CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 23-NOV-16 5U0B  ***

elNémo ID: 19110319113466525

Job options:

ID        	=	 19110319113466525
JOBID     	=	 TRANSFERASE 23-NOV-16 5U0B
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             23-NOV-16   5U0B              
TITLE     STRUCTURE OF FULL-LENGTH ZIKA VIRUS NS5                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GENOME POLYPROTEIN;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 EC: 2.1.1.56,2.1.1.57,2.7.7.48;                                      
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ZIKA VIRUS (STRAIN MR 766);                     
SOURCE   3 ORGANISM_COMMON: ZIKV;                                               
SOURCE   4 ORGANISM_TAXID: 64320;                                               
SOURCE   5 STRAIN: MR 766;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    VIRAL RNA POLYMERASE, TRANSFERASE                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO,F.DU                                                           
REVDAT   2   12-APR-17 5U0B    1       JRNL                                     
REVDAT   1   29-MAR-17 5U0B    0                                                
JRNL        AUTH   B.ZHAO,G.YI,F.DU,Y.C.CHUANG,R.C.VAUGHAN,B.SANKARAN,C.C.KAO,  
JRNL        AUTH 2 P.LI                                                         
JRNL        TITL   STRUCTURE AND FUNCTION OF THE ZIKA VIRUS FULL-LENGTH NS5     
JRNL        TITL 2 PROTEIN.                                                     
JRNL        REF    NAT COMMUN                    V.   8 14762 2017              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        PMID   28345656                                                     
JRNL        DOI    10.1038/NCOMMS14762                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 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) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 85.78                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 50511                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.233                           
REMARK   3   R VALUE            (WORKING SET) : 0.231                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.990                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2521                            
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 85.8096 -  7.8603    0.95     2790   163  0.1742 0.1860        
REMARK   3     2  7.8603 -  6.2395    0.98     2768   159  0.1948 0.2370        
REMARK   3     3  6.2395 -  5.4510    0.98     2727   150  0.1921 0.2200        
REMARK   3     4  5.4510 -  4.9526    0.96     2691   123  0.1884 0.2434        
REMARK   3     5  4.9526 -  4.5977    0.97     2666   151  0.1768 0.2300        
REMARK   3     6  4.5977 -  4.3266    0.98     2701   132  0.1759 0.2308        
REMARK   3     7  4.3266 -  4.1099    0.97     2673   139  0.1981 0.2215        
REMARK   3     8  4.1099 -  3.9310    0.98     2678   141  0.2155 0.2282        
REMARK   3     9  3.9310 -  3.7797    0.95     2591   153  0.2419 0.2971        
REMARK   3    10  3.7797 -  3.6493    0.95     2595   121  0.2521 0.2931        
REMARK   3    11  3.6493 -  3.5352    0.96     2627   116  0.2606 0.3561        
REMARK   3    12  3.5352 -  3.4341    0.95     2597   156  0.2877 0.3223        
REMARK   3    13  3.4341 -  3.3437    0.97     2636   139  0.2862 0.3021        
REMARK   3    14  3.3437 -  3.2621    0.97     2610   151  0.2921 0.3224        
REMARK   3    15  3.2621 -  3.1880    0.97     2662   128  0.3096 0.3026        
REMARK   3    16  3.1880 -  3.1201    0.98     2663   142  0.3238 0.3965        
REMARK   3    17  3.1201 -  3.0577    0.98     2695   114  0.3334 0.3703        
REMARK   3    18  3.0577 -  3.0000    0.98     2620   143  0.3432 0.3877        
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)     : 0.410            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.600           
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          14608                                  
REMARK   3   ANGLE     :  0.511          19740                                  
REMARK   3   CHIRALITY :  0.040           2066                                  
REMARK   3   PLANARITY :  0.004           2528                                  
REMARK   3   DIHEDRAL  : 22.272           8698                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 9                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 174 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.5918 103.9323  37.2374              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9019 T22:   0.1821                                     
REMARK   3      T33:   0.3850 T12:   0.0001                                     
REMARK   3      T13:   0.2148 T23:  -0.0024                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7410 L22:   0.1372                                     
REMARK   3      L33:   1.9360 L12:   0.1791                                     
REMARK   3      L13:  -0.2439 L23:   0.2070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0112 S12:  -0.1107 S13:  -0.0108                       
REMARK   3      S21:  -0.0114 S22:  -0.1003 S23:   0.1448                       
REMARK   3      S31:  -0.0723 S32:  -0.1015 S33:   0.0382                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 175 THROUGH 368 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  36.2085 106.3979  26.8414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7121 T22:   0.1725                                     
REMARK   3      T33:   0.3541 T12:  -0.0448                                     
REMARK   3      T13:   0.1798 T23:   0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4496 L22:   0.4187                                     
REMARK   3      L33:   1.0364 L12:  -0.2653                                     
REMARK   3      L13:  -0.1101 L23:  -0.4686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0600 S12:   0.0437 S13:  -0.0323                       
REMARK   3      S21:  -0.0574 S22:  -0.0783 S23:  -0.0274                       
REMARK   3      S31:   0.2088 S32:   0.0603 S33:   0.0131                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 369 THROUGH 414 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  32.8414 116.5078 -15.5074              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7901 T22:   0.2578                                     
REMARK   3      T33:   0.3081 T12:   0.0328                                     
REMARK   3      T13:   0.2964 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7294 L22:   0.3254                                     
REMARK   3      L33:   1.2779 L12:  -0.0009                                     
REMARK   3      L13:   1.3204 L23:   0.2937                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1536 S12:   0.1724 S13:   0.2206                       
REMARK   3      S21:   0.0185 S22:  -0.0438 S23:   0.1808                       
REMARK   3      S31:  -0.0448 S32:   0.1872 S33:  -0.3901                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 415 THROUGH 695 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.4945 112.5022  -6.9181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7501 T22:   0.2429                                     
REMARK   3      T33:   0.3010 T12:  -0.0400                                     
REMARK   3      T13:   0.2422 T23:  -0.0237                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5091 L22:   0.9408                                     
REMARK   3      L33:   1.2835 L12:  -0.1344                                     
REMARK   3      L13:   0.4636 L23:   0.3742                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0614 S12:   0.0859 S13:   0.0025                       
REMARK   3      S21:  -0.0193 S22:  -0.1182 S23:   0.1409                       
REMARK   3      S31:   0.3109 S32:  -0.0826 S33:   0.1394                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 696 THROUGH 887 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.2126 134.5440   5.7328              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3538 T22:   0.4454                                     
REMARK   3      T33:   0.3868 T12:  -0.0304                                     
REMARK   3      T13:   0.1750 T23:  -0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2038 L22:   2.9491                                     
REMARK   3      L33:   1.8970 L12:  -0.4909                                     
REMARK   3      L13:   0.0575 L23:   0.7595                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:   0.1063 S13:  -0.0047                       
REMARK   3      S21:  -0.0124 S22:  -0.1567 S23:   0.3363                       
REMARK   3      S31:   0.2580 S32:  -0.4514 S33:   0.1349                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 5 THROUGH 174 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6983  64.4922  10.4429              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3484 T22:   0.2352                                     
REMARK   3      T33:   0.3112 T12:   0.0185                                     
REMARK   3      T13:   0.1952 T23:   0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7484 L22:   0.4395                                     
REMARK   3      L33:   4.4219 L12:   0.0301                                     
REMARK   3      L13:   1.5800 L23:   0.6874                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0123 S12:  -0.0474 S13:   0.0164                       
REMARK   3      S21:  -0.0282 S22:  -0.1574 S23:   0.1486                       
REMARK   3      S31:  -0.2408 S32:  -0.3071 S33:   0.1459                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 175 THROUGH 462 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  37.6792  56.9473  33.6322              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1402 T22:   0.2179                                     
REMARK   3      T33:   0.3281 T12:  -0.0092                                     
REMARK   3      T13:   0.1294 T23:  -0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3310 L22:   0.1123                                     
REMARK   3      L33:   1.7135 L12:   0.1751                                     
REMARK   3      L13:  -0.1008 L23:   0.1769                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0181 S12:   0.0281 S13:  -0.0346                       
REMARK   3      S21:  -0.0963 S22:  -0.0391 S23:  -0.0174                       
REMARK   3      S31:  -0.2610 S32:   0.1874 S33:   0.0098                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 463 THROUGH 724 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.1059  57.8335  53.8584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1897 T22:   0.1919                                     
REMARK   3      T33:   0.3071 T12:  -0.0563                                     
REMARK   3      T13:   0.1529 T23:  -0.0057                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6070 L22:   0.5166                                     
REMARK   3      L33:   1.0165 L12:   0.1925                                     
REMARK   3      L13:  -0.1358 L23:   0.2024                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0247 S12:  -0.1146 S13:   0.0628                       
REMARK   3      S21:  -0.0979 S22:  -0.0725 S23:   0.1961                       
REMARK   3      S31:  -0.2179 S32:  -0.0668 S33:  -0.0169                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 725 THROUGH 887 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.1394  30.7205  40.8060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3076 T22:   0.1687                                     
REMARK   3      T33:   0.2705 T12:  -0.0946                                     
REMARK   3      T13:   0.1924 T23:  -0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1674 L22:   2.3396                                     
REMARK   3      L33:   2.4925 L12:  -0.0757                                     
REMARK   3      L13:  -0.0771 L23:   0.1659                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0883 S12:   0.0848 S13:   0.0184                       
REMARK   3      S21:  -0.0539 S22:   0.1001 S23:   0.0232                       
REMARK   3      S31:   0.4154 S32:  -0.1038 S33:  -0.0159                       
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 5U0B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-NOV-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000225103.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 120                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50661                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.775                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.6                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.15600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 6.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
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) : 0.71500                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 4K6M                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.39                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0 M AMMONIUM SULFATE PLUS 1% PE G      
REMARK 280  3350, 0.1 M BIS-TRIS, PH 5.5, EVAPORATION, TEMPERATURE 277K         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       68.25000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       98.50000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       68.25000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       98.50000            
REMARK 290   SMTRY3   4  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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     GLY A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     THR A   888                                                      
REMARK 465     GLN A   889                                                      
REMARK 465     VAL A   890                                                      
REMARK 465     ARG A   891                                                      
REMARK 465     TYR A   892                                                      
REMARK 465     LEU A   893                                                      
REMARK 465     GLY A   894                                                      
REMARK 465     GLU A   895                                                      
REMARK 465     GLU A   896                                                      
REMARK 465     GLY A   897                                                      
REMARK 465     SER A   898                                                      
REMARK 465     THR A   899                                                      
REMARK 465     PRO A   900                                                      
REMARK 465     GLY A   901                                                      
REMARK 465     VAL A   902                                                      
REMARK 465     LEU A   903                                                      
REMARK 465     GLY B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     THR B     4                                                      
REMARK 465     THR B   888                                                      
REMARK 465     GLN B   889                                                      
REMARK 465     VAL B   890                                                      
REMARK 465     ARG B   891                                                      
REMARK 465     TYR B   892                                                      
REMARK 465     LEU B   893                                                      
REMARK 465     GLY B   894                                                      
REMARK 465     GLU B   895                                                      
REMARK 465     GLU B   896                                                      
REMARK 465     GLY B   897                                                      
REMARK 465     SER B   898                                                      
REMARK 465     THR B   899                                                      
REMARK 465     PRO B   900                                                      
REMARK 465     GLY B   901                                                      
REMARK 465     VAL B   902                                                      
REMARK 465     LEU B   903                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A    99     NH1  ARG A   101              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  48       95.32    -62.72                                   
REMARK 500    GLN A 117       43.15   -103.88                                   
REMARK 500    CYS A 180       88.43   -157.28                                   
REMARK 500    LEU A 211       49.57    -76.94                                   
REMARK 500    LYS A 226       16.35   -151.87                                   
REMARK 500    ASN A 274       76.52   -104.55                                   
REMARK 500    ILE A 277      -60.89    -96.53                                   
REMARK 500    GLN A 368     -177.99    -69.35                                   
REMARK 500    ARG A 389       43.33    -96.82                                   
REMARK 500    LYS A 390      129.34   -171.64                                   
REMARK 500    ASN A 407       38.57    -96.97                                   
REMARK 500    ILE A 413      -49.68   -136.36                                   
REMARK 500    LYS A 418       42.94   -100.43                                   
REMARK 500    PHE A 466     -130.19     57.18                                   
REMARK 500    VAL A 508       13.45   -143.39                                   
REMARK 500    ARG A 515      -12.40   -147.07                                   
REMARK 500    ILE A 543       99.21    -62.42                                   
REMARK 500    ASP A 599     -158.61   -136.03                                   
REMARK 500    GLN A 600      173.09     62.97                                   
REMARK 500    GLU A 632     -165.46   -105.72                                   
REMARK 500    ARG A 640      -90.20    -56.29                                   
REMARK 500    ASP A 722       94.03     64.14                                   
REMARK 500    ALA A 746       55.25   -114.02                                   
REMARK 500    ILE A 820      -69.58   -123.72                                   
REMARK 500    HIS A 825       35.62    -86.82                                   
REMARK 500    GLU B   6      108.56    -52.37                                   
REMARK 500    ASP B 146       60.91   -117.59                                   
REMARK 500    ARG B 175       74.76     32.58                                   
REMARK 500    CYS B 180       91.41   -160.64                                   
REMARK 500    LEU B 211       48.88    -87.02                                   
REMARK 500    ASP B 245      147.55   -170.81                                   
REMARK 500    ASN B 407       40.55    -92.64                                   
REMARK 500    GLU B 419      -21.52   -140.01                                   
REMARK 500    PHE B 466     -138.02     56.72                                   
REMARK 500    THR B 573      -35.31   -136.38                                   
REMARK 500    ALA B 585     -165.10   -100.23                                   
REMARK 500    SER B 596     -101.54   -120.39                                   
REMARK 500    ARG B 597      148.56     69.42                                   
REMARK 500    GLN B 600      161.68     69.51                                   
REMARK 500    LEU B 639       76.38     63.78                                   
REMARK 500    LYS B 641       72.78     55.56                                   
REMARK 500    LEU B 680       20.73   -151.90                                   
REMARK 500    SER B 712       -5.85     65.88                                   
REMARK 500    ILE B 820      -60.36   -133.91                                   
REMARK 500    PRO B 857     -167.67    -71.78                                   
REMARK 500    ARG B 858      -51.68     60.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 439   OE1                                                    
REMARK 620 2 HIS A 443   NE2  96.8                                              
REMARK 620 3 CYS A 448   SG  133.4 113.0                                        
REMARK 620 4 CYS A 451   SG   95.5 109.6 106.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 714   NE2                                                    
REMARK 620 2 CYS A 730   SG  104.6                                              
REMARK 620 3 CYS A 849   SG   92.9 106.0                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1002  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 439   OE1                                                    
REMARK 620 2 HIS B 443   NE2  81.7                                              
REMARK 620 3 CYS B 448   SG  136.7 115.9                                        
REMARK 620 4 CYS B 451   SG  100.9 108.4 109.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN B1003  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 714   NE2                                                    
REMARK 620 2 CYS B 730   SG  109.9                                              
REMARK 620 3 CYS B 849   SG   99.1 105.7                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH A 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SAH B 1001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1006                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5U0C   RELATED DB: PDB                                   
DBREF  5U0B A    1   903  UNP    Q32ZE1   POLG_ZIKV     2517   3419             
DBREF  5U0B B    1   903  UNP    Q32ZE1   POLG_ZIKV     2517   3419             
SEQADV 5U0B LEU A   62  UNP  Q32ZE1    ILE  2578 ENGINEERED MUTATION            
SEQADV 5U0B SER A  212  UNP  Q32ZE1    CYS  2728 ENGINEERED MUTATION            
SEQADV 5U0B LEU B   62  UNP  Q32ZE1    ILE  2578 ENGINEERED MUTATION            
SEQADV 5U0B SER B  212  UNP  Q32ZE1    CYS  2728 ENGINEERED MUTATION            
SEQRES   1 A  903  GLY GLY GLY THR GLY GLU THR LEU GLY GLU LYS TRP LYS          
SEQRES   2 A  903  ALA ARG LEU ASN GLN MET SER ALA LEU GLU PHE TYR SER          
SEQRES   3 A  903  TYR LYS LYS SER GLY ILE THR GLU VAL CYS ARG GLU GLU          
SEQRES   4 A  903  ALA ARG ARG ALA LEU LYS ASP GLY VAL ALA THR GLY GLY          
SEQRES   5 A  903  HIS ALA VAL SER ARG GLY SER ALA LYS LEU ARG TRP LEU          
SEQRES   6 A  903  GLU GLU ARG GLY TYR LEU GLN PRO TYR GLY LYS VAL VAL          
SEQRES   7 A  903  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR ALA          
SEQRES   8 A  903  ALA THR ILE ARG LYS VAL GLN GLU VAL ARG GLY TYR THR          
SEQRES   9 A  903  LYS GLY GLY PRO GLY HIS GLU GLU PRO MET LEU VAL GLN          
SEQRES  10 A  903  SER TYR GLY TRP ASN ILE VAL ARG LEU LYS SER GLY VAL          
SEQRES  11 A  903  ASP VAL PHE HIS MET ALA ALA GLU PRO CYS ASP THR LEU          
SEQRES  12 A  903  LEU CYS ASP ILE GLY GLU SER SER SER SER PRO GLU VAL          
SEQRES  13 A  903  GLU GLU THR ARG THR LEU ARG VAL LEU SER MET VAL GLY          
SEQRES  14 A  903  ASP TRP LEU GLU LYS ARG PRO GLY ALA PHE CYS ILE LYS          
SEQRES  15 A  903  VAL LEU CYS PRO TYR THR SER THR MET MET GLU THR MET          
SEQRES  16 A  903  GLU ARG LEU GLN ARG ARG HIS GLY GLY GLY LEU VAL ARG          
SEQRES  17 A  903  VAL PRO LEU SER ARG ASN SER THR HIS GLU MET TYR TRP          
SEQRES  18 A  903  VAL SER GLY ALA LYS SER ASN ILE ILE LYS SER VAL SER          
SEQRES  19 A  903  THR THR SER GLN LEU LEU LEU GLY ARG MET ASP GLY PRO          
SEQRES  20 A  903  ARG ARG PRO VAL LYS TYR GLU GLU ASP VAL ASN LEU GLY          
SEQRES  21 A  903  SER GLY THR ARG ALA VAL ALA SER CYS ALA GLU ALA PRO          
SEQRES  22 A  903  ASN MET LYS ILE ILE GLY ARG ARG ILE GLU ARG ILE ARG          
SEQRES  23 A  903  ASN GLU HIS ALA GLU THR TRP PHE LEU ASP GLU ASN HIS          
SEQRES  24 A  903  PRO TYR ARG THR TRP ALA TYR HIS GLY SER TYR GLU ALA          
SEQRES  25 A  903  PRO THR GLN GLY SER ALA SER SER LEU VAL ASN GLY VAL          
SEQRES  26 A  903  VAL ARG LEU LEU SER LYS PRO TRP ASP VAL VAL THR GLY          
SEQRES  27 A  903  VAL THR GLY ILE ALA MET THR ASP THR THR PRO TYR GLY          
SEQRES  28 A  903  GLN GLN ARG VAL PHE LYS GLU LYS VAL ASP THR ARG VAL          
SEQRES  29 A  903  PRO ASP PRO GLN GLU GLY THR ARG GLN VAL MET ASN ILE          
SEQRES  30 A  903  VAL SER SER TRP LEU TRP LYS GLU LEU GLY LYS ARG LYS          
SEQRES  31 A  903  ARG PRO ARG VAL CYS THR LYS GLU GLU PHE ILE ASN LYS          
SEQRES  32 A  903  VAL ARG SER ASN ALA ALA LEU GLY ALA ILE PHE GLU GLU          
SEQRES  33 A  903  GLU LYS GLU TRP LYS THR ALA VAL GLU ALA VAL ASN ASP          
SEQRES  34 A  903  PRO ARG PHE TRP ALA LEU VAL ASP ARG GLU ARG GLU HIS          
SEQRES  35 A  903  HIS LEU ARG GLY GLU CYS HIS SER CYS VAL TYR ASN MET          
SEQRES  36 A  903  MET GLY LYS ARG GLU LYS LYS GLN GLY GLU PHE GLY LYS          
SEQRES  37 A  903  ALA LYS GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY          
SEQRES  38 A  903  ALA ARG PHE LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN          
SEQRES  39 A  903  GLU ASP HIS TRP MET GLY ARG GLU ASN SER GLY GLY GLY          
SEQRES  40 A  903  VAL GLU GLY LEU GLY LEU GLN ARG LEU GLY TYR ILE LEU          
SEQRES  41 A  903  GLU GLU MET ASN ARG ALA PRO GLY GLY LYS MET TYR ALA          
SEQRES  42 A  903  ASP ASP THR ALA GLY TRP ASP THR ARG ILE SER LYS PHE          
SEQRES  43 A  903  ASP LEU GLU ASN GLU ALA LEU ILE THR ASN GLN MET GLU          
SEQRES  44 A  903  GLU GLY HIS ARG THR LEU ALA LEU ALA VAL ILE LYS TYR          
SEQRES  45 A  903  THR TYR GLN ASN LYS VAL VAL LYS VAL LEU ARG PRO ALA          
SEQRES  46 A  903  GLU GLY GLY LYS THR VAL MET ASP ILE ILE SER ARG GLN          
SEQRES  47 A  903  ASP GLN ARG GLY SER GLY GLN VAL VAL THR TYR ALA LEU          
SEQRES  48 A  903  ASN THR PHE THR ASN LEU VAL VAL GLN LEU ILE ARG ASN          
SEQRES  49 A  903  MET GLU ALA GLU GLU VAL LEU GLU MET GLN ASP LEU TRP          
SEQRES  50 A  903  LEU LEU ARG LYS PRO GLU LYS VAL THR ARG TRP LEU GLN          
SEQRES  51 A  903  SER ASN GLY TRP ASP ARG LEU LYS ARG MET ALA VAL SER          
SEQRES  52 A  903  GLY ASP ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE          
SEQRES  53 A  903  ALA HIS ALA LEU ARG PHE LEU ASN ASP MET GLY LYS VAL          
SEQRES  54 A  903  ARG LYS ASP THR GLN GLU TRP LYS PRO SER THR GLY TRP          
SEQRES  55 A  903  SER ASN TRP GLU GLU VAL PRO PHE CYS SER HIS HIS PHE          
SEQRES  56 A  903  ASN LYS LEU TYR LEU LYS ASP GLY ARG SER ILE VAL VAL          
SEQRES  57 A  903  PRO CYS ARG HIS GLN ASP GLU LEU ILE GLY ARG ALA ARG          
SEQRES  58 A  903  VAL SER PRO GLY ALA GLY TRP SER ILE ARG GLU THR ALA          
SEQRES  59 A  903  CYS LEU ALA LYS SER TYR ALA GLN MET TRP GLN LEU LEU          
SEQRES  60 A  903  TYR PHE HIS ARG ARG ASP LEU ARG LEU MET ALA ASN ALA          
SEQRES  61 A  903  ILE CYS SER ALA VAL PRO VAL ASP TRP VAL PRO THR GLY          
SEQRES  62 A  903  ARG THR THR TRP SER ILE HIS GLY LYS GLY GLU TRP MET          
SEQRES  63 A  903  THR THR GLU ASP MET LEU MET VAL TRP ASN ARG VAL TRP          
SEQRES  64 A  903  ILE GLU GLU ASN ASP HIS MET GLU ASP LYS THR PRO VAL          
SEQRES  65 A  903  THR LYS TRP THR ASP ILE PRO TYR LEU GLY LYS ARG GLU          
SEQRES  66 A  903  ASP LEU TRP CYS GLY SER LEU ILE GLY HIS ARG PRO ARG          
SEQRES  67 A  903  THR THR TRP ALA GLU ASN ILE LYS ASP THR VAL ASN MET          
SEQRES  68 A  903  VAL ARG ARG ILE ILE GLY ASP GLU GLU LYS TYR MET ASP          
SEQRES  69 A  903  TYR LEU SER THR GLN VAL ARG TYR LEU GLY GLU GLU GLY          
SEQRES  70 A  903  SER THR PRO GLY VAL LEU                                      
SEQRES   1 B  903  GLY GLY GLY THR GLY GLU THR LEU GLY GLU LYS TRP LYS          
SEQRES   2 B  903  ALA ARG LEU ASN GLN MET SER ALA LEU GLU PHE TYR SER          
SEQRES   3 B  903  TYR LYS LYS SER GLY ILE THR GLU VAL CYS ARG GLU GLU          
SEQRES   4 B  903  ALA ARG ARG ALA LEU LYS ASP GLY VAL ALA THR GLY GLY          
SEQRES   5 B  903  HIS ALA VAL SER ARG GLY SER ALA LYS LEU ARG TRP LEU          
SEQRES   6 B  903  GLU GLU ARG GLY TYR LEU GLN PRO TYR GLY LYS VAL VAL          
SEQRES   7 B  903  ASP LEU GLY CYS GLY ARG GLY GLY TRP SER TYR TYR ALA          
SEQRES   8 B  903  ALA THR ILE ARG LYS VAL GLN GLU VAL ARG GLY TYR THR          
SEQRES   9 B  903  LYS GLY GLY PRO GLY HIS GLU GLU PRO MET LEU VAL GLN          
SEQRES  10 B  903  SER TYR GLY TRP ASN ILE VAL ARG LEU LYS SER GLY VAL          
SEQRES  11 B  903  ASP VAL PHE HIS MET ALA ALA GLU PRO CYS ASP THR LEU          
SEQRES  12 B  903  LEU CYS ASP ILE GLY GLU SER SER SER SER PRO GLU VAL          
SEQRES  13 B  903  GLU GLU THR ARG THR LEU ARG VAL LEU SER MET VAL GLY          
SEQRES  14 B  903  ASP TRP LEU GLU LYS ARG PRO GLY ALA PHE CYS ILE LYS          
SEQRES  15 B  903  VAL LEU CYS PRO TYR THR SER THR MET MET GLU THR MET          
SEQRES  16 B  903  GLU ARG LEU GLN ARG ARG HIS GLY GLY GLY LEU VAL ARG          
SEQRES  17 B  903  VAL PRO LEU SER ARG ASN SER THR HIS GLU MET TYR TRP          
SEQRES  18 B  903  VAL SER GLY ALA LYS SER ASN ILE ILE LYS SER VAL SER          
SEQRES  19 B  903  THR THR SER GLN LEU LEU LEU GLY ARG MET ASP GLY PRO          
SEQRES  20 B  903  ARG ARG PRO VAL LYS TYR GLU GLU ASP VAL ASN LEU GLY          
SEQRES  21 B  903  SER GLY THR ARG ALA VAL ALA SER CYS ALA GLU ALA PRO          
SEQRES  22 B  903  ASN MET LYS ILE ILE GLY ARG ARG ILE GLU ARG ILE ARG          
SEQRES  23 B  903  ASN GLU HIS ALA GLU THR TRP PHE LEU ASP GLU ASN HIS          
SEQRES  24 B  903  PRO TYR ARG THR TRP ALA TYR HIS GLY SER TYR GLU ALA          
SEQRES  25 B  903  PRO THR GLN GLY SER ALA SER SER LEU VAL ASN GLY VAL          
SEQRES  26 B  903  VAL ARG LEU LEU SER LYS PRO TRP ASP VAL VAL THR GLY          
SEQRES  27 B  903  VAL THR GLY ILE ALA MET THR ASP THR THR PRO TYR GLY          
SEQRES  28 B  903  GLN GLN ARG VAL PHE LYS GLU LYS VAL ASP THR ARG VAL          
SEQRES  29 B  903  PRO ASP PRO GLN GLU GLY THR ARG GLN VAL MET ASN ILE          
SEQRES  30 B  903  VAL SER SER TRP LEU TRP LYS GLU LEU GLY LYS ARG LYS          
SEQRES  31 B  903  ARG PRO ARG VAL CYS THR LYS GLU GLU PHE ILE ASN LYS          
SEQRES  32 B  903  VAL ARG SER ASN ALA ALA LEU GLY ALA ILE PHE GLU GLU          
SEQRES  33 B  903  GLU LYS GLU TRP LYS THR ALA VAL GLU ALA VAL ASN ASP          
SEQRES  34 B  903  PRO ARG PHE TRP ALA LEU VAL ASP ARG GLU ARG GLU HIS          
SEQRES  35 B  903  HIS LEU ARG GLY GLU CYS HIS SER CYS VAL TYR ASN MET          
SEQRES  36 B  903  MET GLY LYS ARG GLU LYS LYS GLN GLY GLU PHE GLY LYS          
SEQRES  37 B  903  ALA LYS GLY SER ARG ALA ILE TRP TYR MET TRP LEU GLY          
SEQRES  38 B  903  ALA ARG PHE LEU GLU PHE GLU ALA LEU GLY PHE LEU ASN          
SEQRES  39 B  903  GLU ASP HIS TRP MET GLY ARG GLU ASN SER GLY GLY GLY          
SEQRES  40 B  903  VAL GLU GLY LEU GLY LEU GLN ARG LEU GLY TYR ILE LEU          
SEQRES  41 B  903  GLU GLU MET ASN ARG ALA PRO GLY GLY LYS MET TYR ALA          
SEQRES  42 B  903  ASP ASP THR ALA GLY TRP ASP THR ARG ILE SER LYS PHE          
SEQRES  43 B  903  ASP LEU GLU ASN GLU ALA LEU ILE THR ASN GLN MET GLU          
SEQRES  44 B  903  GLU GLY HIS ARG THR LEU ALA LEU ALA VAL ILE LYS TYR          
SEQRES  45 B  903  THR TYR GLN ASN LYS VAL VAL LYS VAL LEU ARG PRO ALA          
SEQRES  46 B  903  GLU GLY GLY LYS THR VAL MET ASP ILE ILE SER ARG GLN          
SEQRES  47 B  903  ASP GLN ARG GLY SER GLY GLN VAL VAL THR TYR ALA LEU          
SEQRES  48 B  903  ASN THR PHE THR ASN LEU VAL VAL GLN LEU ILE ARG ASN          
SEQRES  49 B  903  MET GLU ALA GLU GLU VAL LEU GLU MET GLN ASP LEU TRP          
SEQRES  50 B  903  LEU LEU ARG LYS PRO GLU LYS VAL THR ARG TRP LEU GLN          
SEQRES  51 B  903  SER ASN GLY TRP ASP ARG LEU LYS ARG MET ALA VAL SER          
SEQRES  52 B  903  GLY ASP ASP CYS VAL VAL LYS PRO ILE ASP ASP ARG PHE          
SEQRES  53 B  903  ALA HIS ALA LEU ARG PHE LEU ASN ASP MET GLY LYS VAL          
SEQRES  54 B  903  ARG LYS ASP THR GLN GLU TRP LYS PRO SER THR GLY TRP          
SEQRES  55 B  903  SER ASN TRP GLU GLU VAL PRO PHE CYS SER HIS HIS PHE          
SEQRES  56 B  903  ASN LYS LEU TYR LEU LYS ASP GLY ARG SER ILE VAL VAL          
SEQRES  57 B  903  PRO CYS ARG HIS GLN ASP GLU LEU ILE GLY ARG ALA ARG          
SEQRES  58 B  903  VAL SER PRO GLY ALA GLY TRP SER ILE ARG GLU THR ALA          
SEQRES  59 B  903  CYS LEU ALA LYS SER TYR ALA GLN MET TRP GLN LEU LEU          
SEQRES  60 B  903  TYR PHE HIS ARG ARG ASP LEU ARG LEU MET ALA ASN ALA          
SEQRES  61 B  903  ILE CYS SER ALA VAL PRO VAL ASP TRP VAL PRO THR GLY          
SEQRES  62 B  903  ARG THR THR TRP SER ILE HIS GLY LYS GLY GLU TRP MET          
SEQRES  63 B  903  THR THR GLU ASP MET LEU MET VAL TRP ASN ARG VAL TRP          
SEQRES  64 B  903  ILE GLU GLU ASN ASP HIS MET GLU ASP LYS THR PRO VAL          
SEQRES  65 B  903  THR LYS TRP THR ASP ILE PRO TYR LEU GLY LYS ARG GLU          
SEQRES  66 B  903  ASP LEU TRP CYS GLY SER LEU ILE GLY HIS ARG PRO ARG          
SEQRES  67 B  903  THR THR TRP ALA GLU ASN ILE LYS ASP THR VAL ASN MET          
SEQRES  68 B  903  VAL ARG ARG ILE ILE GLY ASP GLU GLU LYS TYR MET ASP          
SEQRES  69 B  903  TYR LEU SER THR GLN VAL ARG TYR LEU GLY GLU GLU GLY          
SEQRES  70 B  903  SER THR PRO GLY VAL LEU                                      
HET    SAH  A1001      26                                                       
HET     ZN  A1002       1                                                       
HET     ZN  A1003       1                                                       
HET    SO4  A1004       5                                                       
HET    SO4  A1005       5                                                       
HET    SO4  A1006       5                                                       
HET    SAH  B1001      26                                                       
HET     ZN  B1002       1                                                       
HET     ZN  B1003       1                                                       
HET    SO4  B1004       5                                                       
HET    SO4  B1005       5                                                       
HET    SO4  B1006       5                                                       
HETNAM     SAH S-ADENOSYL-L-HOMOCYSTEINE                                        
HETNAM      ZN ZINC ION                                                         
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SAH    2(C14 H20 N6 O5 S)                                           
FORMUL   4   ZN    4(ZN 2+)                                                     
FORMUL   6  SO4    6(O4 S 2-)                                                   
HELIX    1 AA1 THR A    7  MET A   19  1                                  13    
HELIX    2 AA2 SER A   20  LYS A   29  1                                  10    
HELIX    3 AA3 ARG A   37  GLY A   47  1                                  11    
HELIX    4 AA4 ARG A   57  ARG A   68  1                                  12    
HELIX    5 AA5 GLY A   85  ALA A   92  1                                   8    
HELIX    6 AA6 GLY A  120  ASN A  122  5                                   3    
HELIX    7 AA7 ASP A  131  MET A  135  5                                   5    
HELIX    8 AA8 SER A  153  LEU A  172  1                                  20    
HELIX    9 AA9 GLU A  173  ARG A  175  5                                   3    
HELIX   10 AB1 THR A  188  GLY A  203  1                                  16    
HELIX   11 AB2 ASN A  228  MET A  244  1                                  17    
HELIX   12 AB3 ILE A  278  HIS A  289  1                                  12    
HELIX   13 AB4 ASN A  323  SER A  330  1                                   8    
HELIX   14 AB5 LYS A  331  ASP A  334  5                                   4    
HELIX   15 AB6 VAL A  336  GLY A  341  1                                   6    
HELIX   16 AB7 THR A  348  VAL A  360  1                                  13    
HELIX   17 AB8 GLN A  368  GLY A  387  1                                  20    
HELIX   18 AB9 THR A  396  ASN A  402  1                                   7    
HELIX   19 AC1 PHE A  414  LYS A  418  5                                   5    
HELIX   20 AC2 THR A  422  VAL A  427  1                                   6    
HELIX   21 AC3 ASP A  429  ARG A  445  1                                  17    
HELIX   22 AC4 TRP A  479  GLY A  491  1                                  13    
HELIX   23 AC5 GLY A  491  ASP A  496  1                                   6    
HELIX   24 AC6 GLY A  500  GLY A  505  1                                   6    
HELIX   25 AC7 GLY A  512  ASN A  524  1                                  13    
HELIX   26 AC8 GLY A  538  ARG A  542  5                                   5    
HELIX   27 AC9 SER A  544  ALA A  552  1                                   9    
HELIX   28 AD1 LEU A  553  MET A  558  5                                   6    
HELIX   29 AD2 GLU A  559  TYR A  572  1                                  14    
HELIX   30 AD3 VAL A  607  GLU A  628  1                                  22    
HELIX   31 AD4 MET A  633  TRP A  637  5                                   5    
HELIX   32 AD5 PRO A  642  ARG A  659  1                                  18    
HELIX   33 AD6 ASP A  673  ALA A  679  5                                   7    
HELIX   34 AD7 LEU A  680  MET A  686  1                                   7    
HELIX   35 AD8 ASN A  704  VAL A  708  5                                   5    
HELIX   36 AD9 HIS A  732  ARG A  741  1                                  10    
HELIX   37 AE1 SER A  749  TYR A  768  1                                  20    
HELIX   38 AE2 ARG A  771  VAL A  785  1                                  15    
HELIX   39 AE3 ASP A  810  ILE A  820  1                                  11    
HELIX   40 AE4 LYS A  834  ILE A  838  5                                   5    
HELIX   41 AE5 GLY A  842  CYS A  849  1                                   8    
HELIX   42 AE6 HIS A  855  ASN A  864  1                                  10    
HELIX   43 AE7 ASN A  864  GLY A  877  1                                  14    
HELIX   44 AE8 THR B    7  GLN B   18  1                                  12    
HELIX   45 AE9 SER B   20  LYS B   28  1                                   9    
HELIX   46 AF1 ARG B   37  GLY B   47  1                                  11    
HELIX   47 AF2 ARG B   57  GLU B   67  1                                  11    
HELIX   48 AF3 GLY B   85  ALA B   92  1                                   8    
HELIX   49 AF4 GLY B  120  ASN B  122  5                                   3    
HELIX   50 AF5 ASP B  131  MET B  135  5                                   5    
HELIX   51 AF6 SER B  153  GLU B  173  1                                  21    
HELIX   52 AF7 THR B  188  GLY B  203  1                                  16    
HELIX   53 AF8 ASN B  228  MET B  244  1                                  17    
HELIX   54 AF9 ASN B  274  HIS B  289  1                                  16    
HELIX   55 AG1 ASN B  323  SER B  330  1                                   8    
HELIX   56 AG2 LYS B  331  ASP B  334  5                                   4    
HELIX   57 AG3 VAL B  336  GLY B  341  1                                   6    
HELIX   58 AG4 THR B  348  VAL B  360  1                                  13    
HELIX   59 AG5 GLN B  368  GLY B  387  1                                  20    
HELIX   60 AG6 THR B  396  ASN B  402  1                                   7    
HELIX   61 AG7 PHE B  414  LYS B  418  5                                   5    
HELIX   62 AG8 THR B  422  VAL B  427  1                                   6    
HELIX   63 AG9 ASP B  429  ARG B  445  1                                  17    
HELIX   64 AH1 TRP B  479  GLY B  491  1                                  13    
HELIX   65 AH2 GLY B  491  ASP B  496  1                                   6    
HELIX   66 AH3 GLY B  500  GLY B  505  1                                   6    
HELIX   67 AH4 GLY B  512  ARG B  525  1                                  14    
HELIX   68 AH5 GLY B  538  ILE B  543  5                                   6    
HELIX   69 AH6 SER B  544  ALA B  552  1                                   9    
HELIX   70 AH7 LEU B  553  MET B  558  5                                   6    
HELIX   71 AH8 GLU B  559  TYR B  572  1                                  14    
HELIX   72 AH9 GLU B  586  GLY B  588  5                                   3    
HELIX   73 AI1 VAL B  607  GLU B  628  1                                  22    
HELIX   74 AI2 PRO B  642  LYS B  658  1                                  17    
HELIX   75 AI3 ASP B  673  ALA B  679  5                                   7    
HELIX   76 AI4 LEU B  680  MET B  686  1                                   7    
HELIX   77 AI5 ASN B  704  VAL B  708  5                                   5    
HELIX   78 AI6 HIS B  732  ARG B  741  1                                  10    
HELIX   79 AI7 SER B  749  TYR B  768  1                                  20    
HELIX   80 AI8 ARG B  771  VAL B  785  1                                  15    
HELIX   81 AI9 ASP B  810  ILE B  820  1                                  11    
HELIX   82 AJ1 LYS B  834  ILE B  838  5                                   5    
HELIX   83 AJ2 GLY B  842  CYS B  849  1                                   8    
HELIX   84 AJ3 HIS B  855  ASN B  864  1                                  10    
HELIX   85 AJ4 ASN B  864  GLY B  877  1                                  14    
SHEET    1 AA1 2 THR A  33  VAL A  35  0                                        
SHEET    2 AA1 2 LYS A 252  GLU A 254  1  O  LYS A 252   N  GLU A  34           
SHEET    1 AA2 7 VAL A 124  LYS A 127  0                                        
SHEET    2 AA2 7 VAL A  97  TYR A 103  1  N  GLY A 102   O  LYS A 127           
SHEET    3 AA2 7 GLY A  75  LEU A  80  1  N  VAL A  77   O  GLU A  99           
SHEET    4 AA2 7 THR A 142  CYS A 145  1  O  LEU A 144   N  VAL A  78           
SHEET    5 AA2 7 ALA A 178  VAL A 183  1  O  CYS A 180   N  LEU A 143           
SHEET    6 AA2 7 MET A 219  VAL A 222 -1  O  TRP A 221   N  ILE A 181           
SHEET    7 AA2 7 GLY A 205  VAL A 207 -1  N  VAL A 207   O  TYR A 220           
SHEET    1 AA3 5 ALA A 305  GLU A 311  0                                        
SHEET    2 AA3 5 THR A 590  ARG A 597 -1  O  MET A 592   N  TYR A 310           
SHEET    3 AA3 5 LYS A 577  PRO A 584 -1  N  VAL A 581   O  ASP A 593           
SHEET    4 AA3 5 TYR A 453  GLY A 457  1  N  TYR A 453   O  VAL A 578           
SHEET    5 AA3 5 ALA A 474  MET A 478 -1  O  TYR A 477   N  ASN A 454           
SHEET    1 AA4 2 LEU A 321  VAL A 322  0                                        
SHEET    2 AA4 2 VAL A 742  SER A 743 -1  O  SER A 743   N  LEU A 321           
SHEET    1 AA5 2 ILE A 342  MET A 344  0                                        
SHEET    2 AA5 2 LYS A 461  GLN A 463 -1  O  LYS A 462   N  ALA A 343           
SHEET    1 AA6 2 MET A 660  SER A 663  0                                        
SHEET    2 AA6 2 ASP A 666  VAL A 669 -1  O  ASP A 666   N  SER A 663           
SHEET    1 AA7 2 HIS A 714  TYR A 719  0                                        
SHEET    2 AA7 2 SER A 725  CYS A 730 -1  O  ILE A 726   N  LEU A 718           
SHEET    1 AA8 2 THR B  33  VAL B  35  0                                        
SHEET    2 AA8 2 LYS B 252  GLU B 254  1  O  LYS B 252   N  GLU B  34           
SHEET    1 AA9 7 VAL B 124  LYS B 127  0                                        
SHEET    2 AA9 7 VAL B  97  TYR B 103  1  N  GLY B 102   O  ARG B 125           
SHEET    3 AA9 7 GLY B  75  LEU B  80  1  N  VAL B  77   O  ARG B 101           
SHEET    4 AA9 7 THR B 142  CYS B 145  1  O  LEU B 144   N  VAL B  78           
SHEET    5 AA9 7 ALA B 178  VAL B 183  1  O  LYS B 182   N  CYS B 145           
SHEET    6 AA9 7 MET B 219  VAL B 222 -1  O  MET B 219   N  VAL B 183           
SHEET    7 AA9 7 GLY B 205  VAL B 207 -1  N  VAL B 207   O  TYR B 220           
SHEET    1 AB1 5 TYR B 306  GLU B 311  0                                        
SHEET    2 AB1 5 THR B 590  ILE B 595 -1  O  MET B 592   N  TYR B 310           
SHEET    3 AB1 5 VAL B 579  PRO B 584 -1  N  VAL B 581   O  ASP B 593           
SHEET    4 AB1 5 TYR B 453  GLY B 457  1  N  TYR B 453   O  LYS B 580           
SHEET    5 AB1 5 ALA B 474  MET B 478 -1  O  TYR B 477   N  ASN B 454           
SHEET    1 AB2 2 ILE B 342  MET B 344  0                                        
SHEET    2 AB2 2 LYS B 461  GLN B 463 -1  O  LYS B 462   N  ALA B 343           
SHEET    1 AB3 2 MET B 660  SER B 663  0                                        
SHEET    2 AB3 2 ASP B 666  VAL B 669 -1  O  ASP B 666   N  SER B 663           
SHEET    1 AB4 2 HIS B 714  TYR B 719  0                                        
SHEET    2 AB4 2 SER B 725  CYS B 730 -1  O  CYS B 730   N  HIS B 714           
LINK         OE1 GLU A 439                ZN    ZN A1002     1555   1555  2.31  
LINK         NE2 HIS A 443                ZN    ZN A1002     1555   1555  2.28  
LINK         SG  CYS A 448                ZN    ZN A1002     1555   1555  2.32  
LINK         SG  CYS A 451                ZN    ZN A1002     1555   1555  2.40  
LINK         NZ  LYS A 691                 O3  SO4 A1005     1555   1555  1.30  
LINK         NE2 HIS A 714                ZN    ZN A1003     1555   1555  2.20  
LINK         SG  CYS A 730                ZN    ZN A1003     1555   1555  2.45  
LINK         SG  CYS A 849                ZN    ZN A1003     1555   1555  2.35  
LINK         OE1 GLU B 439                ZN    ZN B1002     1555   1555  2.10  
LINK         NE2 HIS B 443                ZN    ZN B1002     1555   1555  2.20  
LINK         SG  CYS B 448                ZN    ZN B1002     1555   1555  2.33  
LINK         SG  CYS B 451                ZN    ZN B1002     1555   1555  2.36  
LINK         NZ  LYS B 691                 O1  SO4 B1005     1555   1555  1.30  
LINK         NE2 HIS B 714                ZN    ZN B1003     1555   1555  2.21  
LINK         SG  CYS B 730                ZN    ZN B1003     1555   1555  2.45  
LINK         SG  CYS B 849                ZN    ZN B1003     1555   1555  2.33  
CISPEP   1 ASP A  245    GLY A  246          0        -1.23                     
CISPEP   2 ASP B  245    GLY B  246          0        -0.29                     
SITE     1 AC1 15 SER A  56  GLY A  58  GLY A  81  CYS A  82                    
SITE     2 AC1 15 GLY A  86  TRP A  87  THR A 104  LYS A 105                    
SITE     3 AC1 15 HIS A 110  VAL A 130  ASP A 131  VAL A 132                    
SITE     4 AC1 15 PHE A 133  ASP A 146  ILE A 147                               
SITE     1 AC2  4 GLU A 439  HIS A 443  CYS A 448  CYS A 451                    
SITE     1 AC3  4 HIS A 714  ASN A 716  CYS A 730  CYS A 849                    
SITE     1 AC4  4 ARG A  37  ARG A  41  ARG A  57  ARG A  84                    
SITE     1 AC5  3 ARG A 473  GLY A 538  LYS A 691                               
SITE     1 AC6  3 ALA A 409  LEU A 410  GLY A 411                               
SITE     1 AC7 14 SER B  56  GLY B  58  GLY B  81  CYS B  82                    
SITE     2 AC7 14 GLY B  86  TRP B  87  THR B 104  LYS B 105                    
SITE     3 AC7 14 HIS B 110  VAL B 130  ASP B 131  VAL B 132                    
SITE     4 AC7 14 PHE B 133  ASP B 146                                          
SITE     1 AC8  4 GLU B 439  HIS B 443  CYS B 448  CYS B 451                    
SITE     1 AC9  4 HIS B 714  ASN B 716  CYS B 730  CYS B 849                    
SITE     1 AD1  4 ARG B  37  ARG B  41  ARG B  57  ARG B  84                    
SITE     1 AD2  3 ALA B 409  LEU B 410  GLY B 411                               
CRYST1  136.500  197.000   95.280  90.00  90.00  90.00 P 21 21 2     8          
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      0.007326  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005076  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010495        0.00000                         
ATOM      1  N   GLY A   5      14.184  86.344  58.807  1.00 56.78           N  
ANISOU    1  N   GLY A   5    10910   5374   5291  -2357   3167     57       N  
ATOM      2  CA  GLY A   5      15.213  86.992  59.599  1.00 56.00           C  
ANISOU    2  CA  GLY A   5    10795   5272   5210  -2217   3132    121       C  
ATOM      3  C   GLY A   5      15.952  88.073  58.837  1.00 54.53           C  
ANISOU    3  C   GLY A   5    10597   5037   5083  -2050   3109    111       C  
ATOM      4  O   GLY A   5      16.507  87.816  57.767  1.00 53.97           O  
ANISOU    4  O   GLY A   5    10600   4827   5077  -1971   3076    128       O  
ATOM      5  N   GLU A   6      15.960  89.286  59.384  1.00 56.75           N  
ANISOU    5  N   GLU A   6    10787   5435   5338  -1997   3126     76       N  
ATOM      6  CA  GLU A   6      16.608  90.399  58.704  1.00 56.28           C  
ANISOU    6  CA  GLU A   6    10686   5348   5351  -1821   3069     44       C  
ATOM      7  C   GLU A   6      18.114  90.176  58.631  1.00 54.77           C  
ANISOU    7  C   GLU A   6    10607   5003   5200  -1705   3037    157       C  
ATOM      8  O   GLU A   6      18.746  89.748  59.601  1.00 55.06           O  
ANISOU    8  O   GLU A   6    10656   5041   5222  -1691   3011    228       O  
ATOM      9  CB  GLU A   6      16.295  91.723  59.407  1.00 56.90           C  
ANISOU    9  CB  GLU A   6    10613   5592   5414  -1763   3052    -39       C  
ATOM     10  CG  GLU A   6      16.837  91.856  60.824  1.00 56.54           C  
ANISOU   10  CG  GLU A   6    10567   5603   5312  -1774   3074     22       C  
ATOM     11  CD  GLU A   6      16.516  93.203  61.446  1.00 57.29           C  
ANISOU   11  CD  GLU A   6    10519   5855   5395  -1715   3059    -73       C  
ATOM     12  OE1 GLU A   6      16.504  94.215  60.712  1.00 57.61           O  
ANISOU   12  OE1 GLU A   6    10501   5896   5491  -1597   3016   -150       O  
ATOM     13  OE2 GLU A   6      16.266  93.247  62.670  1.00 57.36           O1+
ANISOU   13  OE2 GLU A   6    10478   5983   5334  -1786   3093    -72       O1+
ATOM     14  N   THR A   7      18.682  90.451  57.459  1.00 51.23           N  
ANISOU   14  N   THR A   7    10204   4446   4817  -1600   3006    156       N  
ATOM     15  CA  THR A   7      20.099  90.238  57.224  1.00 50.58           C  
ANISOU   15  CA  THR A   7    10179   4248   4792  -1462   2937    231       C  
ATOM     16  C   THR A   7      20.926  91.321  57.915  1.00 49.89           C  
ANISOU   16  C   THR A   7    10043   4218   4694  -1365   2920    248       C  
ATOM     17  O   THR A   7      20.406  92.341  58.377  1.00 49.78           O  
ANISOU   17  O   THR A   7     9950   4319   4645  -1381   2950    186       O  
ATOM     18  CB  THR A   7      20.392  90.212  55.723  1.00 49.91           C  
ANISOU   18  CB  THR A   7    10144   4045   4775  -1388   2907    214       C  
ATOM     19  OG1 THR A   7      19.824  91.372  55.100  1.00 49.34           O  
ANISOU   19  OG1 THR A   7     9997   4030   4718  -1359   2909    124       O  
ATOM     20  CG2 THR A   7      19.803  88.961  55.085  1.00 50.70           C  
ANISOU   20  CG2 THR A   7    10303   4076   4883  -1478   2914    205       C  
ATOM     21  N   LEU A   8      22.238  91.075  57.997  1.00 49.36           N  
ANISOU   21  N   LEU A   8    10009   4090   4657  -1256   2861    321       N  
ATOM     22  CA  LEU A   8      23.141  92.054  58.596  1.00 48.75           C  
ANISOU   22  CA  LEU A   8     9889   4069   4567  -1170   2842    338       C  
ATOM     23  C   LEU A   8      23.058  93.394  57.878  1.00 47.87           C  
ANISOU   23  C   LEU A   8     9754   3961   4473  -1117   2853    268       C  
ATOM     24  O   LEU A   8      23.128  94.453  58.513  1.00 47.64           O  
ANISOU   24  O   LEU A   8     9669   4022   4412  -1101   2868    234       O  
ATOM     25  CB  LEU A   8      24.580  91.534  58.578  1.00 48.54           C  
ANISOU   25  CB  LEU A   8     9897   3982   4563  -1060   2780    423       C  
ATOM     26  CG  LEU A   8      25.023  90.590  59.695  1.00 49.40           C  
ANISOU   26  CG  LEU A   8    10015   4122   4631  -1076   2769    510       C  
ATOM     27  CD1 LEU A   8      26.540  90.587  59.804  1.00 49.05           C  
ANISOU   27  CD1 LEU A   8     9977   4069   4592   -949   2719    582       C  
ATOM     28  CD2 LEU A   8      24.387  90.972  61.023  1.00 49.95           C  
ANISOU   28  CD2 LEU A   8    10021   4323   4634  -1171   2809    498       C  
ATOM     29  N   GLY A   9      22.908  93.369  56.552  1.00 47.43           N  
ANISOU   29  N   GLY A   9     9740   3813   4470  -1086   2843    241       N  
ATOM     30  CA  GLY A   9      22.789  94.613  55.810  1.00 46.70           C  
ANISOU   30  CA  GLY A   9     9585   3737   4421  -1007   2805    153       C  
ATOM     31  C   GLY A   9      21.509  95.362  56.128  1.00 47.06           C  
ANISOU   31  C   GLY A   9     9514   3910   4456  -1045   2811     39       C  
ATOM     32  O   GLY A   9      21.499  96.594  56.191  1.00 46.69           O  
ANISOU   32  O   GLY A   9     9402   3918   4420   -978   2787    -29       O  
ATOM     33  N   GLU A  10      20.411  94.630  56.331  1.00 48.79           N  
ANISOU   33  N   GLU A  10     9710   4180   4650  -1155   2845     14       N  
ATOM     34  CA  GLU A  10      19.154  95.274  56.695  1.00 49.30           C  
ANISOU   34  CA  GLU A  10     9651   4388   4691  -1192   2854    -95       C  
ATOM     35  C   GLU A  10      19.229  95.915  58.076  1.00 49.54           C  
ANISOU   35  C   GLU A  10     9620   4533   4669  -1202   2874   -106       C  
ATOM     36  O   GLU A  10      18.556  96.922  58.325  1.00 49.70           O  
ANISOU   36  O   GLU A  10     9539   4662   4683  -1172   2868   -205       O  
ATOM     37  CB  GLU A  10      18.009  94.264  56.621  1.00 50.24           C  
ANISOU   37  CB  GLU A  10     9758   4550   4782  -1326   2890   -117       C  
ATOM     38  CG  GLU A  10      17.542  93.979  55.199  1.00 50.26           C  
ANISOU   38  CG  GLU A  10     9772   4493   4831  -1317   2867   -157       C  
ATOM     39  CD  GLU A  10      16.663  92.748  55.106  1.00 51.12           C  
ANISOU   39  CD  GLU A  10     9904   4615   4904  -1470   2910   -157       C  
ATOM     40  OE1 GLU A  10      16.869  91.811  55.903  1.00 51.70           O  
ANISOU   40  OE1 GLU A  10    10051   4660   4933  -1568   2955    -79       O  
ATOM     41  OE2 GLU A  10      15.767  92.718  54.236  1.00 52.52           O1+
ANISOU   41  OE2 GLU A  10    10028   4834   5093  -1497   2900   -235       O1+
ATOM     42  N   LYS A  11      20.038  95.357  58.981  1.00 48.77           N  
ANISOU   42  N   LYS A  11     9583   4418   4529  -1239   2899     -8       N  
ATOM     43  CA  LYS A  11      20.332  96.041  60.234  1.00 48.89           C  
ANISOU   43  CA  LYS A  11     9546   4537   4494  -1237   2913    -13       C  
ATOM     44  C   LYS A  11      21.305  97.195  60.046  1.00 48.04           C  
ANISOU   44  C   LYS A  11     9437   4399   4415  -1117   2876    -27       C  
ATOM     45  O   LYS A  11      21.302  98.131  60.852  1.00 48.12           O  
ANISOU   45  O   LYS A  11     9383   4504   4394  -1103   2881    -79       O  
ATOM     46  CB  LYS A  11      20.895  95.058  61.261  1.00 49.41           C  
ANISOU   46  CB  LYS A  11     9674   4604   4496  -1312   2950    103       C  
ATOM     47  CG  LYS A  11      19.849  94.482  62.209  1.00 50.50           C  
ANISOU   47  CG  LYS A  11     9766   4856   4567  -1450   3000     89       C  
ATOM     48  CD  LYS A  11      20.484  93.949  63.484  1.00 51.01           C  
ANISOU   48  CD  LYS A  11     9856   4959   4566  -1496   3018    187       C  
ATOM     49  CE  LYS A  11      19.424  93.586  64.512  1.00 52.11           C  
ANISOU   49  CE  LYS A  11     9930   5235   4636  -1631   3061    158       C  
ATOM     50  NZ  LYS A  11      20.025  93.166  65.808  1.00 52.66           N1+
ANISOU   50  NZ  LYS A  11     9981   5361   4664  -1652   3037    240       N1+
ATOM     51  N   TRP A  12      22.130  97.149  58.997  1.00 47.29           N  
ANISOU   51  N   TRP A  12     9417   4179   4374  -1039   2840     13       N  
ATOM     52  CA  TRP A  12      22.999  98.279  58.689  1.00 46.54           C  
ANISOU   52  CA  TRP A  12     9325   4055   4304   -938   2805     -8       C  
ATOM     53  C   TRP A  12      22.200  99.445  58.122  1.00 46.40           C  
ANISOU   53  C   TRP A  12     9242   4065   4325   -880   2781   -132       C  
ATOM     54  O   TRP A  12      22.454 100.604  58.469  1.00 46.25           O  
ANISOU   54  O   TRP A  12     9194   4081   4297   -831   2773   -185       O  
ATOM     55  CB  TRP A  12      24.096  97.847  57.713  1.00 45.88           C  
ANISOU   55  CB  TRP A  12     9335   3840   4259   -876   2775     70       C  
ATOM     56  CG  TRP A  12      24.828  98.998  57.081  1.00 45.14           C  
ANISOU   56  CG  TRP A  12     9247   3707   4197   -782   2736     35       C  
ATOM     57  CD1 TRP A  12      25.949  99.618  57.553  1.00 44.85           C  
ANISOU   57  CD1 TRP A  12     9222   3689   4130   -750   2729     62       C  
ATOM     58  CD2 TRP A  12      24.486  99.666  55.860  1.00 44.70           C  
ANISOU   58  CD2 TRP A  12     9190   3591   4203   -715   2699    -34       C  
ATOM     59  NE1 TRP A  12      26.325 100.630  56.704  1.00 44.27           N  
ANISOU   59  NE1 TRP A  12     9162   3564   4095   -677   2693     14       N  
ATOM     60  CE2 TRP A  12      25.443 100.680  55.657  1.00 44.16           C  
ANISOU   60  CE2 TRP A  12     9143   3496   4139   -649   2673    -42       C  
ATOM     61  CE3 TRP A  12      23.463  99.506  54.922  1.00 44.78           C  
ANISOU   61  CE3 TRP A  12     9182   3575   4258   -710   2685    -88       C  
ATOM     62  CZ2 TRP A  12      25.407 101.529  54.554  1.00 43.71           C  
ANISOU   62  CZ2 TRP A  12     9101   3376   4132   -576   2635    -97       C  
ATOM     63  CZ3 TRP A  12      23.430 100.349  53.829  1.00 44.32           C  
ANISOU   63  CZ3 TRP A  12     9128   3463   4248   -627   2645   -142       C  
ATOM     64  CH2 TRP A  12      24.394 101.347  53.654  1.00 43.79           C  
ANISOU   64  CH2 TRP A  12     9094   3359   4186   -560   2620   -144       C  
ATOM     65  N   LYS A  13      21.232  99.160  57.247  1.00 46.56           N  
ANISOU   65  N   LYS A  13     9241   4068   4380   -884   2771   -178       N  
ATOM     66  CA  LYS A  13      20.384 100.220  56.712  1.00 46.59           C  
ANISOU   66  CA  LYS A  13     9179   4110   4413   -817   2748   -292       C  
ATOM     67  C   LYS A  13      19.437 100.763  57.772  1.00 47.35           C  
ANISOU   67  C   LYS A  13     9175   4355   4462   -849   2778   -375       C  
ATOM     68  O   LYS A  13      19.063 101.941  57.722  1.00 47.42           O  
ANISOU   68  O   LYS A  13     9138   4401   4479   -770   2764   -465       O  
ATOM     69  CB  LYS A  13      19.589  99.708  55.511  1.00 46.66           C  
ANISOU   69  CB  LYS A  13     9182   4086   4462   -816   2730   -318       C  
ATOM     70  CG  LYS A  13      18.987 100.806  54.648  1.00 46.57           C  
ANISOU   70  CG  LYS A  13     9124   4083   4487   -713   2692   -413       C  
ATOM     71  CD  LYS A  13      20.067 101.544  53.873  1.00 45.71           C  
ANISOU   71  CD  LYS A  13     9092   3854   4422   -612   2652   -389       C  
ATOM     72  CE  LYS A  13      19.465 102.557  52.913  1.00 45.71           C  
ANISOU   72  CE  LYS A  13     9063   3846   4457   -506   2613   -471       C  
ATOM     73  NZ  LYS A  13      20.471 103.089  51.951  1.00 44.92           N1+
ANISOU   73  NZ  LYS A  13     9050   3620   4400   -426   2573   -438       N1+
ATOM     74  N   ALA A  14      19.033  99.924  58.728  1.00 48.01           N  
ANISOU   74  N   ALA A  14     9229   4522   4491   -960   2821   -348       N  
ATOM     75  CA  ALA A  14      18.216 100.402  59.837  1.00 48.78           C  
ANISOU   75  CA  ALA A  14     9228   4773   4533   -999   2853   -424       C  
ATOM     76  C   ALA A  14      18.967 101.447  60.651  1.00 48.57           C  
ANISOU   76  C   ALA A  14     9202   4767   4486   -950   2855   -440       C  
ATOM     77  O   ALA A  14      18.427 102.514  60.964  1.00 48.90           O  
ANISOU   77  O   ALA A  14     9179   4883   4518   -898   2857   -541       O  
ATOM     78  CB  ALA A  14      17.790  99.229  60.720  1.00 49.53           C  
ANISOU   78  CB  ALA A  14     9307   4946   4567  -1141   2900   -375       C  
ATOM     79  N   ARG A  15      20.226 101.163  60.991  1.00 48.11           N  
ANISOU   79  N   ARG A  15     9219   4647   4415   -963   2856   -343       N  
ATOM     80  CA  ARG A  15      21.020 102.125  61.749  1.00 47.96           C  
ANISOU   80  CA  ARG A  15     9202   4655   4367   -932   2860   -358       C  
ATOM     81  C   ARG A  15      21.399 103.329  60.896  1.00 47.40           C  
ANISOU   81  C   ARG A  15     9164   4499   4347   -819   2823   -415       C  
ATOM     82  O   ARG A  15      21.418 104.463  61.389  1.00 47.59           O  
ANISOU   82  O   ARG A  15     9166   4563   4352   -783   2830   -491       O  
ATOM     83  CB  ARG A  15      22.273 101.452  62.309  1.00 47.73           C  
ANISOU   83  CB  ARG A  15     9234   4601   4300   -976   2870   -236       C  
ATOM     84  CG  ARG A  15      22.031 100.621  63.558  1.00 48.47           C  
ANISOU   84  CG  ARG A  15     9295   4802   4319  -1084   2914   -187       C  
ATOM     85  CD  ARG A  15      23.237 100.669  64.484  1.00 48.42           C  
ANISOU   85  CD  ARG A  15     9314   4831   4254  -1101   2925   -113       C  
ATOM     86  NE  ARG A  15      24.121  99.518  64.324  1.00 48.26           N  
ANISOU   86  NE  ARG A  15     9372   4739   4224  -1113   2920     25       N  
ATOM     87  CZ  ARG A  15      25.363  99.463  64.794  1.00 48.11           C  
ANISOU   87  CZ  ARG A  15     9383   4732   4166  -1098   2913    105       C  
ATOM     88  NH1 ARG A  15      26.098  98.376  64.610  1.00 48.09           N1+
ANISOU   88  NH1 ARG A  15     9415   4671   4185  -1077   2868    218       N1+
ATOM     89  NH2 ARG A  15      25.874 100.502  65.441  1.00 48.09           N  
ANISOU   89  NH2 ARG A  15     9338   4807   4126  -1088   2912     58       N  
ATOM     90  N   LEU A  16      21.705 103.102  59.615  1.00 46.78           N  
ANISOU   90  N   LEU A  16     9146   4301   4329   -765   2785   -381       N  
ATOM     91  CA  LEU A  16      22.128 104.194  58.742  1.00 46.28           C  
ANISOU   91  CA  LEU A  16     9127   4148   4309   -664   2749   -424       C  
ATOM     92  C   LEU A  16      21.046 105.261  58.630  1.00 46.77           C  
ANISOU   92  C   LEU A  16     9133   4253   4383   -596   2746   -548       C  
ATOM     93  O   LEU A  16      21.349 106.457  58.544  1.00 46.71           O  
ANISOU   93  O   LEU A  16     9158   4208   4383   -526   2735   -603       O  
ATOM     94  CB  LEU A  16      22.496 103.641  57.363  1.00 45.63           C  
ANISOU   94  CB  LEU A  16     9109   3944   4285   -627   2711   -367       C  
ATOM     95  CG  LEU A  16      23.339 104.481  56.393  1.00 44.98           C  
ANISOU   95  CG  LEU A  16     9099   3750   4241   -543   2672   -368       C  
ATOM     96  CD1 LEU A  16      22.493 105.467  55.591  1.00 45.13           C  
ANISOU   96  CD1 LEU A  16     9104   3743   4300   -452   2646   -463       C  
ATOM     97  CD2 LEU A  16      24.476 105.191  57.120  1.00 44.83           C  
ANISOU   97  CD2 LEU A  16     9115   3738   4182   -552   2682   -353       C  
ATOM     98  N   ASN A  17      19.776 104.850  58.638  1.00 47.36           N  
ANISOU   98  N   ASN A  17     9129   4411   4455   -615   2757   -596       N  
ATOM     99  CA  ASN A  17      18.680 105.809  58.564  1.00 47.98           C  
ANISOU   99  CA  ASN A  17     9142   4553   4536   -537   2754   -715       C  
ATOM    100  C   ASN A  17      18.391 106.462  59.910  1.00 48.68           C  
ANISOU  100  C   ASN A  17     9173   4756   4567   -557   2795   -785       C  
ATOM    101  O   ASN A  17      18.002 107.634  59.951  1.00 49.09           O  
ANISOU  101  O   ASN A  17     9213   4819   4620   -466   2793   -880       O  
ATOM    102  CB  ASN A  17      17.416 105.129  58.035  1.00 48.46           C  
ANISOU  102  CB  ASN A  17     9124   4684   4604   -551   2750   -747       C  
ATOM    103  CG  ASN A  17      17.333 105.145  56.521  1.00 48.03           C  
ANISOU  103  CG  ASN A  17     9108   4532   4610   -472   2703   -740       C  
ATOM    104  OD1 ASN A  17      18.328 105.369  55.834  1.00 47.26           O  
ANISOU  104  OD1 ASN A  17     9104   4303   4551   -429   2674   -688       O  
ATOM    105  ND2 ASN A  17      16.137 104.908  55.993  1.00 48.59           N  
ANISOU  105  ND2 ASN A  17     9099   4681   4682   -458   2695   -796       N  
ATOM    106  N   GLN A  18      18.575 105.731  61.012  1.00 48.90           N  
ANISOU  106  N   GLN A  18     9171   4868   4542   -671   2832   -738       N  
ATOM    107  CA  GLN A  18      18.284 106.268  62.337  1.00 49.62           C  
ANISOU  107  CA  GLN A  18     9200   5083   4570   -703   2873   -804       C  
ATOM    108  C   GLN A  18      19.303 107.299  62.804  1.00 49.40           C  
ANISOU  108  C   GLN A  18     9234   5007   4528   -673   2878   -818       C  
ATOM    109  O   GLN A  18      19.049 107.981  63.803  1.00 50.04           O  
ANISOU  109  O   GLN A  18     9272   5179   4562   -681   2911   -893       O  
ATOM    110  CB  GLN A  18      18.209 105.134  63.359  1.00 49.97           C  
ANISOU  110  CB  GLN A  18     9200   5233   4555   -842   2911   -740       C  
ATOM    111  CG  GLN A  18      17.030 104.197  63.169  1.00 50.52           C  
ANISOU  111  CG  GLN A  18     9195   5383   4615   -900   2921   -749       C  
ATOM    112  CD  GLN A  18      17.223 102.878  63.891  1.00 50.71           C  
ANISOU  112  CD  GLN A  18     9225   5453   4591  -1042   2953   -649       C  
ATOM    113  OE1 GLN A  18      18.144 102.728  64.693  1.00 50.56           O  
ANISOU  113  OE1 GLN A  18     9245   5430   4535  -1088   2969   -581       O  
ATOM    114  NE2 GLN A  18      16.358 101.912  63.604  1.00 51.15           N  
ANISOU  114  NE2 GLN A  18     9245   5550   4639  -1114   2963   -639       N  
ATOM    115  N   MET A  19      20.438 107.427  62.121  1.00 48.59           N  
ANISOU  115  N   MET A  19     9230   4772   4459   -646   2849   -753       N  
ATOM    116  CA  MET A  19      21.454 108.387  62.526  1.00 48.44           C  
ANISOU  116  CA  MET A  19     9273   4714   4419   -635   2856   -767       C  
ATOM    117  C   MET A  19      20.929 109.816  62.410  1.00 48.95           C  
ANISOU  117  C   MET A  19     9350   4755   4495   -537   2857   -893       C  
ATOM    118  O   MET A  19      19.994 110.108  61.660  1.00 49.20           O  
ANISOU  118  O   MET A  19     9362   4764   4566   -446   2838   -951       O  
ATOM    119  CB  MET A  19      22.713 108.233  61.671  1.00 47.54           C  
ANISOU  119  CB  MET A  19     9257   4472   4336   -624   2822   -677       C  
ATOM    120  CG  MET A  19      23.583 107.040  62.026  1.00 47.16           C  
ANISOU  120  CG  MET A  19     9216   4446   4258   -711   2826   -552       C  
ATOM    121  SD  MET A  19      25.079 106.990  61.021  1.00 46.23           S  
ANISOU  121  SD  MET A  19     9202   4196   4169   -684   2787   -463       S  
ATOM    122  CE  MET A  19      25.980 105.658  61.809  1.00 46.15           C  
ANISOU  122  CE  MET A  19     9181   4254   4101   -774   2804   -328       C  
ATOM    123  N   SER A  20      21.547 110.713  63.172  1.00 49.21           N  
ANISOU  123  N   SER A  20     9418   4796   4486   -553   2883   -936       N  
ATOM    124  CA  SER A  20      21.298 112.139  63.043  1.00 49.73           C  
ANISOU  124  CA  SER A  20     9532   4803   4560   -461   2888  -1048       C  
ATOM    125  C   SER A  20      22.244 112.735  62.004  1.00 49.13           C  
ANISOU  125  C   SER A  20     9581   4562   4523   -413   2854  -1017       C  
ATOM    126  O   SER A  20      23.158 112.073  61.506  1.00 48.32           O  
ANISOU  126  O   SER A  20     9516   4409   4433   -458   2830   -915       O  
ATOM    127  CB  SER A  20      21.455 112.847  64.392  1.00 50.46           C  
ANISOU  127  CB  SER A  20     9608   4982   4581   -512   2938  -1121       C  
ATOM    128  OG  SER A  20      22.809 112.885  64.804  1.00 50.06           O  
ANISOU  128  OG  SER A  20     9615   4916   4492   -601   2947  -1063       O  
ATOM    129  N   ALA A  21      22.015 114.011  61.681  1.00 49.62           N  
ANISOU  129  N   ALA A  21     9714   4540   4600   -319   2855  -1108       N  
ATOM    130  CA  ALA A  21      22.792 114.663  60.630  1.00 49.20           C  
ANISOU  130  CA  ALA A  21     9788   4324   4580   -272   2824  -1087       C  
ATOM    131  C   ALA A  21      24.281 114.669  60.952  1.00 48.72           C  
ANISOU  131  C   ALA A  21     9790   4243   4479   -381   2833  -1026       C  
ATOM    132  O   ALA A  21      25.119 114.510  60.056  1.00 48.02           O  
ANISOU  132  O   ALA A  21     9768   4063   4415   -387   2800   -955       O  
ATOM    133  CB  ALA A  21      22.288 116.091  60.412  1.00 50.04           C  
ANISOU  133  CB  ALA A  21     9944   4356   4714   -161   2807  -1179       C  
ATOM    134  N   LEU A  22      24.632 114.843  62.227  1.00 49.15           N  
ANISOU  134  N   LEU A  22     9814   4395   4464   -471   2878  -1055       N  
ATOM    135  CA  LEU A  22      26.040 114.859  62.607  1.00 48.83           C  
ANISOU  135  CA  LEU A  22     9818   4366   4371   -578   2888  -1002       C  
ATOM    136  C   LEU A  22      26.635 113.457  62.629  1.00 48.07           C  
ANISOU  136  C   LEU A  22     9658   4340   4266   -647   2870   -873       C  
ATOM    137  O   LEU A  22      27.763 113.255  62.167  1.00 47.51           O  
ANISOU  137  O   LEU A  22     9635   4230   4186   -684   2850   -799       O  
ATOM    138  CB  LEU A  22      26.211 115.527  63.969  1.00 49.64           C  
ANISOU  138  CB  LEU A  22     9882   4566   4413   -653   2922  -1066       C  
ATOM    139  CG  LEU A  22      27.648 115.567  64.484  1.00 49.48           C  
ANISOU  139  CG  LEU A  22     9878   4591   4331   -774   2926  -1014       C  
ATOM    140  CD1 LEU A  22      28.553 116.304  63.506  1.00 49.22           C  
ANISOU  140  CD1 LEU A  22     9954   4420   4325   -767   2891   -997       C  
ATOM    141  CD2 LEU A  22      27.695 116.207  65.855  1.00 50.37           C  
ANISOU  141  CD2 LEU A  22     9942   4812   4386   -848   2957  -1086       C  
ATOM    142  N   GLU A  23      25.896 112.481  63.166  1.00 48.14           N  
ANISOU  142  N   GLU A  23     9564   4456   4273   -664   2879   -846       N  
ATOM    143  CA  GLU A  23      26.349 111.092  63.135  1.00 47.55           C  
ANISOU  143  CA  GLU A  23     9446   4429   4194   -716   2863   -721       C  
ATOM    144  C   GLU A  23      26.679 110.657  61.715  1.00 46.76           C  
ANISOU  144  C   GLU A  23     9401   4206   4159   -661   2814   -651       C  
ATOM    145  O   GLU A  23      27.705 110.012  61.469  1.00 46.22           O  
ANISOU  145  O   GLU A  23     9354   4130   4079   -697   2798   -554       O  
ATOM    146  CB  GLU A  23      25.279 110.178  63.734  1.00 47.88           C  
ANISOU  146  CB  GLU A  23     9386   4575   4231   -736   2879   -714       C  
ATOM    147  CG  GLU A  23      25.531 109.766  65.171  1.00 48.33           C  
ANISOU  147  CG  GLU A  23     9377   4782   4203   -837   2919   -690       C  
ATOM    148  CD  GLU A  23      24.276 109.251  65.849  1.00 48.92           C  
ANISOU  148  CD  GLU A  23     9357   4965   4266   -857   2945   -724       C  
ATOM    149  OE1 GLU A  23      24.363 108.817  67.017  1.00 49.34           O  
ANISOU  149  OE1 GLU A  23     9352   5147   4249   -943   2977   -699       O  
ATOM    150  OE2 GLU A  23      23.200 109.285  65.216  1.00 49.03           O1+
ANISOU  150  OE2 GLU A  23     9350   4946   4334   -791   2932   -775       O1+
ATOM    151  N   PHE A  24      25.813 111.013  60.763  1.00 46.75           N  
ANISOU  151  N   PHE A  24     9421   4116   4224   -568   2791   -701       N  
ATOM    152  CA  PHE A  24      26.036 110.646  59.369  1.00 46.05           C  
ANISOU  152  CA  PHE A  24     9384   3916   4198   -514   2744   -643       C  
ATOM    153  C   PHE A  24      27.326 111.257  58.837  1.00 45.67           C  
ANISOU  153  C   PHE A  24     9430   3782   4139   -524   2728   -617       C  
ATOM    154  O   PHE A  24      28.102 110.584  58.147  1.00 45.02           O  
ANISOU  154  O   PHE A  24     9372   3663   4071   -534   2701   -529       O  
ATOM    155  CB  PHE A  24      24.842 111.090  58.523  1.00 46.28           C  
ANISOU  155  CB  PHE A  24     9414   3883   4288   -409   2724   -713       C  
