82.33           C  
ANISOU 5768  CA  ALA A 790    13156  10550   7573   1381   3146    790       C  
ATOM   5769  C   ALA A 790     -39.488 -43.831 -62.963  1.00 82.83           C  
ANISOU 5769  C   ALA A 790    13381  10413   7676   1110   2938    940       C  
ATOM   5770  O   ALA A 790     -39.768 -43.740 -61.762  1.00 85.09           O  
ANISOU 5770  O   ALA A 790    13457  10636   8237    972   2703    963       O  
ATOM   5771  CB  ALA A 790     -37.196 -44.208 -63.915  1.00 83.90           C  
ANISOU 5771  CB  ALA A 790    13132  11025   7720   1252   3626    860       C  
ATOM   5772  N   ASP A 791     -40.039 -43.038 -63.885  1.00 80.83           N  
ANISOU 5772  N   ASP A 791    13521  10058   7133   1054   3010   1034       N  
ATOM   5773  CA  ASP A 791     -40.995 -42.008 -63.490  1.00 77.39           C  
ANISOU 5773  CA  ASP A 791    13256   9423   6725    835   2794   1151       C  
ATOM   5774  C   ASP A 791     -42.264 -42.623 -62.910  1.00 67.39           C  
ANISOU 5774  C   ASP A 791    12075   7958   5574    934   2347   1030       C  
ATOM   5775  O   ASP A 791     -42.817 -42.112 -61.928  1.00 62.76           O  
ANISOU 5775  O   ASP A 791    11373   7283   5190    749   2134   1073       O  
ATOM   5776  CB  ASP A 791     -41.323 -41.110 -64.683  1.00 84.90           C  
ANISOU 5776  CB  ASP A 791    14667  10282   7310    807   2933   1264       C  
ATOM   5777  CG  ASP A 791     -40.105 -40.370 -65.205  1.00 93.45           C  
ANISOU 5777  CG  ASP A 791    15679  11548   8282    630   3415   1418       C  
ATOM   5778  OD1 ASP A 791     -39.088 -40.318 -64.483  1.00 95.52           O  
ANISOU 5778  OD1 ASP A 791    15480  11998   8815    472   3601   1437       O  
ATOM   5779  OD2 ASP A 791     -40.168 -39.839 -66.334  1.00 97.10           O  
ANISOU 5779  OD2 ASP A 791    16462  11966   8465    632   3533   1483       O  
ATOM   5780  N   ALA A 792     -42.740 -43.722 -63.504  1.00 65.59           N  
ANISOU 5780  N   ALA A 792    12042   7659   5221   1216   2207    867       N  
ATOM   5781  CA  ALA A 792     -43.912 -44.404 -62.962  1.00 65.23           C  
ANISOU 5781  CA  ALA A 792    12045   7425   5312   1281   1808    739       C  
ATOM   5782  C   ALA A 792     -43.656 -44.883 -61.539  1.00 61.61           C  
ANISOU 5782  C   ALA A 792    11199   7007   5202   1174   1698    738       C  
ATOM   5783  O   ALA A 792     -44.503 -44.709 -60.652  1.00 64.30           O  
ANISOU 5783  O   ALA A 792    11483   7237   5711   1032   1449    740       O  
ATOM   5784  CB  ALA A 792     -44.303 -45.575 -63.864  1.00 63.62           C  
ANISOU 5784  CB  ALA A 792    12095   7138   4941   1597   1695    550       C  
ATOM   5785  N   THR A 793     -42.481 -45.469 -61.301  1.00 61.44           N  
ANISOU 5785  N   THR A 793    10910   7155   5280   1251   1880    727       N  
ATOM   5786  CA  THR A 793     -42.124 -45.908 -59.957  1.00 66.35           C  
ANISOU 5786  CA  THR A 793    11191   7815   6202   1178   1767    734       C  
ATOM   5787  C   THR A 793     -42.097 -44.736 -58.984  1.00 60.18           C  
ANISOU 5787  C   THR A 793    10208   7079   5580    873   1765    874       C  
ATOM   5788  O   THR A 793     -42.700 -44.796 -57.908  1.00 56.70           O  
ANISOU 5788  O   THR A 793     9678   6556   5311    761   1532    882       O  
ATOM   5789  CB  THR A 793     -40.768 -46.617 -59.982  1.00 70.42           C  
ANISOU 5789  CB  THR A 793    11453   8523   6783   1349   1963    676       C  
ATOM   5790  OG1 THR A 793     -40.849 -47.781 -60.815  1.00 77.29           O  
ANISOU 5790  OG1 THR A 793    12523   9330   7516   1660   1923    518       O  
ATOM   5791  CG2 THR A 793     -40.354 -47.032 -58.578  1.00 62.22           C  
ANISOU 5791  CG2 THR A 793    10092   7515   6033   1299   1814    686       C  
ATOM   5792  N   ASP A 794     -41.411 -43.650 -59.354  1.00 61.84           N  
ANISOU 5792  N   ASP A 794    10358   7412   5726    726   2029    983       N  
ATOM   5793  CA  ASP A 794     -41.251 -42.526 -58.434  1.00 66.40           C  
ANISOU 5793  CA  ASP A 794    10729   8026   6474    440   2027   1099       C  
ATOM   5794  C   ASP A 794     -42.588 -41.867 -58.113  1.00 65.12           C  
ANISOU 5794  C   ASP A 794    10773   7673   6298    313   1767   1122       C  
ATOM   5795  O   ASP A 794     -42.837 -41.473 -56.966  1.00 67.92           O  
ANISOU 5795  O   ASP A 794    10951   8017   6841    153   1611   1146       O  
ATOM   5796  CB  ASP A 794     -40.275 -41.506 -59.017  1.00 75.06           C  
ANISOU 5796  CB  ASP A 794    11756   9257   7505    286   2375   1211       C  
ATOM   5797  CG  ASP A 794     -38.909 -42.102 -59.295  1.00 84.48           C  
ANISOU 5797  CG  ASP A 794    12671  10686   8741    400   2657   1156       C  
ATOM   5798  OD1 ASP A 794     -38.617 -43.193 -58.763  1.00 85.20           O  
ANISOU 5798  OD1 ASP A 794    12570  10832   8968    586   2536   1040       O  
ATOM   5799  OD2 ASP A 794     -38.127 -41.478 -60.044  1.00 89.69           O  
ANISOU 5799  OD2 ASP A 794    13308  11472   9297    304   3003   1224       O  
ATOM   5800  N   MET A 795     -43.464 -41.735 -59.111  1.00 60.44           N  
ANISOU 5800  N   MET A 795    10550   6938   5475    404   1707   1093       N  
ATOM   5801  CA  MET A 795     -44.778 -41.159 -58.850  1.00 58.97           C  
ANISOU 5801  CA  MET A 795    10537   6581   5286    324   1435   1068       C  
ATOM   5802  C   MET A 795     -45.616 -42.078 -57.971  1.00 60.32           C  
ANISOU 5802  C   MET A 795    10611   6688   5621    365   1158    948       C  
ATOM   5803  O   MET A 795     -46.300 -41.612 -57.049  1.00 64.32           O  
ANISOU 5803  O   MET A 795    11023   7153   6261    217    979    940       O  
ATOM   5804  CB  MET A 795     -45.494 -40.866 -60.168  1.00 57.71           C  
ANISOU 5804  CB  MET A 795    10804   6285   4837    452   1401   1038       C  
ATOM   5805  CG  MET A 795     -44.809 -39.798 -61.006  1.00 64.46           C  
ANISOU 5805  CG  MET A 795    11832   7165   5495    368   1674   1192       C  