ATOM    156  CG  PHE A  24      24.919 110.662  57.086  1.00 45.64           C  
ANISOU  156  CG  PHE A  24     9373   3701   4268   -354   2676   -659       C  
ATOM    157  CD1 PHE A  24      25.528 111.469  56.139  1.00 45.38           C  
ANISOU  157  CD1 PHE A  24     9439   3546   4258   -305   2649   -663       C  
ATOM    158  CD2 PHE A  24      24.371 109.457  56.679  1.00 45.38           C  
ANISOU  158  CD2 PHE A  24     9284   3694   4266   -361   2662   -607       C  
ATOM    159  CE1 PHE A  24      25.598 111.076  54.817  1.00 44.83           C  
ANISOU  159  CE1 PHE A  24     9401   3391   4240   -258   2606   -614       C  
ATOM    160  CE2 PHE A  24      24.437 109.059  55.357  1.00 44.85           C  
ANISOU  160  CE2 PHE A  24     9251   3538   4251   -315   2621   -563       C  
ATOM    161  CZ  PHE A  24      25.050 109.869  54.426  1.00 44.55           C  
ANISOU  161  CZ  PHE A  24     9303   3388   4236   -261   2592   -566       C  
ATOM    162  N   TYR A  25      27.576 112.530  59.153  1.00 46.14           N  
ANISOU  162  N   TYR A  25     9548   3814   4169   -526   2748   -696       N  
ATOM    163  CA  TYR A  25      28.738 113.215  58.597  1.00 45.91           C  
ANISOU  163  CA  TYR A  25     9617   3703   4123   -547   2736   -683       C  
ATOM    164  C   TYR A  25      30.043 112.620  59.111  1.00 45.60           C  
ANISOU  164  C   TYR A  25     9557   3749   4020   -646   2743   -601       C  
ATOM    165  O   TYR A  25      31.032 112.551  58.371  1.00 45.14           O  
ANISOU  165  O   TYR A  25     9548   3645   3959   -659   2719   -545       O  
ATOM    166  CB  TYR A  25      28.675 114.709  58.913  1.00 46.66           C  
ANISOU  166  CB  TYR A  25     9792   3747   4192   -540   2764   -791       C  
ATOM    167  CG  TYR A  25      29.923 115.455  58.505  1.00 46.60           C  
ANISOU  167  CG  TYR A  25     9864   3677   4165   -594   2743   -769       C  
ATOM    168  CD1 TYR A  25      30.357 115.446  57.186  1.00 46.06           C  
ANISOU  168  CD1 TYR A  25     9859   3503   4139   -557   2698   -717       C  
ATOM    169  CD2 TYR A  25      30.669 116.167  59.437  1.00 47.15           C  
ANISOU  169  CD2 TYR A  25     9941   3803   4169   -691   2768   -802       C  
ATOM    170  CE1 TYR A  25      31.499 116.122  56.806  1.00 46.08           C  
ANISOU  170  CE1 TYR A  25     9932   3461   4113   -618   2684   -698       C  
ATOM    171  CE2 TYR A  25      31.813 116.849  59.063  1.00 47.19           C  
ANISOU  171  CE2 TYR A  25    10020   3763   4147   -757   2754   -788       C  
ATOM    172  CZ  TYR A  25      32.222 116.822  57.747  1.00 46.66           C  
ANISOU  172  CZ  TYR A  25    10018   3593   4117   -721   2714   -735       C  
ATOM    173  OH  TYR A  25      33.358 117.498  57.369  1.00 46.77           O  
ANISOU  173  OH  TYR A  25    10104   3572   4096   -797   2705   -723       O  
ATOM    174  N   SER A  26      30.073 112.190  60.374  1.00 45.92           N  
ANISOU  174  N   SER A  26     9520   3925   4003   -713   2777   -591       N  
ATOM    175  CA  SER A  26      31.288 111.580  60.902  1.00 45.75           C  
ANISOU  175  CA  SER A  26     9469   4002   3912   -794   2782   -508       C  
ATOM    176  C   SER A  26      31.527 110.200  60.305  1.00 45.10           C  
ANISOU  176  C   SER A  26     9357   3917   3861   -767   2750   -390       C  
ATOM    177  O   SER A  26      32.681 109.776  60.170  1.00 44.83           O  
ANISOU  177  O   SER A  26     9328   3917   3788   -796   2738   -312       O  
ATOM    178  CB  SER A  26      31.217 111.490  62.427  1.00 46.36           C  
ANISOU  178  CB  SER A  26     9472   4230   3914   -869   2826   -526       C  
ATOM    179  OG  SER A  26      31.044 112.769  63.008  1.00 47.04           O  
ANISOU  179  OG  SER A  26     9582   4318   3974   -896   2852   -639       O  
ATOM    180  N   TYR A  27      30.460 109.495  59.931  1.00 44.94           N  
ANISOU  180  N   TYR A  27     9308   3861   3906   -713   2738   -379       N  
ATOM    181  CA  TYR A  27      30.568 108.104  59.507  1.00 44.49           C  
ANISOU  181  CA  TYR A  27     9229   3801   3875   -698   2718   -273       C  
ATOM    182  C   TYR A  27      30.782 107.946  58.009  1.00 43.86           C  
ANISOU  182  C   TYR A  27     9208   3597   3860   -634   2675   -242       C  
ATOM    183  O   TYR A  27      31.372 106.947  57.581  1.00 43.48           O  
ANISOU  183  O   TYR A  27     9164   3541   3817   -627   2658   -150       O  
ATOM    184  CB  TYR A  27      29.311 107.338  59.930  1.00 44.76           C  
ANISOU  184  CB  TYR A  27     9201   3872   3933   -695   2733   -277       C  
ATOM    185  CG  TYR A  27      29.163 105.968  59.308  1.00 44.40           C  
ANISOU  185  CG  TYR A  27     9154   3789   3928   -676   2714   -186       C  
ATOM    186  CD1 TYR A  27      29.940 104.901  59.738  1.00 44.38           C  
ANISOU  186  CD1 TYR A  27     9144   3837   3882   -709   2721    -79       C  
ATOM    187  CD2 TYR A  27      28.236 105.737  58.298  1.00 44.20           C  
ANISOU  187  CD2 TYR A  27     9138   3678   3976   -624   2692   -210       C  
ATOM    188  CE1 TYR A  27      29.807 103.646  59.174  1.00 44.18           C  
ANISOU  188  CE1 TYR A  27     9134   3761   3891   -691   2709      1       C  
ATOM    189  CE2 TYR A  27      28.094 104.484  57.730  1.00 43.96           C  
ANISOU  189  CE2 TYR A  27     9115   3610   3979   -618   2680   -135       C  
ATOM    190  CZ  TYR A  27      28.882 103.442  58.174  1.00 43.96           C  
ANISOU  190  CZ  TYR A  27     9121   3644   3939   -653   2690    -30       C  
ATOM    191  OH  TYR A  27      28.751 102.191  57.617  1.00 43.85           O  
ANISOU  191  OH  TYR A  27     9130   3575   3954   -646   2684     43       O  
ATOM    192  N   LYS A  28      30.328 108.914  57.207  1.00 43.82           N  
ANISOU  192  N   LYS A  28     9253   3495   3902   -583   2658   -317       N  
ATOM    193  CA  LYS A  28      30.330 108.749  55.755  1.00 43.28           C  
ANISOU  193  CA  LYS A  28     9235   3313   3899   -520   2617   -294       C  
ATOM    194  C   LYS A  28      31.732 108.489  55.216  1.00 42.84           C  
ANISOU  194  C   LYS A  28     9217   3243   3817   -537   2597   -218       C  
ATOM    195  O   LYS A  28      31.907 107.695  54.284  1.00 42.37           O  
ANISOU  195  O   LYS A  28     9170   3132   3796   -502   2570   -158       O  
ATOM    196  CB  LYS A  28      29.719 109.982  55.085  1.00 43.47           C  
ANISOU  196  CB  LYS A  28     9314   3242   3960   -461   2604   -385       C  
ATOM    197  CG  LYS A  28      30.381 111.293  55.473  1.00 43.84           C  
ANISOU  197  CG  LYS A  28     9422   3278   3957   -495   2622   -442       C  
ATOM    198  CD  LYS A  28      30.256 112.335  54.374  1.00 43.87           C  
ANISOU  198  CD  LYS A  28     9520   3150   3997   -434   2598   -491       C  
ATOM    199  CE  LYS A  28      28.859 112.925  54.308  1.00 44.38           C  
ANISOU  199  CE  LYS A  28     9583   3174   4104   -350   2600   -575       C  
ATOM    200  NZ  LYS A  28      28.746 113.953  53.235  1.00 44.52           N1+
ANISOU  200  NZ  LYS A  28     9657   3091   4169   -283   2547   -585       N1+
ATOM    201  N   LYS A  29      32.745 109.135  55.791  1.00 43.05           N  
ANISOU  201  N   LYS A  29     9258   3325   3772   -595   2614   -225       N  
ATOM    202  CA  LYS A  29      34.117 108.993  55.327  1.00 42.75           C  
ANISOU  202  CA  LYS A  29     9247   3302   3696   -617   2597   -164       C  
ATOM    203  C   LYS A  29      35.018 108.267  56.315  1.00 42.94           C  
ANISOU  203  C   LYS A  29     9209   3464   3642   -669   2613    -93       C  
ATOM    204  O   LYS A  29      36.217 108.144  56.056  1.00 42.83           O  
ANISOU  204  O   LYS A  29     9167   3494   3611   -678   2570    -51       O  
ATOM    205  CB  LYS A  29      34.720 110.367  55.012  1.00 42.94           C  
ANISOU  205  CB  LYS A  29     9343   3284   3688   -651   2597   -227       C  
ATOM    206  CG  LYS A  29      34.217 111.001  53.726  1.00 42.72           C  
ANISOU  206  CG  LYS A  29     9393   3110   3730   -589   2568   -267       C  
ATOM    207  CD  LYS A  29      35.286 111.895  53.112  1.00 42.76           C  
ANISOU  207  CD  LYS A  29     9477   3078   3694   -631   2559   -279       C  
ATOM    208  CE  LYS A  29      34.793 112.578  51.847  1.00 42.65           C  
ANISOU  208  CE  LYS A  29     9550   2914   3741   -569   2530   -314       C  
ATOM    209  NZ  LYS A  29      35.892 113.280  51.128  1.00 42.67           N1+
ANISOU  209  NZ  LYS A  29     9632   2881   3701   -618   2519   -310       N1+
ATOM    210  N   SER A  30      34.482 107.777  57.430  1.00 43.29           N  
ANISOU  210  N   SER A  30     9189   3590   3669   -690   2637    -86       N  
ATOM    211  CA  SER A  30      35.321 107.198  58.473  1.00 43.61           C  
ANISOU  211  CA  SER A  30     9130   3775   3664   -727   2614    -28       C  
ATOM    212  C   SER A  30      36.096 105.983  57.976  1.00 43.32           C  
ANISOU  212  C   SER A  30     9060   3753   3646   -676   2567     75       C  
ATOM    213  O   SER A  30      35.521 104.910  57.772  1.00 43.18           O  
ANISOU  213  O   SER A  30     9045   3694   3669   -633   2567    126       O  
ATOM    214  CB  SER A  30      34.471 106.818  59.687  1.00 44.07           C  
ANISOU  214  CB  SER A  30     9133   3908   3701   -756   2649    -34       C  
ATOM    215  OG  SER A  30      35.284 106.411  60.773  1.00 44.49           O  
ANISOU  215  OG  SER A  30     9094   4112   3698   -793   2629     16       O  
ATOM    216  N   GLY A  31      37.400 106.150  57.771  1.00 43.32           N  
ANISOU  216  N   GLY A  31     9031   3815   3612   -681   2528    100       N  
ATOM    217  CA  GLY A  31      38.263 105.025  57.467  1.00 43.23           C  
ANISOU  217  CA  GLY A  31     8977   3848   3600   -626   2487    194       C  
ATOM    218  C   GLY A  31      38.205 104.523  56.047  1.00 42.66           C  
ANISOU  218  C   GLY A  31     8965   3650   3594   -555   2466    218       C  
ATOM    219  O   GLY A  31      38.549 103.361  55.797  1.00 42.63           O  
ANISOU  219  O   GLY A  31     8941   3653   3605   -494   2443    295       O  
ATOM    220  N   ILE A  32      37.772 105.356  55.110  1.00 42.29           N  
ANISOU  220  N   ILE A  32     8996   3488   3583   -559   2474    155       N  
ATOM    221  CA  ILE A  32      37.667 104.966  53.720  1.00 41.77           C  
ANISOU  221  CA  ILE A  32     8985   3308   3578   -497   2451    171       C  
ATOM    222  C   ILE A  32      38.928 105.401  52.980  1.00 41.64           C  
ANISOU  222  C   ILE A  32     8967   3320   3536   -498   2414    174       C  
ATOM    223  O   ILE A  32      39.733 106.183  53.480  1.00 41.96           O  
ANISOU  223  O   ILE A  32     8976   3452   3513   -557   2411    150       O  
ATOM    224  CB  ILE A  32      36.401 105.552  53.050  1.00 41.51           C  
ANISOU  224  CB  ILE A  32     9037   3137   3596   -491   2481    110       C  
ATOM    225  CG1 ILE A  32      36.564 107.055  52.799  1.00 41.56           C  
ANISOU  225  CG1 ILE A  32     9106   3111   3575   -534   2494     37       C  
ATOM    226  CG2 ILE A  32      35.167 105.280  53.892  1.00 41.77           C  
ANISOU  226  CG2 ILE A  32     9063   3170   3637   -507   2526     97       C  
ATOM    227  CD1 ILE A  32      35.424 107.674  51.996  1.00 41.39           C  
ANISOU  227  CD1 ILE A  32     9159   2955   3613   -502   2502    -22       C  
ATOM    228  N   THR A  33      39.102 104.890  51.765  1.00 41.24           N  
ANISOU  228  N   THR A  33     8944   3196   3529   -438   2386    198       N  
ATOM    229  CA  THR A  33      40.184 105.305  50.884  1.00 41.11           C  
ANISOU  229  CA  THR A  33     8932   3196   3490   -439   2354    196       C  
ATOM    230  C   THR A  33      39.654 106.290  49.851  1.00 40.79           C  
ANISOU  230  C   THR A  33     8983   3030   3485   -451   2356    132       C  
ATOM    231  O   THR A  33      38.528 106.151  49.367  1.00 40.52           O  
ANISOU  231  O   THR A  33     8998   2886   3513   -415   2366    114       O  
ATOM    232  CB  THR A  33      40.818 104.104  50.182  1.00 40.96           C  
ANISOU  232  CB  THR A  33     8886   3190   3488   -361   2322    264       C  
ATOM    233  OG1 THR A  33      40.260 102.895  50.708  1.00 41.08           O  
ANISOU  233  OG1 THR A  33     8880   3199   3531   -312   2333    315       O  
ATOM    234  CG2 THR A  33      42.322 104.094  50.407  1.00 41.32           C  
ANISOU  234  CG2 THR A  33     8862   3383   3454   -372   2300    301       C  
ATOM    235  N   GLU A  34      40.474 107.284  49.516  1.00 41.76           N  
ANISOU  235  N   GLU A  34     9126   3176   3564   -505   2344     99       N  
ATOM    236  CA  GLU A  34      40.027 108.387  48.679  1.00 41.64           C  
ANISOU  236  CA  GLU A  34     9210   3043   3567   -525   2349     38       C  
ATOM    237  C   GLU A  34      41.178 108.853  47.798  1.00 41.64           C  
ANISOU  237  C   GLU A  34     9219   3070   3534   -555   2315     34       C  
ATOM    238  O   GLU A  34      42.327 108.903  48.242  1.00 41.97           O  
ANISOU  238  O   GLU A  34     9193   3242   3513   -605   2302     50       O  
ATOM    239  CB  GLU A  34      39.507 109.544  49.541  1.00 42.06           C  
ANISOU  239  CB  GLU A  34     9315   3076   3588   -593   2394    -25       C  
ATOM    240  CG  GLU A  34      38.647 110.555  48.809  1.00 42.28           C  
ANISOU  240  CG  GLU A  34     9468   2953   3643   -586   2414    -80       C  
ATOM    241  CD  GLU A  34      37.668 111.249  49.736  1.00 42.88           C  
ANISOU  241  CD  GLU A  34     9583   2996   3713   -605   2464   -136       C  
ATOM    242  OE1 GLU A  34      36.650 110.620  50.098  1.00 42.94           O  
ANISOU  242  OE1 GLU A  34     9546   2994   3775   -551   2467   -133       O  
ATOM    243  OE2 GLU A  34      37.923 112.414  50.113  1.00 43.30           O1+
ANISOU  243  OE2 GLU A  34     9691   3044   3718   -671   2485   -196       O1+
ATOM    244  N   VAL A  35      40.860 109.190  46.551  1.00 43.64           N  
ANISOU  244  N   VAL A  35     9542   3214   3824   -526   2298     12       N  
ATOM    245  CA  VAL A  35      41.853 109.682  45.608  1.00 43.67           C  
ANISOU  245  CA  VAL A  35     9564   3233   3796   -561   2267      5       C  
ATOM    246  C   VAL A  35      41.950 111.198  45.724  1.00 44.13           C  
ANISOU  246  C   VAL A  35     9710   3249   3810   -653   2286    -59       C  
ATOM    247  O   VAL A  35      41.082 111.865  46.294  1.00 44.35           O  
ANISOU  247  O   VAL A  35     9803   3206   3842   -666   2324   -101       O  
ATOM    248  CB  VAL A  35      41.525 109.253  44.163  1.00 43.20           C  
ANISOU  248  CB  VAL A  35     9523   3098   3791   -484   2232     12       C  
ATOM    249  CG1 VAL A  35      42.510 108.196  43.692  1.00 43.04           C  
ANISOU  249  CG1 VAL A  35     9431   3159   3763   -450   2203     70       C  
ATOM    250  CG2 VAL A  35      40.098 108.733  44.073  1.00 42.88           C  
ANISOU  250  CG2 VAL A  35     9478   2991   3824   -403   2234      6       C  
ATOM    251  N   CYS A  36      43.030 111.750  45.174  1.00 45.95           N  
ANISOU  251  N   CYS A  36     9946   3522   3990   -720   2263    -68       N  
ATOM    252  CA  CYS A  36      43.299 113.185  45.222  1.00 46.71           C  
ANISOU  252  CA  CYS A  36    10134   3579   4035   -824   2280   -129       C  
ATOM    253  C   CYS A  36      42.798 113.803  43.921  1.00 46.77           C  
ANISOU  253  C   CYS A  36    10251   3454   4065   -790   2266   -159       C  
ATOM    254  O   CYS A  36      43.439 113.682  42.874  1.00 46.55           O  
ANISOU  254  O   CYS A  36    10213   3444   4031   -790   2228   -144       O  
ATOM    255  CB  CYS A  36      44.785 113.448  45.439  1.00 47.11           C  
ANISOU  255  CB  CYS A  36    10111   3780   4008   -930   2260   -126       C  
ATOM    256  SG  CYS A  36      45.454 112.712  46.952  1.00 47.57           S  
ANISOU  256  SG  CYS A  36    10007   4050   4020   -952   2263    -92       S  
ATOM    257  N   ARG A  37      41.651 114.472  43.995  1.00 44.82           N  
ANISOU  257  N   ARG A  37    10082   3119   3830   -751   2291   -197       N  
ATOM    258  CA  ARG A  37      41.005 115.069  42.836  1.00 44.81           C  
ANISOU  258  CA  ARG A  37    10099   3080   3846   -691   2251   -192       C  
ATOM    259  C   ARG A  37      41.266 116.563  42.712  1.00 45.59           C  
ANISOU  259  C   ARG A  37    10300   3143   3880   -772   2263   -227       C  
ATOM    260  O   ARG A  37      40.713 117.201  41.811  1.00 45.75           O  
ANISOU  260  O   ARG A  37    10329   3129   3926   -721   2218   -214       O  
ATOM    261  CB  ARG A  37      39.496 114.811  42.893  1.00 44.57           C  
ANISOU  261  CB  ARG A  37    10004   3027   3903   -577   2228   -171       C  
ATOM    262  CG  ARG A  37      39.121 113.338  42.889  1.00 43.89           C  
ANISOU  262  CG  ARG A  37     9824   2972   3879   -501   2215   -136       C  
ATOM    263  CD  ARG A  37      39.422 112.717  41.541  1.00 43.43           C  
ANISOU  263  CD  ARG A  37     9720   2935   3846   -454   2162   -106       C  
ATOM    264  NE  ARG A  37      38.573 113.278  40.495  1.00 43.47           N  
ANISOU  264  NE  ARG A  37     9711   2912   3892   -394   2107   -102       N  
ATOM    265  CZ  ARG A  37      38.897 113.311  39.207  1.00 43.32           C  
ANISOU  265  CZ  ARG A  37     9689   2899   3874   -380   2062    -88       C  
ATOM    266  NH1 ARG A  37      40.063 112.825  38.802  1.00 43.13           N1+
ANISOU  266  NH1 ARG A  37     9672   2905   3811   -420   2065    -80       N1+
ATOM    267  NH2 ARG A  37      38.060 113.841  38.327  1.00 43.45           N  
ANISOU  267  NH2 ARG A  37     9695   2886   3927   -323   2015    -83       N  
ATOM    268  N   GLU A  38      42.095 117.133  43.586  1.00 46.42           N  
ANISOU  268  N   GLU A  38    10481   3252   3905   -901   2317   -276       N  
ATOM    269  CA  GLU A  38      42.328 118.573  43.609  1.00 47.07           C  
ANISOU  269  CA  GLU A  38    10671   3300   3913   -994   2340   -308       C  
ATOM    270  C   GLU A  38      42.968 119.052  42.314  1.00 47.15           C  
ANISOU  270  C   GLU A  38    10722   3304   3888  -1024   2300   -308       C  
ATOM    271  O   GLU A  38      42.356 119.809  41.552  1.00 47.45           O  
ANISOU  271  O   GLU A  38    10786   3296   3948   -971   2264   -285       O  
ATOM    272  CB  GLU A  38      43.213 118.952  44.798  1.00 48.34           C  
ANISOU  272  CB  GLU A  38    10854   3474   4040  -1145   2375   -366       C  
ATOM    273  CG  GLU A  38      42.843 118.259  46.096  1.00 48.38           C  
ANISOU  273  CG  GLU A  38    10809   3485   4089  -1136   2409   -367       C  
ATOM    274  CD  GLU A  38      41.357 118.315  46.388  1.00 48.41           C  
ANISOU  274  CD  GLU A  38    10811   3466   4117  -1021   2438   -332       C  
ATOM    275  OE1 GLU A  38      40.787 117.270  46.769  1.00 47.93           O  
ANISOU  275  OE1 GLU A  38    10680   3422   4109   -940   2441   -311       O  
ATOM    276  OE2 GLU A  38      40.759 119.401  46.230  1.00 48.34           O1+
ANISOU  276  OE2 GLU A  38    10848   3405   4116  -1004   2428   -341       O1+
ATOM    277  N   GLU A  39      44.198 118.611  42.056  1.00 52.12           N  
ANISOU  277  N   GLU A  39    11339   3967   4497  -1107   2284   -335       N  
ATOM    278  CA  GLU A  39      44.930 119.028  40.866  1.00 52.68           C  
ANISOU  278  CA  GLU A  39    11446   4037   4532  -1157   2247   -338       C  
ATOM    279  C   GLU A  39      44.354 118.460  39.574  1.00 52.03           C  
ANISOU  279  C   GLU A  39    11307   3958   4505  -1023   2193   -279       C  
ATOM    280  O   GLU A  39      44.887 118.762  38.500  1.00 52.78           O  
ANISOU  280  O   GLU A  39    11432   4052   4572  -1055   2161   -278       O  
ATOM    281  CB  GLU A  39      46.404 118.642  41.009  1.00 53.18           C  
ANISOU  281  CB  GLU A  39    11425   4190   4592  -1286   2222   -325       C  
ATOM    282  CG  GLU A  39      47.182 119.570  41.934  1.00 54.34           C  
ANISOU  282  CG  GLU A  39    11599   4376   4672  -1460   2251   -368       C  
ATOM    283  CD  GLU A  39      48.473 118.955  42.429  1.00 54.64           C  
ANISOU  283  CD  GLU A  39    11449   4639   4671  -1540   2226   -331       C  
ATOM    284  OE1 GLU A  39      48.482 118.429  43.564  1.00 54.65           O  
ANISOU  284  OE1 GLU A  39    11341   4748   4674  -1525   2238   -317       O  
ATOM    285  OE2 GLU A  39      49.474 118.991  41.681  1.00 54.90           O1+
ANISOU  285  OE2 GLU A  39    11436   4762   4662  -1608   2193   -320       O1+
ATOM    286  N   ALA A  40      43.294 117.655  39.644  1.00 47.04           N  
ANISOU  286  N   ALA A  40    10589   3328   3956   -886   2177   -235       N  
ATOM    287  CA  ALA A  40      42.545 117.225  38.469  1.00 46.53           C  
ANISOU  287  CA  ALA A  40    10460   3257   3963   -764   2116   -189       C  
ATOM    288  C   ALA A  40      41.310 118.079  38.213  1.00 46.88           C  
ANISOU  288  C   ALA A  40    10518   3244   4050   -687   2089   -176       C  
ATOM    289  O   ALA A  40      41.010 118.394  37.057  1.00 46.95           O  
ANISOU  289  O   ALA A  40    10532   3230   4078   -640   2039   -157       O  
ATOM    290  CB  ALA A  40      42.127 115.760  38.612  1.00 45.67           C  
ANISOU  290  CB  ALA A  40    10238   3185   3931   -670   2104   -156       C  
ATOM    291  N   ARG A  41      40.592 118.470  39.271  1.00 45.58           N  
ANISOU  291  N   ARG A  41    10363   3052   3905   -672   2118   -189       N  
ATOM    292  CA  ARG A  41      39.413 119.313  39.098  1.00 46.07           C  
ANISOU  292  CA  ARG A  41    10439   3051   4013   -591   2090   -185       C  
ATOM    293  C   ARG A  41      39.773 120.678  38.531  1.00 47.00           C  
ANISOU  293  C   ARG A  41    10674   3116   4069   -646   2084   -198       C  
ATOM    294  O   ARG A  41      38.985 121.262  37.778  1.00 47.37           O  
ANISOU  294  O   ARG A  41    10736   3110   4151   -564   2041   -183       O  
ATOM    295  CB  ARG A  41      38.680 119.489  40.428  1.00 46.32           C  
ANISOU  295  CB  ARG A  41    10464   3064   4071   -575   2128   -207       C  
ATOM    296  CG  ARG A  41      37.881 118.286  40.896  1.00 45.57           C  
ANISOU  296  CG  ARG A  41    10258   3003   4055   -492   2123   -192       C  
ATOM    297  CD  ARG A  41      37.209 118.595  42.223  1.00 45.96           C  
ANISOU  297  CD  ARG A  41    10314   3029   4120   -489   2165   -222       C  
ATOM    298  NE  ARG A  41      36.896 117.394  42.989  1.00 45.33           N  
ANISOU  298  NE  ARG A  41    10153   2992   4080   -465   2187   -216       N  
ATOM    299  CZ  ARG A  41      36.731 117.381  44.307  1.00 45.54           C  
ANISOU  299  CZ  ARG A  41    10186   3019   4098   -500   2240   -244       C  
ATOM    300  NH1 ARG A  41      36.857 118.506  44.997  1.00 46.35           N1+
ANISOU  300  NH1 ARG A  41    10367   3086   4158   -561   2275   -282       N1+
ATOM    301  NH2 ARG A  41      36.449 116.249  44.939  1.00 45.02           N  
ANISOU  301  NH2 ARG A  41    10054   2988   4064   -479   2261   -234       N  
ATOM    302  N   ARG A  42      40.945 121.208  38.888  1.00 47.61           N  
ANISOU  302  N   ARG A  42    10840   3202   4047   -788   2131   -227       N  
ATOM    303  CA  ARG A  42      41.347 122.518  38.384  1.00 48.63           C  
ANISOU  303  CA  ARG A  42    11094   3277   4106   -858   2133   -242       C  
ATOM    304  C   ARG A  42      41.610 122.471  36.885  1.00 48.50           C  
ANISOU  304  C   ARG A  42    11081   3260   4085   -835   2079   -217       C  
ATOM    305  O   ARG A  42      41.093 123.301  36.128  1.00 49.11           O  
ANISOU  305  O   ARG A  42    11215   3275   4170   -785   2046   -203       O  
ATOM    306  CB  ARG A  42      42.584 123.018  39.130  1.00 49.24           C  
ANISOU  306  CB  ARG A  42    11265   3376   4068  -1038   2201   -288       C  
ATOM    307  CG  ARG A  42      42.326 123.433  40.566  1.00 49.72           C  
ANISOU  307  CG  ARG A  42    11354   3420   4116  -1081   2259   -317       C  
ATOM    308  CD  ARG A  42      43.117 124.684  40.909  1.00 50.96           C  
ANISOU  308  CD  ARG A  42    11653   3548   4160  -1241   2312   -358       C  
ATOM    309  NE  ARG A  42      43.019 125.026  42.325  1.00 51.50           N  
ANISOU  309  NE  ARG A  42    11748   3610   4210  -1307   2375   -390       N  
ATOM    310  CZ  ARG A  42      43.343 126.211  42.832  1.00 52.74           C  
ANISOU  310  CZ  ARG A  42    12023   3725   4292  -1423   2424   -425       C  
ATOM    311  NH1 ARG A  42      43.778 127.180  42.037  1.00 53.62           N1+
ANISOU  311  NH1 ARG A  42    12247   3793   4335  -1484   2417   -431       N1+
ATOM    312  NH2 ARG A  42      43.224 126.432  44.133  1.00 53.08           N  
ANISOU  312  NH2 ARG A  42    12074   3766   4328  -1481   2479   -454       N  
ATOM    313  N   ALA A  43      42.420 121.506  36.438  1.00 47.78           N  
ANISOU  313  N   ALA A  43    10937   3237   3982   -870   2071   -213       N  
ATOM    314  CA  ALA A  43      42.683 121.363  35.010  1.00 47.47           C  
ANISOU  314  CA  ALA A  43    10892   3202   3942   -851   2021   -192       C  
ATOM    315  C   ALA A  43      41.392 121.138  34.235  1.00 47.02           C  
ANISOU  315  C   ALA A  43    10768   3115   3982   -693   1961   -150       C  
ATOM    316  O   ALA A  43      41.227 121.652  33.122  1.00 47.43           O  
ANISOU  316  O   ALA A  43    10861   3131   4029   -666   1921   -133       O  
ATOM    317  CB  ALA A  43      43.664 120.217  34.769  1.00 46.61           C  
ANISOU  317  CB  ALA A  43    10721   3168   3822   -896   2022   -196       C  
ATOM    318  N   LEU A  44      40.458 120.379  34.813  1.00 46.11           N  
ANISOU  318  N   LEU A  44    10555   3016   3951   -595   1956   -137       N  
ATOM    319  CA  LEU A  44      39.160 120.183  34.182  1.00 45.92           C  
ANISOU  319  CA  LEU A  44    10468   2966   4013   -457   1903   -109       C  
ATOM    320  C   LEU A  44      38.281 121.424  34.266  1.00 46.89           C  
ANISOU  320  C   LEU A  44    10667   3006   4142   -405   1895   -113       C  
ATOM    321  O   LEU A  44      37.375 121.582  33.440  1.00 47.05           O  
ANISOU  321  O   LEU A  44    10675   2991   4209   -304   1847    -92       O  
ATOM    322  CB  LEU A  44      38.450 118.985  34.810  1.00 45.09           C  
ANISOU  322  CB  LEU A  44    10242   2903   3987   -384   1904   -101       C  
ATOM    323  CG  LEU A  44      38.945 117.619  34.328  1.00 44.17           C  
ANISOU  323  CG  LEU A  44    10038   2853   3890   -382   1892    -83       C  
ATOM    324  CD1 LEU A  44      38.478 116.511  35.259  1.00 43.54           C  
ANISOU  324  CD1 LEU A  44     9867   2811   3866   -342   1913    -81       C  
ATOM    325  CD2 LEU A  44      38.489 117.359  32.898  1.00 43.97           C  
ANISOU  325  CD2 LEU A  44     9979   2824   3903   -312   1834    -57       C  
ATOM    326  N   LYS A  45      38.523 122.305  35.241  1.00 48.55           N  
ANISOU  326  N   LYS A  45    10962   3181   4305   -471   1942   -142       N  
ATOM    327  CA  LYS A  45      37.816 123.579  35.282  1.00 49.43           C  
ANISOU  327  CA  LYS A  45    11167   3202   4413   -425   1938   -148       C  
ATOM    328  C   LYS A  45      38.378 124.586  34.291  1.00 50.47           C  
ANISOU  328  C   LYS A  45    11421   3281   4474   -475   1924   -142       C  
ATOM    329  O   LYS A  45      37.650 125.493  33.873  1.00 51.21           O  
ANISOU  329  O   LYS A  45    11586   3295   4578   -401   1902   -133       O  
ATOM    330  CB  LYS A  45      37.858 124.182  36.688  1.00 49.93           C  
ANISOU  330  CB  LYS A  45    11283   3240   4450   -481   1997   -185       C  
ATOM    331  CG  LYS A  45      36.695 125.128  36.969  1.00 51.11           C  
ANISOU  331  CG  LYS A  45    11484   3301   4636   -380   1990   -194       C  
ATOM    332  CD  LYS A  45      37.094 126.335  37.806  1.00 52.67           C  
ANISOU  332  CD  LYS A  45    11811   3436   4764   -468   2044   -229       C  
ATOM    333  CE  LYS A  45      37.261 125.983  39.275  1.00 52.63           C  
ANISOU  333  CE  LYS A  45    11768   3470   4758   -530   2101   -263       C  
ATOM    334  NZ  LYS A  45      37.474 127.210  40.094  1.00 53.64           N1+
ANISOU  334  NZ  LYS A  45    12023   3530   4827   -605   2154   -302       N1+
ATOM    335  N   ASP A  46      39.646 124.442  33.901  1.00 50.61           N  
ANISOU  335  N   ASP A  46    11469   3341   4419   -598   1939   -148       N  
ATOM    336  CA  ASP A  46      40.264 125.339  32.933  1.00 51.46           C  
ANISOU  336  CA  ASP A  46    11695   3404   4451   -663   1928   -145       C  
ATOM    337  C   ASP A  46      40.031 124.900  31.495  1.00 51.05           C  
ANISOU  337  C   ASP A  46    11602   3362   4433   -591   1866   -110       C  
ATOM    338  O   ASP A  46      40.082 125.735  30.584  1.00 51.89           O  
ANISOU  338  O   ASP A  46    11806   3409   4500   -595   1844    -97       O  
ATOM    339  CB  ASP A  46      41.772 125.439  33.185  1.00 51.62           C  
ANISOU  339  CB  ASP A  46    11777   3469   4366   -844   1975   -179       C  
ATOM    340  CG  ASP A  46      42.102 126.121  34.497  1.00 52.44           C  
ANISOU  340  CG  ASP A  46    11958   3555   4413   -942   2042   -219       C  
ATOM    341  OD1 ASP A  46      41.228 126.160  35.386  1.00 52.66           O  
ANISOU  341  OD1 ASP A  46    11953   3557   4498   -866   2055   -220       O  
ATOM    342  OD2 ASP A  46      43.242 126.615  34.642  1.00 53.23           O1+
ANISOU  342  OD2 ASP A  46    12150   3668   4407  -1103   2084   -253       O1+
ATOM    343  N   GLY A  47      39.782 123.611  31.270  1.00 48.21           N  
ANISOU  343  N   GLY A  47    11105   3071   4142   -529   1840    -93       N  
ATOM    344  CA  GLY A  47      39.632 123.061  29.937  1.00 47.76           C  
ANISOU  344  CA  GLY A  47    11000   3033   4115   -474   1787    -63       C  
ATOM    345  C   GLY A  47      40.784 122.192  29.483  1.00 47.05           C  
ANISOU  345  C   GLY A  47    10868   3018   3991   -561   1790    -67       C  
ATOM    346  O   GLY A  47      40.744 121.680  28.357  1.00 46.68           O  
ANISOU  346  O   GLY A  47    10781   2989   3965   -524   1749    -44       O  
ATOM    347  N   VAL A  48      41.806 122.005  30.319  1.00 45.48           N  
ANISOU  347  N   VAL A  48    10679   2862   3739   -674   1839    -98       N  
ATOM    348  CA  VAL A  48      42.986 121.223  29.968  1.00 44.96           C  
ANISOU  348  CA  VAL A  48    10584   2865   3635   -761   1846   -110       C  
ATOM    349  C   VAL A  48      42.592 119.776  29.701  1.00 43.83           C  
ANISOU  349  C   VAL A  48    10302   2776   3575   -666   1821    -85       C  
ATOM    350  O   VAL A  48      42.487 118.967  30.630  1.00 43.24           O  
ANISOU  350  O   VAL A  48    10152   2738   3537   -644   1845    -90       O  
ATOM    351  CB  VAL A  48      44.051 121.305  31.078  1.00 45.15           C  
ANISOU  351  CB  VAL A  48    10646   2922   3587   -895   1906   -154       C  
ATOM    352  CG1 VAL A  48      45.343 120.627  30.635  1.00 44.85           C  
ANISOU  352  CG1 VAL A  48    10588   2945   3506   -993   1909   -172       C  
ATOM    353  CG2 VAL A  48      44.306 122.753  31.470  1.00 46.37           C  
ANISOU  353  CG2 VAL A  48    10941   3018   3658   -991   1939   -183       C  
ATOM    354  N   ALA A  49      42.373 119.441  28.431  1.00 43.61           N  
ANISOU  354  N   ALA A  49    10246   2749   3573   -614   1774    -59       N  
ATOM    355  CA  ALA A  49      42.056 118.076  28.033  1.00 42.65           C  
ANISOU  355  CA  ALA A  49    10007   2677   3523   -536   1752    -38       C  
ATOM    356  C   ALA A  49      43.293 117.247  27.715  1.00 42.26           C  
ANISOU  356  C   ALA A  49     9935   2683   3438   -609   1765    -47       C  
ATOM    357  O   ALA A  49      43.170 116.038  27.489  1.00 41.53           O  
ANISOU  357  O   ALA A  49     9752   2629   3398   -550   1756    -31       O  
ATOM    358  CB  ALA A  49      41.123 118.081  26.817  1.00 42.66           C  
ANISOU  358  CB  ALA A  49     9989   2650   3571   -442   1697     -8       C  
ATOM    359  N   THR A  50      44.475 117.863  27.691  1.00 42.81           N  
ANISOU  359  N   THR A  50    10090   2756   3421   -737   1787    -73       N  
ATOM    360  CA  THR A  50      45.724 117.170  27.409  1.00 42.61           C  
ANISOU  360  CA  THR A  50    10046   2783   3361   -817   1798    -84       C  
ATOM    361  C   THR A  50      46.533 116.891  28.670  1.00 42.59           C  
ANISOU  361  C   THR A  50    10029   2818   3335   -893   1845   -109       C  
ATOM    362  O   THR A  50      47.741 116.649  28.584  1.00 42.75           O  
ANISOU  362  O   THR A  50    10041   2888   3316   -992   1853   -116       O  
ATOM    363  CB  THR A  50      46.567 117.980  26.422  1.00 43.34           C  
ANISOU  363  CB  THR A  50    10225   2865   3376   -926   1783    -96       C  
ATOM    364  OG1 THR A  50      46.969 119.211  27.037  1.00 44.23           O  
ANISOU  364  OG1 THR A  50    10442   2948   3417  -1037   1809   -130       O  
ATOM    365  CG2 THR A  50      45.768 118.287  25.166  1.00 43.45           C  
ANISOU  365  CG2 THR A  50    10258   2838   3412   -851   1736    -66       C  
ATOM    366  N   GLY A  51      45.895 116.918  29.835  1.00 42.46           N  
ANISOU  366  N   GLY A  51     9998   2789   3346   -851   1871   -116       N  
ATOM    367  CA  GLY A  51      46.602 116.766  31.087  1.00 42.55           C  
ANISOU  367  CA  GLY A  51    10002   2831   3334   -928   1914   -140       C  
ATOM    368  C   GLY A  51      46.750 115.354  31.604  1.00 41.83           C  
ANISOU  368  C   GLY A  51     9802   2793   3297   -868   1925   -113       C  
ATOM    369  O   GLY A  51      47.409 115.152  32.630  1.00 41.95           O  
ANISOU  369  O   GLY A  51     9787   2855   3296   -930   1953   -115       O  
ATOM    370  N   GLY A  52      46.167 114.363  30.931  1.00 42.40           N  
ANISOU  370  N   GLY A  52     9807   2871   3431   -752   1900    -80       N  
ATOM    371  CA  GLY A  52      46.189 113.008  31.436  1.00 41.81           C  
ANISOU  371  CA  GLY A  52     9642   2837   3407   -683   1914    -51       C  
ATOM    372  C   GLY A  52      45.323 112.771  32.649  1.00 41.57           C  
ANISOU  372  C   GLY A  52     9583   2792   3419   -625   1938    -53       C  
ATOM    373  O   GLY A  52      45.326 111.656  33.182  1.00 41.17           O  
ANISOU  373  O   GLY A  52     9465   2772   3406   -571   1953    -28       O  
ATOM    374  N   HIS A  53      44.585 113.779  33.100  1.00 41.47           N  
ANISOU  374  N   HIS A  53     9619   2738   3399   -634   1944    -77       N  
ATOM    375  CA  HIS A  53      43.744 113.632  34.275  1.00 41.32           C  
ANISOU  375  CA  HIS A  53     9572   2710   3419   -588   1969    -78       C  
ATOM    376  C   HIS A  53      42.533 112.759  33.966  1.00 40.75           C  
ANISOU  376  C   HIS A  53     9411   2637   3433   -463   1940    -48       C  
ATOM    377  O   HIS A  53      42.094 112.641  32.818  1.00 40.58           O  
ANISOU  377  O   HIS A  53     9366   2610   3443   -414   1897    -32       O  
ATOM    378  CB  HIS A  53      43.281 115.002  34.775  1.00 41.93           C  
ANISOU  378  CB  HIS A  53     9726   2744   3463   -629   1982   -106       C  
ATOM    379  CG  HIS A  53      44.400 115.959  35.051  1.00 42.64           C  
ANISOU  379  CG  HIS A  53     9912   2830   3461   -769   2011   -145       C  
ATOM    380  ND1 HIS A  53      44.861 116.855  34.112  1.00 43.17           N  
ANISOU  380  ND1 HIS A  53    10053   2876   3474   -833   1991   -158       N  
ATOM    381  CD2 HIS A  53      45.148 116.158  36.162  1.00 43.00           C  
ANISOU  381  CD2 HIS A  53     9984   2891   3462   -869   2054   -175       C  
ATOM    382  CE1 HIS A  53      45.846 117.566  34.632  1.00 43.84           C  
ANISOU  382  CE1 HIS A  53    10209   2964   3483   -973   2022   -199       C  
ATOM    383  NE2 HIS A  53      46.040 117.163  35.875  1.00 43.74           N  
ANISOU  383  NE2 HIS A  53    10162   2978   3481   -999   2057   -209       N  
ATOM    384  N   ALA A  54      41.999 112.134  35.011  1.00 39.67           N  
ANISOU  384  N   ALA A  54     9228   2510   3337   -424   1964    -42       N  
ATOM    385  CA  ALA A  54      40.779 111.350  34.905  1.00 39.25           C  
ANISOU  385  CA  ALA A  54     9092   2456   3366   -326   1941    -21       C  
ATOM    386  C   ALA A  54      39.570 112.247  35.136  1.00 39.53           C  
ANISOU  386  C   ALA A  54     9135   2454   3431   -297   1927    -32       C  
ATOM    387  O   ALA A  54      39.618 113.194  35.924  1.00 39.98           O  
ANISOU  387  O   ALA A  54     9251   2488   3452   -343   1954    -53       O  
ATOM    388  CB  ALA A  54      40.782 110.197  35.909  1.00 38.96           C  
ANISOU  388  CB  ALA A  54     9005   2443   3355   -302   1975     -8       C  
ATOM    389  N   VAL A  55      38.475 111.938  34.435  1.00 39.34           N  
ANISOU  389  N   VAL A  55     9056   2421   3472   -221   1886    -18       N  
ATOM    390  CA  VAL A  55      37.297 112.804  34.462  1.00 39.72           C  
ANISOU  390  CA  VAL A  55     9114   2427   3551   -178   1865    -27       C  
ATOM    391  C   VAL A  55      36.436 112.627  35.701  1.00 39.76           C  
ANISOU  391  C   VAL A  55     9091   2425   3591   -154   1895    -38       C  
ATOM    392  O   VAL A  55      35.549 113.456  35.941  1.00 40.21           O  
ANISOU  392  O   VAL A  55     9170   2442   3665   -122   1889    -51       O  
ATOM    393  CB  VAL A  55      36.420 112.576  33.217  1.00 39.63           C  
ANISOU  393  CB  VAL A  55     9062   2405   3589   -108   1813    -13       C  
ATOM    394  CG1 VAL A  55      37.067 113.198  32.001  1.00 39.83           C  
ANISOU  394  CG1 VAL A  55     9140   2420   3574   -132   1782     -7       C  
ATOM    395  CG2 VAL A  55      36.196 111.094  32.995  1.00 39.05           C  
ANISOU  395  CG2 VAL A  55     8908   2367   3563    -77   1809      1       C  
ATOM    396  N   SER A  56      36.662 111.582  36.492  1.00 39.39           N  
ANISOU  396  N   SER A  56     9003   2410   3554   -164   1929    -32       N  
ATOM    397  CA  SER A  56      35.855 111.344  37.683  1.00 39.46           C  
ANISOU  397  CA  SER A  56     8989   2411   3592   -148   1961    -42       C  
ATOM    398  C   SER A  56      36.600 110.381  38.599  1.00 39.19           C  
ANISOU  398  C   SER A  56     8943   2409   3538   -183   2007    -33       C  
ATOM    399  O   SER A  56      37.675 109.874  38.264  1.00 38.97           O  
ANISOU  399  O   SER A  56     8920   2408   3480   -208   2010    -19       O  
ATOM    400  CB  SER A  56      34.470 110.799  37.318  1.00 39.36           C  
ANISOU  400  CB  SER A  56     8915   2389   3652    -76   1935    -40       C  
ATOM    401  OG  SER A  56      34.554 109.474  36.822  1.00 38.90           O  
ANISOU  401  OG  SER A  56     8799   2360   3621    -61   1926    -20       O  
ATOM    402  N   ARG A  57      36.009 110.135  39.770  1.00 42.61           N  
ANISOU  402  N   ARG A  57     9365   2837   3988   -182   2045    -41       N  
ATOM    403  CA  ARG A  57      36.584 109.178  40.709  1.00 42.45           C  
ANISOU  403  CA  ARG A  57     9337   2840   3951   -206   2090    -27       C  
ATOM    404  C   ARG A  57      36.504 107.760  40.162  1.00 42.06           C  
ANISOU  404  C   ARG A  57     9225   2813   3941   -163   2072      3       C  
ATOM    405  O   ARG A  57      37.472 106.995  40.252  1.00 42.07           O  
ANISOU  405  O   ARG A  57     9225   2838   3920   -172   2086     26       O  
ATOM    406  CB  ARG A  57      35.869 109.265  42.057  1.00 43.04           C  
ANISOU  406  CB  ARG A  57     9420   2899   4034   -217   2136    -44       C  
ATOM    407  CG  ARG A  57      35.926 110.629  42.710  1.00 43.58           C  
ANISOU  407  CG  ARG A  57     9556   2942   4062   -262   2161    -79       C  
ATOM    408  CD  ARG A  57      35.410 110.575  44.137  1.00 44.06           C  
ANISOU  408  CD  ARG A  57     9628   2991   4122   -282   2217    -97       C  
ATOM    409  NE  ARG A  57      35.592 111.850  44.825  1.00 44.93           N  
ANISOU  409  NE  ARG A  57     9809   3077   4187   -335   2247   -136       N  
ATOM    410  CZ  ARG A  57      36.708 112.207  45.453  1.00 45.34           C  
ANISOU  410  CZ  ARG A  57     9924   3137   4166   -421   2291   -146       C  
ATOM    411  NH1 ARG A  57      37.748 111.383  45.480  1.00 45.08           N1+
ANISOU  411  NH1 ARG A  57     9886   3141   4103   -451   2302   -116       N1+
ATOM    412  NH2 ARG A  57      36.787 113.388  46.052  1.00 45.59           N  
ANISOU  412  NH2 ARG A  57    10022   3142   4157   -477   2320   -187       N  
ATOM    413  N   GLY A  58      35.359 107.397  39.581  1.00 41.49           N  
ANISOU  413  N   GLY A  58     9106   2731   3928   -117   2043      2       N  
ATOM    414  CA  GLY A  58      35.097 106.050  39.107  1.00 41.27           C  
ANISOU  414  CA  GLY A  58     9027   2715   3939    -86   2032     23       C  
ATOM    415  C   GLY A  58      36.186 105.431  38.254  1.00 41.24           C  
ANISOU  415  C   GLY A  58     9017   2734   3918    -80   2013     46       C  
ATOM    416  O   GLY A  58      36.260 104.205  38.129  1.00 41.27           O  
ANISOU  416  O   GLY A  58     8993   2746   3941    -59   2018     67       O  
ATOM    417  N   SER A  59      37.036 106.270  37.655  1.00 38.54           N  
ANISOU  417  N   SER A  59     8711   2397   3536   -100   1996     41       N  
ATOM    418  CA  SER A  59      38.191 105.755  36.929  1.00 38.40           C  
ANISOU  418  CA  SER A  59     8699   2399   3491    -99   1987     59       C  
ATOM    419  C   SER A  59      39.135 105.005  37.860  1.00 38.47           C  
ANISOU  419  C   SER A  59     8722   2425   3471   -106   2029     83       C  
ATOM    420  O   SER A  59      39.673 103.953  37.496  1.00 38.41           O  
ANISOU  420  O   SER A  59     8698   2428   3467    -74   2030    109       O  
ATOM    421  CB  SER A  59      38.923 106.900  36.232  1.00 38.50           C  
ANISOU  421  CB  SER A  59     8761   2410   3458   -136   1968     45       C  
ATOM    422  OG  SER A  59      40.197 106.484  35.770  1.00 38.47           O  
ANISOU  422  OG  SER A  59     8777   2425   3415   -147   1973     60       O  
ATOM    423  N   ALA A  60      39.345 105.527  39.070  1.00 39.18           N  
ANISOU  423  N   ALA A  60     8843   2514   3529   -145   2066     76       N  
ATOM    424  CA  ALA A  60      40.229 104.869  40.024  1.00 39.35           C  
ANISOU  424  CA  ALA A  60     8871   2560   3521   -151   2102    109       C  
ATOM    425  C   ALA A  60      39.604 103.618  40.627  1.00 39.35           C  
ANISOU  425  C   ALA A  60     8832   2558   3562   -107   2118    137       C  
ATOM    426  O   ALA A  60      40.339 102.732  41.077  1.00 39.52           O  
ANISOU  426  O   ALA A  60     8845   2605   3567    -84   2135    182       O  
ATOM    427  CB  ALA A  60      40.630 105.846  41.132  1.00 39.66           C  
ANISOU  427  CB  ALA A  60     8950   2610   3510   -220   2135     96       C  
ATOM    428  N   LYS A  61      38.271 103.532  40.666  1.00 38.85           N  
ANISOU  428  N   LYS A  61     8744   2470   3547    -96   2113    117       N  
ATOM    429  CA  LYS A  61      37.620 102.274  41.021  1.00 38.92           C  
ANISOU  429  CA  LYS A  61     8721   2471   3594    -65   2125    139       C  
ATOM    430  C   LYS A  61      38.006 101.173  40.043  1.00 38.84           C  
ANISOU  430  C   LYS A  61     8691   2464   3601    -19   2104    163       C  
ATOM    431  O   LYS A  61      38.339 100.052  40.445  1.00 39.05           O  
ANISOU  431  O   LYS A  61     8718   2493   3629     10   2123    200       O  
ATOM    432  CB  LYS A  61      36.099 102.446  41.036  1.00 38.91           C  
ANISOU  432  CB  LYS A  61     8698   2446   3639    -72   2121    109       C  
ATOM    433  CG  LYS A  61      35.525 103.195  42.225  1.00 39.12           C  
ANISOU  433  CG  LYS A  61     8748   2462   3656   -107   2156     89       C  
ATOM    434  CD  LYS A  61      34.036 103.443  42.005  1.00 39.18           C  
ANISOU  434  CD  LYS A  61     8736   2443   3708   -104   2149     58       C  
ATOM    435  CE  LYS A  61      33.383 104.135  43.192  1.00 39.48           C  
ANISOU  435  CE  LYS A  61     8801   2462   3737   -133   2191     34       C  
ATOM    436  NZ  LYS A  61      32.762 103.164  44.137  1.00 39.72           N1+
ANISOU  436  NZ  LYS A  61     8826   2484   3781   -150   2234     48       N1+
ATOM    437  N   LEU A  62      37.967 101.483  38.744  1.00 38.66           N  
ANISOU  437  N   LEU A  62     8658   2439   3590    -12   2066    144       N  
ATOM    438  CA  LEU A  62      38.234 100.479  37.721  1.00 38.61           C  
ANISOU  438  CA  LEU A  62     8638   2432   3601     27   2048    159       C  
ATOM    439  C   LEU A  62      39.664  99.961  37.811  1.00 38.78           C  
ANISOU  439  C   LEU A  62     8689   2467   3580     57   2066    196       C  
ATOM    440  O   LEU A  62      39.905  98.757  37.671  1.00 38.99           O  
ANISOU  440  O   LEU A  62     8715   2484   3614    103   2076    224       O  
ATOM    441  CB  LEU A  62      37.962 101.068  36.337  1.00 38.37           C  
ANISOU  441  CB  LEU A  62     8594   2401   3583     22   2004    133       C  
ATOM    442  CG  LEU A  62      37.238 100.186  35.319  1.00 38.34           C  
ANISOU  442  CG  LEU A  62     8559   2384   3624     42   1981    128       C  
ATOM    443  CD1 LEU A  62      38.093  98.995  34.911  1.00 38.48           C  
ANISOU  443  CD1 LEU A  62     8588   2399   3632     80   1993    154       C  
ATOM    444  CD2 LEU A  62      35.897  99.729  35.875  1.00 38.48           C  
ANISOU  444  CD2 LEU A  62     8554   2382   3685     29   1994    118       C  
ATOM    445  N   ARG A  63      40.625 100.858  38.042  1.00 39.83           N  
ANISOU  445  N   ARG A  63     8851   2620   3661     32   2073    199       N  
ATOM    446  CA  ARG A  63      42.017 100.435  38.147  1.00 40.09           C  
ANISOU  446  CA  ARG A  63     8908   2680   3645     59   2091    243       C  
ATOM    447  C   ARG A  63      42.218  99.489  39.323  1.00 40.47           C  
ANISOU  447  C   ARG A  63     8950   2743   3685     95   2124    295       C  
ATOM    448  O   ARG A  63      42.937  98.489  39.207  1.00 40.79           O  
ANISOU  448  O   ARG A  63     8997   2793   3707    159   2135    342       O  
ATOM    449  CB  ARG A  63      42.930 101.652  38.279  1.00 40.15           C  
ANISOU  449  CB  ARG A  63     8939   2724   3592     -1   2092    238       C  
ATOM    450  CG  ARG A  63      44.411 101.310  38.312  1.00 40.51           C  
ANISOU  450  CG  ARG A  63     8984   2839   3570     17   2105    292       C  
ATOM    451  CD  ARG A  63      45.245 102.531  38.648  1.00 40.69           C  
ANISOU  451  CD  ARG A  63     9003   2937   3522    -68   2103    284       C  
ATOM    452  NE  ARG A  63      44.921 103.051  39.972  1.00 40.82           N  
ANISOU  452  NE  ARG A  63     9005   2979   3528   -116   2120    278       N  
ATOM    453  CZ  ARG A  63      45.362 104.210  40.448  1.00 41.02           C  
ANISOU  453  CZ  ARG A  63     9027   3061   3500   -206   2121    254       C  
ATOM    454  NH1 ARG A  63      46.147 104.977  39.704  1.00 41.13           N1+
ANISOU  454  NH1 ARG A  63     9050   3113   3466   -263   2103    235       N1+
ATOM    455  NH2 ARG A  63      45.015 104.604  41.666  1.00 41.18           N  
ANISOU  455  NH2 ARG A  63     9036   3102   3511   -246   2140    246       N  
ATOM    456  N   TRP A  64      41.591  99.789  40.463  1.00 40.05           N  
ANISOU  456  N   TRP A  64     8887   2692   3639     60   2140    290       N  
ATOM    457  CA  TRP A  64      41.688  98.903  41.619  1.00 40.47           C  
ANISOU  457  CA  TRP A  64     8931   2763   3681     90   2168    343       C  
ATOM    458  C   TRP A  64      41.181  97.508  41.276  1.00 40.64           C  
ANISOU  458  C   TRP A  64     8954   2740   3747    149   2170    358       C  
ATOM    459  O   TRP A  64      41.824  96.504  41.603  1.00 41.10           O  
ANISOU  459  O   TRP A  64     9024   2810   3784    210   2187    416       O  
ATOM    460  CB  TRP A  64      40.907  99.486  42.799  1.00 40.48           C  
ANISOU  460  CB  TRP A  64     8924   2770   3689     33   2185    326       C  
ATOM    461  CG  TRP A  64      41.116  98.737  44.083  1.00 40.97           C  
ANISOU  461  CG  TRP A  64     8971   2870   3725     51   2212    386       C  
ATOM    462  CD1 TRP A  64      42.044  99.007  45.047  1.00 41.33           C  
ANISOU  462  CD1 TRP A  64     8991   3010   3701     38   2225    430       C  
ATOM    463  CD2 TRP A  64      40.384  97.593  44.542  1.00 41.25           C  
ANISOU  463  CD2 TRP A  64     9008   2870   3796     81   2226    409       C  
ATOM    464  NE1 TRP A  64      41.935  98.106  46.076  1.00 41.79           N  
ANISOU  464  NE1 TRP A  64     9036   3093   3750     67   2244    484       N  
ATOM    465  CE2 TRP A  64      40.924  97.226  45.791  1.00 41.77           C  
ANISOU  465  CE2 TRP A  64     9058   2999   3813     91   2247    473       C  
ATOM    466  CE3 TRP A  64      39.326  96.844  44.019  1.00 41.19           C  
ANISOU  466  CE3 TRP A  64     9007   2797   3848     90   2222    382       C  
ATOM    467  CZ2 TRP A  64      40.442  96.145  46.524  1.00 42.23           C  
ANISOU  467  CZ2 TRP A  64     9122   3039   3885    115   2266    512       C  
ATOM    468  CZ3 TRP A  64      38.849  95.771  44.748  1.00 41.67           C  
ANISOU  468  CZ3 TRP A  64     9073   2839   3920    102   2243    417       C  
ATOM    469  CH2 TRP A  64      39.406  95.431  45.987  1.00 42.18           C  
ANISOU  469  CH2 TRP A  64     9137   2950   3940    117   2264    482       C  
ATOM    470  N   LEU A  65      40.029  97.427  40.604  1.00 41.59           N  
ANISOU  470  N   LEU A  65     9062   2820   3923    129   2152    310       N  
ATOM    471  CA  LEU A  65      39.516  96.132  40.172  1.00 41.82           C  
ANISOU  471  CA  LEU A  65     9091   2812   3988    165   2153    317       C  
ATOM    472  C   LEU A  65      40.447  95.463  39.169  1.00 41.96           C  
ANISOU  472  C   LEU A  65     9129   2825   3991    227   2146    338       C  
ATOM    473  O   LEU A  65      40.484  94.230  39.086  1.00 42.41           O  
ANISOU  473  O   LEU A  65     9205   2852   4056    276   2160    364       O  
ATOM    474  CB  LEU A  65      38.117  96.289  39.572  1.00 41.55           C  
ANISOU  474  CB  LEU A  65     9028   2756   4004    119   2132    265       C  
ATOM    475  CG  LEU A  65      36.967  96.496  40.558  1.00 41.63           C  
ANISOU  475  CG  LEU A  65     9027   2756   4034     69   2150    250       C  
ATOM    476  CD1 LEU A  65      35.678  96.798  39.818  1.00 41.42           C  
ANISOU  476  CD1 LEU A  65     8973   2714   4049     31   2130    202       C  
ATOM    477  CD2 LEU A  65      36.800  95.271  41.441  1.00 42.19           C  
ANISOU  477  CD2 LEU A  65     9117   2806   4107     81   2182    288       C  
ATOM    478  N   GLU A  66      41.209  96.252  38.405  1.00 42.50           N  
ANISOU  478  N   GLU A  66     9202   2916   4032    226   2130    325       N  
ATOM    479  CA  GLU A  66      42.090  95.667  37.401  1.00 42.67           C  
ANISOU  479  CA  GLU A  66     9246   2931   4034    285   2128    343       C  
ATOM    480  C   GLU A  66      43.365  95.115  38.027  1.00 43.23           C  
ANISOU  480  C   GLU A  66     9350   3027   4047    358   2160    413       C  
ATOM    481  O   GLU A  66      43.758  93.978  37.744  1.00 44.07           O  
ANISOU  481  O   GLU A  66     9487   3110   4149    436   2176    446       O  
ATOM    482  CB  GLU A  66      42.437  96.698  36.327  1.00 42.58           C  
ANISOU  482  CB  GLU A  66     9233   2937   4008    252   2101    308       C  
ATOM    483  CG  GLU A  66      43.175  96.091  35.143  1.00 42.73           C  
ANISOU  483  CG  GLU A  66     9278   2946   4011    305   2099    317       C  
ATOM    484  CD  GLU A  66      44.044  97.092  34.412  1.00 42.54           C  
ANISOU  484  CD  GLU A  66     9271   2950   3942    279   2087    308       C  
ATOM    485  OE1 GLU A  66      44.018  97.103  33.162  1.00 42.39           O  
ANISOU  485  OE1 GLU A  66     9256   2919   3932    277   2067    282       O  
ATOM    486  OE2 GLU A  66      44.755  97.865  35.086  1.00 42.61           O  
ANISOU  486  OE2 GLU A  66     9286   3001   3901    251   2097    329       O  
ATOM    487  N   GLU A  67      44.031  95.913  38.870  1.00 44.73           N  
ANISOU  487  N   GLU A  67     9531   3277   4186    334   2168    441       N  
ATOM    488  CA  GLU A  67      45.281  95.468  39.482  1.00 45.11           C  
ANISOU  488  CA  GLU A  67     9584   3397   4160    401   2192    521       C  
ATOM    489  C   GLU A  67      45.088  94.171  40.256  1.00 45.73           C  
ANISOU  489  C   GLU A  67     9681   3447   4249    476   2216    572       C  
ATOM    490  O   GLU A  67      45.952  93.286  40.227  1.00 46.54           O  
ANISOU  490  O   GLU A  67     9807   3569   4305    577   2235    633       O  
ATOM    491  CB  GLU A  67      45.833  96.544  40.419  1.00 45.17           C  
ANISOU  491  CB  GLU A  67     9547   3514   4103    338   2190    536       C  
ATOM    492  CG  GLU A  67      45.958  97.932  39.831  1.00 44.87           C  
ANISOU  492  CG  GLU A  67     9496   3502   4052    245   2167    480       C  
ATOM    493  CD  GLU A  67      46.323  98.956  40.889  1.00 45.31           C  
ANISOU  493  CD  GLU A  67     9504   3662   4050    167   2167    480       C  
ATOM    494  OE1 GLU A  67      46.783  98.540  41.972  1.00 45.90           O  
ANISOU  494  OE1 GLU A  67     9538   3827   4075    196   2182    533       O  
ATOM    495  OE2 GLU A  67      46.144 100.170  40.649  1.00 45.03           O1+
ANISOU  495  OE2 GLU A  67     9471   3623   4015     77   2152    426       O1+
ATOM    496  N   ARG A  68      43.962  94.044  40.961  1.00 43.87           N  
ANISOU  496  N   ARG A  68     9436   3169   4065    430   2217    549       N  
ATOM    497  CA  ARG A  68      43.713  92.859  41.773  1.00 44.53           C  
ANISOU  497  CA  ARG A  68     9540   3224   4154    482   2239    597       C  
ATOM    498  C   ARG A  68      43.464  91.615  40.930  1.00 44.88           C  
ANISOU  498  C   ARG A  68     9629   3190   4234    542   2245    589       C  
ATOM    499  O   ARG A  68      43.594  90.498  41.443  1.00 45.65           O  
ANISOU  499  O   ARG A  68     9762   3260   4321    610   2268    641       O  
ATOM    500  CB  ARG A  68      42.520  93.100  42.699  1.00 44.35           C  
ANISOU  500  CB  ARG A  68     9496   3185   4172    401   2241    570       C  
ATOM    501  CG  ARG A  68      42.676  94.293  43.631  1.00 44.11           C  
ANISOU  501  CG  ARG A  68     9425   3230   4105    336   2239    572       C  
ATOM    502  CD  ARG A  68      43.944  94.200  44.462  1.00 44.69           C  
ANISOU  502  CD  ARG A  68     9479   3408   4091    388   2252    655       C  
ATOM    503  NE  ARG A  68      43.974  95.205  45.522  1.00 44.59           N  
ANISOU  503  NE  ARG A  68     9417   3485   4040    312   2253    653       N  
ATOM    504  CZ  ARG A  68      44.579  96.384  45.424  1.00 44.31           C  
ANISOU  504  CZ  ARG A  68     9344   3534   3958    257   2240    629       C  
ATOM    505  NH1 ARG A  68      44.550  97.231  46.444  1.00 44.33           N1+
ANISOU  505  NH1 ARG A  68     9302   3618   3924    182   2243    619       N1+
ATOM    506  NH2 ARG A  68      45.217  96.717  44.309  1.00 44.08           N  
ANISOU  506  NH2 ARG A  68     9322   3512   3915    268   2225    609       N  
ATOM    507  N   GLY A  69      43.119  91.780  39.658  1.00 44.00           N  
ANISOU  507  N   GLY A  69     9515   3047   4158    516   2225    529       N  
ATOM    508  CA  GLY A  69      42.764  90.662  38.811  1.00 44.34           C  
ANISOU  508  CA  GLY A  69     9588   3027   4232    549   2228    512       C  
ATOM    509  C   GLY A  69      41.284  90.372  38.729  1.00 44.19           C  
ANISOU  509  C   GLY A  69     9549   2969   4274    466   2217    462       C  
ATOM    510  O   GLY A  69      40.903  89.349  38.147  1.00 44.61           O  
ANISOU  510  O   GLY A  69     9629   2972   4349    478   2222    452       O  
ATOM    511  N   TYR A  70      40.438  91.234  39.298  1.00 42.20           N  
ANISOU  511  N   TYR A  70     9253   2737   4043    382   2205    432       N  
ATOM    512  CA  TYR A  70      38.998  91.012  39.231  1.00 42.12           C  
ANISOU  512  CA  TYR A  70     9225   2699   4082    304   2199    388       C  
ATOM    513  C   TYR A  70      38.456  91.270  37.832  1.00 41.69           C  
ANISOU  513  C   TYR A  70     9141   2640   4058    268   2168    333       C  
ATOM    514  O   TYR A  70      37.467  90.651  37.425  1.00 41.88           O  
ANISOU  514  O   TYR A  70     9167   2631   4116    225   2168    306       O  
ATOM    515  CB  TYR A  70      38.282  91.903  40.244  1.00 41.81           C  
ANISOU  515  CB  TYR A  70     9152   2684   4049    237   2200    375       C  
ATOM    516  CG  TYR A  70      38.502  91.511  41.688  1.00 42.33           C  
ANISOU  516  CG  TYR A  70     9242   2753   4090    253   2230    429       C  
ATOM    517  CD1 TYR A  70      38.668  92.479  42.670  1.00 42.10           C  
ANISOU  517  CD1 TYR A  70     9190   2768   4037    227   2235    440       C  
ATOM    518  CD2 TYR A  70      38.531  90.177  42.073  1.00 43.15           C  
ANISOU  518  CD2 TYR A  70     9393   2813   4189    291   2255    471       C  
ATOM    519  CE1 TYR A  70      38.867  92.129  43.992  1.00 42.62           C  
ANISOU  519  CE1 TYR A  70     9269   2848   4075    237   2260    495       C  
ATOM    520  CE2 TYR A  70      38.727  89.818  43.395  1.00 43.71           C  
ANISOU  520  CE2 TYR A  70     9483   2890   4233    307   2280    529       C  
ATOM    521  CZ  TYR A  70      38.894  90.799  44.349  1.00 43.41           C  
ANISOU  521  CZ  TYR A  70     9413   2910   4172    280   2281    542       C  
ATOM    522  OH  TYR A  70      39.090  90.449  45.665  1.00 44.00           O  
ANISOU  522  OH  TYR A  70     9499   3005   4214    291   2303    605       O  
ATOM    523  N   LEU A  71      39.082  92.173  37.085  1.00 41.28           N  
ANISOU  523  N   LEU A  71     9070   2623   3992    278   2144    318       N  
ATOM    524  CA  LEU A  71      38.610  92.552  35.762  1.00 40.87           C  
ANISOU  524  CA  LEU A  71     8989   2575   3966    244   2111    272       C  
ATOM    525  C   LEU A  71      39.757  92.448  34.770  1.00 40.88           C  
ANISOU  525  C   LEU A  71     9012   2582   3939    301   2105    282       C  
ATOM    526  O   LEU A  71      40.872  92.900  35.052  1.00 40.85           O  
ANISOU  526  O   LEU A  71     9027   2602   3892    343   2114    309       O  
ATOM    527  CB  LEU A  71      38.033  93.971  35.769  1.00 40.25           C  
ANISOU  527  CB  LEU A  71     8865   2530   3897    186   2083    237       C  
ATOM    528  CG  LEU A  71      37.072  94.281  34.622  1.00 39.97           C  
ANISOU  528  CG  LEU A  71     8797   2492   3897    143   2050    193       C  
ATOM    529  CD1 LEU A  71      35.966  93.241  34.574  1.00 40.38           C  
ANISOU  529  CD1 LEU A  71     8853   2504   3983    112   2064    180       C  
ATOM    530  CD2 LEU A  71      36.491  95.678  34.764  1.00 39.51           C  
ANISOU  530  CD2 LEU A  71     8707   2461   3845    101   2027    166       C  
ATOM    531  N   GLN A  72      39.476  91.844  33.613  1.00 43.07           N  
ANISOU  531  N   GLN A  72     9292   2836   4237    300   2093    259       N  
ATOM    532  CA  GLN A  72      40.440  91.668  32.529  1.00 43.14           C  
ANISOU  532  CA  GLN A  72     9325   2844   4222    350   2090    263       C  
ATOM    533  C   GLN A  72      39.827  92.270  31.268  1.00 42.68           C  
ANISOU  533  C   GLN A  72     9229   2798   4188    295   2050    216       C  
ATOM    534  O   GLN A  72      39.346  91.539  30.390  1.00 42.91           O  
ANISOU  534  O   GLN A  72     9262   2799   4242    284   2046    196       O  
ATOM    535  CB  GLN A  72      40.786  90.193  32.330  1.00 44.01           C  
ANISOU  535  CB  GLN A  72     9489   2905   4327    412   2120    285       C  
ATOM    536  CG  GLN A  72      41.324  89.492  33.574  1.00 44.96           C  
ANISOU  536  CG  GLN A  72     9655   3007   4421    478   2159    338       C  
ATOM    537  CD  GLN A  72      42.793  89.782  33.823  1.00 45.15           C  
ANISOU  537  CD  GLN A  72     9712   3056   4386    567   2178    384       C  
ATOM    538  OE1 GLN A  72      43.666  89.009  33.425  1.00 45.42           O  
ANISOU  538  OE1 GLN A  72     9800   3068   4389    659   2202    412       O  
ATOM    539  NE2 GLN A  72      43.074  90.898  34.486  1.00 44.76           N  
ANISOU  539  NE2 GLN A  72     9637   3053   4315    542   2171    392       N  
ATOM    540  N   PRO A  73      39.821  93.596  31.147  1.00 40.03           N  
ANISOU  540  N   PRO A  73     8863   2501   3845    260   2022    201       N  
ATOM    541  CA  PRO A  73      39.153  94.227  30.003  1.00 39.67           C  
ANISOU  541  CA  PRO A  73     8784   2466   3822    213   1983    163       C  
ATOM    542  C   PRO A  73      39.892  93.968  28.700  1.00 39.75           C  
ANISOU  542  C   PRO A  73     8818   2471   3814    240   1976    158       C  
ATOM    543  O   PRO A  73      41.124  93.913  28.659  1.00 39.89           O  
ANISOU  543  O   PRO A  73     8875   2494   3788    290   1995    181       O  
ATOM    544  CB  PRO A  73      39.168  95.719  30.361  1.00 39.20           C  
ANISOU  544  CB  PRO A  73     8704   2441   3748    181   1961    156       C  
ATOM    545  CG  PRO A  73      39.455  95.765  31.842  1.00 39.30           C  
ANISOU  545  CG  PRO A  73     8728   2460   3744    193   1991    182       C  
ATOM    546  CD  PRO A  73      40.336  94.592  32.101  1.00 39.78           C  
ANISOU  546  CD  PRO A  73     8831   2501   3784    256   2027    216       C  
ATOM    547  N   TYR A  74      39.116  93.819  27.626  1.00 39.70           N  
ANISOU  547  N   TYR A  74     8793   2453   3837    208   1953    127       N  
ATOM    548  CA  TYR A  74      39.654  93.557  26.295  1.00 39.81           C  
ANISOU  548  CA  TYR A  74     8829   2459   3837    224   1946    115       C  
ATOM    549  C   TYR A  74      38.530  93.676  25.275  1.00 39.72           C  
ANISOU  549  C   TYR A  74     8790   2440   3861    172   1916     78       C  
ATOM    550  O   TYR A  74      37.349  93.704  25.630  1.00 39.70           O  
ANISOU  550  O   TYR A  74     8760   2431   3894    133   1909     63       O  
ATOM    551  CB  TYR A  74      40.296  92.167  26.211  1.00 40.42           C  
ANISOU  551  CB  TYR A  74     8954   2500   3905    282   1984    131       C  
ATOM    552  CG  TYR A  74      39.294  91.035  26.203  1.00 40.88           C  
ANISOU  552  CG  TYR A  74     9013   2514   4003    258   1998    115       C  
ATOM    553  CD1 TYR A  74      38.871  90.464  25.010  1.00 41.13           C  
ANISOU  553  CD1 TYR A  74     9055   2521   4053    235   1993     82       C  
ATOM    554  CD2 TYR A  74      38.760  90.547  27.388  1.00 41.11           C  
ANISOU  554  CD2 TYR A  74     9045   2527   4049    251   2020    129       C  
ATOM    555  CE1 TYR A  74      37.948  89.437  24.997  1.00 41.65           C  
ANISOU  555  CE1 TYR A  74     9134   2541   4149    201   2012     63       C  
ATOM    556  CE2 TYR A  74      37.837  89.520  27.385  1.00 41.63           C  
ANISOU  556  CE2 TYR A  74     9126   2547   4145    217   2038    112       C  
ATOM    557  CZ  TYR A  74      37.435  88.969  26.188  1.00 41.91           C  
ANISOU  557  CZ  TYR A  74     9175   2554   4195    189   2035     78       C  
ATOM    558  OH  TYR A  74      36.517  87.946  26.180  1.00 42.52           O  
ANISOU  558  OH  TYR A  74     9280   2581   4296    143   2060     57       O  
ATOM    559  N   GLY A  75      38.916  93.739  24.000  1.00 40.72           N  
ANISOU  559  N   GLY A  75     8932   2566   3973    175   1902     63       N  
ATOM    560  CA  GLY A  75      37.975  93.705  22.894  1.00 40.77           C  
ANISOU  560  CA  GLY A  75     8924   2559   4005    133   1879     28       C  
ATOM    561  C   GLY A  75      37.090  94.927  22.794  1.00 40.39           C  
ANISOU  561  C   GLY A  75     8843   2533   3970     94   1841     16       C  
ATOM    562  O   GLY A  75      37.515  96.052  23.067  1.00 40.05           O  
ANISOU  562  O   GLY A  75     8796   2518   3903     98   1822     31       O  
ATOM    563  N   LYS A  76      35.840  94.694  22.386  1.00 43.04           N  
ANISOU  563  N   LYS A  76     9166   2849   4340     57   1834    -13       N  
ATOM    564  CA  LYS A  76      34.844  95.756  22.320  1.00 42.86           C  
ANISOU  564  CA  LYS A  76     9120   2834   4330     33   1803    -25       C  
ATOM    565  C   LYS A  76      34.250  95.965  23.705  1.00 42.79           C  
ANISOU  565  C   LYS A  76     9089   2829   4339     28   1815    -15       C  
ATOM    566  O   LYS A  76      33.530  95.102  24.215  1.00 43.09           O  
ANISOU  566  O   LYS A  76     9128   2843   4403      6   1844    -27       O  
ATOM    567  CB  LYS A  76      33.757  95.417  21.306  1.00 43.18           C  
ANISOU  567  CB  LYS A  76     9168   2848   4391     -1   1799    -64       C  
ATOM    568  CG  LYS A  76      32.538  96.323  21.404  1.00 43.34           C  
ANISOU  568  CG  LYS A  76     9176   2865   4426    -16   1778    -78       C  
ATOM    569  CD  LYS A  76      31.533  96.069  20.298  1.00 43.76           C  
ANISOU  569  CD  LYS A  76     9248   2891   4488    -47   1777   -120       C  
ATOM    570  CE  LYS A  76      30.344  97.007  20.434  1.00 44.08           C  
ANISOU  570  CE  LYS A  76     9288   2922   4538    -45   1761   -135       C  
ATOM    571  NZ  LYS A  76      29.688  97.265  19.124  1.00 44.78           N1+
ANISOU  571  NZ  LYS A  76     9407   2991   4615    -53   1744   -169       N1+
ATOM    572  N   VAL A  77      34.557  97.105  24.319  1.00 39.83           N  
ANISOU  572  N   VAL A  77     8705   2481   3950     42   1798      3       N  
ATOM    573  CA  VAL A  77      34.074  97.441  25.654  1.00 39.77           C  
ANISOU  573  CA  VAL A  77     8680   2477   3954     38   1810     11       C  
ATOM    574  C   VAL A  77      32.815  98.284  25.520  1.00 39.83           C  
ANISOU  574  C   VAL A  77     8678   2474   3981     26   1790    -10       C  
ATOM    575  O   VAL A  77      32.814  99.310  24.829  1.00 39.73           O  
ANISOU  575  O   VAL A  77     8674   2468   3955     38   1755    -11       O  
ATOM    576  CB  VAL A  77      35.150  98.183  26.467  1.00 39.48           C  
ANISOU  576  CB  VAL A  77     8648   2469   3885     58   1810     38       C  
ATOM    577  CG1 VAL A  77      34.611  98.573  27.831  1.00 39.46           C  
ANISOU  577  CG1 VAL A  77     8632   2468   3893     51   1825     42       C  
ATOM    578  CG2 VAL A  77      36.395  97.318  26.607  1.00 39.55           C  
ANISOU  578  CG2 VAL A  77     8677   2481   3868     81   1837     59       C  
ATOM    579  N   VAL A  78      31.743  97.849  26.177  1.00 38.47           N  
ANISOU  579  N   VAL A  78     8500   2281   3837      5   1815    -26       N  
ATOM    580  CA  VAL A  78      30.480  98.576  26.224  1.00 38.66           C  
ANISOU  580  CA  VAL A  78     8523   2288   3876      2   1807    -49       C  
ATOM    581  C   VAL A  78      30.277  99.065  27.650  1.00 38.59           C  
ANISOU  581  C   VAL A  78     8506   2286   3871      7   1824    -39       C  
ATOM    582  O   VAL A  78      30.418  98.291  28.605  1.00 38.64           O  
ANISOU  582  O   VAL A  78     8510   2292   3882    -12   1860    -30       O  
ATOM    583  CB  VAL A  78      29.307  97.696  25.760  1.00 39.14           C  
ANISOU  583  CB  VAL A  78     8598   2314   3960    -36   1831    -87       C  
ATOM    584  CG1 VAL A  78      27.987  98.403  25.993  1.00 39.44           C  
ANISOU  584  CG1 VAL A  78     8644   2331   4010    -33   1835   -117       C  
ATOM    585  CG2 VAL A  78      29.465  97.350  24.290  1.00 39.25           C  
ANISOU  585  CG2 VAL A  78     8626   2320   3967    -42   1814   -103       C  
ATOM    586  N   ASP A  79      29.953 100.351  27.794  1.00 40.04           N  
ANISOU  586  N   ASP A  79     8694   2471   4050     33   1801    -41       N  
ATOM    587  CA  ASP A  79      29.917 101.029  29.091  1.00 39.99           C  
ANISOU  587  CA  ASP A  79     8684   2471   4038     41   1815    -33       C  
ATOM    588  C   ASP A  79      28.539 101.657  29.287  1.00 40.38           C  
ANISOU  588  C   ASP A  79     8745   2491   4106     58   1820    -63       C  
ATOM    589  O   ASP A  79      28.317 102.819  28.936  1.00 40.48           O  
ANISOU  589  O   ASP A  79     8774   2496   4110     99   1789    -67       O  
ATOM    590  CB  ASP A  79      31.030 102.069  29.177  1.00 39.68           C  
ANISOU  590  CB  ASP A  79     8653   2458   3967     60   1790     -9       C  
ATOM    591  CG  ASP A  79      31.168 102.664  30.560  1.00 39.65           C  
ANISOU  591  CG  ASP A  79     8653   2460   3953     58   1811     -2       C  
ATOM    592  OD1 ASP A  79      30.646 102.059  31.521  1.00 39.78           O  
ANISOU  592  OD1 ASP A  79     8661   2468   3985     42   1849     -9       O  
ATOM    593  OD2 ASP A  79      31.805 103.733  30.690  1.00 39.56           O1+
ANISOU  593  OD2 ASP A  79     8660   2458   3913     66   1795      7       O1+
ATOM    594  N   LEU A  80      27.619 100.883  29.855  1.00 39.71           N  
ANISOU  594  N   LEU A  80     8661   2386   4041     28   1862    -87       N  
ATOM    595  CA  LEU A  80      26.290 101.392  30.169  1.00 40.18           C  
ANISOU  595  CA  LEU A  80     8736   2416   4113     45   1879   -127       C  
ATOM    596  C   LEU A  80      26.368 102.380  31.326  1.00 40.14           C  
ANISOU  596  C   LEU A  80     8733   2417   4100     73   1884   -120       C  
ATOM    597  O   LEU A  80      27.013 102.110  32.345  1.00 39.90           O  
ANISOU  597  O   LEU A  80     8694   2404   4062     45   1908    -97       O  
ATOM    598  CB  LEU A  80      25.351 100.237  30.520  1.00 40.60           C  
ANISOU  598  CB  LEU A  80     8799   2445   4182    -12   1933   -163       C  
ATOM    599  CG  LEU A  80      24.536  99.576  29.403  1.00 41.02           C  
ANISOU  599  CG  LEU A  80     8870   2474   4242    -39   1942   -207       C  
ATOM    600  CD1 LEU A  80      25.332  99.441  28.121  1.00 40.73           C  
ANISOU  600  CD1 LEU A  80     8828   2450   4198    -28   1898   -183       C  
ATOM    601  CD2 LEU A  80      24.044  98.212  29.860  1.00 41.39           C  
ANISOU  601  CD2 LEU A  80     8931   2501   4295   -126   2002   -230       C  
ATOM    602  N   GLY A  81      25.704 103.523  31.173  1.00 40.97           N  
ANISOU  602  N   GLY A  81     8858   2506   4205    132   1865   -143       N  
ATOM    603  CA  GLY A  81      25.783 104.570  32.171  1.00 41.03           C  
ANISOU  603  CA  GLY A  81     8874   2514   4202    162   1869   -141       C  
ATOM    604  C   GLY A  81      27.202 105.065  32.358  1.00 40.55           C  
ANISOU  604  C   GLY A  81     8811   2481   4116    149   1845    -96       C  
ATOM    605  O   GLY A  81      27.708 105.109  33.482  1.00 40.39           O  
ANISOU  605  O   GLY A  81     8789   2474   4085    123   1872    -85       O  
ATOM    606  N   CYS A  82      27.855 105.443  31.256  1.00 41.55           N  
ANISOU  606  N   CYS A  82     8944   2615   4227    163   1801    -76       N  
ATOM    607  CA  CYS A  82      29.256 105.842  31.313  1.00 41.22           C  
ANISOU  607  CA  CYS A  82     8908   2601   4153    141   1786    -43       C  
ATOM    608  C   CYS A  82      29.464 107.164  32.042  1.00 41.49           C  
ANISOU  608  C   CYS A  82     8975   2626   4165    157   1784    -44       C  
ATOM    609  O   CYS A  82      30.592 107.458  32.444  1.00 41.10           O  
ANISOU  609  O   CYS A  82     8938   2597   4083    124   1789    -27       O  
ATOM    610  CB  CYS A  82      29.839 105.932  29.899  1.00 41.02           C  
ANISOU  610  CB  CYS A  82     8890   2582   4113    147   1744    -28       C  
ATOM    611  SG  CYS A  82      29.133 107.228  28.851  1.00 41.52           S  
ANISOU  611  SG  CYS A  82     8999   2608   4169    211   1699    -36       S  
ATOM    612  N   GLY A  83      28.413 107.958  32.222  1.00 41.11           N  
ANISOU  612  N   GLY A  83     8948   2543   4128    208   1782    -69       N  
ATOM    613  CA  GLY A  83      28.536 109.237  32.902  1.00 41.42           C  
ANISOU  613  CA  GLY A  83     9027   2565   4146    227   1782    -74       C  
ATOM    614  C   GLY A  83      29.420 110.208  32.150  1.00 41.46           C  
ANISOU  614  C   GLY A  83     9075   2565   4113    226   1746    -53       C  
ATOM    615  O   GLY A  83      29.285 110.396  30.939  1.00 41.59           O  
ANISOU  615  O   GLY A  83     9105   2569   4127    256   1708    -45       O  
ATOM    616  N   ARG A  84      30.343 110.839  32.879  1.00 41.28           N  
ANISOU  616  N   ARG A  84     9082   2548   4055    184   1761    -46       N  
ATOM    617  CA  ARG A  84      31.344 111.685  32.243  1.00 41.35           C  
ANISOU  617  CA  ARG A  84     9141   2552   4017    159   1738    -30       C  
ATOM    618  C   ARG A  84      32.348 110.879  31.430  1.00 40.81           C  
ANISOU  618  C   ARG A  84     9051   2523   3934    116   1727     -9       C  
ATOM    619  O   ARG A  84      33.089 111.462  30.630  1.00 40.90           O  
ANISOU  619  O   ARG A  84     9103   2530   3908     97   1704      2       O  
ATOM    620  CB  ARG A  84      32.072 112.523  33.299  1.00 41.54           C  
ANISOU  620  CB  ARG A  84     9213   2570   4000    113   1768    -37       C  
ATOM    621  CG  ARG A  84      31.145 113.449  34.083  1.00 42.19           C  
ANISOU  621  CG  ARG A  84     9329   2608   4093    158   1780    -62       C  
ATOM    622  CD  ARG A  84      31.915 114.461  34.922  1.00 42.53           C  
ANISOU  622  CD  ARG A  84     9438   2634   4086    107   1808    -71       C  
ATOM    623  NE  ARG A  84      32.071 114.042  36.312  1.00 42.34           N  
ANISOU  623  NE  ARG A  84     9395   2631   4061     65   1859    -85       N  
ATOM    624  CZ  ARG A  84      32.438 114.858  37.296  1.00 42.89           C  
ANISOU  624  CZ  ARG A  84     9520   2682   4094     25   1894   -104       C  
ATOM    625  NH1 ARG A  84      32.557 114.399  38.535  1.00 42.63           N1+
ANISOU  625  NH1 ARG A  84     9469   2668   4058    -14   1943   -116       N1+
ATOM    626  NH2 ARG A  84      32.680 116.136  37.040  1.00 43.94           N  
ANISOU  626  NH2 ARG A  84     9734   2771   4191     19   1883   -111       N  
ATOM    627  N   GLY A  85      32.375 109.567  31.603  1.00 39.06           N  
ANISOU  627  N   GLY A  85     8771   2332   3737    101   1744     -5       N  
ATOM    628  CA  GLY A  85      33.278 108.697  30.890  1.00 38.63           C  
ANISOU  628  CA  GLY A  85     8695   2311   3672     72   1738     11       C  
ATOM    629  C   GLY A  85      34.426 108.128  31.702  1.00 38.31           C  
ANISOU  629  C   GLY A  85     8649   2303   3604     25   1774     19       C  
ATOM    630  O   GLY A  85      35.405 107.666  31.103  1.00 38.08           O  
ANISOU  630  O   GLY A  85     8622   2296   3551      4   1771     31       O  
ATOM    631  N   GLY A  86      34.335 108.136  33.036  1.00 38.88           N  
ANISOU  631  N   GLY A  86     8721   2376   3675     11   1812     13       N  
ATOM    632  CA  GLY A  86      35.452 107.683  33.852  1.00 38.68           C  
ANISOU  632  CA  GLY A  86     8705   2377   3616    -29   1850     22       C  
ATOM    633  C   GLY A  86      35.840 106.242  33.582  1.00 38.37           C  
ANISOU  633  C   GLY A  86     8627   2362   3592    -22   1858     39       C  
ATOM    634  O   GLY A  86      37.027 105.908  33.531  1.00 38.26           O  
ANISOU  634  O   GLY A  86     8630   2367   3541    -41   1872     51       O  
ATOM    635  N   TRP A  87      34.847 105.369  33.405  1.00 37.82           N  
ANISOU  635  N   TRP A  87     8512   2284   3571      5   1854     37       N  
ATOM    636  CA  TRP A  87      35.138 103.975  33.089  1.00 37.65           C  
ANISOU  636  CA  TRP A  87     8463   2276   3565     12   1863     52       C  
ATOM    637  C   TRP A  87      35.574 103.809  31.639  1.00 37.54           C  
ANISOU  637  C   TRP A  87     8450   2268   3546     21   1830     56       C  
ATOM    638  O   TRP A  87      36.468 103.008  31.345  1.00 37.44           O  
ANISOU  638  O   TRP A  87     8439   2268   3518     23   1840     69       O  
ATOM    639  CB  TRP A  87      33.916 103.103  33.376  1.00 37.76           C  
ANISOU  639  CB  TRP A  87     8445   2274   3628     21   1877     44       C  
ATOM    640  CG  TRP A  87      33.746 102.759  34.822  1.00 37.87           C  
ANISOU  640  CG  TRP A  87     8461   2286   3641      8   1921     48       C  
ATOM    641  CD1 TRP A  87      34.410 103.307  35.877  1.00 37.89           C  
ANISOU  641  CD1 TRP A  87     8489   2297   3608     -8   1947     53       C  
ATOM    642  CD2 TRP A  87      32.860 101.775  35.371  1.00 38.05           C  
ANISOU  642  CD2 TRP A  87     8468   2293   3696      1   1950     45       C  
ATOM    643  NE1 TRP A  87      33.990 102.730  37.052  1.00 38.04           N  
ANISOU  643  NE1 TRP A  87     8507   2310   3637    -19   1989     57       N  
ATOM    644  CE2 TRP A  87      33.039 101.786  36.768  1.00 38.15           C  
ANISOU  644  CE2 TRP A  87     8496   2308   3691    -15   1991     52       C  
ATOM    645  CE3 TRP A  87      31.933 100.888  34.817  1.00 38.21           C  
ANISOU  645  CE3 TRP A  87     8471   2295   3752     -2   1950     34       C  
ATOM    646  CZ2 TRP A  87      32.325 100.946  37.619  1.00 38.40           C  
ANISOU  646  CZ2 TRP A  87     8526   2323   3741    -31   2030     53       C  
ATOM    647  CZ3 TRP A  87      31.224 100.054  35.664  1.00 38.49           C  
ANISOU  647  CZ3 TRP A  87     8508   2311   3803    -25   1991     31       C  
ATOM    648  CH2 TRP A  87      31.425 100.089  37.049  1.00 38.57           C  
ANISOU  648  CH2 TRP A  87     8534   2325   3797    -39   2030     42       C  
ATOM    649  N   SER A  88      34.963 104.563  30.723  1.00 37.63           N  
ANISOU  649  N   SER A  88     8467   2265   3567     31   1792     44       N  
ATOM    650  CA  SER A  88      35.272 104.409  29.305  1.00 37.58           C  
ANISOU  650  CA  SER A  88     8464   2260   3555     37   1762     47       C  
ATOM    651  C   SER A  88      36.687 104.880  28.991  1.00 37.51           C  
ANISOU  651  C   SER A  88     8495   2267   3490     14   1761     56       C  
ATOM    652  O   SER A  88      37.443 104.186  28.301  1.00 37.42           O  
ANISOU  652  O   SER A  88     8487   2266   3464     14   1763     64       O  
ATOM    653  CB  SER A  88      34.249 105.170  28.461  1.00 37.80           C  
ANISOU  653  CB  SER A  88     8499   2262   3600     58   1725     35       C  
ATOM    654  OG  SER A  88      32.991 104.519  28.476  1.00 37.93           O  
ANISOU  654  OG  SER A  88     8486   2262   3663     76   1730     21       O  
ATOM    655  N   TYR A  89      37.065 106.061  29.491  1.00 37.65           N  
ANISOU  655  N   TYR A  89     8553   2281   3470    -10   1764     53       N  
ATOM    656  CA  TYR A  89      38.384 106.601  29.177  1.00 37.70           C  
ANISOU  656  CA  TYR A  89     8612   2297   3415    -47   1768     57       C  
ATOM    657  C   TYR A  89      39.503 105.761  29.781  1.00 37.59           C  
ANISOU  657  C   TYR A  89     8603   2305   3374    -58   1808     67       C  
ATOM    658  O   TYR A  89      40.575 105.643  29.178  1.00 37.62           O  
ANISOU  658  O   TYR A  89     8640   2318   3337    -75   1813     72       O  
ATOM    659  CB  TYR A  89      38.492 108.052  29.647  1.00 38.00           C  
ANISOU  659  CB  TYR A  89     8703   2319   3415    -81   1767     46       C  
ATOM    660  CG  TYR A  89      37.793 109.040  28.737  1.00 38.27           C  
ANISOU  660  CG  TYR A  89     8763   2325   3455    -67   1725     42       C  
ATOM    661  CD1 TYR A  89      38.290 109.314  27.469  1.00 38.37           C  
ANISOU  661  CD1 TYR A  89     8809   2333   3437    -81   1699     47       C  
ATOM    662  CD2 TYR A  89      36.644 109.705  29.147  1.00 38.53           C  
ANISOU  662  CD2 TYR A  89     8794   2328   3517    -35   1714     35       C  
ATOM    663  CE1 TYR A  89      37.657 110.216  26.633  1.00 38.72           C  
ANISOU  663  CE1 TYR A  89     8886   2345   3481    -62   1661     48       C  
ATOM    664  CE2 TYR A  89      36.005 110.609  28.317  1.00 38.91           C  
ANISOU  664  CE2 TYR A  89     8876   2342   3566     -8   1678     36       C  
ATOM    665  CZ  TYR A  89      36.516 110.860  27.062  1.00 39.01           C  
ANISOU  665  CZ  TYR A  89     8923   2350   3547    -21   1650     44       C  
ATOM    666  OH  TYR A  89      35.882 111.760  26.235  1.00 39.47           O  
ANISOU  666  OH  TYR A  89     9026   2370   3603     11   1615     49       O  
ATOM    667  N   TYR A  90      39.285 105.171  30.958  1.00 37.54           N  
ANISOU  667  N   TYR A  90     8573   2303   3388    -46   1840     72       N  
ATOM    668  CA  TYR A  90      40.304 104.287  31.513  1.00 37.54           C  
ANISOU  668  CA  TYR A  90     8583   2318   3363    -40   1878     89       C  
ATOM    669  C   TYR A  90      40.414 103.003  30.703  1.00 37.47           C  
ANISOU  669  C   TYR A  90     8550   2309   3377      1   1876    102       C  
ATOM    670  O   TYR A  90      41.515 102.472  30.514  1.00 37.57           O  
ANISOU  670  O   TYR A  90     8591   2329   3355     13   1897    118       O  
ATOM    671  CB  TYR A  90      40.009 103.962  32.976  1.00 37.59           C  
ANISOU  671  CB  TYR A  90     8576   2324   3382    -35   1913     95       C  
ATOM    672  CG  TYR A  90      41.055 103.052  33.577  1.00 37.71           C  
ANISOU  672  CG  TYR A  90     8607   2350   3370    -18   1953    122       C  
ATOM    673  CD1 TYR A  90      42.308 103.542  33.919  1.00 37.90           C  
ANISOU  673  CD1 TYR A  90     8681   2389   3332    -51   1975    131       C  
ATOM    674  CD2 TYR A  90      40.801 101.703  33.783  1.00 37.74           C  
ANISOU  674  CD2 TYR A  90     8582   2349   3407     31   1967    143       C  
ATOM    675  CE1 TYR A  90      43.274 102.719  34.458  1.00 38.12           C  
ANISOU  675  CE1 TYR A  90     8719   2435   3332    -24   2009    168       C  
ATOM    676  CE2 TYR A  90      41.762 100.872  34.322  1.00 37.97           C  
ANISOU  676  CE2 TYR A  90     8633   2385   3410     63   2003    177       C  
ATOM    677  CZ  TYR A  90      42.997 101.385  34.658  1.00 38.16           C  
ANISOU  677  CZ  TYR A  90     8698   2431   3372     42   2022    194       C  
ATOM    678  OH  TYR A  90      43.955 100.559  35.195  1.00 38.50           O  
ANISOU  678  OH  TYR A  90     8752   2495   3382     85   2054    244       O  
ATOM    679  N   ALA A  91      39.280 102.487  30.222  1.00 37.38           N  
ANISOU  679  N   ALA A  91     8494   2288   3422     23   1853     96       N  
ATOM    680  CA  ALA A  91      39.295 101.246  29.455  1.00 37.40           C  
ANISOU  680  CA  ALA A  91     8480   2285   3446     54   1854    102       C  
ATOM    681  C   ALA A  91      40.108 101.396  28.177  1.00 37.42           C  
ANISOU  681  C   ALA A  91     8512   2290   3414     52   1839    101       C  
ATOM    682  O   ALA A  91      40.789 100.455  27.752  1.00 37.53           O  
ANISOU  682  O   ALA A  91     8541   2301   3417     79   1857    112       O  
ATOM    683  CB  ALA A  91      37.865 100.811  29.136  1.00 37.40           C  
ANISOU  683  CB  ALA A  91     8437   2269   3505     59   1835     88       C  
ATOM    684  N   ALA A  92      40.069 102.579  27.561  1.00 37.38           N  
ANISOU  684  N   ALA A  92     8528   2287   3390     21   1809     89       N  
ATOM    685  CA  ALA A  92      40.765 102.816  26.302  1.00 37.44           C  
ANISOU  685  CA  ALA A  92     8571   2295   3361      8   1793     87       C  
ATOM    686  C   ALA A  92      42.279 102.895  26.452  1.00 37.59           C  
ANISOU  686  C   ALA A  92     8646   2323   3313     -8   1825     98       C  
ATOM    687  O   ALA A  92      42.965 103.132  25.452  1.00 37.70           O  
ANISOU  687  O   ALA A  92     8701   2337   3288    -28   1819     96       O  
ATOM    688  CB  ALA A  92      40.250 104.100  25.655  1.00 37.49           C  
ANISOU  688  CB  ALA A  92     8592   2292   3359    -21   1753     75       C  
ATOM    689  N   THR A  93      42.816 102.712  27.658  1.00 37.66           N  
ANISOU  689  N   THR A  93     8664   2340   3305     -4   1862    110       N  
ATOM    690  CA  THR A  93      44.255 102.726  27.880  1.00 37.91           C  
ANISOU  690  CA  THR A  93     8750   2383   3270    -19   1897    127       C  
ATOM    691  C   THR A  93      44.849 101.333  28.040  1.00 38.08           C  
ANISOU  691  C   THR A  93     8775   2403   3291     50   1935    156       C  
ATOM    692  O   THR A  93      46.077 101.198  28.042  1.00 38.39           O  
ANISOU  692  O   THR A  93     8854   2463   3269     53   1964    184       O  
ATOM    693  CB  THR A  93      44.594 103.562  29.122  1.00 38.02           C  
ANISOU  693  CB  THR A  93     8782   2410   3253    -65   1915    128       C  
ATOM    694  OG1 THR A  93      43.745 103.172  30.209  1.00 37.89           O  
ANISOU  694  OG1 THR A  93     8723   2388   3284    -35   1925    131       O  
ATOM    695  CG2 THR A  93      44.400 105.040  28.842  1.00 38.06           C  
ANISOU  695  CG2 THR A  93     8815   2411   3235   -138   1887    101       C  
ATOM    696  N   ILE A  94      44.018 100.306  28.162  1.00 38.00           N  
ANISOU  696  N   ILE A  94     8723   2377   3339    102   1934    157       N  
ATOM    697  CA  ILE A  94      44.489  98.950  28.418  1.00 38.29           C  
ANISOU  697  CA  ILE A  94     8771   2402   3377    176   1972    186       C  
ATOM    698  C   ILE A  94      45.024  98.343  27.127  1.00 38.48           C  
ANISOU  698  C   ILE A  94     8826   2412   3383    208   1976    186       C  
ATOM    699  O   ILE A  94      44.491  98.585  26.036  1.00 38.31           O  
ANISOU  699  O   ILE A  94     8789   2385   3381    180   1942    158       O  
ATOM    700  CB  ILE A  94      43.354  98.110  29.033  1.00 38.25           C  
ANISOU  700  CB  ILE A  94     8715   2382   3436    201   1970    184       C  
ATOM    701  CG1 ILE A  94      43.043  98.624  30.441  1.00 38.17           C  
ANISOU  701  CG1 ILE A  94     8689   2383   3430    177   1979    191       C  
ATOM    702  CG2 ILE A  94      43.715  96.632  29.074  1.00 38.67           C  
ANISOU  702  CG2 ILE A  94     8787   2411   3494    277   2004    210       C  
ATOM    703  CD1 ILE A  94      41.613  98.433  30.868  1.00 38.01           C  
ANISOU  703  CD1 ILE A  94     8617   2354   3473    161   1962    174       C  
ATOM    704  N   ARG A  95      46.101  97.558  27.252  1.00 41.67           N  
ANISOU  704  N   ARG A  95     9278   2812   3743    274   2020    223       N  
ATOM    705  CA  ARG A  95      46.772  96.998  26.082  1.00 41.96           C  
ANISOU  705  CA  ARG A  95     9360   2834   3750    315   2035    226       C  
ATOM    706  C   ARG A  95      45.821  96.170  25.225  1.00 41.91           C  
ANISOU  706  C   ARG A  95     9321   2796   3808    331   2013    191       C  
ATOM    707  O   ARG A  95      45.821  96.287  23.995  1.00 41.88           O  
ANISOU  707  O   ARG A  95     9328   2786   3799    311   1996    167       O  
ATOM    708  CB  ARG A  95      47.961  96.146  26.526  1.00 42.57           C  
ANISOU  708  CB  ARG A  95     9488   2924   3764    409   2091    289       C  
ATOM    709  CG  ARG A  95      49.010  95.917  25.456  1.00 42.97           C  
ANISOU  709  CG  ARG A  95     9530   3053   3745    444   2093    282       C  
ATOM    710  CD  ARG A  95      49.657  94.549  25.616  1.00 43.68           C  
ANISOU  710  CD  ARG A  95     9615   3164   3816    581   2124    303       C  
ATOM    711  NE  ARG A  95      50.978  94.481  24.998  1.00 44.22           N  
ANISOU  711  NE  ARG A  95     9621   3393   3789    626   2120    294       N  
ATOM    712  CZ  ARG A  95      51.192  94.315  23.697  1.00 44.35           C  
ANISOU  712  CZ  ARG A  95     9636   3419   3796    630   2109    251       C  
ATOM    713  NH1 ARG A  95      52.432  94.262  23.228  1.00 44.92           N1+
ANISOU  713  NH1 ARG A  95     9642   3656   3772    672   2107    242       N1+
ATOM    714  NH2 ARG A  95      50.168  94.207  22.860  1.00 43.96           N  
ANISOU  714  NH2 ARG A  95     9647   3229   3827    590   2100    215       N  
ATOM    715  N   LYS A  96      44.998  95.331  25.856  1.00 39.47           N  
ANISOU  715  N   LYS A  96     8972   2473   3554    356   2014    193       N  
ATOM    716  CA  LYS A  96      44.155  94.401  25.115  1.00 39.59           C  
ANISOU  716  CA  LYS A  96     8960   2462   3621    360   2000    169       C  
ATOM    717  C   LYS A  96      42.851  95.018  24.624  1.00 39.15           C  
ANISOU  717  C   LYS A  96     8845   2417   3614    282   1950    135       C  
ATOM    718  O   LYS A  96      42.155  94.384  23.825  1.00 39.27           O  
ANISOU  718  O   LYS A  96     8844   2412   3665    272   1938    112       O  
ATOM    719  CB  LYS A  96      43.844  93.173  25.975  1.00 40.00           C  
ANISOU  719  CB  LYS A  96     9011   2487   3702    410   2027    189       C  
ATOM    720  CG  LYS A  96      45.038  92.271  26.229  1.00 40.66           C  
ANISOU  720  CG  LYS A  96     9161   2549   3740    516   2078    226       C  
ATOM    721  CD  LYS A  96      44.617  90.996  26.944  1.00 41.20           C  
ANISOU  721  CD  LYS A  96     9235   2580   3838    561   2101    244       C  
ATOM    722  CE  LYS A  96      45.767  90.006  27.031  1.00 42.02           C  
ANISOU  722  CE  LYS A  96     9413   2656   3896    687   2149    283       C  
ATOM    723  NZ  LYS A  96      45.349  88.705  27.623  1.00 42.69           N1+
ANISOU  723  NZ  LYS A  96     9517   2696   4008    730   2171    301       N1+
ATOM    724  N   VAL A  97      42.502  96.219  25.075  1.00 39.51           N  
ANISOU  724  N   VAL A  97     8865   2489   3659    231   1925    131       N  
ATOM    725  CA  VAL A  97      41.272  96.869  24.635  1.00 39.21           C  
ANISOU  725  CA  VAL A  97     8779   2457   3660    177   1880    104       C  
ATOM    726  C   VAL A  97      41.514  97.547  23.294  1.00 39.12           C  
ANISOU  726  C   VAL A  97     8789   2452   3624    151   1853     88       C  
ATOM    727  O   VAL A  97      42.549  98.190  23.082  1.00 39.13           O  
ANISOU  727  O   VAL A  97     8834   2463   3570    145   1860     96       O  
ATOM    728  CB  VAL A  97      40.784  97.874  25.694  1.00 38.93           C  
ANISOU  728  CB  VAL A  97     8717   2441   3632    145   1867    107       C  
ATOM    729  CG1 VAL A  97      39.598  98.672  25.173  1.00 38.72           C  
ANISOU  729  CG1 VAL A  97     8658   2417   3638    106   1824     84       C  
ATOM    730  CG2 VAL A  97      40.414  97.150  26.979  1.00 39.05           C  
ANISOU  730  CG2 VAL A  97     8715   2448   3673    165   1895    121       C  
ATOM    731  N   GLN A  98      40.555  97.401  22.376  1.00 40.05           N  
ANISOU  731  N   GLN A  98     8882   2558   3777    131   1826     65       N  
ATOM    732  CA  GLN A  98      40.660  97.996  21.050  1.00 40.03           C  
ANISOU  732  CA  GLN A  98     8902   2556   3752    107   1799     50       C  
ATOM    733  C   GLN A  98      39.440  98.805  20.628  1.00 39.89           C  
ANISOU  733  C   GLN A  98     8857   2538   3762     73   1756     35       C  
ATOM    734  O   GLN A  98      39.503  99.473  19.589  1.00 39.92           O  
ANISOU  734  O   GLN A  98     8886   2540   3740     54   1730     28       O  
ATOM    735  CB  GLN A  98      40.931  96.910  19.997  1.00 40.35           C  
ANISOU  735  CB  GLN A  98     8965   2574   3791    126   1816     35       C  
ATOM    736  CG  GLN A  98      40.012  95.705  20.089  1.00 40.58           C  
ANISOU  736  CG  GLN A  98     8965   2578   3875    134   1828     20       C  
ATOM    737  CD  GLN A  98      40.618  94.463  19.463  1.00 41.03           C  
ANISOU  737  CD  GLN A  98     9057   2608   3924    169   1860     10       C  
ATOM    738  OE1 GLN A  98      41.668  93.986  19.895  1.00 41.24           O  
ANISOU  738  OE1 GLN A  98     9117   2631   3923    220   1894     30       O  
ATOM    739  NE2 GLN A  98      39.958  93.933  18.440  1.00 41.27           N  
ANISOU  739  NE2 GLN A  98     9087   2617   3977    146   1854    -23       N  
ATOM    740  N   GLU A  99      38.344  98.775  21.385  1.00 41.55           N  
ANISOU  740  N   GLU A  99     9025   2745   4017     70   1750     31       N  
ATOM    741  CA  GLU A  99      37.187  99.608  21.089  1.00 41.53           C  
ANISOU  741  CA  GLU A  99     9007   2736   4036     53   1715     20       C  
ATOM    742  C   GLU A  99      36.407  99.848  22.372  1.00 41.44           C  
ANISOU  742  C   GLU A  99     8964   2727   4056     55   1719     24       C  
ATOM    743  O   GLU A  99      36.185  98.920  23.156  1.00 41.51           O  
ANISOU  743  O   GLU A  99     8951   2729   4090     60   1748     23       O  
ATOM    744  CB  GLU A  99      36.276  98.969  20.033  1.00 41.77           C  
ANISOU  744  CB  GLU A  99     9036   2743   4094     45   1707     -6       C  
ATOM    745  CG  GLU A  99      35.048  99.808  19.694  1.00 41.87           C  
ANISOU  745  CG  GLU A  99     9045   2741   4121     40   1675    -18       C  
ATOM    746  CD  GLU A  99      34.146  99.149  18.669  1.00 42.25           C  
ANISOU  746  CD  GLU A  99     9101   2762   4190     26   1675    -49       C  
ATOM    747  OE1 GLU A  99      34.480  98.038  18.205  1.00 42.43           O  
ANISOU  747  OE1 GLU A  99     9129   2777   4215     15   1699    -65       O  
ATOM    748  OE2 GLU A  99      33.099  99.741  18.327  1.00 42.48           O1+
ANISOU  748  OE2 GLU A  99     9139   2773   4227     29   1654    -62       O1+
ATOM    749  N   VAL A 100      35.995 101.097  22.578  1.00 37.96           N  
ANISOU  749  N   VAL A 100     8526   2288   3608     52   1694     27       N  
ATOM    750  CA  VAL A 100      35.217 101.497  23.744  1.00 37.94           C  
ANISOU  750  CA  VAL A 100     8501   2283   3631     56   1699     27       C  
ATOM    751  C   VAL A 100      33.958 102.205  23.262  1.00 38.16           C  
ANISOU  751  C   VAL A 100     8533   2288   3678     66   1670     13       C  
ATOM    752  O   VAL A 100      34.032 103.106  22.419  1.00 38.26           O  
ANISOU  752  O   VAL A 100     8578   2293   3666     73   1639     17       O  
ATOM    753  CB  VAL A 100      36.028 102.406  24.688  1.00 37.79           C  
ANISOU  753  CB  VAL A 100     8498   2283   3579     51   1704     43       C  
ATOM    754  CG1 VAL A 100      35.129 103.000  25.754  1.00 37.85           C  
ANISOU  754  CG1 VAL A 100     8489   2282   3609     56   1707     39       C  
ATOM    755  CG2 VAL A 100      37.167 101.625  25.328  1.00 37.68           C  
ANISOU  755  CG2 VAL A 100     8487   2286   3545     50   1740     57       C  
ATOM    756  N   ARG A 101      32.808 101.800  23.799  1.00 40.73           N  
ANISOU  756  N   ARG A 101     8836   2596   4042     69   1685     -3       N  
ATOM    757  CA  ARG A 101      31.513 102.340  23.388  1.00 41.06           C  
ANISOU  757  CA  ARG A 101     8890   2609   4101     89   1667    -21       C  
ATOM    758  C   ARG A 101      30.665 102.546  24.637  1.00 41.17           C  
ANISOU  758  C   ARG A 101     8890   2614   4139     97   1688    -30       C  
ATOM    759  O   ARG A 101      30.200 101.573  25.237  1.00 41.24           O  
ANISOU  759  O   ARG A 101     8878   2617   4173     75   1722    -43       O  
ATOM    760  CB  ARG A 101      30.820 101.398  22.402  1.00 41.32           C  
ANISOU  760  CB  ARG A 101     8928   2622   4151     75   1674    -48       C  
ATOM    761  CG  ARG A 101      30.147 102.083  21.223  1.00 41.67           C  
ANISOU  761  CG  ARG A 101     9009   2640   4183    101   1642    -60       C  
ATOM    762  CD  ARG A 101      30.797 101.693  19.897  1.00 41.65           C  
ANISOU  762  CD  ARG A 101     9027   2640   4158     84   1630    -61       C  
ATOM    763  NE  ARG A 101      31.876 102.604  19.523  1.00 41.45           N  
ANISOU  763  NE  ARG A 101     9025   2631   4092     93   1601    -30       N  
ATOM    764  CZ  ARG A 101      32.562 102.533  18.386  1.00 41.46           C  
ANISOU  764  CZ  ARG A 101     9055   2635   4063     81   1588    -26       C  
ATOM    765  NH1 ARG A 101      32.288 101.583  17.502  1.00 41.74           N1+
ANISOU  765  NH1 ARG A 101     9095   2658   4105     63   1599    -52       N1+
ATOM    766  NH2 ARG A 101      33.525 103.410  18.132  1.00 41.39           N  
ANISOU  766  NH2 ARG A 101     9076   2638   4011     79   1567     -1       N  
ATOM    767  N   GLY A 102      30.456 103.802  25.023  1.00 38.89           N  
ANISOU  767  N   GLY A 102     8620   2318   3839    127   1670    -23       N  
ATOM    768  CA  GLY A 102      29.727 104.125  26.234  1.00 39.04           C  
ANISOU  768  CA  GLY A 102     8632   2327   3876    140   1692    -33       C  
ATOM    769  C   GLY A 102      28.436 104.865  25.937  1.00 39.57           C  
ANISOU  769  C   GLY A 102     8726   2356   3953    191   1678    -56       C  
ATOM    770  O   GLY A 102      28.344 105.621  24.969  1.00 39.81           O  
ANISOU  770  O   GLY A 102     8791   2370   3964    228   1643    -51       O  
ATOM    771  N   TYR A 103      27.438 104.646  26.793  1.00 40.87           N  
ANISOU  771  N   TYR A 103     8882   2505   4141    199   1710    -83       N  
ATOM    772  CA  TYR A 103      26.117 105.239  26.633  1.00 41.49           C  
ANISOU  772  CA  TYR A 103     8990   2548   4227    260   1709   -117       C  
ATOM    773  C   TYR A 103      25.626 105.758  27.976  1.00 41.69           C  
ANISOU  773  C   TYR A 103     9014   2566   4261    282   1735   -132       C  
ATOM    774  O   TYR A 103      25.849 105.124  29.011  1.00 41.43           O  
ANISOU  774  O   TYR A 103     8954   2550   4239    232   1771   -131       O  
ATOM    775  CB  TYR A 103      25.117 104.221  26.072  1.00 41.83           C  
ANISOU  775  CB  TYR A 103     9034   2574   4286    245   1734   -162       C  
ATOM    776  CG  TYR A 103      25.604 103.510  24.832  1.00 41.65           C  
ANISOU  776  CG  TYR A 103     9013   2557   4256    209   1718   -154       C  
ATOM    777  CD1 TYR A 103      25.445 104.077  23.574  1.00 41.93           C  
ANISOU  777  CD1 TYR A 103     9085   2576   4270    255   1681   -155       C  
ATOM    778  CD2 TYR A 103      26.221 102.269  24.917  1.00 41.30           C  
ANISOU  778  CD2 TYR A 103     8939   2532   4222    136   1742   -146       C  
ATOM    779  CE1 TYR A 103      25.889 103.430  22.436  1.00 41.80           C  
ANISOU  779  CE1 TYR A 103     9075   2564   4245    220   1670   -153       C  
ATOM    780  CE2 TYR A 103      26.669 101.614  23.787  1.00 41.21           C  
ANISOU  780  CE2 TYR A 103     8932   2524   4203    108   1731   -145       C  
ATOM    781  CZ  TYR A 103      26.498 102.199  22.549  1.00 41.44           C  
ANISOU  781  CZ  TYR A 103     8995   2539   4212    145   1696   -150       C  
ATOM    782  OH  TYR A 103      26.939 101.552  21.418  1.00 41.39           O  
ANISOU  782  OH  TYR A 103     8997   2535   4195    114   1688   -153       O  
ATOM    783  N   THR A 104      24.957 106.910  27.956  1.00 43.58           N  
ANISOU  783  N   THR A 104     9289   2780   4491    364   1717   -147       N  
ATOM    784  CA  THR A 104      24.450 107.503  29.186  1.00 44.01           C  
ANISOU  784  CA  THR A 104     9346   2826   4550    397   1742   -169       C  
ATOM    785  C   THR A 104      23.191 108.309  28.902  1.00 45.62           C  
ANISOU  785  C   THR A 104     9587   3001   4748    509   1735   -214       C  
ATOM    786  O   THR A 104      22.987 108.808  27.791  1.00 46.21           O  
ANISOU  786  O   THR A 104     9696   3057   4804    573   1698   -208       O  
ATOM    787  CB  THR A 104      25.479 108.420  29.857  1.00 43.52           C  
ANISOU  787  CB  THR A 104     9295   2772   4470    383   1729   -132       C  
ATOM    788  OG1 THR A 104      26.803 108.054  29.451  1.00 42.88           O  
ANISOU  788  OG1 THR A 104     9199   2721   4374    316   1713    -91       O  
ATOM    789  CG2 THR A 104      25.371 108.302  31.365  1.00 43.48           C  
ANISOU  789  CG2 THR A 104     9271   2775   4474    356   1774   -148       C  
ATOM    790  N   LYS A 105      22.354 108.431  29.931  1.00 47.02           N  
ANISOU  790  N   LYS A 105     9756   3178   4932    543   1774   -262       N  
ATOM    791  CA  LYS A 105      21.226 109.348  29.903  1.00 48.82           C  
ANISOU  791  CA  LYS A 105    10014   3393   5144    674   1771   -313       C  
ATOM    792  C   LYS A 105      21.733 110.763  30.152  1.00 48.15           C  
ANISOU  792  C   LYS A 105     9968   3283   5045    728   1735   -274       C  
ATOM    793  O   LYS A 105      22.529 110.995  31.067  1.00 47.17           O  
ANISOU  793  O   LYS A 105     9837   3162   4925    664   1745   -247       O  
ATOM    794  CB  LYS A 105      20.189 108.956  30.958  1.00 50.33           C  
ANISOU  794  CB  LYS A 105    10176   3611   5337    689   1833   -392       C  
ATOM    795  CG  LYS A 105      18.762 109.376  30.620  1.00 53.49           C  
ANISOU  795  CG  LYS A 105    10506   4110   5708    808   1812   -449       C  
ATOM    796  CD  LYS A 105      17.854 109.407  31.849  1.00 54.86           C  
ANISOU  796  CD  LYS A 105    10593   4377   5873    824   1846   -507       C  
ATOM    797  CE  LYS A 105      17.655 108.032  32.467  1.00 55.16           C  
ANISOU  797  CE  LYS A 105    10543   4493   5922    684   1889   -528       C  
ATOM    798  NZ  LYS A 105      16.737 108.089  33.641  1.00 56.39           N1+
ANISOU  798  NZ  LYS A 105    10609   4753   6061    695   1921   -586       N1+
ATOM    799  N   GLY A 106      21.282 111.708  29.334  1.00 49.59           N  
ANISOU  799  N   GLY A 106    10199   3438   5204    844   1697   -273       N  
ATOM    800  CA  GLY A 106      21.772 113.069  29.434  1.00 49.94           C  
ANISOU  800  CA  GLY A 106    10297   3448   5229    887   1663   -235       C  
ATOM    801  C   GLY A 106      20.746 114.048  29.962  1.00 51.01           C  
ANISOU  801  C   GLY A 106    10461   3568   5353   1027   1669   -281       C  
ATOM    802  O   GLY A 106      20.080 113.781  30.967  1.00 51.20           O  
ANISOU  802  O   GLY A 106    10447   3620   5388   1045   1713   -338       O  
ATOM    803  N   GLY A 107      20.616 115.189  29.293  1.00 55.25           N  
ANISOU  803  N   GLY A 107    11068   4064   5862   1133   1627   -256       N  
ATOM    804  CA  GLY A 107      19.628 116.177  29.649  1.00 56.88           C  
ANISOU  804  CA  GLY A 107    11306   4256   6051   1292   1627   -296       C  
ATOM    805  C   GLY A 107      19.871 116.806  31.005  1.00 56.29           C  
ANISOU  805  C   GLY A 107    11235   4168   5984   1264   1653   -311       C  
ATOM    806  O   GLY A 107      20.983 116.785  31.541  1.00 54.63           O  
ANISOU  806  O   GLY A 107    11026   3948   5781   1127   1662   -277       O  
ATOM    807  N   PRO A 108      18.821 117.387  31.582  1.00 57.87           N  
ANISOU  807  N   PRO A 108    11437   4378   6175   1403   1668   -370       N  
ATOM    808  CA  PRO A 108      18.969 118.055  32.880  1.00 57.39           C  
ANISOU  808  CA  PRO A 108    11385   4302   6118   1387   1696   -393       C  
ATOM    809  C   PRO A 108      19.168 117.056  34.007  1.00 56.71           C  
ANISOU  809  C   PRO A 108    11222   4265   6058   1262   1750   -427       C  
ATOM    810  O   PRO A 108      18.574 115.976  34.019  1.00 57.28           O  
ANISOU  810  O   PRO A 108    11227   4397   6140   1253   1780   -470       O  
ATOM    811  CB  PRO A 108      17.646 118.817  33.042  1.00 59.50           C  
ANISOU  811  CB  PRO A 108    11661   4584   6363   1591   1697   -455       C  
ATOM    812  CG  PRO A 108      17.041 118.857  31.659  1.00 60.93           C  
ANISOU  812  CG  PRO A 108    11863   4769   6518   1722   1656   -440       C  
ATOM    813  CD  PRO A 108      17.485 117.593  31.003  1.00 60.45           C  
ANISOU  813  CD  PRO A 108    11759   4735   6473   1598   1658   -418       C  
ATOM    814  N   GLY A 109      20.017 117.431  34.961  1.00 56.92           N  
ANISOU  814  N   GLY A 109    11267   4269   6089   1164   1768   -410       N  
ATOM    815  CA  GLY A 109      20.183 116.647  36.168  1.00 55.91           C  
ANISOU  815  CA  GLY A 109    11080   4185   5979   1061   1821   -441       C  
ATOM    816  C   GLY A 109      21.249 115.575  36.080  1.00 54.86           C  
ANISOU  816  C   GLY A 109    10916   4069   5860    899   1828   -389       C  
ATOM    817  O   GLY A 109      21.875 115.234  37.089  1.00 54.68           O  
ANISOU  817  O   GLY A 109    10873   4062   5840    795   1864   -386       O  
ATOM    818  N   HIS A 110      21.471 115.040  34.884  1.00 52.29           N  
ANISOU  818  N   HIS A 110    10585   3744   5537    883   1796   -350       N  
ATOM    819  CA  HIS A 110      22.391 113.931  34.686  1.00 50.87           C  
ANISOU  819  CA  HIS A 110    10369   3590   5369    749   1801   -307       C  
ATOM    820  C   HIS A 110      23.702 114.413  34.074  1.00 50.34           C  
ANISOU  820  C   HIS A 110    10343   3503   5280    684   1764   -240       C  
ATOM    821  O   HIS A 110      23.750 115.433  33.382  1.00 50.89           O  
ANISOU  821  O   HIS A 110    10474   3534   5329    745   1727   -222       O  
ATOM    822  CB  HIS A 110      21.763 112.861  33.793  1.00 51.63           C  
ANISOU  822  CB  HIS A 110    10428   3710   5480    763   1799   -320       C  
ATOM    823  CG  HIS A 110      20.462 112.332  34.310  1.00 53.49           C  
ANISOU  823  CG  HIS A 110    10624   3978   5720    819   1846   -401       C  
ATOM    824  ND1 HIS A 110      20.149 112.309  35.652  1.00 54.04           N  
ANISOU  824  ND1 HIS A 110    10671   4072   5792    804   1896   -448       N  
ATOM    825  CD2 HIS A 110      19.390 111.813  33.665  1.00 55.25           C  
ANISOU  825  CD2 HIS A 110    10827   4230   5936    888   1856   -456       C  
ATOM    826  CE1 HIS A 110      18.943 111.793  35.811  1.00 55.92           C  
ANISOU  826  CE1 HIS A 110    10870   4358   6020    859   1937   -529       C  
ATOM    827  NE2 HIS A 110      18.461 111.484  34.621  1.00 57.01           N  
ANISOU  827  NE2 HIS A 110    11008   4504   6149    910   1916   -538       N  
ATOM    828  N   GLU A 111      24.769 113.665  34.344  1.00 47.65           N  
ANISOU  828  N   GLU A 111     9972   3194   4938    563   1779   -207       N  
ATOM    829  CA  GLU A 111      26.080 114.003  33.810  1.00 47.26           C  
ANISOU  829  CA  GLU A 111     9952   3145   4859    496   1753   -158       C  
ATOM    830  C   GLU A 111      26.139 113.709  32.315  1.00 47.10           C  
ANISOU  830  C   GLU A 111     9933   3126   4838    514   1710   -131       C  
ATOM    831  O   GLU A 111      25.625 112.692  31.844  1.00 46.83           O  
ANISOU  831  O   GLU A 111     9853   3111   4828    520   1711   -139       O  
ATOM    832  CB  GLU A 111      27.166 113.213  34.541  1.00 46.54           C  
ANISOU  832  CB  GLU A 111     9826   3098   4760    381   1785   -140       C  
ATOM    833  CG  GLU A 111      27.103 113.310  36.061  1.00 46.77           C  
ANISOU  833  CG  GLU A 111     9852   3130   4788    354   1835   -167       C  
ATOM    834  CD  GLU A 111      27.797 114.546  36.601  1.00 47.31           C  
ANISOU  834  CD  GLU A 111     9986   3172   4817    331   1841   -167       C  
ATOM    835  OE1 GLU A 111      28.186 114.538  37.790  1.00 47.29           O  
ANISOU  835  OE1 GLU A 111     9987   3181   4801    276   1884   -180       O  
ATOM    836  OE2 GLU A 111      27.960 115.522  35.838  1.00 47.46           O1+
ANISOU  836  OE2 GLU A 111    10063   3156   4814    363   1807   -155       O1+
ATOM    837  N   GLU A 112      26.767 114.612  31.567  1.00 45.39           N  
ANISOU  837  N   GLU A 112     9776   2884   4587    517   1676   -103       N  
ATOM    838  CA  GLU A 112      26.978 114.425  30.141  1.00 45.26           C  
ANISOU  838  CA  GLU A 112     9768   2868   4560    524   1636    -75       C  
ATOM    839  C   GLU A 112      28.445 114.102  29.868  1.00 44.54           C  
ANISOU  839  C   GLU A 112     9669   2812   4441    417   1634    -44       C  
ATOM    840  O   GLU A 112      29.332 114.587  30.577  1.00 44.46           O  
ANISOU  840  O   GLU A 112     9684   2806   4402    356   1654    -41       O  
ATOM    841  CB  GLU A 112      26.571 115.674  29.349  1.00 46.28           C  
ANISOU  841  CB  GLU A 112     9982   2940   4664    615   1600    -65       C  
ATOM    842  CG  GLU A 112      25.090 116.013  29.449  1.00 47.28           C  
ANISOU  842  CG  GLU A 112    10121   3034   4809    750   1598    -99       C  
ATOM    843  CD  GLU A 112      24.340 115.760  28.154  1.00 47.84           C  
ANISOU  843  CD  GLU A 112    10202   3096   4880    834   1565    -94       C  
ATOM    844  OE1 GLU A 112      23.149 116.132  28.070  1.00 48.48           O  
ANISOU  844  OE1 GLU A 112    10303   3154   4963    966   1560   -122       O  
ATOM    845  OE2 GLU A 112      24.942 115.194  27.218  1.00 47.59           O1+
ANISOU  845  OE2 GLU A 112    10158   3083   4841    776   1546    -65       O1+
ATOM    846  N   PRO A 113      28.727 113.280  28.856  1.00 41.65           N  
ANISOU  846  N   PRO A 113     9272   2472   4079    394   1616    -28       N  
ATOM    847  CA  PRO A 113      30.110 112.843  28.618  1.00 41.00           C  
ANISOU  847  CA  PRO A 113     9177   2431   3971    302   1618     -7       C  
ATOM    848  C   PRO A 113      31.061 114.013  28.403  1.00 41.32           C  
ANISOU  848  C   PRO A 113     9293   2451   3956    269   1607      7       C  
ATOM    849  O   PRO A 113      30.721 115.008  27.759  1.00 42.00           O  
ANISOU  849  O   PRO A 113     9447   2489   4022    318   1579     15       O  
ATOM    850  CB  PRO A 113      29.992 111.981  27.356  1.00 40.73           C  
ANISOU  850  CB  PRO A 113     9114   2413   3950    309   1594      3       C  
ATOM    851  CG  PRO A 113      28.585 111.497  27.363  1.00 40.99           C  
ANISOU  851  CG  PRO A 113     9120   2430   4025    376   1598    -19       C  
ATOM    852  CD  PRO A 113      27.774 112.618  27.948  1.00 41.74           C  
ANISOU  852  CD  PRO A 113     9261   2480   4119    450   1598    -35       C  
ATOM    853  N   MET A 114      32.262 113.881  28.959  1.00 42.05           N  
ANISOU  853  N   MET A 114     9384   2575   4018    185   1632     10       N  
ATOM    854  CA  MET A 114      33.313 114.874  28.792  1.00 42.35           C  
ANISOU  854  CA  MET A 114     9501   2598   3994    130   1632     17       C  
ATOM    855  C   MET A 114      34.181 114.538  27.586  1.00 42.08           C  
ANISOU  855  C   MET A 114     9473   2586   3930     90   1610     33       C  
ATOM    856  O   MET A 114      34.306 113.377  27.185  1.00 41.49           O  
ANISOU  856  O   MET A 114     9334   2553   3880     85   1608     38       O  
ATOM    857  CB  MET A 114      34.190 114.968  30.043  1.00 42.19           C  
ANISOU  857  CB  MET A 114     9489   2598   3943     56   1677      4       C  
ATOM    858  CG  MET A 114      33.590 115.790  31.171  1.00 42.72           C  
ANISOU  858  CG  MET A 114     9591   2627   4015     78   1701    -15       C  
ATOM    859  SD  MET A 114      34.834 116.763  32.045  1.00 43.09           S  
ANISOU  859  SD  MET A 114     9725   2662   3985    -23   1743    -29       S  
ATOM    860  CE  MET A 114      34.956 115.882  33.598  1.00 42.56           C  
ANISOU  860  CE  MET A 114     9596   2639   3936    -57   1796    -45       C  
ATOM    861  N   LEU A 115      34.786 115.574  27.014  1.00 41.46           N  
ANISOU  861  N   LEU A 115     9482   2476   3795     60   1598     41       N  
ATOM    862  CA  LEU A 115      35.687 115.441  25.876  1.00 41.34           C  
ANISOU  862  CA  LEU A 115     9491   2477   3740     13   1581     53       C  
ATOM    863  C   LEU A 115      37.105 115.701  26.368  1.00 41.30           C  
ANISOU  863  C   LEU A 115     9528   2492   3671    -90   1614     42       C  
ATOM    864  O   LEU A 115      37.445 116.832  26.730  1.00 41.92           O  
ANISOU  864  O   LEU A 115     9693   2534   3702   -130   1627     34       O  
ATOM    865  CB  LEU A 115      35.297 116.405  24.758  1.00 42.08           C  
ANISOU  865  CB  LEU A 115     9665   2516   3810     51   1542     70       C  
ATOM    866  CG  LEU A 115      33.890 116.203  24.190  1.00 42.28           C  
ANISOU  866  CG  LEU A 115     9662   2515   3886    158   1510     79       C  
ATOM    867  CD1 LEU A 115      33.650 117.138  23.018  1.00 43.08           C  
ANISOU  867  CD1 LEU A 115     9855   2561   3951    196   1473    101       C  
ATOM    868  CD2 LEU A 115      33.670 114.753  23.783  1.00 41.52           C  
ANISOU  868  CD2 LEU A 115     9471   2469   3835    168   1507     78       C  
ATOM    869  N   VAL A 116      37.924 114.651  26.392  1.00 40.65           N  
ANISOU  869  N   VAL A 116     9395   2465   3587   -133   1632     40       N  
ATOM    870  CA  VAL A 116      39.295 114.719  26.884  1.00 40.62           C  
ANISOU  870  CA  VAL A 116     9427   2485   3520   -228   1668     26       C  
ATOM    871  C   VAL A 116      40.183 113.941  25.921  1.00 40.28           C  
ANISOU  871  C   VAL A 116     9371   2478   3456   -260   1662     32       C  
ATOM    872  O   VAL A 116      39.736 113.003  25.254  1.00 39.87           O  
ANISOU  872  O   VAL A 116     9256   2444   3450   -207   1642     45       O  
ATOM    873  CB  VAL A 116      39.414 114.169  28.328  1.00 40.27           C  
ANISOU  873  CB  VAL A 116     9338   2469   3492   -239   1712     14       C  
ATOM    874  CG1 VAL A 116      40.838 114.283  28.852  1.00 40.35           C  
ANISOU  874  CG1 VAL A 116     9398   2502   3430   -339   1753     -3       C  
ATOM    875  CG2 VAL A 116      38.466 114.906  29.255  1.00 40.63           C  
ANISOU  875  CG2 VAL A 116     9398   2479   3562   -204   1719      6       C  
ATOM    876  N   GLN A 117      41.446 114.351  25.834  1.00 40.54           N  
ANISOU  876  N   GLN A 117     9471   2519   3414   -353   1682     20       N  
ATOM    877  CA  GLN A 117      42.428 113.722  24.959  1.00 40.36           C  
ANISOU  877  CA  GLN A 117     9450   2527   3359   -394   1681     22       C  
ATOM    878  C   GLN A 117      43.396 112.835  25.736  1.00 40.01           C  
ANISOU  878  C   GLN A 117     9376   2526   3301   -431   1724     13       C  
ATOM    879  O   GLN A 117      44.605 112.852  25.497  1.00 40.21           O  
ANISOU  879  O   GLN A 117     9442   2570   3266   -511   1741      4       O  
ATOM    880  CB  GLN A 117      43.196 114.776  24.167  1.00 41.03           C  
ANISOU  880  CB  GLN A 117     9635   2589   3365   -480   1671     15       C  
ATOM    881  CG  GLN A 117      42.308 115.699  23.358  1.00 41.53           C  
ANISOU  881  CG  GLN A 117     9745   2600   3434   -440   1629     31       C  
ATOM    882  CD  GLN A 117      43.094 116.764  22.627  1.00 42.31           C  
ANISOU  882  CD  GLN A 117     9954   2672   3449   -533   1621     25       C  
ATOM    883  OE1 GLN A 117      44.275 116.587  22.331  1.00 42.36           O  
ANISOU  883  OE1 GLN A 117     9986   2710   3401   -626   1636     12       O  
ATOM    884  NE2 GLN A 117      42.443 117.884  22.336  1.00 43.01           N  
ANISOU  884  NE2 GLN A 117    10115   2700   3526   -511   1599     35       N  
ATOM    885  N   SER A 118      42.878 112.050  26.678  1.00 39.58           N  
ANISOU  885  N   SER A 118     9251   2486   3300   -374   1743     17       N  
ATOM    886  CA  SER A 118      43.703 111.055  27.342  1.00 39.29           C  
ANISOU  886  CA  SER A 118     9185   2485   3257   -386   1781     17       C  
ATOM    887  C   SER A 118      44.126 109.979  26.341  1.00 39.02           C  
ANISOU  887  C   SER A 118     9121   2472   3232   -357   1774     33       C  
ATOM    888  O   SER A 118      43.611 109.895  25.222  1.00 38.96           O  
ANISOU  888  O   SER A 118     9103   2453   3245   -324   1740     40       O  
ATOM    889  CB  SER A 118      42.957 110.440  28.525  1.00 38.96           C  
ANISOU  889  CB  SER A 118     9081   2449   3272   -327   1801     22       C  
ATOM    890  OG  SER A 118      41.674 109.981  28.139  1.00 38.67           O  
ANISOU  890  OG  SER A 118     8980   2404   3309   -245   1770     34       O  
ATOM    891  N   TYR A 119      45.087 109.152  26.753  1.00 38.94           N  
ANISOU  891  N   TYR A 119     9100   2492   3203   -369   1809     41       N  
ATOM    892  CA  TYR A 119      45.636 108.148  25.849  1.00 38.82           C  
ANISOU  892  CA  TYR A 119     9070   2495   3185   -342   1811     59       C  
ATOM    893  C   TYR A 119      44.544 107.199  25.373  1.00 38.41           C  
ANISOU  893  C   TYR A 119     8958   2430   3207   -247   1793     66       C  
ATOM    894  O   TYR A 119      43.779 106.658  26.174  1.00 38.16           O  
ANISOU  894  O   TYR A 119     8873   2396   3229   -194   1800     70       O  
ATOM    895  CB  TYR A 119      46.754 107.361  26.532  1.00 38.91           C  
ANISOU  895  CB  TYR A 119     9065   2552   3166   -348   1853     83       C  
ATOM    896  CG  TYR A 119      47.406 106.338  25.628  1.00 38.92           C  
ANISOU  896  CG  TYR A 119     9054   2582   3151   -313   1861    108       C  
ATOM    897  CD1 TYR A 119      48.362 106.718  24.694  1.00 39.28           C  
ANISOU  897  CD1 TYR A 119     9118   2679   3127   -381   1852    115       C  
ATOM    898  CD2 TYR A 119      47.062 104.995  25.704  1.00 38.66           C  
ANISOU  898  CD2 TYR A 119     8988   2535   3166   -214   1880    125       C  
ATOM    899  CE1 TYR A 119      48.958 105.788  23.863  1.00 39.35           C  
ANISOU  899  CE1 TYR A 119     9109   2736   3108   -343   1863    137       C  
ATOM    900  CE2 TYR A 119      47.653 104.059  24.877  1.00 38.77           C  
ANISOU  900  CE2 TYR A 119     9004   2569   3158   -174   1895    147       C  
ATOM    901  CZ  TYR A 119      48.600 104.461  23.959  1.00 39.10           C  
ANISOU  901  CZ  TYR A 119     9060   2674   3123   -235   1888    153       C  
ATOM    902  OH  TYR A 119      49.190 103.530  23.134  1.00 39.27           O  
ANISOU  902  OH  TYR A 119     9075   2740   3108   -188   1906    170       O  
ATOM    903  N   GLY A 120      44.469 107.012  24.059  1.00 38.42           N  
ANISOU  903  N   GLY A 120     8966   2424   3207   -237   1768     68       N  
ATOM    904  CA  GLY A 120      43.488 106.122  23.472  1.00 38.14           C  
ANISOU  904  CA  GLY A 120     8874   2380   3237   -166   1749     72       C  
ATOM    905  C   GLY A 120      42.127 106.726  23.224  1.00 38.10           C  
ANISOU  905  C   GLY A 120     8841   2357   3278   -145   1706     67       C  
ATOM    906  O   GLY A 120      41.160 105.978  23.046  1.00 37.90           O  
ANISOU  906  O   GLY A 120     8760   2328   3313    -93   1694     68       O  
ATOM    907  N   TRP A 121      42.017 108.057  23.198  1.00 38.38           N  
ANISOU  907  N   TRP A 121     8922   2377   3284   -184   1686     63       N  
ATOM    908  CA  TRP A 121      40.717 108.691  23.021  1.00 38.48           C  
ANISOU  908  CA  TRP A 121     8920   2364   3336   -149   1649     64       C  
ATOM    909  C   TRP A 121      40.120 108.436  21.644  1.00 38.52           C  
ANISOU  909  C   TRP A 121     8919   2357   3361   -120   1614     69       C  
ATOM    910  O   TRP A 121      38.914 108.631  21.462  1.00 38.60           O  
ANISOU  910  O   TRP A 121     8908   2346   3414    -75   1587     71       O  
ATOM    911  CB  TRP A 121      40.822 110.199  23.264  1.00 38.93           C  
ANISOU  911  CB  TRP A 121     9045   2397   3349   -192   1639     60       C  
ATOM    912  CG  TRP A 121      41.599 110.942  22.212  1.00 39.33           C  
ANISOU  912  CG  TRP A 121     9175   2437   3334   -251   1624     60       C  
ATOM    913  CD1 TRP A 121      42.930 111.238  22.236  1.00 39.55           C  
ANISOU  913  CD1 TRP A 121     9260   2478   3291   -334   1647     51       C  
ATOM    914  CD2 TRP A 121      41.089 111.490  20.988  1.00 39.66           C  
ANISOU  914  CD2 TRP A 121     9251   2449   3368   -237   1582     71       C  
ATOM    915  NE1 TRP A 121      43.282 111.931  21.103  1.00 39.99           N  
ANISOU  915  NE1 TRP A 121     9382   2516   3296   -380   1623     55       N  
ATOM    916  CE2 TRP A 121      42.170 112.099  20.321  1.00 40.05           C  
ANISOU  916  CE2 TRP A 121     9380   2497   3342   -317   1583     69       C  
ATOM    917  CE3 TRP A 121      39.824 111.522  20.392  1.00 39.73           C  
ANISOU  917  CE3 TRP A 121     9239   2433   3424   -167   1547     82       C  
ATOM    918  CZ2 TRP A 121      42.027 112.732  19.089  1.00 40.50           C  
ANISOU  918  CZ2 TRP A 121     9493   2526   3368   -328   1547     81       C  
ATOM    919  CZ3 TRP A 121      39.684 112.151  19.167  1.00 40.18           C  
ANISOU  919  CZ3 TRP A 121     9355   2460   3451   -170   1513     95       C  
ATOM    920  CH2 TRP A 121      40.780 112.747  18.530  1.00 40.55           C  
ANISOU  920  CH2 TRP A 121     9480   2505   3422   -249   1513     96       C  
ATOM    921  N   ASN A 122      40.927 108.005  20.673  1.00 38.54           N  
ANISOU  921  N   ASN A 122     8947   2368   3328   -144   1617     70       N  
ATOM    922  CA  ASN A 122      40.403 107.762  19.336  1.00 38.63           C  
ANISOU  922  CA  ASN A 122     8962   2365   3350   -123   1588     74       C  
ATOM    923  C   ASN A 122      39.529 106.518  19.265  1.00 38.35           C  
ANISOU  923  C   ASN A 122     8857   2333   3382    -68   1591     68       C  
ATOM    924  O   ASN A 122      38.738 106.386  18.325  1.00 38.48           O  
ANISOU  924  O   ASN A 122     8871   2331   3417    -45   1566     67       O  
ATOM    925  CB  ASN A 122      41.548 107.647  18.324  1.00 38.78           C  
ANISOU  925  CB  ASN A 122     9037   2391   3307   -171   1595     75       C  
ATOM    926  CG  ASN A 122      42.724 106.847  18.851  1.00 38.62           C  
ANISOU  926  CG  ASN A 122     9014   2397   3262   -190   1642     70       C  
ATOM    927  OD1 ASN A 122      43.186 107.063  19.970  1.00 38.57           O  
ANISOU  927  OD1 ASN A 122     9008   2403   3245   -207   1666     69       O  
ATOM    928  ND2 ASN A 122      43.217 105.916  18.040  1.00 38.60           N  
ANISOU  928  ND2 ASN A 122     9019   2399   3248   -183   1658     69       N  
ATOM    929  N   ILE A 123      39.636 105.608  20.231  1.00 38.06           N  
ANISOU  929  N   ILE A 123     8771   2315   3377    -52   1624     64       N  
ATOM    930  CA  ILE A 123      38.877 104.362  20.164  1.00 37.91           C  
ANISOU  930  CA  ILE A 123     8695   2295   3415    -14   1631     55       C  
ATOM    931  C   ILE A 123      37.641 104.477  21.050  1.00 37.87           C  
ANISOU  931  C   ILE A 123     8644   2281   3463     12   1625     52       C  
ATOM    932  O   ILE A 123      36.932 103.490  21.289  1.00 37.80           O  
ANISOU  932  O   ILE A 123     8590   2270   3502     32   1637     42       O  
ATOM    933  CB  ILE A 123      39.742 103.151  20.567  1.00 37.77           C  
ANISOU  933  CB  ILE A 123     8662   2292   3395     -7   1674     56       C  
ATOM    934  CG1 ILE A 123      39.884 103.056  22.091  1.00 37.62           C  
ANISOU  934  CG1 ILE A 123     8619   2287   3389      0   1701     63       C  
ATOM    935  CG2 ILE A 123      41.109 103.233  19.908  1.00 37.89           C  
ANISOU  935  CG2 ILE A 123     8738   2314   3346    -33   1689     60       C  
ATOM    936  CD1 ILE A 123      40.606 101.810  22.553  1.00 37.60           C  
ANISOU  936  CD1 ILE A 123     8609   2291   3387     24   1743     69       C  
ATOM    937  N   VAL A 124      37.360 105.693  21.519  1.00 38.00           N  
ANISOU  937  N   VAL A 124     8682   2289   3469     10   1608     57       N  
ATOM    938  CA  VAL A 124      36.229 105.960  22.400  1.00 38.05           C  
ANISOU  938  CA  VAL A 124     8658   2282   3518     37   1606     53       C  
ATOM    939  C   VAL A 124      35.104 106.595  21.593  1.00 38.40           C  
ANISOU  939  C   VAL A 124     8724   2294   3575     69   1570     51       C  
ATOM    940  O   VAL A 124      35.335 107.526  20.810  1.00 38.69           O  
ANISOU  940  O   VAL A 124     8815   2312   3572     66   1544     61       O  
ATOM    941  CB  VAL A 124      36.640 106.863  23.574  1.00 38.08           C  
ANISOU  941  CB  VAL A 124     8680   2290   3498     20   1619     57       C  
ATOM    942  CG1 VAL A 124      35.425 107.235  24.400  1.00 38.22           C  
ANISOU  942  CG1 VAL A 124     8677   2288   3556     52   1617     50       C  
ATOM    943  CG2 VAL A 124      37.670 106.172  24.433  1.00 37.81           C  
ANISOU  943  CG2 VAL A 124     8632   2284   3449     -4   1659     59       C  
ATOM    944  N   ARG A 125      33.886 106.089  21.783  1.00 41.32           N  
ANISOU  944  N   ARG A 125     9058   2648   3992    101   1573     38       N  
ATOM    945  CA  ARG A 125      32.679 106.639  21.167  1.00 41.76           C  
ANISOU  945  CA  ARG A 125     9139   2667   4060    145   1546     33       C  
ATOM    946  C   ARG A 125      31.618 106.757  22.256  1.00 41.90           C  
ANISOU  946  C   ARG A 125     9134   2671   4116    177   1561     20       C  
ATOM    947  O   ARG A 125      31.000 105.759  22.639  1.00 41.82           O  
ANISOU  947  O   ARG A 125     9082   2663   4142    173   1586      1       O  
ATOM    948  CB  ARG A 125      32.187 105.760  20.024  1.00 41.86           C  
ANISOU  948  CB  ARG A 125     9149   2669   4086    149   1542     19       C  
ATOM    949  CG  ARG A 125      31.903 106.487  18.723  1.00 42.35           C  
ANISOU  949  CG  ARG A 125     9274   2701   4117    175   1506     28       C  
ATOM    950  CD  ARG A 125      30.990 107.692  18.899  1.00 43.13           C  
ANISOU  950  CD  ARG A 125     9415   2762   4211    237   1483     36       C  
ATOM    951  NE  ARG A 125      30.678 108.308  17.610  1.00 43.99           N  
ANISOU  951  NE  ARG A 125     9592   2836   4285    273   1449     49       N  
ATOM    952  CZ  ARG A 125      30.365 109.588  17.446  1.00 44.54           C  
ANISOU  952  CZ  ARG A 125     9728   2870   4327    326   1420     71       C  
ATOM    953  NH1 ARG A 125      30.096 110.056  16.235  1.00 44.90           N1+
ANISOU  953  NH1 ARG A 125     9843   2881   4336    362   1389     89       N1+
ATOM    954  NH2 ARG A 125      30.332 110.404  18.491  1.00 44.55           N  
ANISOU  954  NH2 ARG A 125     9733   2863   4332    344   1424     76       N  
ATOM    955  N   LEU A 126      31.404 107.973  22.747  1.00 39.62           N  
ANISOU  955  N   LEU A 126     8880   2362   3814    206   1549     28       N  
ATOM    956  CA  LEU A 126      30.409 108.238  23.777  1.00 39.86           C  
ANISOU  956  CA  LEU A 126     8898   2374   3873    243   1564     13       C  
ATOM    957  C   LEU A 126      29.148 108.811  23.145  1.00 40.51           C  
ANISOU  957  C   LEU A 126     9021   2411   3961    319   1542      4       C  
ATOM    958  O   LEU A 126      29.220 109.654  22.245  1.00 40.89           O  
ANISOU  958  O   LEU A 126     9127   2434   3976    350   1508     21       O  
ATOM    959  CB  LEU A 126      30.961 109.203  24.828  1.00 39.88           C  
ANISOU  959  CB  LEU A 126     8920   2378   3855    232   1572     22       C  
ATOM    960  CG  LEU A 126      32.266 108.746  25.484  1.00 39.35           C  
ANISOU  960  CG  LEU A 126     8828   2353   3770    164   1598     29       C  
ATOM    961  CD1 LEU A 126      32.721 109.729  26.551  1.00 39.48           C  
ANISOU  961  CD1 LEU A 126     8875   2364   3760    148   1612     30       C  
ATOM    962  CD2 LEU A 126      32.111 107.348  26.063  1.00 38.97           C  
ANISOU  962  CD2 LEU A 126     8717   2330   3758    146   1630     19       C  
ATOM    963  N   LYS A 127      27.993 108.346  23.617  1.00 40.63           N  
ANISOU  963  N   LYS A 127     9014   2413   4011    352   1563    -25       N  
ATOM    964  CA  LYS A 127      26.706 108.774  23.084  1.00 41.35           C  
ANISOU  964  CA  LYS A 127     9146   2463   4103    439   1550    -45       C  
ATOM    965  C   LYS A 127      25.766 109.088  24.237  1.00 41.71           C  
ANISOU  965  C   LYS A 127     9185   2494   4171    488   1575    -74       C  
ATOM    966  O   LYS A 127      25.563 108.250  25.122  1.00 41.43           O  
ANISOU  966  O   LYS A 127     9101   2478   4164    446   1614    -97       O  
ATOM    967  CB  LYS A 127      26.101 107.701  22.171  1.00 41.42           C  
ANISOU  967  CB  LYS A 127     9147   2469   4124    431   1558    -73       C  
ATOM    968  CG  LYS A 127      25.131 108.252  21.136  1.00 42.20           C  
ANISOU  968  CG  LYS A 127     9309   2527   4200    526   1534    -86       C  
ATOM    969  CD  LYS A 127      24.999 107.322  19.937  1.00 42.21           C  
ANISOU  969  CD  LYS A 127     9317   2528   4193    496   1535   -106       C  
ATOM    970  CE  LYS A 127      24.134 106.114  20.254  1.00 42.28           C  
ANISOU  970  CE  LYS A 127     9291   2544   4230    462   1584   -171       C  
ATOM    971  NZ  LYS A 127      23.980 105.219  19.072  1.00 42.40           N1+
ANISOU  971  NZ  LYS A 127     9321   2556   4232    424   1591   -204       N1+
ATOM    972  N   SER A 128      25.198 110.291  24.223  1.00 42.71           N  
ANISOU  972  N   SER A 128     9365   2584   4279    582   1554    -73       N  
ATOM    973  CA  SER A 128      24.285 110.748  25.256  1.00 43.20           C  
ANISOU  973  CA  SER A 128     9430   2631   4355    649   1576   -106       C  
ATOM    974  C   SER A 128      22.842 110.617  24.775  1.00 43.98           C  
ANISOU  974  C   SER A 128     9546   2711   4452    755   1583   -156       C  
ATOM    975  O   SER A 128      22.567 110.241  23.633  1.00 44.14           O  
ANISOU  975  O   SER A 128     9587   2727   4459    776   1568   -162       O  
ATOM    976  CB  SER A 128      24.606 112.191  25.652  1.00 43.63           C  
ANISOU  976  CB  SER A 128     9535   2657   4384    693   1556    -82       C  
ATOM    977  OG  SER A 128      23.632 112.701  26.547  1.00 44.26           O  
ANISOU  977  OG  SER A 128     9623   2719   4474    777   1575   -119       O  
ATOM    978  N   GLY A 129      21.904 110.938  25.666  1.00 44.78           N  
ANISOU  978  N   GLY A 129     9644   2810   4560    830   1609   -202       N  
ATOM    979  CA  GLY A 129      20.496 110.805  25.352  1.00 45.62           C  
ANISOU  979  CA  GLY A 129     9759   2923   4651    946   1626   -272       C  
ATOM    980  C   GLY A 129      19.992 109.384  25.268  1.00 45.39           C  
ANISOU  980  C   GLY A 129     9613   3001   4634    856   1647   -313       C  
ATOM    981  O   GLY A 129      18.853 109.170  24.843  1.00 46.13           O  
ANISOU  981  O   GLY A 129     9600   3226   4702    902   1626   -352       O  
ATOM    982  N   VAL A 130      20.800 108.407  25.665  1.00 48.36           N  
ANISOU  982  N   VAL A 130     9997   3336   5040    724   1687   -305       N  
ATOM    983  CA  VAL A 130      20.439 106.999  25.561  1.00 48.79           C  
ANISOU  983  CA  VAL A 130     9956   3477   5105    621   1709   -337       C  
ATOM    984  C   VAL A 130      19.866 106.533  26.891  1.00 49.02           C  
ANISOU  984  C   VAL A 130     9917   3559   5148    580   1756   -379       C  
ATOM    985  O   VAL A 130      20.423 106.825  27.956  1.00 47.56           O  
ANISOU  985  O   VAL A 130     9784   3303   4983    567   1787   -365       O  
ATOM    986  CB  VAL A 130      21.657 106.150  25.160  1.00 46.69           C  
ANISOU  986  CB  VAL A 130     9748   3133   4860    513   1726   -301       C  
ATOM    987  CG1 VAL A 130      21.292 104.674  25.130  1.00 47.03           C  
ANISOU  987  CG1 VAL A 130     9713   3243   4914    406   1758   -336       C  
ATOM    988  CG2 VAL A 130      22.195 106.601  23.810  1.00 46.53           C  
ANISOU  988  CG2 VAL A 130     9771   3090   4818    544   1675   -260       C  
ATOM    989  N   ASP A 131      18.743 105.821  26.832  1.00 52.79           N  
ANISOU  989  N   ASP A 131    10277   4172   5610    552   1762   -432       N  
ATOM    990  CA  ASP A 131      18.175 105.128  27.982  1.00 53.32           C  
ANISOU  990  CA  ASP A 131    10271   4304   5683    481   1811   -473       C  
ATOM    991  C   ASP A 131      18.389 103.636  27.757  1.00 52.89           C  
ANISOU  991  C   ASP A 131    10199   4256   5642    335   1844   -479       C  
ATOM    992  O   ASP A 131      17.723 103.029  26.911  1.00 54.91           O  
ANISOU  992  O   ASP A 131    10386   4605   5874    299   1831   -513       O  
ATOM    993  CB  ASP A 131      16.695 105.462  28.159  1.00 56.55           C  
ANISOU  993  CB  ASP A 131    10558   4874   6054    551   1798   -536       C  
ATOM    994  CG  ASP A 131      16.093 104.805  29.386  1.00 57.64           C  
ANISOU  994  CG  ASP A 131    10620   5088   6192    470   1850   -580       C  
ATOM    995  OD1 ASP A 131      16.846 104.521  30.342  1.00 55.58           O  
ANISOU  995  OD1 ASP A 131    10420   4736   5963    404   1892   -555       O  
ATOM    996  OD2 ASP A 131      14.865 104.573  29.396  1.00 60.43           O1+
ANISOU  996  OD2 ASP A 131    10849   5604   6506    471   1850   -641       O1+
ATOM    997  N   VAL A 132      19.319 103.050  28.517  1.00 51.49           N  
ANISOU  997  N   VAL A 132    10088   3980   5497    254   1887   -447       N  
ATOM    998  CA  VAL A 132      19.778 101.693  28.239  1.00 51.16           C  
ANISOU  998  CA  VAL A 132    10066   3903   5468    132   1919   -439       C  
ATOM    999  C   VAL A 132      18.687 100.649  28.444  1.00 51.83           C  
ANISOU  999  C   VAL A 132    10060   4099   5534     36   1951   -497       C  
ATOM   1000  O   VAL A 132      18.806  99.531  27.929  1.00 51.84           O  
ANISOU 1000  O   VAL A 132    10073   4086   5537    -61   1973   -505       O  
ATOM   1001  CB  VAL A 132      21.013 101.366  29.099  1.00 50.37           C  
ANISOU 1001  CB  VAL A 132    10056   3682   5400     87   1957   -387       C  
ATOM   1002  CG1 VAL A 132      22.166 102.292  28.739  1.00 49.77           C  
ANISOU 1002  CG1 VAL A 132    10027   3554   5330    153   1911   -322       C  
ATOM   1003  CG2 VAL A 132      20.678 101.474  30.577  1.00 50.50           C  
ANISOU 1003  CG2 VAL A 132    10047   3723   5418     74   1995   -398       C  
ATOM   1004  N   PHE A 133      17.622 100.976  29.181  1.00 52.36           N  
ANISOU 1004  N   PHE A 133    10038   4277   5578     56   1959   -542       N  
ATOM   1005  CA  PHE A 133      16.513 100.036  29.311  1.00 54.42           C  
ANISOU 1005  CA  PHE A 133    10204   4665   5808    -46   1989   -603       C  
ATOM   1006  C   PHE A 133      15.809  99.831  27.976  1.00 56.74           C  
ANISOU 1006  C   PHE A 133    10429   5063   6065    -51   1955   -645       C  
ATOM   1007  O   PHE A 133      15.466  98.698  27.615  1.00 57.63           O  
ANISOU 1007  O   PHE A 133    10518   5216   6162   -177   1983   -678       O  
ATOM   1008  CB  PHE A 133      15.526 100.526  30.370  1.00 56.38           C  
ANISOU 1008  CB  PHE A 133    10361   5031   6031    -16   2001   -647       C  
ATOM   1009  CG  PHE A 133      16.084 100.527  31.763  1.00 55.10           C  
ANISOU 1009  CG  PHE A 133    10251   4789   5895    -41   2044   -616       C  
ATOM   1010  CD1 PHE A 133      16.229  99.343  32.465  1.00 54.49           C  
ANISOU 1010  CD1 PHE A 133    10196   4683   5823   -180   2102   -610       C  
ATOM   1011  CD2 PHE A 133      16.457 101.712  32.374  1.00 54.18           C  
ANISOU 1011  CD2 PHE A 133    10167   4627   5792     72   2028   -594       C  
ATOM   1012  CE1 PHE A 133      16.742  99.339  33.747  1.00 52.99           C  
ANISOU 1012  CE1 PHE A 133    10051   4432   5650   -201   2139   -578       C  
ATOM   1013  CE2 PHE A 133      16.969 101.715  33.657  1.00 52.68           C  
ANISOU 1013  CE2 PHE A 133    10019   4379   5620     43   2067   -569       C  
ATOM   1014  CZ  PHE A 133      17.111 100.527  34.344  1.00 52.17           C  
ANISOU 1014  CZ  PHE A 133     9966   4298   5558    -91   2121   -559       C  
ATOM   1015  N   HIS A 134      15.590 100.914  27.228  1.00 55.05           N  
ANISOU 1015  N   HIS A 134    10189   4892   5834     82   1895   -642       N  
ATOM   1016  CA  HIS A 134      14.992 100.853  25.900  1.00 56.71           C  
ANISOU 1016  CA  HIS A 134    10335   5207   6004     96   1855   -673       C  
ATOM   1017  C   HIS A 134      16.028 100.620  24.807  1.00 54.79           C  
ANISOU 1017  C   HIS A 134    10185   4849   5783     83   1835   -628       C  
ATOM   1018  O   HIS A 134      15.809 101.016  23.653  1.00 56.09           O  
ANISOU 1018  O   HIS A 134    10323   5070   5918    143   1786   -631       O  
ATOM   1019  CB  HIS A 134      14.202 102.134  25.621  1.00 59.16           C  
ANISOU 1019  CB  HIS A 134    10573   5628   6276    259   1799   -687       C  
ATOM   1020  CG  HIS A 134      13.257 102.515  26.719  1.00 60.92           C  
ANISOU 1020  CG  HIS A 134    10707   5964   6477    298   1816   -731       C  
ATOM   1021  ND1 HIS A 134      12.756 101.604  27.624  1.00 61.36           N  
ANISOU 1021  ND1 HIS A 134    10705   6085   6524    168   1872   -775       N  
ATOM   1022  CD2 HIS A 134      12.726 103.713  27.060  1.00 62.33           C  
ANISOU 1022  CD2 HIS A 134    10847   6200   6635    454   1786   -739       C  
ATOM   1023  CE1 HIS A 134      11.956 102.223  28.473  1.00 62.97           C  
ANISOU 1023  CE1 HIS A 134    10829   6395   6703    239   1875   -811       C  
ATOM   1024  NE2 HIS A 134      11.920 103.504  28.152  1.00 63.59           N  
ANISOU 1024  NE2 HIS A 134    10917   6469   6775    418   1824   -792       N  
ATOM   1025  N   MET A 135      17.154  99.993  25.141  1.00 58.56           N  
ANISOU 1025  N   MET A 135    10769   5176   6306     11   1872   -587       N  
ATOM   1026  CA  MET A 135      18.251  99.768  24.209  1.00 56.60           C  
ANISOU 1026  CA  MET A 135    10612   4817   6078      2   1859   -545       C  
ATOM   1027  C   MET A 135      18.521  98.274  24.119  1.00 55.55           C  
ANISOU 1027  C   MET A 135    10511   4640   5955   -144   1911   -562       C  
ATOM   1028  O   MET A 135      18.829  97.635  25.132  1.00 54.45           O  
ANISOU 1028  O   MET A 135    10413   4434   5840   -210   1963   -551       O  
ATOM   1029  CB  MET A 135      19.505 100.519  24.656  1.00 54.00           C  
ANISOU 1029  CB  MET A 135    10390   4343   5785     72   1852   -475       C  
ATOM   1030  CG  MET A 135      20.729 100.240  23.810  1.00 51.87           C  
ANISOU 1030  CG  MET A 135    10209   3966   5531     55   1844   -432       C  
ATOM   1031  SD  MET A 135      22.178 101.144  24.378  1.00 48.86           S  
ANISOU 1031  SD  MET A 135     9940   3445   5178    121   1839   -356       S  
ATOM   1032  CE  MET A 135      23.435 100.427  23.327  1.00 47.16           C  
ANISOU 1032  CE  MET A 135     9739   3212   4967     68   1818   -310       C  
ATOM   1033  N   ALA A 136      18.417  97.724  22.912  1.00 52.58           N  
ANISOU 1033  N   ALA A 136    10122   4298   5557   -190   1898   -589       N  
ATOM   1034  CA  ALA A 136      18.582  96.289  22.724  1.00 52.72           C  
ANISOU 1034  CA  ALA A 136    10179   4273   5580   -329   1950   -615       C  
ATOM   1035  C   ALA A 136      20.048  95.893  22.843  1.00 51.85           C  
ANISOU 1035  C   ALA A 136    10197   3990   5515   -331   1974   -556       C  
ATOM   1036  O   ALA A 136      20.944  96.618  22.401  1.00 51.23           O  
ANISOU 1036  O   ALA A 136    10166   3851   5450   -245   1937   -507       O  
ATOM   1037  CB  ALA A 136      18.032  95.861  21.363  1.00 53.37           C  
ANISOU 1037  CB  ALA A 136    10209   4451   5620   -379   1931   -668       C  
ATOM   1038  N   ALA A 137      20.286  94.728  23.441  1.00 54.39           N  
ANISOU 1038  N   ALA A 137    10576   4236   5853   -431   2037   -559       N  
ATOM   1039  CA  ALA A 137      21.647  94.270  23.678  1.00 52.08           C  
ANISOU 1039  CA  ALA A 137    10401   3791   5598   -424   2064   -503       C  
ATOM   1040  C   ALA A 137      22.314  93.842  22.378  1.00 51.84           C  
ANISOU 1040  C   ALA A 137    10391   3743   5562   -429   2042   -499       C  
ATOM   1041  O   ALA A 137      21.688  93.232  21.507  1.00 53.06           O  
ANISOU 1041  O   ALA A 137    10542   3927   5692   -504   2057   -565       O  
ATOM   1042  CB  ALA A 137      21.651  93.112  24.674  1.00 51.94           C  
ANISOU 1042  CB  ALA A 137    10411   3735   5590   -518   2125   -493       C  
ATOM   1043  N   GLU A 138      23.594  94.168  22.255  1.00 53.67           N  
ANISOU 1043  N   GLU A 138    10595   3990   5808   -354   1992   -415       N  
ATOM   1044  CA  GLU A 138      24.439  93.781  21.140  1.00 53.05           C  
ANISOU 1044  CA  GLU A 138    10518   3915   5722   -348   1967   -400       C  
ATOM   1045  C   GLU A 138      25.640  93.006  21.666  1.00 52.29           C  
ANISOU 1045  C   GLU A 138    10407   3824   5638   -339   1971   -338       C  
ATOM   1046  O   GLU A 138      26.015  93.149  22.836  1.00 52.33           O  
ANISOU 1046  O   GLU A 138    10391   3839   5652   -311   1973   -292       O  
ATOM   1047  CB  GLU A 138      24.906  95.017  20.356  1.00 52.74           C  
ANISOU 1047  CB  GLU A 138    10468   3897   5672   -258   1905   -373       C  
ATOM   1048  CG  GLU A 138      25.696  96.020  21.180  1.00 51.77           C  
ANISOU 1048  CG  GLU A 138    10312   3800   5558   -177   1867   -300       C  
ATOM   1049  CD  GLU A 138      25.396  97.454  20.790  1.00 52.55           C  
ANISOU 1049  CD  GLU A 138    10420   3905   5643   -102   1823   -296       C  
ATOM   1050  OE1 GLU A 138      24.200  97.806  20.703  1.00 54.17           O  
ANISOU 1050  OE1 GLU A 138    10650   4093   5840    -96   1837   -353       O  
ATOM   1051  OE2 GLU A 138      26.351  98.229  20.565  1.00 51.69           O1+
ANISOU 1051  OE2 GLU A 138    10300   3817   5525    -48   1778   -244       O1+
ATOM   1052  N   PRO A 139      26.253  92.157  20.841  1.00 51.81           N  
ANISOU 1052  N   PRO A 139    10361   3754   5570   -358   1975   -342       N  
ATOM   1053  CA  PRO A 139      27.413  91.392  21.312  1.00 51.78           C  
ANISOU 1053  CA  PRO A 139    10353   3750   5570   -333   1982   -293       C  
ATOM   1054  C   PRO A 139      28.576  92.307  21.660  1.00 51.11           C  
ANISOU 1054  C   PRO A 139    10231   3707   5483   -241   1936   -230       C  
ATOM   1055  O   PRO A 139      28.777  93.357  21.045  1.00 50.76           O  
ANISOU 1055  O   PRO A 139    10171   3686   5429   -199   1893   -222       O  
ATOM   1056  CB  PRO A 139      27.752  90.486  20.122  1.00 52.22           C  
ANISOU 1056  CB  PRO A 139    10440   3787   5615   -362   1993   -323       C  
ATOM   1057  CG  PRO A 139      26.501  90.425  19.314  1.00 52.82           C  
ANISOU 1057  CG  PRO A 139    10542   3846   5683   -442   2012   -400       C  
ATOM   1058  CD  PRO A 139      25.850  91.763  19.480  1.00 52.45           C  
ANISOU 1058  CD  PRO A 139    10472   3821   5635   -408   1982   -404       C  
ATOM   1059  N   CYS A 140      29.345  91.898  22.666  1.00 47.47           N  
ANISOU 1059  N   CYS A 140     9763   3251   5023   -213   1949   -187       N  
ATOM   1060  CA  CYS A 140      30.510  92.659  23.092  1.00 46.60           C  
ANISOU 1060  CA  CYS A 140     9623   3180   4902   -140   1916   -136       C  
ATOM   1061  C   CYS A 140      31.456  91.724  23.829  1.00 46.62           C  
ANISOU 1061  C   CYS A 140     9640   3174   4898   -116   1943   -104       C  
ATOM   1062  O   CYS A 140      31.123  90.573  24.121  1.00 47.36           O  
ANISOU 1062  O   CYS A 140     9767   3230   4999   -152   1984   -116       O  
ATOM   1063  CB  CYS A 140      30.115  93.846  23.977  1.00 46.11           C  
ANISOU 1063  CB  CYS A 140     9532   3142   4845   -122   1898   -121       C  
ATOM   1064  SG  CYS A 140      29.789  93.417  25.703  1.00 46.36           S  
ANISOU 1064  SG  CYS A 140     9564   3165   4887   -139   1939   -104       S  
ATOM   1065  N   ASP A 141      32.647  92.240  24.132  1.00 44.38           N  
ANISOU 1065  N   ASP A 141     9341   2923   4597    -56   1923    -64       N  
ATOM   1066  CA  ASP A 141      33.654  91.492  24.874  1.00 44.51           C  
ANISOU 1066  CA  ASP A 141     9378   2934   4600    -15   1948    -31       C  
ATOM   1067  C   ASP A 141      33.703  91.861  26.350  1.00 44.32           C  
ANISOU 1067  C   ASP A 141     9340   2926   4574     -2   1957     -1       C  
ATOM   1068  O   ASP A 141      33.788  90.971  27.201  1.00 44.70           O  
ANISOU 1068  O   ASP A 141     9413   2948   4621      2   1993     15       O  
ATOM   1069  CB  ASP A 141      35.037  91.702  24.253  1.00 44.34           C  
ANISOU 1069  CB  ASP A 141     9364   2933   4550     41   1932    -11       C  