ATOM   5806  SD  MET A 795     -45.561 -39.584 -62.629  1.00 69.81           S  
ANISOU 5806  SD  MET A 795    13081   7680   5762    574   1632   1164       S  
ATOM   5807  CE  MET A 795     -47.145 -38.879 -62.185  1.00 64.61           C  
ANISOU 5807  CE  MET A 795    12574   6805   5170    537   1198   1077       C  
ATOM   5808  N   LEU A 796     -45.570 -43.388 -58.233  1.00 55.47           N  
ANISOU 5808  N   LEU A 796    10025   6058   4995    557   1128    852       N  
ATOM   5809  CA  LEU A 796     -46.324 -44.322 -57.405  1.00 51.38           C  
ANISOU 5809  CA  LEU A 796     9437   5452   4632    562    890    760       C  
ATOM   5810  C   LEU A 796     -45.856 -44.268 -55.956  1.00 46.94           C  
ANISOU 5810  C   LEU A 796     8562   4985   4288    404    876    838       C  
ATOM   5811  O   LEU A 796     -46.674 -44.185 -55.033  1.00 43.36           O  
ANISOU 5811  O   LEU A 796     8048   4483   3945    271    701    819       O  
ATOM   5812  CB  LEU A 796     -46.207 -45.742 -57.961  1.00 53.64           C  
ANISOU 5812  CB  LEU A 796     9829   5677   4875    796    864    653       C  
ATOM   5813  CG  LEU A 796     -46.928 -46.828 -57.153  1.00 51.67           C  
ANISOU 5813  CG  LEU A 796     9546   5298   4788    782    636    575       C  
ATOM   5814  CD1 LEU A 796     -48.417 -46.530 -57.038  1.00 47.97           C  
ANISOU 5814  CD1 LEU A 796     9182   4702   4344    663    420    487       C  
ATOM   5815  CD2 LEU A 796     -46.701 -48.197 -57.776  1.00 53.93           C  
ANISOU 5815  CD2 LEU A 796     9966   5492   5034   1025    605    467       C  
ATOM   5816  N   VAL A 797     -44.538 -44.295 -55.735  1.00 51.34           N  
ANISOU 5816  N   VAL A 797     8910   5694   4902    423   1059    911       N  
ATOM   5817  CA  VAL A 797     -44.036 -44.319 -54.364  1.00 54.36           C  
ANISOU 5817  CA  VAL A 797     9009   6166   5477    314   1009    965       C  
ATOM   5818  C   VAL A 797     -44.298 -42.991 -53.669  1.00 53.59           C  
ANISOU 5818  C   VAL A 797     8810   6107   5445     76    977   1030       C  
ATOM   5819  O   VAL A 797     -44.581 -42.963 -52.466  1.00 53.46           O  
ANISOU 5819  O   VAL A 797     8662   6102   5546    -32    836   1039       O  
ATOM   5820  CB  VAL A 797     -42.541 -44.699 -54.320  1.00 61.26           C  
ANISOU 5820  CB  VAL A 797     9654   7203   6420    423   1178    984       C  
ATOM   5821  CG1 VAL A 797     -42.312 -46.065 -54.955  1.00 61.90           C  
ANISOU 5821  CG1 VAL A 797     9845   7233   6441    694   1177    890       C  
ATOM   5822  CG2 VAL A 797     -41.682 -43.644 -54.991  1.00 67.34           C  
ANISOU 5822  CG2 VAL A 797    10333   8112   7142    343   1444   1042       C  
ATOM   5823  N   GLY A 798     -44.227 -41.874 -54.397  1.00 55.62           N  
ANISOU 5823  N   GLY A 798     9154   6369   5610     -3   1098   1075       N  
ATOM   5824  CA  GLY A 798     -44.579 -40.599 -53.790  1.00 48.83           C  
ANISOU 5824  CA  GLY A 798     8242   5500   4811   -211   1029   1117       C  
ATOM   5825  C   GLY A 798     -46.032 -40.559 -53.356  1.00 47.75           C  
ANISOU 5825  C   GLY A 798     8223   5248   4674   -246    783   1031       C  
ATOM   5826  O   GLY A 798     -46.351 -40.162 -52.230  1.00 51.02           O  
ANISOU 5826  O   GLY A 798     8490   5694   5200   -375    662   1021       O  
ATOM   5827  N   ASN A 799     -46.932 -40.991 -54.244  1.00 50.43           N  
ANISOU 5827  N   ASN A 799     8811   5463   4885   -124    705    946       N  
ATOM   5828  CA  ASN A 799     -48.353 -41.040 -53.914  1.00 49.42           C  
ANISOU 5828  CA  ASN A 799     8756   5241   4779   -152    476    824       C  
ATOM   5829  C   ASN A 799     -48.612 -41.935 -52.705  1.00 50.80           C  
ANISOU 5829  C   ASN A 799     8754   5453   5094   -210    386    796       C  
ATOM   5830  O   ASN A 799     -49.353 -41.560 -51.788  1.00 51.39           O  
ANISOU 5830  O   ASN A 799     8732   5548   5245   -338    266    748       O  
ATOM   5831  CB  ASN A 799     -49.148 -41.526 -55.127  1.00 49.91           C  
ANISOU 5831  CB  ASN A 799     9094   5171   4699     13    397    712       C  
ATOM   5832  CG  ASN A 799     -50.639 -41.561 -54.871  1.00 57.60           C  
ANISOU 5832  CG  ASN A 799    10103   6061   5723    -16    157    546       C  
ATOM   5833  OD1 ASN A 799     -51.179 -42.564 -54.405  1.00 65.23           O  
ANISOU 5833  OD1 ASN A 799    10999   7002   6783    -30     72    466       O  
ATOM   5834  ND2 ASN A 799     -51.316 -40.461 -55.177  1.00 60.80           N  
ANISOU 5834  ND2 ASN A 799    10615   6414   6072    -28     44    486       N  
ATOM   5835  N   ALA A 800     -48.003 -43.125 -52.686  1.00 51.90           N  
ANISOU 5835  N   ALA A 800     8868   5598   5254   -110    443    825       N  
ATOM   5836  CA  ALA A 800     -48.245 -44.071 -51.598  1.00 50.90           C  
ANISOU 5836  CA  ALA A 800     8647   5463   5229   -159    353    823       C  
ATOM   5837  C   ALA A 800     -47.691 -43.555 -50.276  1.00 42.85           C  
ANISOU 5837  C   ALA A 800     7406   4577   4298   -289    360    910       C  
ATOM   5838  O   ALA A 800     -48.326 -43.714 -49.226  1.00 48.64           O  
ANISOU 5838  O   ALA A 800     8082   5320   5078   -406    265    897       O  
ATOM   5839  CB  ALA A 800     -47.636 -45.432 -51.940  1.00 49.69           C  
ANISOU 5839  CB  ALA A 800     8560   5249   5071     11    387    834       C  
ATOM   5840  N   GLU A 801     -46.504 -42.945 -50.304  1.00 55.10           N  
ANISOU 5840  N   GLU A 801     8827   6239   5871   -277    478    987       N  
ATOM   5841  CA  GLU A 801     -45.960 -42.327 -49.099  1.00 57.41           C  
ANISOU 5841  CA  GLU A 801     8903   6658   6254   -394    454   1041       C  
ATOM   5842  C   GLU A 801     -46.896 -41.247 -48.570  1.00 55.07           C  
ANISOU 5842  C   GLU A 801     8595   6367   5963   -554    357    991       C  
ATOM   5843  O   GLU A 801     -47.186 -41.193 -47.368  1.00 52.57           O  
ANISOU 5843  O   GLU A 801     8179   6112   5683   -645    265    982       O  