ATOM   1070  CG  ASP A 141      35.163  91.054  22.893  1.00 44.91           C  
ANISOU 1070  CG  ASP A 141     9463   2980   4620     34   1935    -38       C  
ATOM   1071  OD1 ASP A 141      35.169  89.805  22.832  1.00 45.92           O  
ANISOU 1071  OD1 ASP A 141     9630   3066   4753     31   1970    -46       O  
ATOM   1072  OD2 ASP A 141      35.265  91.788  21.886  1.00 44.36           O1+
ANISOU 1072  OD2 ASP A 141     9382   2931   4540     30   1904    -52       O1+
ATOM   1073  N   THR A 142      33.655  93.150  26.676  1.00 40.57           N  
ANISOU 1073  N   THR A 142     8830   2488   4095      6   1929      6       N  
ATOM   1074  CA  THR A 142      33.600  93.610  28.056  1.00 40.40           C  
ANISOU 1074  CA  THR A 142     8797   2482   4072     11   1939     27       C  
ATOM   1075  C   THR A 142      32.344  94.447  28.249  1.00 40.31           C  
ANISOU 1075  C   THR A 142     8762   2472   4080    -26   1928      3       C  
ATOM   1076  O   THR A 142      32.117  95.412  27.512  1.00 40.06           O  
ANISOU 1076  O   THR A 142     8716   2456   4049    -22   1893    -10       O  
ATOM   1077  CB  THR A 142      34.842  94.427  28.432  1.00 39.98           C  
ANISOU 1077  CB  THR A 142     8738   2466   3987     56   1925     58       C  
ATOM   1078  OG1 THR A 142      36.018  93.625  28.260  1.00 40.18           O  
ANISOU 1078  OG1 THR A 142     8793   2483   3988     99   1943     79       O  
ATOM   1079  CG2 THR A 142      34.757  94.881  29.883  1.00 39.88           C  
ANISOU 1079  CG2 THR A 142     8717   2465   3969     56   1940     75       C  
ATOM   1080  N   LEU A 143      31.533  94.075  29.236  1.00 39.45           N  
ANISOU 1080  N   LEU A 143     8660   2344   3984    -58   1960     -2       N  
ATOM   1081  CA  LEU A 143      30.287  94.766  29.544  1.00 39.50           C  
ANISOU 1081  CA  LEU A 143     8656   2345   4007    -89   1962    -28       C  
ATOM   1082  C   LEU A 143      30.441  95.508  30.864  1.00 39.27           C  
ANISOU 1082  C   LEU A 143     8615   2336   3969    -74   1969     -7       C  
ATOM   1083  O   LEU A 143      30.650  94.884  31.909  1.00 39.45           O  
ANISOU 1083  O   LEU A 143     8652   2351   3986    -81   2003     12       O  
ATOM   1084  CB  LEU A 143      29.119  93.784  29.622  1.00 40.13           C  
ANISOU 1084  CB  LEU A 143     8763   2381   4102   -154   2005    -60       C  
ATOM   1085  CG  LEU A 143      27.810  94.366  30.158  1.00 40.33           C  
ANISOU 1085  CG  LEU A 143     8789   2395   4139   -190   2023    -90       C  
ATOM   1086  CD1 LEU A 143      27.229  95.396  29.198  1.00 40.21           C  
ANISOU 1086  CD1 LEU A 143     8763   2385   4131   -172   1989   -120       C  
ATOM   1087  CD2 LEU A 143      26.809  93.259  30.442  1.00 41.05           C  
ANISOU 1087  CD2 LEU A 143     8919   2443   4235   -272   2079   -121       C  
ATOM   1088  N   LEU A 144      30.326  96.832  30.817  1.00 38.96           N  
ANISOU 1088  N   LEU A 144     8559   2316   3927    -52   1940    -12       N  
ATOM   1089  CA  LEU A 144      30.422  97.671  32.003  1.00 38.80           C  
ANISOU 1089  CA  LEU A 144     8533   2311   3896    -41   1947      0       C  
ATOM   1090  C   LEU A 144      29.083  98.336  32.283  1.00 39.03           C  
ANISOU 1090  C   LEU A 144     8565   2321   3944    -55   1956    -31       C  
ATOM   1091  O   LEU A 144      28.399  98.791  31.361  1.00 39.14           O  
ANISOU 1091  O   LEU A 144     8580   2323   3969    -46   1934    -57       O  
ATOM   1092  CB  LEU A 144      31.507  98.739  31.840  1.00 38.37           C  
ANISOU 1092  CB  LEU A 144     8472   2290   3816     -4   1913     19       C  
ATOM   1093  CG  LEU A 144      32.929  98.237  31.586  1.00 38.19           C  
ANISOU 1093  CG  LEU A 144     8456   2286   3768     15   1910     47       C  
ATOM   1094  CD1 LEU A 144      33.914  99.394  31.618  1.00 37.87           C  
ANISOU 1094  CD1 LEU A 144     8422   2274   3694     33   1889     59       C  
ATOM   1095  CD2 LEU A 144      33.316  97.166  32.594  1.00 38.40           C  
ANISOU 1095  CD2 LEU A 144     8496   2305   3788     14   1952     68       C  
ATOM   1096  N   CYS A 145      28.712  98.386  33.560  1.00 39.18           N  
ANISOU 1096  N   CYS A 145     8592   2334   3961    -71   1993    -31       N  
ATOM   1097  CA  CYS A 145      27.496  99.068  33.982  1.00 39.48           C  
ANISOU 1097  CA  CYS A 145     8638   2350   4011    -77   2010    -66       C  
ATOM   1098  C   CYS A 145      27.709  99.608  35.385  1.00 39.42           C  
ANISOU 1098  C   CYS A 145     8636   2352   3990    -75   2034    -54       C  
ATOM   1099  O   CYS A 145      28.144  98.874  36.278  1.00 39.45           O  
ANISOU 1099  O   CYS A 145     8648   2360   3983   -101   2067    -30       O  
ATOM   1100  CB  CYS A 145      26.285  98.130  33.943  1.00 40.04           C  
ANISOU 1100  CB  CYS A 145     8729   2384   4099   -133   2053   -102       C  
ATOM   1101  SG  CYS A 145      24.702  98.926  34.301  1.00 40.55           S  
ANISOU 1101  SG  CYS A 145     8813   2420   4175   -133   2082   -164       S  
ATOM   1102  N   ASP A 146      27.409 100.888  35.570  1.00 41.05           N  
ANISOU 1102  N   ASP A 146     8844   2558   4194    -41   2020    -70       N  
ATOM   1103  CA  ASP A 146      27.536 101.565  36.854  1.00 41.07           C  
ANISOU 1103  CA  ASP A 146     8859   2565   4181    -39   2045    -69       C  
ATOM   1104  C   ASP A 146      26.263 102.342  37.153  1.00 41.52           C  
ANISOU 1104  C   ASP A 146     8929   2594   4252    -19   2061   -118       C  
ATOM   1105  O   ASP A 146      26.289 103.514  37.533  1.00 41.67           O  
ANISOU 1105  O   ASP A 146     8957   2614   4261     18   2051   -130       O  
ATOM   1106  CB  ASP A 146      28.761 102.477  36.852  1.00 40.68           C  
ANISOU 1106  CB  ASP A 146     8809   2544   4104    -13   2012    -43       C  
ATOM   1107  CG  ASP A 146      29.164 102.924  38.243  1.00 40.71           C  
ANISOU 1107  CG  ASP A 146     8831   2555   4084    -28   2047    -36       C  
ATOM   1108  OD1 ASP A 146      28.915 102.172  39.205  1.00 41.21           O  
ANISOU 1108  OD1 ASP A 146     8902   2611   4147    -61   2095    -32       O  
ATOM   1109  OD2 ASP A 146      29.735 104.027  38.372  1.00 40.61           O1+
ANISOU 1109  OD2 ASP A 146     8832   2550   4047    -12   2030    -36       O1+
ATOM   1110  N   ILE A 147      25.117 101.689  36.978  1.00 42.32           N  
ANISOU 1110  N   ILE A 147     9038   2670   4372    -42   2092   -157       N  
ATOM   1111  CA  ILE A 147      23.821 102.352  37.041  1.00 43.38           C  
ANISOU 1111  CA  ILE A 147     9185   2783   4516     -8   2108   -225       C  
ATOM   1112  C   ILE A 147      23.090 101.857  38.282  1.00 44.51           C  
ANISOU 1112  C   ILE A 147     9346   2912   4654    -60   2182   -263       C  
ATOM   1113  O   ILE A 147      22.494 100.773  38.292  1.00 45.18           O  
ANISOU 1113  O   ILE A 147     9445   2980   4743   -128   2225   -285       O  
ATOM   1114  CB  ILE A 147      22.988 102.126  35.776  1.00 44.18           C  
ANISOU 1114  CB  ILE A 147     9287   2870   4628     10   2093   -267       C  
ATOM   1115  CG1 ILE A 147      23.678 102.770  34.573  1.00 43.29           C  
ANISOU 1115  CG1 ILE A 147     9164   2769   4516     65   2022   -231       C  
ATOM   1116  CG2 ILE A 147      21.596 102.715  35.947  1.00 46.01           C  
ANISOU 1116  CG2 ILE A 147     9520   3107   4853     59   2118   -356       C  
ATOM   1117  CD1 ILE A 147      22.806 102.848  33.339  1.00 44.28           C  
ANISOU 1117  CD1 ILE A 147     9299   2880   4646    104   2003   -277       C  
ATOM   1118  N   GLY A 148      23.162 102.661  39.342  1.00 46.95           N  
ANISOU 1118  N   GLY A 148     9660   3229   4950    -37   2199   -274       N  
ATOM   1119  CA  GLY A 148      22.178 102.633  40.396  1.00 48.44           C  
ANISOU 1119  CA  GLY A 148     9816   3465   5124    -61   2246   -329       C  
ATOM   1120  C   GLY A 148      21.843 104.061  40.787  1.00 48.93           C  
ANISOU 1120  C   GLY A 148     9863   3552   5175     25   2231   -374       C  
ATOM   1121  O   GLY A 148      22.512 105.010  40.372  1.00 48.20           O  
ANISOU 1121  O   GLY A 148     9821   3406   5087     87   2198   -357       O  
ATOM   1122  N   GLU A 149      20.778 104.203  41.568  1.00 48.81           N  
ANISOU 1122  N   GLU A 149     9769   3636   5141     23   2251   -430       N  
ATOM   1123  CA  GLU A 149      20.486 105.464  42.237  1.00 49.40           C  
ANISOU 1123  CA  GLU A 149     9833   3737   5200     99   2251   -476       C  
ATOM   1124  C   GLU A 149      20.223 105.169  43.702  1.00 50.19           C  
ANISOU 1124  C   GLU A 149     9885   3911   5275     33   2299   -491       C  
ATOM   1125  O   GLU A 149      19.242 104.496  44.035  1.00 51.76           O  
ANISOU 1125  O   GLU A 149     9998   4211   5459    -17   2320   -524       O  
ATOM   1126  CB  GLU A 149      19.293 106.198  41.622  1.00 51.02           C  
ANISOU 1126  CB  GLU A 149     9979   4008   5400    200   2219   -544       C  
ATOM   1127  CG  GLU A 149      18.868 107.389  42.476  1.00 51.67           C  
ANISOU 1127  CG  GLU A 149    10048   4123   5461    280   2229   -599       C  
ATOM   1128  CD  GLU A 149      18.118 108.458  41.710  1.00 52.71           C  
ANISOU 1128  CD  GLU A 149    10171   4268   5588    423   2189   -647       C  
ATOM   1129  OE1 GLU A 149      17.935 108.305  40.484  1.00 53.27           O  
ANISOU 1129  OE1 GLU A 149    10242   4329   5670    459   2150   -635       O  
ATOM   1130  OE2 GLU A 149      17.716 109.459  42.343  1.00 52.97           O1+
ANISOU 1130  OE2 GLU A 149    10202   4322   5604    505   2197   -698       O1+
ATOM   1131  N   SER A 150      21.102 105.663  44.568  1.00 47.68           N  
ANISOU 1131  N   SER A 150     9619   3551   4946     23   2319   -468       N  
ATOM   1132  CA  SER A 150      20.913 105.477  45.996  1.00 48.55           C  
ANISOU 1132  CA  SER A 150     9685   3735   5027    -37   2364   -482       C  
ATOM   1133  C   SER A 150      19.634 106.159  46.458  1.00 50.43           C  
ANISOU 1133  C   SER A 150     9839   4077   5245     18   2371   -571       C  
ATOM   1134  O   SER A 150      19.215 107.187  45.919  1.00 51.02           O  
ANISOU 1134  O   SER A 150     9919   4140   5325    127   2342   -618       O  
ATOM   1135  CB  SER A 150      22.106 106.029  46.776  1.00 47.45           C  
ANISOU 1135  CB  SER A 150     9614   3542   4872    -51   2380   -448       C  
ATOM   1136  OG  SER A 150      23.228 105.173  46.669  1.00 47.05           O  
ANISOU 1136  OG  SER A 150     9616   3435   4825   -115   2386   -365       O  
ATOM   1137  N   SER A 151      19.006 105.559  47.462  1.00 47.15           N  
ANISOU 1137  N   SER A 151     9347   3768   4801    -56   2410   -592       N  
ATOM   1138  CA  SER A 151      17.855 106.141  48.128  1.00 48.58           C  
ANISOU 1138  CA  SER A 151     9436   4068   4952    -15   2425   -678       C  
ATOM   1139  C   SER A 151      18.017 105.881  49.619  1.00 48.83           C  
ANISOU 1139  C   SER A 151     9444   4161   4948   -102   2475   -675       C  
ATOM   1140  O   SER A 151      19.078 105.455  50.084  1.00 47.99           O  
ANISOU 1140  O   SER A 151     9399   3995   4841   -171   2492   -605       O  
ATOM   1141  CB  SER A 151      16.548 105.564  47.569  1.00 50.30           C  
ANISOU 1141  CB  SER A 151     9551   4400   5160    -21   2416   -725       C  
ATOM   1142  OG  SER A 151      15.942 104.683  48.498  1.00 51.44           O  
ANISOU 1142  OG  SER A 151     9617   4660   5269   -135   2460   -738       O  
ATOM   1143  N   SER A 152      16.954 106.145  50.377  1.00 46.77           N  
ANISOU 1143  N   SER A 152     9087   4032   4652    -94   2498   -751       N  
ATOM   1144  CA  SER A 152      16.943 105.865  51.803  1.00 47.06           C  
ANISOU 1144  CA  SER A 152     9085   4149   4647   -182   2547   -755       C  
ATOM   1145  C   SER A 152      16.052 104.692  52.179  1.00 47.60           C  
ANISOU 1145  C   SER A 152     9061   4341   4683   -295   2577   -760       C  
ATOM   1146  O   SER A 152      16.230 104.125  53.261  1.00 47.72           O  
ANISOU 1146  O   SER A 152     9064   4403   4664   -397   2618   -733       O  
ATOM   1147  CB  SER A 152      16.495 107.106  52.589  1.00 47.73           C  
ANISOU 1147  CB  SER A 152     9135   4296   4705   -101   2561   -842       C  
ATOM   1148  OG  SER A 152      15.249 107.590  52.116  1.00 48.54           O  
ANISOU 1148  OG  SER A 152     9155   4488   4801     -4   2543   -928       O  
ATOM   1149  N   SER A 153      15.112 104.310  51.316  1.00 49.69           N  
ANISOU 1149  N   SER A 153     9263   4664   4951   -286   2558   -794       N  
ATOM   1150  CA  SER A 153      14.216 103.198  51.590  1.00 50.32           C  
ANISOU 1150  CA  SER A 153     9260   4867   4994   -408   2589   -806       C  
ATOM   1151  C   SER A 153      14.745 101.944  50.915  1.00 49.80           C  
ANISOU 1151  C   SER A 153     9264   4706   4951   -505   2588   -722       C  
ATOM   1152  O   SER A 153      14.892 101.933  49.682  1.00 49.43           O  
ANISOU 1152  O   SER A 153     9252   4585   4942   -453   2549   -710       O  
ATOM   1153  CB  SER A 153      12.809 103.515  51.094  1.00 51.83           C  
ANISOU 1153  CB  SER A 153     9328   5205   5161   -351   2573   -904       C  
ATOM   1154  OG  SER A 153      12.050 102.335  50.897  1.00 53.03           O  
ANISOU 1154  OG  SER A 153     9416   5449   5281   -479   2593   -908       O  
ATOM   1155  N   PRO A 154      15.040 100.876  51.662  1.00 49.97           N  
ANISOU 1155  N   PRO A 154     9313   4723   4949   -640   2630   -662       N  
ATOM   1156  CA  PRO A 154      15.603  99.672  51.029  1.00 49.56           C  
ANISOU 1156  CA  PRO A 154     9348   4563   4920   -721   2633   -580       C  
ATOM   1157  C   PRO A 154      14.658  99.003  50.051  1.00 50.07           C  
ANISOU 1157  C   PRO A 154     9366   4676   4980   -769   2626   -618       C  
ATOM   1158  O   PRO A 154      15.119  98.233  49.199  1.00 49.69           O  
ANISOU 1158  O   PRO A 154     9396   4522   4962   -802   2617   -566       O  
ATOM   1159  CB  PRO A 154      15.913  98.761  52.224  1.00 49.80           C  
ANISOU 1159  CB  PRO A 154     9409   4602   4910   -848   2685   -518       C  
ATOM   1160  CG  PRO A 154      14.962  99.206  53.285  1.00 50.63           C  
ANISOU 1160  CG  PRO A 154     9402   4875   4961   -876   2713   -594       C  
ATOM   1161  CD  PRO A 154      14.815 100.691  53.105  1.00 50.50           C  
ANISOU 1161  CD  PRO A 154     9337   4889   4963   -725   2678   -668       C  
ATOM   1162  N   GLU A 155      13.352  99.265  50.143  1.00 51.33           N  
ANISOU 1162  N   GLU A 155     9399   5003   5099   -776   2630   -712       N  
ATOM   1163  CA  GLU A 155      12.423  98.733  49.155  1.00 52.00           C  
ANISOU 1163  CA  GLU A 155     9426   5160   5172   -819   2620   -758       C  
ATOM   1164  C   GLU A 155      12.577  99.414  47.802  1.00 51.84           C  
ANISOU 1164  C   GLU A 155     9419   5079   5199   -683   2561   -773       C  
ATOM   1165  O   GLU A 155      12.186  98.834  46.783  1.00 52.52           O  
ANISOU 1165  O   GLU A 155     9495   5174   5287   -721   2547   -785       O  
ATOM   1166  CB  GLU A 155      10.980  98.872  49.645  1.00 53.86           C  
ANISOU 1166  CB  GLU A 155     9506   5619   5340   -859   2641   -858       C  
ATOM   1167  CG  GLU A 155      10.661  98.069  50.898  1.00 54.73           C  
ANISOU 1167  CG  GLU A 155     9594   5810   5391  -1020   2703   -849       C  
ATOM   1168  CD  GLU A 155      10.839  98.875  52.171  1.00 54.32           C  
ANISOU 1168  CD  GLU A 155     9513   5805   5320   -971   2719   -862       C  
ATOM   1169  OE1 GLU A 155      10.843 100.122  52.089  1.00 53.99           O  
ANISOU 1169  OE1 GLU A 155     9435   5779   5298   -813   2686   -909       O  
ATOM   1170  OE2 GLU A 155      10.973  98.263  53.252  1.00 54.16           O1+
ANISOU 1170  OE2 GLU A 155     9511   5804   5262  -1090   2767   -825       O1+
ATOM   1171  N   VAL A 156      13.135 100.625  47.768  1.00 49.85           N  
ANISOU 1171  N   VAL A 156     9194   4766   4979   -533   2527   -774       N  
ATOM   1172  CA  VAL A 156      13.372 101.307  46.500  1.00 49.41           C  
ANISOU 1172  CA  VAL A 156     9168   4640   4966   -404   2471   -778       C  
ATOM   1173  C   VAL A 156      14.677 100.835  45.874  1.00 48.37           C  
ANISOU 1173  C   VAL A 156     9173   4322   4885   -419   2458   -685       C  
ATOM   1174  O   VAL A 156      14.735 100.536  44.676  1.00 48.17           O  
ANISOU 1174  O   VAL A 156     9172   4248   4882   -407   2429   -674       O  
ATOM   1175  CB  VAL A 156      13.364 102.833  46.701  1.00 49.44           C  
ANISOU 1175  CB  VAL A 156     9157   4653   4976   -241   2443   -821       C  
ATOM   1176  CG1 VAL A 156      13.362 103.545  45.355  1.00 49.27           C  
ANISOU 1176  CG1 VAL A 156     9155   4582   4985   -107   2385   -832       C  
ATOM   1177  CG2 VAL A 156      12.168 103.255  47.538  1.00 50.52           C  
ANISOU 1177  CG2 VAL A 156     9162   4976   5058   -225   2465   -911       C  
ATOM   1178  N   GLU A 157      15.746 100.766  46.674  1.00 51.69           N  
ANISOU 1178  N   GLU A 157     9677   4646   5317   -443   2479   -619       N  
ATOM   1179  CA  GLU A 157      17.028 100.298  46.157  1.00 50.03           C  
ANISOU 1179  CA  GLU A 157     9587   4275   5146   -452   2470   -531       C  
ATOM   1180  C   GLU A 157      16.922  98.873  45.632  1.00 50.44           C  
ANISOU 1180  C   GLU A 157     9670   4298   5198   -567   2489   -498       C  
ATOM   1181  O   GLU A 157      17.502  98.543  44.591  1.00 49.38           O  
ANISOU 1181  O   GLU A 157     9603   4063   5097   -549   2466   -462       O  
ATOM   1182  CB  GLU A 157      18.103 100.392  47.240  1.00 48.98           C  
ANISOU 1182  CB  GLU A 157     9520   4080   5009   -466   2494   -469       C  
ATOM   1183  CG  GLU A 157      18.487 101.813  47.611  1.00 48.20           C  
ANISOU 1183  CG  GLU A 157     9426   3973   4915   -358   2475   -494       C  
ATOM   1184  CD  GLU A 157      19.748 101.874  48.449  1.00 47.07           C  
ANISOU 1184  CD  GLU A 157     9356   3762   4767   -376   2493   -426       C  
ATOM   1185  OE1 GLU A 157      19.914 101.018  49.344  1.00 47.56           O  
ANISOU 1185  OE1 GLU A 157     9422   3847   4802   -470   2533   -384       O  
ATOM   1186  OE2 GLU A 157      20.579 102.774  48.204  1.00 45.74           O1+
ANISOU 1186  OE2 GLU A 157     9242   3521   4614   -300   2468   -415       O1+
ATOM   1187  N   GLU A 158      16.183  98.014  46.337  1.00 48.48           N  
ANISOU 1187  N   GLU A 158     9377   4134   4908   -690   2535   -513       N  
ATOM   1188  CA  GLU A 158      15.948  96.660  45.845  1.00 48.95           C  
ANISOU 1188  CA  GLU A 158     9473   4167   4960   -812   2560   -493       C  
ATOM   1189  C   GLU A 158      15.164  96.684  44.540  1.00 49.84           C  
ANISOU 1189  C   GLU A 158     9529   4330   5076   -795   2528   -555       C  
ATOM   1190  O   GLU A 158      15.510  95.985  43.580  1.00 49.48           O  
ANISOU 1190  O   GLU A 158     9551   4196   5054   -824   2521   -528       O  
ATOM   1191  CB  GLU A 158      15.209  95.840  46.901  1.00 50.05           C  
ANISOU 1191  CB  GLU A 158     9575   4399   5043   -957   2618   -504       C  
ATOM   1192  CG  GLU A 158      14.820  94.446  46.440  1.00 50.49           C  
ANISOU 1192  CG  GLU A 158     9672   4431   5080  -1102   2653   -495       C  
ATOM   1193  CD  GLU A 158      14.017  93.691  47.479  1.00 51.64           C  
ANISOU 1193  CD  GLU A 158     9783   4677   5161  -1258   2712   -510       C  
ATOM   1194  OE1 GLU A 158      13.819  94.231  48.588  1.00 51.70           O  
ANISOU 1194  OE1 GLU A 158     9730   4774   5140  -1248   2726   -523       O  
ATOM   1195  OE2 GLU A 158      13.582  92.558  47.187  1.00 52.37           O1+
ANISOU 1195  OE2 GLU A 158     9913   4759   5227  -1397   2747   -511       O1+
ATOM   1196  N   THR A 159      14.094  97.482  44.491  1.00 49.29           N  
ANISOU 1196  N   THR A 159     9335   4413   4981   -743   2509   -641       N  
ATOM   1197  CA  THR A 159      13.318  97.615  43.263  1.00 49.67           C  
ANISOU 1197  CA  THR A 159     9315   4534   5024   -711   2473   -702       C  
ATOM   1198  C   THR A 159      14.177  98.149  42.123  1.00 48.80           C  
ANISOU 1198  C   THR A 159     9278   4296   4967   -592   2420   -666       C  
ATOM   1199  O   THR A 159      14.079  97.674  40.985  1.00 48.83           O  
ANISOU 1199  O   THR A 159     9294   4280   4979   -613   2402   -671       O  
ATOM   1200  CB  THR A 159      12.111  98.524  43.504  1.00 50.50           C  
ANISOU 1200  CB  THR A 159     9271   4830   5085   -642   2458   -795       C  
ATOM   1201  OG1 THR A 159      11.137  97.830  44.295  1.00 51.50           O  
ANISOU 1201  OG1 THR A 159     9313   5105   5150   -781   2507   -840       O  
ATOM   1202  CG2 THR A 159      11.476  98.952  42.188  1.00 50.81           C  
ANISOU 1202  CG2 THR A 159     9242   4941   5121   -558   2407   -847       C  
ATOM   1203  N   ARG A 160      15.036  99.130  42.411  1.00 49.15           N  
ANISOU 1203  N   ARG A 160     9374   4258   5044   -476   2398   -631       N  
ATOM   1204  CA  ARG A 160      15.907  99.671  41.373  1.00 48.37           C  
ANISOU 1204  CA  ARG A 160     9350   4039   4989   -373   2350   -595       C  
ATOM   1205  C   ARG A 160      17.008  98.685  41.004  1.00 47.71           C  
ANISOU 1205  C   ARG A 160     9383   3810   4936   -439   2364   -517       C  
ATOM   1206  O   ARG A 160      17.344  98.538  39.824  1.00 47.40           O  
ANISOU 1206  O   ARG A 160     9383   3708   4919   -414   2334   -504       O  
ATOM   1207  CB  ARG A 160      16.510 101.000  41.826  1.00 47.91           C  
ANISOU 1207  CB  ARG A 160     9321   3936   4948   -248   2328   -585       C  
ATOM   1208  CG  ARG A 160      15.516 102.144  41.901  1.00 48.58           C  
ANISOU 1208  CG  ARG A 160     9312   4139   5009   -140   2304   -662       C  
ATOM   1209  CD  ARG A 160      16.177 103.396  42.452  1.00 48.22           C  
ANISOU 1209  CD  ARG A 160     9319   4026   4977    -34   2293   -652       C  
ATOM   1210  NE  ARG A 160      15.236 104.501  42.601  1.00 48.99           N  
ANISOU 1210  NE  ARG A 160     9340   4224   5051     82   2276   -726       N  
ATOM   1211  CZ  ARG A 160      15.509 105.631  43.245  1.00 49.01           C  
ANISOU 1211  CZ  ARG A 160     9375   4194   5053    171   2276   -741       C  
ATOM   1212  NH1 ARG A 160      16.696 105.803  43.809  1.00 48.29           N1+
ANISOU 1212  NH1 ARG A 160     9381   3986   4980    145   2292   -687       N1+
ATOM   1213  NH2 ARG A 160      14.594 106.587  43.333  1.00 49.85           N  
ANISOU 1213  NH2 ARG A 160     9417   4390   5136    288   2262   -812       N  
ATOM   1214  N   THR A 161      17.581  97.998  41.996  1.00 50.38           N  
ANISOU 1214  N   THR A 161     9776   4096   5269   -518   2408   -464       N  
ATOM   1215  CA  THR A 161      18.641  97.039  41.701  1.00 48.06           C  
ANISOU 1215  CA  THR A 161     9596   3666   4998   -565   2424   -388       C  
ATOM   1216  C   THR A 161      18.103  95.842  40.926  1.00 48.68           C  
ANISOU 1216  C   THR A 161     9684   3743   5069   -667   2442   -405       C  
ATOM   1217  O   THR A 161      18.762  95.346  40.004  1.00 47.13           O  
ANISOU 1217  O   THR A 161     9563   3445   4898   -662   2431   -372       O  
ATOM   1218  CB  THR A 161      19.320  96.580  42.991  1.00 47.31           C  
ANISOU 1218  CB  THR A 161     9555   3529   4891   -615   2467   -325       C  
ATOM   1219  OG1 THR A 161      19.779  97.724  43.722  1.00 47.04           O  
ANISOU 1219  OG1 THR A 161     9507   3509   4857   -532   2453   -320       O  
ATOM   1220  CG2 THR A 161      20.506  95.692  42.674  1.00 46.07           C  
ANISOU 1220  CG2 THR A 161     9517   3232   4754   -631   2479   -242       C  
ATOM   1221  N   LEU A 162      16.909  95.363  41.286  1.00 48.46           N  
ANISOU 1221  N   LEU A 162     9581   3832   5000   -766   2472   -460       N  
ATOM   1222  CA  LEU A 162      16.287  94.285  40.522  1.00 49.29           C  
ANISOU 1222  CA  LEU A 162     9690   3950   5088   -879   2492   -490       C  
ATOM   1223  C   LEU A 162      16.035  94.710  39.081  1.00 49.33           C  
ANISOU 1223  C   LEU A 162     9656   3979   5107   -812   2441   -533       C  
ATOM   1224  O   LEU A 162      16.235  93.924  38.147  1.00 48.95           O  
ANISOU 1224  O   LEU A 162     9665   3863   5069   -862   2444   -527       O  
ATOM   1225  CB  LEU A 162      14.978  93.854  41.185  1.00 51.65           C  
ANISOU 1225  CB  LEU A 162     9896   4400   5328  -1003   2533   -552       C  
ATOM   1226  CG  LEU A 162      15.061  92.910  42.384  1.00 51.78           C  
ANISOU 1226  CG  LEU A 162     9971   4386   5316  -1131   2598   -510       C  
ATOM   1227  CD1 LEU A 162      13.681  92.695  42.985  1.00 54.21           C  
ANISOU 1227  CD1 LEU A 162    10167   4873   5558  -1248   2632   -584       C  
ATOM   1228  CD2 LEU A 162      15.672  91.586  41.965  1.00 50.37           C  
ANISOU 1228  CD2 LEU A 162     9934   4054   5150  -1221   2633   -454       C  
ATOM   1229  N   ARG A 163      15.597  95.956  38.883  1.00 50.98           N  
ANISOU 1229  N   ARG A 163     9774   4282   5315   -696   2394   -577       N  
ATOM   1230  CA  ARG A 163      15.334  96.446  37.535  1.00 51.32           C  
ANISOU 1230  CA  ARG A 163     9778   4356   5364   -620   2341   -612       C  
ATOM   1231  C   ARG A 163      16.609  96.482  36.701  1.00 48.88           C  
ANISOU 1231  C   ARG A 163     9581   3886   5104   -557   2314   -549       C  
ATOM   1232  O   ARG A 163      16.578  96.213  35.494  1.00 49.16           O  
ANISOU 1232  O   ARG A 163     9624   3909   5143   -559   2291   -563       O  
ATOM   1233  CB  ARG A 163      14.695  97.834  37.600  1.00 52.49           C  
ANISOU 1233  CB  ARG A 163     9825   4619   5499   -487   2299   -660       C  
ATOM   1234  CG  ARG A 163      14.396  98.444  36.241  1.00 52.92           C  
ANISOU 1234  CG  ARG A 163     9839   4713   5553   -391   2240   -690       C  
ATOM   1235  CD  ARG A 163      13.955  99.894  36.366  1.00 54.05           C  
ANISOU 1235  CD  ARG A 163     9914   4934   5687   -234   2198   -722       C  
ATOM   1236  NE  ARG A 163      13.790 100.529  35.062  1.00 54.54           N  
ANISOU 1236  NE  ARG A 163     9957   5016   5748   -127   2139   -735       N  
ATOM   1237  CZ  ARG A 163      12.634 100.610  34.410  1.00 56.92           C  
ANISOU 1237  CZ  ARG A 163    10142   5482   6004   -107   2116   -800       C  
ATOM   1238  NH1 ARG A 163      11.532 100.100  34.943  1.00 58.99           N1+
ANISOU 1238  NH1 ARG A 163    10290   5908   6214   -194   2148   -864       N1+
ATOM   1239  NH2 ARG A 163      12.580 101.204  33.225  1.00 57.22           N  
ANISOU 1239  NH2 ARG A 163    10173   5531   6039     -3   2060   -801       N  
ATOM   1240  N   VAL A 164      17.742  96.809  37.326  1.00 50.55           N  
ANISOU 1240  N   VAL A 164     9874   3987   5345   -505   2317   -482       N  
ATOM   1241  CA  VAL A 164      19.007  96.856  36.598  1.00 47.73           C  
ANISOU 1241  CA  VAL A 164     9616   3494   5025   -448   2293   -423       C  
ATOM   1242  C   VAL A 164      19.410  95.461  36.137  1.00 47.80           C  
ANISOU 1242  C   VAL A 164     9705   3417   5041   -545   2326   -395       C  
ATOM   1243  O   VAL A 164      19.799  95.258  34.981  1.00 47.57           O  
ANISOU 1243  O   VAL A 164     9714   3334   5028   -526   2303   -391       O  
ATOM   1244  CB  VAL A 164      20.104  97.502  37.466  1.00 47.03           C  
ANISOU 1244  CB  VAL A 164     9585   3330   4953   -383   2294   -363       C  
ATOM   1245  CG1 VAL A 164      21.452  97.428  36.764  1.00 46.27           C  
ANISOU 1245  CG1 VAL A 164     9586   3110   4885   -340   2275   -303       C  
ATOM   1246  CG2 VAL A 164      19.749  98.944  37.786  1.00 47.02           C  
ANISOU 1246  CG2 VAL A 164     9525   3395   4946   -282   2262   -396       C  
ATOM   1247  N   LEU A 165      19.312  94.475  37.031  1.00 46.74           N  
ANISOU 1247  N   LEU A 165     9603   3264   4891   -649   2383   -377       N  
ATOM   1248  CA  LEU A 165      19.761  93.125  36.711  1.00 46.93           C  
ANISOU 1248  CA  LEU A 165     9727   3182   4920   -734   2421   -345       C  
ATOM   1249  C   LEU A 165      18.855  92.423  35.708  1.00 47.65           C  
ANISOU 1249  C   LEU A 165     9792   3319   4993   -825   2428   -410       C  
ATOM   1250  O   LEU A 165      19.284  91.442  35.089  1.00 47.77           O  
ANISOU 1250  O   LEU A 165     9897   3236   5017   -876   2451   -393       O  
ATOM   1251  CB  LEU A 165      19.879  92.301  37.994  1.00 47.30           C  
ANISOU 1251  CB  LEU A 165     9829   3193   4950   -818   2482   -301       C  
ATOM   1252  CG  LEU A 165      21.058  92.712  38.878  1.00 46.61           C  
ANISOU 1252  CG  LEU A 165     9793   3038   4876   -738   2481   -223       C  
ATOM   1253  CD1 LEU A 165      20.808  92.342  40.329  1.00 47.07           C  
ANISOU 1253  CD1 LEU A 165     9853   3125   4905   -807   2529   -198       C  
ATOM   1254  CD2 LEU A 165      22.346  92.075  38.374  1.00 46.19           C  
ANISOU 1254  CD2 LEU A 165     9732   2992   4826   -669   2430   -161       C  
ATOM   1255  N   SER A 166      17.619  92.893  35.529  1.00 48.85           N  
ANISOU 1255  N   SER A 166     9822   3625   5114   -844   2411   -486       N  
ATOM   1256  CA  SER A 166      16.794  92.391  34.438  1.00 50.28           C  
ANISOU 1256  CA  SER A 166     9961   3874   5271   -918   2408   -552       C  
ATOM   1257  C   SER A 166      17.216  92.964  33.093  1.00 49.38           C  
ANISOU 1257  C   SER A 166     9845   3738   5181   -817   2349   -556       C  
ATOM   1258  O   SER A 166      16.889  92.382  32.054  1.00 49.85           O  
ANISOU 1258  O   SER A 166     9903   3812   5225   -877   2349   -596       O  
ATOM   1259  CB  SER A 166      15.320  92.712  34.688  1.00 53.63           C  
ANISOU 1259  CB  SER A 166    10239   4496   5643   -966   2407   -634       C  
ATOM   1260  OG  SER A 166      15.033  94.064  34.376  1.00 54.76           O  
ANISOU 1260  OG  SER A 166    10284   4735   5787   -824   2345   -659       O  
ATOM   1261  N   MET A 167      17.937  94.084  33.095  1.00 53.20           N  
ANISOU 1261  N   MET A 167    10332   4188   5694   -675   2303   -517       N  
ATOM   1262  CA  MET A 167      18.402  94.725  31.872  1.00 52.35           C  
ANISOU 1262  CA  MET A 167    10230   4056   5604   -577   2247   -512       C  
ATOM   1263  C   MET A 167      19.743  94.161  31.413  1.00 49.98           C  
ANISOU 1263  C   MET A 167    10054   3598   5337   -568   2255   -452       C  
ATOM   1264  O   MET A 167      19.908  93.830  30.235  1.00 50.13           O  
ANISOU 1264  O   MET A 167    10095   3594   5358   -575   2238   -466       O  
ATOM   1265  CB  MET A 167      18.495  96.241  32.080  1.00 52.54           C  
ANISOU 1265  CB  MET A 167    10208   4119   5636   -435   2196   -502       C  
ATOM   1266  CG  MET A 167      19.012  97.016  30.878  1.00 51.71           C  
ANISOU 1266  CG  MET A 167    10119   3983   5544   -332   2138   -488       C  
ATOM   1267  SD  MET A 167      20.789  97.310  30.948  1.00 48.43           S  
ANISOU 1267  SD  MET A 167     9830   3403   5169   -267   2130   -401       S  
ATOM   1268  CE  MET A 167      20.914  98.296  32.438  1.00 48.16           C  
ANISOU 1268  CE  MET A 167     9785   3378   5137   -208   2138   -379       C  
ATOM   1269  N   VAL A 168      20.709  94.043  32.329  1.00 47.79           N  
ANISOU 1269  N   VAL A 168     9854   3223   5081   -549   2279   -386       N  
ATOM   1270  CA  VAL A 168      21.988  93.429  31.989  1.00 47.32           C  
ANISOU 1270  CA  VAL A 168     9803   3147   5030   -521   2250   -312       C  
ATOM   1271  C   VAL A 168      21.860  91.935  31.737  1.00 47.95           C  
ANISOU 1271  C   VAL A 168     9924   3198   5098   -625   2292   -321       C  
ATOM   1272  O   VAL A 168      22.782  91.328  31.179  1.00 47.75           O  
ANISOU 1272  O   VAL A 168     9896   3175   5074   -595   2265   -282       O  
ATOM   1273  CB  VAL A 168      23.040  93.686  33.091  1.00 46.75           C  
ANISOU 1273  CB  VAL A 168     9707   3099   4958   -459   2233   -235       C  
ATOM   1274  CG1 VAL A 168      22.789  95.024  33.774  1.00 46.47           C  
ANISOU 1274  CG1 VAL A 168     9651   3079   4926   -400   2223   -243       C  
ATOM   1275  CG2 VAL A 168      23.066  92.548  34.107  1.00 47.21           C  
ANISOU 1275  CG2 VAL A 168     9800   3137   5002   -533   2286   -212       C  
ATOM   1276  N   GLY A 169      20.734  91.329  32.126  1.00 50.85           N  
ANISOU 1276  N   GLY A 169    10334   3537   5449   -751   2361   -379       N  
ATOM   1277  CA  GLY A 169      20.533  89.915  31.865  1.00 51.52           C  
ANISOU 1277  CA  GLY A 169    10467   3593   5516   -865   2404   -393       C  
ATOM   1278  C   GLY A 169      20.434  89.586  30.390  1.00 52.17           C  
ANISOU 1278  C   GLY A 169    10556   3669   5596   -887   2387   -438       C  
ATOM   1279  O   GLY A 169      20.722  88.456  29.983  1.00 51.95           O  
ANISOU 1279  O   GLY A 169    10563   3619   5558   -937   2403   -430       O  
ATOM   1280  N   ASP A 170      20.025  90.556  29.569  1.00 54.58           N  
ANISOU 1280  N   ASP A 170    10836   3994   5908   -843   2357   -491       N  
ATOM   1281  CA  ASP A 170      19.998  90.340  28.126  1.00 54.62           C  
ANISOU 1281  CA  ASP A 170    10844   4001   5907   -854   2337   -533       C  
ATOM   1282  C   ASP A 170      21.391  90.454  27.519  1.00 52.85           C  
ANISOU 1282  C   ASP A 170    10590   3787   5703   -736   2270   -452       C  
ATOM   1283  O   ASP A 170      21.720  89.727  26.576  1.00 52.97           O  
ANISOU 1283  O   ASP A 170    10622   3792   5713   -760   2266   -460       O  
ATOM   1284  CB  ASP A 170      19.045  91.331  27.457  1.00 55.93           C  
ANISOU 1284  CB  ASP A 170    10872   4333   6047   -817   2279   -589       C  
ATOM   1285  CG  ASP A 170      17.592  90.933  27.605  1.00 58.18           C  
ANISOU 1285  CG  ASP A 170    11065   4760   6282   -939   2304   -667       C  
ATOM   1286  OD1 ASP A 170      17.163  89.984  26.914  1.00 58.48           O  
ANISOU 1286  OD1 ASP A 170    11119   4809   6292  -1058   2333   -720       O  
ATOM   1287  OD2 ASP A 170      16.877  91.575  28.404  1.00 59.70           O1+
ANISOU 1287  OD2 ASP A 170    11166   5060   6457   -920   2295   -680       O1+
ATOM   1288  N   TRP A 171      22.218  91.362  28.045  1.00 49.88           N  
ANISOU 1288  N   TRP A 171    10171   3438   5344   -617   2222   -383       N  
ATOM   1289  CA  TRP A 171      23.571  91.521  27.522  1.00 49.18           C  
ANISOU 1289  CA  TRP A 171    10050   3371   5263   -519   2163   -320       C  
ATOM   1290  C   TRP A 171      24.442  90.318  27.859  1.00 49.32           C  
ANISOU 1290  C   TRP A 171    10089   3374   5276   -528   2180   -277       C  
ATOM   1291  O   TRP A 171      25.206  89.841  27.013  1.00 49.26           O  
ANISOU 1291  O   TRP A 171    10085   3364   5267   -501   2160   -265       O  
ATOM   1292  CB  TRP A 171      24.196  92.803  28.069  1.00 48.37           C  
ANISOU 1292  CB  TRP A 171     9901   3306   5170   -413   2115   -271       C  
ATOM   1293  CG  TRP A 171      23.528  94.052  27.592  1.00 48.26           C  
ANISOU 1293  CG  TRP A 171     9874   3303   5158   -372   2088   -306       C  
ATOM   1294  CD1 TRP A 171      22.344  94.566  28.033  1.00 48.66           C  
ANISOU 1294  CD1 TRP A 171     9939   3344   5207   -393   2118   -363       C  
ATOM   1295  CD2 TRP A 171      24.009  94.954  26.588  1.00 47.81           C  
ANISOU 1295  CD2 TRP A 171     9797   3269   5102   -294   2028   -294       C  
ATOM   1296  NE1 TRP A 171      22.055  95.730  27.363  1.00 48.54           N  
ANISOU 1296  NE1 TRP A 171     9913   3341   5187   -316   2078   -388       N  
ATOM   1297  CE2 TRP A 171      23.061  95.990  26.470  1.00 48.01           C  
ANISOU 1297  CE2 TRP A 171     9828   3292   5123   -260   2021   -340       C  
ATOM   1298  CE3 TRP A 171      25.147  94.985  25.775  1.00 47.35           C  
ANISOU 1298  CE3 TRP A 171     9720   3230   5039   -249   1983   -254       C  
ATOM   1299  CZ2 TRP A 171      23.215  97.045  25.574  1.00 47.79           C  
ANISOU 1299  CZ2 TRP A 171     9793   3276   5088   -180   1967   -336       C  
ATOM   1300  CZ3 TRP A 171      25.298  96.034  24.886  1.00 47.08           C  
ANISOU 1300  CZ3 TRP A 171     9678   3212   4999   -187   1932   -252       C  
ATOM   1301  CH2 TRP A 171      24.338  97.049  24.792  1.00 47.31           C  
ANISOU 1301  CH2 TRP A 171     9719   3233   5025   -153   1923   -288       C  
ATOM   1302  N   LEU A 172      24.341  89.814  29.092  1.00 49.47           N  
ANISOU 1302  N   LEU A 172    10128   3378   5289   -561   2219   -256       N  
ATOM   1303  CA  LEU A 172      25.114  88.643  29.487  1.00 49.78           C  
ANISOU 1303  CA  LEU A 172    10201   3394   5318   -559   2238   -218       C  
ATOM   1304  C   LEU A 172      24.693  87.390  28.730  1.00 50.85           C  
ANISOU 1304  C   LEU A 172    10396   3483   5442   -648   2278   -260       C  
ATOM   1305  O   LEU A 172      25.451  86.415  28.702  1.00 51.06           O  
ANISOU 1305  O   LEU A 172    10459   3482   5461   -626   2286   -233       O  
ATOM   1306  CB  LEU A 172      24.982  88.413  30.993  1.00 49.91           C  
ANISOU 1306  CB  LEU A 172    10235   3401   5326   -579   2274   -190       C  
ATOM   1307  CG  LEU A 172      25.542  89.518  31.889  1.00 48.94           C  
ANISOU 1307  CG  LEU A 172    10063   3322   5210   -494   2242   -146       C  
ATOM   1308  CD1 LEU A 172      25.085  89.335  33.327  1.00 49.30           C  
ANISOU 1308  CD1 LEU A 172    10131   3356   5244   -540   2286   -134       C  
ATOM   1309  CD2 LEU A 172      27.060  89.546  31.810  1.00 48.40           C  
ANISOU 1309  CD2 LEU A 172     9972   3278   5139   -389   2199    -92       C  
ATOM   1310  N   GLU A 173      23.506  87.395  28.120  1.00 54.12           N  
ANISOU 1310  N   GLU A 173    10826   3886   5850   -749   2306   -331       N  
ATOM   1311  CA  GLU A 173      23.083  86.285  27.276  1.00 55.09           C  
ANISOU 1311  CA  GLU A 173    11005   3971   5956   -848   2344   -383       C  
ATOM   1312  C   GLU A 173      23.949  86.142  26.032  1.00 54.78           C  
ANISOU 1312  C   GLU A 173    10958   3934   5924   -783   2305   -376       C  
ATOM   1313  O   GLU A 173      23.863  85.113  25.352  1.00 55.48           O  
ANISOU 1313  O   GLU A 173    11097   3985   5998   -847   2336   -410       O  
ATOM   1314  CB  GLU A 173      21.618  86.469  26.872  1.00 55.59           C  
ANISOU 1314  CB  GLU A 173    11082   4036   6005   -980   2383   -475       C  
ATOM   1315  CG  GLU A 173      20.773  85.207  26.959  1.00 57.23           C  
ANISOU 1315  CG  GLU A 173    11360   4205   6178  -1146   2458   -531       C  
ATOM   1316  CD  GLU A 173      20.715  84.639  28.364  1.00 58.08           C  
ANISOU 1316  CD  GLU A 173    11503   4290   6273  -1182   2499   -491       C  
ATOM   1317  OE1 GLU A 173      21.518  83.733  28.674  1.00 58.49           O  
ANISOU 1317  OE1 GLU A 173    11596   4305   6321  -1142   2503   -439       O  
ATOM   1318  OE2 GLU A 173      19.873  85.105  29.163  1.00 58.13           O1+
ANISOU 1318  OE2 GLU A 173    11501   4315   6273  -1247   2528   -515       O1+
ATOM   1319  N   LYS A 174      24.773  87.142  25.722  1.00 53.08           N  
ANISOU 1319  N   LYS A 174    10684   3760   5726   -665   2242   -338       N  
ATOM   1320  CA  LYS A 174      25.682  87.111  24.585  1.00 52.70           C  
ANISOU 1320  CA  LYS A 174    10624   3719   5680   -602   2204   -328       C  
ATOM   1321  C   LYS A 174      27.078  86.633  24.968  1.00 52.37           C  
ANISOU 1321  C   LYS A 174    10586   3673   5638   -510   2191   -263       C  
ATOM   1322  O   LYS A 174      28.005  86.745  24.160  1.00 52.09           O  
ANISOU 1322  O   LYS A 174    10537   3652   5604   -443   2157   -248       O  
ATOM   1323  CB  LYS A 174      25.760  88.497  23.940  1.00 51.73           C  
ANISOU 1323  CB  LYS A 174    10444   3644   5567   -539   2147   -329       C  
ATOM   1324  CG  LYS A 174      24.407  89.141  23.655  1.00 51.85           C  
ANISOU 1324  CG  LYS A 174    10457   3663   5579   -605   2158   -394       C  
ATOM   1325  CD  LYS A 174      23.799  88.641  22.353  1.00 52.20           C  
ANISOU 1325  CD  LYS A 174    10534   3693   5608   -687   2176   -470       C  
ATOM   1326  CE  LYS A 174      22.474  89.331  22.058  1.00 52.75           C  
ANISOU 1326  CE  LYS A 174    10603   3775   5663   -745   2188   -551       C  
ATOM   1327  NZ  LYS A 174      21.428  88.989  23.062  1.00 53.85           N1+
ANISOU 1327  NZ  LYS A 174    10767   3900   5792   -845   2247   -592       N1+
ATOM   1328  N   ARG A 175      27.249  86.125  26.187  1.00 52.45           N  
ANISOU 1328  N   ARG A 175    10426   3727   5777   -931   1247   -189       N  
ATOM   1329  CA  ARG A 175      28.477  85.502  26.672  1.00 52.57           C  
ANISOU 1329  CA  ARG A 175    10486   3717   5772   -834   1292   -176       C  
ATOM   1330  C   ARG A 175      29.691  86.424  26.571  1.00 51.65           C  
ANISOU 1330  C   ARG A 175    10332   3651   5640   -728   1343   -168       C  
ATOM   1331  O   ARG A 175      30.617  86.149  25.797  1.00 51.77           O  
ANISOU 1331  O   ARG A 175    10422   3642   5608   -649   1364   -182       O  
ATOM   1332  CB  ARG A 175      28.737  84.207  25.904  1.00 54.20           C  
ANISOU 1332  CB  ARG A 175    10829   3836   5927   -818   1277   -205       C  
ATOM   1333  CG  ARG A 175      29.400  83.110  26.718  1.00 54.81           C  
ANISOU 1333  CG  ARG A 175    10962   3864   5998   -768   1307   -184       C  
ATOM   1334  CD  ARG A 175      28.533  82.677  27.898  1.00 55.06           C  
ANISOU 1334  CD  ARG A 175    10949   3888   6083   -848   1290   -156       C  
ATOM   1335  NE  ARG A 175      27.177  82.297  27.503  1.00 55.94           N  
ANISOU 1335  NE  ARG A 175    11077   3966   6211   -972   1227   -173       N  
ATOM   1336  CZ  ARG A 175      26.314  81.674  28.301  1.00 56.38           C  
ANISOU 1336  CZ  ARG A 175    11119   3996   6307  -1054   1204   -150       C  
ATOM   1337  NH1 ARG A 175      26.668  81.348  29.537  1.00 56.05           N1+
ANISOU 1337  NH1 ARG A 175    11050   3956   6292  -1020   1240   -112       N1+
ATOM   1338  NH2 ARG A 175      25.099  81.368  27.864  1.00 56.99           N  
ANISOU 1338  NH2 ARG A 175    11211   4044   6397  -1171   1145   -163       N  
ATOM   1339  N   PRO A 176      29.731  87.524  27.325  1.00 49.19           N  
ANISOU 1339  N   PRO A 176     9912   3412   5367   -722   1364   -142       N  
ATOM   1340  CA  PRO A 176      30.933  88.368  27.337  1.00 48.16           C  
ANISOU 1340  CA  PRO A 176     9746   3326   5227   -627   1413   -129       C  
ATOM   1341  C   PRO A 176      32.012  87.785  28.239  1.00 48.53           C  
ANISOU 1341  C   PRO A 176     9813   3358   5266   -550   1456   -101       C  
ATOM   1342  O   PRO A 176      31.734  87.267  29.324  1.00 48.71           O  
ANISOU 1342  O   PRO A 176     9821   3371   5314   -576   1456    -80       O  
ATOM   1343  CB  PRO A 176      30.421  89.711  27.883  1.00 47.14           C  
ANISOU 1343  CB  PRO A 176     9497   3271   5142   -664   1413   -113       C  
ATOM   1344  CG  PRO A 176      28.916  89.606  27.870  1.00 47.71           C  
ANISOU 1344  CG  PRO A 176     9550   3337   5239   -774   1365   -120       C  
ATOM   1345  CD  PRO A 176      28.625  88.160  28.055  1.00 48.87           C  
ANISOU 1345  CD  PRO A 176     9776   3415   5377   -806   1343   -124       C  
ATOM   1346  N   GLY A 177      33.262  87.885  27.778  1.00 43.26           N  
ANISOU 1346  N   GLY A 177     9182   2692   4564   -452   1496    -97       N  
ATOM   1347  CA  GLY A 177      34.367  87.288  28.512  1.00 43.44           C  
ANISOU 1347  CA  GLY A 177     9236   2698   4572   -371   1542    -68       C  
ATOM   1348  C   GLY A 177      34.683  87.991  29.816  1.00 42.70           C  
ANISOU 1348  C   GLY A 177     9049   2658   4517   -362   1567    -33       C  
ATOM   1349  O   GLY A 177      35.158  87.361  30.766  1.00 42.92           O  
ANISOU 1349  O   GLY A 177     9093   2670   4545   -328   1592     -7       O  
ATOM   1350  N   ALA A 178      34.434  89.296  29.885  1.00 41.67           N  
ANISOU 1350  N   ALA A 178     8826   2590   4417   -389   1561    -32       N  
ATOM   1351  CA  ALA A 178      34.655  90.058  31.102  1.00 41.00           C  
ANISOU 1351  CA  ALA A 178     8654   2557   4368   -388   1579     -3       C  
ATOM   1352  C   ALA A 178      33.499  91.024  31.297  1.00 40.45           C  
ANISOU 1352  C   ALA A 178     8499   2533   4337   -471   1547    -11       C  
ATOM   1353  O   ALA A 178      32.929  91.535  30.330  1.00 40.34           O  
ANISOU 1353  O   ALA A 178     8476   2529   4321   -505   1524    -35       O  
ATOM   1354  CB  ALA A 178      35.983  90.827  31.060  1.00 40.57           C  
ANISOU 1354  CB  ALA A 178     8577   2534   4302   -306   1622     16       C  
ATOM   1355  N   PHE A 179      33.147  91.264  32.556  1.00 37.76           N  
ANISOU 1355  N   PHE A 179     8099   2219   4029   -499   1547     11       N  
ATOM   1356  CA  PHE A 179      32.085  92.213  32.852  1.00 37.26           C  
ANISOU 1356  CA  PHE A 179     7956   2202   4000   -567   1524     10       C  
ATOM   1357  C   PHE A 179      32.279  92.764  34.258  1.00 36.81           C  
ANISOU 1357  C   PHE A 179     7836   2184   3967   -558   1543     39       C  
ATOM   1358  O   PHE A 179      32.975  92.176  35.090  1.00 37.00           O  
ANISOU 1358  O   PHE A 179     7882   2191   3984   -517   1566     60       O  
ATOM   1359  CB  PHE A 179      30.697  91.580  32.696  1.00 37.74           C  
ANISOU 1359  CB  PHE A 179     8031   2236   4074   -650   1484      1       C  
ATOM   1360  CG  PHE A 179      30.473  90.371  33.559  1.00 38.34           C  
ANISOU 1360  CG  PHE A 179     8143   2269   4155   -665   1482     19       C  
ATOM   1361  CD1 PHE A 179      30.025  90.505  34.863  1.00 38.15           C  
ANISOU 1361  CD1 PHE A 179     8066   2268   4162   -688   1487     49       C  
ATOM   1362  CD2 PHE A 179      30.689  89.098  33.061  1.00 39.14           C  
ANISOU 1362  CD2 PHE A 179     8337   2304   4231   -653   1476      7       C  
ATOM   1363  CE1 PHE A 179      29.813  89.395  35.656  1.00 38.73           C  
ANISOU 1363  CE1 PHE A 179     8173   2301   4243   -700   1487     70       C  
ATOM   1364  CE2 PHE A 179      30.477  87.984  33.849  1.00 39.74           C  
ANISOU 1364  CE2 PHE A 179     8449   2337   4314   -667   1476     26       C  
ATOM   1365  CZ  PHE A 179      30.038  88.133  35.148  1.00 39.53           C  
ANISOU 1365  CZ  PHE A 179     8363   2335   4321   -691   1482     58       C  
ATOM   1366  N   CYS A 180      31.640  93.909  34.505  1.00 37.23           N  
ANISOU 1366  N   CYS A 180     7816   2286   4044   -595   1535     40       N  
ATOM   1367  CA  CYS A 180      31.743  94.595  35.791  1.00 36.81           C  
ANISOU 1367  CA  CYS A 180     7705   2271   4009   -589   1550     63       C  
ATOM   1368  C   CYS A 180      30.505  95.489  35.931  1.00 36.49           C  
ANISOU 1368  C   CYS A 180     7603   2268   3992   -649   1532     63       C  
ATOM   1369  O   CYS A 180      30.529  96.657  35.544  1.00 36.01           O  
ANISOU 1369  O   CYS A 180     7502   2245   3935   -647   1536     54       O  
ATOM   1370  CB  CYS A 180      33.025  95.401  35.886  1.00 36.39           C  
ANISOU 1370  CB  CYS A 180     7636   2244   3947   -530   1578     68       C  
ATOM   1371  SG  CYS A 180      33.160  96.430  37.364  1.00 35.90           S  
ANISOU 1371  SG  CYS A 180     7511   2228   3903   -530   1592     90       S  
ATOM   1372  N   ILE A 181      29.435  94.921  36.481  1.00 37.59           N  
ANISOU 1372  N   ILE A 181     7738   2396   4148   -700   1516     78       N  
ATOM   1373  CA  ILE A 181      28.141  95.586  36.580  1.00 37.44           C  
ANISOU 1373  CA  ILE A 181     7670   2407   4150   -758   1502     87       C  
ATOM   1374  C   ILE A 181      27.863  95.903  38.044  1.00 37.28           C  
ANISOU 1374  C   ILE A 181     7610   2411   4145   -758   1518    118       C  
ATOM   1375  O   ILE A 181      28.184  95.109  38.936  1.00 37.56           O  
ANISOU 1375  O   ILE A 181     7666   2425   4179   -741   1528    137       O  
ATOM   1376  CB  ILE A 181      27.030  94.715  35.955  1.00 38.05           C  
ANISOU 1376  CB  ILE A 181     7774   2449   4234   -825   1470     85       C  
ATOM   1377  CG1 ILE A 181      25.639  95.324  36.183  1.00 38.00           C  
ANISOU 1377  CG1 ILE A 181     7715   2474   4250   -888   1460    107       C  
ATOM   1378  CG2 ILE A 181      27.128  93.280  36.454  1.00 38.69           C  
ANISOU 1378  CG2 ILE A 181     7906   2479   4315   -829   1465     98       C  
ATOM   1379  CD1 ILE A 181      24.810  94.636  37.253  1.00 38.43           C  
ANISOU 1379  CD1 ILE A 181     7758   2517   4326   -928   1456    147       C  
ATOM   1380  N   LYS A 182      27.271  97.069  38.289  1.00 39.02           N  
ANISOU 1380  N   LYS A 182     7777   2674   4373   -772   1524    126       N  
ATOM   1381  CA  LYS A 182      27.128  97.602  39.638  1.00 38.82           C  
ANISOU 1381  CA  LYS A 182     7720   2676   4354   -760   1545    152       C  
ATOM   1382  C   LYS A 182      25.825  97.122  40.266  1.00 39.22           C  
ANISOU 1382  C   LYS A 182     7755   2723   4423   -810   1538    188       C  
ATOM   1383  O   LYS A 182      24.738  97.422  39.761  1.00 39.31           O  
ANISOU 1383  O   LYS A 182     7743   2747   4445   -857   1527    197       O  
ATOM   1384  CB  LYS A 182      27.169  99.129  39.619  1.00 38.27           C  
ANISOU 1384  CB  LYS A 182     7611   2650   4281   -745   1558    143       C  
ATOM   1385  CG  LYS A 182      27.003  99.773  40.984  1.00 38.12           C  
ANISOU 1385  CG  LYS A 182     7569   2655   4261   -730   1580    167       C  
ATOM   1386  CD  LYS A 182      26.471 101.188  40.852  1.00 37.77           C  
ANISOU 1386  CD  LYS A 182     7490   2646   4216   -733   1592    164       C  
ATOM   1387  CE  LYS A 182      26.635 101.959  42.147  1.00 37.62           C  
ANISOU 1387  CE  LYS A 182     7464   2645   4184   -706   1616    178       C  
ATOM   1388  NZ  LYS A 182      26.212 103.379  42.005  1.00 37.33           N1+
ANISOU 1388  NZ  LYS A 182     7405   2636   4142   -702   1630    173       N1+
ATOM   1389  N   VAL A 183      25.937  96.391  41.371  1.00 40.33           N  
ANISOU 1389  N   VAL A 183     7909   2848   4566   -798   1549    215       N  
ATOM   1390  CA  VAL A 183      24.791  96.033  42.198  1.00 40.71           C  
ANISOU 1390  CA  VAL A 183     7936   2898   4632   -838   1551    260       C  
ATOM   1391  C   VAL A 183      24.706  97.046  43.333  1.00 40.37           C  
ANISOU 1391  C   VAL A 183     7862   2895   4582   -807   1580    281       C  
ATOM   1392  O   VAL A 183      25.633  97.162  44.142  1.00 40.20           O  
ANISOU 1392  O   VAL A 183     7855   2874   4545   -758   1599    279       O  
ATOM   1393  CB  VAL A 183      24.916  94.601  42.739  1.00 41.29           C  
ANISOU 1393  CB  VAL A 183     8046   2928   4713   -842   1548    281       C  
ATOM   1394  CG1 VAL A 183      23.692  94.235  43.565  1.00 41.73           C  
ANISOU 1394  CG1 VAL A 183     8076   2989   4792   -887   1550    335       C  
ATOM   1395  CG2 VAL A 183      25.108  93.613  41.597  1.00 41.68           C  
ANISOU 1395  CG2 VAL A 183     8143   2931   4762   -865   1520    254       C  
ATOM   1396  N   LEU A 184      23.602  97.791  43.386  1.00 45.00           N  
ANISOU 1396  N   LEU A 184     8409   3513   5176   -836   1586    305       N  
ATOM   1397  CA  LEU A 184      23.484  98.856  44.377  1.00 44.67           C  
ANISOU 1397  CA  LEU A 184     8346   3506   5121   -803   1617    323       C  
ATOM   1398  C   LEU A 184      23.020  98.327  45.729  1.00 45.31           C  
ANISOU 1398  C   LEU A 184     8424   3587   5204   -798   1636    374       C  
ATOM   1399  O   LEU A 184      23.487  98.796  46.773  1.00 45.29           O  
ANISOU 1399  O   LEU A 184     8431   3596   5180   -752   1662    381       O  
ATOM   1400  CB  LEU A 184      22.524  99.937  43.878  1.00 44.51           C  
ANISOU 1400  CB  LEU A 184     8290   3520   5101   -823   1623    331       C  
ATOM   1401  CG  LEU A 184      22.333 101.142  44.804  1.00 44.35           C  
ANISOU 1401  CG  LEU A 184     8257   3532   5061   -784   1659    348       C  
ATOM   1402  CD1 LEU A 184      23.195 102.314  44.354  1.00 44.04           C  
ANISOU 1402  CD1 LEU A 184     8226   3501   5004   -749   1664    300       C  
ATOM   1403  CD2 LEU A 184      20.868 101.541  44.881  1.00 44.55           C  
ANISOU 1403  CD2 LEU A 184     8245   3590   5093   -812   1674    399       C  
ATOM   1404  N   CYS A 185      22.106  97.356  45.730  1.00 45.18           N  
ANISOU 1404  N   CYS A 185     8398   3558   5211   -847   1624    413       N  
ATOM   1405  CA  CYS A 185      21.473  96.852  46.950  1.00 45.58           C  
ANISOU 1405  CA  CYS A 185     8437   3614   5268   -849   1644    474       C  
ATOM   1406  C   CYS A 185      21.633  95.339  47.014  1.00 46.29           C  
ANISOU 1406  C   CYS A 185     8554   3658   5377   -873   1626    486       C  
ATOM   1407  O   CYS A 185      20.714  94.588  46.662  1.00 46.93           O  
ANISOU 1407  O   CYS A 185     8621   3725   5484   -936   1606    518       O  
ATOM   1408  CB  CYS A 185      19.998  97.255  47.001  1.00 45.78           C  
ANISOU 1408  CB  CYS A 185     8413   3676   5305   -890   1652    529       C  
ATOM   1409  SG  CYS A 185      19.105  96.712  48.474  1.00 46.47           S  
ANISOU 1409  SG  CYS A 185     8475   3781   5400   -890   1681    618       S  
ATOM   1410  N   PRO A 186      22.789  94.853  47.463  1.00 42.63           N  
ANISOU 1410  N   PRO A 186     8131   3168   4900   -826   1634    466       N  
ATOM   1411  CA  PRO A 186      23.029  93.403  47.517  1.00 43.18           C  
ANISOU 1411  CA  PRO A 186     8234   3189   4983   -839   1623    476       C  
ATOM   1412  C   PRO A 186      22.703  92.736  48.847  1.00 43.66           C  
ANISOU 1412  C   PRO A 186     8293   3245   5050   -828   1647    536       C  
ATOM   1413  O   PRO A 186      22.992  91.544  48.993  1.00 44.14           O  
ANISOU 1413  O   PRO A 186     8388   3262   5120   -831   1643    547       O  
ATOM   1414  CB  PRO A 186      24.537  93.326  47.246  1.00 42.85           C  
ANISOU 1414  CB  PRO A 186     8237   3126   4917   -784   1625    426       C  
ATOM   1415  CG  PRO A 186      25.072  94.551  47.926  1.00 42.29           C  
ANISOU 1415  CG  PRO A 186     8154   3095   4820   -732   1651    418       C  
ATOM   1416  CD  PRO A 186      24.008  95.622  47.772  1.00 42.08           C  
ANISOU 1416  CD  PRO A 186     8081   3110   4799   -761   1651    429       C  
ATOM   1417  N   TYR A 187      22.102  93.445  49.804  1.00 44.49           N  
ANISOU 1417  N   TYR A 187     8363   3392   5147   -813   1674    579       N  
ATOM   1418  CA  TYR A 187      22.077  93.000  51.191  1.00 44.83           C  
ANISOU 1418  CA  TYR A 187     8411   3439   5184   -779   1706    632       C  
ATOM   1419  C   TYR A 187      20.732  92.463  51.667  1.00 45.50           C  
ANISOU 1419  C   TYR A 187     8456   3534   5297   -827   1710    708       C  
ATOM   1420  O   TYR A 187      20.632  92.052  52.828  1.00 45.85           O  
ANISOU 1420  O   TYR A 187     8500   3584   5337   -799   1738    759       O  
ATOM   1421  CB  TYR A 187      22.521  94.145  52.112  1.00 44.38           C  
ANISOU 1421  CB  TYR A 187     8355   3421   5088   -713   1740    629       C  
ATOM   1422  CG  TYR A 187      21.673  95.394  52.002  1.00 44.12           C  
ANISOU 1422  CG  TYR A 187     8282   3435   5047   -722   1748    637       C  
ATOM   1423  CD1 TYR A 187      20.514  95.539  52.754  1.00 44.50           C  
ANISOU 1423  CD1 TYR A 187     8293   3519   5098   -729   1772    706       C  
ATOM   1424  CD2 TYR A 187      22.035  96.430  51.152  1.00 43.55           C  
ANISOU 1424  CD2 TYR A 187     8210   3373   4962   -718   1737    581       C  
ATOM   1425  CE1 TYR A 187      19.737  96.675  52.657  1.00 44.33           C  
ANISOU 1425  CE1 TYR A 187     8238   3542   5064   -728   1786    719       C  
ATOM   1426  CE2 TYR A 187      21.264  97.574  51.050  1.00 43.36           C  
ANISOU 1426  CE2 TYR A 187     8155   3390   4928   -720   1749    591       C  
ATOM   1427  CZ  TYR A 187      20.115  97.690  51.805  1.00 43.75           C  
ANISOU 1427  CZ  TYR A 187     8172   3474   4979   -723   1775    660       C  
ATOM   1428  OH  TYR A 187      19.342  98.825  51.708  1.00 43.63           O  
ANISOU 1428  OH  TYR A 187     8128   3500   4948   -716   1793    675       O  
ATOM   1429  N   THR A 188      19.700  92.452  50.830  1.00 47.52           N  
ANISOU 1429  N   THR A 188     8677   3797   5580   -899   1684    722       N  
ATOM   1430  CA  THR A 188      18.403  91.978  51.290  1.00 48.47           C  
ANISOU 1430  CA  THR A 188     8753   3935   5729   -950   1688    805       C  
ATOM   1431  C   THR A 188      18.241  90.485  51.006  1.00 49.46           C  
ANISOU 1431  C   THR A 188     8900   4002   5890  -1008   1661    822       C  
ATOM   1432  O   THR A 188      18.994  89.884  50.235  1.00 49.40           O  
ANISOU 1432  O   THR A 188     8942   3943   5886  -1015   1635    766       O  
ATOM   1433  CB  THR A 188      17.267  92.770  50.639  1.00 48.38           C  
ANISOU 1433  CB  THR A 188     8687   3969   5726  -1000   1679    828       C  
ATOM   1434  OG1 THR A 188      17.113  92.366  49.274  1.00 48.59           O  
ANISOU 1434  OG1 THR A 188     8723   3964   5776  -1070   1633    791       O  
ATOM   1435  CG2 THR A 188      17.556  94.260  50.696  1.00 47.46           C  
ANISOU 1435  CG2 THR A 188     8564   3898   5573   -940   1704    795       C  
ATOM   1436  N   SER A 189      17.238  89.886  51.654  1.00 50.62           N  
ANISOU 1436  N   SER A 189     9010   4159   6064  -1049   1668    906       N  
ATOM   1437  CA  SER A 189      16.976  88.462  51.467  1.00 51.49           C  
ANISOU 1437  CA  SER A 189     9141   4211   6212  -1112   1642    931       C  
ATOM   1438  C   SER A 189      16.602  88.156  50.023  1.00 51.61           C  
ANISOU 1438  C   SER A 189     9166   4193   6250  -1197   1590    895       C  
ATOM   1439  O   SER A 189      17.090  87.182  49.437  1.00 51.87           O  
ANISOU 1439  O   SER A 189     9257   4159   6294  -1220   1563    857       O  
ATOM   1440  CB  SER A 189      15.867  88.003  52.414  1.00 52.32           C  
ANISOU 1440  CB  SER A 189     9193   4342   6343  -1146   1660   1037       C  
ATOM   1441  OG  SER A 189      16.150  88.374  53.751  1.00 52.16           O  
ANISOU 1441  OG  SER A 189     9164   4359   6295  -1062   1710   1073       O  
ATOM   1442  N   THR A 190      15.738  88.983  49.430  1.00 51.32           N  
ANISOU 1442  N   THR A 190     9078   4205   6217  -1241   1579    908       N  
ATOM   1443  CA  THR A 190      15.329  88.761  48.047  1.00 51.38           C  
ANISOU 1443  CA  THR A 190     9094   4187   6241  -1324   1529    876       C  
ATOM   1444  C   THR A 190      16.485  89.002  47.086  1.00 50.60           C  
ANISOU 1444  C   THR A 190     9056   4055   6115  -1285   1513    773       C  
ATOM   1445  O   THR A 190      16.674  88.241  46.128  1.00 50.76           O  
ANISOU 1445  O   THR A 190     9124   4018   6143  -1329   1475    732       O  
ATOM   1446  CB  THR A 190      14.146  89.664  47.697  1.00 51.54           C  
ANISOU 1446  CB  THR A 190     9041   4276   6265  -1374   1528    922       C  
ATOM   1447  OG1 THR A 190      13.073  89.427  48.617  1.00 52.47           O  
ANISOU 1447  OG1 THR A 190     9096   4434   6406  -1407   1547   1028       O  
ATOM   1448  CG2 THR A 190      13.664  89.389  46.281  1.00 51.84           C  
ANISOU 1448  CG2 THR A 190     9088   4289   6319  -1467   1475    894       C  
ATOM   1449  N   MET A 191      17.274  90.051  47.326  1.00 50.87           N  
ANISOU 1449  N   MET A 191     9091   4123   6114  -1200   1542    734       N  
ATOM   1450  CA  MET A 191      18.399  90.351  46.450  1.00 49.90           C  
ANISOU 1450  CA  MET A 191     9017   3977   5965  -1159   1530    646       C  
ATOM   1451  C   MET A 191      19.513  89.319  46.548  1.00 50.06           C  
ANISOU 1451  C   MET A 191     9107   3936   5979  -1121   1529    611       C  
ATOM   1452  O   MET A 191      20.361  89.257  45.651  1.00 49.81           O  
ANISOU 1452  O   MET A 191     9121   3876   5929  -1101   1514    546       O  
ATOM   1453  CB  MET A 191      18.957  91.741  46.761  1.00 48.99           C  
ANISOU 1453  CB  MET A 191     8883   3915   5818  -1083   1562    620       C  
ATOM   1454  CG  MET A 191      18.170  92.877  46.136  1.00 49.03           C  
ANISOU 1454  CG  MET A 191     8840   3970   5820  -1111   1559    624       C  
ATOM   1455  SD  MET A 191      18.094  92.729  44.342  1.00 49.10           S  
ANISOU 1455  SD  MET A 191     8872   3950   5832  -1173   1510    568       S  
ATOM   1456  CE  MET A 191      19.815  92.431  43.942  1.00 48.54           C  
ANISOU 1456  CE  MET A 191     8873   3833   5737  -1102   1507    485       C  
ATOM   1457  N   MET A 192      19.534  88.510  47.607  1.00 50.11           N  
ANISOU 1457  N   MET A 192     9122   3921   5996  -1107   1549    658       N  
ATOM   1458  CA  MET A 192      20.621  87.551  47.765  1.00 50.28           C  
ANISOU 1458  CA  MET A 192     9211   3886   6007  -1062   1556    631       C  
ATOM   1459  C   MET A 192      20.405  86.303  46.917  1.00 51.31           C  
ANISOU 1459  C   MET A 192     9392   3946   6158  -1126   1519    619       C  
ATOM   1460  O   MET A 192      21.351  85.807  46.296  1.00 51.29           O  
ANISOU 1460  O   MET A 192     9455   3898   6136  -1094   1512    566       O  
ATOM   1461  CB  MET A 192      20.792  87.189  49.239  1.00 50.40           C  
ANISOU 1461  CB  MET A 192     9222   3906   6021  -1014   1596    686       C  
ATOM   1462  CG  MET A 192      21.887  87.992  49.925  1.00 49.81           C  
ANISOU 1462  CG  MET A 192     9154   3865   5907   -918   1634    662       C  
ATOM   1463  SD  MET A 192      21.847  87.898  51.722  1.00 50.25           S  
ANISOU 1463  SD  MET A 192     9192   3947   5955   -863   1683    734       S  
ATOM   1464  CE  MET A 192      23.542  88.321  52.114  1.00 49.73           C  
ANISOU 1464  CE  MET A 192     9171   3885   5841   -759   1712    685       C  
ATOM   1465  N   GLU A 193      19.181  85.783  46.868  1.00 50.69           N  
ANISOU 1465  N   GLU A 193     9288   3856   6117  -1215   1495    669       N  
ATOM   1466  CA  GLU A 193      18.898  84.652  45.994  1.00 51.48           C  
ANISOU 1466  CA  GLU A 193     9440   3885   6235  -1288   1454    654       C  
ATOM   1467  C   GLU A 193      18.442  85.084  44.605  1.00 51.76           C  
ANISOU 1467  C   GLU A 193     9474   3926   6268  -1350   1411    612       C  
ATOM   1468  O   GLU A 193      18.168  84.224  43.762  1.00 52.88           O  
ANISOU 1468  O   GLU A 193     9663   4008   6419  -1415   1371    593       O  
ATOM   1469  CB  GLU A 193      17.869  83.713  46.636  1.00 52.37           C  
ANISOU 1469  CB  GLU A 193     9533   3972   6392  -1361   1446    733       C  
ATOM   1470  CG  GLU A 193      16.440  84.211  46.688  1.00 52.75           C  
ANISOU 1470  CG  GLU A 193     9497   4075   6471  -1445   1432    798       C  
ATOM   1471  CD  GLU A 193      15.542  83.244  47.438  1.00 54.13           C  
ANISOU 1471  CD  GLU A 193     9650   4227   6691  -1510   1430    885       C  
ATOM   1472  OE1 GLU A 193      14.761  83.696  48.302  1.00 54.14           O  
ANISOU 1472  OE1 GLU A 193     9574   4290   6708  -1518   1453    964       O  
ATOM   1473  OE2 GLU A 193      15.634  82.025  47.176  1.00 54.87           O1+
ANISOU 1473  OE2 GLU A 193     9805   4240   6802  -1550   1407    877       O1+
ATOM   1474  N   THR A 194      18.348  86.392  44.350  1.00 50.41           N  
ANISOU 1474  N   THR A 194     9252   3822   6081  -1330   1418    597       N  
ATOM   1475  CA  THR A 194      18.381  86.877  42.974  1.00 49.78           C  
ANISOU 1475  CA  THR A 194     9187   3743   5983  -1355   1387    539       C  
ATOM   1476  C   THR A 194      19.807  86.843  42.437  1.00 49.21           C  
ANISOU 1476  C   THR A 194     9182   3642   5874  -1274   1395    465       C  
ATOM   1477  O   THR A 194      20.035  86.457  41.285  1.00 49.79           O  
ANISOU 1477  O   THR A 194     9309   3675   5933  -1296   1364    415       O  
ATOM   1478  CB  THR A 194      17.804  88.295  42.887  1.00 48.79           C  
ANISOU 1478  CB  THR A 194     8987   3697   5853  -1357   1397    552       C  
ATOM   1479  OG1 THR A 194      16.373  88.235  42.860  1.00 49.88           O  
ANISOU 1479  OG1 THR A 194     9072   3858   6022  -1454   1377    616       O  
ATOM   1480  CG2 THR A 194      18.297  89.016  41.635  1.00 48.16           C  
ANISOU 1480  CG2 THR A 194     8928   3626   5744  -1340   1382    482       C  
ATOM   1481  N   MET A 195      20.779  87.221  43.270  1.00 47.33           N  
ANISOU 1481  N   MET A 195     8941   3425   5616  -1182   1436    460       N  
ATOM   1482  CA  MET A 195      22.182  87.107  42.892  1.00 46.83           C  
ANISOU 1482  CA  MET A 195     8937   3339   5519  -1103   1449    404       C  
ATOM   1483  C   MET A 195      22.672  85.665  42.915  1.00 47.85           C  
ANISOU 1483  C   MET A 195     9145   3391   5646  -1095   1447    401       C  
ATOM   1484  O   MET A 195      23.596  85.326  42.168  1.00 47.89           O  
ANISOU 1484  O   MET A 195     9214   3362   5622  -1055   1446    354       O  
ATOM   1485  CB  MET A 195      23.051  87.972  43.808  1.00 46.02           C  
ANISOU 1485  CB  MET A 195     8806   3284   5395  -1014   1493    407       C  
ATOM   1486  CG  MET A 195      23.044  89.450  43.447  1.00 45.56           C  
ANISOU 1486  CG  MET A 195     8697   3288   5324   -999   1496    384       C  
ATOM   1487  SD  MET A 195      23.441  89.725  41.709  1.00 45.36           S  
ANISOU 1487  SD  MET A 195     8705   3251   5279  -1007   1466    317       S  
ATOM   1488  CE  MET A 195      25.099  89.054  41.622  1.00 45.38           C  
ANISOU 1488  CE  MET A 195     8781   3213   5249   -921   1486    282       C  
ATOM   1489  N   GLU A 196      22.074  84.804  43.745  1.00 48.14           N  
ANISOU 1489  N   GLU A 196     9182   3400   5711  -1131   1450    454       N  
ATOM   1490  CA  GLU A 196      22.494  83.405  43.768  1.00 48.97           C  
ANISOU 1490  CA  GLU A 196     9367   3426   5815  -1125   1451    453       C  
ATOM   1491  C   GLU A 196      22.169  82.707  42.453  1.00 49.66           C  
ANISOU 1491  C   GLU A 196     9515   3453   5900  -1190   1405    414       C  
ATOM   1492  O   GLU A 196      22.962  81.892  41.967  1.00 50.05           O  
ANISOU 1492  O   GLU A 196     9651   3443   5924  -1155   1407    380       O  
ATOM   1493  CB  GLU A 196      21.844  82.666  44.940  1.00 49.64           C  
ANISOU 1493  CB  GLU A 196     9434   3493   5934  -1154   1464    523       C  
ATOM   1494  CG  GLU A 196      22.529  82.896  46.280  1.00 49.22           C  
ANISOU 1494  CG  GLU A 196     9360   3471   5870  -1068   1516    556       C  
ATOM   1495  CD  GLU A 196      21.980  82.009  47.381  1.00 49.99           C  
ANISOU 1495  CD  GLU A 196     9453   3543   5999  -1090   1532    626       C  
ATOM   1496  OE1 GLU A 196      21.157  81.118  47.079  1.00 50.91           O  
ANISOU 1496  OE1 GLU A 196     9588   3609   6148  -1173   1502    649       O  
ATOM   1497  OE2 GLU A 196      22.375  82.204  48.551  1.00 49.72           O1+
ANISOU 1497  OE2 GLU A 196     9398   3539   5956  -1026   1574    661       O1+
ATOM   1498  N   ARG A 197      21.011  83.009  41.861  1.00 48.89           N  
ANISOU 1498  N   ARG A 197     9379   3371   5826  -1284   1365    422       N  
ATOM   1499  CA  ARG A 197      20.689  82.438  40.557  1.00 49.56           C  
ANISOU 1499  CA  ARG A 197     9524   3401   5903  -1350   1317    381       C  
ATOM   1500  C   ARG A 197      21.570  83.034  39.467  1.00 48.92           C  
ANISOU 1500  C   ARG A 197     9479   3333   5778  -1294   1316    312       C  
ATOM   1501  O   ARG A 197      22.066  82.312  38.594  1.00 49.42           O  
ANISOU 1501  O   ARG A 197     9629   3334   5812  -1286   1301    268       O  
ATOM   1502  CB  ARG A 197      19.212  82.651  40.225  1.00 49.99           C  
ANISOU 1502  CB  ARG A 197     9525   3476   5992  -1469   1275    412       C  
ATOM   1503  CG  ARG A 197      18.279  81.628  40.843  1.00 51.08           C  
ANISOU 1503  CG  ARG A 197     9661   3573   6176  -1553   1258    473       C  
ATOM   1504  CD  ARG A 197      17.088  81.357  39.934  1.00 51.93           C  
ANISOU 1504  CD  ARG A 197     9767   3661   6302  -1682   1199    478       C  
ATOM   1505  NE  ARG A 197      16.214  80.313  40.467  1.00 53.11           N  
ANISOU 1505  NE  ARG A 197     9916   3765   6497  -1770   1181    538       N  
ATOM   1506  CZ  ARG A 197      16.320  79.021  40.170  1.00 54.19           C  
ANISOU 1506  CZ  ARG A 197    10144   3807   6637  -1805   1157    521       C  
ATOM   1507  NH1 ARG A 197      15.478  78.146  40.701  1.00 55.28           N1+
ANISOU 1507  NH1 ARG A 197    10273   3908   6822  -1890   1142    582       N1+
ATOM   1508  NH2 ARG A 197      17.268  78.602  39.341  1.00 54.23           N  
ANISOU 1508  NH2 ARG A 197    10252   3757   6599  -1755   1152    446       N  
ATOM   1509  N   LEU A 198      21.775  84.355  39.499  1.00 45.16           N  
ANISOU 1509  N   LEU A 198     8937   2932   5291  -1254   1334    305       N  
ATOM   1510  CA  LEU A 198      22.565  85.001  38.457  1.00 44.57           C  
ANISOU 1510  CA  LEU A 198     8885   2872   5177  -1204   1333    246       C  
ATOM   1511  C   LEU A 198      24.024  84.570  38.510  1.00 44.44           C  
ANISOU 1511  C   LEU A 198     8934   2827   5125  -1102   1367    220       C  
ATOM   1512  O   LEU A 198      24.732  84.649  37.499  1.00 44.32           O  
ANISOU 1512  O   LEU A 198     8967   2798   5074  -1065   1364    173       O  
ATOM   1513  CB  LEU A 198      22.454  86.524  38.574  1.00 43.55           C  
ANISOU 1513  CB  LEU A 198     8670   2828   5049  -1183   1348    250       C  
ATOM   1514  CG  LEU A 198      21.353  87.241  37.780  1.00 43.51           C  
ANISOU 1514  CG  LEU A 198     8621   2856   5055  -1262   1315    248       C  
ATOM   1515  CD1 LEU A 198      20.285  86.275  37.292  1.00 44.59           C  
ANISOU 1515  CD1 LEU A 198     8788   2942   5210  -1370   1268    261       C  
ATOM   1516  CD2 LEU A 198      20.730  88.350  38.619  1.00 42.92           C  
ANISOU 1516  CD2 LEU A 198     8450   2855   5001  -1266   1337    293       C  
ATOM   1517  N   GLN A 199      24.498  84.123  39.675  1.00 43.02           N  
ANISOU 1517  N   GLN A 199     8756   2638   4952  -1055   1402    253       N  
ATOM   1518  CA  GLN A 199      25.875  83.653  39.771  1.00 43.00           C  
ANISOU 1518  CA  GLN A 199     8817   2608   4914   -959   1438    237       C  
ATOM   1519  C   GLN A 199      26.028  82.248  39.199  1.00 44.05           C  
ANISOU 1519  C   GLN A 199     9055   2651   5032   -969   1426    220       C  
ATOM   1520  O   GLN A 199      27.047  81.939  38.571  1.00 44.13           O  
ANISOU 1520  O   GLN A 199     9135   2633   5000   -903   1442    188       O  
ATOM   1521  CB  GLN A 199      26.350  83.688  41.222  1.00 42.74           C  
ANISOU 1521  CB  GLN A 199     8752   2598   4888   -901   1483    280       C  
ATOM   1522  CG  GLN A 199      27.849  83.504  41.361  1.00 42.55           C  
ANISOU 1522  CG  GLN A 199     8777   2564   4825   -795   1525    268       C  
ATOM   1523  CD  GLN A 199      28.269  83.113  42.761  1.00 42.65           C  
ANISOU 1523  CD  GLN A 199     8785   2576   4842   -746   1567    314       C  
ATOM   1524  OE1 GLN A 199      27.551  82.398  43.461  1.00 43.24           O  
ANISOU 1524  OE1 GLN A 199     8861   2623   4944   -787   1564    351       O  
ATOM   1525  NE2 GLN A 199      29.440  83.579  43.178  1.00 42.12           N  
ANISOU 1525  NE2 GLN A 199     8715   2541   4747   -658   1605    315       N  
ATOM   1526  N   ARG A 200      25.033  81.382  39.409  1.00 44.67           N  
ANISOU 1526  N   ARG A 200     9149   2682   5141  -1052   1399    245       N  