ATOM   5844  CB  GLU A 801     -44.573 -41.749 -49.385  1.00 60.03           C  
ANISOU 5844  CB  GLU A 801     9074   7100   6634   -377    601   1100       C  
ATOM   5845  CG  GLU A 801     -43.481 -42.795 -49.516  1.00 65.30           C  
ANISOU 5845  CG  GLU A 801     9655   7821   7335   -205    674   1120       C  
ATOM   5846  CD  GLU A 801     -42.173 -42.214 -50.016  1.00 72.27           C  
ANISOU 5846  CD  GLU A 801    10351   8835   8275   -198    862   1144       C  
ATOM   5847  OE1 GLU A 801     -42.207 -41.161 -50.686  1.00 75.18           O  
ANISOU 5847  OE1 GLU A 801    10760   9198   8606   -311    979   1168       O  
ATOM   5848  OE2 GLU A 801     -41.110 -42.808 -49.736  1.00 75.89           O  
ANISOU 5848  OE2 GLU A 801    10622   9396   8817    -80    892   1134       O  
ATOM   5849  N   ASN A 802     -47.389 -40.381 -49.462  1.00 50.91           N  
ANISOU 5849  N   ASN A 802     8189   5775   5381   -571    368    947       N  
ATOM   5850  CA  ASN A 802     -48.330 -39.349 -49.037  1.00 52.71           C  
ANISOU 5850  CA  ASN A 802     8418   5993   5618   -681    245    866       C  
ATOM   5851  C   ASN A 802     -49.585 -39.961 -48.421  1.00 53.32           C  
ANISOU 5851  C   ASN A 802     8502   6058   5697   -713    123    758       C  
ATOM   5852  O   ASN A 802     -50.086 -39.475 -47.396  1.00 57.59           O  
ANISOU 5852  O   ASN A 802     8932   6676   6273   -817     42    701       O  
ATOM   5853  CB  ASN A 802     -48.685 -38.452 -50.220  1.00 60.33           C  
ANISOU 5853  CB  ASN A 802     9572   6847   6501   -649    245    835       C  
ATOM   5854  CG  ASN A 802     -49.779 -37.464 -49.889  1.00 63.07           C  
ANISOU 5854  CG  ASN A 802     9946   7159   6858   -710     76    712       C  
ATOM   5855  OD1 ASN A 802     -50.808 -37.416 -50.559  1.00 66.10           O  
ANISOU 5855  OD1 ASN A 802    10488   7447   7180   -637    -31    596       O  
ATOM   5856  ND2 ASN A 802     -49.567 -36.674 -48.845  1.00 63.78           N  
ANISOU 5856  ND2 ASN A 802     9875   7329   7029   -824     29    710       N  
ATOM   5857  N   LEU A 803     -50.101 -41.037 -49.023  1.00 48.76           N  
ANISOU 5857  N   LEU A 803     8049   5390   5087   -634    116    717       N  
ATOM   5858  CA  LEU A 803     -51.276 -41.701 -48.464  1.00 54.81           C  
ANISOU 5858  CA  LEU A 803     8806   6140   5880   -705     29    615       C  
ATOM   5859  C   LEU A 803     -50.999 -42.243 -47.067  1.00 55.40           C  
ANISOU 5859  C   LEU A 803     8758   6306   5986   -805     49    696       C  
ATOM   5860  O   LEU A 803     -51.834 -42.108 -46.166  1.00 60.14           O  
ANISOU 5860  O   LEU A 803     9279   6974   6597   -931      5    626       O  
ATOM   5861  CB  LEU A 803     -51.740 -42.832 -49.381  1.00 54.16           C  
ANISOU 5861  CB  LEU A 803     8881   5917   5779   -613     12    559       C  
ATOM   5862  CG  LEU A 803     -52.942 -43.622 -48.854  1.00 52.22           C  
ANISOU 5862  CG  LEU A 803     8613   5635   5592   -728    -57    451       C  
ATOM   5863  CD1 LEU A 803     -54.139 -42.704 -48.640  1.00 50.55           C  
ANISOU 5863  CD1 LEU A 803     8308   5488   5412   -815   -153    273       C  
ATOM   5864  CD2 LEU A 803     -53.300 -44.766 -49.790  1.00 50.63           C  
ANISOU 5864  CD2 LEU A 803     8572   5268   5398   -640    -93    387       C  
ATOM   5865  N   MET A 804     -49.832 -42.860 -46.865  1.00 51.36           N  
ANISOU 5865  N   MET A 804     8234   5804   5475   -735    111    833       N  
ATOM   5866  CA  MET A 804     -49.530 -43.424 -45.552  1.00 54.06           C  
ANISOU 5866  CA  MET A 804     8513   6211   5816   -796     98    918       C  
ATOM   5867  C   MET A 804     -49.359 -42.334 -44.498  1.00 55.80           C  
ANISOU 5867  C   MET A 804     8577   6589   6037   -889     64    914       C  
ATOM   5868  O   MET A 804     -49.867 -42.466 -43.376  1.00 58.69           O  
ANISOU 5868  O   MET A 804     8914   7024   6362   -994     34    909       O  
ATOM   5869  CB  MET A 804     -48.289 -44.311 -45.636  1.00 54.13           C  
ANISOU 5869  CB  MET A 804     8548   6186   5832   -650    129   1036       C  
ATOM   5870  CG  MET A 804     -48.564 -45.657 -46.294  1.00 55.77           C  
ANISOU 5870  CG  MET A 804     8937   6221   6033   -564    126   1035       C  
ATOM   5871  SD  MET A 804     -50.228 -46.257 -45.911  1.00 56.35           S  
ANISOU 5871  SD  MET A 804     9115   6193   6101   -751     80    961       S  
ATOM   5872  CE  MET A 804     -49.884 -47.881 -45.260  1.00 59.30           C  
ANISOU 5872  CE  MET A 804     9655   6416   6460   -724     49   1094       C  
ATOM   5873  N   ARG A 805     -48.655 -41.248 -44.836  1.00 54.50           N  
ANISOU 5873  N   ARG A 805     8322   6476   5911   -863     75    912       N  
ATOM   5874  CA  ARG A 805     -48.568 -40.110 -43.923  1.00 53.22           C  
ANISOU 5874  CA  ARG A 805     8022   6435   5766   -951     15    874       C  
ATOM   5875  C   ARG A 805     -49.956 -39.613 -43.541  1.00 53.50           C  
ANISOU 5875  C   ARG A 805     8063   6498   5768  -1049    -48    733       C  
ATOM   5876  O   ARG A 805     -50.249 -39.377 -42.360  1.00 58.41           O  
ANISOU 5876  O   ARG A 805     8604   7237   6352  -1125    -92    695       O  
ATOM   5877  CB  ARG A 805     -47.757 -38.980 -44.559  1.00 55.50           C  
ANISOU 5877  CB  ARG A 805     8246   6721   6121   -941     41    882       C  
ATOM   5878  CG  ARG A 805     -46.266 -39.238 -44.634  1.00 63.77           C  
ANISOU 5878  CG  ARG A 805     9187   7812   7231   -876    110    985       C  
ATOM   5879  CD  ARG A 805     -45.516 -37.963 -44.989  1.00 68.95           C  
ANISOU 5879  CD  ARG A 805     9741   8483   7973   -940    147    987       C  
ATOM   5880  NE  ARG A 805     -45.953 -37.411 -46.268  1.00 73.42           N  
ANISOU 5880  NE  ARG A 805    10465   8927   8502   -947    217    976       N  
ATOM   5881  CZ  ARG A 805     -45.368 -37.670 -47.432  1.00 74.30           C  
ANISOU 5881  CZ  ARG A 805    10647   8990   8595   -883    368   1041       C  
ATOM   5882  NH1 ARG A 805     -44.314 -38.472 -47.482  1.00 75.45           N  
ANISOU 5882  NH1 ARG A 805    10678   9210   8781   -802    467   1099       N  
ATOM   5883  NH2 ARG A 805     -45.835 -37.124 -48.546  1.00 75.61           N  
ANISOU 5883  NH2 ARG A 805    11007   9037   8685   -881    413   1036       N  
ATOM   5884  N   THR A 806     -50.832 -39.471 -44.538  1.00 49.32           N  
ANISOU 5884  N   THR A 806     7624   5873   5244  -1029    -58    635       N  
ATOM   5885  CA  THR A 806     -52.184 -38.993 -44.271  1.00 50.83           C  
ANISOU 5885  CA  THR A 806     7782   6101   5428  -1095   -132    456       C  
ATOM   5886  C   THR A 806     -52.936 -39.937 -43.338  1.00 55.07           C  
ANISOU 5886  C   THR A 806     8284   6712   5930  -1199    -94    433       C  
ATOM   5887  O   THR A 806     -53.594 -39.487 -42.394  1.00 56.45           O  
ANISOU 5887  O   THR A 806     8352   7019   6076  -1286   -115    328       O  
ATOM   5888  CB  THR A 806     -52.939 -38.816 -45.588  1.00 48.45           C  
ANISOU 5888  CB  THR A 806     7596   5671   5140  -1020   -181    343       C  
ATOM   5889  OG1 THR A 806     -52.243 -37.871 -46.408  1.00 49.80           O  
ANISOU 5889  OG1 THR A 806     7847   5766   5311   -945   -196    390       O  
ATOM   5890  CG2 THR A 806     -54.349 -38.313 -45.332  1.00 46.89           C  
ANISOU 5890  CG2 THR A 806     7326   5526   4962  -1060   -284    114       C  
ATOM   5891  N   VAL A 807     -52.842 -41.249 -43.576  1.00 53.40           N  
ANISOU 5891  N   VAL A 807     8172   6409   5710  -1197    -30    530       N  
ATOM   5892  CA  VAL A 807     -53.559 -42.211 -42.740  1.00 53.34           C  
ANISOU 5892  CA  VAL A 807     8172   6429   5665  -1332     25    536       C  
ATOM   5893  C   VAL A 807     -53.046 -42.166 -41.305  1.00 54.46           C  
ANISOU 5893  C   VAL A 807     8271   6709   5712  -1392     49    640       C  
ATOM   5894  O   VAL A 807     -53.829 -42.227 -40.348  1.00 56.68           O  
ANISOU 5894  O   VAL A 807     8506   7104   5926  -1530     97    586       O  
ATOM   5895  CB  VAL A 807     -53.448 -43.627 -43.336  1.00 51.77           C  
ANISOU 5895  CB  VAL A 807     8132   6053   5487  -1308     63    631       C  
ATOM   5896  CG1 VAL A 807     -54.021 -44.660 -42.373  1.00 47.95           C  
ANISOU 5896  CG1 VAL A 807     7699   5562   4957  -1479    134    689       C  
ATOM   5897  CG2 VAL A 807     -54.164 -43.697 -44.677  1.00 49.40           C  
ANISOU 5897  CG2 VAL A 807     7879   5629   5261  -1252     18    486       C  
ATOM   5898  N   LYS A 808     -51.728 -42.061 -41.131  1.00 52.04           N  
ANISOU 5898  N   LYS A 808     7974   6407   5392  -1286     18    775       N  
ATOM   5899  CA  LYS A 808     -51.154 -41.980 -39.790  1.00 55.87           C  
ANISOU 5899  CA  LYS A 808     8431   7019   5779  -1305     -5    857       C  
ATOM   5900  C   LYS A 808     -51.655 -40.741 -39.049  1.00 59.56           C  
ANISOU 5900  C   LYS A 808     8759   7661   6212  -1369    -45    709       C  
ATOM   5901  O   LYS A 808     -52.155 -40.828 -37.911  1.00 62.21           O  
ANISOU 5901  O   LYS A 808     9090   8124   6421  -1462    -14    690       O  
ATOM   5902  CB  LYS A 808     -49.629 -41.986 -39.905  1.00 55.34           C  
ANISOU 5902  CB  LYS A 808     8348   6930   5750  -1156    -61    975       C  
ATOM   5903  CG  LYS A 808     -48.869 -41.583 -38.665  1.00 58.20           C  
ANISOU 5903  CG  LYS A 808     8642   7431   6042  -1132   -145   1013       C  
ATOM   5904  CD  LYS A 808     -47.376 -41.686 -38.932  1.00 60.50           C  
ANISOU 5904  CD  LYS A 808     8873   7698   6417   -980   -204   1095       C  
ATOM   5905  CE  LYS A 808     -46.558 -41.146 -37.777  1.00 69.52           C  
ANISOU 5905  CE  LYS A 808     9912   8981   7522   -939   -330   1091       C  
ATOM   5906  NZ  LYS A 808     -45.098 -41.311 -38.018  1.00 74.95           N  
ANISOU 5906  NZ  LYS A 808    10493   9664   8321   -789   -395   1138       N  
ATOM   5907  N   ASP A 809     -51.550 -39.574 -39.692  1.00 60.32           N  
ANISOU 5907  N   ASP A 809     8762   7755   6404  -1317   -111    599       N  
ATOM   5908  CA  ASP A 809     -52.079 -38.359 -39.083  1.00 63.34           C  
ANISOU 5908  CA  ASP A 809     9027   8270   6770  -1353   -179    429       C  
ATOM   5909  C   ASP A 809     -53.579 -38.464 -38.830  1.00 60.38           C  
ANISOU 5909  C   ASP A 809     8615   7976   6352  -1450   -126    264       C  
ATOM   5910  O   ASP A 809     -54.101 -37.803 -37.926  1.00 68.19           O  
ANISOU 5910  O   ASP A 809     9507   9128   7272  -1489   -148    124       O  
ATOM   5911  CB  ASP A 809     -51.763 -37.149 -39.962  1.00 69.97           C  
ANISOU 5911  CB  ASP A 809     9827   9030   7727  -1285   -269    353       C  
ATOM   5912  CG  ASP A 809     -50.281 -36.825 -39.993  1.00 76.12           C  
ANISOU 5912  CG  ASP A 809    10577   9780   8566  -1234   -303    479       C  
ATOM   5913  OD1 ASP A 809     -49.616 -36.978 -38.947  1.00 78.83           O  
ANISOU 5913  OD1 ASP A 809    10867  10227   8857  -1233   -337    535       O  
ATOM   5914  OD2 ASP A 809     -49.780 -36.421 -41.064  1.00 78.09           O  
ANISOU 5914  OD2 ASP A 809    10853   9909   8909  -1196   -295    515       O  
ATOM   5915  N   VAL A 810     -54.284 -39.293 -39.604  1.00 54.23           N  
ANISOU 5915  N   VAL A 810     7893   7095   5618  -1489    -58    253       N  
ATOM   5916  CA  VAL A 810     -55.703 -39.520 -39.349  1.00 55.26           C  
ANISOU 5916  CA  VAL A 810     7945   7314   5739  -1609     10     82       C  
ATOM   5917  C   VAL A 810     -55.894 -40.377 -38.102  1.00 58.22           C  
ANISOU 5917  C   VAL A 810     8351   7802   5968  -1760    149    180       C  
ATOM   5918  O   VAL A 810     -56.872 -40.199 -37.365  1.00 60.19           O  
ANISOU 5918  O   VAL A 810     8487   8225   6155  -1876    230     30       O  
ATOM   5919  CB  VAL A 810     -56.376 -40.145 -40.587  1.00 52.84           C  
ANISOU 5919  CB  VAL A 810     7681   6849   5545  -1609     14     19       C  