ATOM   1527  CA  ARG A 200      25.065  80.067  38.781  1.00 45.78           C  
ANISOU 1527  CA  ARG A 200     9397   2730   5267  -1074   1381    225       C  
ATOM   1528  C   ARG A 200      25.049  80.187  37.264  1.00 45.92           C  
ANISOU 1528  C   ARG A 200     9464   2730   5254  -1097   1345    168       C  
ATOM   1529  O   ARG A 200      25.666  79.379  36.562  1.00 46.54           O  
ANISOU 1529  O   ARG A 200     9645   2745   5294  -1064   1346    136       O  
ATOM   1530  CB  ARG A 200      23.880  79.220  39.249  1.00 46.74           C  
ANISOU 1530  CB  ARG A 200     9518   2807   5435  -1174   1352    265       C  
ATOM   1531  CG  ARG A 200      23.907  78.839  40.717  1.00 46.85           C  
ANISOU 1531  CG  ARG A 200     9502   2822   5476  -1149   1390    324       C  
ATOM   1532  CD  ARG A 200      22.756  77.904  41.064  1.00 47.95           C  
ANISOU 1532  CD  ARG A 200     9648   2908   5662  -1252   1360    366       C  
ATOM   1533  NE  ARG A 200      22.151  78.232  42.352  1.00 47.72           N  
ANISOU 1533  NE  ARG A 200     9528   2927   5675  -1269   1379    435       N  
ATOM   1534  CZ  ARG A 200      20.946  78.775  42.497  1.00 47.67           C  
ANISOU 1534  CZ  ARG A 200     9438   2966   5710  -1355   1351    471       C  
ATOM   1535  NH1 ARG A 200      20.204  79.044  41.432  1.00 47.85           N1+
ANISOU 1535  NH1 ARG A 200     9454   2991   5736  -1438   1302    444       N1+
ATOM   1536  NH2 ARG A 200      20.478  79.042  43.710  1.00 47.51           N  
ANISOU 1536  NH2 ARG A 200     9341   2989   5721  -1357   1376    538       N  
ATOM   1537  N   ARG A 201      24.360  81.201  36.740  1.00 45.67           N  
ANISOU 1537  N   ARG A 201     9365   2754   5234  -1149   1315    157       N  
ATOM   1538  CA  ARG A 201      24.143  81.269  35.303  1.00 45.93           C  
ANISOU 1538  CA  ARG A 201     9445   2767   5240  -1187   1275    107       C  
ATOM   1539  C   ARG A 201      25.280  81.987  34.583  1.00 45.17           C  
ANISOU 1539  C   ARG A 201     9364   2703   5098  -1092   1301     68       C  
ATOM   1540  O   ARG A 201      25.604  81.638  33.443  1.00 45.59           O  
ANISOU 1540  O   ARG A 201     9497   2715   5111  -1081   1285     26       O  
ATOM   1541  CB  ARG A 201      22.798  81.948  35.019  1.00 45.85           C  
ANISOU 1541  CB  ARG A 201     9361   2798   5262  -1293   1231    118       C  
ATOM   1542  CG  ARG A 201      22.426  82.003  33.553  1.00 46.22           C  
ANISOU 1542  CG  ARG A 201     9455   2824   5281  -1346   1185     70       C  
ATOM   1543  CD  ARG A 201      20.937  81.747  33.332  1.00 47.00           C  
ANISOU 1543  CD  ARG A 201     9534   2909   5413  -1484   1130     89       C  
ATOM   1544  NE  ARG A 201      20.077  82.724  33.995  1.00 46.39           N  
ANISOU 1544  NE  ARG A 201     9337   2910   5378  -1528   1133    136       N  
ATOM   1545  CZ  ARG A 201      19.254  82.438  35.000  1.00 46.75           C  
ANISOU 1545  CZ  ARG A 201     9329   2962   5470  -1587   1131    197       C  
ATOM   1546  NH1 ARG A 201      18.505  83.393  35.538  1.00 46.20           N1+
ANISOU 1546  NH1 ARG A 201     9154   2968   5431  -1617   1139    242       N1+
ATOM   1547  NH2 ARG A 201      19.171  81.198  35.462  1.00 47.70           N  
ANISOU 1547  NH2 ARG A 201     9504   3013   5608  -1613   1125    215       N  
ATOM   1548  N   HIS A 202      25.910  82.970  35.227  1.00 45.91           N  
ANISOU 1548  N   HIS A 202     9384   2866   5194  -1023   1340     84       N  
ATOM   1549  CA  HIS A 202      26.907  83.801  34.566  1.00 45.17           C  
ANISOU 1549  CA  HIS A 202     9288   2810   5064   -944   1362     55       C  
ATOM   1550  C   HIS A 202      28.258  83.847  35.268  1.00 44.74           C  
ANISOU 1550  C   HIS A 202     9240   2770   4991   -833   1418     70       C  
ATOM   1551  O   HIS A 202      29.210  84.392  34.697  1.00 44.28           O  
ANISOU 1551  O   HIS A 202     9189   2734   4900   -763   1440     50       O  
ATOM   1552  CB  HIS A 202      26.376  85.234  34.404  1.00 44.27           C  
ANISOU 1552  CB  HIS A 202     9077   2775   4969   -973   1352     54       C  
ATOM   1553  CG  HIS A 202      25.100  85.319  33.624  1.00 44.65           C  
ANISOU 1553  CG  HIS A 202     9118   2817   5031  -1077   1300     42       C  
ATOM   1554  ND1 HIS A 202      25.056  85.172  32.254  1.00 45.03           N  
ANISOU 1554  ND1 HIS A 202     9227   2834   5046  -1095   1271     -1       N  
ATOM   1555  CD2 HIS A 202      23.824  85.538  34.021  1.00 44.77           C  
ANISOU 1555  CD2 HIS A 202     9072   2853   5086  -1168   1274     71       C  
ATOM   1556  CE1 HIS A 202      23.807  85.296  31.841  1.00 45.36           C  
ANISOU 1556  CE1 HIS A 202     9248   2880   5108  -1198   1227     -1       C  
ATOM   1557  NE2 HIS A 202      23.040  85.520  32.893  1.00 45.22           N  
ANISOU 1557  NE2 HIS A 202     9153   2894   5134  -1244   1229     46       N  
ATOM   1558  N   GLY A 203      28.376  83.302  36.468  1.00 43.12           N  
ANISOU 1558  N   GLY A 203     9029   2552   4802   -817   1443    107       N  
ATOM   1559  CA  GLY A 203      29.650  83.300  37.157  1.00 42.81           C  
ANISOU 1559  CA  GLY A 203     8999   2525   4742   -715   1496    125       C  
ATOM   1560  C   GLY A 203      29.985  84.638  37.790  1.00 41.74           C  
ANISOU 1560  C   GLY A 203     8768   2472   4619   -683   1517    139       C  
ATOM   1561  O   GLY A 203      29.146  85.534  37.926  1.00 41.24           O  
ANISOU 1561  O   GLY A 203     8627   2458   4585   -739   1496    142       O  
ATOM   1562  N   GLY A 204      31.250  84.767  38.185  1.00 41.21           N  
ANISOU 1562  N   GLY A 204     8712   2419   4527   -591   1562    150       N  
ATOM   1563  CA  GLY A 204      31.720  85.961  38.853  1.00 40.32           C  
ANISOU 1563  CA  GLY A 204     8521   2377   4421   -556   1583    165       C  
ATOM   1564  C   GLY A 204      31.233  86.048  40.280  1.00 40.20           C  
ANISOU 1564  C   GLY A 204     8453   2384   4436   -576   1593    204       C  
ATOM   1565  O   GLY A 204      30.461  85.218  40.762  1.00 40.78           O  
ANISOU 1565  O   GLY A 204     8541   2422   4530   -621   1582    224       O  
ATOM   1566  N   GLY A 205      31.707  87.082  40.973  1.00 39.50           N  
ANISOU 1566  N   GLY A 205     8305   2354   4350   -543   1613    217       N  
ATOM   1567  CA  GLY A 205      31.334  87.292  42.359  1.00 39.36           C  
ANISOU 1567  CA  GLY A 205     8238   2363   4353   -552   1626    254       C  
ATOM   1568  C   GLY A 205      31.025  88.738  42.687  1.00 38.56           C  
ANISOU 1568  C   GLY A 205     8056   2330   4265   -570   1620    253       C  
ATOM   1569  O   GLY A 205      30.905  89.573  41.787  1.00 38.14           O  
ANISOU 1569  O   GLY A 205     7977   2303   4211   -588   1602    222       O  
ATOM   1570  N   LEU A 206      30.890  89.043  43.972  1.00 38.39           N  
ANISOU 1570  N   LEU A 206     7998   2335   4252   -562   1638    286       N  
ATOM   1571  CA  LEU A 206      30.663  90.399  44.449  1.00 37.72           C  
ANISOU 1571  CA  LEU A 206     7847   2311   4174   -571   1638    287       C  
ATOM   1572  C   LEU A 206      31.916  90.898  45.152  1.00 37.41           C  
ANISOU 1572  C   LEU A 206     7810   2294   4110   -502   1670    297       C  
ATOM   1573  O   LEU A 206      32.452  90.218  46.033  1.00 37.75           O  
ANISOU 1573  O   LEU A 206     7883   2319   4141   -461   1696    328       O  
ATOM   1574  CB  LEU A 206      29.465  90.463  45.402  1.00 37.83           C  
ANISOU 1574  CB  LEU A 206     7821   2341   4212   -616   1635    321       C  
ATOM   1575  CG  LEU A 206      28.063  90.452  44.787  1.00 38.00           C  
ANISOU 1575  CG  LEU A 206     7816   2361   4262   -695   1602    318       C  
ATOM   1576  CD1 LEU A 206      27.980  91.398  43.596  1.00 37.52           C  
ANISOU 1576  CD1 LEU A 206     7733   2326   4198   -714   1581    277       C  
ATOM   1577  CD2 LEU A 206      27.638  89.047  44.400  1.00 38.79           C  
ANISOU 1577  CD2 LEU A 206     7964   2400   4375   -731   1586    325       C  
ATOM   1578  N   VAL A 207      32.377  92.082  44.758  1.00 37.97           N  
ANISOU 1578  N   VAL A 207     7851   2403   4174   -493   1666    274       N  
ATOM   1579  CA  VAL A 207      33.562  92.710  45.327  1.00 37.70           C  
ANISOU 1579  CA  VAL A 207     7817   2391   4118   -440   1690    283       C  
ATOM   1580  C   VAL A 207      33.174  94.082  45.861  1.00 37.19           C  
ANISOU 1580  C   VAL A 207     7699   2374   4058   -463   1684    279       C  
ATOM   1581  O   VAL A 207      32.413  94.816  45.221  1.00 36.88           O  
ANISOU 1581  O   VAL A 207     7624   2355   4033   -505   1663    255       O  
ATOM   1582  CB  VAL A 207      34.694  92.825  44.285  1.00 37.61           C  
ANISOU 1582  CB  VAL A 207     7829   2371   4090   -402   1695    263       C  
ATOM   1583  CG1 VAL A 207      35.836  93.676  44.821  1.00 37.33           C  
ANISOU 1583  CG1 VAL A 207     7783   2364   4037   -362   1714    277       C  
ATOM   1584  CG2 VAL A 207      35.195  91.445  43.893  1.00 38.21           C  
ANISOU 1584  CG2 VAL A 207     7970   2396   4151   -364   1710    273       C  
ATOM   1585  N   ARG A 208      33.692  94.416  47.040  1.00 38.17           N  
ANISOU 1585  N   ARG A 208     7824   2514   4166   -434   1705    304       N  
ATOM   1586  CA  ARG A 208      33.526  95.734  47.638  1.00 37.77           C  
ANISOU 1586  CA  ARG A 208     7740   2502   4110   -448   1704    300       C  
ATOM   1587  C   ARG A 208      34.788  96.549  47.377  1.00 37.52           C  
ANISOU 1587  C   ARG A 208     7711   2482   4060   -422   1707    287       C  
ATOM   1588  O   ARG A 208      35.882  96.155  47.794  1.00 37.75           O  
ANISOU 1588  O   ARG A 208     7772   2501   4069   -379   1726    311       O  
ATOM   1589  CB  ARG A 208      33.254  95.617  49.138  1.00 37.99           C  
ANISOU 1589  CB  ARG A 208     7775   2536   4124   -435   1723    337       C  
ATOM   1590  CG  ARG A 208      33.311  96.933  49.897  1.00 37.70           C  
ANISOU 1590  CG  ARG A 208     7723   2531   4069   -437   1727    334       C  
ATOM   1591  CD  ARG A 208      32.053  97.762  49.700  1.00 37.44           C  
ANISOU 1591  CD  ARG A 208     7653   2520   4051   -479   1714    318       C  
ATOM   1592  NE  ARG A 208      32.147  99.048  50.384  1.00 37.22           N  
ANISOU 1592  NE  ARG A 208     7624   2516   4001   -477   1720    312       N  
ATOM   1593  CZ  ARG A 208      31.149  99.920  50.484  1.00 37.05           C  
ANISOU 1593  CZ  ARG A 208     7581   2515   3982   -500   1720    305       C  
ATOM   1594  NH1 ARG A 208      29.969  99.645  49.946  1.00 37.07           N1+
ANISOU 1594  NH1 ARG A 208     7553   2520   4010   -529   1713    309       N1+
ATOM   1595  NH2 ARG A 208      31.331 101.067  51.125  1.00 36.93           N  
ANISOU 1595  NH2 ARG A 208     7580   2513   3940   -493   1727    298       N  
ATOM   1596  N   VAL A 209      34.634  97.671  46.684  1.00 38.64           N  
ANISOU 1596  N   VAL A 209     7822   2648   4211   -449   1690    256       N  
ATOM   1597  CA  VAL A 209      35.760  98.537  46.332  1.00 38.42           C  
ANISOU 1597  CA  VAL A 209     7793   2632   4174   -436   1690    245       C  
ATOM   1598  C   VAL A 209      35.968  99.521  47.474  1.00 38.34           C  
ANISOU 1598  C   VAL A 209     7781   2641   4146   -441   1695    254       C  
ATOM   1599  O   VAL A 209      35.045 100.288  47.793  1.00 38.15           O  
ANISOU 1599  O   VAL A 209     7737   2634   4125   -470   1688    241       O  
ATOM   1600  CB  VAL A 209      35.507  99.271  45.009  1.00 38.07           C  
ANISOU 1600  CB  VAL A 209     7717   2600   4147   -461   1672    209       C  
ATOM   1601  CG1 VAL A 209      36.710 100.122  44.632  1.00 37.91           C  
ANISOU 1601  CG1 VAL A 209     7694   2589   4122   -449   1674    205       C  
ATOM   1602  CG2 VAL A 209      35.185  98.273  43.908  1.00 38.22           C  
ANISOU 1602  CG2 VAL A 209     7747   2596   4177   -460   1665    200       C  
ATOM   1603  N   PRO A 210      37.148  99.549  48.106  1.00 39.27           N  
ANISOU 1603  N   PRO A 210     7926   2755   4239   -414   1708    280       N  
ATOM   1604  CA  PRO A 210      37.351 100.433  49.267  1.00 39.30           C  
ANISOU 1604  CA  PRO A 210     7942   2773   4218   -424   1710    290       C  
ATOM   1605  C   PRO A 210      37.194 101.912  48.954  1.00 38.96           C  
ANISOU 1605  C   PRO A 210     7877   2747   4180   -463   1692    254       C  
ATOM   1606  O   PRO A 210      36.973 102.705  49.877  1.00 39.00           O  
ANISOU 1606  O   PRO A 210     7897   2758   4164   -477   1691    252       O  
ATOM   1607  CB  PRO A 210      38.785 100.105  49.710  1.00 39.64           C  
ANISOU 1607  CB  PRO A 210     8018   2810   4233   -391   1725    329       C  
ATOM   1608  CG  PRO A 210      39.429  99.483  48.509  1.00 39.66           C  
ANISOU 1608  CG  PRO A 210     8016   2800   4252   -367   1729    331       C  
ATOM   1609  CD  PRO A 210      38.339  98.739  47.808  1.00 39.55           C  
ANISOU 1609  CD  PRO A 210     7989   2774   4266   -371   1724    307       C  
ATOM   1610  N   LEU A 211      37.287 102.309  47.686  1.00 39.92           N  
ANISOU 1610  N   LEU A 211     7969   2872   4326   -476   1679    227       N  
ATOM   1611  CA  LEU A 211      37.117 103.706  47.302  1.00 39.64           C  
ANISOU 1611  CA  LEU A 211     7911   2852   4298   -510   1664    195       C  
ATOM   1612  C   LEU A 211      35.644 104.101  47.299  1.00 39.42           C  
ANISOU 1612  C   LEU A 211     7862   2836   4279   -528   1661    175       C  
ATOM   1613  O   LEU A 211      35.156 104.687  46.327  1.00 39.14           O  
ANISOU 1613  O   LEU A 211     7796   2813   4263   -544   1652    150       O  
ATOM   1614  CB  LEU A 211      37.727 103.956  45.922  1.00 39.45           C  
ANISOU 1614  CB  LEU A 211     7863   2831   4297   -513   1656    182       C  
ATOM   1615  CG  LEU A 211      39.229 103.720  45.764  1.00 39.69           C  
ANISOU 1615  CG  LEU A 211     7910   2852   4320   -494   1664    210       C  
ATOM   1616  CD1 LEU A 211      39.583 103.639  44.290  1.00 39.56           C  
ANISOU 1616  CD1 LEU A 211     7871   2834   4325   -484   1665    202       C  
ATOM   1617  CD2 LEU A 211      40.031 104.820  46.447  1.00 39.83           C  
ANISOU 1617  CD2 LEU A 211     7940   2873   4322   -524   1657    216       C  
ATOM   1618  N   SER A 212      34.931 103.792  48.379  1.00 39.55           N  
ANISOU 1618  N   SER A 212     7897   2850   4278   -521   1673    192       N  
ATOM   1619  CA  SER A 212      33.500 104.051  48.463  1.00 39.44           C  
ANISOU 1619  CA  SER A 212     7867   2848   4272   -533   1677    187       C  
ATOM   1620  C   SER A 212      33.151 104.501  49.871  1.00 39.65           C  
ANISOU 1620  C   SER A 212     7927   2873   4265   -526   1692    201       C  
ATOM   1621  O   SER A 212      33.567 103.868  50.845  1.00 39.95           O  
ANISOU 1621  O   SER A 212     7996   2901   4281   -506   1703    229       O  
ATOM   1622  CB  SER A 212      32.695 102.799  48.092  1.00 39.53           C  
ANISOU 1622  CB  SER A 212     7861   2855   4304   -531   1679    203       C  
ATOM   1623  OG  SER A 212      31.311 103.088  47.997  1.00 39.46           O  
ANISOU 1623  OG  SER A 212     7829   2858   4304   -550   1682    204       O  
ATOM   1624  N   ARG A 213      32.392 105.592  49.972  1.00 38.04           N  
ANISOU 1624  N   ARG A 213     7722   2677   4053   -537   1697    186       N  
ATOM   1625  CA  ARG A 213      31.932 106.064  51.270  1.00 38.28           C  
ANISOU 1625  CA  ARG A 213     7795   2704   4047   -524   1716    201       C  
ATOM   1626  C   ARG A 213      31.119 104.980  51.967  1.00 38.52           C  
ANISOU 1626  C   ARG A 213     7824   2737   4076   -505   1736    242       C  
ATOM   1627  O   ARG A 213      30.461 104.155  51.327  1.00 38.47           O  
ANISOU 1627  O   ARG A 213     7778   2737   4101   -513   1734    253       O  
ATOM   1628  CB  ARG A 213      31.090 107.333  51.117  1.00 38.17           C  
ANISOU 1628  CB  ARG A 213     7781   2696   4025   -531   1725    181       C  
ATOM   1629  CG  ARG A 213      31.891 108.581  50.789  1.00 38.07           C  
ANISOU 1629  CG  ARG A 213     7786   2675   4005   -549   1709    143       C  
ATOM   1630  CD  ARG A 213      30.982 109.722  50.361  1.00 37.95           C  
ANISOU 1630  CD  ARG A 213     7765   2665   3989   -551   1720    126       C  
ATOM   1631  NE  ARG A 213      31.658 110.635  49.443  1.00 37.76           N  
ANISOU 1631  NE  ARG A 213     7725   2641   3980   -573   1700     91       N  
ATOM   1632  CZ  ARG A 213      31.988 111.889  49.732  1.00 37.90           C  
ANISOU 1632  CZ  ARG A 213     7783   2642   3976   -582   1697     66       C  
ATOM   1633  NH1 ARG A 213      32.604 112.638  48.825  1.00 37.75           N1+
ANISOU 1633  NH1 ARG A 213     7742   2625   3977   -605   1679     40       N1+
ATOM   1634  NH2 ARG A 213      31.694 112.401  50.919  1.00 38.25           N  
ANISOU 1634  NH2 ARG A 213     7894   2664   3974   -568   1713     67       N  
ATOM   1635  N   ASN A 214      31.172 104.986  53.296  1.00 37.71           N  
ANISOU 1635  N   ASN A 214     7767   2629   3933   -482   1755    267       N  
ATOM   1636  CA  ASN A 214      30.482 103.977  54.091  1.00 38.01           C  
ANISOU 1636  CA  ASN A 214     7805   2671   3966   -459   1776    313       C  
ATOM   1637  C   ASN A 214      28.967 104.133  54.077  1.00 38.04           C  
ANISOU 1637  C   ASN A 214     7782   2691   3980   -460   1795    333       C  
ATOM   1638  O   ASN A 214      28.279 103.338  54.727  1.00 38.33           O  
ANISOU 1638  O   ASN A 214     7812   2736   4018   -445   1814    377       O  
ATOM   1639  CB  ASN A 214      30.990 104.015  55.534  1.00 38.39           C  
ANISOU 1639  CB  ASN A 214     7913   2714   3959   -428   1794    339       C  
ATOM   1640  CG  ASN A 214      32.458 103.655  55.646  1.00 38.47           C  
ANISOU 1640  CG  ASN A 214     7949   2712   3957   -425   1779    337       C  
ATOM   1641  OD1 ASN A 214      32.978 102.867  54.855  1.00 38.35           O  
ANISOU 1641  OD1 ASN A 214     7904   2693   3976   -432   1766    335       O  
ATOM   1642  ND2 ASN A 214      33.134 104.229  56.633  1.00 38.75           N  
ANISOU 1642  ND2 ASN A 214     8019   2764   3939   -408   1770    331       N  
ATOM   1643  N   SER A 215      28.431 105.115  53.355  1.00 38.47           N  
ANISOU 1643  N   SER A 215     7819   2753   4044   -476   1792    307       N  
ATOM   1644  CA  SER A 215      27.002 105.396  53.353  1.00 38.56           C  
ANISOU 1644  CA  SER A 215     7807   2783   4060   -474   1815    333       C  
ATOM   1645  C   SER A 215      26.224 104.578  52.329  1.00 38.44           C  
ANISOU 1645  C   SER A 215     7730   2779   4095   -505   1802    346       C  
ATOM   1646  O   SER A 215      24.993 104.676  52.290  1.00 38.58           O  
ANISOU 1646  O   SER A 215     7721   2815   4121   -509   1819    378       O  
ATOM   1647  CB  SER A 215      26.764 106.892  53.114  1.00 38.70           C  
ANISOU 1647  CB  SER A 215     7846   2802   4058   -470   1824    305       C  
ATOM   1648  OG  SER A 215      27.631 107.400  52.115  1.00 38.53           O  
ANISOU 1648  OG  SER A 215     7815   2770   4054   -494   1795    255       O  
ATOM   1649  N   THR A 216      26.900 103.785  51.497  1.00 39.14           N  
ANISOU 1649  N   THR A 216     7801   2856   4215   -528   1773    326       N  
ATOM   1650  CA  THR A 216      26.233 102.883  50.570  1.00 39.17           C  
ANISOU 1650  CA  THR A 216     7760   2862   4260   -561   1757    337       C  
ATOM   1651  C   THR A 216      26.856 101.498  50.671  1.00 39.36           C  
ANISOU 1651  C   THR A 216     7792   2865   4297   -561   1745    347       C  
ATOM   1652  O   THR A 216      28.055 101.353  50.921  1.00 39.32           O  
ANISOU 1652  O   THR A 216     7816   2846   4277   -540   1740    331       O  
ATOM   1653  CB  THR A 216      26.313 103.369  49.109  1.00 38.80           C  
ANISOU 1653  CB  THR A 216     7689   2820   4236   -587   1734    297       C  
ATOM   1654  OG1 THR A 216      27.642 103.182  48.609  1.00 38.60           O  
ANISOU 1654  OG1 THR A 216     7676   2779   4212   -582   1713    261       O  
ATOM   1655  CG2 THR A 216      25.931 104.840  49.002  1.00 38.60           C  
ANISOU 1655  CG2 THR A 216     7664   2810   4193   -579   1749    282       C  
ATOM   1656  N   HIS A 217      26.021 100.480  50.467  1.00 39.98           N  
ANISOU 1656  N   HIS A 217     7847   2939   4404   -587   1740    378       N  
ATOM   1657  CA  HIS A 217      26.438  99.086  50.497  1.00 40.26           C  
ANISOU 1657  CA  HIS A 217     7894   2948   4454   -589   1730    391       C  
ATOM   1658  C   HIS A 217      26.798  98.558  49.113  1.00 40.10           C  
ANISOU 1658  C   HIS A 217     7869   2909   4458   -616   1700    356       C  
ATOM   1659  O   HIS A 217      26.898  97.339  48.931  1.00 40.32           O  
ANISOU 1659  O   HIS A 217     7909   2909   4501   -625   1691    367       O  
ATOM   1660  CB  HIS A 217      25.331  98.226  51.113  1.00 40.56           C  
ANISOU 1660  CB  HIS A 217     7916   2986   4508   -606   1742    448       C  
ATOM   1661  CG  HIS A 217      25.831  97.004  51.817  1.00 40.86           C  
ANISOU 1661  CG  HIS A 217     7981   2999   4547   -587   1749    474       C  
ATOM   1662  ND1 HIS A 217      26.643  96.071  51.209  1.00 41.04           N  
ANISOU 1662  ND1 HIS A 217     8025   2988   4580   -588   1732    453       N  
ATOM   1663  CD2 HIS A 217      25.625  96.558  53.078  1.00 41.22           C  
ANISOU 1663  CD2 HIS A 217     8035   3047   4579   -561   1776    523       C  
ATOM   1664  CE1 HIS A 217      26.920  95.105  52.067  1.00 41.50           C  
ANISOU 1664  CE1 HIS A 217     8107   3028   4634   -563   1749    488       C  
ATOM   1665  NE2 HIS A 217      26.314  95.377  53.209  1.00 41.50           N  
ANISOU 1665  NE2 HIS A 217     8098   3051   4621   -548   1774    531       N  
ATOM   1666  N   GLU A 218      27.002  99.448  48.143  1.00 40.17           N  
ANISOU 1666  N   GLU A 218     7865   2929   4467   -625   1687    317       N  
ATOM   1667  CA  GLU A 218      27.140  99.034  46.752  1.00 39.90           C  
ANISOU 1667  CA  GLU A 218     7826   2882   4453   -650   1660    288       C  
ATOM   1668  C   GLU A 218      28.359  98.138  46.563  1.00 40.06           C  
ANISOU 1668  C   GLU A 218     7880   2873   4468   -624   1654    275       C  
ATOM   1669  O   GLU A 218      29.444  98.414  47.083  1.00 40.07           O  
ANISOU 1669  O   GLU A 218     7901   2875   4449   -587   1666    269       O  
ATOM   1670  CB  GLU A 218      27.228 100.263  45.840  1.00 39.46           C  
ANISOU 1670  CB  GLU A 218     7750   2847   4394   -654   1653    253       C  
ATOM   1671  CG  GLU A 218      28.507 101.083  45.964  1.00 39.30           C  
ANISOU 1671  CG  GLU A 218     7745   2833   4354   -619   1658    225       C  
ATOM   1672  CD  GLU A 218      28.467 102.350  45.132  1.00 39.17           C  
ANISOU 1672  CD  GLU A 218     7708   2837   4338   -626   1654    196       C  
ATOM   1673  OE1 GLU A 218      27.418 103.030  45.138  1.00 39.18           O  
ANISOU 1673  OE1 GLU A 218     7689   2856   4341   -641   1662    205       O  
ATOM   1674  OE2 GLU A 218      29.477 102.664  44.465  1.00 38.95           O1+
ANISOU 1674  OE2 GLU A 218     7684   2808   4308   -614   1645    169       O1+
ATOM   1675  N   MET A 219      28.160  97.044  45.834  1.00 38.03           N  
ANISOU 1675  N   MET A 219     7634   2587   4227   -646   1638    275       N  
ATOM   1676  CA  MET A 219      29.225  96.128  45.462  1.00 38.21           C  
ANISOU 1676  CA  MET A 219     7696   2577   4243   -619   1636    263       C  
ATOM   1677  C   MET A 219      29.134  95.869  43.967  1.00 38.21           C  
ANISOU 1677  C   MET A 219     7703   2563   4253   -643   1611    233       C  
ATOM   1678  O   MET A 219      28.054  95.943  43.375  1.00 38.27           O  
ANISOU 1678  O   MET A 219     7690   2575   4277   -691   1594    231       O  
ATOM   1679  CB  MET A 219      29.135  94.802  46.233  1.00 38.76           C  
ANISOU 1679  CB  MET A 219     7796   2614   4316   -613   1646    298       C  
ATOM   1680  CG  MET A 219      28.900  94.966  47.728  1.00 38.86           C  
ANISOU 1680  CG  MET A 219     7801   2643   4321   -596   1670    336       C  
ATOM   1681  SD  MET A 219      28.838  93.398  48.617  1.00 39.55           S  
ANISOU 1681  SD  MET A 219     7923   2692   4414   -583   1686    382       S  
ATOM   1682  CE  MET A 219      30.558  92.906  48.560  1.00 39.59           C  
ANISOU 1682  CE  MET A 219     7978   2672   4391   -518   1701    370       C  
ATOM   1683  N   TYR A 220      30.273  95.568  43.356  1.00 37.78           N  
ANISOU 1683  N   TYR A 220     7680   2491   4185   -608   1613    213       N  
ATOM   1684  CA  TYR A 220      30.343  95.376  41.915  1.00 37.80           C  
ANISOU 1684  CA  TYR A 220     7698   2478   4188   -620   1595    183       C  
ATOM   1685  C   TYR A 220      30.412  93.892  41.586  1.00 38.41           C  
ANISOU 1685  C   TYR A 220     7828   2503   4262   -620   1589    187       C  
ATOM   1686  O   TYR A 220      31.277  93.174  42.098  1.00 38.67           O  
ANISOU 1686  O   TYR A 220     7899   2511   4281   -575   1609    201       O  
ATOM   1687  CB  TYR A 220      31.544  96.114  41.325  1.00 37.43           C  
ANISOU 1687  CB  TYR A 220     7652   2445   4125   -579   1603    161       C  
ATOM   1688  CG  TYR A 220      31.412  97.616  41.417  1.00 36.90           C  
ANISOU 1688  CG  TYR A 220     7536   2423   4062   -587   1604    152       C  
ATOM   1689  CD1 TYR A 220      31.921  98.311  42.504  1.00 36.71           C  
ANISOU 1689  CD1 TYR A 220     7499   2419   4029   -565   1621    164       C  
ATOM   1690  CD2 TYR A 220      30.763  98.336  40.423  1.00 36.66           C  
ANISOU 1690  CD2 TYR A 220     7479   2410   4040   -617   1590    131       C  
ATOM   1691  CE1 TYR A 220      31.798  99.685  42.595  1.00 36.30           C  
ANISOU 1691  CE1 TYR A 220     7414   2401   3978   -574   1622    154       C  
ATOM   1692  CE2 TYR A 220      30.634  99.709  40.505  1.00 36.23           C  
ANISOU 1692  CE2 TYR A 220     7386   2392   3988   -621   1594    123       C  
ATOM   1693  CZ  TYR A 220      31.153 100.378  41.592  1.00 36.07           C  
ANISOU 1693  CZ  TYR A 220     7357   2388   3959   -600   1610    133       C  
ATOM   1694  OH  TYR A 220      31.025 101.745  41.673  1.00 35.72           O  
ANISOU 1694  OH  TYR A 220     7284   2373   3915   -605   1614    124       O  
ATOM   1695  N   TRP A 221      29.491  93.441  40.739  1.00 36.36           N  
ANISOU 1695  N   TRP A 221     7577   2224   4015   -670   1563    176       N  
ATOM   1696  CA  TRP A 221      29.474  92.071  40.237  1.00 37.02           C  
ANISOU 1696  CA  TRP A 221     7722   2251   4094   -679   1552    173       C  
ATOM   1697  C   TRP A 221      30.496  91.978  39.111  1.00 37.00           C  
ANISOU 1697  C   TRP A 221     7762   2231   4065   -636   1555    142       C  
ATOM   1698  O   TRP A 221      30.232  92.390  37.979  1.00 36.87           O  
ANISOU 1698  O   TRP A 221     7743   2221   4046   -657   1537    115       O  
ATOM   1699  CB  TRP A 221      28.072  91.698  39.767  1.00 37.41           C  
ANISOU 1699  CB  TRP A 221     7765   2285   4164   -758   1519    174       C  
ATOM   1700  CG  TRP A 221      27.939  90.311  39.215  1.00 38.19           C  
ANISOU 1700  CG  TRP A 221     7932   2319   4258   -780   1502    168       C  
ATOM   1701  CD1 TRP A 221      28.782  89.259  39.421  1.00 38.63           C  
ANISOU 1701  CD1 TRP A 221     8052   2329   4298   -734   1519    171       C  
ATOM   1702  CD2 TRP A 221      26.897  89.829  38.357  1.00 38.69           C  
ANISOU 1702  CD2 TRP A 221     8014   2354   4333   -854   1464    157       C  
ATOM   1703  NE1 TRP A 221      28.328  88.151  38.746  1.00 39.39           N  
ANISOU 1703  NE1 TRP A 221     8208   2367   4393   -773   1494    161       N  
ATOM   1704  CE2 TRP A 221      27.173  88.476  38.085  1.00 39.45           C  
ANISOU 1704  CE2 TRP A 221     8189   2384   4418   -851   1458    151       C  
ATOM   1705  CE3 TRP A 221      25.757  90.411  37.795  1.00 38.63           C  
ANISOU 1705  CE3 TRP A 221     7967   2370   4342   -923   1437    155       C  
ATOM   1706  CZ2 TRP A 221      26.352  87.696  37.275  1.00 40.18           C  
ANISOU 1706  CZ2 TRP A 221     8324   2428   4514   -920   1420    139       C  
ATOM   1707  CZ3 TRP A 221      24.945  89.636  36.990  1.00 39.33           C  
ANISOU 1707  CZ3 TRP A 221     8094   2415   4435   -993   1400    146       C  
ATOM   1708  CH2 TRP A 221      25.245  88.292  36.738  1.00 40.11           C  
ANISOU 1708  CH2 TRP A 221     8273   2444   4522   -994   1389    136       C  
ATOM   1709  N   VAL A 222      31.674  91.445  39.422  1.00 37.16           N  
ANISOU 1709  N   VAL A 222     7824   2230   4065   -571   1583    151       N  
ATOM   1710  CA  VAL A 222      32.767  91.357  38.466  1.00 37.19           C  
ANISOU 1710  CA  VAL A 222     7871   2218   4040   -518   1595    133       C  
ATOM   1711  C   VAL A 222      32.979  89.893  38.090  1.00 37.97           C  
ANISOU 1711  C   VAL A 222     8055   2252   4120   -499   1598    132       C  
ATOM   1712  O   VAL A 222      32.460  88.979  38.731  1.00 38.46           O  
ANISOU 1712  O   VAL A 222     8139   2282   4192   -522   1595    149       O  
ATOM   1713  CB  VAL A 222      34.064  91.992  39.008  1.00 36.82           C  
ANISOU 1713  CB  VAL A 222     7809   2198   3980   -451   1629    149       C  
ATOM   1714  CG1 VAL A 222      33.816  93.440  39.401  1.00 36.13           C  
ANISOU 1714  CG1 VAL A 222     7648   2170   3912   -475   1623    147       C  
ATOM   1715  CG2 VAL A 222      34.592  91.197  40.189  1.00 37.16           C  
ANISOU 1715  CG2 VAL A 222     7882   2222   4017   -412   1656    184       C  
ATOM   1716  N   SER A 223      33.765  89.679  37.034  1.00 38.13           N  
ANISOU 1716  N   SER A 223     8127   2251   4112   -454   1607    114       N  
ATOM   1717  CA  SER A 223      33.925  88.359  36.433  1.00 38.94           C  
ANISOU 1717  CA  SER A 223     8321   2286   4187   -435   1608    106       C  
ATOM   1718  C   SER A 223      35.127  87.585  36.956  1.00 39.32           C  
ANISOU 1718  C   SER A 223     8426   2306   4209   -350   1653    133       C  
ATOM   1719  O   SER A 223      35.082  86.351  36.991  1.00 40.08           O  
ANISOU 1719  O   SER A 223     8594   2344   4289   -339   1658    138       O  
ATOM   1720  CB  SER A 223      34.037  88.486  34.908  1.00 39.02           C  
ANISOU 1720  CB  SER A 223     8369   2284   4174   -430   1595     71       C  
ATOM   1721  OG  SER A 223      35.045  89.415  34.541  1.00 38.50           O  
ANISOU 1721  OG  SER A 223     8279   2255   4096   -372   1620     73       O  
ATOM   1722  N   GLY A 224      36.197  88.267  37.357  1.00 40.63           N  
ANISOU 1722  N   GLY A 224     8564   2508   4366   -288   1687    154       N  
ATOM   1723  CA  GLY A 224      37.356  87.594  37.903  1.00 41.02           C  
ANISOU 1723  CA  GLY A 224     8663   2534   4388   -202   1733    188       C  
ATOM   1724  C   GLY A 224      37.248  87.181  39.350  1.00 41.15           C  
ANISOU 1724  C   GLY A 224     8667   2550   4419   -201   1748    223       C  
ATOM   1725  O   GLY A 224      38.220  86.676  39.918  1.00 41.47           O  
ANISOU 1725  O   GLY A 224     8743   2576   4436   -126   1790    258       O  
ATOM   1726  N   ALA A 225      36.091  87.385  39.969  1.00 41.03           N  
ANISOU 1726  N   ALA A 225     8602   2550   4438   -278   1718    219       N  
ATOM   1727  CA  ALA A 225      35.857  87.002  41.352  1.00 41.18           C  
ANISOU 1727  CA  ALA A 225     8608   2569   4471   -281   1731    254       C  
ATOM   1728  C   ALA A 225      35.032  85.724  41.411  1.00 41.94           C  
ANISOU 1728  C   ALA A 225     8754   2606   4574   -317   1719    256       C  
ATOM   1729  O   ALA A 225      34.340  85.360  40.458  1.00 42.23           O  
ANISOU 1729  O   ALA A 225     8818   2613   4615   -366   1687    226       O  
ATOM   1730  CB  ALA A 225      35.145  88.120  42.116  1.00 40.53           C  
ANISOU 1730  CB  ALA A 225     8437   2543   4419   -335   1712    258       C  
ATOM   1731  N   LYS A 226      35.121  85.037  42.552  1.00 44.38           N  
ANISOU 1731  N   LYS A 226     9078   2898   4885   -294   1744    294       N  
ATOM   1732  CA  LYS A 226      34.318  83.835  42.750  1.00 45.14           C  
ANISOU 1732  CA  LYS A 226     9219   2938   4995   -333   1734    303       C  
ATOM   1733  C   LYS A 226      34.010  83.590  44.224  1.00 45.26           C  
ANISOU 1733  C   LYS A 226     9207   2961   5029   -335   1753    348       C  
ATOM   1734  O   LYS A 226      33.621  82.472  44.582  1.00 46.00           O  
ANISOU 1734  O   LYS A 226     9346   3003   5130   -346   1758    368       O  
ATOM   1735  CB  LYS A 226      35.024  82.614  42.146  1.00 45.97           C  
ANISOU 1735  CB  LYS A 226     9428   2974   5063   -275   1758    300       C  
ATOM   1736  CG  LYS A 226      36.412  82.347  42.704  1.00 46.11           C  
ANISOU 1736  CG  LYS A 226     9481   2993   5045   -165   1816    336       C  
ATOM   1737  CD  LYS A 226      37.115  81.239  41.933  1.00 46.93           C  
ANISOU 1737  CD  LYS A 226     9692   3032   5107   -100   1842    331       C  
ATOM   1738  CE  LYS A 226      36.203  80.038  41.745  1.00 47.80           C  
ANISOU 1738  CE  LYS A 226     9866   3070   5227   -155   1821    320       C  
ATOM   1739  NZ  LYS A 226      35.696  79.538  43.052  1.00 48.08           N1+
ANISOU 1739  NZ  LYS A 226     9882   3095   5290   -177   1832    360       N1+
ATOM   1740  N   SER A 227      34.182  84.593  45.083  1.00 46.86           N  
ANISOU 1740  N   SER A 227     9343   3225   5239   -323   1762    366       N  
ATOM   1741  CA  SER A 227      33.799  84.464  46.480  1.00 47.04           C  
ANISOU 1741  CA  SER A 227     9336   3259   5276   -327   1778    410       C  
ATOM   1742  C   SER A 227      32.311  84.158  46.594  1.00 47.25           C  
ANISOU 1742  C   SER A 227     9339   3272   5344   -417   1745    414       C  
ATOM   1743  O   SER A 227      31.501  84.625  45.788  1.00 47.00           O  
ANISOU 1743  O   SER A 227     9277   3249   5330   -484   1706    383       O  
ATOM   1744  CB  SER A 227      34.140  85.749  47.232  1.00 46.56           C  
ANISOU 1744  CB  SER A 227     9211   3268   5213   -309   1787    421       C  
ATOM   1745  OG  SER A 227      33.799  86.886  46.462  1.00 45.95           O  
ANISOU 1745  OG  SER A 227     9084   3229   5146   -353   1755    382       O  
ATOM   1746  N   ASN A 228      31.957  83.358  47.597  1.00 45.26           N  
ANISOU 1746  N   ASN A 228     9099   2996   5104   -417   1763    457       N  
ATOM   1747  CA  ASN A 228      30.562  82.993  47.804  1.00 45.64           C  
ANISOU 1747  CA  ASN A 228     9122   3026   5191   -501   1736    474       C  
ATOM   1748  C   ASN A 228      29.727  84.239  48.073  1.00 44.95           C  
ANISOU 1748  C   ASN A 228     8949   3005   5127   -551   1714    474       C  
ATOM   1749  O   ASN A 228      30.181  85.194  48.706  1.00 44.35           O  
ANISOU 1749  O   ASN A 228     8832   2982   5035   -512   1733    481       O  
ATOM   1750  CB  ASN A 228      30.434  82.002  48.961  1.00 46.32           C  
ANISOU 1750  CB  ASN A 228     9231   3082   5286   -482   1766    529       C  
ATOM   1751  CG  ASN A 228      29.025  81.469  49.117  1.00 46.87           C  
ANISOU 1751  CG  ASN A 228     9282   3125   5401   -572   1739    554       C  
ATOM   1752  OD1 ASN A 228      28.255  81.951  49.948  1.00 46.69           O  
ANISOU 1752  OD1 ASN A 228     9197   3143   5401   -602   1738    589       O  
ATOM   1753  ND2 ASN A 228      28.677  80.471  48.311  1.00 47.61           N  
ANISOU 1753  ND2 ASN A 228     9434   3151   5506   -616   1716    539       N  
ATOM   1754  N   ILE A 229      28.487  84.218  47.583  1.00 45.94           N  
ANISOU 1754  N   ILE A 229     9047   3123   5284   -638   1676    470       N  
ATOM   1755  CA  ILE A 229      27.691  85.439  47.517  1.00 45.31           C  
ANISOU 1755  CA  ILE A 229     8892   3103   5221   -684   1655    464       C  
ATOM   1756  C   ILE A 229      27.308  85.918  48.911  1.00 45.15           C  
ANISOU 1756  C   ILE A 229     8820   3126   5208   -672   1679    513       C  
ATOM   1757  O   ILE A 229      27.553  87.075  49.272  1.00 44.60           O  
ANISOU 1757  O   ILE A 229     8711   3113   5124   -645   1690    507       O  
ATOM   1758  CB  ILE A 229      26.454  85.224  46.630  1.00 45.66           C  
ANISOU 1758  CB  ILE A 229     8925   3128   5297   -779   1610    454       C  
ATOM   1759  CG1 ILE A 229      26.886  85.127  45.164  1.00 45.64           C  
ANISOU 1759  CG1 ILE A 229     8968   3098   5277   -783   1585    397       C  
ATOM   1760  CG2 ILE A 229      25.438  86.335  46.852  1.00 45.21           C  
ANISOU 1760  CG2 ILE A 229     8786   3132   5259   -825   1597    470       C  
ATOM   1761  CD1 ILE A 229      25.955  85.807  44.196  1.00 45.43           C  
ANISOU 1761  CD1 ILE A 229     8902   3094   5265   -856   1544    373       C  
ATOM   1762  N   ILE A 230      26.693  85.045  49.711  1.00 44.75           N  
ANISOU 1762  N   ILE A 230     8773   3049   5179   -692   1690    564       N  
ATOM   1763  CA  ILE A 230      26.277  85.453  51.050  1.00 44.66           C  
ANISOU 1763  CA  ILE A 230     8717   3081   5172   -677   1716    617       C  
ATOM   1764  C   ILE A 230      27.492  85.804  51.900  1.00 44.31           C  
ANISOU 1764  C   ILE A 230     8688   3060   5088   -585   1756    621       C  
ATOM   1765  O   ILE A 230      27.461  86.752  52.693  1.00 43.87           O  
ANISOU 1765  O   ILE A 230     8594   3058   5018   -560   1773    636       O  
ATOM   1766  CB  ILE A 230      25.413  84.357  51.701  1.00 45.54           C  
ANISOU 1766  CB  ILE A 230     8831   3157   5315   -716   1721    678       C  
ATOM   1767  CG1 ILE A 230      24.096  84.208  50.940  1.00 45.90           C  
ANISOU 1767  CG1 ILE A 230     8848   3190   5401   -818   1678    684       C  
ATOM   1768  CG2 ILE A 230      25.139  84.681  53.161  1.00 45.52           C  
ANISOU 1768  CG2 ILE A 230     8789   3199   5310   -683   1756    738       C  
ATOM   1769  CD1 ILE A 230      23.114  83.265  51.595  1.00 46.79           C  
ANISOU 1769  CD1 ILE A 230     8950   3276   5552   -869   1679    753       C  
ATOM   1770  N   LYS A 231      28.589  85.062  51.732  1.00 43.52           N  
ANISOU 1770  N   LYS A 231     8648   2921   4965   -530   1773    609       N  
ATOM   1771  CA  LYS A 231      29.817  85.391  52.448  1.00 43.23           C  
ANISOU 1771  CA  LYS A 231     8629   2908   4890   -444   1810    615       C  
ATOM   1772  C   LYS A 231      30.376  86.736  51.996  1.00 42.40           C  
ANISOU 1772  C   LYS A 231     8497   2851   4764   -430   1799    572       C  
ATOM   1773  O   LYS A 231      30.900  87.502  52.813  1.00 42.05           O  
ANISOU 1773  O   LYS A 231     8438   2848   4693   -387   1820    585       O  
ATOM   1774  CB  LYS A 231      30.852  84.284  52.249  1.00 43.74           C  
ANISOU 1774  CB  LYS A 231     8765   2920   4934   -387   1832    617       C  
ATOM   1775  CG  LYS A 231      32.150  84.489  53.014  1.00 43.59           C  
ANISOU 1775  CG  LYS A 231     8765   2925   4873   -294   1873    636       C  
ATOM   1776  CD  LYS A 231      33.150  83.384  52.704  1.00 44.15           C  
ANISOU 1776  CD  LYS A 231     8909   2944   4922   -233   1899    641       C  
ATOM   1777  CE  LYS A 231      34.451  83.573  53.470  1.00 44.08           C  
ANISOU 1777  CE  LYS A 231     8915   2962   4869   -138   1940    670       C  
ATOM   1778  NZ  LYS A 231      34.260  83.447  54.942  1.00 44.32           N1+
ANISOU 1778  NZ  LYS A 231     8929   3017   4892   -109   1969    729       N1+
ATOM   1779  N   SER A 232      30.266  87.043  50.701  1.00 43.81           N  
ANISOU 1779  N   SER A 232     8672   3022   4950   -468   1767    523       N  
ATOM   1780  CA  SER A 232      30.766  88.318  50.193  1.00 43.06           C  
ANISOU 1780  CA  SER A 232     8552   2970   4840   -459   1756    484       C  
ATOM   1781  C   SER A 232      29.950  89.484  50.736  1.00 42.62           C  
ANISOU 1781  C   SER A 232     8436   2966   4791   -490   1750    490       C  
ATOM   1782  O   SER A 232      30.506  90.455  51.261  1.00 42.19           O  
ANISOU 1782  O   SER A 232     8367   2949   4712   -456   1763    487       O  
ATOM   1783  CB  SER A 232      30.746  88.321  48.664  1.00 42.95           C  
ANISOU 1783  CB  SER A 232     8548   2937   4833   -491   1725    434       C  
ATOM   1784  OG  SER A 232      31.493  87.239  48.140  1.00 43.42           O  
ANISOU 1784  OG  SER A 232     8673   2946   4880   -457   1734    428       O  
ATOM   1785  N   VAL A 233      28.624  89.403  50.614  1.00 42.22           N  
ANISOU 1785  N   VAL A 233     8354   2917   4772   -553   1731    503       N  
ATOM   1786  CA  VAL A 233      27.767  90.513  51.021  1.00 41.86           C  
ANISOU 1786  CA  VAL A 233     8254   2921   4732   -579   1728    513       C  
ATOM   1787  C   VAL A 233      27.824  90.719  52.530  1.00 41.94           C  
ANISOU 1787  C   VAL A 233     8258   2955   4722   -536   1763    558       C  
ATOM   1788  O   VAL A 233      27.843  91.858  53.014  1.00 41.53           O  
ANISOU 1788  O   VAL A 233     8185   2945   4649   -519   1773    555       O  
ATOM   1789  CB  VAL A 233      26.325  90.275  50.536  1.00 42.15           C  
ANISOU 1789  CB  VAL A 233     8258   2952   4806   -656   1703    528       C  
ATOM   1790  CG1 VAL A 233      25.405  91.370  51.044  1.00 41.87           C  
ANISOU 1790  CG1 VAL A 233     8169   2969   4772   -673   1709    550       C  
ATOM   1791  CG2 VAL A 233      26.282  90.193  49.016  1.00 42.06           C  
ANISOU 1791  CG2 VAL A 233     8256   2920   4806   -696   1667    480       C  
ATOM   1792  N   SER A 234      27.865  89.628  53.298  1.00 41.35           N  
ANISOU 1792  N   SER A 234     8207   2854   4650   -516   1784    603       N  
ATOM   1793  CA  SER A 234      27.798  89.743  54.751  1.00 41.52           C  
ANISOU 1793  CA  SER A 234     8223   2901   4651   -475   1818    653       C  
ATOM   1794  C   SER A 234      29.105  90.254  55.347  1.00 41.24           C  
ANISOU 1794  C   SER A 234     8216   2882   4569   -404   1841    644       C  
ATOM   1795  O   SER A 234      29.084  91.088  56.259  1.00 41.06           O  
ANISOU 1795  O   SER A 234     8184   2899   4518   -378   1858    660       O  
ATOM   1796  CB  SER A 234      27.423  88.398  55.372  1.00 42.29           C  
ANISOU 1796  CB  SER A 234     8336   2964   4767   -474   1835    708       C  
ATOM   1797  OG  SER A 234      26.127  87.996  54.967  1.00 42.64           O  
ANISOU 1797  OG  SER A 234     8349   2996   4854   -548   1813    728       O  
ATOM   1798  N   THR A 235      30.248  89.761  54.858  1.00 39.01           N  
ANISOU 1798  N   THR A 235     7974   2572   4275   -372   1842    622       N  
ATOM   1799  CA  THR A 235      31.534  90.232  55.365  1.00 38.81           C  
ANISOU 1799  CA  THR A 235     7974   2566   4206   -309   1861    621       C  
ATOM   1800  C   THR A 235      31.666  91.742  55.203  1.00 38.18           C  
ANISOU 1800  C   THR A 235     7872   2526   4109   -322   1846    585       C  
ATOM   1801  O   THR A 235      32.245  92.420  56.060  1.00 38.08           O  
ANISOU 1801  O   THR A 235     7871   2541   4058   -286   1862    598       O  
ATOM   1802  CB  THR A 235      32.680  89.514  54.651  1.00 38.95           C  
ANISOU 1802  CB  THR A 235     8034   2550   4217   -275   1864    606       C  
ATOM   1803  OG1 THR A 235      32.535  88.098  54.819  1.00 39.62           O  
ANISOU 1803  OG1 THR A 235     8148   2590   4314   -262   1880    638       O  
ATOM   1804  CG2 THR A 235      34.025  89.947  55.217  1.00 38.86           C  
ANISOU 1804  CG2 THR A 235     8045   2560   4159   -211   1885    618       C  
ATOM   1805  N   THR A 236      31.122  92.287  54.113  1.00 40.30           N  
ANISOU 1805  N   THR A 236     8113   2797   4404   -374   1816    542       N  
ATOM   1806  CA  THR A 236      31.114  93.734  53.934  1.00 39.76           C  
ANISOU 1806  CA  THR A 236     8022   2762   4323   -389   1804    509       C  
ATOM   1807  C   THR A 236      30.214  94.410  54.963  1.00 39.77           C  
ANISOU 1807  C   THR A 236     8005   2795   4312   -392   1818    537       C  
ATOM   1808  O   THR A 236      30.554  95.477  55.488  1.00 39.54           O  
ANISOU 1808  O   THR A 236     7984   2790   4248   -375   1825    528       O  
ATOM   1809  CB  THR A 236      30.669  94.081  52.512  1.00 39.41           C  
ANISOU 1809  CB  THR A 236     7951   2715   4309   -439   1772    464       C  
ATOM   1810  OG1 THR A 236      31.689  93.694  51.583  1.00 39.36           O  
ANISOU 1810  OG1 THR A 236     7967   2685   4302   -424   1763    436       O  
ATOM   1811  CG2 THR A 236      30.405  95.573  52.373  1.00 38.92           C  
ANISOU 1811  CG2 THR A 236     7862   2687   4238   -457   1763    435       C  
ATOM   1812  N   SER A 237      29.065  93.799  55.269  1.00 39.50           N  
ANISOU 1812  N   SER A 237     7950   2758   4301   -414   1824    573       N  
ATOM   1813  CA  SER A 237      28.165  94.369  56.267  1.00 39.60           C  
ANISOU 1813  CA  SER A 237     7945   2803   4300   -409   1844    609       C  
ATOM   1814  C   SER A 237      28.832  94.443  57.634  1.00 39.82           C  
ANISOU 1814  C   SER A 237     8007   2845   4278   -347   1876    641       C  
ATOM   1815  O   SER A 237      28.622  95.401  58.385  1.00 39.74           O  
ANISOU 1815  O   SER A 237     8002   2865   4232   -327   1890    649       O  
ATOM   1816  CB  SER A 237      26.878  93.549  56.343  1.00 40.05           C  
ANISOU 1816  CB  SER A 237     7970   2854   4394   -444   1847    654       C  
ATOM   1817  OG  SER A 237      26.124  93.659  55.149  1.00 39.89           O  
ANISOU 1817  OG  SER A 237     7917   2829   4412   -505   1817    629       O  
ATOM   1818  N   GLN A 238      29.640  93.437  57.974  1.00 39.57           N  
ANISOU 1818  N   GLN A 238     8004   2792   4238   -312   1888    663       N  
ATOM   1819  CA  GLN A 238      30.360  93.463  59.243  1.00 39.82           C  
ANISOU 1819  CA  GLN A 238     8070   2842   4218   -249   1916    698       C  
ATOM   1820  C   GLN A 238      31.378  94.593  59.281  1.00 39.45           C  
ANISOU 1820  C   GLN A 238     8052   2813   4127   -233   1908    664       C  
ATOM   1821  O   GLN A 238      31.627  95.171  60.345  1.00 39.58           O  
ANISOU 1821  O   GLN A 238     8094   2857   4089   -197   1925    684       O  
ATOM   1822  CB  GLN A 238      31.043  92.116  59.482  1.00 40.28           C  
ANISOU 1822  CB  GLN A 238     8153   2874   4279   -212   1933    731       C  
ATOM   1823  CG  GLN A 238      30.115  90.925  59.323  1.00 40.72           C  
ANISOU 1823  CG  GLN A 238     8189   2901   4382   -238   1936    762       C  
ATOM   1824  CD  GLN A 238      30.750  89.622  59.763  1.00 41.28           C  
ANISOU 1824  CD  GLN A 238     8292   2945   4449   -192   1960    801       C  
ATOM   1825  OE1 GLN A 238      31.796  89.222  59.252  1.00 41.28           O  
ANISOU 1825  OE1 GLN A 238     8322   2920   4441   -168   1958    783       O  
ATOM   1826  NE2 GLN A 238      30.121  88.955  60.723  1.00 41.82           N  
ANISOU 1826  NE2 GLN A 238     8352   3017   4520   -174   1986    860       N  
ATOM   1827  N   LEU A 239      31.975  94.923  58.133  1.00 38.46           N  
ANISOU 1827  N   LEU A 239     7922   2671   4018   -261   1882    614       N  
ATOM   1828  CA  LEU A 239      32.887  96.059  58.067  1.00 38.14           C  
ANISOU 1828  CA  LEU A 239     7904   2645   3943   -259   1870    582       C  
ATOM   1829  C   LEU A 239      32.141  97.377  58.235  1.00 37.87           C  
ANISOU 1829  C   LEU A 239     7863   2631   3895   -283   1865    559       C  
ATOM   1830  O   LEU A 239      32.580  98.252  58.989  1.00 37.91           O  
ANISOU 1830  O   LEU A 239     7904   2653   3847   -267   1870    560       O  
ATOM   1831  CB  LEU A 239      33.646  96.039  56.741  1.00 37.83           C  
ANISOU 1831  CB  LEU A 239     7858   2586   3931   -280   1846    541       C  
ATOM   1832  CG  LEU A 239      34.507  97.259  56.411  1.00 37.50           C  
ANISOU 1832  CG  LEU A 239     7827   2554   3866   -294   1828    505       C  
ATOM   1833  CD1 LEU A 239      35.755  97.301  57.282  1.00 37.79           C  
ANISOU 1833  CD1 LEU A 239     7907   2605   3848   -254   1841    538       C  
ATOM   1834  CD2 LEU A 239      34.873  97.280  54.935  1.00 37.16           C  
ANISOU 1834  CD2 LEU A 239     7762   2496   3862   -320   1805    464       C  
ATOM   1835  N   LEU A 240      31.008  97.534  57.546  1.00 38.42           N  
ANISOU 1835  N   LEU A 240     7892   2700   4007   -322   1855    542       N  
ATOM   1836  CA  LEU A 240      30.250  98.779  57.645  1.00 38.21           C  
ANISOU 1836  CA  LEU A 240     7860   2692   3966   -338   1855    525       C  
ATOM   1837  C   LEU A 240      29.637  98.948  59.030  1.00 38.59           C  
ANISOU 1837  C   LEU A 240     7928   2763   3971   -301   1887    571       C  
ATOM   1838  O   LEU A 240      29.626 100.057  59.577  1.00 38.56           O  
ANISOU 1838  O   LEU A 240     7957   2773   3921   -287   1895    560       O  
ATOM   1839  CB  LEU A 240      29.167  98.823  56.568  1.00 37.97           C  
ANISOU 1839  CB  LEU A 240     7779   2662   3988   -384   1840    507       C  
ATOM   1840  CG  LEU A 240      29.668  98.848  55.123  1.00 37.59           C  
ANISOU 1840  CG  LEU A 240     7711   2598   3974   -418   1808    458       C  
ATOM   1841  CD1 LEU A 240      28.509  98.760  54.140  1.00 37.47           C  
ANISOU 1841  CD1 LEU A 240     7648   2586   4002   -462   1794    450       C  
ATOM   1842  CD2 LEU A 240      30.501 100.095  54.872  1.00 37.24           C  
ANISOU 1842  CD2 LEU A 240     7688   2558   3906   -420   1796    415       C  
ATOM   1843  N   LEU A 241      29.115  97.864  59.609  1.00 38.04           N  
ANISOU 1843  N   LEU A 241     7843   2697   3913   -281   1907    623       N  
ATOM   1844  CA  LEU A 241      28.613  97.930  60.978  1.00 38.46           C  
ANISOU 1844  CA  LEU A 241     7914   2779   3922   -235   1941    674       C  
ATOM   1845  C   LEU A 241      29.734  98.251  61.957  1.00 38.65           C  
ANISOU 1845  C   LEU A 241     7998   2813   3873   -187   1950    679       C  
ATOM   1846  O   LEU A 241      29.561  99.071  62.866  1.00 38.82           O  
ANISOU 1846  O   LEU A 241     8056   2861   3833   -155   1967    689       O  
ATOM   1847  CB  LEU A 241      27.938  96.612  61.360  1.00 38.92           C  
ANISOU 1847  CB  LEU A 241     7940   2836   4011   -226   1958    733       C  
ATOM   1848  CG  LEU A 241      26.563  96.322  60.761  1.00 38.96           C  
ANISOU 1848  CG  LEU A 241     7888   2843   4074   -271   1954    751       C  
ATOM   1849  CD1 LEU A 241      26.017  95.003  61.287  1.00 39.53           C  
ANISOU 1849  CD1 LEU A 241     7937   2912   4172   -265   1972    815       C  
ATOM   1850  CD2 LEU A 241      25.607  97.459  61.069  1.00 38.92           C  
ANISOU 1850  CD2 LEU A 241     7871   2872   4043   -265   1970    758       C  
ATOM   1851  N   GLY A 242      30.897  97.622  61.776  1.00 39.93           N  
ANISOU 1851  N   GLY A 242     8176   2960   4035   -180   1940    676       N  
ATOM   1852  CA  GLY A 242      31.998  97.838  62.695  1.00 40.18           C  
ANISOU 1852  CA  GLY A 242     8243   3026   4000   -133   1936    680       C  
ATOM   1853  C   GLY A 242      32.539  99.253  62.669  1.00 39.96           C  
ANISOU 1853  C   GLY A 242     8213   3035   3937   -143   1892    611       C  
ATOM   1854  O   GLY A 242      33.118  99.714  63.655  1.00 40.28           O  
ANISOU 1854  O   GLY A 242     8259   3129   3915   -104   1872    598       O  
ATOM   1855  N   ARG A 243      32.365  99.961  61.550  1.00 39.83           N  
ANISOU 1855  N   ARG A 243     8189   2986   3957   -197   1876    566       N  
ATOM   1856  CA  ARG A 243      32.855 101.332  61.458  1.00 39.66           C  
ANISOU 1856  CA  ARG A 243     8170   2990   3908   -213   1836    502       C  
ATOM   1857  C   ARG A 243      31.937 102.334  62.145  1.00 39.78           C  
ANISOU 1857  C   ARG A 243     8207   3025   3885   -197   1846    493       C  
ATOM   1858  O   ARG A 243      32.357 103.470  62.390  1.00 39.82           O  
ANISOU 1858  O   ARG A 243     8229   3052   3851   -200   1814    442       O  
ATOM   1859  CB  ARG A 243      33.051 101.734  59.994  1.00 39.13           C  
ANISOU 1859  CB  ARG A 243     8091   2884   3894   -271   1819    462       C  
ATOM   1860  CG  ARG A 243      34.505 101.718  59.540  1.00 39.08           C  
ANISOU 1860  CG  ARG A 243     8068   2891   3889   -280   1781    434       C  
ATOM   1861  CD  ARG A 243      34.760 100.610  58.530  1.00 38.90           C  
ANISOU 1861  CD  ARG A 243     8036   2827   3919   -293   1796    457       C  
ATOM   1862  NE  ARG A 243      34.776 101.103  57.153  1.00 38.44           N  
ANISOU 1862  NE  ARG A 243     7967   2733   3905   -342   1784    420       N  
ATOM   1863  CZ  ARG A 243      35.803 100.964  56.321  1.00 38.31           C  
ANISOU 1863  CZ  ARG A 243     7936   2714   3907   -351   1765    405       C  
ATOM   1864  NH1 ARG A 243      36.900 100.334  56.717  1.00 38.63           N1+
ANISOU 1864  NH1 ARG A 243     7967   2786   3925   -314   1756    425       N1+
ATOM   1865  NH2 ARG A 243      35.730 101.445  55.087  1.00 37.91           N  
ANISOU 1865  NH2 ARG A 243     7877   2633   3895   -392   1757    374       N  
ATOM   1866  N   MET A 244      30.701 101.946  62.462  1.00 42.58           N  
ANISOU 1866  N   MET A 244     8563   3370   4246   -181   1890    543       N  
ATOM   1867  CA  MET A 244      29.777 102.835  63.161  1.00 42.76           C  
ANISOU 1867  CA  MET A 244     8605   3415   4226   -151   1908    545       C  
ATOM   1868  C   MET A 244      30.150 103.052  64.621  1.00 43.69           C  
ANISOU 1868  C   MET A 244     8751   3586   4264    -87   1901    547       C  
ATOM   1869  O   MET A 244      29.473 103.828  65.305  1.00 44.15           O  
ANISOU 1869  O   MET A 244     8837   3666   4274    -51   1916    546       O  
ATOM   1870  CB  MET A 244      28.350 102.290  63.066  1.00 42.72           C  
ANISOU 1870  CB  MET A 244     8583   3394   4252   -151   1959    610       C  
ATOM   1871  CG  MET A 244      27.742 102.406  61.680  1.00 42.25           C  
ANISOU 1871  CG  MET A 244     8495   3298   4262   -212   1959    597       C  
ATOM   1872  SD  MET A 244      26.107 101.664  61.555  1.00 42.65           S  
ANISOU 1872  SD  MET A 244     8466   3373   4365   -214   1981    653       S  
ATOM   1873  CE  MET A 244      25.632 102.187  59.910  1.00 41.85           C  
ANISOU 1873  CE  MET A 244     8316   3257   4327   -278   1953    605       C  
ATOM   1874  N   ASP A 245      31.200 102.395  65.105  1.00 44.28           N  
ANISOU 1874  N   ASP A 245     8820   3685   4318    -67   1881    553       N  
ATOM   1875  CA  ASP A 245      31.664 102.552  66.477  1.00 44.83           C  
ANISOU 1875  CA  ASP A 245     8914   3812   4307     -7   1868    554       C  
ATOM   1876  C   ASP A 245      33.098 102.046  66.600  1.00 45.21           C  
ANISOU 1876  C   ASP A 245     8946   3888   4343     -6   1830    543       C  
ATOM   1877  O   ASP A 245      33.446 101.015  66.027  1.00 45.84           O  
ANISOU 1877  O   ASP A 245     8999   3946   4471    -19   1841    574       O  
ATOM   1878  CB  ASP A 245      30.743 101.809  67.449  1.00 45.21           C  
ANISOU 1878  CB  ASP A 245     8965   3880   4333     53   1921    629       C  
ATOM   1879  CG  ASP A 245      30.183 100.526  66.860  1.00 44.96           C  
ANISOU 1879  CG  ASP A 245     8902   3807   4374     34   1962    694       C  
ATOM   1880  OD1 ASP A 245      30.951  99.761  66.241  1.00 44.81           O  
ANISOU 1880  OD1 ASP A 245     8865   3765   4395      7   1949    694       O  
ATOM   1881  OD2 ASP A 245      28.966 100.287  67.010  1.00 45.00           O1+
ANISOU 1881  OD2 ASP A 245     8900   3803   4393     44   2008    747       O1+
ATOM   1882  N   GLY A 246      33.936 102.775  67.331  1.00 46.42           N  
ANISOU 1882  N   GLY A 246     9119   4091   4429      9   1784    500       N  
ATOM   1883  CA  GLY A 246      33.544 104.017  67.975  1.00 46.95           C  
ANISOU 1883  CA  GLY A 246     9231   4172   4434     24   1769    458       C  
ATOM   1884  C   GLY A 246      34.215 105.259  67.410  1.00 47.02           C  
ANISOU 1884  C   GLY A 246     9257   4170   4439    -34   1714    378       C  
ATOM   1885  O   GLY A 246      33.541 106.125  66.848  1.00 46.86           O  
ANISOU 1885  O   GLY A 246     9258   4109   4437    -61   1722    348       O  
ATOM   1886  N   PRO A 247      35.538 105.353  67.553  1.00 44.83           N  
ANISOU 1886  N   PRO A 247     8965   3930   4137    -54   1658    349       N  
ATOM   1887  CA  PRO A 247      36.241 106.554  67.090  1.00 44.79           C  
ANISOU 1887  CA  PRO A 247     8975   3918   4127   -115   1600    277       C  
ATOM   1888  C   PRO A 247      36.189 106.691  65.578  1.00 44.10           C  
ANISOU 1888  C   PRO A 247     8857   3775   4125   -177   1607    263       C  
ATOM   1889  O   PRO A 247      36.097 105.706  64.840  1.00 43.71           O  
ANISOU 1889  O   PRO A 247     8766   3705   4136   -181   1637    305       O  
ATOM   1890  CB  PRO A 247      37.682 106.336  67.573  1.00 45.25           C  
ANISOU 1890  CB  PRO A 247     9006   4041   4145   -121   1543    270       C  
ATOM   1891  CG  PRO A 247      37.607 105.236  68.586  1.00 45.63           C  
ANISOU 1891  CG  PRO A 247     9045   4137   4156    -46   1572    331       C  
ATOM   1892  CD  PRO A 247      36.460 104.382  68.165  1.00 45.19           C  
ANISOU 1892  CD  PRO A 247     8980   4033   4158    -21   1645    386       C  
ATOM   1893  N   ARG A 248      36.244 107.939  65.120  1.00 46.87           N  
ANISOU 1893  N   ARG A 248     9235   4097   4475   -225   1578    204       N  
ATOM   1894  CA  ARG A 248      36.353 108.213  63.696  1.00 46.06           C  
ANISOU 1894  CA  ARG A 248     9104   3950   4447   -285   1577    186       C  
ATOM   1895  C   ARG A 248      37.789 107.977  63.246  1.00 46.41           C  
ANISOU 1895  C   ARG A 248     9100   4025   4509   -324   1529    179       C  
ATOM   1896  O   ARG A 248      38.733 108.485  63.860  1.00 47.32           O  
ANISOU 1896  O   ARG A 248     9221   4184   4576   -340   1474    151       O  
ATOM   1897  CB  ARG A 248      35.928 109.647  63.388  1.00 46.00           C  
ANISOU 1897  CB  ARG A 248     9145   3901   4431   -318   1566    130       C  
ATOM   1898  CG  ARG A 248      35.321 109.823  62.007  1.00 44.85           C  
ANISOU 1898  CG  ARG A 248     8980   3700   4361   -352   1597    130       C  
ATOM   1899  CD  ARG A 248      35.362 111.273  61.551  1.00 45.28           C  
ANISOU 1899  CD  ARG A 248     9073   3718   4412   -396   1574     71       C  
ATOM   1900  NE  ARG A 248      36.691 111.654  61.083  1.00 45.85           N  
ANISOU 1900  NE  ARG A 248     9119   3801   4499   -457   1517     39       N  
ATOM   1901  CZ  ARG A 248      37.111 111.500  59.831  1.00 45.14           C  
ANISOU 1901  CZ  ARG A 248     8979   3694   4476   -499   1515     43       C  
ATOM   1902  NH1 ARG A 248      36.305 110.972  58.919  1.00 43.66           N1+
ANISOU 1902  NH1 ARG A 248     8769   3475   4346   -490   1563     72       N1+
ATOM   1903  NH2 ARG A 248      38.338 111.873  59.490  1.00 45.80           N  
ANISOU 1903  NH2 ARG A 248     9036   3796   4569   -551   1464     21       N  
ATOM   1904  N   ARG A 249      37.952 107.211  62.185  1.00 45.71           N  
ANISOU 1904  N   ARG A 249     8963   3916   4488   -339   1549    208       N  
ATOM   1905  CA  ARG A 249      39.294 106.908  61.717  1.00 46.02           C  
ANISOU 1905  CA  ARG A 249     8953   3990   4544   -364   1512    212       C  
ATOM   1906  C   ARG A 249      39.666 107.802  60.540  1.00 45.51           C  
ANISOU 1906  C   ARG A 249     8873   3895   4524   -430   1489    174       C  
ATOM   1907  O   ARG A 249      38.791 108.265  59.802  1.00 44.47           O  
ANISOU 1907  O   ARG A 249     8761   3707   4430   -449   1516    156       O  
ATOM   1908  CB  ARG A 249      39.400 105.439  61.296  1.00 45.72           C  
ANISOU 1908  CB  ARG A 249     8876   3950   4544   -330   1550    271       C  
ATOM   1909  CG  ARG A 249      39.316 104.445  62.448  1.00 46.36           C  
ANISOU 1909  CG  ARG A 249     8962   4070   4582   -265   1570    318       C  
ATOM   1910  CD  ARG A 249      40.583 104.459  63.297  1.00 47.68           C  
ANISOU 1910  CD  ARG A 249     9107   4318   4690   -251   1521    321       C  
ATOM   1911  NE  ARG A 249      40.658 103.299  64.183  1.00 48.25           N  
ANISOU 1911  NE  ARG A 249     9173   4428   4730   -183   1546    377       N  
ATOM   1912  CZ  ARG A 249      40.328 103.315  65.471  1.00 49.18           C  
ANISOU 1912  CZ  ARG A 249     9321   4582   4785   -139   1547    385       C  
ATOM   1913  NH1 ARG A 249      40.426 102.208  66.198  1.00 49.52           N1+
ANISOU 1913  NH1 ARG A 249     9354   4658   4802    -74   1574    442       N1+
ATOM   1914  NH2 ARG A 249      39.903 104.436  66.036  1.00 49.65           N  
ANISOU 1914  NH2 ARG A 249     9423   4641   4801   -156   1523    337       N  
ATOM   1915  N   PRO A 250      40.957 108.070  60.347  1.00 42.74           N  
ANISOU 1915  N   PRO A 250     8485   3585   4169   -465   1439    164       N  
ATOM   1916  CA  PRO A 250      41.371 108.925  59.230  1.00 42.49           C  
ANISOU 1916  CA  PRO A 250     8436   3528   4181   -528   1418    133       C  
ATOM   1917  C   PRO A 250      41.073 108.283  57.883  1.00 41.85           C  
ANISOU 1917  C   PRO A 250     8325   3405   4172   -525   1460    158       C  
ATOM   1918  O   PRO A 250      40.929 107.065  57.756  1.00 41.70           O  
ANISOU 1918  O   PRO A 250     8288   3386   4168   -482   1495    202       O  
ATOM   1919  CB  PRO A 250      42.882 109.086  59.443  1.00 43.03           C  
ANISOU 1919  CB  PRO A 250     8457   3666   4226   -558   1357    137       C  
ATOM   1920  CG  PRO A 250      43.103 108.768  60.883  1.00 43.64           C  
ANISOU 1920  CG  PRO A 250     8548   3801   4231   -521   1336    146       C  
ATOM   1921  CD  PRO A 250      42.086 107.728  61.228  1.00 43.36           C  
ANISOU 1921  CD  PRO A 250     8535   3744   4197   -451   1397    182       C  
ATOM   1922  N   VAL A 251      40.972 109.135  56.868  1.00 42.58           N  
ANISOU 1922  N   VAL A 251     8416   3457   4304   -572   1457    128       N  
ATOM   1923  CA  VAL A 251      40.834 108.700  55.484  1.00 41.72           C  
ANISOU 1923  CA  VAL A 251     8279   3313   4258   -577   1489    145       C  
ATOM   1924  C   VAL A 251      42.223 108.450  54.916  1.00 42.15           C  
ANISOU 1924  C   VAL A 251     8274   3412   4329   -591   1461    166       C  
ATOM   1925  O   VAL A 251      43.132 109.273  55.084  1.00 42.86           O  
ANISOU 1925  O   VAL A 251     8345   3538   4403   -632   1413    148       O  
ATOM   1926  CB  VAL A 251      40.078 109.747  54.649  1.00 41.05           C  
ANISOU 1926  CB  VAL A 251     8219   3172   4207   -614   1501    108       C  
ATOM   1927  CG1 VAL A 251      38.587 109.599  54.834  1.00 40.66           C  
ANISOU 1927  CG1 VAL A 251     8212   3081   4158   -587   1547    109       C  
ATOM   1928  CG2 VAL A 251      40.511 111.144  55.046  1.00 41.68           C  
ANISOU 1928  CG2 VAL A 251     8321   3258   4259   -662   1456     64       C  
ATOM   1929  N   LYS A 252      42.395 107.310  54.255  1.00 40.94           N  
ANISOU 1929  N   LYS A 252     8093   3256   4204   -555   1491    205       N  
ATOM   1930  CA  LYS A 252      43.644 106.999  53.577  1.00 41.36           C  
ANISOU 1930  CA  LYS A 252     8091   3351   4274   -554   1476    233       C  
ATOM   1931  C   LYS A 252      43.578 107.523  52.148  1.00 40.79           C  
ANISOU 1931  C   LYS A 252     8006   3239   4255   -587   1487    219       C  
ATOM   1932  O   LYS A 252      42.579 107.321  51.451  1.00 40.34           O  
ANISOU 1932  O   LYS A 252     7976   3121   4229   -580   1525    209       O  
ATOM   1933  CB  LYS A 252      43.913 105.493  53.589  1.00 41.42           C  
ANISOU 1933  CB  LYS A 252     8086   3373   4279   -489   1508    286       C  
ATOM   1934  CG  LYS A 252      43.960 104.882  54.984  1.00 42.13           C  
ANISOU 1934  CG  LYS A 252     8187   3503   4317   -449   1504    308       C  
ATOM   1935  CD  LYS A 252      44.695 103.547  54.986  1.00 42.64           C  
ANISOU 1935  CD  LYS A 252     8227   3601   4373   -386   1525    366       C  
ATOM   1936  CE  LYS A 252      44.714 102.915  56.373  1.00 43.21           C  
ANISOU 1936  CE  LYS A 252     8310   3715   4392   -340   1526    392       C  
ATOM   1937  NZ  LYS A 252      43.486 102.118  56.648  1.00 42.45           N1+
ANISOU 1937  NZ  LYS A 252     8267   3557   4305   -308   1574    402       N1+
ATOM   1938  N   TYR A 253      44.638 108.200  51.718  1.00 39.96           N  
ANISOU 1938  N   TYR A 253     7855   3171   4157   -623   1452    220       N  
ATOM   1939  CA  TYR A 253      44.668 108.868  50.425  1.00 39.65           C  
ANISOU 1939  CA  TYR A 253     7800   3100   4163   -656   1459    207       C  
ATOM   1940  C   TYR A 253      45.575 108.114  49.464  1.00 39.67           C  
ANISOU 1940  C   TYR A 253     7752   3133   4189   -624   1473    252       C  
ATOM   1941  O   TYR A 253      46.732 107.825  49.790  1.00 40.16           O  
ANISOU 1941  O   TYR A 253     7765   3265   4230   -611   1449    289       O  
ATOM   1942  CB  TYR A 253      45.146 110.314  50.567  1.00 39.95           C  
ANISOU 1942  CB  TYR A 253     7828   3152   4197   -726   1412    176       C  
ATOM   1943  CG  TYR A 253      44.210 111.204  51.351  1.00 39.95           C  
ANISOU 1943  CG  TYR A 253     7891   3112   4175   -754   1404    126       C  
ATOM   1944  CD1 TYR A 253      43.156 111.855  50.726  1.00 39.50           C  
ANISOU 1944  CD1 TYR A 253     7875   2988   4145   -768   1432     95       C  
ATOM   1945  CD2 TYR A 253      44.389 111.405  52.714  1.00 40.45           C  
ANISOU 1945  CD2 TYR A 253     7977   3208   4184   -761   1368    113       C  
ATOM   1946  CE1 TYR A 253      42.302 112.673  51.434  1.00 39.56           C  
ANISOU 1946  CE1 TYR A 253     7943   2960   4127   -783   1430     55       C  
ATOM   1947  CE2 TYR A 253      43.537 112.223  53.432  1.00 40.52           C  
ANISOU 1947  CE2 TYR A 253     8051   3178   4165   -778   1364     69       C  
ATOM   1948  CZ  TYR A 253      42.495 112.855  52.785  1.00 40.07           C  
ANISOU 1948  CZ  TYR A 253     8035   3053   4137   -786   1397     41       C  
ATOM   1949  OH  TYR A 253      41.638 113.674  53.482  1.00 40.19           O  
ANISOU 1949  OH  TYR A 253     8119   3031   4121   -792   1398      2       O  
ATOM   1950  N   GLU A 254      45.047 107.803  48.286  1.00 45.32           N  
ANISOU 1950  N   GLU A 254     8479   3798   4943   -607   1511    252       N  
ATOM   1951  CA  GLU A 254      45.829 107.263  47.186  1.00 45.41           C  
ANISOU 1951  CA  GLU A 254     8451   3827   4975   -575   1528    289       C  
ATOM   1952  C   GLU A 254      46.147 108.369  46.187  1.00 45.72           C  
ANISOU 1952  C   GLU A 254     8459   3863   5048   -620   1517    276       C  
ATOM   1953  O   GLU A 254      45.629 109.485  46.266  1.00 45.62           O  
ANISOU 1953  O   GLU A 254     8466   3823   5046   -674   1502    237       O  
ATOM   1954  CB  GLU A 254      45.078 106.123  46.490  1.00 44.64           C  
ANISOU 1954  CB  GLU A 254     8394   3674   4894   -524   1577    296       C  
ATOM   1955  CG  GLU A 254      44.811 104.908  47.360  1.00 45.02           C  
ANISOU 1955  CG  GLU A 254     8473   3718   4914   -475   1594    317       C  
ATOM   1956  CD  GLU A 254      44.280 103.734  46.560  1.00 45.19           C  
ANISOU 1956  CD  GLU A 254     8535   3685   4952   -429   1638    328       C  
ATOM   1957  OE1 GLU A 254      44.169 103.863  45.322  1.00 45.17           O  
ANISOU 1957  OE1 GLU A 254     8532   3651   4977   -432   1652    320       O  
ATOM   1958  OE2 GLU A 254      43.976 102.683  47.167  1.00 45.48           O1+
ANISOU 1958  OE2 GLU A 254     8604   3705   4971   -392   1657    347       O1+
ATOM   1959  N   GLU A 255      47.015 108.044  45.235  1.00 47.51           N  
ANISOU 1959  N   GLU A 255     8642   4120   5290   -592   1528    315       N  
ATOM   1960  CA  GLU A 255      47.308 108.945  44.132  1.00 47.24           C  
ANISOU 1960  CA  GLU A 255     8578   4082   5291   -624   1527    313       C  
ATOM   1961  C   GLU A 255      46.404 108.608  42.954  1.00 46.18           C  
ANISOU 1961  C   GLU A 255     8481   3883   5184   -596   1570    297       C  
ATOM   1962  O   GLU A 255      46.143 107.435  42.672  1.00 45.73           O  
ANISOU 1962  O   GLU A 255     8450   3804   5120   -539   1601    310       O  
ATOM   1963  CB  GLU A 255      48.777 108.849  43.717  1.00 48.15           C  
ANISOU 1963  CB  GLU A 255     8617   4275   5405   -607   1515    371       C  
ATOM   1964  CG  GLU A 255      49.270 110.056  42.934  1.00 48.84           C  
ANISOU 1964  CG  GLU A 255     8658   4374   5523   -660   1499    374       C  
ATOM   1965  CD  GLU A 255      50.694 109.899  42.438  1.00 50.13           C  
ANISOU 1965  CD  GLU A 255     8739   4620   5687   -638   1494    442       C  
ATOM   1966  OE1 GLU A 255      51.360 108.916  42.828  1.00 50.68           O  
ANISOU 1966  OE1 GLU A 255     8785   4744   5727   -581   1498    487       O  
ATOM   1967  OE2 GLU A 255      51.145 110.761  41.652  1.00 50.36           O1+
ANISOU 1967  OE2 GLU A 255     8726   4662   5746   -673   1488    456       O1+
ATOM   1968  N   ASP A 256      45.920 109.643  42.276  1.00 45.48           N  
ANISOU 1968  N   ASP A 256     8397   3759   5124   -639   1572    268       N  
ATOM   1969  CA  ASP A 256      44.991 109.438  41.175  1.00 44.96           C  
ANISOU 1969  CA  ASP A 256     8365   3637   5082   -619   1609    250       C  
ATOM   1970  C   ASP A 256      45.712 108.853  39.966  1.00 45.08           C  
ANISOU 1970  C   ASP A 256     8352   3671   5107   -568   1632    287       C  
ATOM   1971  O   ASP A 256      46.899 109.105  39.738  1.00 45.42           O  
ANISOU 1971  O   ASP A 256     8337   3770   5151   -564   1620    326       O  
ATOM   1972  CB  ASP A 256      44.315 110.755  40.795  1.00 44.36           C  
ANISOU 1972  CB  ASP A 256     8300   3526   5030   -671   1607    214       C  
ATOM   1973  CG  ASP A 256      43.083 110.550  39.942  1.00 44.07           C  
ANISOU 1973  CG  ASP A 256     8286   3451   5008   -649   1632    185       C  
ATOM   1974  OD1 ASP A 256      42.773 109.386  39.608  1.00 43.92           O  
ANISOU 1974  OD1 ASP A 256     8276   3430   4981   -601   1646    189       O  
ATOM   1975  OD2 ASP A 256      42.427 111.556  39.599  1.00 44.00           O1+
ANISOU 1975  OD2 ASP A 256     8257   3448   5012   -671   1621    151       O1+
ATOM   1976  N   VAL A 257      44.980 108.053  39.188  1.00 43.60           N  
ANISOU 1976  N   VAL A 257     8206   3437   4923   -528   1665    277       N  
ATOM   1977  CA  VAL A 257      45.542 107.483  37.971  1.00 43.76           C  
ANISOU 1977  CA  VAL A 257     8215   3466   4947   -472   1690    307       C  
ATOM   1978  C   VAL A 257      45.774 108.596  36.958  1.00 43.50           C  
ANISOU 1978  C   VAL A 257     8145   3443   4942   -496   1692    308       C  
ATOM   1979  O   VAL A 257      45.021 109.577  36.896  1.00 42.95           O  
ANISOU 1979  O   VAL A 257     8084   3344   4892   -547   1686    273       O  
ATOM   1980  CB  VAL A 257      44.621 106.385  37.408  1.00 43.74           C  
ANISOU 1980  CB  VAL A 257     8278   3402   4937   -433   1719    289       C  
ATOM   1981  CG1 VAL A 257      43.375 106.984  36.763  1.00 43.34           C  
ANISOU 1981  CG1 VAL A 257     8222   3338   4906   -460   1708    234       C  
ATOM   1982  CG2 VAL A 257      45.376 105.501  36.418  1.00 43.99           C  
ANISOU 1982  CG2 VAL A 257     8312   3444   4956   -358   1745    323       C  
ATOM   1983  N   ASN A 258      46.842 108.468  36.178  1.00 42.97           N  
ANISOU 1983  N   ASN A 258     8033   3418   4874   -455   1703    353       N  