ATOM   5920  CG1 VAL A 810     -57.710 -40.784 -40.224  1.00 49.62           C  
ANISOU 5920  CG1 VAL A 810     7182   6523   5150  -1784    120   -119       C  
ATOM   5921  CG2 VAL A 810     -56.590 -39.089 -41.658  1.00 56.71           C  
ANISOU 5921  CG2 VAL A 810     8145   7270   6131  -1467   -133   -142       C  
ATOM   5922  N   ILE A 811     -54.977 -41.313 -37.839  1.00 57.24           N  
ANISOU 5922  N   ILE A 811     8389   7584   5773  -1754    183    425       N  
ATOM   5923  CA  ILE A 811     -55.017 -42.047 -36.575  1.00 58.92           C  
ANISOU 5923  CA  ILE A 811     8701   7883   5804  -1875    291    553       C  
ATOM   5924  C   ILE A 811     -54.925 -41.073 -35.410  1.00 56.06           C  
ANISOU 5924  C   ILE A 811     8249   7752   5301  -1858    260    471       C  
ATOM   5925  O   ILE A 811     -55.796 -41.034 -34.530  1.00 56.51           O  
ANISOU 5925  O   ILE A 811     8258   7986   5229  -1992    380    380       O  
ATOM   5926  CB  ILE A 811     -53.886 -43.087 -36.505  1.00 58.44           C  
ANISOU 5926  CB  ILE A 811     8855   7661   5690  -1804    264    821       C  
ATOM   5927  CG1 ILE A 811     -53.942 -44.056 -37.680  1.00 57.72           C  
ANISOU 5927  CG1 ILE A 811     8864   7332   5734  -1794    279    880       C  
ATOM   5928  CG2 ILE A 811     -53.950 -43.853 -35.189  1.00 59.16           C  
ANISOU 5928  CG2 ILE A 811     9114   7809   5557  -1920    357    973       C  
ATOM   5929  CD1 ILE A 811     -52.744 -44.969 -37.718  1.00 56.81           C  
ANISOU 5929  CD1 ILE A 811     8940   7056   5589  -1665    218   1102       C  
ATOM   5930  N   ARG A 812     -53.865 -40.257 -35.398  1.00 52.72           N  
ANISOU 5930  N   ARG A 812     7792   7334   4904  -1698    104    486       N  
ATOM   5931  CA  ARG A 812     -53.674 -39.352 -34.267  1.00 56.03           C  
ANISOU 5931  CA  ARG A 812     8144   7952   5194  -1663     37    399       C  
ATOM   5932  C   ARG A 812     -54.819 -38.348 -34.150  1.00 59.32           C  
ANISOU 5932  C   ARG A 812     8381   8528   5630  -1703     51    115       C  
ATOM   5933  O   ARG A 812     -55.322 -38.092 -33.047  1.00 61.28           O  
ANISOU 5933  O   ARG A 812     8592   8987   5704  -1755    111     17       O  
ATOM   5934  CB  ARG A 812     -52.331 -38.635 -34.389  1.00 56.49           C  
ANISOU 5934  CB  ARG A 812     8169   7963   5332  -1504   -148    440       C  
ATOM   5935  CG  ARG A 812     -51.140 -39.577 -34.349  1.00 57.37           C  
ANISOU 5935  CG  ARG A 812     8415   7961   5421  -1428   -184    676       C  
ATOM   5936  CD  ARG A 812     -49.826 -38.821 -34.415  1.00 58.51           C  
ANISOU 5936  CD  ARG A 812     8463   8095   5672  -1293   -355    677       C  
ATOM   5937  NE  ARG A 812     -48.687 -39.730 -34.482  1.00 61.52           N  
ANISOU 5937  NE  ARG A 812     8930   8381   6065  -1190   -401    862       N  
ATOM   5938  CZ  ARG A 812     -47.420 -39.337 -34.547  1.00 66.78           C  
ANISOU 5938  CZ  ARG A 812     9490   9042   6843  -1074   -535    874       C  
ATOM   5939  NH1 ARG A 812     -47.124 -38.044 -34.552  1.00 67.44           N  
ANISOU 5939  NH1 ARG A 812     9401   9185   7039  -1076   -629    733       N  
ATOM   5940  NH2 ARG A 812     -46.448 -40.237 -34.603  1.00 71.02           N  
ANISOU 5940  NH2 ARG A 812    10085   9507   7394   -956   -582   1012       N  
ATOM   5941  N   ALA A 813     -55.255 -37.778 -35.277  1.00 57.30           N  
ANISOU 5941  N   ALA A 813     8025   8179   5567  -1660    -10    -31       N  
ATOM   5942  CA  ALA A 813     -56.335 -36.798 -35.239  1.00 59.10           C  
ANISOU 5942  CA  ALA A 813     8082   8538   5833  -1652    -42   -330       C  
ATOM   5943  C   ALA A 813     -57.654 -37.425 -34.807  1.00 61.66           C  
ANISOU 5943  C   ALA A 813     8324   9019   6087  -1813    152   -447       C  
ATOM   5944  O   ALA A 813     -58.493 -36.747 -34.204  1.00 64.61           O  
ANISOU 5944  O   ALA A 813     8538   9601   6407  -1821    173   -695       O  
ATOM   5945  CB  ALA A 813     -56.489 -36.127 -36.604  1.00 58.75           C  
ANISOU 5945  CB  ALA A 813     8003   8324   5995  -1549   -178   -442       C  
ATOM   5946  N   SER A 814     -57.858 -38.709 -35.109  1.00 62.25           N  
ANISOU 5946  N   SER A 814     8492   8991   6167  -1948    298   -289       N  
ATOM   5947  CA  SER A 814     -59.068 -39.390 -34.661  1.00 64.77           C  
ANISOU 5947  CA  SER A 814     8730   9448   6433  -2155    514   -380       C  
ATOM   5948  C   SER A 814     -59.026 -39.643 -33.161  1.00 68.07           C  
ANISOU 5948  C   SER A 814     9216  10070   6576  -2266    673   -291       C  
ATOM   5949  O   SER A 814     -60.031 -39.454 -32.461  1.00 66.60           O  
ANISOU 5949  O   SER A 814     8879  10127   6300  -2384    830   -482       O  
ATOM   5950  CB  SER A 814     -59.245 -40.702 -35.424  1.00 66.26           C  
ANISOU 5950  CB  SER A 814     9029   9426   6720  -2283    606   -229       C  
ATOM   5951  OG  SER A 814     -59.293 -40.480 -36.822  1.00 65.69           O  
ANISOU 5951  OG  SER A 814     8919   9174   6865  -2160    454   -320       O  
ATOM   5952  N   GLU A 815     -57.868 -40.073 -32.650  1.00 71.69           N  
ANISOU 5952  N   GLU A 815     9905  10445   6888  -2216    631    -16       N  
ATOM   5953  CA  GLU A 815     -57.711 -40.207 -31.206  1.00 75.32           C  
ANISOU 5953  CA  GLU A 815    10481  11091   7046  -2272    733     72       C  
ATOM   5954  C   GLU A 815     -57.952 -38.874 -30.508  1.00 73.96           C  
ANISOU 5954  C   GLU A 815    10134  11178   6790  -2164    661   -194       C  
ATOM   5955  O   GLU A 815     -58.536 -38.830 -29.419  1.00 75.63           O  
ANISOU 5955  O   GLU A 815    10331  11637   6767  -2256    824   -273       O  
ATOM   5956  CB  GLU A 815     -56.320 -40.751 -30.877  1.00 79.46           C  
ANISOU 5956  CB  GLU A 815    11272  11466   7455  -2165    616    373       C  
ATOM   5957  CG  GLU A 815     -56.125 -41.161 -29.421  1.00 86.98           C  
ANISOU 5957  CG  GLU A 815    12435  12559   8053  -2217    709    518       C  
ATOM   5958  CD  GLU A 815     -55.682 -40.012 -28.534  1.00 91.19           C  
ANISOU 5958  CD  GLU A 815    12906  13304   8440  -2051    560    373       C  
ATOM   5959  OE1 GLU A 815     -55.291 -38.956 -29.075  1.00 90.01           O  
ANISOU 5959  OE1 GLU A 815    12574  13136   8488  -1892    356    207       O  
ATOM   5960  OE2 GLU A 815     -55.725 -40.167 -27.294  1.00 95.15           O  
ANISOU 5960  OE2 GLU A 815    13560  13976   8618  -2083    644    427       O  
ATOM   5961  N   ALA A 816     -57.517 -37.773 -31.128  1.00 70.13           N  
ANISOU 5961  N   ALA A 816     9530  10630   6485  -1971    422   -339       N  
ATOM   5962  CA  ALA A 816     -57.764 -36.457 -30.547  1.00 67.53           C  
ANISOU 5962  CA  ALA A 816     9047  10504   6108  -1852    314   -618       C  
ATOM   5963  C   ALA A 816     -59.238 -36.082 -30.629  1.00 72.03           C  
ANISOU 5963  C   ALA A 816     9376  11261   6734  -1918    434   -940       C  
ATOM   5964  O   ALA A 816     -59.767 -35.419 -29.728  1.00 77.66           O  
ANISOU 5964  O   ALA A 816     9974  12236   7298  -1887    474  -1168       O  
ATOM   5965  CB  ALA A 816     -56.903 -35.404 -31.243  1.00 65.16           C  
ANISOU 5965  CB  ALA A 816     8714  10038   6005  -1657     25   -670       C  
ATOM   5966  N   ALA A 817     -59.921 -36.497 -31.697  1.00 70.76           N  
ANISOU 5966  N   ALA A 817     9121  10979   6785  -1991    482   -989       N  
ATOM   5967  CA  ALA A 817     -61.335 -36.178 -31.842  1.00 73.39           C  
ANISOU 5967  CA  ALA A 817     9185  11492   7209  -2040    572  -1329       C  
ATOM   5968  C   ALA A 817     -62.211 -36.993 -30.901  1.00 80.27           C  
ANISOU 5968  C   ALA A 817     9993  12613   7893  -2289    912  -1344       C  
ATOM   5969  O   ALA A 817     -63.326 -36.562 -30.585  1.00 85.34           O  
ANISOU 5969  O   ALA A 817    10371  13514   8541  -2321   1020  -1670       O  
ATOM   5970  CB  ALA A 817     -61.779 -36.397 -33.288  1.00 68.02           C  
ANISOU 5970  CB  ALA A 817     8431  10599   6812  -2029    487  -1393       C  
ATOM   5971  N   CYS A 818     -61.738 -38.154 -30.445  1.00 81.69           N  
ANISOU 5971  N   CYS A 818    10414  12719   7906  -2465   1088  -1005       N  
ATOM   5972  CA  CYS A 818     -62.505 -38.995 -29.534  1.00 85.03           C  
ANISOU 5972  CA  CYS A 818    10841  13343   8123  -2742   1441   -962       C  
ATOM   5973  C   CYS A 818     -62.420 -38.538 -28.079  1.00 87.45           C  
ANISOU 5973  C   CYS A 818    11202  13947   8078  -2717   1546  -1001       C  
ATOM   5974  O   CYS A 818     -62.776 -39.313 -27.182  1.00 91.13           O  
ANISOU 5974  O   CYS A 818    11783  14555   8287  -2947   1850   -870       O  
ATOM   5975  CB  CYS A 818     -62.046 -40.452 -29.647  1.00 88.13           C  
ANISOU 5975  CB  CYS A 818    11530  13489   8465  -2937   1567   -568       C  
ATOM   5976  SG  CYS A 818     -62.473 -41.259 -31.212  1.00 87.54           S  
ANISOU 5976  SG  CYS A 818    11386  13113   8764  -3040   1533   -558       S  
ATOM   5977  N   ILE A 819     -61.970 -37.314 -27.819  1.00 84.17           N  
ANISOU 5977  N   ILE A 819    10729  13619   7633  -2452   1305  -1179       N  
ATOM   5978  CA  ILE A 819     -61.839 -36.830 -26.447  1.00 84.76           C  
ANISOU 5978  CA  ILE A 819    10871  13973   7363  -2390   1364  -1243       C  
ATOM   5979  C   ILE A 819     -63.130 -36.188 -25.953  1.00 90.10           C  
ANISOU 5979  C   ILE A 819    11227  15020   7986  -2417   1544  -1654       C  
ATOM   5980  O   ILE A 819     -63.538 -36.404 -24.809  1.00 93.69           O  
ANISOU 5980  O   ILE A 819    11720  15765   8114  -2536   1816  -1674       O  
ATOM   5981  CB  ILE A 819     -60.649 -35.856 -26.347  1.00 79.09           C  
ANISOU 5981  CB  ILE A 819    10256  13151   6643  -2096    997  -1241       C  
ATOM   5982  CG1 ILE A 819     -59.348 -36.571 -26.717  1.00 77.77           C  
ANISOU 5982  CG1 ILE A 819    10374  12667   6508  -2074    854   -850       C  
ATOM   5983  CG2 ILE A 819     -60.552 -35.270 -24.947  1.00 79.17           C  
ANISOU 5983  CG2 ILE A 819    10326  13453   6301  -1998   1015  -1363       C  
ATOM   5984  CD1 ILE A 819     -58.164 -35.642 -26.880  1.00 76.87           C  
ANISOU 5984  CD1 ILE A 819    10298  12414   6493  -1822    493   -860       C  
ATOM   5985  N   ARG A 820     -63.793 -35.396 -26.794  1.00 90.05           N  
ANISOU 5985  N   ARG A 820    10912  15018   8284  -2295   1396  -1995       N  
ATOM   5986  CA  ARG A 820     -65.045 -34.725 -26.443  1.00 93.33           C  
ANISOU 5986  CA  ARG A 820    10973  15785   8704  -2273   1523  -2447       C  
ATOM   5987  C   ARG A 820     -66.125 -35.186 -27.416  1.00 95.72           C  
ANISOU 5987  C   ARG A 820    10992  16061   9315  -2427   1636  -2610       C  
ATOM   5988  O   ARG A 820     -66.506 -34.460 -28.338  1.00 89.54           O  
ANISOU 5988  O   ARG A 820    10000  15194   8826  -2240   1385  -2888       O  
ATOM   5989  CB  ARG A 820     -64.882 -33.200 -26.461  1.00 89.70           C  
ANISOU 5989  CB  ARG A 820    10398  15364   8322  -1922   1173  -2780       C  
ATOM   5990  CG  ARG A 820     -64.055 -32.646 -25.313  1.00 85.96           C  
ANISOU 5990  CG  ARG A 820    10130  15000   7530  -1774   1081  -2733       C  
ATOM   5991  CD  ARG A 820     -64.108 -31.127 -25.288  1.00 81.05           C  
ANISOU 5991  CD  ARG A 820     9362  14431   7003  -1451    755  -3126       C  
ATOM   5992  NE  ARG A 820     -63.365 -30.570 -24.161  1.00 77.81           N  
ANISOU 5992  NE  ARG A 820     9133  14135   6297  -1304    646  -3127       N  
ATOM   5993  CZ  ARG A 820     -63.878 -30.379 -22.950  1.00 78.70           C  
ANISOU 5993  CZ  ARG A 820     9190  14634   6079  -1286    844  -3336       C  
ATOM   5994  NH1 ARG A 820     -65.140 -30.702 -22.702  1.00 78.31           N  
ANISOU 5994  NH1 ARG A 820     8882  14909   5965  -1428   1193  -3559       N  
ATOM   5995  NH2 ARG A 820     -63.127 -29.865 -21.985  1.00 81.08           N  