ATOM   1984  CA  ASN A 258      47.168 109.428  35.129  1.00 42.89           C  
ANISOU 1984  CA  ASN A 258     7982   3423   4891   -468   1710    365       C  
ATOM   1985  C   ASN A 258      47.070 108.696  33.797  1.00 42.76           C  
ANISOU 1985  C   ASN A 258     7990   3388   4868   -397   1747    375       C  
ATOM   1986  O   ASN A 258      47.942 107.889  33.457  1.00 43.59           O  
ANISOU 1986  O   ASN A 258     8082   3528   4954   -330   1764    419       O  
ATOM   1987  CB  ASN A 258      48.552 110.034  35.339  1.00 43.82           C  
ANISOU 1987  CB  ASN A 258     8020   3617   5015   -485   1689    417       C  
ATOM   1988  CG  ASN A 258      48.714 111.371  34.639  1.00 44.04           C  
ANISOU 1988  CG  ASN A 258     8008   3650   5077   -532   1686    421       C  
ATOM   1989  OD1 ASN A 258      49.111 111.432  33.474  1.00 44.25           O  
ANISOU 1989  OD1 ASN A 258     8007   3692   5113   -494   1712    452       O  
ATOM   1990  ND2 ASN A 258      48.403 112.453  35.348  1.00 43.85           N  
ANISOU 1990  ND2 ASN A 258     7984   3609   5067   -613   1657    391       N  
ATOM   1991  N   LEU A 259      46.004 108.978  33.051  1.00 40.30           N  
ANISOU 1991  N   LEU A 259     7718   3025   4571   -409   1761    335       N  
ATOM   1992  CA  LEU A 259      45.702 108.251  31.827  1.00 40.25           C  
ANISOU 1992  CA  LEU A 259     7748   2992   4552   -348   1791    332       C  
ATOM   1993  C   LEU A 259      46.606 108.632  30.662  1.00 40.50           C  
ANISOU 1993  C   LEU A 259     7734   3066   4590   -306   1811    374       C  
ATOM   1994  O   LEU A 259      46.547 107.975  29.617  1.00 40.57           O  
ANISOU 1994  O   LEU A 259     7774   3060   4581   -243   1837    378       O  
ATOM   1995  CB  LEU A 259      44.238 108.479  31.446  1.00 39.78           C  
ANISOU 1995  CB  LEU A 259     7717   2896   4501   -374   1783    271       C  
ATOM   1996  CG  LEU A 259      43.255 108.199  32.584  1.00 39.55           C  
ANISOU 1996  CG  LEU A 259     7695   2866   4465   -409   1749    225       C  
ATOM   1997  CD1 LEU A 259      41.844 108.618  32.209  1.00 39.15           C  
ANISOU 1997  CD1 LEU A 259     7630   2826   4420   -431   1729    171       C  
ATOM   1998  CD2 LEU A 259      43.297 106.731  32.967  1.00 39.74           C  
ANISOU 1998  CD2 LEU A 259     7768   2870   4462   -368   1755    230       C  
ATOM   1999  N   GLY A 260      47.437 109.658  30.811  1.00 40.60           N  
ANISOU 1999  N   GLY A 260     7673   3128   4624   -340   1799    408       N  
ATOM   2000  CA  GLY A 260      48.310 110.078  29.736  1.00 40.99           C  
ANISOU 2000  CA  GLY A 260     7669   3222   4682   -303   1820    458       C  
ATOM   2001  C   GLY A 260      47.573 110.870  28.672  1.00 41.02           C  
ANISOU 2001  C   GLY A 260     7683   3195   4707   -315   1837    433       C  
ATOM   2002  O   GLY A 260      46.437 111.312  28.850  1.00 40.82           O  
ANISOU 2002  O   GLY A 260     7694   3121   4693   -364   1829    381       O  
ATOM   2003  N   SER A 261      48.242 111.043  27.534  1.00 40.32           N  
ANISOU 2003  N   SER A 261     7558   3142   4619   -264   1863    477       N  
ATOM   2004  CA  SER A 261      47.680 111.815  26.436  1.00 40.09           C  
ANISOU 2004  CA  SER A 261     7530   3094   4607   -266   1883    464       C  
ATOM   2005  C   SER A 261      48.155 111.234  25.112  1.00 40.50           C  
ANISOU 2005  C   SER A 261     7583   3169   4634   -169   1920    499       C  
ATOM   2006  O   SER A 261      49.072 110.410  25.061  1.00 41.59           O  
ANISOU 2006  O   SER A 261     7710   3345   4746   -104   1931    542       O  
ATOM   2007  CB  SER A 261      48.051 113.298  26.553  1.00 40.18           C  
ANISOU 2007  CB  SER A 261     7478   3128   4661   -334   1874    487       C  
ATOM   2008  OG  SER A 261      49.434 113.459  26.817  1.00 41.03           O  
ANISOU 2008  OG  SER A 261     7511   3303   4777   -334   1866    553       O  
ATOM   2009  N   GLY A 262      47.513 111.675  24.036  1.00 39.95           N  
ANISOU 2009  N   GLY A 262     7530   3080   4569   -156   1940    481       N  
ATOM   2010  CA  GLY A 262      47.824 111.244  22.688  1.00 40.77           C  
ANISOU 2010  CA  GLY A 262     7642   3202   4645    -64   1975    507       C  
ATOM   2011  C   GLY A 262      46.767 110.301  22.141  1.00 40.36           C  
ANISOU 2011  C   GLY A 262     7683   3095   4555    -26   1979    450       C  
ATOM   2012  O   GLY A 262      45.696 110.106  22.722  1.00 40.13           O  
ANISOU 2012  O   GLY A 262     7703   3016   4528    -78   1956    392       O  
ATOM   2013  N   THR A 263      47.085 109.722  20.988  1.00 36.60           N  
ANISOU 2013  N   THR A 263     7231   2632   4044     66   2008    468       N  
ATOM   2014  CA  THR A 263      46.301 108.655  20.384  1.00 36.60           C  
ANISOU 2014  CA  THR A 263     7326   2582   3998    112   2011    419       C  
ATOM   2015  C   THR A 263      47.069 107.345  20.499  1.00 37.07           C  
ANISOU 2015  C   THR A 263     7428   2643   4014    191   2022    441       C  
ATOM   2016  O   THR A 263      48.263 107.324  20.806  1.00 37.44           O  
ANISOU 2016  O   THR A 263     7420   2742   4062    227   2036    504       O  
ATOM   2017  CB  THR A 263      45.981 108.962  18.915  1.00 36.68           C  
ANISOU 2017  CB  THR A 263     7348   2599   3989    162   2034    416       C  
ATOM   2018  OG1 THR A 263      47.198 109.164  18.185  1.00 37.15           O  
ANISOU 2018  OG1 THR A 263     7356   2720   4040    241   2069    487       O  
ATOM   2019  CG2 THR A 263      45.114 110.206  18.806  1.00 36.23           C  
ANISOU 2019  CG2 THR A 263     7257   2537   3971     88   2026    393       C  
ATOM   2020  N   ARG A 264      46.369 106.242  20.257  1.00 36.39           N  
ANISOU 2020  N   ARG A 264     7441   2497   3887    218   2017    391       N  
ATOM   2021  CA  ARG A 264      46.967 104.918  20.331  1.00 36.99           C  
ANISOU 2021  CA  ARG A 264     7579   2558   3916    298   2031    405       C  
ATOM   2022  C   ARG A 264      46.933 104.254  18.963  1.00 37.52           C  
ANISOU 2022  C   ARG A 264     7722   2607   3928    393   2056    395       C  
ATOM   2023  O   ARG A 264      45.976 104.423  18.199  1.00 37.25           O  
ANISOU 2023  O   ARG A 264     7727   2541   3885    373   2045    346       O  
ATOM   2024  CB  ARG A 264      46.258 104.038  21.367  1.00 36.58           C  
ANISOU 2024  CB  ARG A 264     7595   2442   3861    248   2003    357       C  
ATOM   2025  CG  ARG A 264      44.789 103.765  21.094  1.00 36.09           C  
ANISOU 2025  CG  ARG A 264     7608   2310   3792    194   1977    282       C  
ATOM   2026  CD  ARG A 264      44.261 102.732  22.076  1.00 36.09           C  
ANISOU 2026  CD  ARG A 264     7678   2250   3785    160   1956    248       C  
ATOM   2027  NE  ARG A 264      44.929 101.445  21.904  1.00 36.71           N  
ANISOU 2027  NE  ARG A 264     7832   2301   3814    250   1978    264       N  
ATOM   2028  CZ  ARG A 264      45.060 100.532  22.861  1.00 36.88           C  
ANISOU 2028  CZ  ARG A 264     7897   2290   3828    252   1975    266       C  
ATOM   2029  NH1 ARG A 264      44.574 100.765  24.072  1.00 36.48           N1+
ANISOU 2029  NH1 ARG A 264     7799   2249   3812    166   1942    250       N1+
ATOM   2030  NH2 ARG A 264      45.684  99.388  22.610  1.00 37.51           N  
ANISOU 2030  NH2 ARG A 264     8052   2342   3858    345   2001    283       N  
ATOM   2031  N   ALA A 265      47.997 103.511  18.659  1.00 37.00           N  
ANISOU 2031  N   ALA A 265     7675   2563   3820    501   2089    444       N  
ATOM   2032  CA  ALA A 265      48.087 102.797  17.395  1.00 37.53           C  
ANISOU 2032  CA  ALA A 265     7825   2611   3824    607   2117    437       C  
ATOM   2033  C   ALA A 265      46.922 101.828  17.247  1.00 37.54           C  
ANISOU 2033  C   ALA A 265     7955   2516   3791    583   2090    353       C  
ATOM   2034  O   ALA A 265      46.355 101.344  18.230  1.00 37.31           O  
ANISOU 2034  O   ALA A 265     7962   2437   3778    515   2062    317       O  
ATOM   2035  CB  ALA A 265      49.411 102.043  17.301  1.00 38.25           C  
ANISOU 2035  CB  ALA A 265     7924   2738   3872    730   2160    506       C  
ATOM   2036  N   VAL A 266      46.573 101.536  15.995  1.00 37.86           N  
ANISOU 2036  N   VAL A 266     8068   2533   3783    640   2099    323       N  
ATOM   2037  CA  VAL A 266      45.374 100.778  15.675  1.00 37.92           C  
ANISOU 2037  CA  VAL A 266     8192   2455   3759    603   2066    240       C  
ATOM   2038  C   VAL A 266      45.681  99.832  14.521  1.00 38.72           C  
ANISOU 2038  C   VAL A 266     8407   2525   3779    722   2091    230       C  
ATOM   2039  O   VAL A 266      46.611 100.047  13.741  1.00 39.10           O  
ANISOU 2039  O   VAL A 266     8430   2629   3799    828   2133    284       O  
ATOM   2040  CB  VAL A 266      44.197 101.722  15.327  1.00 37.36           C  
ANISOU 2040  CB  VAL A 266     8085   2390   3721    509   2033    196       C  
ATOM   2041  CG1 VAL A 266      44.483 102.485  14.041  1.00 37.50           C  
ANISOU 2041  CG1 VAL A 266     8063   2464   3720    573   2060    221       C  
ATOM   2042  CG2 VAL A 266      42.885 100.963  15.245  1.00 37.41           C  
ANISOU 2042  CG2 VAL A 266     8194   2315   3705    445   1990    116       C  
ATOM   2043  N   ALA A 267      44.898  98.758  14.439  1.00 39.03           N  
ANISOU 2043  N   ALA A 267     8577   2473   3779    704   2064    164       N  
ATOM   2044  CA  ALA A 267      45.040  97.799  13.353  1.00 39.87           C  
ANISOU 2044  CA  ALA A 267     8811   2536   3800    807   2078    140       C  
ATOM   2045  C   ALA A 267      44.816  98.482  12.012  1.00 39.93           C  
ANISOU 2045  C   ALA A 267     8809   2581   3783    843   2084    130       C  
ATOM   2046  O   ALA A 267      43.805  99.161  11.807  1.00 39.46           O  
ANISOU 2046  O   ALA A 267     8714   2529   3752    751   2047     90       O  
ATOM   2047  CB  ALA A 267      44.052  96.646  13.534  1.00 40.18           C  
ANISOU 2047  CB  ALA A 267     8924   2535   3806    731   2011     74       C  
ATOM   2048  N   SER A 268      45.765  98.302  11.098  1.00 41.75           N  
ANISOU 2048  N   SER A 268     9064   2843   3955    982   2131    172       N  
ATOM   2049  CA  SER A 268      45.730  98.946   9.793  1.00 42.14           C  
ANISOU 2049  CA  SER A 268     9095   2941   3974   1037   2145    176       C  
ATOM   2050  C   SER A 268      45.200  97.975   8.747  1.00 42.46           C  
ANISOU 2050  C   SER A 268     9294   2913   3924   1088   2127    108       C  
ATOM   2051  O   SER A 268      45.710  96.857   8.613  1.00 43.07           O  
ANISOU 2051  O   SER A 268     9454   2970   3940   1163   2132    117       O  
ATOM   2052  CB  SER A 268      47.121  99.443   9.395  1.00 42.90           C  
ANISOU 2052  CB  SER A 268     9108   3128   4062   1161   2209    273       C  
ATOM   2053  OG  SER A 268      47.072 100.179   8.184  1.00 43.23           O  
ANISOU 2053  OG  SER A 268     9119   3224   4082   1209   2225    284       O  
ATOM   2054  N   CYS A 269      44.170  98.403   8.016  1.00 45.78           N  
ANISOU 2054  N   CYS A 269     9719   3339   4338   1027   2086     56       N  
ATOM   2055  CA  CYS A 269      43.667  97.672   6.859  1.00 46.39           C  
ANISOU 2055  CA  CYS A 269     9896   3400   4331   1057   2046      8       C  
ATOM   2056  C   CYS A 269      43.678  98.542   5.607  1.00 46.51           C  
ANISOU 2056  C   CYS A 269     9888   3468   4317   1126   2074     15       C  
ATOM   2057  O   CYS A 269      42.927  98.275   4.662  1.00 46.91           O  
ANISOU 2057  O   CYS A 269    10001   3511   4314   1116   2029    -36       O  
ATOM   2058  CB  CYS A 269      42.258  97.139   7.125  1.00 46.36           C  
ANISOU 2058  CB  CYS A 269     9935   3348   4332    912   1958    -69       C  
ATOM   2059  SG  CYS A 269      40.994  98.423   7.268  1.00 45.58           S  
ANISOU 2059  SG  CYS A 269     9744   3272   4303    777   1928   -105       S  
ATOM   2060  N   ALA A 270      44.518  99.575   5.586  1.00 44.42           N  
ANISOU 2060  N   ALA A 270     9513   3274   4089   1187   2138     88       N  
ATOM   2061  CA  ALA A 270      44.540 100.532   4.492  1.00 44.41           C  
ANISOU 2061  CA  ALA A 270     9448   3351   4075   1237   2158    114       C  
ATOM   2062  C   ALA A 270      45.183  99.934   3.247  1.00 45.40           C  
ANISOU 2062  C   ALA A 270     9674   3480   4098   1401   2197    123       C  
ATOM   2063  O   ALA A 270      46.096  99.108   3.326  1.00 46.01           O  
ANISOU 2063  O   ALA A 270     9806   3541   4134   1499   2228    159       O  
ATOM   2064  CB  ALA A 270      45.290 101.796   4.907  1.00 43.80           C  
ANISOU 2064  CB  ALA A 270     9196   3368   4078   1232   2199    207       C  
ATOM   2065  N   GLU A 271      44.704 100.381   2.089  1.00 48.50           N  
ANISOU 2065  N   GLU A 271    10075   3906   4448   1429   2191    102       N  
ATOM   2066  CA  GLU A 271      45.143  99.836   0.814  1.00 49.44           C  
ANISOU 2066  CA  GLU A 271    10268   4046   4472   1563   2198    116       C  
ATOM   2067  C   GLU A 271      46.615 100.158   0.564  1.00 49.69           C  
ANISOU 2067  C   GLU A 271    10240   4147   4494   1716   2288    221       C  
ATOM   2068  O   GLU A 271      47.182 101.097   1.131  1.00 49.13           O  
ANISOU 2068  O   GLU A 271    10035   4135   4495   1703   2334    290       O  
ATOM   2069  CB  GLU A 271      44.275 100.389  -0.315  1.00 49.99           C  
ANISOU 2069  CB  GLU A 271    10339   4148   4508   1551   2169     76       C  
ATOM   2070  CG  GLU A 271      44.072  99.439  -1.479  1.00 51.44           C  
ANISOU 2070  CG  GLU A 271    10643   4311   4590   1618   2123     39       C  
ATOM   2071  CD  GLU A 271      42.664  99.508  -2.035  1.00 51.68           C  
ANISOU 2071  CD  GLU A 271    10715   4325   4597   1522   2049    -49       C  
ATOM   2072  OE1 GLU A 271      41.707  99.396  -1.239  1.00 51.37           O  
ANISOU 2072  OE1 GLU A 271    10682   4236   4600   1377   1998   -108       O  
ATOM   2073  OE2 GLU A 271      42.513  99.683  -3.264  1.00 52.04           O1+
ANISOU 2073  OE2 GLU A 271    10782   4410   4578   1591   2043    -55       O1+
ATOM   2074  N   ALA A 272      47.234  99.361  -0.299  1.00 47.60           N  
ANISOU 2074  N   ALA A 272    10051   3888   4146   1845   2295    248       N  
ATOM   2075  CA  ALA A 272      48.654  99.531  -0.583  1.00 48.04           C  
ANISOU 2075  CA  ALA A 272    10054   4014   4185   2001   2378    356       C  
ATOM   2076  C   ALA A 272      48.877 100.793  -1.409  1.00 47.86           C  
ANISOU 2076  C   ALA A 272     9921   4088   4174   2054   2426    412       C  
ATOM   2077  O   ALA A 272      48.249 100.957  -2.462  1.00 48.21           O  
ANISOU 2077  O   ALA A 272     9996   4146   4177   2065   2393    377       O  
ATOM   2078  CB  ALA A 272      49.204  98.312  -1.322  1.00 49.26           C  
ANISOU 2078  CB  ALA A 272    10326   4145   4243   2128   2369    371       C  
ATOM   2079  N   PRO A 273      49.748 101.702  -0.972  1.00 46.01           N  
ANISOU 2079  N   PRO A 273     9558   3929   3995   2085   2504    502       N  
ATOM   2080  CA  PRO A 273      49.991 102.925  -1.744  1.00 45.89           C  
ANISOU 2080  CA  PRO A 273     9420   4015   4003   2121   2542    572       C  
ATOM   2081  C   PRO A 273      50.607 102.627  -3.103  1.00 46.93           C  
ANISOU 2081  C   PRO A 273     9587   4191   4052   2289   2566    622       C  
ATOM   2082  O   PRO A 273      51.257 101.601  -3.316  1.00 47.77           O  
ANISOU 2082  O   PRO A 273     9773   4276   4100   2393   2567    644       O  
ATOM   2083  CB  PRO A 273      50.962 103.717  -0.860  1.00 45.47           C  
ANISOU 2083  CB  PRO A 273     9196   4033   4047   2090   2579    682       C  
ATOM   2084  CG  PRO A 273      50.767 103.158   0.516  1.00 45.28           C  
ANISOU 2084  CG  PRO A 273     9191   3940   4071   1980   2537    641       C  
ATOM   2085  CD  PRO A 273      50.455 101.709   0.319  1.00 45.63           C  
ANISOU 2085  CD  PRO A 273     9426   3889   4021   2038   2517    560       C  
ATOM   2086  N   ASN A 274      50.387 103.550  -4.033  1.00 46.35           N  
ANISOU 2086  N   ASN A 274     9447   4183   3980   2311   2577    646       N  
ATOM   2087  CA  ASN A 274      51.001 103.507  -5.355  1.00 47.28           C  
ANISOU 2087  CA  ASN A 274     9566   4361   4039   2466   2598    710       C  
ATOM   2088  C   ASN A 274      52.121 104.542  -5.409  1.00 47.26           C  
ANISOU 2088  C   ASN A 274     9399   4467   4089   2533   2681    846       C  
ATOM   2089  O   ASN A 274      51.984 105.616  -5.997  1.00 47.05           O  
ANISOU 2089  O   ASN A 274     9278   4507   4094   2530   2700    884       O  
ATOM   2090  CB  ASN A 274      49.950 103.757  -6.445  1.00 47.40           C  
ANISOU 2090  CB  ASN A 274     9623   4375   4011   2449   2547    643       C  
ATOM   2091  CG  ASN A 274      49.092 102.541  -6.716  1.00 47.88           C  
ANISOU 2091  CG  ASN A 274     9852   4343   3996   2421   2464    530       C  
ATOM   2092  OD1 ASN A 274      48.032 102.367  -6.116  1.00 47.32           O  
ANISOU 2092  OD1 ASN A 274     9827   4206   3944   2282   2408    434       O  
ATOM   2093  ND2 ASN A 274      49.549 101.686  -7.624  1.00 48.99           N  
ANISOU 2093  ND2 ASN A 274    10084   4479   4050   2550   2455    544       N  
ATOM   2094  N   MET A 275      53.251 104.200  -4.783  1.00 47.28           N  
ANISOU 2094  N   MET A 275     9365   4493   4106   2593   2727    926       N  
ATOM   2095  CA  MET A 275      54.359 105.139  -4.647  1.00 47.28           C  
ANISOU 2095  CA  MET A 275     9196   4601   4169   2634   2798   1062       C  
ATOM   2096  C   MET A 275      54.967 105.546  -5.984  1.00 48.08           C  
ANISOU 2096  C   MET A 275     9240   4784   4245   2775   2827   1147       C  
ATOM   2097  O   MET A 275      55.776 106.479  -6.016  1.00 48.11           O  
ANISOU 2097  O   MET A 275     9088   4881   4310   2796   2877   1260       O  
ATOM   2098  CB  MET A 275      55.440 104.542  -3.742  1.00 47.56           C  
ANISOU 2098  CB  MET A 275     9209   4649   4214   2675   2833   1130       C  
ATOM   2099  CG  MET A 275      54.967 104.246  -2.324  1.00 46.77           C  
ANISOU 2099  CG  MET A 275     9145   4480   4147   2535   2811   1065       C  
ATOM   2100  SD  MET A 275      54.444 105.714  -1.414  1.00 45.59           S  
ANISOU 2100  SD  MET A 275     8827   4352   4142   2319   2770   1069       S  
ATOM   2101  CE  MET A 275      56.003 106.573  -1.217  1.00 45.88           C  
ANISOU 2101  CE  MET A 275     8669   4520   4242   2369   2839   1248       C  
ATOM   2102  N   LYS A 276      54.615 104.870  -7.079  1.00 48.73           N  
ANISOU 2102  N   LYS A 276     9440   4835   4240   2867   2793   1100       N  
ATOM   2103  CA  LYS A 276      54.986 105.373  -8.397  1.00 49.40           C  
ANISOU 2103  CA  LYS A 276     9474   4996   4301   2986   2816   1170       C  
ATOM   2104  C   LYS A 276      54.167 106.602  -8.769  1.00 48.73           C  
ANISOU 2104  C   LYS A 276     9310   4943   4263   2897   2808   1150       C  
ATOM   2105  O   LYS A 276      54.618 107.427  -9.572  1.00 49.05           O  
ANISOU 2105  O   LYS A 276     9247   5066   4324   2967   2843   1236       O  
ATOM   2106  CB  LYS A 276      54.809 104.279  -9.449  1.00 50.41           C  
ANISOU 2106  CB  LYS A 276     9759   5081   4314   3103   2777   1124       C  
ATOM   2107  CG  LYS A 276      56.083 103.523  -9.781  1.00 51.55           C  
ANISOU 2107  CG  LYS A 276     9922   5255   4408   3276   2816   1219       C  
ATOM   2108  CD  LYS A 276      55.871 102.020  -9.720  1.00 52.16           C  
ANISOU 2108  CD  LYS A 276    10189   5236   4394   3309   2771   1144       C  
ATOM   2109  CE  LYS A 276      57.091 101.272 -10.230  1.00 53.43           C  
ANISOU 2109  CE  LYS A 276    10381   5429   4492   3498   2811   1244       C  
ATOM   2110  NZ  LYS A 276      56.970  99.804 -10.015  1.00 54.05           N1+
ANISOU 2110  NZ  LYS A 276    10641   5409   4487   3523   2774   1181       N1+
ATOM   2111  N   ILE A 277      52.974 106.742  -8.195  1.00 47.85           N  
ANISOU 2111  N   ILE A 277     9243   4767   4171   2747   2762   1043       N  
ATOM   2112  CA  ILE A 277      52.084 107.860  -8.487  1.00 47.21           C  
ANISOU 2112  CA  ILE A 277     9098   4709   4131   2658   2752   1017       C  
ATOM   2113  C   ILE A 277      52.256 108.943  -7.431  1.00 46.32           C  
ANISOU 2113  C   ILE A 277     8846   4626   4126   2537   2790   1069       C  
ATOM   2114  O   ILE A 277      52.640 110.076  -7.742  1.00 46.26           O  
ANISOU 2114  O   ILE A 277     8705   4693   4178   2542   2830   1158       O  
ATOM   2115  CB  ILE A 277      50.618 107.392  -8.560  1.00 46.88           C  
ANISOU 2115  CB  ILE A 277     9183   4587   4043   2566   2676    873       C  
ATOM   2116  CG1 ILE A 277      50.409 106.465  -9.761  1.00 47.88           C  
ANISOU 2116  CG1 ILE A 277     9436   4694   4060   2675   2632    829       C  
ATOM   2117  CG2 ILE A 277      49.676 108.585  -8.625  1.00 46.12           C  
ANISOU 2117  CG2 ILE A 277     9011   4515   3998   2460   2670    851       C  
ATOM   2118  CD1 ILE A 277      49.008 105.899  -9.856  1.00 47.72           C  
ANISOU 2118  CD1 ILE A 277     9542   4599   3991   2581   2550    690       C  
ATOM   2119  N   ILE A 278      51.976 108.598  -6.170  1.00 45.68           N  
ANISOU 2119  N   ILE A 278     8799   4483   4073   2424   2774   1016       N  
ATOM   2120  CA  ILE A 278      51.990 109.582  -5.089  1.00 44.82           C  
ANISOU 2120  CA  ILE A 278     8571   4388   4069   2283   2788   1053       C  
ATOM   2121  C   ILE A 278      53.368 109.805  -4.493  1.00 45.04           C  
ANISOU 2121  C   ILE A 278     8485   4477   4152   2310   2837   1178       C  
ATOM   2122  O   ILE A 278      53.511 110.650  -3.600  1.00 44.45           O  
ANISOU 2122  O   ILE A 278     8291   4414   4184   2185   2825   1216       O  
ATOM   2123  CB  ILE A 278      51.040 109.156  -3.952  1.00 44.03           C  
ANISOU 2123  CB  ILE A 278     8528   4193   4009   2124   2709    941       C  
ATOM   2124  CG1 ILE A 278      51.480 107.805  -3.383  1.00 44.39           C  
ANISOU 2124  CG1 ILE A 278     8674   4185   4006   2167   2699    912       C  
ATOM   2125  CG2 ILE A 278      49.604 109.102  -4.454  1.00 43.76           C  
ANISOU 2125  CG2 ILE A 278     8582   4110   3936   2071   2655    826       C  
ATOM   2126  CD1 ILE A 278      50.888 107.479  -2.025  1.00 43.64           C  
ANISOU 2126  CD1 ILE A 278     8598   4011   3971   2011   2634    838       C  
ATOM   2127  N   GLY A 279      54.388 109.084  -4.963  1.00 45.95           N  
ANISOU 2127  N   GLY A 279     8617   4629   4213   2462   2870   1240       N  
ATOM   2128  CA  GLY A 279      55.679 109.119  -4.294  1.00 46.24           C  
ANISOU 2128  CA  GLY A 279     8549   4722   4296   2485   2907   1352       C  
ATOM   2129  C   GLY A 279      56.343 110.483  -4.329  1.00 46.19           C  
ANISOU 2129  C   GLY A 279     8356   4807   4387   2448   2940   1471       C  
ATOM   2130  O   GLY A 279      56.935 110.920  -3.339  1.00 45.94           O  
ANISOU 2130  O   GLY A 279     8221   4802   4431   2361   2946   1536       O  
ATOM   2131  N   ARG A 280      56.260 111.173  -5.469  1.00 46.49           N  
ANISOU 2131  N   ARG A 280     8348   4892   4425   2510   2955   1502       N  
ATOM   2132  CA  ARG A 280      56.934 112.462  -5.595  1.00 46.58           C  
ANISOU 2132  CA  ARG A 280     8182   4988   4529   2482   2986   1618       C  
ATOM   2133  C   ARG A 280      56.324 113.503  -4.665  1.00 45.61           C  
ANISOU 2133  C   ARG A 280     7997   4834   4499   2290   2966   1600       C  
ATOM   2134  O   ARG A 280      57.039 114.343  -4.105  1.00 45.59           O  
ANISOU 2134  O   ARG A 280     7855   4879   4588   2217   2978   1690       O  
ATOM   2135  CB  ARG A 280      56.887 112.942  -7.045  1.00 47.13           C  
ANISOU 2135  CB  ARG A 280     8227   5106   4573   2592   3006   1649       C  
ATOM   2136  CG  ARG A 280      58.225 112.847  -7.756  1.00 48.22           C  
ANISOU 2136  CG  ARG A 280     8280   5339   4704   2747   3048   1773       C  
ATOM   2137  CD  ARG A 280      59.285 113.663  -7.029  1.00 48.31           C  
ANISOU 2137  CD  ARG A 280     8113   5423   4819   2678   3072   1894       C  
ATOM   2138  NE  ARG A 280      59.314 115.058  -7.460  1.00 48.26           N  
ANISOU 2138  NE  ARG A 280     7978   5465   4894   2626   3088   1959       N  
ATOM   2139  CZ  ARG A 280      59.918 116.032  -6.787  1.00 48.16           C  
ANISOU 2139  CZ  ARG A 280     7818   5496   4986   2516   3094   2044       C  
ATOM   2140  NH1 ARG A 280      59.901 117.275  -7.252  1.00 48.20           N1+
ANISOU 2140  NH1 ARG A 280     7719   5535   5060   2474   3108   2098       N1+
ATOM   2141  NH2 ARG A 280      60.530 115.766  -5.642  1.00 48.08           N  
ANISOU 2141  NH2 ARG A 280     7766   5492   5011   2443   3084   2074       N  
ATOM   2142  N   ARG A 281      55.004 113.461  -4.481  1.00 44.87           N  
ANISOU 2142  N   ARG A 281     8003   4660   4384   2203   2932   1484       N  
ATOM   2143  CA  ARG A 281      54.354 114.426  -3.601  1.00 43.98           C  
ANISOU 2143  CA  ARG A 281     7834   4509   4367   2023   2899   1456       C  
ATOM   2144  C   ARG A 281      54.700 114.164  -2.140  1.00 43.59           C  
ANISOU 2144  C   ARG A 281     7755   4426   4381   1910   2859   1447       C  
ATOM   2145  O   ARG A 281      54.865 115.108  -1.358  1.00 43.21           O  
ANISOU 2145  O   ARG A 281     7604   4382   4431   1784   2846   1484       O  
ATOM   2146  CB  ARG A 281      52.843 114.393  -3.819  1.00 43.37           C  
ANISOU 2146  CB  ARG A 281     7854   4361   4265   1964   2850   1325       C  
ATOM   2147  CG  ARG A 281      52.415 114.944  -5.168  1.00 43.67           C  
ANISOU 2147  CG  ARG A 281     7896   4438   4258   2048   2885   1338       C  
ATOM   2148  CD  ARG A 281      50.956 114.645  -5.453  1.00 43.24           C  
ANISOU 2148  CD  ARG A 281     7952   4323   4156   2010   2832   1206       C  
ATOM   2149  NE  ARG A 281      50.780 113.407  -6.206  1.00 43.80           N  
ANISOU 2149  NE  ARG A 281     8159   4378   4104   2132   2825   1146       N  
ATOM   2150  CZ  ARG A 281      49.597 112.877  -6.499  1.00 43.63           C  
ANISOU 2150  CZ  ARG A 281     8251   4304   4022   2111   2773   1028       C  
ATOM   2151  NH1 ARG A 281      49.527 111.750  -7.193  1.00 44.26           N1+
ANISOU 2151  NH1 ARG A 281     8454   4365   3997   2217   2756    975       N1+
ATOM   2152  NH2 ARG A 281      48.483 113.474  -6.095  1.00 42.89           N  
ANISOU 2152  NH2 ARG A 281     8142   4175   3980   1978   2727    965       N  
ATOM   2153  N   ILE A 282      54.813 112.892  -1.751  1.00 43.73           N  
ANISOU 2153  N   ILE A 282     7867   4408   4340   1953   2838   1397       N  
ATOM   2154  CA  ILE A 282      55.240 112.566  -0.393  1.00 43.46           C  
ANISOU 2154  CA  ILE A 282     7804   4352   4357   1863   2806   1399       C  
ATOM   2155  C   ILE A 282      56.664 113.056  -0.160  1.00 44.02           C  
ANISOU 2155  C   ILE A 282     7734   4516   4476   1887   2851   1545       C  
ATOM   2156  O   ILE A 282      56.973 113.662   0.873  1.00 43.70           O  
ANISOU 2156  O   ILE A 282     7600   4481   4523   1761   2826   1576       O  
ATOM   2157  CB  ILE A 282      55.117 111.053  -0.136  1.00 43.62           C  
ANISOU 2157  CB  ILE A 282     7961   4317   4297   1924   2784   1325       C  
ATOM   2158  CG1 ILE A 282      53.700 110.566  -0.450  1.00 43.19           C  
ANISOU 2158  CG1 ILE A 282     8044   4175   4193   1896   2737   1184       C  
ATOM   2159  CG2 ILE A 282      55.495 110.721   1.300  1.00 43.33           C  
ANISOU 2159  CG2 ILE A 282     7894   4257   4311   1830   2749   1324       C  
ATOM   2160  CD1 ILE A 282      52.619 111.260   0.343  1.00 42.22           C  
ANISOU 2160  CD1 ILE A 282     7900   3994   4148   1718   2677   1108       C  
ATOM   2161  N   GLU A 283      57.550 112.805  -1.127  1.00 44.93           N  
ANISOU 2161  N   GLU A 283     7830   4709   4531   2050   2917   1641       N  
ATOM   2162  CA  GLU A 283      58.936 113.246  -1.001  1.00 45.59           C  
ANISOU 2162  CA  GLU A 283     7765   4895   4664   2080   2952   1785       C  
ATOM   2163  C   GLU A 283      59.033 114.765  -0.950  1.00 45.40           C  
ANISOU 2163  C   GLU A 283     7600   4905   4745   1967   2952   1847       C  
ATOM   2164  O   GLU A 283      59.856 115.317  -0.210  1.00 45.56           O  
ANISOU 2164  O   GLU A 283     7497   4973   4841   1888   2947   1931       O  
ATOM   2165  CB  GLU A 283      59.765 112.698  -2.162  1.00 46.65           C  
ANISOU 2165  CB  GLU A 283     7890   5103   4732   2278   2993   1850       C  
ATOM   2166  CG  GLU A 283      61.236 113.069  -2.109  1.00 47.48           C  
ANISOU 2166  CG  GLU A 283     7828   5324   4888   2320   3021   1998       C  
ATOM   2167  CD  GLU A 283      61.910 112.959  -3.463  1.00 48.49           C  
ANISOU 2167  CD  GLU A 283     7921   5530   4973   2502   3064   2070       C  
ATOM   2168  OE1 GLU A 283      61.191 112.856  -4.478  1.00 48.48           O  
ANISOU 2168  OE1 GLU A 283     8010   5495   4916   2577   3069   2009       O  
ATOM   2169  OE2 GLU A 283      63.158 112.978  -3.513  1.00 49.34           O1+
ANISOU 2169  OE2 GLU A 283     7910   5737   5101   2570   3089   2190       O1+
ATOM   2170  N   ARG A 284      58.200 115.461  -1.730  1.00 45.11           N  
ANISOU 2170  N   ARG A 284     7582   4846   4713   1957   2955   1807       N  
ATOM   2171  CA  ARG A 284      58.247 116.920  -1.741  1.00 44.99           C  
ANISOU 2171  CA  ARG A 284     7443   4854   4796   1856   2957   1863       C  
ATOM   2172  C   ARG A 284      57.807 117.501  -0.403  1.00 44.20           C  
ANISOU 2172  C   ARG A 284     7328   4689   4776   1663   2916   1825       C  
ATOM   2173  O   ARG A 284      58.361 118.508   0.053  1.00 44.31           O  
ANISOU 2173  O   ARG A 284     7221   4734   4882   1565   2910   1898       O  
ATOM   2174  CB  ARG A 284      57.384 117.475  -2.876  1.00 44.87           C  
ANISOU 2174  CB  ARG A 284     7460   4825   4762   1897   2970   1823       C  
ATOM   2175  CG  ARG A 284      58.173 117.866  -4.118  1.00 45.78           C  
ANISOU 2175  CG  ARG A 284     7486   5033   4873   2029   3012   1922       C  
ATOM   2176  CD  ARG A 284      57.325 118.640  -5.126  1.00 45.63           C  
ANISOU 2176  CD  ARG A 284     7479   5004   4854   2046   3022   1893       C  
ATOM   2177  NE  ARG A 284      57.094 120.026  -4.722  1.00 45.25           N  
ANISOU 2177  NE  ARG A 284     7341   4941   4910   1903   3013   1917       N  
ATOM   2178  CZ  ARG A 284      56.639 120.975  -5.535  1.00 45.28           C  
ANISOU 2178  CZ  ARG A 284     7311   4952   4939   1910   3028   1927       C  
ATOM   2179  NH1 ARG A 284      56.458 122.210  -5.085  1.00 44.98           N1+
ANISOU 2179  NH1 ARG A 284     7200   4893   4997   1777   3020   1946       N1+
ATOM   2180  NH2 ARG A 284      56.371 120.693  -6.802  1.00 45.65           N  
ANISOU 2180  NH2 ARG A 284     7403   5029   4915   2052   3050   1917       N  
ATOM   2181  N   ILE A 285      56.815 116.886   0.243  1.00 43.45           N  
ANISOU 2181  N   ILE A 285     7343   4506   4661   1600   2861   1694       N  
ATOM   2182  CA  ILE A 285      56.369 117.382   1.541  1.00 42.73           C  
ANISOU 2182  CA  ILE A 285     7232   4352   4651   1421   2800   1637       C  
ATOM   2183  C   ILE A 285      57.388 117.044   2.621  1.00 42.98           C  
ANISOU 2183  C   ILE A 285     7201   4415   4715   1377   2782   1692       C  
ATOM   2184  O   ILE A 285      57.690 117.871   3.491  1.00 42.85           O  
ANISOU 2184  O   ILE A 285     7099   4400   4784   1246   2757   1724       O  
ATOM   2185  CB  ILE A 285      54.974 116.826   1.882  1.00 41.91           C  
ANISOU 2185  CB  ILE A 285     7256   4151   4517   1370   2746   1485       C  
ATOM   2186  CG1 ILE A 285      53.939 117.319   0.866  1.00 41.69           C  
ANISOU 2186  CG1 ILE A 285     7273   4101   4464   1397   2760   1438       C  
ATOM   2187  CG2 ILE A 285      54.571 117.227   3.293  1.00 41.23           C  
ANISOU 2187  CG2 ILE A 285     7153   4004   4506   1199   2686   1430       C  
ATOM   2188  CD1 ILE A 285      52.512 116.934   1.206  1.00 40.92           C  
ANISOU 2188  CD1 ILE A 285     7285   3918   4347   1330   2704   1298       C  
ATOM   2189  N   ARG A 286      57.938 115.827   2.582  1.00 45.78           N  
ANISOU 2189  N   ARG A 286     7600   4796   4999   1488   2795   1704       N  
ATOM   2190  CA  ARG A 286      58.923 115.427   3.583  1.00 46.21           C  
ANISOU 2190  CA  ARG A 286     7594   4889   5074   1460   2781   1761       C  
ATOM   2191  C   ARG A 286      60.159 116.314   3.529  1.00 46.68           C  
ANISOU 2191  C   ARG A 286     7494   5049   5193   1447   2814   1913       C  
ATOM   2192  O   ARG A 286      60.713 116.685   4.570  1.00 47.06           O  
ANISOU 2192  O   ARG A 286     7458   5117   5305   1335   2782   1951       O  
ATOM   2193  CB  ARG A 286      59.317 113.965   3.383  1.00 46.68           C  
ANISOU 2193  CB  ARG A 286     7734   4963   5037   1607   2801   1758       C  
ATOM   2194  CG  ARG A 286      60.307 113.454   4.417  1.00 47.14           C  
ANISOU 2194  CG  ARG A 286     7736   5066   5108   1591   2789   1817       C  
ATOM   2195  CD  ARG A 286      61.119 112.287   3.887  1.00 47.78           C  
ANISOU 2195  CD  ARG A 286     7855   5204   5096   1776   2841   1877       C  
ATOM   2196  NE  ARG A 286      60.314 111.391   3.064  1.00 47.89           N  
ANISOU 2196  NE  ARG A 286     8027   5152   5017   1887   2853   1783       N  
ATOM   2197  CZ  ARG A 286      60.733 110.213   2.615  1.00 48.41           C  
ANISOU 2197  CZ  ARG A 286     8175   5230   4987   2048   2891   1798       C  
ATOM   2198  NH1 ARG A 286      59.933 109.465   1.867  1.00 48.14           N1+
ANISOU 2198  NH1 ARG A 286     8294   5128   4871   2133   2894   1703       N1+
ATOM   2199  NH2 ARG A 286      61.948 109.779   2.919  1.00 49.26           N  
ANISOU 2199  NH2 ARG A 286     8217   5421   5078   2126   2925   1908       N  
ATOM   2200  N   ASN A 287      60.607 116.666   2.323  1.00 45.24           N  
ANISOU 2200  N   ASN A 287     7266   4935   4988   1558   2879   2003       N  
ATOM   2201  CA  ASN A 287      61.809 117.480   2.190  1.00 46.04           C  
ANISOU 2201  CA  ASN A 287     7204   5139   5152   1548   2900   2146       C  
ATOM   2202  C   ASN A 287      61.573 118.920   2.629  1.00 45.73           C  
ANISOU 2202  C   ASN A 287     7086   5072   5217   1377   2875   2157       C  
ATOM   2203  O   ASN A 287      62.512 119.588   3.076  1.00 46.27           O  
ANISOU 2203  O   ASN A 287     7023   5202   5353   1301   2867   2256       O  
ATOM   2204  CB  ASN A 287      62.312 117.436   0.746  1.00 46.85           C  
ANISOU 2204  CB  ASN A 287     7267   5320   5214   1716   2948   2213       C  
ATOM   2205  CG  ASN A 287      62.940 116.102   0.390  1.00 47.48           C  
ANISOU 2205  CG  ASN A 287     7390   5450   5202   1890   2974   2235       C  
ATOM   2206  OD1 ASN A 287      62.982 115.185   1.211  1.00 47.31           O  
ANISOU 2206  OD1 ASN A 287     7430   5402   5144   1886   2958   2200       O  
ATOM   2207  ND2 ASN A 287      63.430 115.987  -0.838  1.00 48.27           N  
ANISOU 2207  ND2 ASN A 287     7460   5618   5262   2046   3016   2294       N  
ATOM   2208  N   GLU A 288      60.338 119.414   2.518  1.00 48.83           N  
ANISOU 2208  N   GLU A 288     7559   5373   5622   1312   2861   2058       N  
ATOM   2209  CA  GLU A 288      60.066 120.795   2.907  1.00 48.64           C  
ANISOU 2209  CA  GLU A 288     7473   5313   5695   1156   2838   2062       C  
ATOM   2210  C   GLU A 288      60.151 120.976   4.417  1.00 48.37           C  
ANISOU 2210  C   GLU A 288     7417   5239   5722    993   2773   2029       C  
ATOM   2211  O   GLU A 288      60.729 121.959   4.897  1.00 48.92           O  
ANISOU 2211  O   GLU A 288     7387   5329   5872    879   2761   2099       O  
ATOM   2212  CB  GLU A 288      58.695 121.233   2.392  1.00 47.95           C  
ANISOU 2212  CB  GLU A 288     7475   5143   5601   1142   2837   1960       C  
ATOM   2213  CG  GLU A 288      58.706 121.716   0.952  1.00 48.42           C  
ANISOU 2213  CG  GLU A 288     7499   5250   5647   1250   2879   2002       C  
ATOM   2214  CD  GLU A 288      57.822 122.929   0.740  1.00 47.98           C  
ANISOU 2214  CD  GLU A 288     7444   5138   5648   1164   2872   1962       C  
ATOM   2215  OE1 GLU A 288      56.862 123.108   1.521  1.00 47.28           O  
ANISOU 2215  OE1 GLU A 288     7427   4960   5578   1055   2836   1868       O  
ATOM   2216  OE2 GLU A 288      58.093 123.707  -0.201  1.00 48.18           O1+
ANISOU 2216  OE2 GLU A 288     7398   5211   5698   1209   2901   2026       O1+
ATOM   2217  N   HIS A 289      59.579 120.048   5.180  1.00 47.68           N  
ANISOU 2217  N   HIS A 289     7423   5094   5598    977   2727   1920       N  
ATOM   2218  CA  HIS A 289      59.641 120.072   6.640  1.00 47.31           C  
ANISOU 2218  CA  HIS A 289     7364   5013   5598    836   2661   1880       C  
ATOM   2219  C   HIS A 289      60.630 119.043   7.168  1.00 47.99           C  
ANISOU 2219  C   HIS A 289     7419   5166   5647    891   2655   1932       C  
ATOM   2220  O   HIS A 289      60.396 118.422   8.210  1.00 48.04           O  
ANISOU 2220  O   HIS A 289     7474   5134   5646    837   2606   1861       O  
ATOM   2221  CB  HIS A 289      58.256 119.838   7.235  1.00 46.52           C  
ANISOU 2221  CB  HIS A 289     7385   4801   5489    768   2612   1726       C  
ATOM   2222  CG  HIS A 289      57.173 120.628   6.572  1.00 46.05           C  
ANISOU 2222  CG  HIS A 289     7372   4682   5442    749   2626   1671       C  
ATOM   2223  ND1 HIS A 289      56.697 121.815   7.085  1.00 45.80           N  
ANISOU 2223  ND1 HIS A 289     7322   4595   5484    612   2601   1647       N  
ATOM   2224  CD2 HIS A 289      56.468 120.398   5.439  1.00 45.85           C  
ANISOU 2224  CD2 HIS A 289     7414   4646   5363    854   2661   1637       C  
ATOM   2225  CE1 HIS A 289      55.747 122.284   6.295  1.00 45.39           C  
ANISOU 2225  CE1 HIS A 289     7319   4504   5424    637   2625   1605       C  
ATOM   2226  NE2 HIS A 289      55.588 121.443   5.289  1.00 45.57           N  
ANISOU 2226  NE2 HIS A 289     7390   4555   5369    780   2659   1598       N  
ATOM   2227  N   ALA A 290      61.750 118.853   6.462  1.00 49.26           N  
ANISOU 2227  N   ALA A 290     7498   5433   5784   1003   2709   2061       N  
ATOM   2228  CA  ALA A 290      62.681 117.779   6.797  1.00 49.93           C  
ANISOU 2228  CA  ALA A 290     7560   5591   5820   1088   2716   2118       C  
ATOM   2229  C   ALA A 290      63.251 117.929   8.202  1.00 50.50           C  
ANISOU 2229  C   ALA A 290     7560   5681   5945    954   2658   2138       C  
ATOM   2230  O   ALA A 290      63.656 116.934   8.815  1.00 51.04           O  
ANISOU 2230  O   ALA A 290     7645   5777   5973    996   2645   2138       O  
ATOM   2231  CB  ALA A 290      63.811 117.729   5.769  1.00 50.74           C  
ANISOU 2231  CB  ALA A 290     7571   5814   5894   1229   2789   2270       C  
ATOM   2232  N   GLU A 291      63.274 119.151   8.736  1.00 52.09           N  
ANISOU 2232  N   GLU A 291     7690   5866   6234    793   2622   2151       N  
ATOM   2233  CA  GLU A 291      63.923 119.375  10.022  1.00 52.76           C  
ANISOU 2233  CA  GLU A 291     7698   5981   6368    663   2565   2181       C  
ATOM   2234  C   GLU A 291      63.092 118.842  11.184  1.00 52.44           C  
ANISOU 2234  C   GLU A 291     7758   5849   6317    587   2501   2044       C  
ATOM   2235  O   GLU A 291      63.650 118.506  12.235  1.00 53.14           O  
ANISOU 2235  O   GLU A 291     7808   5972   6411    532   2460   2060       O  
ATOM   2236  CB  GLU A 291      64.214 120.864  10.202  1.00 53.19           C  
ANISOU 2236  CB  GLU A 291     7655   6038   6515    513   2544   2236       C  
ATOM   2237  CG  GLU A 291      64.862 121.497   8.979  1.00 53.71           C  
ANISOU 2237  CG  GLU A 291     7630   6180   6598    582   2610   2365       C  
ATOM   2238  CD  GLU A 291      65.233 122.950   9.188  1.00 54.10           C  
ANISOU 2238  CD  GLU A 291     7582   6232   6743    426   2589   2429       C  
ATOM   2239  OE1 GLU A 291      65.306 123.383  10.357  1.00 54.27           O  
ANISOU 2239  OE1 GLU A 291     7584   6224   6813    269   2521   2399       O  
ATOM   2240  OE2 GLU A 291      65.452 123.658   8.181  1.00 54.21           O1+
ANISOU 2240  OE2 GLU A 291     7542   6275   6780    461   2642   2511       O1+
ATOM   2241  N   THR A 292      61.770 118.753  11.022  1.00 48.20           N  
ANISOU 2241  N   THR A 292     7346   5203   5764    583   2494   1915       N  
ATOM   2242  CA  THR A 292      60.889 118.253  12.073  1.00 47.68           C  
ANISOU 2242  CA  THR A 292     7379   5050   5689    515   2438   1787       C  
ATOM   2243  C   THR A 292      60.135 116.996  11.655  1.00 47.03           C  
ANISOU 2243  C   THR A 292     7423   4920   5525    637   2457   1703       C  
ATOM   2244  O   THR A 292      59.200 116.586  12.354  1.00 46.32           O  
ANISOU 2244  O   THR A 292     7428   4747   5425    587   2416   1589       O  
ATOM   2245  CB  THR A 292      59.886 119.332  12.496  1.00 46.79           C  
ANISOU 2245  CB  THR A 292     7302   4841   5636    372   2400   1701       C  
ATOM   2246  OG1 THR A 292      58.804 119.376  11.557  1.00 46.17           O  
ANISOU 2246  OG1 THR A 292     7311   4699   5532    430   2431   1633       O  
ATOM   2247  CG2 THR A 292      60.555 120.698  12.546  1.00 47.04           C  
ANISOU 2247  CG2 THR A 292     7222   4906   5744    265   2395   1787       C  
ATOM   2248  N   TRP A 293      60.515 116.375  10.543  1.00 43.36           N  
ANISOU 2248  N   TRP A 293     6968   4506   5001    795   2516   1757       N  
ATOM   2249  CA  TRP A 293      59.791 115.216  10.036  1.00 43.02           C  
ANISOU 2249  CA  TRP A 293     7056   4412   4877    911   2533   1675       C  
ATOM   2250  C   TRP A 293      60.057 113.987  10.898  1.00 43.06           C  
ANISOU 2250  C   TRP A 293     7106   4416   4838    943   2512   1652       C  
ATOM   2251  O   TRP A 293      61.175 113.772  11.375  1.00 43.70           O  
ANISOU 2251  O   TRP A 293     7103   4580   4922    959   2516   1744       O  
ATOM   2252  CB  TRP A 293      60.199 114.942   8.588  1.00 43.62           C  
ANISOU 2252  CB  TRP A 293     7133   4546   4897   1076   2604   1745       C  
ATOM   2253  CG  TRP A 293      59.446 113.824   7.932  1.00 43.39           C  
ANISOU 2253  CG  TRP A 293     7246   4460   4780   1196   2621   1660       C  
ATOM   2254  CD1 TRP A 293      59.773 112.499   7.937  1.00 43.73           C  
ANISOU 2254  CD1 TRP A 293     7358   4511   4747   1312   2637   1657       C  
ATOM   2255  CD2 TRP A 293      58.244 113.937   7.161  1.00 42.86           C  
ANISOU 2255  CD2 TRP A 293     7274   4319   4690   1208   2623   1567       C  
ATOM   2256  NE1 TRP A 293      58.846 111.779   7.221  1.00 43.46           N  
ANISOU 2256  NE1 TRP A 293     7461   4405   4645   1390   2645   1564       N  
ATOM   2257  CE2 TRP A 293      57.897 112.640   6.734  1.00 42.92           C  
ANISOU 2257  CE2 TRP A 293     7408   4292   4608   1326   2634   1508       C  
ATOM   2258  CE3 TRP A 293      57.426 115.009   6.792  1.00 42.39           C  
ANISOU 2258  CE3 TRP A 293     7207   4221   4676   1132   2615   1530       C  
ATOM   2259  CZ2 TRP A 293      56.769 112.386   5.957  1.00 42.55           C  
ANISOU 2259  CZ2 TRP A 293     7474   4178   4515   1361   2632   1413       C  
ATOM   2260  CZ3 TRP A 293      56.307 114.755   6.021  1.00 41.99           C  
ANISOU 2260  CZ3 TRP A 293     7264   4111   4579   1175   2618   1440       C  
ATOM   2261  CH2 TRP A 293      55.988 113.455   5.613  1.00 42.08           C  
ANISOU 2261  CH2 TRP A 293     7395   4093   4501   1284   2623   1382       C  
ATOM   2262  N   PHE A 294      59.020 113.175  11.090  1.00 41.97           N  
ANISOU 2262  N   PHE A 294     7100   4186   4659    953   2490   1533       N  
ATOM   2263  CA  PHE A 294      59.147 111.931  11.840  1.00 41.99           C  
ANISOU 2263  CA  PHE A 294     7165   4175   4616    992   2475   1502       C  
ATOM   2264  C   PHE A 294      57.942 111.050  11.543  1.00 41.45           C  
ANISOU 2264  C   PHE A 294     7252   4004   4492   1033   2467   1380       C  
ATOM   2265  O   PHE A 294      56.964 111.482  10.928  1.00 40.98           O  
ANISOU 2265  O   PHE A 294     7243   3889   4437   1009   2464   1314       O  
ATOM   2266  CB  PHE A 294      59.278 112.190  13.347  1.00 41.74           C  
ANISOU 2266  CB  PHE A 294     7085   4137   4637    853   2417   1488       C  
ATOM   2267  CG  PHE A 294      58.022 112.712  13.991  1.00 40.81           C  
ANISOU 2267  CG  PHE A 294     7023   3920   4562    717   2364   1372       C  
ATOM   2268  CD1 PHE A 294      57.123 111.845  14.595  1.00 40.25           C  
ANISOU 2268  CD1 PHE A 294     7064   3766   4462    702   2334   1267       C  
ATOM   2269  CD2 PHE A 294      57.750 114.070  14.008  1.00 40.56           C  
ANISOU 2269  CD2 PHE A 294     6934   3879   4600    605   2347   1372       C  
ATOM   2270  CE1 PHE A 294      55.971 112.320  15.194  1.00 39.45           C  
ANISOU 2270  CE1 PHE A 294     7010   3583   4398    583   2289   1169       C  
ATOM   2271  CE2 PHE A 294      56.601 114.553  14.607  1.00 39.78           C  
ANISOU 2271  CE2 PHE A 294     6888   3691   4534    490   2304   1271       C  
ATOM   2272  CZ  PHE A 294      55.710 113.676  15.201  1.00 39.22           C  
ANISOU 2272  CZ  PHE A 294     6922   3546   4432    481   2275   1171       C  
ATOM   2273  N   LEU A 295      58.030 109.801  11.995  1.00 41.57           N  
ANISOU 2273  N   LEU A 295     7344   3998   4454   1093   2464   1354       N  
ATOM   2274  CA  LEU A 295      56.962 108.816  11.867  1.00 41.18           C  
ANISOU 2274  CA  LEU A 295     7446   3848   4350   1123   2451   1240       C  
ATOM   2275  C   LEU A 295      56.411 108.519  13.255  1.00 40.60           C  
ANISOU 2275  C   LEU A 295     7406   3714   4306   1009   2394   1167       C  
ATOM   2276  O   LEU A 295      57.162 108.126  14.153  1.00 40.88           O  
ANISOU 2276  O   LEU A 295     7402   3787   4344   1006   2387   1212       O  
ATOM   2277  CB  LEU A 295      57.474 107.534  11.208  1.00 41.89           C  
ANISOU 2277  CB  LEU A 295     7617   3950   4349   1294   2498   1267       C  
ATOM   2278  CG  LEU A 295      57.943 107.621   9.755  1.00 42.53           C  
ANISOU 2278  CG  LEU A 295     7692   4085   4382   1433   2559   1331       C  
ATOM   2279  CD1 LEU A 295      58.900 106.484   9.441  1.00 43.44           C  
ANISOU 2279  CD1 LEU A 295     7845   4243   4417   1601   2611   1398       C  
ATOM   2280  CD2 LEU A 295      56.755 107.594   8.805  1.00 42.16           C  
ANISOU 2280  CD2 LEU A 295     7753   3962   4304   1445   2554   1235       C  
ATOM   2281  N   ASP A 296      55.106 108.707  13.428  1.00 42.78           N  
ANISOU 2281  N   ASP A 296     7752   3903   4601    920   2356   1061       N  
ATOM   2282  CA  ASP A 296      54.455 108.494  14.715  1.00 42.11           C  
ANISOU 2282  CA  ASP A 296     7699   3756   4543    810   2304    989       C  
ATOM   2283  C   ASP A 296      53.923 107.068  14.784  1.00 42.31           C  
ANISOU 2283  C   ASP A 296     7860   3710   4505    869   2300    921       C  
ATOM   2284  O   ASP A 296      53.077 106.674  13.974  1.00 42.37           O  
ANISOU 2284  O   ASP A 296     7965   3660   4474    905   2304    857       O  
ATOM   2285  CB  ASP A 296      53.327 109.503  14.928  1.00 41.12           C  
ANISOU 2285  CB  ASP A 296     7570   3580   4473    681   2266    919       C  
ATOM   2286  CG  ASP A 296      52.686 109.382  16.298  1.00 40.71           C  
ANISOU 2286  CG  ASP A 296     7544   3474   4452    569   2215    853       C  
ATOM   2287  OD1 ASP A 296      53.268 108.706  17.173  1.00 41.00           O  
ANISOU 2287  OD1 ASP A 296     7577   3525   4478    577   2206    875       O  
ATOM   2288  OD2 ASP A 296      51.604 109.971  16.502  1.00 39.82           O1+
ANISOU 2288  OD2 ASP A 296     7452   3307   4370    477   2186    785       O1+
ATOM   2289  N   GLU A 297      54.417 106.301  15.758  1.00 45.33           N  
ANISOU 2289  N   GLU A 297     8250   4096   4876    877   2292    937       N  
ATOM   2290  CA  GLU A 297      53.956 104.935  15.968  1.00 45.32           C  
ANISOU 2290  CA  GLU A 297     8378   4020   4819    924   2288    877       C  
ATOM   2291  C   GLU A 297      52.524 104.867  16.480  1.00 44.55           C  
ANISOU 2291  C   GLU A 297     8357   3827   4744    814   2239    766       C  
ATOM   2292  O   GLU A 297      51.945 103.776  16.495  1.00 44.45           O  
ANISOU 2292  O   GLU A 297     8462   3739   4686    843   2233    707       O  
ATOM   2293  CB  GLU A 297      54.879 104.218  16.956  1.00 46.01           C  
ANISOU 2293  CB  GLU A 297     8444   4143   4893    958   2294    931       C  
ATOM   2294  CG  GLU A 297      56.360 104.348  16.644  1.00 47.45           C  
ANISOU 2294  CG  GLU A 297     8528   4438   5061   1055   2339   1055       C  
ATOM   2295  CD  GLU A 297      57.236 103.689  17.694  1.00 48.24           C  
ANISOU 2295  CD  GLU A 297     8598   4583   5150   1081   2342   1112       C  
ATOM   2296  OE1 GLU A 297      56.713 103.352  18.778  1.00 47.84           O  
ANISOU 2296  OE1 GLU A 297     8583   4481   5115   1003   2303   1056       O  
ATOM   2297  OE2 GLU A 297      58.445 103.506  17.434  1.00 48.99           O1+
ANISOU 2297  OE2 GLU A 297     8629   4770   5216   1184   2384   1217       O1+
ATOM   2298  N   ASN A 298      51.942 105.995  16.892  1.00 41.66           N  
ANISOU 2298  N   ASN A 298     7928   3460   4442    692   2206    740       N  
ATOM   2299  CA  ASN A 298      50.635 106.022  17.535  1.00 40.82           C  
ANISOU 2299  CA  ASN A 298     7875   3275   4359    584   2160    648       C  
ATOM   2300  C   ASN A 298      49.568 106.709  16.688  1.00 40.16           C  
ANISOU 2300  C   ASN A 298     7811   3161   4286    546   2152    596       C  
ATOM   2301  O   ASN A 298      48.582 107.209  17.235  1.00 38.92           O  
ANISOU 2301  O   ASN A 298     7656   2965   4166    441   2118    540       O  
ATOM   2302  CB  ASN A 298      50.737 106.708  18.898  1.00 40.15           C  
ANISOU 2302  CB  ASN A 298     7713   3209   4335    472   2127    657       C  
ATOM   2303  CG  ASN A 298      51.522 105.893  19.905  1.00 40.20           C  
ANISOU 2303  CG  ASN A 298     7716   3234   4326    497   2125    691       C  
ATOM   2304  OD1 ASN A 298      51.442 104.665  19.924  1.00 40.35           O  
ANISOU 2304  OD1 ASN A 298     7824   3211   4296    561   2134    671       O  
ATOM   2305  ND2 ASN A 298      52.286 106.574  20.751  1.00 40.20           N  
ANISOU 2305  ND2 ASN A 298     7614   3296   4366    444   2111    745       N  
ATOM   2306  N   HIS A 299      49.735 106.739  15.367  1.00 38.00           N  
ANISOU 2306  N   HIS A 299     7554   2908   3978    633   2185    614       N  
ATOM   2307  CA  HIS A 299      48.756 107.404  14.523  1.00 37.65           C  
ANISOU 2307  CA  HIS A 299     7523   2844   3939    604   2179    570       C  
ATOM   2308  C   HIS A 299      47.446 106.612  14.497  1.00 37.32           C  
ANISOU 2308  C   HIS A 299     7595   2719   3866    572   2147    474       C  
ATOM   2309  O   HIS A 299      47.448 105.387  14.646  1.00 37.61           O  
ANISOU 2309  O   HIS A 299     7721   2711   3858    614   2143    449       O  
ATOM   2310  CB  HIS A 299      49.298 107.582  13.106  1.00 38.30           C  
ANISOU 2310  CB  HIS A 299     7595   2974   3984    714   2224    617       C  
ATOM   2311  CG  HIS A 299      49.417 106.305  12.335  1.00 39.01           C  
ANISOU 2311  CG  HIS A 299     7794   3037   3992    832   2244    600       C  
ATOM   2312  ND1 HIS A 299      48.340 105.704  11.720  1.00 39.01           N  
ANISOU 2312  ND1 HIS A 299     7904   2971   3945    836   2224    519       N  
ATOM   2313  CD2 HIS A 299      50.487 105.518  12.073  1.00 39.81           C  
ANISOU 2313  CD2 HIS A 299     7914   3167   4043    951   2282    656       C  
ATOM   2314  CE1 HIS A 299      48.741 104.600  11.116  1.00 39.77           C  
ANISOU 2314  CE1 HIS A 299     8092   3049   3968    950   2247    519       C  
ATOM   2315  NE2 HIS A 299      50.040 104.464  11.314  1.00 40.27           N  
ANISOU 2315  NE2 HIS A 299     8104   3169   4027   1027   2286    603       N  
ATOM   2316  N   PRO A 300      46.306 107.296  14.314  1.00 37.08           N  
ANISOU 2316  N   PRO A 300     7563   2666   3859    495   2123    424       N  
ATOM   2317  CA  PRO A 300      45.008 106.628  14.473  1.00 36.85           C  
ANISOU 2317  CA  PRO A 300     7625   2565   3810    442   2085    340       C  
ATOM   2318  C   PRO A 300      44.301 106.300  13.165  1.00 37.10           C  
ANISOU 2318  C   PRO A 300     7731   2578   3788    489   2085    298       C  
ATOM   2319  O   PRO A 300      43.067 106.322  13.115  1.00 36.82           O  
ANISOU 2319  O   PRO A 300     7731   2508   3752    422   2052    237       O  
ATOM   2320  CB  PRO A 300      44.208 107.663  15.267  1.00 36.19           C  
ANISOU 2320  CB  PRO A 300     7481   2479   3789    323   2059    320       C  
ATOM   2321  CG  PRO A 300      44.700 108.975  14.688  1.00 36.15           C  
ANISOU 2321  CG  PRO A 300     7383   2535   3815    336   2088    374       C  
ATOM   2322  CD  PRO A 300      46.151 108.760  14.268  1.00 36.70           C  
ANISOU 2322  CD  PRO A 300     7421   2656   3867    435   2127    448       C  
ATOM   2323  N   TYR A 301      45.045 105.988  12.109  1.00 37.00           N  
ANISOU 2323  N   TYR A 301     7741   2592   3724    605   2120    330       N  
ATOM   2324  CA  TYR A 301      44.468 105.829  10.774  1.00 37.30           C  
ANISOU 2324  CA  TYR A 301     7841   2623   3706    657   2122    296       C  
ATOM   2325  C   TYR A 301      44.292 104.345  10.467  1.00 37.85           C  
ANISOU 2325  C   TYR A 301     8050   2629   3704    710   2109    246       C  
ATOM   2326  O   TYR A 301      45.259 103.634  10.183  1.00 38.44           O  
ANISOU 2326  O   TYR A 301     8166   2707   3733    816   2141    279       O  
ATOM   2327  CB  TYR A 301      45.337 106.523   9.731  1.00 37.62           C  
ANISOU 2327  CB  TYR A 301     7822   2737   3735    753   2171    364       C  
ATOM   2328  CG  TYR A 301      45.496 107.997  10.006  1.00 37.15           C  
ANISOU 2328  CG  TYR A 301     7635   2732   3749    694   2184    413       C  
ATOM   2329  CD1 TYR A 301      44.426 108.867   9.856  1.00 36.69           C  
ANISOU 2329  CD1 TYR A 301     7549   2671   3719    618   2164    379       C  
ATOM   2330  CD2 TYR A 301      46.711 108.518  10.430  1.00 37.25           C  
ANISOU 2330  CD2 TYR A 301     7554   2797   3800    714   2215    495       C  
ATOM   2331  CE1 TYR A 301      44.560 110.214  10.114  1.00 36.33           C  
ANISOU 2331  CE1 TYR A 301     7399   2665   3738    566   2179    423       C  
ATOM   2332  CE2 TYR A 301      46.855 109.868  10.689  1.00 36.90           C  
ANISOU 2332  CE2 TYR A 301     7403   2795   3824    652   2223    538       C  
ATOM   2333  CZ  TYR A 301      45.774 110.710  10.529  1.00 36.44           C  
ANISOU 2333  CZ  TYR A 301     7331   2723   3793    580   2206    499       C  
ATOM   2334  OH  TYR A 301      45.900 112.055  10.784  1.00 36.17           O  
ANISOU 2334  OH  TYR A 301     7201   2719   3822    521   2217    540       O  
ATOM   2335  N   ARG A 302      43.040 103.887  10.519  1.00 40.44           N  
ANISOU 2335  N   ARG A 302     8450   2897   4017    636   2062    168       N  
ATOM   2336  CA  ARG A 302      42.724 102.509  10.156  1.00 40.61           C  
ANISOU 2336  CA  ARG A 302     8615   2847   3969    672   2042    112       C  
ATOM   2337  C   ARG A 302      42.837 102.297   8.651  1.00 41.34           C  
ANISOU 2337  C   ARG A 302     8772   2951   3985    776   2059    103       C  
ATOM   2338  O   ARG A 302      43.616 101.457   8.185  1.00 41.83           O  
ANISOU 2338  O   ARG A 302     8913   2996   3985    888   2088    116       O  
ATOM   2339  CB  ARG A 302      41.314 102.150  10.634  1.00 39.94           C  
ANISOU 2339  CB  ARG A 302     8579   2700   3895    550   1983     37       C  
ATOM   2340  CG  ARG A 302      41.251 101.464  11.985  1.00 39.40           C  
ANISOU 2340  CG  ARG A 302     8534   2578   3858    486   1964     26       C  
ATOM   2341  CD  ARG A 302      39.809 101.299  12.438  1.00 39.08           C  
ANISOU 2341  CD  ARG A 302     8519   2492   3837    360   1907    -36       C  
ATOM   2342  NE  ARG A 302      39.583 101.907  13.746  1.00 38.35           N  
ANISOU 2342  NE  ARG A 302     8335   2416   3818    268   1898    -17       N  
ATOM   2343  CZ  ARG A 302      39.548 101.231  14.890  1.00 38.28           C  
ANISOU 2343  CZ  ARG A 302     8319   2400   3826    219   1871    -19       C  
ATOM   2344  NH1 ARG A 302      39.342 101.869  16.034  1.00 37.68           N1+
ANISOU 2344  NH1 ARG A 302     8154   2350   3811    143   1862     -3       N1+
ATOM   2345  NH2 ARG A 302      39.720  99.916  14.891  1.00 38.87           N  
ANISOU 2345  NH2 ARG A 302     8476   2442   3854    249   1855    -37       N  
ATOM   2346  N   THR A 303      42.067 103.059   7.873  1.00 39.03           N  
ANISOU 2346  N   THR A 303     8447   2691   3690    749   2045     83       N  
ATOM   2347  CA  THR A 303      41.861 102.776   6.458  1.00 39.65           C  
ANISOU 2347  CA  THR A 303     8603   2775   3689    828   2047     55       C  
ATOM   2348  C   THR A 303      42.480 103.829   5.541  1.00 39.67           C  
ANISOU 2348  C   THR A 303     8518   2865   3691    912   2095    118       C  
ATOM   2349  O   THR A 303      42.122 103.903   4.361  1.00 40.06           O  
ANISOU 2349  O   THR A 303     8605   2933   3682    962   2094     97       O  
ATOM   2350  CB  THR A 303      40.366 102.635   6.168  1.00 39.62           C  
ANISOU 2350  CB  THR A 303     8649   2737   3667    734   1985    -25       C  
ATOM   2351  OG1 THR A 303      39.752 103.929   6.179  1.00 38.98           O  
ANISOU 2351  OG1 THR A 303     8452   2717   3640    666   1981     -8       O  
ATOM   2352  CG2 THR A 303      39.707 101.771   7.233  1.00 39.51           C  
ANISOU 2352  CG2 THR A 303     8696   2644   3673    631   1938    -75       C  
ATOM   2353  N   TRP A 304      43.393 104.647   6.056  1.00 39.10           N  
ANISOU 2353  N   TRP A 304     8330   2847   3679    924   2137    197       N  
ATOM   2354  CA  TRP A 304      44.211 105.535   5.241  1.00 39.25           C  
ANISOU 2354  CA  TRP A 304     8268   2948   3699   1014   2191    272       C  
ATOM   2355  C   TRP A 304      45.670 105.137   5.405  1.00 39.69           C  
ANISOU 2355  C   TRP A 304     8311   3027   3743   1117   2240    345       C  
ATOM   2356  O   TRP A 304      46.111 104.810   6.510  1.00 39.51           O  
ANISOU 2356  O   TRP A 304     8272   2984   3757   1081   2237    362       O  
ATOM   2357  CB  TRP A 304      44.044 107.009   5.638  1.00 38.55           C  
ANISOU 2357  CB  TRP A 304     8039   2911   3696    933   2198    313       C  
ATOM   2358  CG  TRP A 304      42.669 107.591   5.456  1.00 38.13           C  
ANISOU 2358  CG  TRP A 304     7978   2852   3657    842   2160    259       C  
ATOM   2359  CD1 TRP A 304      41.530 107.226   6.113  1.00 37.80           C  
ANISOU 2359  CD1 TRP A 304     7977   2757   3627    734   2105    189       C  
ATOM   2360  CD2 TRP A 304      42.301 108.677   4.593  1.00 38.03           C  
ANISOU 2360  CD2 TRP A 304     7904   2896   3650    854   2178    280       C  
ATOM   2361  NE1 TRP A 304      40.474 108.000   5.698  1.00 37.52           N  
ANISOU 2361  NE1 TRP A 304     7910   2746   3601    681   2087    166       N  
ATOM   2362  CE2 TRP A 304      40.921 108.900   4.766  1.00 37.65           C  
ANISOU 2362  CE2 TRP A 304     7865   2828   3614    754   2131    219       C  
ATOM   2363  CE3 TRP A 304      43.002 109.474   3.681  1.00 38.28           C  
ANISOU 2363  CE3 TRP A 304     7872   2996   3677    942   2231    349       C  
ATOM   2364  CZ2 TRP A 304      40.229 109.884   4.064  1.00 37.51           C  
ANISOU 2364  CZ2 TRP A 304     7797   2857   3600    744   2138    225       C  
ATOM   2365  CZ3 TRP A 304      42.312 110.452   2.986  1.00 38.12           C  
ANISOU 2365  CZ3 TRP A 304     7805   3016   3664    930   2237    352       C  
ATOM   2366  CH2 TRP A 304      40.940 110.648   3.181  1.00 37.74           C  
ANISOU 2366  CH2 TRP A 304     7769   2947   3624    833   2191    290       C  
ATOM   2367  N   ALA A 305      46.418 105.157   4.307  1.00 40.31           N  
ANISOU 2367  N   ALA A 305     8396   3153   3767   1251   2288    394       N  
ATOM   2368  CA  ALA A 305      47.853 104.931   4.398  1.00 40.77           C  
ANISOU 2368  CA  ALA A 305     8421   3255   3817   1357   2343    482       C  
ATOM   2369  C   ALA A 305      48.516 106.118   5.085  1.00 40.30           C  
ANISOU 2369  C   ALA A 305     8199   3262   3849   1302   2365    566       C  
ATOM   2370  O   ALA A 305      48.143 107.271   4.861  1.00 39.88           O  
ANISOU 2370  O   ALA A 305     8062   3246   3845   1247   2364    580       O  
ATOM   2371  CB  ALA A 305      48.453 104.714   3.010  1.00 41.61           C  
ANISOU 2371  CB  ALA A 305     8569   3401   3839   1518   2392    519       C  
ATOM   2372  N   TYR A 306      49.498 105.830   5.934  1.00 40.41           N  
ANISOU 2372  N   TYR A 306     8174   3293   3888   1317   2383    622       N  
ATOM   2373  CA  TYR A 306      50.176 106.842   6.733  1.00 40.05           C  
ANISOU 2373  CA  TYR A 306     7983   3307   3929   1253   2394    699       C  
ATOM   2374  C   TYR A 306      51.612 106.999   6.251  1.00 40.73           C  
ANISOU 2374  C   TYR A 306     7997   3480   3999   1374   2456    815       C  
ATOM   2375  O   TYR A 306      52.315 106.003   6.053  1.00 41.40           O  
ANISOU 2375  O   TYR A 306     8142   3567   4020   1489   2485    841       O  
ATOM   2376  CB  TYR A 306      50.150 106.470   8.217  1.00 39.65           C  
ANISOU 2376  CB  TYR A 306     7928   3216   3923   1157   2358    677       C  
ATOM   2377  CG  TYR A 306      50.941 107.410   9.093  1.00 39.42           C  
ANISOU 2377  CG  TYR A 306     7757   3247   3973   1094   2365    755       C  
ATOM   2378  CD1 TYR A 306      50.461 108.676   9.395  1.00 38.82           C  
ANISOU 2378  CD1 TYR A 306     7596   3182   3970    980   2345    752       C  
ATOM   2379  CD2 TYR A 306      52.168 107.030   9.619  1.00 39.86           C  
ANISOU 2379  CD2 TYR A 306     7769   3349   4028   1147   2390    832       C  
ATOM   2380  CE1 TYR A 306      51.182 109.540  10.196  1.00 38.69           C  
ANISOU 2380  CE1 TYR A 306     7461   3214   4024    915   2347    818       C  
ATOM   2381  CE2 TYR A 306      52.896 107.886  10.422  1.00 39.73           C  
ANISOU 2381  CE2 TYR A 306     7623   3391   4082   1080   2389    902       C  
ATOM   2382  CZ  TYR A 306      52.399 109.139  10.707  1.00 39.15           C  
ANISOU 2382  CZ  TYR A 306     7474   3320   4081    961   2365    892       C  
ATOM   2383  OH  TYR A 306      53.121 109.995  11.506  1.00 39.10           O  
ANISOU 2383  OH  TYR A 306     7350   3365   4143    887   2360    957       O  
ATOM   2384  N   HIS A 307      52.046 108.250   6.078  1.00 40.62           N  
ANISOU 2384  N   HIS A 307     7853   3536   4043   1349   2479    888       N  
ATOM   2385  CA  HIS A 307      53.342 108.539   5.482  1.00 41.31           C  
ANISOU 2385  CA  HIS A 307     7859   3717   4121   1460   2540   1008       C  
ATOM   2386  C   HIS A 307      54.272 109.372   6.356  1.00 41.25           C  
ANISOU 2386  C   HIS A 307     7704   3774   4195   1392   2546   1100       C  
ATOM   2387  O   HIS A 307      55.470 109.431   6.059  1.00 41.92           O  
ANISOU 2387  O   HIS A 307     7717   3941   4271   1481   2594   1208       O  
ATOM   2388  CB  HIS A 307      53.159 109.249   4.131  1.00 41.52           C  
ANISOU 2388  CB  HIS A 307     7867   3783   4126   1523   2574   1031       C  
ATOM   2389  CG  HIS A 307      52.372 108.455   3.135  1.00 41.76           C  
ANISOU 2389  CG  HIS A 307     8037   3764   4065   1604   2570    951       C  
ATOM   2390  ND1 HIS A 307      52.956 107.547   2.278  1.00 42.61           N  
ANISOU 2390  ND1 HIS A 307     8223   3887   4079   1767   2612    975       N  
ATOM   2391  CD2 HIS A 307      51.046 108.432   2.860  1.00 41.33           C  
ANISOU 2391  CD2 HIS A 307     8061   3647   3995   1544   2528    847       C  
ATOM   2392  CE1 HIS A 307      52.024 106.999   1.519  1.00 42.70           C  
ANISOU 2392  CE1 HIS A 307     8360   3843   4020   1798   2591    885       C  
ATOM   2393  NE2 HIS A 307      50.856 107.518   1.852  1.00 41.93           N  
ANISOU 2393  NE2 HIS A 307     8261   3701   3970   1662   2539    807       N  
ATOM   2394  N   GLY A 308      53.777 110.014   7.400  1.00 40.55           N  
ANISOU 2394  N   GLY A 308     7570   3654   4182   1240   2499   1063       N  
ATOM   2395  CA  GLY A 308      54.645 110.758   8.295  1.00 40.56           C  
ANISOU 2395  CA  GLY A 308     7443   3710   4257   1165   2496   1143       C  
ATOM   2396  C   GLY A 308      53.939 111.959   8.886  1.00 39.85           C  
ANISOU 2396  C   GLY A 308     7300   3592   4250   1010   2458   1108       C  
ATOM   2397  O   GLY A 308      52.804 112.284   8.543  1.00 39.36           O  
ANISOU 2397  O   GLY A 308     7288   3477   4190    968   2441   1033       O  
ATOM   2398  N   SER A 309      54.650 112.629   9.794  1.00 39.88           N  
ANISOU 2398  N   SER A 309     7199   3633   4320    926   2445   1167       N  
ATOM   2399  CA  SER A 309      54.109 113.767  10.523  1.00 39.31           C  
ANISOU 2399  CA  SER A 309     7079   3531   4325    777   2409   1138       C  
ATOM   2400  C   SER A 309      55.203 114.801  10.755  1.00 39.74           C  
ANISOU 2400  C   SER A 309     6998   3658   4443    731   2421   1245       C  
ATOM   2401  O   SER A 309      56.395 114.483  10.771  1.00 40.40           O  
ANISOU 2401  O   SER A 309     7019   3817   4516    791   2444   1336       O  
ATOM   2402  CB  SER A 309      53.502 113.337  11.866  1.00 38.74           C  
ANISOU 2402  CB  SER A 309     7057   3395   4269    678   2352   1056       C  
ATOM   2403  OG  SER A 309      52.576 112.279  11.695  1.00 38.46           O  
ANISOU 2403  OG  SER A 309     7144   3294   4176    717   2340    966       O  
ATOM   2404  N   TYR A 310      54.780 116.053  10.936  1.00 41.90           N  
ANISOU 2404  N   TYR A 310     7229   3909   4781    623   2407   1236       N  
ATOM   2405  CA  TYR A 310      55.690 117.135  11.290  1.00 42.18           C  
ANISOU 2405  CA  TYR A 310     7145   3997   4885    548   2407   1326       C  
ATOM   2406  C   TYR A 310      54.937 118.163  12.124  1.00 41.53           C  
ANISOU 2406  C   TYR A 310     7064   3849   4867    397   2365   1267       C  
ATOM   2407  O   TYR A 310      53.733 118.365  11.943  1.00 40.74           O  
ANISOU 2407  O   TYR A 310     7036   3681   4762    374   2358   1184       O  
ATOM   2408  CB  TYR A 310      56.314 117.797  10.049  1.00 42.64           C  
ANISOU 2408  CB  TYR A 310     7131   4120   4949    621   2464   1424       C  
ATOM   2409  CG  TYR A 310      55.355 118.576   9.168  1.00 42.11           C  
ANISOU 2409  CG  TYR A 310     7097   4012   4891    620   2485   1387       C  
ATOM   2410  CD1 TYR A 310      54.824 118.011   8.016  1.00 42.02           C  
ANISOU 2410  CD1 TYR A 310     7155   3997   4813    740   2519   1359       C  
ATOM   2411  CD2 TYR A 310      55.003 119.886   9.474  1.00 41.64           C  
ANISOU 2411  CD2 TYR A 310     7001   3919   4902    502   2472   1383       C  
ATOM   2412  CE1 TYR A 310      53.957 118.722   7.204  1.00 41.79           C  
ANISOU 2412  CE1 TYR A 310     7150   3940   4788    743   2538   1330       C  
ATOM   2413  CE2 TYR A 310      54.134 120.601   8.673  1.00 41.03           C  
ANISOU 2413  CE2 TYR A 310     6952   3808   4831    509   2496   1356       C  
ATOM   2414  CZ  TYR A 310      53.616 120.016   7.538  1.00 41.04           C  
ANISOU 2414  CZ  TYR A 310     7014   3815   4765    630   2529   1331       C  
ATOM   2415  OH  TYR A 310      52.755 120.728   6.736  1.00 40.74           O  
ANISOU 2415  OH  TYR A 310     6998   3751   4728    639   2552   1307       O  
ATOM   2416  N   GLU A 311      55.662 118.815  13.035  1.00 45.10           N  
ANISOU 2416  N   GLU A 311     7438   4324   5375    296   2337   1314       N  
ATOM   2417  CA  GLU A 311      55.046 119.770  13.951  1.00 44.48           C  
ANISOU 2417  CA  GLU A 311     7367   4181   5353    152   2295   1259       C  
ATOM   2418  C   GLU A 311      54.454 120.951  13.192  1.00 43.88           C  
ANISOU 2418  C   GLU A 311     7289   4071   5310    128   2322   1259       C  
ATOM   2419  O   GLU A 311      55.101 121.530  12.316  1.00 44.26           O  
ANISOU 2419  O   GLU A 311     7269   4170   5377    165   2363   1346       O  
ATOM   2420  CB  GLU A 311      56.072 120.268  14.970  1.00 45.35           C  
ANISOU 2420  CB  GLU A 311     7391   4329   5512     52   2260   1318       C  
ATOM   2421  CG  GLU A 311      55.899 119.697  16.368  1.00 45.34           C  
ANISOU 2421  CG  GLU A 311     7426   4298   5502    -15   2203   1255       C  
ATOM   2422  CD  GLU A 311      56.545 120.564  17.434  1.00 45.91           C  
ANISOU 2422  CD  GLU A 311     7431   4382   5631   -149   2158   1286       C  
ATOM   2423  OE1 GLU A 311      55.806 121.205  18.213  1.00 45.41           O  
ANISOU 2423  OE1 GLU A 311     7412   4245   5595   -253   2122   1215       O  
ATOM   2424  OE2 GLU A 311      57.791 120.614  17.484  1.00 46.80           O1+
ANISOU 2424  OE2 GLU A 311     7446   4580   5757   -150   2157   1385       O1+
ATOM   2425  N   ALA A 312      53.227 121.316  13.548  1.00 41.59           N  
ANISOU 2425  N   ALA A 312     7073   3701   5030     67   2302   1166       N  
ATOM   2426  CA  ALA A 312      52.485 122.361  12.862  1.00 41.38           C  
ANISOU 2426  CA  ALA A 312     7059   3636   5028     52   2329   1156       C  
ATOM   2427  C   ALA A 312      51.657 123.150  13.865  1.00 40.95           C  
ANISOU 2427  C   ALA A 312     7045   3502   5011    -70   2293   1086       C  
ATOM   2428  O   ALA A 312      51.262 122.614  14.906  1.00 40.56           O  
ANISOU 2428  O   ALA A 312     7042   3418   4950   -116   2249   1020       O  
ATOM   2429  CB  ALA A 312      51.560 121.775  11.782  1.00 41.02           C  
ANISOU 2429  CB  ALA A 312     7081   3581   4925    159   2360   1110       C  
ATOM   2430  N   PRO A 313      51.386 124.421  13.583  1.00 42.10           N  
ANISOU 2430  N   PRO A 313     7179   3617   5201   -119   2313   1103       N  
ATOM   2431  CA  PRO A 313      50.523 125.210  14.466  1.00 41.46           C  
ANISOU 2431  CA  PRO A 313     7149   3455   5150   -221   2286   1037       C  
ATOM   2432  C   PRO A 313      49.055 124.844  14.298  1.00 40.60           C  
ANISOU 2432  C   PRO A 313     7120   3306   5000   -182   2282    942       C  
ATOM   2433  O   PRO A 313      48.619 124.344  13.259  1.00 40.33           O  
ANISOU 2433  O   PRO A 313     7111   3288   4924    -88   2320    942       O  
ATOM   2434  CB  PRO A 313      50.785 126.652  14.017  1.00 41.94           C  
ANISOU 2434  CB  PRO A 313     7153   3518   5266   -260   2298   1083       C  
ATOM   2435  CG  PRO A 313      51.185 126.523  12.588  1.00 42.44           C  
ANISOU 2435  CG  PRO A 313     7175   3637   5312   -153   2360   1158       C  
ATOM   2436  CD  PRO A 313      51.955 125.234  12.493  1.00 42.62           C  
ANISOU 2436  CD  PRO A 313     7179   3720   5293    -83   2364   1193       C  
ATOM   2437  N   THR A 314      48.290 125.115  15.353  1.00 39.69           N  
ANISOU 2437  N   THR A 314     7042   3142   4894   -257   2232    862       N  
ATOM   2438  CA  THR A 314      46.880 124.757  15.386  1.00 39.05           C  
ANISOU 2438  CA  THR A 314     7029   3031   4777   -233   2221    774       C  
ATOM   2439  C   THR A 314      46.054 125.723  14.539  1.00 38.99           C  
ANISOU 2439  C   THR A 314     7020   3019   4778   -205   2247    764       C  
ATOM   2440  O   THR A 314      46.500 126.816  14.176  1.00 39.42           O  