ANISOU 5995  NH2 ARG A 820     9684  15008   6112  -1126    696  -3338       N  
ATOM   5996  N   LEU A 821     -66.622 -36.399 -27.202  1.00106.95           N  
ANISOU 5996  N   LEU A 821    12427  17541  10667  -2769   2000  -2438       N  
ATOM   5997  CA  LEU A 821     -67.696 -36.960 -28.006  1.00114.69           C  
ANISOU 5997  CA  LEU A 821    13122  18520  11936  -2966   2139  -2603       C  
ATOM   5998  C   LEU A 821     -69.038 -36.744 -27.320  1.00125.70           C  
ANISOU 5998  C   LEU A 821    14117  20366  13277  -3095   2452  -3005       C  
ATOM   5999  O   LEU A 821     -69.118 -36.606 -26.096  1.00129.57           O  
ANISOU 5999  O   LEU A 821    14640  21163  13427  -3149   2693  -3027       O  
ATOM   6000  CB  LEU A 821     -67.479 -38.454 -28.249  1.00114.45           C  
ANISOU 6000  CB  LEU A 821    13327  18249  11908  -3295   2348  -2194       C  
ATOM   6001  CG  LEU A 821     -66.309 -38.856 -29.146  1.00110.66           C  
ANISOU 6001  CG  LEU A 821    13178  17320  11547  -3187   2065  -1838       C  
ATOM   6002  CD1 LEU A 821     -66.222 -40.371 -29.254  1.00112.04           C  
ANISOU 6002  CD1 LEU A 821    13581  17283  11705  -3513   2290  -1477       C  
ATOM   6003  CD2 LEU A 821     -66.450 -38.223 -30.521  1.00107.17           C  
ANISOU 6003  CD2 LEU A 821    12557  16692  11471  -2957   1726  -2066       C  
ATOM   6004  N   ARG A 822     -70.093 -36.715 -28.125  1.00136.04           N  
ANISOU 6004  N   ARG A 822    15040  21728  14921  -3133   2443  -3343       N  
ATOM   6005  CA  ARG A 822     -71.437 -36.642 -27.580  1.00146.49           C  
ANISOU 6005  CA  ARG A 822    15916  23492  16252  -3291   2768  -3751       C  
ATOM   6006  C   ARG A 822     -71.743 -37.913 -26.790  1.00149.19           C  
ANISOU 6006  C   ARG A 822    16344  23963  16377  -3773   3296  -3481       C  
ATOM   6007  O   ARG A 822     -71.348 -39.009 -27.198  1.00153.18           O  
ANISOU 6007  O   ARG A 822    17113  24153  16934  -4015   3360  -3093       O  
ATOM   6008  CB  ARG A 822     -72.456 -36.457 -28.703  1.00152.63           C  
ANISOU 6008  CB  ARG A 822    16262  24260  17470  -3231   2609  -4164       C  
ATOM   6009  CG  ARG A 822     -72.262 -35.171 -29.491  1.00157.25           C  
ANISOU 6009  CG  ARG A 822    16789  24707  18251  -2752   2086  -4445       C  
ATOM   6010  CD  ARG A 822     -72.513 -35.375 -30.976  1.00160.25           C  
ANISOU 6010  CD  ARG A 822    17091  24777  19022  -2682   1796  -4520       C  
ATOM   6011  NE  ARG A 822     -73.900 -35.728 -31.264  1.00168.62           N  
ANISOU 6011  NE  ARG A 822    17655  26067  20344  -2851   1960  -4923       N  
ATOM   6012  CZ  ARG A 822     -74.370 -35.963 -32.485  1.00171.21           C  
ANISOU 6012  CZ  ARG A 822    17836  26195  21021  -2809   1733  -5079       C  
ATOM   6013  NH1 ARG A 822     -73.563 -35.885 -33.535  1.00167.85           N  
ANISOU 6013  NH1 ARG A 822    17748  25338  20691  -2605   1359  -4847       N  
ATOM   6014  NH2 ARG A 822     -75.647 -36.278 -32.658  1.00175.84           N  
ANISOU 6014  NH2 ARG A 822    17931  27023  21857  -2972   1882  -5482       N  
ATOM   6015  N   PRO A 823     -72.437 -37.800 -25.654  1.00147.12           N  
ANISOU 6015  N   PRO A 823    15952  24027  15922  -3860   3568  -3620       N  
ATOM   6016  CA  PRO A 823     -72.648 -38.979 -24.799  1.00153.34           C  
ANISOU 6016  CA  PRO A 823    16986  24746  16532  -4219   3920  -3249       C  
ATOM   6017  C   PRO A 823     -73.574 -40.026 -25.396  1.00162.30           C  
ANISOU 6017  C   PRO A 823    17936  25751  17979  -4562   4099  -3258       C  
ATOM   6018  O   PRO A 823     -73.626 -41.146 -24.868  1.00164.00           O  
ANISOU 6018  O   PRO A 823    18421  25814  18078  -4864   4358  -2897       O  
ATOM   6019  CB  PRO A 823     -73.247 -38.378 -23.522  1.00150.52           C  
ANISOU 6019  CB  PRO A 823    16488  24771  15931  -4148   4105  -3466       C  
ATOM   6020  CG  PRO A 823     -73.930 -37.134 -23.990  1.00146.88           C  
ANISOU 6020  CG  PRO A 823    15525  24581  15703  -3853   3891  -4072       C  
ATOM   6021  CD  PRO A 823     -73.075 -36.592 -25.102  1.00143.64           C  
ANISOU 6021  CD  PRO A 823    15174  23960  15443  -3588   3506  -4103       C  
ATOM   6022  N   ASP A 824     -74.293 -39.712 -26.473  1.00168.68           N  
ANISOU 6022  N   ASP A 824    18314  26593  19182  -4501   3943  -3663       N  
ATOM   6023  CA  ASP A 824     -75.282 -40.619 -27.042  1.00175.36           C  
ANISOU 6023  CA  ASP A 824    18940  27338  20351  -4794   4076  -3749       C  
ATOM   6024  C   ASP A 824     -74.835 -41.307 -28.322  1.00168.99           C  
ANISOU 6024  C   ASP A 824    18264  26129  19816  -4860   3877  -3562       C  
ATOM   6025  O   ASP A 824     -75.316 -42.404 -28.612  1.00172.07           O  
ANISOU 6025  O   ASP A 824    18681  26318  20377  -5154   4015  -3432       O  
ATOM   6026  CB  ASP A 824     -76.590 -39.869 -27.322  1.00182.96           C  
ANISOU 6026  CB  ASP A 824    19300  28622  21594  -4671   4023  -4385       C  
ATOM   6027  CG  ASP A 824     -76.420 -38.767 -28.353  1.00183.59           C  
ANISOU 6027  CG  ASP A 824    19131  28717  21906  -4268   3596  -4762       C  
ATOM   6028  OD1 ASP A 824     -75.313 -38.191 -28.433  1.00180.84           O  
ANISOU 6028  OD1 ASP A 824    19027  28290  21394  -4033   3399  -4603       O  
ATOM   6029  OD2 ASP A 824     -77.390 -38.480 -29.086  1.00186.02           O  
ANISOU 6029  OD2 ASP A 824    19016  29103  22560  -4168   3442  -5218       O  
ATOM   6030  N   SER A 825     -73.938 -40.693 -29.092  1.00158.07           N  
ANISOU 6030  N   SER A 825    16962  24620  18479  -4593   3558  -3552       N  
ATOM   6031  CA  SER A 825     -73.546 -41.257 -30.374  1.00148.65           C  
ANISOU 6031  CA  SER A 825    15861  23055  17563  -4630   3341  -3414       C  
ATOM   6032  C   SER A 825     -72.875 -42.615 -30.177  1.00139.80           C  
ANISOU 6032  C   SER A 825    15251  21567  16299  -4912   3492  -2837       C  
ATOM   6033  O   SER A 825     -72.213 -42.846 -29.160  1.00141.24           O  
ANISOU 6033  O   SER A 825    15809  21740  16117  -4955   3644  -2482       O  
ATOM   6034  CB  SER A 825     -72.604 -40.305 -31.110  1.00145.75           C  
ANISOU 6034  CB  SER A 825    15688  22461  17230  -4141   2833  -3397       C  
ATOM   6035  OG  SER A 825     -73.290 -39.147 -31.554  1.00147.78           O  
ANISOU 6035  OG  SER A 825    15545  22911  17693  -3818   2571  -3921       O  
ATOM   6036  N   PRO A 826     -73.040 -43.538 -31.130  1.00127.98           N  
ANISOU 6036  N   PRO A 826    13794  19744  15089  -5068   3414  -2749       N  
ATOM   6037  CA  PRO A 826     -72.380 -44.847 -30.992  1.00125.24           C  
ANISOU 6037  CA  PRO A 826    13947  19012  14624  -5288   3511  -2218       C  
ATOM   6038  C   PRO A 826     -70.866 -44.745 -30.956  1.00117.10           C  
ANISOU 6038  C   PRO A 826    13379  17773  13340  -5120   3351  -1820       C  
ATOM   6039  O   PRO A 826     -70.201 -45.645 -30.419  1.00118.57           O  
ANISOU 6039  O   PRO A 826    14025  17714  13312  -5221   3436  -1372       O  
ATOM   6040  CB  PRO A 826     -72.869 -45.620 -32.225  1.00126.23           C  
ANISOU 6040  CB  PRO A 826    13958  18850  15154  -5402   3375  -2310       C  
ATOM   6041  CG  PRO A 826     -73.274 -44.564 -33.203  1.00124.49           C  
ANISOU 6041  CG  PRO A 826    13303  18779  15219  -5142   3082  -2797       C  
ATOM   6042  CD  PRO A 826     -73.812 -43.433 -32.378  1.00126.55           C  
ANISOU 6042  CD  PRO A 826    13230  19506  15346  -5003   3186  -3139       C  
ATOM   6043  N   ILE A 827     -70.309 -43.662 -31.501  1.00109.93           N  
ANISOU 6043  N   ILE A 827    12425  16871  12474  -4714   2997  -1965       N  
ATOM   6044  CA  ILE A 827     -68.869 -43.456 -31.630  1.00103.81           C  
ANISOU 6044  CA  ILE A 827    12082  15829  11530  -4413   2715  -1625       C  
ATOM   6045  C   ILE A 827     -68.288 -43.390 -30.225  1.00106.08           C  
ANISOU 6045  C   ILE A 827    12634  16286  11386  -4455   2921  -1373       C  
ATOM   6046  O   ILE A 827     -67.106 -43.672 -29.999  1.00105.35           O  
ANISOU 6046  O   ILE A 827    12963  15972  11092  -4346   2808   -996       O  
ATOM   6047  CB  ILE A 827     -68.546 -42.176 -32.432  1.00 98.56           C  
ANISOU 6047  CB  ILE A 827    11290  15147  11011  -3957   2294  -1873       C  
ATOM   6048  CG1 ILE A 827     -69.137 -42.239 -33.839  1.00 97.99           C  
ANISOU 6048  CG1 ILE A 827    11002  14904  11327  -3886   2067  -2125       C  
ATOM   6049  CG2 ILE A 827     -67.044 -41.978 -32.539  1.00 92.92           C  
ANISOU 6049  CG2 ILE A 827    10987  14177  10142  -3691   2042  -1527       C  
ATOM   6050  CD1 ILE A 827     -70.488 -41.580 -33.980  1.00100.31           C  
ANISOU 6050  CD1 ILE A 827    10775  15506  11832  -3873   2080  -2660       C  
ATOM   6051  N   ALA A 828     -69.139 -43.014 -29.270  1.00110.36           N  
ANISOU 6051  N   ALA A 828    12916  17239  11778  -4601   3221  -1607       N  
ATOM   6052  CA  ALA A 828     -68.714 -42.918 -27.881  1.00112.05           C  
ANISOU 6052  CA  ALA A 828    13380  17640  11555  -4619   3414  -1407       C  
ATOM   6053  C   ALA A 828     -68.221 -44.257 -27.350  1.00112.51           C  
ANISOU 6053  C   ALA A 828    13925  17365  11458  -4788   3513   -907       C  
ATOM   6054  O   ALA A 828     -67.381 -44.291 -26.443  1.00111.92           O  
ANISOU 6054  O   ALA A 828    14214  17258  11054  -4669   3489   -625       O  
ATOM   6055  CB  ALA A 828     -69.864 -42.385 -27.023  1.00118.18           C  
ANISOU 6055  CB  ALA A 828    13798  18830  12274  -4667   3647  -1763       C  
ATOM   6056  N   SER A 829     -68.703 -45.366 -27.913  1.00112.53           N  
ANISOU 6056  N   SER A 829    13948  17106  11703  -5032   3590   -809       N  
ATOM   6057  CA  SER A 829     -68.297 -46.697 -27.475  1.00114.16           C  
ANISOU 6057  CA  SER A 829    14608  16974  11794  -5177   3668   -362       C  
ATOM   6058  C   SER A 829     -66.966 -47.148 -28.073  1.00110.23           C  
ANISOU 6058  C   SER A 829    14514  16083  11286  -5004   3381    -22       C  
ATOM   6059  O   SER A 829     -66.582 -48.307 -27.878  1.00113.96           O  
ANISOU 6059  O   SER A 829    15357  16233  11711  -5083   3390    323       O  
ATOM   6060  CB  SER A 829     -69.387 -47.717 -27.813  1.00116.23           C  
ANISOU 6060  CB  SER A 829    14724  17115  12325  -5507   3862   -416       C  
ATOM   6061  OG  SER A 829     -70.580 -47.442 -27.101  1.00120.82           O  
ANISOU 6061  OG  SER A 829    14969  18050  12886  -5681   4157   -686       O  
ATOM   6062  N   ILE A 830     -66.259 -46.274 -28.793  1.00105.04           N  
ANISOU 6062  N   ILE A 830    13791  15444  10674  -4764   3127   -119       N  
ATOM   6063  CA  ILE A 830     -64.966 -46.646 -29.351  1.00100.53           C  
ANISOU 6063  CA  ILE A 830    13583  14522  10092  -4580   2856    189       C  
ATOM   6064  C   ILE A 830     -63.934 -46.720 -28.231  1.00103.59           C  
ANISOU 6064  C   ILE A 830    14363  14879  10119  -4398   2794    496       C  
ATOM   6065  O   ILE A 830     -64.007 -45.987 -27.234  1.00109.21           O  
ANISOU 6065  O   ILE A 830    15021  15895  10579  -4327   2878    406       O  
ATOM   6066  CB  ILE A 830     -64.538 -45.657 -30.453  1.00 99.72           C  
ANISOU 6066  CB  ILE A 830    13278  14403  10210  -4269   2528    -25       C  
ATOM   6067  CG1 ILE A 830     -63.483 -46.287 -31.363  1.00 99.17           C  
ANISOU 6067  CG1 ILE A 830    13500  13914  10264  -4102   2258    235       C  
ATOM   6068  CG2 ILE A 830     -64.014 -44.356 -29.851  1.00100.23           C  
ANISOU 6068  CG2 ILE A 830    13277  14719  10088  -3962   2381   -145       C  
ATOM   6069  CD1 ILE A 830     -63.079 -45.406 -32.523  1.00 96.61           C  
ANISOU 6069  CD1 ILE A 830    13001  13518  10187  -3759   1918     41       C  
ATOM   6070  N   LEU A 831     -62.974 -47.630 -28.381  1.00 97.50           N  
ANISOU 6070  N   LEU A 831    13979  13737   9328  -4300   2629    837       N  
ATOM   6071  CA  LEU A 831