ANISOU 2440  O   THR A 314     7026   3079   4872   -223   2264    811       O  
ATOM   2441  CB  THR A 314      46.358 124.744  16.825  1.00 38.72           C  
ANISOU 2441  CB  THR A 314     7020   2951   4741   -313   2162    699       C  
ATOM   2442  OG1 THR A 314      45.256 123.833  16.930  1.00 38.16           O  
ANISOU 2442  OG1 THR A 314     7010   2865   4623   -279   2152    630       O  
ATOM   2443  CG2 THR A 314      45.893 126.133  17.247  1.00 38.80           C  
ANISOU 2443  CG2 THR A 314     7021   2933   4787   -375   2142    672       C  
ATOM   2444  N   GLN A 315      44.833 125.297  14.219  1.00 39.82           N  
ANISOU 2444  N   GLN A 315     7178   3113   4842   -162   2252    706       N  
ATOM   2445  CA  GLN A 315      43.910 126.090  13.421  1.00 39.49           C  
ANISOU 2445  CA  GLN A 315     7139   3069   4795   -128   2280    696       C  
ATOM   2446  C   GLN A 315      42.499 125.908  13.962  1.00 38.95           C  
ANISOU 2446  C   GLN A 315     7125   2976   4700   -143   2255    614       C  
ATOM   2447  O   GLN A 315      42.232 125.032  14.790  1.00 38.75           O  
ANISOU 2447  O   GLN A 315     7133   2936   4653   -169   2218    567       O  
ATOM   2448  CB  GLN A 315      43.965 125.705  11.935  1.00 39.40           C  
ANISOU 2448  CB  GLN A 315     7127   3093   4749    -28   2336    742       C  
ATOM   2449  CG  GLN A 315      45.289 126.006  11.244  1.00 40.15           C  
ANISOU 2449  CG  GLN A 315     7159   3227   4870      2   2370    834       C  
ATOM   2450  CD  GLN A 315      45.653 127.479  11.282  1.00 40.87           C  
ANISOU 2450  CD  GLN A 315     7194   3313   5023    -47   2374    871       C  
ATOM   2451  OE1 GLN A 315      44.790 128.349  11.148  1.00 41.24           O  
ANISOU 2451  OE1 GLN A 315     7251   3340   5079    -53   2380    842       O  
ATOM   2452  NE2 GLN A 315      46.936 127.766  11.469  1.00 41.31           N  
ANISOU 2452  NE2 GLN A 315     7191   3387   5119    -81   2373    938       N  
ATOM   2453  N   GLY A 316      41.590 126.754  13.482  1.00 37.23           N  
ANISOU 2453  N   GLY A 316     6910   2755   4481   -124   2276    603       N  
ATOM   2454  CA  GLY A 316      40.188 126.647  13.841  1.00 36.82           C  
ANISOU 2454  CA  GLY A 316     6901   2690   4398   -128   2262    539       C  
ATOM   2455  C   GLY A 316      39.905 127.081  15.270  1.00 36.68           C  
ANISOU 2455  C   GLY A 316     6892   2645   4400   -203   2216    492       C  
ATOM   2456  O   GLY A 316      40.791 127.449  16.040  1.00 36.90           O  
ANISOU 2456  O   GLY A 316     6898   2660   4464   -259   2190    502       O  
ATOM   2457  N   SER A 317      38.619 127.033  15.618  1.00 37.25           N  
ANISOU 2457  N   SER A 317     6998   2712   4444   -202   2208    443       N  
ATOM   2458  CA  SER A 317      38.173 127.365  16.963  1.00 37.47           C  
ANISOU 2458  CA  SER A 317     7040   2718   4477   -259   2169    397       C  
ATOM   2459  C   SER A 317      36.906 126.582  17.274  1.00 36.90           C  
ANISOU 2459  C   SER A 317     7006   2653   4362   -249   2157    351       C  
ATOM   2460  O   SER A 317      36.241 126.057  16.379  1.00 36.72           O  
ANISOU 2460  O   SER A 317     6998   2646   4308   -203   2181    355       O  
ATOM   2461  CB  SER A 317      37.921 128.869  17.127  1.00 37.98           C  
ANISOU 2461  CB  SER A 317     7099   2765   4566   -272   2185    403       C  
ATOM   2462  OG  SER A 317      36.590 129.205  16.768  1.00 37.93           O  
ANISOU 2462  OG  SER A 317     7115   2765   4532   -231   2215    389       O  
ATOM   2463  N   ALA A 318      36.582 126.513  18.564  1.00 37.69           N  
ANISOU 2463  N   ALA A 318     7121   2741   4458   -295   2118    310       N  
ATOM   2464  CA  ALA A 318      35.363 125.872  19.041  1.00 37.25           C  
ANISOU 2464  CA  ALA A 318     7094   2692   4366   -294   2104    271       C  
ATOM   2465  C   ALA A 318      34.360 126.878  19.589  1.00 37.28           C  
ANISOU 2465  C   ALA A 318     7112   2689   4364   -297   2116    257       C  
ATOM   2466  O   ALA A 318      33.401 126.483  20.259  1.00 37.07           O  
ANISOU 2466  O   ALA A 318     7108   2667   4312   -305   2102    229       O  
ATOM   2467  CB  ALA A 318      35.693 124.831  20.113  1.00 37.40           C  
ANISOU 2467  CB  ALA A 318     7123   2708   4377   -334   2054    241       C  
ATOM   2468  N   SER A 319      34.552 128.163  19.313  1.00 38.72           N  
ANISOU 2468  N   SER A 319     7285   2857   4568   -288   2144    279       N  
ATOM   2469  CA  SER A 319      33.745 129.223  19.899  1.00 39.04           C  
ANISOU 2469  CA  SER A 319     7348   2882   4603   -287   2160    268       C  
ATOM   2470  C   SER A 319      32.537 129.552  19.028  1.00 39.39           C  
ANISOU 2470  C   SER A 319     7401   2941   4623   -229   2210    286       C  
ATOM   2471  O   SER A 319      32.565 129.407  17.803  1.00 39.82           O  
ANISOU 2471  O   SER A 319     7439   3015   4676   -188   2240    316       O  
ATOM   2472  CB  SER A 319      34.596 130.477  20.114  1.00 39.73           C  
ANISOU 2472  CB  SER A 319     7430   2939   4726   -313   2164    282       C  
ATOM   2473  OG  SER A 319      35.665 130.535  19.187  1.00 40.12           O  
ANISOU 2473  OG  SER A 319     7445   2993   4807   -308   2174    320       O  
ATOM   2474  N   SER A 320      31.471 130.008  19.685  1.00 36.17           N  
ANISOU 2474  N   SER A 320     7022   2529   4194   -220   2223    272       N  
ATOM   2475  CA  SER A 320      30.215 130.342  19.022  1.00 36.23           C  
ANISOU 2475  CA  SER A 320     7038   2552   4175   -165   2272    293       C  
ATOM   2476  C   SER A 320      29.591 131.530  19.733  1.00 36.53           C  
ANISOU 2476  C   SER A 320     7109   2565   4206   -151   2299    291       C  
ATOM   2477  O   SER A 320      29.308 131.457  20.933  1.00 36.49           O  
ANISOU 2477  O   SER A 320     7131   2546   4188   -179   2277    263       O  
ATOM   2478  CB  SER A 320      29.250 129.153  19.026  1.00 35.92           C  
ANISOU 2478  CB  SER A 320     7004   2542   4101   -162   2258    285       C  
ATOM   2479  OG  SER A 320      27.958 129.546  18.595  1.00 36.05           O  
ANISOU 2479  OG  SER A 320     7028   2577   4091   -114   2302    310       O  
ATOM   2480  N   LEU A 321      29.372 132.614  18.995  1.00 35.77           N  
ANISOU 2480  N   LEU A 321     7014   2461   4115   -104   2351    323       N  
ATOM   2481  CA  LEU A 321      28.757 133.809  19.545  1.00 36.15           C  
ANISOU 2481  CA  LEU A 321     7102   2480   4153    -80   2388    325       C  
ATOM   2482  C   LEU A 321      27.249 133.785  19.306  1.00 36.15           C  
ANISOU 2482  C   LEU A 321     7113   2507   4116    -20   2430    347       C  
ATOM   2483  O   LEU A 321      26.708 132.896  18.642  1.00 35.90           O  
ANISOU 2483  O   LEU A 321     7053   2518   4068     -4   2426    362       O  
ATOM   2484  CB  LEU A 321      29.390 135.063  18.941  1.00 36.61           C  
ANISOU 2484  CB  LEU A 321     7161   2510   4240    -63   2422    350       C  
ATOM   2485  CG  LEU A 321      30.782 135.452  19.447  1.00 36.83           C  
ANISOU 2485  CG  LEU A 321     7188   2502   4304   -129   2384    334       C  
ATOM   2486  CD1 LEU A 321      31.322 136.629  18.652  1.00 37.34           C  
ANISOU 2486  CD1 LEU A 321     7246   2541   4399   -110   2422    369       C  
ATOM   2487  CD2 LEU A 321      30.739 135.778  20.931  1.00 36.99           C  
ANISOU 2487  CD2 LEU A 321     7258   2487   4311   -171   2357    296       C  
ATOM   2488  N   VAL A 322      26.558 134.778  19.861  1.00 34.67           N  
ANISOU 2488  N   VAL A 322     6968   2294   3912     13   2469    352       N  
ATOM   2489  CA  VAL A 322      25.113 134.910  19.732  1.00 34.80           C  
ANISOU 2489  CA  VAL A 322     6992   2336   3893     77   2512    382       C  
ATOM   2490  C   VAL A 322      24.811 136.253  19.084  1.00 35.31           C  
ANISOU 2490  C   VAL A 322     7072   2386   3959    147   2578    418       C  
ATOM   2491  O   VAL A 322      25.434 137.267  19.419  1.00 35.68           O  
ANISOU 2491  O   VAL A 322     7156   2381   4020    138   2594    407       O  
ATOM   2492  CB  VAL A 322      24.409 134.790  21.101  1.00 34.82           C  
ANISOU 2492  CB  VAL A 322     7038   2326   3867     68   2505    361       C  
ATOM   2493  CG1 VAL A 322      22.918 134.586  20.916  1.00 34.90           C  
ANISOU 2493  CG1 VAL A 322     7035   2382   3843    126   2536    401       C  
ATOM   2494  CG2 VAL A 322      25.011 133.652  21.912  1.00 34.39           C  
ANISOU 2494  CG2 VAL A 322     6976   2272   3819     -8   2437    318       C  
ATOM   2495  N   ASN A 323      23.864 136.258  18.149  1.00 35.40           N  
ANISOU 2495  N   ASN A 323     7052   2445   3952    213   2612    465       N  
ATOM   2496  CA  ASN A 323      23.432 137.490  17.497  1.00 35.92           C  
ANISOU 2496  CA  ASN A 323     7127   2505   4016    292   2677    506       C  
ATOM   2497  C   ASN A 323      22.472 138.220  18.428  1.00 36.32           C  
ANISOU 2497  C   ASN A 323     7231   2531   4038    337   2715    512       C  
ATOM   2498  O   ASN A 323      21.348 137.763  18.656  1.00 36.28           O  
ANISOU 2498  O   ASN A 323     7210   2573   4003    367   2715    534       O  
ATOM   2499  CB  ASN A 323      22.776 137.186  16.153  1.00 35.91           C  
ANISOU 2499  CB  ASN A 323     7063   2579   4002    348   2691    558       C  
ATOM   2500  CG  ASN A 323      22.645 138.418  15.273  1.00 36.43           C  
ANISOU 2500  CG  ASN A 323     7127   2639   4075    427   2752    601       C  
ATOM   2501  OD1 ASN A 323      22.405 139.525  15.758  1.00 36.90           O  
ANISOU 2501  OD1 ASN A 323     7237   2650   4133    465   2797    606       O  
ATOM   2502  ND2 ASN A 323      22.810 138.230  13.969  1.00 36.40           N  
ANISOU 2502  ND2 ASN A 323     7069   2684   4076    454   2755    634       N  
ATOM   2503  N   GLY A 324      22.908 139.368  18.952  1.00 36.77           N  
ANISOU 2503  N   GLY A 324     7352   2519   4101    342   2748    495       N  
ATOM   2504  CA  GLY A 324      22.129 140.055  19.967  1.00 37.21           C  
ANISOU 2504  CA  GLY A 324     7475   2538   4123    382   2786    493       C  
ATOM   2505  C   GLY A 324      20.808 140.607  19.470  1.00 37.62           C  
ANISOU 2505  C   GLY A 324     7519   2625   4151    491   2845    553       C  
ATOM   2506  O   GLY A 324      19.834 140.664  20.225  1.00 37.83           O  
ANISOU 2506  O   GLY A 324     7571   2657   4145    532   2862    565       O  
ATOM   2507  N   VAL A 325      20.746 141.017  18.204  1.00 37.79           N  
ANISOU 2507  N   VAL A 325     7496   2675   4187    542   2872    596       N  
ATOM   2508  CA  VAL A 325      19.527 141.657  17.721  1.00 38.28           C  
ANISOU 2508  CA  VAL A 325     7543   2776   4226    650   2923    658       C  
ATOM   2509  C   VAL A 325      18.471 140.621  17.337  1.00 38.00           C  
ANISOU 2509  C   VAL A 325     7418   2854   4166    667   2886    698       C  
ATOM   2510  O   VAL A 325      17.270 140.881  17.471  1.00 38.38           O  
ANISOU 2510  O   VAL A 325     7448   2951   4183    739   2907    744       O  
ATOM   2511  CB  VAL A 325      19.857 142.617  16.561  1.00 38.68           C  
ANISOU 2511  CB  VAL A 325     7584   2815   4298    704   2970    691       C  
ATOM   2512  CG1 VAL A 325      21.362 142.699  16.357  1.00 38.50           C  
ANISOU 2512  CG1 VAL A 325     7575   2739   4313    626   2953    650       C  
ATOM   2513  CG2 VAL A 325      19.156 142.201  15.281  1.00 38.61           C  
ANISOU 2513  CG2 VAL A 325     7476   2912   4281    758   2960    751       C  
ATOM   2514  N   VAL A 326      18.884 139.441  16.870  1.00 37.41           N  
ANISOU 2514  N   VAL A 326     7285   2829   4100    600   2829    683       N  
ATOM   2515  CA  VAL A 326      17.923 138.361  16.659  1.00 37.19           C  
ANISOU 2515  CA  VAL A 326     7179   2910   4040    595   2788    711       C  
ATOM   2516  C   VAL A 326      17.460 137.805  17.998  1.00 37.05           C  
ANISOU 2516  C   VAL A 326     7189   2886   4004    560   2765    689       C  
ATOM   2517  O   VAL A 326      16.276 137.500  18.189  1.00 37.24           O  
ANISOU 2517  O   VAL A 326     7167   2989   3993    592   2760    729       O  
ATOM   2518  CB  VAL A 326      18.535 137.261  15.771  1.00 36.67           C  
ANISOU 2518  CB  VAL A 326     7060   2891   3983    535   2740    697       C  
ATOM   2519  CG1 VAL A 326      17.604 136.064  15.685  1.00 36.49           C  
ANISOU 2519  CG1 VAL A 326     6971   2973   3921    511   2696    716       C  
ATOM   2520  CG2 VAL A 326      18.833 137.802  14.384  1.00 36.88           C  
ANISOU 2520  CG2 VAL A 326     7052   2940   4019    584   2765    730       C  
ATOM   2521  N   ARG A 327      18.387 137.684  18.949  1.00 38.09           N  
ANISOU 2521  N   ARG A 327     7388   2930   4156    494   2750    628       N  
ATOM   2522  CA  ARG A 327      18.071 137.130  20.262  1.00 37.96           C  
ANISOU 2522  CA  ARG A 327     7400   2901   4122    458   2727    603       C  
ATOM   2523  C   ARG A 327      17.049 137.986  21.000  1.00 38.55           C  
ANISOU 2523  C   ARG A 327     7512   2968   4168    538   2775    635       C  
ATOM   2524  O   ARG A 327      16.163 137.458  21.684  1.00 38.59           O  
ANISOU 2524  O   ARG A 327     7495   3022   4144    544   2761    654       O  
ATOM   2525  CB  ARG A 327      19.365 136.996  21.064  1.00 37.66           C  
ANISOU 2525  CB  ARG A 327     7425   2774   4109    377   2701    533       C  
ATOM   2526  CG  ARG A 327      19.235 136.536  22.500  1.00 37.55           C  
ANISOU 2526  CG  ARG A 327     7454   2735   4078    339   2678    500       C  
ATOM   2527  CD  ARG A 327      20.629 136.238  23.018  1.00 37.21           C  
ANISOU 2527  CD  ARG A 327     7444   2633   4060    250   2635    434       C  
ATOM   2528  NE  ARG A 327      20.765 136.311  24.467  1.00 37.30           N  
ANISOU 2528  NE  ARG A 327     7523   2597   4054    223   2626    396       N  
ATOM   2529  CZ  ARG A 327      21.939 136.328  25.089  1.00 37.19           C  
ANISOU 2529  CZ  ARG A 327     7541   2537   4053    153   2588    343       C  
ATOM   2530  NH1 ARG A 327      23.060 136.285  24.382  1.00 36.99           N1+
ANISOU 2530  NH1 ARG A 327     7484   2506   4064    107   2559    326       N1+
ATOM   2531  NH2 ARG A 327      21.995 136.396  26.412  1.00 37.34           N  
ANISOU 2531  NH2 ARG A 327     7618   2520   4047    132   2578    312       N  
ATOM   2532  N   LEU A 328      17.147 139.311  20.868  1.00 37.78           N  
ANISOU 2532  N   LEU A 328     7470   2811   4073    604   2835    645       N  
ATOM   2533  CA  LEU A 328      16.187 140.192  21.527  1.00 38.44           C  
ANISOU 2533  CA  LEU A 328     7598   2880   4126    693   2887    678       C  
ATOM   2534  C   LEU A 328      14.820 140.124  20.858  1.00 38.74           C  
ANISOU 2534  C   LEU A 328     7543   3038   4139    771   2894    758       C  
ATOM   2535  O   LEU A 328      13.790 140.085  21.542  1.00 39.06           O  
ANISOU 2535  O   LEU A 328     7572   3122   4147    816   2901    792       O  
ATOM   2536  CB  LEU A 328      16.711 141.628  21.537  1.00 38.99           C  
ANISOU 2536  CB  LEU A 328     7764   2849   4204    739   2953    664       C  
ATOM   2537  CG  LEU A 328      17.901 141.901  22.460  1.00 38.94           C  
ANISOU 2537  CG  LEU A 328     7857   2737   4202    665   2951    586       C  
ATOM   2538  CD1 LEU A 328      18.394 143.332  22.302  1.00 39.59           C  
ANISOU 2538  CD1 LEU A 328     8021   2738   4283    702   3016    576       C  
ATOM   2539  CD2 LEU A 328      17.535 141.609  23.907  1.00 38.99           C  
ANISOU 2539  CD2 LEU A 328     7920   2720   4175    654   2943    561       C  
ATOM   2540  N   LEU A 329      14.788 140.108  19.525  1.00 38.71           N  
ANISOU 2540  N   LEU A 329     7466   3097   4144    789   2889    791       N  
ATOM   2541  CA  LEU A 329      13.534 140.049  18.784  1.00 39.05           C  
ANISOU 2541  CA  LEU A 329     7410   3271   4156    857   2889    866       C  
ATOM   2542  C   LEU A 329      12.937 138.649  18.728  1.00 38.68           C  
ANISOU 2542  C   LEU A 329     7269   3342   4085    798   2827    879       C  
ATOM   2543  O   LEU A 329      11.839 138.485  18.186  1.00 39.01           O  
ANISOU 2543  O   LEU A 329     7221   3509   4093    842   2821    941       O  
ATOM   2544  CB  LEU A 329      13.740 140.583  17.363  1.00 39.21           C  
ANISOU 2544  CB  LEU A 329     7391   3318   4190    899   2908    896       C  
ATOM   2545  CG  LEU A 329      13.948 142.095  17.258  1.00 39.82           C  
ANISOU 2545  CG  LEU A 329     7544   3304   4282    982   2980    909       C  
ATOM   2546  CD1 LEU A 329      14.597 142.464  15.938  1.00 39.80           C  
ANISOU 2546  CD1 LEU A 329     7517   3301   4306    993   2992    918       C  
ATOM   2547  CD2 LEU A 329      12.629 142.836  17.428  1.00 40.59           C  
ANISOU 2547  CD2 LEU A 329     7625   3453   4344   1094   3021    976       C  
ATOM   2548  N   SER A 330      13.623 137.642  19.271  1.00 38.07           N  
ANISOU 2548  N   SER A 330     7211   3231   4022    700   2782    824       N  
ATOM   2549  CA  SER A 330      13.084 136.288  19.320  1.00 37.77           C  
ANISOU 2549  CA  SER A 330     7099   3291   3961    638   2727    833       C  
ATOM   2550  C   SER A 330      13.042 135.787  20.759  1.00 37.61           C  
ANISOU 2550  C   SER A 330     7122   3230   3937    595   2710    803       C  
ATOM   2551  O   SER A 330      13.516 134.685  21.057  1.00 37.09           O  
ANISOU 2551  O   SER A 330     7055   3157   3880    506   2663    764       O  
ATOM   2552  CB  SER A 330      13.916 135.342  18.454  1.00 37.20           C  
ANISOU 2552  CB  SER A 330     7001   3229   3906    558   2683    799       C  
ATOM   2553  OG  SER A 330      15.220 135.180  18.984  1.00 36.73           O  
ANISOU 2553  OG  SER A 330     7017   3054   3884    492   2670    729       O  
ATOM   2554  N   LYS A 331      12.471 136.595  21.651  1.00 40.38           N  
ANISOU 2554  N   LYS A 331     7516   3554   4273    664   2751    823       N  
ATOM   2555  CA  LYS A 331      12.433 136.247  23.071  1.00 40.31           C  
ANISOU 2555  CA  LYS A 331     7557   3502   4257    636   2742    797       C  
ATOM   2556  C   LYS A 331      11.690 134.947  23.368  1.00 40.14           C  
ANISOU 2556  C   LYS A 331     7456   3583   4213    584   2694    821       C  
ATOM   2557  O   LYS A 331      12.216 134.132  24.146  1.00 39.71           O  
ANISOU 2557  O   LYS A 331     7433   3486   4169    507   2659    775       O  
ATOM   2558  CB  LYS A 331      11.829 137.413  23.859  1.00 41.00           C  
ANISOU 2558  CB  LYS A 331     7704   3551   4323    736   2801    824       C  
ATOM   2559  CG  LYS A 331      11.810 137.217  25.364  1.00 41.03           C  
ANISOU 2559  CG  LYS A 331     7774   3501   4313    722   2801    797       C  
ATOM   2560  CD  LYS A 331      10.818 138.170  26.006  1.00 41.84           C  
ANISOU 2560  CD  LYS A 331     7905   3609   4381    837   2856    847       C  
ATOM   2561  CE  LYS A 331      11.141 138.425  27.465  1.00 41.97           C  
ANISOU 2561  CE  LYS A 331     8037   3524   4386    840   2875    805       C  
ATOM   2562  NZ  LYS A 331      10.204 139.432  28.033  1.00 42.85           N1+
ANISOU 2562  NZ  LYS A 331     8188   3631   4461    962   2935    854       N1+
ATOM   2563  N   PRO A 332      10.494 134.685  22.822  1.00 38.33           N  
ANISOU 2563  N   PRO A 332     7124   3489   3950    616   2689    892       N  
ATOM   2564  CA  PRO A 332       9.756 133.473  23.225  1.00 38.28           C  
ANISOU 2564  CA  PRO A 332     7048   3576   3920    560   2647    919       C  
ATOM   2565  C   PRO A 332      10.446 132.168  22.866  1.00 37.64           C  
ANISOU 2565  C   PRO A 332     6954   3491   3855    445   2591    875       C  
ATOM   2566  O   PRO A 332       9.970 131.107  23.287  1.00 37.58           O  
ANISOU 2566  O   PRO A 332     6906   3540   3834    386   2557    889       O  
ATOM   2567  CB  PRO A 332       8.421 133.603  22.479  1.00 38.90           C  
ANISOU 2567  CB  PRO A 332     7018   3805   3958    617   2656   1006       C  
ATOM   2568  CG  PRO A 332       8.311 135.021  22.137  1.00 39.36           C  
ANISOU 2568  CG  PRO A 332     7104   3836   4017    725   2711   1028       C  
ATOM   2569  CD  PRO A 332       9.695 135.505  21.893  1.00 38.91           C  
ANISOU 2569  CD  PRO A 332     7139   3641   4002    706   2722    957       C  
ATOM   2570  N   TRP A 333      11.536 132.203  22.103  1.00 38.41           N  
ANISOU 2570  N   TRP A 333     7086   3524   3983    412   2582    826       N  
ATOM   2571  CA  TRP A 333      12.264 130.997  21.739  1.00 37.84           C  
ANISOU 2571  CA  TRP A 333     7012   3439   3926    310   2532    782       C  
ATOM   2572  C   TRP A 333      13.506 130.780  22.594  1.00 37.32           C  
ANISOU 2572  C   TRP A 333     7034   3248   3899    254   2515    706       C  
ATOM   2573  O   TRP A 333      14.298 129.879  22.301  1.00 36.85           O  
ANISOU 2573  O   TRP A 333     6983   3161   3858    177   2475    664       O  
ATOM   2574  CB  TRP A 333      12.636 131.034  20.255  1.00 37.75           C  
ANISOU 2574  CB  TRP A 333     6972   3455   3917    311   2529    783       C  
ATOM   2575  CG  TRP A 333      11.474 130.726  19.358  1.00 38.19           C  
ANISOU 2575  CG  TRP A 333     6932   3652   3926    328   2524    851       C  
ATOM   2576  CD1 TRP A 333      11.059 129.491  18.952  1.00 38.17           C  
ANISOU 2576  CD1 TRP A 333     6880   3726   3896    255   2484    864       C  
ATOM   2577  CD2 TRP A 333      10.569 131.668  18.765  1.00 38.79           C  
ANISOU 2577  CD2 TRP A 333     6952   3811   3976    422   2561    915       C  
ATOM   2578  NE1 TRP A 333       9.957 129.604  18.141  1.00 38.73           N  
ANISOU 2578  NE1 TRP A 333     6866   3929   3921    293   2493    934       N  
ATOM   2579  CE2 TRP A 333       9.634 130.930  18.012  1.00 39.11           C  
ANISOU 2579  CE2 TRP A 333     6903   3987   3969    398   2538    967       C  
ATOM   2580  CE3 TRP A 333      10.459 133.061  18.797  1.00 39.15           C  
ANISOU 2580  CE3 TRP A 333     7019   3828   4030    522   2611    936       C  
ATOM   2581  CZ2 TRP A 333       8.606 131.538  17.295  1.00 39.75           C  
ANISOU 2581  CZ2 TRP A 333     6907   4185   4013    473   2560   1039       C  
ATOM   2582  CZ3 TRP A 333       9.436 133.663  18.085  1.00 39.78           C  
ANISOU 2582  CZ3 TRP A 333     7026   4015   4075    601   2635   1007       C  
ATOM   2583  CH2 TRP A 333       8.524 132.902  17.344  1.00 40.07           C  
ANISOU 2583  CH2 TRP A 333     6964   4196   4065    576   2608   1058       C  
ATOM   2584  N   ASP A 334      13.691 131.577  23.648  1.00 39.38           N  
ANISOU 2584  N   ASP A 334     7361   3434   4167    293   2544    689       N  
ATOM   2585  CA  ASP A 334      14.799 131.358  24.568  1.00 38.97           C  
ANISOU 2585  CA  ASP A 334     7388   3276   4143    237   2526    619       C  
ATOM   2586  C   ASP A 334      14.601 130.129  25.444  1.00 38.75           C  
ANISOU 2586  C   ASP A 334     7347   3266   4108    170   2482    609       C  
ATOM   2587  O   ASP A 334      15.548 129.718  26.123  1.00 38.37           O  
ANISOU 2587  O   ASP A 334     7352   3145   4083    114   2455    552       O  
ATOM   2588  CB  ASP A 334      15.006 132.590  25.452  1.00 39.28           C  
ANISOU 2588  CB  ASP A 334     7512   3232   4182    297   2573    603       C  
ATOM   2589  CG  ASP A 334      15.466 133.797  24.666  1.00 39.49           C  
ANISOU 2589  CG  ASP A 334     7570   3213   4222    349   2615    601       C  
ATOM   2590  OD1 ASP A 334      15.198 134.935  25.107  1.00 39.98           O  
ANISOU 2590  OD1 ASP A 334     7687   3233   4271    422   2666    613       O  
ATOM   2591  OD2 ASP A 334      16.095 133.607  23.603  1.00 39.27           O1+
ANISOU 2591  OD2 ASP A 334     7514   3190   4216    320   2599    589       O1+
ATOM   2592  N   VAL A 335      13.404 129.542  25.448  1.00 38.82           N  
ANISOU 2592  N   VAL A 335     7285   3376   4087    174   2474    667       N  
ATOM   2593  CA  VAL A 335      13.116 128.338  26.218  1.00 38.68           C  
ANISOU 2593  CA  VAL A 335     7249   3384   4065    108   2434    667       C  
ATOM   2594  C   VAL A 335      12.935 127.116  25.337  1.00 38.52           C  
ANISOU 2594  C   VAL A 335     7169   3427   4040     34   2391    679       C  
ATOM   2595  O   VAL A 335      12.698 126.019  25.863  1.00 38.45           O  
ANISOU 2595  O   VAL A 335     7144   3435   4028    -31   2356    681       O  
ATOM   2596  CB  VAL A 335      11.884 128.531  27.120  1.00 39.22           C  
ANISOU 2596  CB  VAL A 335     7287   3514   4099    161   2458    727       C  
ATOM   2597  CG1 VAL A 335      12.222 129.440  28.294  1.00 39.34           C  
ANISOU 2597  CG1 VAL A 335     7388   3443   4116    215   2492    700       C  
ATOM   2598  CG2 VAL A 335      10.722 129.097  26.317  1.00 39.78           C  
ANISOU 2598  CG2 VAL A 335     7281   3694   4139    231   2488    804       C  
ATOM   2599  N   VAL A 336      13.031 127.264  24.020  1.00 39.51           N  
ANISOU 2599  N   VAL A 336     7266   3584   4162     40   2394    688       N  
ATOM   2600  CA  VAL A 336      12.941 126.137  23.100  1.00 39.47           C  
ANISOU 2600  CA  VAL A 336     7221   3629   4146    -31   2357    693       C  
ATOM   2601  C   VAL A 336      14.352 125.603  22.888  1.00 38.98           C  
ANISOU 2601  C   VAL A 336     7217   3472   4120    -91   2325    619       C  
ATOM   2602  O   VAL A 336      15.211 126.298  22.339  1.00 38.93           O  
ANISOU 2602  O   VAL A 336     7242   3416   4135    -61   2341    589       O  
ATOM   2603  CB  VAL A 336      12.299 126.544  21.768  1.00 39.75           C  
ANISOU 2603  CB  VAL A 336     7198   3755   4151     11   2377    742       C  
ATOM   2604  CG1 VAL A 336      11.997 125.313  20.918  1.00 39.83           C  
ANISOU 2604  CG1 VAL A 336     7173   3827   4135    -68   2340    754       C  
ATOM   2605  CG2 VAL A 336      11.039 127.363  22.004  1.00 40.34           C  
ANISOU 2605  CG2 VAL A 336     7216   3918   4195     92   2415    815       C  
ATOM   2606  N   THR A 337      14.597 124.368  23.335  1.00 41.30           N  
ANISOU 2606  N   THR A 337     7525   3743   4423   -173   2279    592       N  
ATOM   2607  CA  THR A 337      15.882 123.734  23.069  1.00 40.83           C  
ANISOU 2607  CA  THR A 337     7512   3606   4394   -227   2244    528       C  
ATOM   2608  C   THR A 337      16.106 123.531  21.577  1.00 40.97           C  
ANISOU 2608  C   THR A 337     7518   3649   4398   -235   2242    530       C  
ATOM   2609  O   THR A 337      17.252 123.385  21.142  1.00 40.71           O  
ANISOU 2609  O   THR A 337     7522   3556   4390   -249   2227    484       O  
ATOM   2610  CB  THR A 337      15.977 122.391  23.794  1.00 40.65           C  
ANISOU 2610  CB  THR A 337     7504   3561   4380   -308   2194    505       C  
ATOM   2611  OG1 THR A 337      15.129 122.415  24.949  1.00 40.69           O  
ANISOU 2611  OG1 THR A 337     7491   3594   4375   -299   2202    538       O  
ATOM   2612  CG2 THR A 337      17.413 122.126  24.232  1.00 40.28           C  
ANISOU 2612  CG2 THR A 337     7511   3420   4374   -334   2165    434       C  
ATOM   2613  N   GLY A 338      15.033 123.527  20.786  1.00 40.19           N  
ANISOU 2613  N   GLY A 338     7368   3647   4257   -221   2256    586       N  
ATOM   2614  CA  GLY A 338      15.146 123.372  19.349  1.00 40.32           C  
ANISOU 2614  CA  GLY A 338     7372   3699   4250   -222   2255    590       C  
ATOM   2615  C   GLY A 338      15.880 124.502  18.661  1.00 40.19           C  
ANISOU 2615  C   GLY A 338     7367   3653   4249   -149   2293    580       C  
ATOM   2616  O   GLY A 338      16.286 124.351  17.507  1.00 40.33           O  
ANISOU 2616  O   GLY A 338     7387   3681   4254   -147   2291    572       O  
ATOM   2617  N   VAL A 339      16.070 125.628  19.341  1.00 39.28           N  
ANISOU 2617  N   VAL A 339     7262   3501   4162    -90   2323    578       N  
ATOM   2618  CA  VAL A 339      16.770 126.757  18.739  1.00 39.04           C  
ANISOU 2618  CA  VAL A 339     7245   3436   4153    -27   2358    570       C  
ATOM   2619  C   VAL A 339      17.982 127.120  19.593  1.00 38.83           C  
ANISOU 2619  C   VAL A 339     7277   3300   4175    -38   2354    516       C  
ATOM   2620  O   VAL A 339      19.026 127.525  19.066  1.00 38.80           O  
ANISOU 2620  O   VAL A 339     7296   3248   4198    -27   2361    491       O  
ATOM   2621  CB  VAL A 339      15.829 127.967  18.541  1.00 39.43           C  
ANISOU 2621  CB  VAL A 339     7254   3545   4183     62   2405    626       C  
ATOM   2622  CG1 VAL A 339      14.407 127.609  18.942  1.00 39.83           C  
ANISOU 2622  CG1 VAL A 339     7252   3690   4194     61   2402    679       C  
ATOM   2623  CG2 VAL A 339      16.323 129.196  19.290  1.00 39.41           C  
ANISOU 2623  CG2 VAL A 339     7296   3463   4214    114   2440    610       C  
ATOM   2624  N   THR A 340      17.863 126.970  20.918  1.00 38.81           N  
ANISOU 2624  N   THR A 340     7298   3266   4182    -60   2341    500       N  
ATOM   2625  CA  THR A 340      18.981 127.315  21.790  1.00 38.53           C  
ANISOU 2625  CA  THR A 340     7316   3138   4184    -73   2334    447       C  
ATOM   2626  C   THR A 340      20.150 126.355  21.633  1.00 38.13           C  
ANISOU 2626  C   THR A 340     7283   3045   4159   -138   2286    398       C  
ATOM   2627  O   THR A 340      21.286 126.727  21.945  1.00 37.95           O  
ANISOU 2627  O   THR A 340     7289   2962   4167   -145   2279    358       O  
ATOM   2628  CB  THR A 340      18.544 127.350  23.259  1.00 38.59           C  
ANISOU 2628  CB  THR A 340     7346   3128   4187    -77   2332    443       C  
ATOM   2629  OG1 THR A 340      18.078 126.054  23.656  1.00 38.65           O  
ANISOU 2629  OG1 THR A 340     7335   3168   4184   -135   2292    446       O  
ATOM   2630  CG2 THR A 340      17.442 128.381  23.471  1.00 39.05           C  
ANISOU 2630  CG2 THR A 340     7393   3224   4220     -1   2383    494       C  
ATOM   2631  N   GLY A 341      19.900 125.134  21.156  1.00 38.20           N  
ANISOU 2631  N   GLY A 341     7275   3088   4152   -185   2254    401       N  
ATOM   2632  CA  GLY A 341      20.976 124.182  20.954  1.00 37.96           C  
ANISOU 2632  CA  GLY A 341     7265   3017   4142   -236   2210    357       C  
ATOM   2633  C   GLY A 341      21.824 124.463  19.732  1.00 38.31           C  
ANISOU 2633  C   GLY A 341     7310   3051   4195   -213   2223    353       C  
ATOM   2634  O   GLY A 341      22.983 124.042  19.686  1.00 38.26           O  
ANISOU 2634  O   GLY A 341     7320   3003   4214   -236   2195    316       O  
ATOM   2635  N   ILE A 342      21.277 125.171  18.746  1.00 36.97           N  
ANISOU 2635  N   ILE A 342     7116   2927   4004   -162   2264    394       N  
ATOM   2636  CA  ILE A 342      22.011 125.447  17.515  1.00 36.74           C  
ANISOU 2636  CA  ILE A 342     7085   2896   3979   -132   2281    398       C  
ATOM   2637  C   ILE A 342      23.176 126.378  17.825  1.00 36.56           C  
ANISOU 2637  C   ILE A 342     7076   2814   4003   -112   2292    375       C  
ATOM   2638  O   ILE A 342      22.982 127.516  18.266  1.00 36.85           O  
ANISOU 2638  O   ILE A 342     7113   2837   4050    -76   2324    385       O  
ATOM   2639  CB  ILE A 342      21.090 126.053  16.447  1.00 36.90           C  
ANISOU 2639  CB  ILE A 342     7069   2991   3962    -75   2322    450       C  
ATOM   2640  CG1 ILE A 342      19.852 125.174  16.249  1.00 37.34           C  
ANISOU 2640  CG1 ILE A 342     7102   3120   3964   -103   2307    476       C  
ATOM   2641  CG2 ILE A 342      21.841 126.223  15.136  1.00 36.86           C  
ANISOU 2641  CG2 ILE A 342     7062   2989   3955    -42   2339    456       C  
ATOM   2642  CD1 ILE A 342      20.159 123.803  15.693  1.00 37.81           C  
ANISOU 2642  CD1 ILE A 342     7165   3188   4011   -155   2246    440       C  
ATOM   2643  N   ALA A 343      24.393 125.895  17.591  1.00 35.68           N  
ANISOU 2643  N   ALA A 343     6975   2666   3914   -137   2267    345       N  
ATOM   2644  CA  ALA A 343      25.593 126.699  17.760  1.00 35.64           C  
ANISOU 2644  CA  ALA A 343     6972   2618   3949   -127   2273    329       C  
ATOM   2645  C   ALA A 343      26.626 126.236  16.747  1.00 35.58           C  
ANISOU 2645  C   ALA A 343     6960   2607   3950   -124   2266    328       C  
ATOM   2646  O   ALA A 343      26.511 125.152  16.169  1.00 35.52           O  
ANISOU 2646  O   ALA A 343     6962   2616   3918   -137   2249    328       O  
ATOM   2647  CB  ALA A 343      26.145 126.604  19.187  1.00 35.46           C  
ANISOU 2647  CB  ALA A 343     6965   2559   3950   -171   2236    287       C  
ATOM   2648  N   MET A 344      27.642 127.072  16.539  1.00 35.12           N  
ANISOU 2648  N   MET A 344     6891   2527   3926   -106   2281    332       N  
ATOM   2649  CA  MET A 344      28.675 126.783  15.551  1.00 35.14           C  
ANISOU 2649  CA  MET A 344     6884   2528   3938    -92   2284    343       C  
ATOM   2650  C   MET A 344      29.379 125.467  15.873  1.00 34.91           C  
ANISOU 2650  C   MET A 344     6869   2485   3910   -135   2236    312       C  
ATOM   2651  O   MET A 344      29.369 124.991  17.011  1.00 34.73           O  
ANISOU 2651  O   MET A 344     6855   2448   3892   -180   2196    279       O  
ATOM   2652  CB  MET A 344      29.699 127.918  15.492  1.00 35.31           C  
ANISOU 2652  CB  MET A 344     6887   2528   4003    -79   2303    355       C  
ATOM   2653  CG  MET A 344      29.110 129.276  15.153  1.00 35.61           C  
ANISOU 2653  CG  MET A 344     6918   2570   4043    -32   2354    386       C  
ATOM   2654  SD  MET A 344      28.399 129.358  13.499  1.00 35.82           S  
ANISOU 2654  SD  MET A 344     6927   2648   4034     41   2402    436       S  
ATOM   2655  CE  MET A 344      29.861 129.176  12.492  1.00 35.89           C  
ANISOU 2655  CE  MET A 344     6918   2654   4066     57   2408    456       C  
ATOM   2656  N   THR A 345      29.991 124.872  14.850  1.00 32.66           N  
ANISOU 2656  N   THR A 345     6589   2206   3614   -114   2242    326       N  
ATOM   2657  CA  THR A 345      30.714 123.623  15.024  1.00 32.52           C  
ANISOU 2657  CA  THR A 345     6592   2172   3593   -142   2203    302       C  
ATOM   2658  C   THR A 345      32.166 123.895  15.415  1.00 32.53           C  
ANISOU 2658  C   THR A 345     6569   2154   3636   -152   2191    301       C  
ATOM   2659  O   THR A 345      32.652 125.026  15.362  1.00 32.68           O  
ANISOU 2659  O   THR A 345     6559   2171   3686   -140   2213    322       O  
ATOM   2660  CB  THR A 345      30.644 122.782  13.751  1.00 32.66           C  
ANISOU 2660  CB  THR A 345     6640   2202   3569   -110   2218    319       C  
ATOM   2661  OG1 THR A 345      31.229 123.504  12.662  1.00 32.88           O  
ANISOU 2661  OG1 THR A 345     6648   2246   3601    -54   2263    361       O  
ATOM   2662  CG2 THR A 345      29.197 122.445  13.413  1.00 32.73           C  
ANISOU 2662  CG2 THR A 345     6654   2252   3532   -109   2210    313       C  
ATOM   2663  N   ASP A 346      32.860 122.828  15.805  1.00 32.90           N  
ANISOU 2663  N   ASP A 346     6630   2187   3683   -176   2155    280       N  
ATOM   2664  CA  ASP A 346      34.209 122.902  16.361  1.00 32.93           C  
ANISOU 2664  CA  ASP A 346     6612   2178   3722   -194   2136    282       C  
ATOM   2665  C   ASP A 346      35.209 122.450  15.303  1.00 33.12           C  
ANISOU 2665  C   ASP A 346     6640   2204   3743   -153   2159    316       C  
ATOM   2666  O   ASP A 346      35.239 121.271  14.937  1.00 33.12           O  
ANISOU 2666  O   ASP A 346     6677   2196   3710   -139   2150    307       O  
ATOM   2667  CB  ASP A 346      34.304 122.044  17.623  1.00 32.73           C  
ANISOU 2667  CB  ASP A 346     6597   2142   3696   -243   2085    243       C  
ATOM   2668  CG  ASP A 346      35.718 121.932  18.162  1.00 32.81           C  
ANISOU 2668  CG  ASP A 346     6588   2143   3736   -262   2066    251       C  
ATOM   2669  OD1 ASP A 346      36.556 122.799  17.846  1.00 33.03           O  
ANISOU 2669  OD1 ASP A 346     6586   2171   3793   -254   2087    284       O  
ATOM   2670  OD2 ASP A 346      35.982 120.973  18.917  1.00 32.70           O1+
ANISOU 2670  OD2 ASP A 346     6588   2122   3714   -286   2030    228       O1+
ATOM   2671  N   THR A 347      36.040 123.380  14.830  1.00 33.09           N  
ANISOU 2671  N   THR A 347     6599   2206   3769   -132   2188    356       N  
ATOM   2672  CA  THR A 347      36.971 123.119  13.738  1.00 33.35           C  
ANISOU 2672  CA  THR A 347     6628   2247   3796    -81   2221    402       C  
ATOM   2673  C   THR A 347      38.423 123.020  14.193  1.00 33.51           C  
ANISOU 2673  C   THR A 347     6621   2262   3851    -99   2208    426       C  
ATOM   2674  O   THR A 347      39.325 123.024  13.349  1.00 33.81           O  
ANISOU 2674  O   THR A 347     6642   2313   3891    -56   2241    477       O  
ATOM   2675  CB  THR A 347      36.840 124.198  12.659  1.00 33.59           C  
ANISOU 2675  CB  THR A 347     6632   2299   3833    -34   2272    446       C  
ATOM   2676  OG1 THR A 347      37.211 125.471  13.204  1.00 33.72           O  
ANISOU 2676  OG1 THR A 347     6604   2308   3900    -65   2272    458       O  
ATOM   2677  CG2 THR A 347      35.410 124.269  12.148  1.00 33.50           C  
ANISOU 2677  CG2 THR A 347     6647   2300   3781    -11   2288    433       C  
ATOM   2678  N   THR A 348      38.674 122.934  15.499  1.00 33.42           N  
ANISOU 2678  N   THR A 348     6601   2236   3861   -160   2164    396       N  
ATOM   2679  CA  THR A 348      40.023 122.682  15.977  1.00 33.61           C  
ANISOU 2679  CA  THR A 348     6603   2257   3910   -180   2151    422       C  
ATOM   2680  C   THR A 348      40.468 121.286  15.543  1.00 33.65           C  
ANISOU 2680  C   THR A 348     6644   2261   3879   -138   2156    432       C  
ATOM   2681  O   THR A 348      39.639 120.456  15.161  1.00 33.48           O  
ANISOU 2681  O   THR A 348     6673   2233   3815   -112   2155    402       O  
ATOM   2682  CB  THR A 348      40.087 122.809  17.500  1.00 33.48           C  
ANISOU 2682  CB  THR A 348     6580   2227   3915   -252   2101    386       C  
ATOM   2683  OG1 THR A 348      39.392 121.713  18.108  1.00 33.16           O  
ANISOU 2683  OG1 THR A 348     6580   2179   3842   -262   2070    337       O  
ATOM   2684  CG2 THR A 348      39.462 124.120  17.958  1.00 33.48           C  
ANISOU 2684  CG2 THR A 348     6564   2220   3936   -286   2097    369       C  
ATOM   2685  N   PRO A 349      41.780 121.012  15.561  1.00 33.65           N  
ANISOU 2685  N   PRO A 349     6624   2269   3893   -129   2164    479       N  
ATOM   2686  CA  PRO A 349      42.243 119.651  15.233  1.00 33.75           C  
ANISOU 2686  CA  PRO A 349     6675   2281   3865    -79   2169    488       C  
ATOM   2687  C   PRO A 349      41.505 118.552  15.979  1.00 33.43           C  
ANISOU 2687  C   PRO A 349     6693   2213   3797   -102   2129    424       C  
ATOM   2688  O   PRO A 349      41.154 117.533  15.373  1.00 33.45           O  
ANISOU 2688  O   PRO A 349     6734   2223   3753    -52   2122    399       O  
ATOM   2689  CB  PRO A 349      43.727 119.701  15.609  1.00 34.10           C  
ANISOU 2689  CB  PRO A 349     6670   2349   3939    -86   2169    543       C  
ATOM   2690  CG  PRO A 349      44.110 121.109  15.338  1.00 34.34           C  
ANISOU 2690  CG  PRO A 349     6645   2387   4014   -110   2196    592       C  
ATOM   2691  CD  PRO A 349      42.911 121.946  15.719  1.00 34.01           C  
ANISOU 2691  CD  PRO A 349     6607   2328   3986   -154   2173    534       C  
ATOM   2692  N   TYR A 350      41.251 118.729  17.278  1.00 35.62           N  
ANISOU 2692  N   TYR A 350     6957   2481   4097   -171   2087    387       N  
ATOM   2693  CA  TYR A 350      40.468 117.738  18.008  1.00 35.30           C  
ANISOU 2693  CA  TYR A 350     6961   2422   4030   -193   2048    329       C  
ATOM   2694  C   TYR A 350      39.025 117.713  17.524  1.00 35.11           C  
ANISOU 2694  C   TYR A 350     6966   2396   3979   -188   2046    289       C  
ATOM   2695  O   TYR A 350      38.410 116.644  17.444  1.00 35.02           O  
ANISOU 2695  O   TYR A 350     7005   2368   3931   -180   2030    256       O  
ATOM   2696  CB  TYR A 350      40.517 118.016  19.511  1.00 35.28           C  
ANISOU 2696  CB  TYR A 350     6931   2420   4053   -261   2005    303       C  
ATOM   2697  CG  TYR A 350      39.579 117.143  20.320  1.00 34.88           C  
ANISOU 2697  CG  TYR A 350     6915   2361   3978   -285   1966    247       C  
ATOM   2698  CD1 TYR A 350      39.951 115.861  20.704  1.00 34.92           C  
ANISOU 2698  CD1 TYR A 350     6955   2352   3962   -275   1950    239       C  
ATOM   2699  CD2 TYR A 350      38.320 117.598  20.697  1.00 34.61           C  
ANISOU 2699  CD2 TYR A 350     6876   2333   3940   -315   1949    209       C  
ATOM   2700  CE1 TYR A 350      39.100 115.057  21.440  1.00 34.71           C  
ANISOU 2700  CE1 TYR A 350     6955   2319   3915   -299   1915    193       C  
ATOM   2701  CE2 TYR A 350      37.460 116.799  21.433  1.00 34.40           C  
ANISOU 2701  CE2 TYR A 350     6874   2305   3893   -337   1916    168       C  
ATOM   2702  CZ  TYR A 350      37.857 115.530  21.802  1.00 34.46           C  
ANISOU 2702  CZ  TYR A 350     6912   2299   3882   -332   1897    159       C  
ATOM   2703  OH  TYR A 350      37.011 114.729  22.534  1.00 34.32           O  
ANISOU 2703  OH  TYR A 350     6914   2279   3845   -357   1864    123       O  
ATOM   2704  N   GLY A 351      38.469 118.881  17.198  1.00 34.07           N  
ANISOU 2704  N   GLY A 351     6804   2278   3863   -194   2064    295       N  
ATOM   2705  CA  GLY A 351      37.071 118.944  16.807  1.00 33.91           C  
ANISOU 2705  CA  GLY A 351     6807   2260   3818   -192   2066    267       C  
ATOM   2706  C   GLY A 351      36.761 118.188  15.530  1.00 34.07           C  
ANISOU 2706  C   GLY A 351     6880   2271   3794   -140   2090    274       C  
ATOM   2707  O   GLY A 351      35.662 117.649  15.376  1.00 33.99           O  
ANISOU 2707  O   GLY A 351     6909   2254   3752   -149   2076    244       O  
ATOM   2708  N   GLN A 352      37.714 118.137  14.598  1.00 32.93           N  
ANISOU 2708  N   GLN A 352     6727   2143   3643    -81   2118    313       N  
ATOM   2709  CA  GLN A 352      37.502 117.435  13.338  1.00 33.16           C  
ANISOU 2709  CA  GLN A 352     6779   2201   3621    -14   2119    304       C  
ATOM   2710  C   GLN A 352      37.978 115.987  13.412  1.00 33.32           C  
ANISOU 2710  C   GLN A 352     6844   2208   3607      9   2091    279       C  
ATOM   2711  O   GLN A 352      37.283 115.080  12.944  1.00 33.42           O  
ANISOU 2711  O   GLN A 352     6907   2217   3573     24   2067    240       O  
ATOM   2712  CB  GLN A 352      38.210 118.178  12.198  1.00 33.46           C  
ANISOU 2712  CB  GLN A 352     6775   2277   3660     53   2164    357       C  
ATOM   2713  CG  GLN A 352      37.791 117.744  10.794  1.00 33.72           C  
ANISOU 2713  CG  GLN A 352     6831   2346   3637    127   2170    348       C  
ATOM   2714  CD  GLN A 352      38.453 116.452  10.346  1.00 34.03           C  
ANISOU 2714  CD  GLN A 352     6912   2387   3630    183   2156    336       C  
ATOM   2715  OE1 GLN A 352      39.646 116.241  10.569  1.00 34.19           O  
ANISOU 2715  OE1 GLN A 352     6916   2408   3665    207   2167    369       O  
ATOM   2716  NE2 GLN A 352      37.676 115.578   9.716  1.00 34.18           N  
ANISOU 2716  NE2 GLN A 352     6987   2408   3591    205   2130    290       N  
ATOM   2717  N   GLN A 353      39.157 115.758  14.000  1.00 33.72           N  
ANISOU 2717  N   GLN A 353     6882   2252   3680     12   2093    305       N  
ATOM   2718  CA  GLN A 353      39.666 114.397  14.145  1.00 33.91           C  
ANISOU 2718  CA  GLN A 353     6952   2261   3673     40   2072    288       C  
ATOM   2719  C   GLN A 353      38.703 113.524  14.940  1.00 33.70           C  
ANISOU 2719  C   GLN A 353     6980   2194   3632    -16   2030    230       C  
ATOM   2720  O   GLN A 353      38.675 112.303  14.758  1.00 33.92           O  
ANISOU 2720  O   GLN A 353     7067   2201   3618     10   2010    202       O  
ATOM   2721  CB  GLN A 353      41.039 114.418  14.820  1.00 34.04           C  
ANISOU 2721  CB  GLN A 353     6931   2284   3718     44   2081    332       C  
ATOM   2722  CG  GLN A 353      41.917 113.222  14.493  1.00 34.43           C  
ANISOU 2722  CG  GLN A 353     7014   2339   3728    116   2082    342       C  
ATOM   2723  CD  GLN A 353      42.511 113.305  13.101  1.00 34.85           C  
ANISOU 2723  CD  GLN A 353     7055   2434   3751    211   2118    381       C  
ATOM   2724  OE1 GLN A 353      42.879 114.383  12.634  1.00 34.91           O  
ANISOU 2724  OE1 GLN A 353     7000   2476   3786    222   2149    429       O  
ATOM   2725  NE2 GLN A 353      42.603 112.165  12.428  1.00 35.19           N  
ANISOU 2725  NE2 GLN A 353     7164   2472   3736    283   2116    363       N  
ATOM   2726  N   ARG A 354      37.908 114.133  15.821  1.00 35.12           N  
ANISOU 2726  N   ARG A 354     7145   2357   3843    -89   2018    215       N  
ATOM   2727  CA  ARG A 354      36.919 113.379  16.583  1.00 34.96           C  
ANISOU 2727  CA  ARG A 354     7168   2303   3811   -144   1981    168       C  
ATOM   2728  C   ARG A 354      35.826 112.830  15.673  1.00 35.10           C  
ANISOU 2728  C   ARG A 354     7227   2327   3783   -133   1964    133       C  
ATOM   2729  O   ARG A 354      35.339 111.713  15.882  1.00 35.21           O  
ANISOU 2729  O   ARG A 354     7296   2313   3771   -153   1931     97       O  
ATOM   2730  CB  ARG A 354      36.318 114.268  17.669  1.00 34.60           C  
ANISOU 2730  CB  ARG A 354     7066   2278   3802   -209   1965    158       C  
ATOM   2731  CG  ARG A 354      35.919 113.541  18.936  1.00 34.45           C  
ANISOU 2731  CG  ARG A 354     7047   2258   3782   -258   1918    123       C  
ATOM   2732  CD  ARG A 354      34.668 114.163  19.524  1.00 34.20           C  
ANISOU 2732  CD  ARG A 354     6986   2248   3760   -306   1901    104       C  
ATOM   2733  NE  ARG A 354      34.747 115.618  19.580  1.00 34.08           N  
ANISOU 2733  NE  ARG A 354     6919   2255   3775   -308   1926    126       N  
ATOM   2734  CZ  ARG A 354      33.686 116.416  19.635  1.00 33.96           C  
ANISOU 2734  CZ  ARG A 354     6885   2256   3763   -326   1932    122       C  
ATOM   2735  NH1 ARG A 354      33.840 117.732  19.686  1.00 33.93           N1+
ANISOU 2735  NH1 ARG A 354     6840   2266   3784   -322   1955    142       N1+
ATOM   2736  NH2 ARG A 354      32.467 115.895  19.630  1.00 33.95           N  
ANISOU 2736  NH2 ARG A 354     6908   2254   3737   -347   1918    103       N  
ATOM   2737  N   VAL A 355      35.418 113.606  14.667  1.00 34.15           N  
ANISOU 2737  N   VAL A 355     7080   2243   3653   -105   1985    146       N  
ATOM   2738  CA  VAL A 355      34.427 113.130  13.706  1.00 34.38           C  
ANISOU 2738  CA  VAL A 355     7142   2287   3633    -93   1966    116       C  
ATOM   2739  C   VAL A 355      35.093 112.315  12.601  1.00 34.82           C  
ANISOU 2739  C   VAL A 355     7242   2349   3640    -17   1967    110       C  
ATOM   2740  O   VAL A 355      34.496 111.365  12.076  1.00 35.13           O  
ANISOU 2740  O   VAL A 355     7340   2376   3630    -15   1935     71       O  
ATOM   2741  CB  VAL A 355      33.635 114.324  13.138  1.00 34.29           C  
ANISOU 2741  CB  VAL A 355     7084   2319   3626    -92   1988    134       C  
ATOM   2742  CG1 VAL A 355      32.801 113.908  11.930  1.00 34.63           C  
ANISOU 2742  CG1 VAL A 355     7152   2394   3612    -66   1971    111       C  
ATOM   2743  CG2 VAL A 355      32.747 114.921  14.213  1.00 33.95           C  
ANISOU 2743  CG2 VAL A 355     7016   2268   3617   -163   1983    132       C  
ATOM   2744  N   PHE A 356      36.335 112.659  12.251  1.00 35.07           N  
ANISOU 2744  N   PHE A 356     7248   2396   3683     46   2003    152       N  
ATOM   2745  CA  PHE A 356      37.045 111.971  11.176  1.00 35.83           C  
ANISOU 2745  CA  PHE A 356     7383   2503   3729    134   2013    156       C  
ATOM   2746  C   PHE A 356      37.178 110.476  11.454  1.00 36.14           C  
ANISOU 2746  C   PHE A 356     7505   2494   3732    137   1981    117       C  
ATOM   2747  O   PHE A 356      36.955 109.649  10.561  1.00 36.89           O  
ANISOU 2747  O   PHE A 356     7668   2582   3768    180   1965     86       O  
ATOM   2748  CB  PHE A 356      38.422 112.611  10.987  1.00 35.92           C  
ANISOU 2748  CB  PHE A 356     7340   2542   3766    193   2059    219       C  
ATOM   2749  CG  PHE A 356      39.310 111.878  10.024  1.00 36.80           C  
ANISOU 2749  CG  PHE A 356     7489   2667   3828    294   2076    233       C  
ATOM   2750  CD1 PHE A 356      40.284 111.007  10.484  1.00 37.10           C  
ANISOU 2750  CD1 PHE A 356     7556   2684   3858    324   2077    244       C  
ATOM   2751  CD2 PHE A 356      39.182 112.068   8.661  1.00 37.47           C  
ANISOU 2751  CD2 PHE A 356     7580   2788   3867    365   2095    241       C  
ATOM   2752  CE1 PHE A 356      41.105 110.332   9.603  1.00 38.01           C  
ANISOU 2752  CE1 PHE A 356     7710   2812   3922    428   2098    262       C  
ATOM   2753  CE2 PHE A 356      40.001 111.394   7.775  1.00 38.35           C  
ANISOU 2753  CE2 PHE A 356     7732   2912   3926    467   2114    255       C  
ATOM   2754  CZ  PHE A 356      40.964 110.526   8.248  1.00 38.60           C  
ANISOU 2754  CZ  PHE A 356     7796   2921   3951    500   2117    267       C  
ATOM   2755  N   LYS A 357      37.526 110.112  12.691  1.00 38.78           N  
ANISOU 2755  N   LYS A 357     7842   2794   4099     93   1970    116       N  
ATOM   2756  CA  LYS A 357      37.817 108.716  13.008  1.00 38.59           C  
ANISOU 2756  CA  LYS A 357     7897   2722   4044    106   1948     89       C  
ATOM   2757  C   LYS A 357      36.598 107.819  12.827  1.00 38.69           C  
ANISOU 2757  C   LYS A 357     7984   2698   4018     61   1902     28       C  
ATOM   2758  O   LYS A 357      36.745 106.639  12.490  1.00 39.12           O  
ANISOU 2758  O   LYS A 357     8125   2714   4025     94   1886     -1       O  
ATOM   2759  CB  LYS A 357      38.342 108.606  14.439  1.00 37.74           C  
ANISOU 2759  CB  LYS A 357     7767   2591   3982     62   1946    105       C  
ATOM   2760  CG  LYS A 357      37.332 109.021  15.497  1.00 36.74           C  
ANISOU 2760  CG  LYS A 357     7615   2449   3894    -38   1921     85       C  
ATOM   2761  CD  LYS A 357      37.971 109.151  16.867  1.00 36.43           C  
ANISOU 2761  CD  LYS A 357     7544   2399   3900    -73   1924    107       C  
ATOM   2762  CE  LYS A 357      36.927 109.465  17.927  1.00 36.04           C  
ANISOU 2762  CE  LYS A 357     7457   2359   3877   -160   1890     81       C  
ATOM   2763  NZ  LYS A 357      35.909 108.383  18.039  1.00 36.28           N1+
ANISOU 2763  NZ  LYS A 357     7537   2370   3877   -196   1847     35       N1+
ATOM   2764  N   GLU A 358      35.395 108.349  13.049  1.00 42.04           N  
ANISOU 2764  N   GLU A 358     8379   3134   4461    -13   1881     11       N  
ATOM   2765  CA  GLU A 358      34.180 107.549  12.955  1.00 42.27           C  
ANISOU 2765  CA  GLU A 358     8466   3136   4458    -70   1833    -40       C  
ATOM   2766  C   GLU A 358      33.562 107.587  11.563  1.00 43.21           C  
ANISOU 2766  C   GLU A 358     8606   3286   4523    -41   1821    -61       C  
ATOM   2767  O   GLU A 358      33.018 106.578  11.101  1.00 43.72           O  
ANISOU 2767  O   GLU A 358     8750   3322   4540    -55   1782   -105       O  
ATOM   2768  CB  GLU A 358      33.151 108.031  13.980  1.00 41.38           C  
ANISOU 2768  CB  GLU A 358     8308   3027   4389   -166   1816    -42       C  
ATOM   2769  CG  GLU A 358      33.600 107.931  15.425  1.00 40.65           C  
ANISOU 2769  CG  GLU A 358     8201   2903   4343   -202   1820    -28       C  
ATOM   2770  CD  GLU A 358      33.672 106.500  15.915  1.00 41.28           C  
ANISOU 2770  CD  GLU A 358     8352   2931   4402   -219   1788    -57       C  
ATOM   2771  OE1 GLU A 358      34.656 106.154  16.604  1.00 41.39           O  
ANISOU 2771  OE1 GLU A 358     8353   2946   4428   -192   1794    -41       O  
ATOM   2772  OE2 GLU A 358      32.743 105.720  15.614  1.00 41.58           O1+
ANISOU 2772  OE2 GLU A 358     8444   2945   4408   -259   1749    -94       O1+
ATOM   2773  N   LYS A 359      33.644 108.728  10.883  1.00 39.05           N  
ANISOU 2773  N   LYS A 359     8015   2819   4004     -2   1854    -28       N  
ATOM   2774  CA  LYS A 359      32.921 108.946   9.637  1.00 39.94           C  
ANISOU 2774  CA  LYS A 359     8132   2974   4069     20   1843    -43       C  
ATOM   2775  C   LYS A 359      33.774 108.750   8.391  1.00 40.76           C  
ANISOU 2775  C   LYS A 359     8272   3095   4122    128   1867    -36       C  
ATOM   2776  O   LYS A 359      33.295 108.179   7.409  1.00 41.69           O  
ANISOU 2776  O   LYS A 359     8449   3217   4175    149   1839    -72       O  
ATOM   2777  CB  LYS A 359      32.325 110.358   9.619  1.00 39.50           C  
ANISOU 2777  CB  LYS A 359     7983   2977   4047      0   1867     -9       C  
ATOM   2778  CG  LYS A 359      31.165 110.561  10.588  1.00 38.84           C  
ANISOU 2778  CG  LYS A 359     7870   2891   3996    -98   1841    -17       C  
ATOM   2779  CD  LYS A 359      29.938 109.760  10.162  1.00 39.69           C  
ANISOU 2779  CD  LYS A 359     8022   3003   4056   -148   1785    -61       C  
ATOM   2780  CE  LYS A 359      28.734 110.053  11.047  1.00 39.07           C  
ANISOU 2780  CE  LYS A 359     7899   2938   4006   -239   1765    -57       C  
ATOM   2781  NZ  LYS A 359      28.932 109.563  12.438  1.00 38.17           N1+
ANISOU 2781  NZ  LYS A 359     7800   2768   3935   -293   1756    -61       N1+
ATOM   2782  N   VAL A 360      35.024 109.207   8.392  1.00 36.95           N  
ANISOU 2782  N   VAL A 360     7754   2623   3662    197   1916     12       N  
ATOM   2783  CA  VAL A 360      35.800 109.245   7.157  1.00 37.39           C  
ANISOU 2783  CA  VAL A 360     7825   2710   3671    307   1948     33       C  
ATOM   2784  C   VAL A 360      36.853 108.140   7.143  1.00 37.80           C  
ANISOU 2784  C   VAL A 360     7952   2720   3691    372   1955     28       C  
ATOM   2785  O   VAL A 360      37.248 107.661   6.072  1.00 38.38           O  
ANISOU 2785  O   VAL A 360     8083   2800   3699    462   1964     22       O  
ATOM   2786  CB  VAL A 360      36.431 110.637   6.952  1.00 37.10           C  
ANISOU 2786  CB  VAL A 360     7688   2729   3678    347   2005    101       C  
ATOM   2787  CG1 VAL A 360      37.141 110.714   5.599  1.00 37.60           C  
ANISOU 2787  CG1 VAL A 360     7762   2833   3691    464   2040    128       C  
ATOM   2788  CG2 VAL A 360      35.364 111.706   7.049  1.00 36.73           C  
ANISOU 2788  CG2 VAL A 360     7576   2716   3662    285   2002    105       C  
ATOM   2789  N   ASP A 361      37.324 107.721   8.318  1.00 38.48           N  
ANISOU 2789  N   ASP A 361     8042   2764   3816    336   1952     34       N  
ATOM   2790  CA  ASP A 361      38.235 106.579   8.388  1.00 38.78           C  
ANISOU 2790  CA  ASP A 361     8158   2758   3819    398   1958     30       C  
ATOM   2791  C   ASP A 361      37.393 105.307   8.366  1.00 38.92           C  
ANISOU 2791  C   ASP A 361     8289   2710   3787    357   1904    -42       C  
ATOM   2792  O   ASP A 361      37.204 104.619   9.373  1.00 38.51           O  
ANISOU 2792  O   ASP A 361     8271   2604   3756    295   1879    -64       O  
ATOM   2793  CB  ASP A 361      39.127 106.648   9.621  1.00 38.18           C  
ANISOU 2793  CB  ASP A 361     8036   2670   3800    382   1978     70       C  
ATOM   2794  CG  ASP A 361      40.326 105.724   9.517  1.00 38.69           C  
ANISOU 2794  CG  ASP A 361     8157   2715   3828    477   2003     91       C  
ATOM   2795  OD1 ASP A 361      40.316 104.838   8.638  1.00 39.32           O  
ANISOU 2795  OD1 ASP A 361     8335   2770   3837    543   1997     60       O  
ATOM   2796  OD2 ASP A 361      41.277 105.883  10.310  1.00 38.47           O1+
ANISOU 2796  OD2 ASP A 361     8079   2698   3839    487   2028    140       O1+
ATOM   2797  N   THR A 362      36.859 105.010   7.184  1.00 38.94           N  
ANISOU 2797  N   THR A 362     8352   2720   3724    389   1885    -79       N  
ATOM   2798  CA  THR A 362      36.061 103.819   6.943  1.00 39.33           C  
ANISOU 2798  CA  THR A 362     8518   2707   3716    352   1829   -149       C  
ATOM   2799  C   THR A 362      36.570 103.129   5.685  1.00 40.11           C  
ANISOU 2799  C   THR A 362     8717   2795   3726    464   1838   -168       C  
ATOM   2800  O   THR A 362      37.439 103.642   4.975  1.00 40.35           O  
ANISOU 2800  O   THR A 362     8715   2875   3740    569   1888   -123       O  
ATOM   2801  CB  THR A 362      34.570 104.155   6.799  1.00 39.43           C  
ANISOU 2801  CB  THR A 362     8508   2742   3732    251   1779   -185       C  
ATOM   2802  OG1 THR A 362      34.391 105.088   5.726  1.00 39.84           O  
ANISOU 2802  OG1 THR A 362     8506   2869   3762    298   1797   -167       O  
ATOM   2803  CG2 THR A 362      34.030 104.758   8.088  1.00 38.64           C  
ANISOU 2803  CG2 THR A 362     8320   2647   3713    147   1773   -167       C  
ATOM   2804  N   ARG A 363      36.006 101.952   5.409  1.00 39.72           N  
ANISOU 2804  N   ARG A 363     8795   2679   3618    439   1789   -235       N  
ATOM   2805  CA  ARG A 363      36.427 101.161   4.254  1.00 40.63           C  
ANISOU 2805  CA  ARG A 363     9030   2769   3638    544   1792   -263       C  
ATOM   2806  C   ARG A 363      35.298 100.186   3.918  1.00 41.29           C  
ANISOU 2806  C   ARG A 363     9232   2791   3665    467   1716   -347       C  
ATOM   2807  O   ARG A 363      35.131  99.172   4.602  1.00 41.54           O  
ANISOU 2807  O   ARG A 363     9335   2748   3700    410   1682   -376       O  
ATOM   2808  CB  ARG A 363      37.732 100.435   4.539  1.00 40.93           C  
ANISOU 2808  CB  ARG A 363     9129   2763   3660    643   1837   -236       C  
ATOM   2809  CG  ARG A 363      38.125  99.400   3.502  1.00 41.98           C  
ANISOU 2809  CG  ARG A 363     9389   2868   3694    743   1827   -261       C  
ATOM   2810  CD  ARG A 363      39.390  98.666   3.921  1.00 42.28           C  
ANISOU 2810  CD  ARG A 363     9452   2888   3726    830   1863   -212       C  
ATOM   2811  NE  ARG A 363      39.503  97.359   3.279  1.00 43.36           N  
ANISOU 2811  NE  ARG A 363     9714   2982   3778    880   1826   -240       N  
ATOM   2812  CZ  ARG A 363      40.061  97.154   2.091  1.00 44.11           C  
ANISOU 2812  CZ  ARG A 363     9866   3099   3796   1006   1845   -229       C  
ATOM   2813  NH1 ARG A 363      40.563  98.173   1.406  1.00 43.89           N1+
ANISOU 2813  NH1 ARG A 363     9772   3141   3764   1097   1903   -187       N1+
ATOM   2814  NH2 ARG A 363      40.117  95.928   1.588  1.00 45.14           N  
ANISOU 2814  NH2 ARG A 363    10118   3181   3853   1043   1808   -257       N  
ATOM   2815  N   VAL A 364      34.541 100.501   2.871  1.00 41.62           N  
ANISOU 2815  N   VAL A 364     9277   2878   3659    461   1685   -376       N  
ATOM   2816  CA  VAL A 364      33.429  99.666   2.420  1.00 42.35           C  
ANISOU 2816  CA  VAL A 364     9474   2925   3693    382   1607   -453       C  
ATOM   2817  C   VAL A 364      33.977  98.567   1.515  1.00 43.43           C  
ANISOU 2817  C   VAL A 364     9764   3005   3731    478   1598   -492       C  
ATOM   2818  O   VAL A 364      34.826  98.842   0.654  1.00 43.67           O  
ANISOU 2818  O   VAL A 364     9798   3077   3717    612   1645   -463       O  
ATOM   2819  CB  VAL A 364      32.355 100.513   1.714  1.00 42.29           C  
ANISOU 2819  CB  VAL A 364     9390   3003   3674    331   1573   -461       C  
ATOM   2820  CG1 VAL A 364      32.983 101.419   0.661  1.00 42.26           C  
ANISOU 2820  CG1 VAL A 364     9333   3084   3640    458   1627   -419       C  
ATOM   2821  CG2 VAL A 364      31.283  99.628   1.096  1.00 43.21           C  
ANISOU 2821  CG2 VAL A 364     9618   3083   3718    256   1488   -540       C  
ATOM   2822  N   PRO A 365      33.550  97.316   1.686  1.00 44.14           N  
ANISOU 2822  N   PRO A 365     9947   3029   3796    410   1529   -534       N  
ATOM   2823  CA  PRO A 365      34.084  96.234   0.852  1.00 45.25           C  
ANISOU 2823  CA  PRO A 365    10205   3136   3854    496   1507   -551       C  
ATOM   2824  C   PRO A 365      33.733  96.422  -0.616  1.00 45.95           C  
ANISOU 2824  C   PRO A 365    10348   3259   3852    550   1486   -591       C  
ATOM   2825  O   PRO A 365      32.717  97.027  -0.965  1.00 45.82           O  
ANISOU 2825  O   PRO A 365    10310   3275   3824    479   1457   -629       O  
ATOM   2826  CB  PRO A 365      33.413  94.978   1.423  1.00 45.85           C  
ANISOU 2826  CB  PRO A 365    10360   3132   3930    380   1431   -595       C  
ATOM   2827  CG  PRO A 365      33.006  95.358   2.812  1.00 44.89           C  
ANISOU 2827  CG  PRO A 365    10143   3007   3906    268   1436   -573       C  
ATOM   2828  CD  PRO A 365      32.649  96.810   2.736  1.00 44.00           C  
ANISOU 2828  CD  PRO A 365     9927   2961   3829    258   1473   -559       C  
ATOM   2829  N   ASP A 366      34.602  95.894  -1.475  1.00 46.74           N  
ANISOU 2829  N   ASP A 366    10519   3357   3884    682   1502   -578       N  
ATOM   2830  CA  ASP A 366      34.384  95.974  -2.912  1.00 47.53           C  
ANISOU 2830  CA  ASP A 366    10677   3491   3890    750   1481   -611       C  
ATOM   2831  C   ASP A 366      33.032  95.364  -3.273  1.00 48.28           C  
ANISOU 2831  C   ASP A 366    10859   3548   3938    622   1381   -699       C  
ATOM   2832  O   ASP A 366      32.665  94.311  -2.736  1.00 48.77           O  
ANISOU 2832  O   ASP A 366    10992   3531   4007    531   1324   -732       O  
ATOM   2833  CB  ASP A 366      35.494  95.239  -3.669  1.00 48.45           C  
ANISOU 2833  CB  ASP A 366    10876   3593   3939    902   1505   -586       C  
ATOM   2834  CG  ASP A 366      36.840  95.911  -3.532  1.00 47.86           C  
ANISOU 2834  CG  ASP A 366    10716   3573   3897   1039   1604   -495       C  
ATOM   2835  OD1 ASP A 366      37.813  95.419  -4.141  1.00 48.58           O  
ANISOU 2835  OD1 ASP A 366    10862   3663   3934   1175   1633   -462       O  
ATOM   2836  OD2 ASP A 366      36.922  96.937  -2.826  1.00 46.75           O1+
ANISOU 2836  OD2 ASP A 366    10453   3476   3834   1012   1653   -454       O1+
ATOM   2837  N   PRO A 367      32.263  95.997  -4.159  1.00 48.44           N  
ANISOU 2837  N   PRO A 367    10873   3625   3907    608   1357   -737       N  
ATOM   2838  CA  PRO A 367      31.054  95.346  -4.676  1.00 49.39           C  
ANISOU 2838  CA  PRO A 367    11088   3713   3964    497   1255   -822       C  
ATOM   2839  C   PRO A 367      31.407  94.048  -5.386  1.00 50.78           C  
ANISOU 2839  C   PRO A 367    11407   3824   4062    550   1209   -854       C  
ATOM   2840  O   PRO A 367      32.545  93.833  -5.807  1.00 51.07           O  
ANISOU 2840  O   PRO A 367    11469   3862   4073    698   1260   -813       O  
ATOM   2841  CB  PRO A 367      30.480  96.382  -5.651  1.00 49.32           C  
ANISOU 2841  CB  PRO A 367    11039   3802   3899    521   1259   -839       C  
ATOM   2842  CG  PRO A 367      31.042  97.687  -5.195  1.00 48.03           C  
ANISOU 2842  CG  PRO A 367    10735   3710   3805    585   1358   -765       C  
ATOM   2843  CD  PRO A 367      32.406  97.379  -4.649  1.00 47.75           C  
ANISOU 2843  CD  PRO A 367    10683   3639   3820    683   1421   -700       C  
ATOM   2844  N   GLN A 368      30.413  93.172  -5.519  1.00 51.71           N  
ANISOU 2844  N   GLN A 368    11620   3884   4143    425   1111   -926       N  
ATOM   2845  CA  GLN A 368      30.643  91.889  -6.164  1.00 53.15           C  
ANISOU 2845  CA  GLN A 368    11949   3994   4251    461   1062   -963       C  
ATOM   2846  C   GLN A 368      30.894  92.092  -7.658  1.00 53.95           C  
ANISOU 2846  C   GLN A 368    12103   4148   4250    587   1061   -981       C  
ATOM   2847  O   GLN A 368      30.920  93.213  -8.171  1.00 53.37           O  
ANISOU 2847  O   GLN A 368    11945   4169   4164    650   1102   -960       O  
ATOM   2848  CB  GLN A 368      29.465  90.950  -5.917  1.00 54.00           C  
ANISOU 2848  CB  GLN A 368    12140   4029   4349    283    955  -1034       C  
ATOM   2849  CG  GLN A 368      29.238  90.615  -4.456  1.00 53.36           C  
ANISOU 2849  CG  GLN A 368    12013   3895   4367    164    953  -1012       C  
ATOM   2850  CD  GLN A 368      28.429  89.348  -4.278  1.00 54.53           C  
ANISOU 2850  CD  GLN A 368    12268   3953   4498     25    857  -1068       C  
ATOM   2851  OE1 GLN A 368      28.772  88.298  -4.823  1.00 55.77           O  
ANISOU 2851  OE1 GLN A 368    12551   4046   4594     72    830  -1092       O  
ATOM   2852  NE2 GLN A 368      27.347  89.438  -3.513  1.00 54.20           N  
ANISOU 2852  NE2 GLN A 368    12177   3906   4512   -147    808  -1084       N  
ATOM   2853  N   GLU A 369      31.078  90.982  -8.371  1.00 46.97           N  
ANISOU 2853  N   GLU A 369    10271   2842   4732    364   2093    113       N  
ATOM   2854  CA  GLU A 369      31.454  91.063  -9.778  1.00 46.51           C  
ANISOU 2854  CA  GLU A 369    10140   2837   4693    496   2034     -6       C  
ATOM   2855  C   GLU A 369      30.257  91.364 -10.672  1.00 46.22           C  
ANISOU 2855  C   GLU A 369    10030   2816   4715    458   2081    -23       C  
ATOM   2856  O   GLU A 369      30.358  92.190 -11.586  1.00 45.25           O  
ANISOU 2856  O   GLU A 369     9813   2816   4562    521   2144    -84       O  
ATOM   2857  CB  GLU A 369      32.143  89.769 -10.212  1.00 47.68           C  
ANISOU 2857  CB  GLU A 369    10326   2879   4909    595   1802    -76       C  
ATOM   2858  CG  GLU A 369      33.486  89.561  -9.529  1.00 47.86           C  
ANISOU 2858  CG  GLU A 369    10405   2910   4871    664   1749    -88       C  
ATOM   2859  CD  GLU A 369      34.537  89.013 -10.469  1.00 48.24           C  
ANISOU 2859  CD  GLU A 369    10410   2984   4936    834   1586   -227       C  
ATOM   2860  OE1 GLU A 369      34.824  87.799 -10.402  1.00 49.61           O  
ANISOU 2860  OE1 GLU A 369    10644   3021   5186    877   1384   -260       O  
ATOM   2861  OE2 GLU A 369      35.078  89.798 -11.278  1.00 47.29           O1+
ANISOU 2861  OE2 GLU A 369    10181   3031   4757    920   1648   -303       O1+
ATOM   2862  N   GLY A 370      29.123  90.703 -10.435  1.00 47.00           N  
ANISOU 2862  N   GLY A 370    10158   2799   4899    347   2037     41       N  
ATOM   2863  CA  GLY A 370      27.924  91.029 -11.192  1.00 46.74           C  
ANISOU 2863  CA  GLY A 370    10058   2781   4920    303   2092     29       C  
ATOM   2864  C   GLY A 370      27.454  92.449 -10.938  1.00 45.52           C  
ANISOU 2864  C   GLY A 370     9846   2758   4693    253   2311     51       C  
ATOM   2865  O   GLY A 370      27.031  93.151 -11.862  1.00 44.77           O  
ANISOU 2865  O   GLY A 370     9669   2737   4603    285   2370     -1       O  
ATOM   2866  N   THR A 371      27.519  92.888  -9.678  1.00 47.01           N  
ANISOU 2866  N   THR A 371    10069   2977   4816    175   2419    125       N  
ATOM   2867  CA  THR A 371      27.205  94.275  -9.344  1.00 45.95           C  
ANISOU 2867  CA  THR A 371     9881   2965   4614    146   2612    126       C  
ATOM   2868  C   THR A 371      28.099  95.235 -10.115  1.00 44.73           C  
ANISOU 2868  C   THR A 371     9671   2924   4399    260   2657     61       C  
ATOM   2869  O   THR A 371      27.619  96.171 -10.767  1.00 43.96           O  
ANISOU 2869  O   THR A 371     9488   2906   4307    261   2731     45       O  
ATOM   2870  CB  THR A 371      27.370  94.501  -7.840  1.00 46.17           C  
ANISOU 2870  CB  THR A 371     9936   3026   4582     70   2683    193       C  
ATOM   2871  OG1 THR A 371      26.720  93.447  -7.119  1.00 47.56           O  
ANISOU 2871  OG1 THR A 371    10137   3125   4809    -52   2593    291       O  
ATOM   2872  CG2 THR A 371      26.778  95.834  -7.433  1.00 45.40           C  
ANISOU 2872  CG2 THR A 371     9754   3041   4455     37   2843    170       C  
ATOM   2873  N   ARG A 372      29.413  95.005 -10.054  1.00 46.29           N  
ANISOU 2873  N   ARG A 372     9894   3142   4552    343   2585     47       N  
ATOM   2874  CA  ARG A 372      30.380  95.866 -10.725  1.00 45.30           C  
ANISOU 2874  CA  ARG A 372     9674   3144   4393    425   2580     24       C  
ATOM   2875  C   ARG A 372      30.117  95.958 -12.222  1.00 45.05           C  
ANISOU 2875  C   ARG A 372     9537   3164   4418    480   2509    -37       C  
ATOM   2876  O   ARG A 372      30.435  96.976 -12.847  1.00 44.20           O  
ANISOU 2876  O   ARG A 372     9314   3169   4311    502   2520    -36       O  
ATOM   2877  CB  ARG A 372      31.786  95.335 -10.456  1.00 45.56           C  
ANISOU 2877  CB  ARG A 372     9746   3180   4385    507   2484      4       C  
ATOM   2878  CG  ARG A 372      32.933  96.170 -10.967  1.00 44.72           C  
ANISOU 2878  CG  ARG A 372     9523   3209   4259    578   2454    -11       C  
ATOM   2879  CD  ARG A 372      34.210  95.386 -10.748  1.00 45.38           C  
ANISOU 2879  CD  ARG A 372     9652   3284   4305    667   2346    -54       C  
ATOM   2880  NE  ARG A 372      34.202  94.753  -9.430  1.00 46.08           N  
ANISOU 2880  NE  ARG A 372     9889   3260   4360    622   2370     -9       N  
ATOM   2881  CZ  ARG A 372      34.710  93.553  -9.170  1.00 47.19           C  
ANISOU 2881  CZ  ARG A 372    10120   3301   4508    673   2243    -45       C  
ATOM   2882  NH1 ARG A 372      35.262  92.842 -10.142  1.00 47.66           N1+
ANISOU 2882  NH1 ARG A 372    10138   3363   4605    782   2088   -141       N1+
ATOM   2883  NH2 ARG A 372      34.657  93.058  -7.940  1.00 47.79           N  
ANISOU 2883  NH2 ARG A 372    10321   3274   4565    613   2252     13       N  
ATOM   2884  N   GLN A 373      29.534  94.912 -12.813  1.00 43.01           N  
ANISOU 2884  N   GLN A 373     9307   2813   4221    496   2414    -86       N  
ATOM   2885  CA  GLN A 373      29.221  94.939 -14.237  1.00 42.89           C  
ANISOU 2885  CA  GLN A 373     9197   2844   4254    553   2348   -154       C  
ATOM   2886  C   GLN A 373      27.976  95.770 -14.521  1.00 42.37           C  
ANISOU 2886  C   GLN A 373     9075   2805   4219    476   2453   -126       C  
ATOM   2887  O   GLN A 373      27.968  96.588 -15.447  1.00 41.70           O  
ANISOU 2887  O   GLN A 373     8884   2822   4138    504   2458   -145       O  
ATOM   2888  CB  GLN A 373      29.051  93.514 -14.767  1.00 44.05           C  
ANISOU 2888  CB  GLN A 373     9390   2872   4477    605   2185   -221       C  
ATOM   2889  CG  GLN A 373      28.606  93.466 -16.215  1.00 44.06           C  
ANISOU 2889  CG  GLN A 373     9301   2913   4528    664   2119   -301       C  
ATOM   2890  CD  GLN A 373      28.969  92.167 -16.900  1.00 45.18           C  
ANISOU 2890  CD  GLN A 373     9459   2979   4730    767   1926   -401       C  
ATOM   2891  OE1 GLN A 373      29.099  91.127 -16.255  1.00 46.18           O  
ANISOU 2891  OE1 GLN A 373     9679   2965   4901    760   1825   -392       O  
ATOM   2892  NE2 GLN A 373      29.143  92.221 -18.215  1.00 45.14           N  
ANISOU 2892  NE2 GLN A 373     9358   3065   4729    864   1860   -499       N  
ATOM   2893  N   VAL A 374      26.915  95.569 -13.734  1.00 42.96           N  
ANISOU 2893  N   VAL A 374     9214   2788   4321    376   2528    -81       N  
ATOM   2894  CA  VAL A 374      25.687  96.347 -13.902  1.00 42.59           C  
ANISOU 2894  CA  VAL A 374     9114   2765   4304    304   2632    -66       C  
ATOM   2895  C   VAL A 374      25.986  97.834 -13.787  1.00 41.51           C  
ANISOU 2895  C   VAL A 374     8895   2748   4127    296   2722    -30       C  
ATOM   2896  O   VAL A 374      25.511  98.648 -14.588  1.00 40.97           O  
ANISOU 2896  O   VAL A 374     8730   2741   4096    297   2727    -42       O  
ATOM   2897  CB  VAL A 374      24.627  95.912 -12.874  1.00 43.36           C  
ANISOU 2897  CB  VAL A 374     9286   2759   4431    189   2701    -21       C  
ATOM   2898  CG1 VAL A 374      23.432  96.856 -12.910  1.00 42.99           C  
ANISOU 2898  CG1 VAL A 374     9180   2752   4402    123   2827    -19       C  
ATOM   2899  CG2 VAL A 374      24.189  94.482 -13.136  1.00 44.56           C  
ANISOU 2899  CG2 VAL A 374     9484   2773   4673    170   2556    -22       C  
ATOM   2900  N   MET A 375      26.783  98.205 -12.781  1.00 42.69           N  
ANISOU 2900  N   MET A 375     9079   2916   4226    284   2764     19       N  
ATOM   2901  CA  MET A 375      27.239  99.585 -12.648  1.00 41.77           C  
ANISOU 2901  CA  MET A 375     8864   2876   4131    280   2775     53       C  
ATOM   2902  C   MET A 375      27.913 100.072 -13.923  1.00 41.21           C  
ANISOU 2902  C   MET A 375     8684   2902   4073    355   2680     18       C  
ATOM   2903  O   MET A 375      27.653 101.188 -14.384  1.00 40.63           O  
ANISOU 2903  O   MET A 375     8513   2883   4040    343   2678     20       O  
ATOM   2904  CB  MET A 375      28.201  99.699 -11.464  1.00 41.70           C  
ANISOU 2904  CB  MET A 375     8900   2851   4092    278   2782     92       C  
ATOM   2905  CG  MET A 375      27.566 100.197 -10.182  1.00 41.80           C  
ANISOU 2905  CG  MET A 375     8914   2821   4148    210   2849    100       C  
ATOM   2906  SD  MET A 375      28.280  99.415  -8.725  1.00 42.44           S  
ANISOU 2906  SD  MET A 375     9092   2859   4172    208   2852     99       S  
ATOM   2907  CE  MET A 375      30.021  99.425  -9.143  1.00 41.93           C  
ANISOU 2907  CE  MET A 375     9035   2836   4062    293   2771    133       C  
ATOM   2908  N   ASN A 376      28.778  99.241 -14.510  1.00 39.95           N  
ANISOU 2908  N   ASN A 376     8541   2762   3876    435   2595    -25       N  
ATOM   2909  CA  ASN A 376      29.503  99.641 -15.712  1.00 39.61           C  
ANISOU 2909  CA  ASN A 376     8398   2823   3829    509   2513    -69       C  
ATOM   2910  C   ASN A 376      28.564  99.832 -16.896  1.00 39.58           C  
ANISOU 2910  C   ASN A 376     8336   2839   3865    512   2502   -107       C  
ATOM   2911  O   ASN A 376      28.779 100.722 -17.727  1.00 39.13           O  
ANISOU 2911  O   ASN A 376     8188   2868   3810    531   2480   -115       O  
ATOM   2912  CB  ASN A 376      30.581  98.606 -16.037  1.00 40.16           C  
ANISOU 2912  CB  ASN A 376     8495   2911   3855    606   2418   -131       C  
ATOM   2913  CG  ASN A 376      31.196  98.811 -17.409  1.00 40.10           C  
ANISOU 2913  CG  ASN A 376     8384   3023   3831    689   2338   -199       C  
ATOM   2914  OD1 ASN A 376      30.929  98.050 -18.340  1.00 40.66           O  
ANISOU 2914  OD1 ASN A 376     8447   3091   3911    750   2272   -277       O  
ATOM   2915  ND2 ASN A 376      32.016  99.846 -17.542  1.00 39.53           N  
ANISOU 2915  ND2 ASN A 376     8229   3057   3735    692   2339   -177       N  
ATOM   2916  N   ILE A 377      27.517  99.011 -16.989  1.00 39.09           N  
ANISOU 2916  N   ILE A 377     8328   2692   3834    492   2514   -131       N  
ATOM   2917  CA  ILE A 377      26.575  99.133 -18.097  1.00 39.12           C  
ANISOU 2917  CA  ILE A 377     8276   2707   3882    496   2498   -171       C  
ATOM   2918  C   ILE A 377      25.743 100.402 -17.953  1.00 38.51           C  
ANISOU 2918  C   ILE A 377     8145   2651   3838    422   2578   -125       C  
ATOM   2919  O   ILE A 377      25.617 101.192 -18.896  1.00 38.15           O  
ANISOU 2919  O   ILE A 377     8020   2670   3804    439   2557   -140       O  
ATOM   2920  CB  ILE A 377      25.681  97.883 -18.181  1.00 39.99           C  
ANISOU 2920  CB  ILE A 377     8452   2704   4037    492   2469   -215       C  
ATOM   2921  CG1 ILE A 377      26.508  96.657 -18.573  1.00 40.72           C  
ANISOU 2921  CG1 ILE A 377     8581   2768   4123    587   2342   -285       C  
ATOM   2922  CG2 ILE A 377      24.542  98.111 -19.163  1.00 39.98           C  
ANISOU 2922  CG2 ILE A 377     8392   2705   4093    481   2467   -248       C  
ATOM   2923  CD1 ILE A 377      25.719  95.366 -18.584  1.00 41.74           C  
ANISOU 2923  CD1 ILE A 377     8780   2753   4328    579   2270   -322       C  
ATOM   2924  N   VAL A 378      25.170 100.618 -16.767  1.00 38.52           N  
ANISOU 2924  N   VAL A 378     8188   2596   3851    343   2666    -77       N  
ATOM   2925  CA  VAL A 378      24.288 101.763 -16.557  1.00 38.13           C  
ANISOU 2925  CA  VAL A 378     8083   2559   3846    283   2727    -55       C  
ATOM   2926  C   VAL A 378      25.065 103.069 -16.668  1.00 37.42           C  
ANISOU 2926  C   VAL A 378     7919   2543   3757    299   2695    -34       C  
ATOM   2927  O   VAL A 378      24.557 104.068 -17.191  1.00 37.11           O  
ANISOU 2927  O   VAL A 378     7815   2535   3751    289   2694    -42       O  
ATOM   2928  CB  VAL A 378      23.575 101.639 -15.197  1.00 38.49           C  
ANISOU 2928  CB  VAL A 378     8187   2535   3901    204   2824    -27       C  
ATOM   2929  CG1 VAL A 378      22.695 102.853 -14.938  1.00 38.20           C  
ANISOU 2929  CG1 VAL A 378     8076   2521   3919    159   2866    -29       C  
ATOM   2930  CG2 VAL A 378      22.751 100.362 -15.148  1.00 39.34           C  
ANISOU 2930  CG2 VAL A 378     8381   2560   4008    178   2860    -52       C  
ATOM   2931  N   SER A 379      26.311 103.081 -16.190  1.00 37.72           N  
ANISOU 2931  N   SER A 379     7970   2603   3758    327   2665    -12       N  
ATOM   2932  CA  SER A 379      27.098 104.309 -16.229  1.00 37.15           C  
ANISOU 2932  CA  SER A 379     7833   2594   3689    339   2633      3       C  
ATOM   2933  C   SER A 379      27.526 104.653 -17.650  1.00 37.02           C  
ANISOU 2933  C   SER A 379     7761   2653   3651    391   2577    -24       C  
ATOM   2934  O   SER A 379      27.534 105.829 -18.033  1.00 36.70           O  
ANISOU 2934  O   SER A 379     7673   2647   3624    382   2571    -18       O  
ATOM   2935  CB  SER A 379      28.317 104.183 -15.317  1.00 37.07           C  
ANISOU 2935  CB  SER A 379     7846   2590   3647    355   2614     25       C  
ATOM   2936  OG  SER A 379      27.927 104.104 -13.957  1.00 37.21           O  
ANISOU 2936  OG  SER A 379     7908   2545   3684    306   2668     47       O  
ATOM   2937  N   SER A 380      27.890 103.646 -18.447  1.00 36.90           N  
ANISOU 2937  N   SER A 380     7758   2666   3597    449   2534    -63       N  
ATOM   2938  CA  SER A 380      28.250 103.914 -19.834  1.00 36.93           C  
ANISOU 2938  CA  SER A 380     7704   2758   3570    502   2484   -100       C  
ATOM   2939  C   SER A 380      27.030 104.319 -20.652  1.00 36.94           C  
ANISOU 2939  C   SER A 380     7682   2743   3609    481   2503   -115       C  
ATOM   2940  O   SER A 380      27.154 105.094 -21.607  1.00 36.84           O  
ANISOU 2940  O   SER A 380     7625   2796   3578    498   2486   -124       O  
ATOM   2941  CB  SER A 380      28.931 102.691 -20.450  1.00 37.47           C  
ANISOU 2941  CB  SER A 380     7778   2871   3587    584   2422   -161       C  
ATOM   2942  OG  SER A 380      29.755 103.063 -21.539  1.00 37.55           O  
ANISOU 2942  OG  SER A 380     7718   3010   3540    642   2374   -196       O  
ATOM   2943  N   TRP A 381      25.849 103.812 -20.291  1.00 37.13           N  
ANISOU 2943  N   TRP A 381     7740   2686   3681    443   2541   -120       N  
ATOM   2944  CA  TRP A 381      24.624 104.230 -20.963  1.00 37.15           C  
ANISOU 2944  CA  TRP A 381     7715   2673   3727    420   2559   -139       C  
ATOM   2945  C   TRP A 381      24.211 105.636 -20.549  1.00 36.75           C  
ANISOU 2945  C   TRP A 381     7638   2616   3709    368   2599   -104       C  
ATOM   2946  O   TRP A 381      23.614 106.365 -21.349  1.00 36.71           O  
ANISOU 2946  O   TRP A 381     7602   2624   3721    367   2597   -119       O  
ATOM   2947  CB  TRP A 381      23.494 103.241 -20.668  1.00 37.59           C  
ANISOU 2947  CB  TRP A 381     7807   2651   3825    393   2587   -163       C  
ATOM   2948  CG  TRP A 381      22.161 103.670 -21.210  1.00 37.65           C  
ANISOU 2948  CG  TRP A 381     7778   2640   3886    364   2608   -186       C  
ATOM   2949  CD1 TRP A 381      21.654 103.401 -22.449  1.00 37.88           C  
ANISOU 2949  CD1 TRP A 381     7780   2682   3931    403   2564   -238       C  
ATOM   2950  CD2 TRP A 381      21.165 104.446 -20.531  1.00 37.54           C  
ANISOU 2950  CD2 TRP A 381     7746   2598   3920    299   2670   -171       C  
ATOM   2951  NE1 TRP A 381      20.407 103.960 -22.583  1.00 37.89           N  
ANISOU 2951  NE1 TRP A 381     7749   2658   3988    363   2595   -250       N  
ATOM   2952  CE2 TRP A 381      20.083 104.608 -21.420  1.00 37.70           C  
ANISOU 2952  CE2 TRP A 381     7727   2614   3985    301   2660   -214       C  
ATOM   2953  CE3 TRP A 381      21.083 105.020 -19.259  1.00 37.40           C  
ANISOU 2953  CE3 TRP A 381     7735   2564   3913    248   2726   -138       C  
ATOM   2954  CZ2 TRP A 381      18.935 105.318 -21.077  1.00 37.75           C  
ANISOU 2954  CZ2 TRP A 381     7698   2602   4044    255   2704   -227       C  
ATOM   2955  CZ3 TRP A 381      19.943 105.725 -18.921  1.00 37.50           C  
ANISOU 2955  CZ3 TRP A 381     7708   2564   3974    205   2769   -157       C  
ATOM   2956  CH2 TRP A 381      18.884 105.868 -19.826  1.00 37.67           C  
ANISOU 2956  CH2 TRP A 381     7690   2585   4039    210   2758   -202       C  
ATOM   2957  N   LEU A 382      24.517 106.034 -19.313  1.00 36.54           N  
ANISOU 2957  N   LEU A 382     7626   2567   3691    332   2629    -67       N  
ATOM   2958  CA  LEU A 382      24.094 107.348 -18.845  1.00 36.31           C  
ANISOU 2958  CA  LEU A 382     7570   2529   3696    294   2655    -54       C  
ATOM   2959  C   LEU A 382      24.974 108.457 -19.412  1.00 36.04           C  
ANISOU 2959  C   LEU A 382     7520   2540   3635    318   2623    -39       C  
ATOM   2960  O   LEU A 382      24.479 109.551 -19.703  1.00 36.01           O  
ANISOU 2960  O   LEU A 382     7504   2529   3650    304   2634    -43       O  
ATOM   2961  CB  LEU A 382      24.085 107.389 -17.316  1.00 36.30           C  
ANISOU 2961  CB  LEU A 382     7585   2496   3712    255   2694    -35       C  
ATOM   2962  CG  LEU A 382      23.394 108.614 -16.713  1.00 36.27           C  
ANISOU 2962  CG  LEU A 382     7545   2488   3747    224   2720    -46       C  
ATOM   2963  CD1 LEU A 382      22.024 108.821 -17.341  1.00 36.51           C  
ANISOU 2963  CD1 LEU A 382     7544   2512   3816    210   2740    -86       C  
ATOM   2964  CD2 LEU A 382      23.275 108.476 -15.203  1.00 36.44           C  
ANISOU 2964  CD2 LEU A 382     7574   2492   3779    192   2759    -44       C  
ATOM   2965  N   TRP A 383      26.277 108.203 -19.570  1.00 37.18           N  
ANISOU 2965  N   TRP A 383     7668   2731   3728    354   2586    -27       N  
ATOM   2966  CA  TRP A 383      27.136 109.188 -20.222  1.00 37.10           C  
ANISOU 2966  CA  TRP A 383     7642   2776   3677    372   2562    -15       C  
ATOM   2967  C   TRP A 383      26.726 109.398 -21.675  1.00 37.33           C  
ANISOU 2967  C   TRP A 383     7659   2842   3681    393   2553    -35       C  
ATOM   2968  O   TRP A 383      26.648 110.539 -22.146  1.00 37.37           O  
ANISOU 2968  O   TRP A 383     7673   2850   3676    381   2564    -22       O  
ATOM   2969  CB  TRP A 383      28.603 108.760 -20.143  1.00 37.09           C  
ANISOU 2969  CB  TRP A 383     7627   2847   3618    408   2522     -9       C  
ATOM   2970  CG  TRP A 383      29.259 108.972 -18.805  1.00 36.86           C  
ANISOU 2970  CG  TRP A 383     7608   2793   3604    390   2526     15       C  
ATOM   2971  CD1 TRP A 383      29.866 108.025 -18.034  1.00 36.87           C  
ANISOU 2971  CD1 TRP A 383     7623   2792   3593    406   2513     16       C  
ATOM   2972  CD2 TRP A 383      29.386 110.211 -18.091  1.00 36.67           C  
ANISOU 2972  CD2 TRP A 383     7589   2740   3602    360   2541     36       C  
ATOM   2973  NE1 TRP A 383      30.360 108.593 -16.884  1.00 36.65           N  
ANISOU 2973  NE1 TRP A 383     7600   2743   3581    385   2519     38       N  
ATOM   2974  CE2 TRP A 383      30.077 109.933 -16.894  1.00 36.53           C  
ANISOU 2974  CE2 TRP A 383     7577   2714   3589    358   2535     46       C  
ATOM   2975  CE3 TRP A 383      28.979 111.525 -18.344  1.00 36.69           C  
ANISOU 2975  CE3 TRP A 383     7603   2718   3619    338   2561     42       C  
ATOM   2976  CZ2 TRP A 383      30.370 110.920 -15.954  1.00 36.39           C  
ANISOU 2976  CZ2 TRP A 383     7564   2673   3589    338   2544     59       C  
ATOM   2977  CZ3 TRP A 383      29.273 112.504 -17.410  1.00 36.60           C  
ANISOU 2977  CZ3 TRP A 383     7608   2676   3624    318   2572     54       C  
ATOM   2978  CH2 TRP A 383      29.961 112.196 -16.230  1.00 36.44           C  
ANISOU 2978  CH2 TRP A 383     7580   2657   3608    320   2562     60       C  
ATOM   2979  N   LYS A 384      26.464 108.307 -22.403  1.00 36.36           N  
ANISOU 2979  N   LYS A 384     7526   2746   3543    428   2533    -70       N  
ATOM   2980  CA  LYS A 384      25.984 108.426 -23.777  1.00 36.64           C  
ANISOU 2980  CA  LYS A 384     7547   2821   3553    453   2523    -98       C  
ATOM   2981  C   LYS A 384      24.650 109.155 -23.842  1.00 36.60           C  
ANISOU 2981  C   LYS A 384     7557   2740   3611    415   2559   -101       C  
ATOM   2982  O   LYS A 384      24.380 109.869 -24.814  1.00 36.79           O  
ANISOU 2982  O   LYS A 384     7585   2782   3611    422   2561   -105       O  
ATOM   2983  CB  LYS A 384      25.865 107.041 -24.413  1.00 36.98           C  
ANISOU 2983  CB  LYS A 384     7576   2896   3579    505   2489   -151       C  
ATOM   2984  CG  LYS A 384      27.198 106.421 -24.807  1.00 37.25           C  
ANISOU 2984  CG  LYS A 384     7579   3044   3529    567   2441   -174       C  
ATOM   2985  CD  LYS A 384      27.045 104.952 -25.167  1.00 37.68           C  
ANISOU 2985  CD  LYS A 384     7634   3103   3580    627   2400   -243       C  
ATOM   2986  CE  LYS A 384      28.390 104.331 -25.504  1.00 38.07           C  
ANISOU 2986  CE  LYS A 384     7645   3277   3543    700   2346   -284       C  
ATOM   2987  NZ  LYS A 384      28.330 102.844 -25.475  1.00 38.55           N1+
ANISOU 2987  NZ  LYS A 384     7727   3304   3615    762   2299   -357       N1+
ATOM   2988  N   GLU A 385      23.811 108.997 -22.816  1.00 38.85           N  
ANISOU 2988  N   GLU A 385     7845   2951   3965    375   2587   -101       N  
ATOM   2989  CA  GLU A 385      22.546 109.721 -22.771  1.00 38.91           C  
ANISOU 2989  CA  GLU A 385     7844   2908   4031    343   2614   -118       C  
ATOM   2990  C   GLU A 385      22.775 111.205 -22.518  1.00 38.83           C  
ANISOU 2990  C   GLU A 385     7854   2880   4018    326   2628    -96       C  
ATOM   2991  O   GLU A 385      22.246 112.057 -23.241  1.00 39.02           O  
ANISOU 2991  O   GLU A 385     7892   2886   4049    329   2629   -110       O  
ATOM   2992  CB  GLU A 385      21.640 109.123 -21.695  1.00 38.95           C  
ANISOU 2992  CB  GLU A 385     7833   2872   4095    306   2643   -134       C  
ATOM   2993  CG  GLU A 385      20.242 109.717 -21.651  1.00 39.14           C  
ANISOU 2993  CG  GLU A 385     7822   2866   4182    281   2661   -173       C  
ATOM   2994  CD  GLU A 385      19.525 109.610 -22.980  1.00 39.36           C  
ANISOU 2994  CD  GLU A 385     7836   2894   4225    307   2634   -211       C  
ATOM   2995  OE1 GLU A 385      19.182 110.663 -23.560  1.00 39.44           O  
ANISOU 2995  OE1 GLU A 385     7843   2895   4248    314   2622   -224       O  
ATOM   2996  OE2 GLU A 385      19.320 108.473 -23.455  1.00 39.52           O1+
ANISOU 2996  OE2 GLU A 385     7854   2917   4245    323   2621   -231       O1+
ATOM   2997  N   LEU A 386      23.571 111.533 -21.495  1.00 36.29           N  
ANISOU 2997  N   LEU A 386     7544   2557   3688    311   2635    -65       N  
ATOM   2998  CA  LEU A 386      23.834 112.932 -21.171  1.00 36.32           C  
ANISOU 2998  CA  LEU A 386     7577   2535   3688    299   2647    -50       C  
ATOM   2999  C   LEU A 386      24.514 113.664 -22.320  1.00 36.52           C  
ANISOU 2999  C   LEU A 386     7650   2579   3646    316   2641    -28       C  
ATOM   3000  O   LEU A 386      24.291 114.864 -22.511  1.00 36.77           O  
ANISOU 3000  O   LEU A 386     7732   2563   3675    307   2656    -29       O  
ATOM   3001  CB  LEU A 386      24.702 113.025 -19.915  1.00 36.10           C  
ANISOU 3001  CB  LEU A 386     7551   2509   3656    287   2649    -25       C  
ATOM   3002  CG  LEU A 386      24.155 112.475 -18.594  1.00 36.03           C  
ANISOU 3002  CG  LEU A 386     7508   2490   3693    265   2666    -41       C  
ATOM   3003  CD1 LEU A 386      25.223 112.512 -17.509  1.00 35.84           C  
ANISOU 3003  CD1 LEU A 386     7493   2473   3651    263   2660    -14       C  
ATOM   3004  CD2 LEU A 386      22.928 113.248 -18.160  1.00 36.30           C  
ANISOU 3004  CD2 LEU A 386     7511   2502   3778    249   2684    -87       C  
ATOM   3005  N   GLY A 387      25.341 112.971 -23.092  1.00 37.38           N  
ANISOU 3005  N   GLY A 387     7743   2769   3692    341   2616    -14       N  
ATOM   3006  CA  GLY A 387      26.136 113.627 -24.111  1.00 37.71           C  
ANISOU 3006  CA  GLY A 387     7802   2887   3639    344   2607     21       C  
ATOM   3007  C   GLY A 387      25.563 113.558 -25.512  1.00 38.09           C  
ANISOU 3007  C   GLY A 387     7852   2976   3643    359   2606     11       C  
ATOM   3008  O   GLY A 387      26.302 113.702 -26.491  1.00 38.47           O  
ANISOU 3008  O   GLY A 387     7877   3151   3588    357   2583     53       O  
ATOM   3009  N   LYS A 388      24.250 113.350 -25.632  1.00 38.88           N  
ANISOU 3009  N   LYS A 388     7962   2992   3817    367   2621    -39       N  
ATOM   3010  CA  LYS A 388      23.633 113.256 -26.953  1.00 39.25           C  
ANISOU 3010  CA  LYS A 388     8014   3068   3830    389   2618    -61       C  
ATOM   3011  C   LYS A 388      23.636 114.609 -27.660  1.00 39.78           C  
ANISOU 3011  C   LYS A 388     8135   3139   3841    354   2617     -5       C  
ATOM   3012  O   LYS A 388      24.282 114.780 -28.699  1.00 40.27           O  
ANISOU 3012  O   LYS A 388     8161   3335   3805    334   2570     69       O  
ATOM   3013  CB  LYS A 388      22.210 112.702 -26.832  1.00 39.30           C  
ANISOU 3013  CB  LYS A 388     7992   2991   3948    398   2609   -127       C  
ATOM   3014  CG  LYS A 388      22.061 111.286 -27.363  1.00 39.32           C  
ANISOU 3014  CG  LYS A 388     7941   3052   3948    434   2579   -163       C  
ATOM   3015  CD  LYS A 388      20.636 110.775 -27.222  1.00 39.46           C  
ANISOU 3015  CD  LYS A 388     7922   3001   4069    427   2567   -216       C  
ATOM   3016  CE  LYS A 388      20.488 109.385 -27.827  1.00 39.36           C  
ANISOU 3016  CE  LYS A 388     7874   3031   4051    467   2534   -258       C  
ATOM   3017  NZ  LYS A 388      20.705 109.400 -29.301  1.00 40.13           N1+
ANISOU 3017  NZ  LYS A 388     7976   3201   4070    519   2514   -281       N1+
ATOM   3018  N   ARG A 389      22.923 115.587 -27.107  1.00 39.27           N  
ANISOU 3018  N   ARG A 389     8082   2947   3891    324   2577     -7       N  
ATOM   3019  CA  ARG A 389      22.886 116.941 -27.656  1.00 39.95           C  
ANISOU 3019  CA  ARG A 389     8153   3016   4009    263   2462     83       C  
ATOM   3020  C   ARG A 389      23.871 117.862 -26.946  1.00 39.86           C  
ANISOU 3020  C   ARG A 389     8158   3003   3986    211   2429    164       C  
ATOM   3021  O   ARG A 389      23.547 119.014 -26.640  1.00 40.19           O  
ANISOU 3021  O   ARG A 389     8208   2940   4122    176   2340    188       O  
ATOM   3022  CB  ARG A 389      21.470 117.505 -27.574  1.00 40.08           C  
ANISOU 3022  CB  ARG A 389     8170   2889   4170    272   2409     17       C  
ATOM   3023  CG  ARG A 389      20.402 116.651 -28.250  1.00 40.17           C  
ANISOU 3023  CG  ARG A 389     8163   2892   4208    318   2434    -66       C  
ATOM   3024  CD  ARG A 389      20.434 116.790 -29.764  1.00 41.14           C  
ANISOU 3024  CD  ARG A 389     8255   3105   4271    298   2358      4       C  
ATOM   3025  NE  ARG A 389      19.420 115.955 -30.406  1.00 41.36           N  
ANISOU 3025  NE  ARG A 389     8265   3122   4328    349   2378    -84       N  
ATOM   3026  CZ  ARG A 389      19.220 115.894 -31.718  1.00 42.29           C  
ANISOU 3026  CZ  ARG A 389     8352   3315   4400    349   2321    -53       C  
ATOM   3027  NH1 ARG A 389      18.276 115.106 -32.212  1.00 42.51           N1+
ANISOU 3027  NH1 ARG A 389     8365   3322   4464    400   2339   -144       N1+
ATOM   3028  NH2 ARG A 389      19.965 116.622 -32.539  1.00 43.03           N  
ANISOU 3028  NH2 ARG A 389     8426   3513   4409    293   2242     72       N  
ATOM   3029  N   LYS A 390      25.089 117.377 -26.690  1.00 38.50           N  
ANISOU 3029  N   LYS A 390     7987   2940   3701    210   2488    200       N  
ATOM   3030  CA  LYS A 390      26.051 118.085 -25.852  1.00 38.50           C  
ANISOU 3030  CA  LYS A 390     8004   2935   3690    170   2474    261       C  
ATOM   3031  C   LYS A 390      27.415 117.401 -25.905  1.00 38.37           C  
ANISOU 3031  C   LYS A 390     7975   3080   3526    174   2535    301       C  
ATOM   3032  O   LYS A 390      27.504 116.185 -25.704  1.00 37.94           O  
ANISOU 3032  O   LYS A 390     7883   3065   3466    240   2575    213       O  
ATOM   3033  CB  LYS A 390      25.533 118.146 -24.414  1.00 38.05           C  
ANISOU 3033  CB  LYS A 390     7984   2739   3736    207   2520    165       C  
ATOM   3034  CG  LYS A 390      26.333 119.017 -23.474  1.00 38.13           C  
ANISOU 3034  CG  LYS A 390     8012   2715   3760    174   2488    209       C  
ATOM   3035  CD  LYS A 390      25.454 119.511 -22.337  1.00 38.06           C  
ANISOU 3035  CD  LYS A 390     8022   2559   3880    205   2482    112       C  
ATOM   3036  CE  LYS A 390      24.272 120.304 -22.876  1.00 38.59           C  
ANISOU 3036  CE  LYS A 390     8073   2526   4063    200   2377     87       C  
ATOM   3037  NZ  LYS A 390      23.493 120.968 -21.796  1.00 38.75           N1+
ANISOU 3037  NZ  LYS A 390     8097   2421   4206    237   2347    -16       N1+
ATOM   3038  N   ARG A 391      28.484 118.159 -26.169  1.00 39.75           N  
ANISOU 3038  N   ARG A 391     8126   3347   3629    102   2477    423       N  
ATOM   3039  CA  ARG A 391      29.795 117.537 -26.297  1.00 39.76           C  
ANISOU 3039  CA  ARG A 391     8023   3535   3548    115   2453    425       C  
ATOM   3040  C   ARG A 391      30.786 118.109 -25.291  1.00 39.68           C  
ANISOU 3040  C   ARG A 391     8005   3519   3553     83   2428    459       C  
ATOM   3041  O   ARG A 391      30.732 119.302 -24.974  1.00 40.01           O  
ANISOU 3041  O   ARG A 391     8105   3465   3632     15   2391    542       O  
ATOM   3042  CB  ARG A 391      30.365 117.709 -27.717  1.00 40.58           C  
ANISOU 3042  CB  ARG A 391     8048   3840   3531     61   2391    527       C  
ATOM   3043  CG  ARG A 391      30.550 119.149 -28.165  1.00 41.42           C  
ANISOU 3043  CG  ARG A 391     8175   3944   3619    -62   2308    695       C  
ATOM   3044  CD  ARG A 391      30.993 119.218 -29.623  1.00 42.36           C  
ANISOU 3044  CD  ARG A 391     8204   4284   3607   -121   2249    799       C  
ATOM   3045  NE  ARG A 391      32.389 118.826 -29.807  1.00 42.68           N  
ANISOU 3045  NE  ARG A 391     8112   4568   3538   -128   2228    816       N  
ATOM   3046  CZ  ARG A 391      32.968 118.662 -30.992  1.00 43.56           C  
ANISOU 3046  CZ  ARG A 391     8111   4931   3508   -163   2192    881       C  
ATOM   3047  NH1 ARG A 391      32.269 118.848 -32.103  1.00 44.15           N1+
ANISOU 3047  NH1 ARG A 391     8196   5044   3534   -193   2171    938       N1+
ATOM   3048  NH2 ARG A 391      34.245 118.308 -31.071  1.00 43.92           N  
ANISOU 3048  NH2 ARG A 391     8030   5203   3453   -165   2177    887       N  
ATOM   3049  N   PRO A 392      31.694 117.285 -24.769  1.00 38.44           N  
ANISOU 3049  N   PRO A 392     7778   3448   3378    130   2431    402       N  
ATOM   3050  CA  PRO A 392      32.705 117.793 -23.837  1.00 38.39           C  
ANISOU 3050  CA  PRO A 392     7761   3449   3377    103   2409    432       C  
ATOM   3051  C   PRO A 392      33.681 118.732 -24.526  1.00 39.24           C  
ANISOU 3051  C   PRO A 392     7810   3699   3398      4   2334    573       C  
ATOM   3052  O   PRO A 392      33.929 118.640 -25.730  1.00 39.85           O  
ANISOU 3052  O   PRO A 392     7816   3940   3384    -30   2299    636       O  
ATOM   3053  CB  PRO A 392      33.415 116.522 -23.351  1.00 37.92           C  
ANISOU 3053  CB  PRO A 392     7633   3463   3312    177   2418    346       C  
ATOM   3054  CG  PRO A 392      32.461 115.407 -23.643  1.00 37.58           C  
ANISOU 3054  CG  PRO A 392     7600   3372   3308    244   2448    261       C  
ATOM   3055  CD  PRO A 392      31.745 115.819 -24.893  1.00 38.07           C  
ANISOU 3055  CD  PRO A 392     7675   3464   3327    213   2447    306       C  
ATOM   3056  N   ARG A 393      34.241 119.645 -23.736  1.00 39.37           N  
ANISOU 3056  N   ARG A 393     7855   3661   3443    -48   2304    629       N  
ATOM   3057  CA  ARG A 393      35.200 120.614 -24.240  1.00 40.28           C  
ANISOU 3057  CA  ARG A 393     7914   3895   3495   -161   2216    782       C  
ATOM   3058  C   ARG A 393      36.167 120.975 -23.124  1.00 40.15           C  
ANISOU 3058  C   ARG A 393     7897   3862   3497   -172   2205    785       C  
ATOM   3059  O   ARG A 393      35.879 120.785 -21.940  1.00 39.45           O  
ANISOU 3059  O   ARG A 393     7877   3628   3483   -104   2259    685       O  
ATOM   3060  CB  ARG A 393      34.507 121.878 -24.763  1.00 41.02           C  
ANISOU 3060  CB  ARG A 393     8075   3875   3636   -261   2136    909       C  
ATOM   3061  CG  ARG A 393      33.876 122.710 -23.659  1.00 40.81           C  
ANISOU 3061  CG  ARG A 393     8171   3592   3744   -259   2122    888       C  
ATOM   3062  CD  ARG A 393      33.183 123.948 -24.196  1.00 41.68           C  
ANISOU 3062  CD  ARG A 393     8341   3559   3937   -351   1998   1008       C  
ATOM   3063  NE  ARG A 393      32.476 124.664 -23.137  1.00 41.55           N  
ANISOU 3063  NE  ARG A 393     8407   3298   4083   -318   1952    939       N  
ATOM   3064  CZ  ARG A 393      33.009 125.638 -22.407  1.00 42.01           C  
ANISOU 3064  CZ  ARG A 393     8484   3265   4213   -365   1854    985       C  
ATOM   3065  NH1 ARG A 393      34.260 126.022 -22.621  1.00 42.60           N1+
ANISOU 3065  NH1 ARG A 393     8517   3462   4207   -462   1804   1122       N1+
ATOM   3066  NH2 ARG A 393      32.290 126.230 -21.464  1.00 41.97           N  
ANISOU 3066  NH2 ARG A 393     8521   3062   4363   -309   1794    881       N  
ATOM   3067  N   VAL A 394      37.321 121.505 -23.515  1.00 40.93           N  
ANISOU 3067  N   VAL A 394     7911   4121   3519   -262   2136    905       N  
ATOM   3068  CA  VAL A 394      38.288 122.009 -22.547  1.00 40.98           C  
ANISOU 3068  CA  VAL A 394     7918   4114   3540   -290   2114    931       C  
ATOM   3069  C   VAL A 394      37.913 123.438 -22.178  1.00 41.51           C  
ANISOU 3069  C   VAL A 394     8081   3990   3701   -379   2033   1032       C  
ATOM   3070  O   VAL A 394      37.646 124.271 -23.053  1.00 42.41           O  
ANISOU 3070  O   VAL A 394     8194   4098   3822   -483   1937   1168       O  
ATOM   3071  CB  VAL A 394      39.717 121.930 -23.108  1.00 41.70           C  
ANISOU 3071  CB  VAL A 394     7867   4469   3506   -352   2073   1017       C  
ATOM   3072  CG1 VAL A 394      40.210 120.493 -23.097  1.00 41.13           C  
ANISOU 3072  CG1 VAL A 394     7712   4546   3371   -242   2138    887       C  
ATOM   3073  CG2 VAL A 394      39.775 122.499 -24.519  1.00 42.86           C  
ANISOU 3073  CG2 VAL A 394     7942   4770   3575   -470   1996   1178       C  
ATOM   3074  N   CYS A 395      37.872 123.722 -20.881  1.00 41.05           N  
ANISOU 3074  N   CYS A 395     8107   3767   3723   -336   2056    966       N  
ATOM   3075  CA  CYS A 395      37.623 125.074 -20.410  1.00 41.65           C  
ANISOU 3075  CA  CYS A 395     8272   3648   3907   -407   1955   1046       C  
ATOM   3076  C   CYS A 395      38.935 125.845 -20.341  1.00 42.49           C  
ANISOU 3076  C   CYS A 395     8322   3839   3982   -515   1860   1179       C  
ATOM   3077  O   CYS A 395      40.010 125.265 -20.163  1.00 42.29           O  
ANISOU 3077  O   CYS A 395     8216   3990   3864   -500   1910   1163       O  
ATOM   3078  CB  CYS A 395      36.936 125.059 -19.045  1.00 40.93           C  
ANISOU 3078  CB  CYS A 395     8292   3346   3915   -307   2020    909       C  
ATOM   3079  SG  CYS A 395      35.197 124.562 -19.103  1.00 40.34           S  
ANISOU 3079  SG  CYS A 395     8294   3123   3910   -215   2096    787       S  
ATOM   3080  N   THR A 396      38.838 127.161 -20.488  1.00 43.52           N  
ANISOU 3080  N   THR A 396     8492   3839   4203   -626   1705   1311       N  
ATOM   3081  CA  THR A 396      40.005 128.007 -20.682  1.00 44.62           C  
ANISOU 3081  CA  THR A 396     8569   4065   4320   -762   1583   1478       C  
ATOM   3082  C   THR A 396      40.379 128.746 -19.401  1.00 44.71           C  
ANISOU 3082  C   THR A 396     8658   3897   4432   -758   1528   1457       C  
ATOM   3083  O   THR A 396      39.586 128.869 -18.465  1.00 44.17           O  
ANISOU 3083  O   THR A 396     8697   3611   4474   -663   1548   1331       O  
ATOM   3084  CB  THR A 396      39.756 129.019 -21.804  1.00 46.01           C  
ANISOU 3084  CB  THR A 396     8720   4224   4537   -911   1407   1665       C  
ATOM   3085  OG1 THR A 396      38.937 130.089 -21.315  1.00 46.46           O  
ANISOU 3085  OG1 THR A 396     8890   3983   4781   -923   1263   1664       O  
ATOM   3086  CG2 THR A 396      39.052 128.350 -22.976  1.00 45.87           C  
ANISOU 3086  CG2 THR A 396     8660   4323   4444   -894   1461   1661       C  
ATOM   3087  N   LYS A 397      41.622 129.234 -19.379  1.00 45.49           N  
ANISOU 3087  N   LYS A 397     8691   4104   4488   -861   1458   1580       N  
ATOM   3088  CA  LYS A 397      42.062 130.110 -18.298  1.00 45.86           C  
ANISOU 3088  CA  LYS A 397     8808   3979   4639   -882   1368   1590       C  
ATOM   3089  C   LYS A 397      41.219 131.378 -18.246  1.00 46.79           C  
ANISOU 3089  C   LYS A 397     9011   3819   4948   -932   1167   1635       C  
ATOM   3090  O   LYS A 397      40.900 131.879 -17.161  1.00 46.70           O  
ANISOU 3090  O   LYS A 397     9094   3583   5068   -864   1116   1537       O  
ATOM   3091  CB  LYS A 397      43.544 130.445 -18.480  1.00 46.74           C  
ANISOU 3091  CB  LYS A 397     8819   4272   4669  -1005   1312   1739       C  
ATOM   3092  CG  LYS A 397      43.947 131.837 -18.021  1.00 47.98           C  
ANISOU 3092  CG  LYS A 397     9018   4251   4961  -1117   1110   1855       C  
ATOM   3093  CD  LYS A 397      45.392 132.134 -18.384  1.00 49.01           C  
ANISOU 3093  CD  LYS A 397     9027   4595   4999  -1256   1058   2024       C  
ATOM   3094  CE  LYS A 397      45.790 133.537 -17.961  1.00 50.38           C  
ANISOU 3094  CE  LYS A 397     9235   4584   5324  -1375    834   2145       C  
ATOM   3095  NZ  LYS A 397      47.201 133.843 -18.323  1.00 51.52           N1+
ANISOU 3095  NZ  LYS A 397     9250   4945   5379  -1517    788   2316       N1+
ATOM   3096  N   GLU A 398      40.837 131.902 -19.414  1.00 47.89           N  
ANISOU 3096  N   GLU A 398     9108   3975   5112  -1040   1037   1772       N  
ATOM   3097  CA  GLU A 398      40.001 133.097 -19.460  1.00 48.91           C  
ANISOU 3097  CA  GLU A 398     9301   3844   5438  -1081    814   1806       C  
ATOM   3098  C   GLU A 398      38.645 132.856 -18.808  1.00 48.01           C  
ANISOU 3098  C   GLU A 398     9292   3517   5431   -917    867   1596       C  
ATOM   3099  O   GLU A 398      38.054 133.784 -18.243  1.00 48.63           O  
ANISOU 3099  O   GLU A 398     9422   3358   5697   -883    697   1531       O  
ATOM   3100  CB  GLU A 398      39.827 133.555 -20.908  1.00 50.11           C  
ANISOU 3100  CB  GLU A 398     9378   4084   5578  -1220    683   1990       C  
ATOM   3101  CG  GLU A 398      41.137 133.694 -21.676  1.00 51.13           C  
ANISOU 3101  CG  GLU A 398     9370   4479   5579  -1376    655   2197       C  
ATOM   3102  CD  GLU A 398      41.542 132.415 -22.386  1.00 50.34           C  
ANISOU 3102  CD  GLU A 398     9173   4697   5258  -1347    867   2186       C  
ATOM   3103  OE1 GLU A 398      40.757 131.928 -23.228  1.00 50.08           O  
ANISOU 3103  OE1 GLU A 398     9130   4719   5179  -1319    917   2168       O  
ATOM   3104  OE2 GLU A 398      42.640 131.891 -22.099  1.00 50.05           O1+
ANISOU 3104  OE2 GLU A 398     9064   4852   5099  -1342    973   2184       O1+
ATOM   3105  N   GLU A 399      38.139 131.623 -18.874  1.00 47.90           N  
ANISOU 3105  N   GLU A 399     9277   3609   5312   -805   1085   1472       N  
ATOM   3106  CA  GLU A 399      36.910 131.277 -18.168  1.00 47.03           C  
ANISOU 3106  CA  GLU A 399     9211   3363   5297   -639   1149   1251       C  
ATOM   3107  C   GLU A 399      37.139 131.220 -16.663  1.00 46.47           C  
ANISOU 3107  C   GLU A 399     9168   3217   5272   -528   1203   1095       C  
ATOM   3108  O   GLU A 399      36.339 131.751 -15.882  1.00 46.64           O  
ANISOU 3108  O   GLU A 399     9222   3058   5440   -437   1121    953       O  
ATOM   3109  CB  GLU A 399      36.379 129.933 -18.669  1.00 45.88           C  
ANISOU 3109  CB  GLU A 399     9048   3361   5024   -565   1359   1178       C  
ATOM   3110  CG  GLU A 399      35.447 130.010 -19.859  1.00 46.27           C  
ANISOU 3110  CG  GLU A 399     9087   3397   5094   -601   1300   1228       C  
ATOM   3111  CD  GLU A 399      35.113 128.638 -20.410  1.00 45.22           C  
ANISOU 3111  CD  GLU A 399     8932   3428   4822   -537   1503   1168       C  
ATOM   3112  OE1 GLU A 399      35.990 128.032 -21.063  1.00 45.15           O  
ANISOU 3112  OE1 GLU A 399     8864   3639   4653   -591   1582   1260       O  
ATOM   3113  OE2 GLU A 399      33.982 128.158 -20.176  1.00 44.56           O1+
ANISOU 3113  OE2 GLU A 399     8870   3266   4792   -427   1570   1017       O1+
ATOM   3114  N   PHE A 400      38.228 130.571 -16.243  1.00 44.54           N  
ANISOU 3114  N   PHE A 400     8905   3122   4895   -528   1338   1111       N  
ATOM   3115  CA  PHE A 400      38.482 130.348 -14.823  1.00 43.91           C  
ANISOU 3115  CA  PHE A 400     8851   3001   4832   -418   1415    963       C  
ATOM   3116  C   PHE A 400      38.629 131.663 -14.066  1.00 44.94           C  
ANISOU 3116  C   PHE A 400     9004   2944   5127   -431   1209    951       C  
ATOM   3117  O   PHE A 400      38.215 131.768 -12.906  1.00 44.69           O  
ANISOU 3117  O   PHE A 400     8999   2808   5173   -310   1216    779       O  
ATOM   3118  CB  PHE A 400      39.735 129.485 -14.664  1.00 43.28           C  
ANISOU 3118  CB  PHE A 400     8746   3120   4580   -433   1570   1007       C  
ATOM   3119  CG  PHE A 400      40.063 129.134 -13.240  1.00 42.61           C  
ANISOU 3119  CG  PHE A 400     8688   3012   4490   -323   1663    865       C  
ATOM   3120  CD1 PHE A 400      39.482 128.035 -12.633  1.00 41.48           C  
ANISOU 3120  CD1 PHE A 400     8566   2901   4294   -193   1842    709       C  
ATOM   3121  CD2 PHE A 400      40.973 129.888 -12.518  1.00 43.19           C  
ANISOU 3121  CD2 PHE A 400     8764   3039   4608   -357   1565    897       C  
ATOM   3122  CE1 PHE A 400      39.788 127.704 -11.327  1.00 40.97           C  
ANISOU 3122  CE1 PHE A 400     8525   2827   4214   -101   1924    591       C  
ATOM   3123  CE2 PHE A 400      41.283 129.562 -11.211  1.00 42.61           C  
ANISOU 3123  CE2 PHE A 400     8714   2954   4523   -253   1650    766       C  
ATOM   3124  CZ  PHE A 400      40.689 128.468 -10.616  1.00 41.51           C  
ANISOU 3124  CZ  PHE A 400     8596   2854   4322   -126   1830    616       C  
ATOM   3125  N   ILE A 401      39.214 132.676 -14.708  1.00 46.22           N  
ANISOU 3125  N   ILE A 401     9154   3067   5342   -580   1014   1133       N  
ATOM   3126  CA  ILE A 401      39.437 133.960 -14.046  1.00 47.39           C  
ANISOU 3126  CA  ILE A 401     9326   3024   5657   -603    788   1136       C  
ATOM   3127  C   ILE A 401      38.111 134.593 -13.647  1.00 47.80           C  
ANISOU 3127  C   ILE A 401     9412   2858   5893   -496    657    975       C  
ATOM   3128  O   ILE A 401      37.937 135.053 -12.512  1.00 48.01           O  
ANISOU 3128  O   ILE A 401     9459   2756   6026   -392    592    821       O  
ATOM   3129  CB  ILE A 401      40.260 134.892 -14.955  1.00 48.87           C  
ANISOU 3129  CB  ILE A 401     9490   3213   5865   -807    590   1389       C  
ATOM   3130  CG1 ILE A 401      41.747 134.541 -14.872  1.00 48.75           C  
ANISOU 3130  CG1 ILE A 401     9433   3387   5701   -893    680   1507       C  
ATOM   3131  CG2 ILE A 401      40.015 136.354 -14.599  1.00 50.39           C  
ANISOU 3131  CG2 ILE A 401     9719   3144   6284   -835    290   1395       C  
ATOM   3132  CD1 ILE A 401      42.605 135.267 -15.886  1.00 50.20           C  
ANISOU 3132  CD1 ILE A 401     9571   3643   5860  -1113    523   1777       C  
ATOM   3133  N   ASN A 402      37.151 134.618 -14.568  1.00 48.36           N  
ANISOU 3133  N   ASN A 402     9484   2894   5997   -512    617    997       N  
ATOM   3134  CA  ASN A 402      35.856 135.230 -14.307  1.00 48.88           C  
ANISOU 3134  CA  ASN A 402     9574   2763   6235   -411    482    844       C  
ATOM   3135  C   ASN A 402      34.928 134.338 -13.489  1.00 47.66           C  
ANISOU 3135  C   ASN A 402     9417   2644   6049   -229    679    602       C  
ATOM   3136  O   ASN A 402      33.711 134.562 -13.504  1.00 47.91           O  
ANISOU 3136  O   ASN A 402     9451   2571   6181   -145    619    474       O  
ATOM   3137  CB  ASN A 402      35.184 135.618 -15.626  1.00 49.64           C  
ANISOU 3137  CB  ASN A 402     9672   2809   6381   -501    353    965       C  
ATOM   3138  CG  ASN A 402      35.970 136.663 -16.394  1.00 51.19           C  
ANISOU 3138  CG  ASN A 402     9871   2948   6633   -692    116   1211       C  
ATOM   3139  OD1 ASN A 402      36.859 136.334 -17.178  1.00 51.18           O  
ANISOU 3139  OD1 ASN A 402     9831   3127   6489   -831    180   1407       O  
ATOM   3140  ND2 ASN A 402      35.648 137.933 -16.168  1.00 52.68           N  
ANISOU 3140  ND2 ASN A 402    10044   2940   7030   -691   -166   1185       N  
ATOM   3141  N   LYS A 403      35.461 133.342 -12.775  1.00 48.83           N  
ANISOU 3141  N   LYS A 403     9555   2938   6058   -171    903    540       N  
ATOM   3142  CA  LYS A 403      34.640 132.473 -11.941  1.00 47.74           C  
ANISOU 3142  CA  LYS A 403     9413   2846   5880    -17   1086    331       C  
ATOM   3143  C   LYS A 403      35.230 132.264 -10.550  1.00 47.58           C  
ANISOU 3143  C   LYS A 403     9396   2858   5823     68   1170    218       C  
ATOM   3144  O   LYS A 403      34.690 131.465  -9.776  1.00 46.67           O  
ANISOU 3144  O   LYS A 403     9275   2808   5651    181   1337     63       O  
ATOM   3145  CB  LYS A 403      34.423 131.116 -12.621  1.00 46.43           C  
ANISOU 3145  CB  LYS A 403     9235   2848   5557    -23   1313    363       C  
ATOM   3146  CG  LYS A 403      33.094 130.465 -12.266  1.00 45.57           C  
ANISOU 3146  CG  LYS A 403     9118   2739   5457    101   1429    181       C  
ATOM   3147  CD  LYS A 403      33.120 128.963 -12.481  1.00 44.24           C  
ANISOU 3147  CD  LYS A 403     8945   2740   5124    115   1674    185       C  
ATOM   3148  CE  LYS A 403      31.843 128.323 -11.960  1.00 43.49           C  
ANISOU 3148  CE  LYS A 403     8838   2647   5039    229   1787      7       C  
ATOM   3149  NZ  LYS A 403      31.956 126.841 -11.883  1.00 42.34           N1+
ANISOU 3149  NZ  LYS A 403     8695   2648   4744    250   2013     -1       N1+
ATOM   3150  N   VAL A 404      36.316 132.951 -10.207  1.00 49.59           N  
ANISOU 3150  N   VAL A 404     9660   3076   6108     10   1058    296       N  
ATOM   3151  CA  VAL A 404      36.883 132.893  -8.864  1.00 49.38           C  
ANISOU 3151  CA  VAL A 404     9637   3065   6062     92   1109    185       C  
ATOM   3152  C   VAL A 404      36.346 134.081  -8.075  1.00 50.58           C  
ANISOU 3152  C   VAL A 404     9790   3032   6396    178    897     38       C  
ATOM   3153  O   VAL A 404      36.575 135.241  -8.439  1.00 51.85           O  
ANISOU 3153  O   VAL A 404     9961   3045   6694    106    652    119       O  
ATOM   3154  CB  VAL A 404      38.422 132.868  -8.890  1.00 49.35           C  
ANISOU 3154  CB  VAL A 404     9634   3142   5973    -11   1121    341       C  
ATOM   3155  CG1 VAL A 404      38.916 131.527  -9.413  1.00 48.12           C  
ANISOU 3155  CG1 VAL A 404     9469   3193   5623    -48   1354    424       C  
ATOM   3156  CG2 VAL A 404      38.989 133.999  -9.738  1.00 50.65           C  
ANISOU 3156  CG2 VAL A 404     9798   3213   6233   -162    885    529       C  
ATOM   3157  N   ARG A 405      35.610 133.795  -7.006  1.00 57.47           N  
ANISOU 3157  N   ARG A 405    10648   3918   7269    330    981   -180       N  
ATOM   3158  CA  ARG A 405      35.014 134.840  -6.184  1.00 58.37           C  
ANISOU 3158  CA  ARG A 405    10750   3885   7544    441    791   -361       C  
ATOM   3159  C   ARG A 405      36.108 135.558  -5.396  1.00 59.62           C  
ANISOU 3159  C   ARG A 405    10920   3984   7751    436    668   -353       C  
ATOM   3160  O   ARG A 405      37.307 135.312  -5.559  1.00 60.24           O  
ANISOU 3160  O   ARG A 405    11014   4128   7745    335    720   -196       O  
ATOM   3161  CB  ARG A 405      33.961 134.256  -5.248  1.00 57.03           C  
ANISOU 3161  CB  ARG A 405    10498   3840   7330    593    923   -587       C  
ATOM   3162  CG  ARG A 405      32.752 133.640  -5.925  1.00 56.05           C  
ANISOU 3162  CG  ARG A 405    10333   3785   7179    605   1014   -616       C  
ATOM   3163  CD  ARG A 405      31.631 133.453  -4.912  1.00 55.46           C  
ANISOU 3163  CD  ARG A 405    10140   3825   7106    746   1057   -845       C  
ATOM   3164  NE  ARG A 405      31.130 132.082  -4.870  1.00 53.79           N  
ANISOU 3164  NE  ARG A 405     9888   3811   6739    750   1304   -848       N  
ATOM   3165  CZ  ARG A 405      30.318 131.616  -3.927  1.00 53.61           C  
ANISOU 3165  CZ  ARG A 405     9756   3946   6668    839   1389  -1001       C  
ATOM   3166  NH1 ARG A 405      29.920 132.410  -2.942  1.00 54.72           N1+
ANISOU 3166  NH1 ARG A 405     9816   4080   6894    946   1261  -1184       N1+
ATOM   3167  NH2 ARG A 405      29.908 130.355  -3.963  1.00 52.61           N  
ANISOU 3167  NH2 ARG A 405     9594   3986   6409    815   1589   -967       N  
ATOM   3168  N   SER A 406      35.689 136.466  -4.514  1.00 58.38           N  
ANISOU 3168  N   SER A 406    10730   3721   7730    551    493   -536       N  
ATOM   3169  CA  SER A 406      36.638 137.081  -3.594  1.00 59.16           C  
ANISOU 3169  CA  SER A 406    10840   3765   7874    575    388   -569       C  
ATOM   3170  C   SER A 406      37.091 136.084  -2.536  1.00 57.71           C  
ANISOU 3170  C   SER A 406    10646   3762   7520    649    636   -650       C  
ATOM   3171  O   SER A 406      38.259 136.086  -2.129  1.00 58.16           O  
ANISOU 3171  O   SER A 406    10730   3837   7532    608    650   -578       O  
ATOM   3172  CB  SER A 406      36.014 138.313  -2.942  1.00 59.85           C  
ANISOU 3172  CB  SER A 406    10849   3732   8159    686    121   -757       C  
ATOM   3173  OG  SER A 406      35.468 139.181  -3.918  1.00 60.95           O  
ANISOU 3173  OG  SER A 406    10979   3720   8460    624   -108   -691       O  
ATOM   3174  N   ASN A 407      36.186 135.214  -2.089  1.00 58.84           N  
ANISOU 3174  N   ASN A 407    10716   4075   7566    742    819   -782       N  
ATOM   3175  CA  ASN A 407      36.489 134.210  -1.072  1.00 57.57           C  
ANISOU 3175  CA  ASN A 407    10521   4114   7240    802   1042   -847       C  
ATOM   3176  C   ASN A 407      36.820 132.855  -1.684  1.00 56.36           C  
ANISOU 3176  C   ASN A 407    10413   4089   6911    719   1293   -701       C  
ATOM   3177  O   ASN A 407      36.419 131.812  -1.161  1.00 54.24           O  
ANISOU 3177  O   ASN A 407    10084   4010   6516    762   1477   -755       O  
ATOM   3178  CB  ASN A 407      35.334 134.089  -0.079  1.00 56.86           C  
ANISOU 3178  CB  ASN A 407    10298   4160   7148    938   1067  -1068       C  
ATOM   3179  CG  ASN A 407      33.996 133.818  -0.751  1.00 56.57           C  
ANISOU 3179  CG  ASN A 407    10208   4155   7130    947   1093  -1106       C  
ATOM   3180  OD1 ASN A 407      33.923 133.177  -1.800  1.00 55.62           O  
ANISOU 3180  OD1 ASN A 407    10141   4038   6953    857   1195   -964       O  
ATOM   3181  ND2 ASN A 407      32.924 134.308  -0.138  1.00 57.33           N  
ANISOU 3181  ND2 ASN A 407    10193   4283   7308   1060    999  -1307       N  
ATOM   3182  N   ALA A 408      37.539 132.844  -2.802  1.00 51.85           N  
ANISOU 3182  N   ALA A 408     9928   3439   6333    591   1284   -505       N  
ATOM   3183  CA  ALA A 408      38.101 131.607  -3.321  1.00 50.80           C  
ANISOU 3183  CA  ALA A 408     9814   3455   6034    515   1496   -369       C  
ATOM   3184  C   ALA A 408      39.379 131.291  -2.556  1.00 51.05           C  
ANISOU 3184  C   ALA A 408     9860   3565   5971    512   1569   -338       C  
ATOM   3185  O   ALA A 408      40.253 132.151  -2.408  1.00 52.92           O  
ANISOU 3185  O   ALA A 408    10102   3726   6278    470   1418   -285       O  
ATOM   3186  CB  ALA A 408      38.382 131.724  -4.819  1.00 51.93           C  
ANISOU 3186  CB  ALA A 408     9966   3577   6189    371   1436   -166       C  
ATOM   3187  N   ALA A 409      39.478 130.065  -2.055  1.00 45.02           N  
ANISOU 3187  N   ALA A 409     9104   2945   5055    554   1789   -370       N  
ATOM   3188  CA  ALA A 409      40.607 129.680  -1.221  1.00 44.67           C  
ANISOU 3188  CA  ALA A 409     9076   2979   4916    569   1866   -362       C  
ATOM   3189  C   ALA A 409      41.852 129.476  -2.073  1.00 44.35           C  
ANISOU 3189  C   ALA A 409     9048   2987   4814    446   1872   -169       C  
ATOM   3190  O   ALA A 409      41.827 128.734  -3.061  1.00 43.73           O  
ANISOU 3190  O   ALA A 409     8972   2983   4660    381   1964    -66       O  
ATOM   3191  CB  ALA A 409      40.282 128.408  -0.440  1.00 43.81           C  
ANISOU 3191  CB  ALA A 409     8914   3061   4669    627   2051   -421       C  
ATOM   3192  N   LEU A 410      42.941 130.144  -1.692  1.00 43.60           N  
ANISOU 3192  N   LEU A 410     8954   2861   4750    415   1768   -127       N  
ATOM   3193  CA  LEU A 410      44.225 129.948  -2.351  1.00 44.27           C  
ANISOU 3193  CA  LEU A 410     9036   3023   4760    302   1780     44       C  
ATOM   3194  C   LEU A 410      44.694 128.517  -2.122  1.00 43.20           C  
ANISOU 3194  C   LEU A 410     8916   3051   4447    334   2002     44       C  
ATOM   3195  O   LEU A 410      44.771 127.723  -3.065  1.00 42.79           O  
ANISOU 3195  O   LEU A 410     8859   3093   4305    280   2097    135       O  
ATOM   3196  CB  LEU A 410      45.258 130.950  -1.831  1.00 45.64           C  
ANISOU 3196  CB  LEU A 410     9204   3130   5007    270   1623     72       C  
ATOM   3197  CG  LEU A 410      46.398 131.317  -2.784  1.00 46.56           C  
ANISOU 3197  CG  LEU A 410     9297   3284   5110    113   1540    276       C  
ATOM   3198  CD1 LEU A 410      45.913 132.284  -3.855  1.00 47.20           C  
ANISOU 3198  CD1 LEU A 410     9363   3252   5318      7   1355    383       C  
ATOM   3199  CD2 LEU A 410      47.581 131.899  -2.024  1.00 47.69           C  
ANISOU 3199  CD2 LEU A 410     9435   3409   5275     98   1451    288       C  
ATOM   3200  N   GLY A 411      45.002 128.184  -0.871  1.00 41.22           N  
ANISOU 3200  N   GLY A 411     8683   2832   4146    426   2073    -63       N  
ATOM   3201  CA  GLY A 411      45.275 126.808  -0.504  1.00 40.26           C  
ANISOU 3201  CA  GLY A 411     8586   2842   3870    472   2269    -83       C  
ATOM   3202  C   GLY A 411      46.644 126.288  -0.875  1.00 39.95           C  
ANISOU 3202  C   GLY A 411     8545   2912   3724    412   2317     29       C  
ATOM   3203  O   GLY A 411      46.778 125.104  -1.198  1.00 39.23           O  
ANISOU 3203  O   GLY A 411     8466   2926   3514    420   2456     53       O  
ATOM   3204  N   ALA A 412      47.670 127.134  -0.825  1.00 43.11           N  
ANISOU 3204  N   ALA A 412     8923   3291   4165    355   2199     93       N  
ATOM   3205  CA  ALA A 412      49.018 126.706  -1.168  1.00 42.14           C  
ANISOU 3205  CA  ALA A 412     8783   3291   3937    297   2238    193       C  
ATOM   3206  C   ALA A 412      49.517 125.644  -0.190  1.00 39.70           C  
ANISOU 3206  C   ALA A 412     8509   3069   3508    391   2381    112       C  
ATOM   3207  O   ALA A 412      48.984 125.468   0.909  1.00 39.07           O  
ANISOU 3207  O   ALA A 412     8464   2947   3434    490   2424    -11       O  
ATOM   3208  CB  ALA A 412      49.972 127.899  -1.174  1.00 44.74           C  
ANISOU 3208  CB  ALA A 412     9080   3576   4344    214   2072    273       C  
ATOM   3209  N   ILE A 413      50.562 124.930  -0.606  1.00 42.55           N  
ANISOU 3209  N   ILE A 413     8831   3561   3774    359   2425    180       N  
ATOM   3210  CA  ILE A 413      51.136 123.862   0.206  1.00 41.26           C  
ANISOU 3210  CA  ILE A 413     8556   3479   3642    423   2400    124       C  
ATOM   3211  C   ILE A 413      52.655 123.956   0.174  1.00 41.56           C  
ANISOU 3211  C   ILE A 413     8563   3613   3616    390   2378    171       C  
ATOM   3212  O   ILE A 413      53.311 123.938   1.222  1.00 41.60           O  
ANISOU 3212  O   ILE A 413     8574   3620   3612    438   2369    126       O  
ATOM   3213  CB  ILE A 413      50.649 122.480  -0.269  1.00 40.53           C  
ANISOU 3213  CB  ILE A 413     8338   3460   3603    437   2378    121       C  
ATOM   3214  CG1 ILE A 413      49.216 122.229   0.211  1.00 40.24           C  
ANISOU 3214  CG1 ILE A 413     8311   3348   3632    474   2390     76       C  
ATOM   3215  CG2 ILE A 413      51.584 121.382   0.215  1.00 40.18           C  
ANISOU 3215  CG2 ILE A 413     8193   3517   3555    469   2340    109       C  
ATOM   3216  CD1 ILE A 413      48.675 120.874  -0.157  1.00 39.63           C  
ANISOU 3216  CD1 ILE A 413     8137   3324   3596    479   2369     82       C  
ATOM   3217  N   PHE A 414      53.223 124.065  -1.020  1.00 43.84           N  
ANISOU 3217  N   PHE A 414     8797   4000   3861    301   2356    266       N  
ATOM   3218  CA  PHE A 414      54.663 124.180  -1.177  1.00 44.39           C  
ANISOU 3218  CA  PHE A 414     8809   4192   3864    252   2326    325       C  
ATOM   3219  C   PHE A 414      55.072 125.651  -1.198  1.00 47.20           C  
ANISOU 3219  C   PHE A 414     9282   4473   4180    150   2307    442       C  
ATOM   3220  O   PHE A 414      54.282 126.535  -1.539  1.00 50.26           O  
ANISOU 3220  O   PHE A 414     9676   4740   4680     95   2212    480       O  
ATOM   3221  CB  PHE A 414      55.118 123.467  -2.450  1.00 44.32           C  
ANISOU 3221  CB  PHE A 414     8647   4367   3827    201   2293    376       C  
ATOM   3222  CG  PHE A 414      54.614 122.054  -2.559  1.00 43.25           C  
ANISOU 3222  CG  PHE A 414     8424   4272   3738    282   2291    295       C  
ATOM   3223  CD1 PHE A 414      55.310 121.008  -1.977  1.00 42.90           C  
ANISOU 3223  CD1 PHE A 414     8308   4299   3693    350   2272    236       C  
ATOM   3224  CD2 PHE A 414      53.436 121.774  -3.233  1.00 42.93           C  
ANISOU 3224  CD2 PHE A 414     8382   4187   3743    281   2299    291       C  
ATOM   3225  CE1 PHE A 414      54.844 119.707  -2.070  1.00 42.30           C  
ANISOU 3225  CE1 PHE A 414     8172   4243   3659    406   2254    188       C  
ATOM   3226  CE2 PHE A 414      52.966 120.476  -3.330  1.00 42.29           C  
ANISOU 3226  CE2 PHE A 414     8234   4130   3703    341   2287    235       C  
ATOM   3227  CZ  PHE A 414      53.672 119.442  -2.748  1.00 42.01           C  
ANISOU 3227  CZ  PHE A 414     8138   4159   3664    399   2262    191       C  
ATOM   3228  N   GLU A 415      56.331 125.903  -0.822  1.00 50.91           N  
ANISOU 3228  N   GLU A 415     7996   5205   6141     91   1752    592       N  
ATOM   3229  CA  GLU A 415      56.796 127.275  -0.627  1.00 53.82           C  
ANISOU 3229  CA  GLU A 415     8245   5537   6668     -6   1667    614       C  
ATOM   3230  C   GLU A 415      56.675 128.112  -1.896  1.00 52.80           C  
ANISOU 3230  C   GLU A 415     8065   5394   6601   -132   1690    737       C  
ATOM   3231  O   GLU A 415      56.403 129.317  -1.817  1.00 53.26           O  
ANISOU 3231  O   GLU A 415     8086   5360   6791   -224   1611    761       O  
ATOM   3232  CB  GLU A 415      58.243 127.275  -0.132  1.00 57.61           C  
ANISOU 3232  CB  GLU A 415     8596   6103   7191     23   1639    587       C  
ATOM   3233  CG  GLU A 415      59.263 126.794  -1.157  1.00 58.46           C  
ANISOU 3233  CG  GLU A 415     8614   6344   7252     21   1731    661       C  
ATOM   3234  CD  GLU A 415      60.625 127.430  -0.961  1.00 62.24           C  
ANISOU 3234  CD  GLU A 415     8916   6893   7841    -23   1689    668       C  
ATOM   3235  OE1 GLU A 415      61.565 126.717  -0.550  1.00 63.71           O  
ANISOU 3235  OE1 GLU A 415     9046   7176   7983     70   1699    614       O  
ATOM   3236  OE2 GLU A 415      60.749 128.648  -1.208  1.00 63.59           O1+
ANISOU 3236  OE2 GLU A 415     9001   7015   8146   -152   1641    727       O1+
ATOM   3237  N   GLU A 416      56.854 127.499  -3.068  1.00 55.36           N  
ANISOU 3237  N   GLU A 416     8394   5809   6832   -134   1793    815       N  
ATOM   3238  CA  GLU A 416      56.771 128.243  -4.318  1.00 54.20           C  
ANISOU 3238  CA  GLU A 416     8204   5666   6722   -252   1822    944       C  
ATOM   3239  C   GLU A 416      55.364 128.749  -4.594  1.00 51.77           C  
ANISOU 3239  C   GLU A 416     7999   5238   6434   -298   1786    966       C  
ATOM   3240  O   GLU A 416      55.193 129.655  -5.416  1.00 51.64           O  
ANISOU 3240  O   GLU A 416     7952   5187   6482   -405   1771   1072       O  
ATOM   3241  CB  GLU A 416      57.239 127.369  -5.481  1.00 53.10           C  
ANISOU 3241  CB  GLU A 416     8054   5667   6454   -229   1944   1007       C  
ATOM   3242  CG  GLU A 416      56.335 126.176  -5.747  1.00 50.02           C  
ANISOU 3242  CG  GLU A 416     7808   5282   5914   -137   2008    962       C  
ATOM   3243  CD  GLU A 416      56.845 125.290  -6.865  1.00 49.07           C  
ANISOU 3243  CD  GLU A 416     7675   5304   5668   -102   2123   1005       C  
ATOM   3244  OE1 GLU A 416      57.896 125.617  -7.456  1.00 50.44           O  
ANISOU 3244  OE1 GLU A 416     7721   5584   5861   -151   2161   1074       O  
ATOM   3245  OE2 GLU A 416      56.192 124.262  -7.151  1.00 47.07           O1+
ANISOU 3245  OE2 GLU A 416     7534   5055   5293    -26   2176    964       O1+
ATOM   3246  N   GLU A 417      54.360 128.187  -3.928  1.00 51.27           N  
ANISOU 3246  N   GLU A 417     8054   5113   6315   -221   1772    872       N  
ATOM   3247  CA  GLU A 417      52.967 128.541  -4.146  1.00 49.31           C  
ANISOU 3247  CA  GLU A 417     7898   4762   6074   -250   1742    874       C  
ATOM   3248  C   GLU A 417      52.448 129.554  -3.132  1.00 50.85           C  
ANISOU 3248  C   GLU A 417     8088   4831   6402   -273   1623    806       C  
ATOM   3249  O   GLU A 417      51.277 129.940  -3.207  1.00 49.63           O  
ANISOU 3249  O   GLU A 417     7999   4588   6271   -290   1586    793       O  
ATOM   3250  CB  GLU A 417      52.106 127.274  -4.111  1.00 46.85           C  
ANISOU 3250  CB  GLU A 417     7715   4468   5618   -160   1808    809       C  
ATOM   3251  CG  GLU A 417      52.639 126.149  -4.994  1.00 45.98           C  
ANISOU 3251  CG  GLU A 417     7618   4479   5374   -116   1919    847       C  
ATOM   3252  CD  GLU A 417      52.089 124.788  -4.610  1.00 44.17           C  
ANISOU 3252  CD  GLU A 417     7506   4258   5020    -13   1970    761       C  
ATOM   3253  OE1 GLU A 417      51.367 124.703  -3.594  1.00 43.71           O  
ANISOU 3253  OE1 GLU A 417     7512   4123   4972     20   1926    677       O  
ATOM   3254  OE2 GLU A 417      52.383 123.803  -5.323  1.00 42.97           O1+
ANISOU 3254  OE2 GLU A 417     7381   4188   4758     34   2054    775       O1+
ATOM   3255  N   LYS A 418      53.289 130.000  -2.199  1.00 47.95           N  
ANISOU 3255  N   LYS A 418     7638   4456   6123   -269   1559    755       N  
ATOM   3256  CA  LYS A 418      52.882 130.869  -1.095  1.00 48.51           C  
ANISOU 3256  CA  LYS A 418     7702   4418   6311   -273   1443    664       C  
ATOM   3257  C   LYS A 418      53.230 132.331  -1.344  1.00 49.63           C  
ANISOU 3257  C   LYS A 418     7749   4476   6631   -386   1352    727       C  
ATOM   3258  O   LYS A 418      53.696 133.023  -0.434  1.00 51.28           O  
ANISOU 3258  O   LYS A 418     7893   4638   6954   -395   1259    659       O  
ATOM   3259  CB  LYS A 418      53.526 130.399   0.206  1.00 49.64           C  
ANISOU 3259  CB  LYS A 418     7826   4604   6431   -187   1417    549       C  
ATOM   3260  CG  LYS A 418      53.269 128.951   0.572  1.00 48.73           C  
ANISOU 3260  CG  LYS A 418     7809   4558   6147    -75   1497    492       C  
ATOM   3261  CD  LYS A 418      54.001 128.604   1.859  1.00 51.38           C  
ANISOU 3261  CD  LYS A 418     8120   4934   6467      7   1456    393       C  
ATOM   3262  CE  LYS A 418      53.636 127.221   2.365  1.00 49.64           C  
ANISOU 3262  CE  LYS A 418     8015   4759   6086    117   1520    337       C  
ATOM   3263  NZ  LYS A 418      54.301 126.932   3.666  1.00 52.35           N1+
ANISOU 3263  NZ  LYS A 418     8344   5138   6408    200   1469    246       N1+
ATOM   3264  N   GLU A 419      53.006 132.842  -2.553  1.00 51.12           N  
ANISOU 3264  N   GLU A 419     7934   4641   6850   -474   1370    857       N  
ATOM   3265  CA  GLU A 419      53.459 134.178  -2.911  1.00 52.08           C  
ANISOU 3265  CA  GLU A 419     7967   4683   7139   -594   1291    945       C  
ATOM   3266  C   GLU A 419      52.334 135.198  -3.022  1.00 50.90           C  
ANISOU 3266  C   GLU A 419     7868   4377   7097   -637   1194    952       C  
ATOM   3267  O   GLU A 419      52.599 136.348  -3.387  1.00 51.81           O  
ANISOU 3267  O   GLU A 419     7925   4403   7359   -740   1120   1036       O  
ATOM   3268  CB  GLU A 419      54.240 134.127  -4.230  1.00 51.94           C  
ANISOU 3268  CB  GLU A 419     7890   4760   7085   -677   1377   1109       C  
ATOM   3269  CG  GLU A 419      55.292 133.030  -4.270  1.00 52.64           C  
ANISOU 3269  CG  GLU A 419     7929   5016   7054   -621   1482   1100       C  
ATOM   3270  CD  GLU A 419      56.315 133.237  -5.368  1.00 53.82           C  
ANISOU 3270  CD  GLU A 419     7977   5265   7206   -717   1550   1247       C  
ATOM   3271  OE1 GLU A 419      55.976 133.033  -6.553  1.00 52.23           O  
ANISOU 3271  OE1 GLU A 419     7816   5111   6916   -750   1625   1355       O  
ATOM   3272  OE2 GLU A 419      57.460 133.616  -5.042  1.00 56.67           O1+
ANISOU 3272  OE2 GLU A 419     8213   5665   7655   -762   1529   1253       O1+
ATOM   3273  N   TRP A 420      51.096 134.825  -2.707  1.00 52.29           N  
ANISOU 3273  N   TRP A 420     8144   4514   7209   -562   1190    865       N  
ATOM   3274  CA  TRP A 420      49.953 135.694  -2.940  1.00 51.22           C  
ANISOU 3274  CA  TRP A 420     8056   4244   7161   -589   1105    870       C  
ATOM   3275  C   TRP A 420      49.036 135.717  -1.728  1.00 51.05           C  
ANISOU 3275  C   TRP A 420     8080   4159   7158   -503   1040    695       C  
ATOM   3276  O   TRP A 420      48.878 134.709  -1.033  1.00 50.88           O  
ANISOU 3276  O   TRP A 420     8101   4218   7015   -415   1100    595       O  
ATOM   3277  CB  TRP A 420      49.181 135.248  -4.186  1.00 49.18           C  
ANISOU 3277  CB  TRP A 420     7873   4020   6794   -599   1178    970       C  
ATOM   3278  CG  TRP A 420      50.041 135.254  -5.408  1.00 49.28           C  
ANISOU 3278  CG  TRP A 420     7841   4109   6775   -683   1246   1142       C  
ATOM   3279  CD1 TRP A 420      50.447 136.347  -6.114  1.00 50.07           C  
ANISOU 3279  CD1 TRP A 420     7887   4143   6992   -797   1192   1281       C  
ATOM   3280  CD2 TRP A 420      50.622 134.117  -6.060  1.00 48.62           C  
ANISOU 3280  CD2 TRP A 420     7760   4186   6528   -660   1381   1193       C  
ATOM   3281  NE1 TRP A 420      51.239 135.964  -7.167  1.00 50.01           N  
ANISOU 3281  NE1 TRP A 420     7846   4260   6896   -851   1294   1419       N  
ATOM   3282  CE2 TRP A 420      51.360 134.599  -7.159  1.00 49.07           C  
ANISOU 3282  CE2 TRP A 420     7758   4284   6605   -763   1410   1360       C  
ATOM   3283  CE3 TRP A 420      50.586 132.739  -5.825  1.00 47.69           C  
ANISOU 3283  CE3 TRP A 420     7691   4178   6251   -562   1479   1114       C  
ATOM   3284  CZ2 TRP A 420      52.057 133.754  -8.021  1.00 48.65           C  
ANISOU 3284  CZ2 TRP A 420     7684   4391   6411   -764   1536   1437       C  
ATOM   3285  CZ3 TRP A 420      51.278 131.901  -6.683  1.00 47.20           C  
ANISOU 3285  CZ3 TRP A 420     7614   4258   6062   -560   1594   1188       C  
ATOM   3286  CH2 TRP A 420      52.004 132.412  -7.766  1.00 47.70           C  
ANISOU 3286  CH2 TRP A 420     7610   4372   6142   -657   1624   1342       C  
ATOM   3287  N   LYS A 421      48.432 136.882  -1.481  1.00 51.42           N  
ANISOU 3287  N   LYS A 421     8119   4062   7356   -529    916    660       N  
ATOM   3288  CA  LYS A 421      47.552 137.040  -0.330  1.00 51.64           C  
ANISOU 3288  CA  LYS A 421     8177   4033   7410   -449    848    485       C  
ATOM   3289  C   LYS A 421      46.137 136.559  -0.627  1.00 49.88           C  
ANISOU 3289  C   LYS A 421     8042   3814   7095   -397    885    451       C  
ATOM   3290  O   LYS A 421      45.473 136.004   0.256  1.00 49.60           O  
ANISOU 3290  O   LYS A 421     8046   3814   6986   -315    905    313       O  
ATOM   3291  CB  LYS A 421      47.535 138.504   0.124  1.00 53.08           C  
ANISOU 3291  CB  LYS A 421     8306   4058   7804   -488    691    439       C  
ATOM   3292  CG  LYS A 421      48.776 138.944   0.883  1.00 55.23           C  
ANISOU 3292  CG  LYS A 421     8488   4324   8173   -516    634    401       C  
ATOM   3293  CD  LYS A 421      48.461 139.219   2.348  1.00 55.98           C  
ANISOU 3293  CD  LYS A 421     8574   4382   8312   -435    548    197       C  
ATOM   3294  CE  LYS A 421      48.062 137.947   3.083  1.00 55.02           C  
ANISOU 3294  CE  LYS A 421     8512   4395   7997   -327    645     91       C  
ATOM   3295  NZ  LYS A 421      47.632 138.216   4.482  1.00 55.08           N1+
ANISOU 3295  NZ  LYS A 421     8518   4382   8026   -246    567   -106       N1+
ATOM   3296  N   THR A 422      45.654 136.772  -1.852  1.00 51.71           N  
ANISOU 3296  N   THR A 422     8304   4015   7328   -445    894    574       N  
ATOM   3297  CA  THR A 422      44.297 136.404  -2.232  1.00 50.24           C  
ANISOU 3297  CA  THR A 422     8191   3829   7069   -402    917    544       C  
ATOM   3298  C   THR A 422      44.318 135.631  -3.543  1.00 49.08           C  
ANISOU 3298  C   THR A 422     8087   3770   6792   -432   1022    683       C  
ATOM   3299  O   THR A 422      45.335 135.566  -4.240  1.00 49.12           O  
ANISOU 3299  O   THR A 422     8060   3824   6778   -492   1068    811       O  
ATOM   3300  CB  THR A 422      43.387 137.635  -2.367  1.00 50.29           C  
ANISOU 3300  CB  THR A 422     8196   3685   7228   -414    783    526       C  
ATOM   3301  OG1 THR A 422      43.815 138.431  -3.478  1.00 50.81           O  
ANISOU 3301  OG1 THR A 422     8244   3682   7381   -505    738    699       O  
ATOM   3302  CG2 THR A 422      43.424 138.479  -1.100  1.00 51.21           C  
ANISOU 3302  CG2 THR A 422     8264   3710   7484   -382    669    380       C  
ATOM   3303  N   ALA A 423      43.165 135.048  -3.879  1.00 50.07           N  
ANISOU 3303  N   ALA A 423     8278   3921   6824   -391   1061    648       N  
ATOM   3304  CA  ALA A 423      43.063 134.238  -5.088  1.00 49.11           C  
ANISOU 3304  CA  ALA A 423     8204   3889   6568   -408   1157    755       C  
ATOM   3305  C   ALA A 423      42.970 135.103  -6.340  1.00 49.27           C  
ANISOU 3305  C   ALA A 423     8221   3850   6649   -479   1102    908       C  
ATOM   3306  O   ALA A 423      43.626 134.812  -7.347  1.00 48.55           O  
ANISOU 3306  O   ALA A 423     8129   3833   6484   -527   1169   1044       O  
ATOM   3307  CB  ALA A 423      41.859 133.300  -4.990  1.00 48.15           C  
ANISOU 3307  CB  ALA A 423     8150   3813   6330   -344   1213    658       C  
ATOM   3308  N   VAL A 424      42.162 136.165  -6.298  1.00 47.66           N  
ANISOU 3308  N   VAL A 424     8014   3517   6576   -483    979    888       N  
ATOM   3309  CA  VAL A 424      42.045 137.050  -7.453  1.00 47.73           C  
ANISOU 3309  CA  VAL A 424     8030   3455   6651   -549    911   1043       C  
ATOM   3310  C   VAL A 424      43.369 137.754  -7.727  1.00 48.67           C  
ANISOU 3310  C   VAL A 424     8091   3547   6855   -641    892   1179       C  
ATOM   3311  O   VAL A 424      43.683 138.080  -8.878  1.00 49.22           O  
ANISOU 3311  O   VAL A 424     8166   3623   6910   -714    898   1352       O  
ATOM   3312  CB  VAL A 424      40.891 138.050  -7.238  1.00 48.26           C  
ANISOU 3312  CB  VAL A 424     8106   3376   6853   -519    769    977       C  
ATOM   3313  CG1 VAL A 424      41.147 138.919  -6.014  1.00 49.04           C  
ANISOU 3313  CG1 VAL A 424     8151   3362   7120   -506    667    867       C  
ATOM   3314  CG2 VAL A 424      40.676 138.905  -8.481  1.00 49.08           C  
ANISOU 3314  CG2 VAL A 424     8232   3403   7013   -578    692   1146       C  
ATOM   3315  N   GLU A 425      44.173 137.986  -6.689  1.00 48.55           N  
ANISOU 3315  N   GLU A 425     8017   3508   6924   -644    871   1107       N  
ATOM   3316  CA  GLU A 425      45.497 138.562  -6.897  1.00 49.58           C  
ANISOU 3316  CA  GLU A 425     8077   3626   7133   -738    863   1226       C  
ATOM   3317  C   GLU A 425      46.420 137.576  -7.601  1.00 49.07           C  
ANISOU 3317  C   GLU A 425     8001   3734   6911   -766   1010   1325       C  
ATOM   3318  O   GLU A 425      47.211 137.966  -8.468  1.00 49.46           O  
ANISOU 3318  O   GLU A 425     8014   3804   6974   -860   1029   1489       O  
ATOM   3319  CB  GLU A 425      46.088 138.995  -5.556  1.00 50.76           C  
ANISOU 3319  CB  GLU A 425     8163   3717   7407   -725    798   1102       C  
ATOM   3320  CG  GLU A 425      47.555 139.374  -5.599  1.00 52.27           C  
ANISOU 3320  CG  GLU A 425     8267   3924   7668   -817    806   1195       C  
ATOM   3321  CD  GLU A 425      48.146 139.538  -4.213  1.00 54.13           C  
ANISOU 3321  CD  GLU A 425     8441   4137   7990   -785    756   1048       C  
ATOM   3322  OE1 GLU A 425      47.446 140.066  -3.322  1.00 54.45           O  
ANISOU 3322  OE1 GLU A 425     8494   4070   8126   -731    653    907       O  
ATOM   3323  OE2 GLU A 425      49.309 139.128  -4.012  1.00 55.26           O1+
ANISOU 3323  OE2 GLU A 425     8519   4376   8100   -808    819   1065       O1+
ATOM   3324  N   ALA A 426      46.321 136.292  -7.254  1.00 48.84           N  
ANISOU 3324  N   ALA A 426     8001   3826   6728   -685   1115   1227       N  
ATOM   3325  CA  ALA A 426      47.218 135.295  -7.829  1.00 48.36           C  
ANISOU 3325  CA  ALA A 426     7926   3926   6521   -692   1250   1295       C  
ATOM   3326  C   ALA A 426      46.907 135.039  -9.297  1.00 47.35           C  
ANISOU 3326  C   ALA A 426     7844   3866   6281   -726   1309   1433       C  
ATOM   3327  O   ALA A 426      47.824 134.824 -10.098  1.00 47.75           O  
ANISOU 3327  O   ALA A 426     7858   4021   6264   -778   1388   1552       O  
ATOM   3328  CB  ALA A 426      47.131 133.992  -7.037  1.00 47.59           C  
ANISOU 3328  CB  ALA A 426     7861   3921   6300   -590   1334   1152       C  
ATOM   3329  N   VAL A 427      45.628 135.063  -9.671  1.00 47.11           N  
ANISOU 3329  N   VAL A 427     7887   3787   6224   -694   1272   1413       N  
ATOM   3330  CA  VAL A 427      45.217 134.680 -11.019  1.00 47.12           C  
ANISOU 3330  CA  VAL A 427     7942   3865   6097   -708   1326   1519       C  
ATOM   3331  C   VAL A 427      45.617 135.748 -12.032  1.00 48.48           C  
ANISOU 3331  C   VAL A 427     8090   3998   6332   -814   1278   1714       C  
ATOM   3332  O   VAL A 427      45.445 135.567 -13.243  1.00 48.82           O  
ANISOU 3332  O   VAL A 427     8169   4114   6265   -840   1319   1830       O  
ATOM   3333  CB  VAL A 427      43.700 134.403 -11.087  1.00 46.72           C  
ANISOU 3333  CB  VAL A 427     7971   3776   6007   -642   1290   1431       C  
ATOM   3334  CG1 VAL A 427      43.320 133.264 -10.161  1.00 45.67           C  
ANISOU 3334  CG1 VAL A 427     7865   3692   5795   -552   1354   1257       C  
ATOM   3335  CG2 VAL A 427      42.907 135.657 -10.775  1.00 47.60           C  
ANISOU 3335  CG2 VAL A 427     8081   3718   6286   -653   1140   1417       C  
ATOM   3336  N   ASN A 428      46.147 136.868 -11.548  1.00 47.35           N  
ANISOU 3336  N   ASN A 428     7887   3738   6365   -878   1186   1751       N  
ATOM   3337  CA  ASN A 428      46.679 137.915 -12.409  1.00 48.91           C  
ANISOU 3337  CA  ASN A 428     8057   3888   6640   -996   1142   1948       C  
ATOM   3338  C   ASN A 428      48.201 137.957 -12.419  1.00 49.76           C  
ANISOU 3338  C   ASN A 428     8068   4078   6761  -1077   1211   2030       C  
ATOM   3339  O   ASN A 428      48.782 138.770 -13.147  1.00 51.08           O  
ANISOU 3339  O   ASN A 428     8200   4223   6983  -1191   1192   2206       O  
ATOM   3340  CB  ASN A 428      46.118 139.278 -11.987  1.00 49.76           C  
ANISOU 3340  CB  ASN A 428     8169   3781   6957  -1023    971   1947       C  
ATOM   3341  CG  ASN A 428      44.735 139.531 -12.544  1.00 49.91           C  
ANISOU 3341  CG  ASN A 428     8274   3727   6963   -980    894   1955       C  
ATOM   3342  OD1 ASN A 428      43.767 138.865 -12.172  1.00 48.92           O  
ANISOU 3342  OD1 ASN A 428     8193   3623   6772   -880    903   1809       O  
ATOM   3343  ND2 ASN A 428      44.634 140.497 -13.448  1.00 50.99           N  
ANISOU 3343  ND2 ASN A 428     8433   3780   7162  -1059    816   2130       N  
ATOM   3344  N   ASP A 429      48.860 137.107 -11.638  1.00 46.75           N  
ANISOU 3344  N   ASP A 429     7642   3791   6332  -1023   1289   1911       N  
ATOM   3345  CA  ASP A 429      50.315 137.052 -11.623  1.00 47.52           C  
ANISOU 3345  CA  ASP A 429     7635   3984   6435  -1087   1359   1972       C  
ATOM   3346  C   ASP A 429      50.791 136.006 -12.620  1.00 47.49           C  
ANISOU 3346  C   ASP A 429     7631   4186   6227  -1077   1512   2040       C  
ATOM   3347  O   ASP A 429      50.503 134.818 -12.431  1.00 46.23           O  
ANISOU 3347  O   ASP A 429     7514   4118   5931   -971   1588   1925       O  
ATOM   3348  CB  ASP A 429      50.819 136.708 -10.234  1.00 46.75           C  
ANISOU 3348  CB  ASP A 429     7485   3883   6395  -1025   1350   1804       C  
ATOM   3349  CG  ASP A 429      52.227 137.204  -9.986  1.00 47.93           C  
ANISOU 3349  CG  ASP A 429     7510   4057   6645  -1113   1353   1860       C  
ATOM   3350  OD1 ASP A 429      52.972 137.419 -10.969  1.00 49.16           O  
ANISOU 3350  OD1 ASP A 429     7612   4295   6771  -1211   1414   2023       O  
ATOM   3351  OD2 ASP A 429      52.591 137.383  -8.804  1.00 47.73           O1+
ANISOU 3351  OD2 ASP A 429     7435   3976   6724  -1086   1295   1738       O1+
ATOM   3352  N   PRO A 430      51.510 136.389 -13.680  1.00 48.28           N  
ANISOU 3352  N   PRO A 430     7684   4364   6297  -1183   1562   2222       N  
ATOM   3353  CA  PRO A 430      51.980 135.382 -14.650  1.00 48.39           C  
ANISOU 3353  CA  PRO A 430     7691   4591   6105  -1165   1712   2275       C  
ATOM   3354  C   PRO A 430      52.807 134.265 -14.029  1.00 47.63           C  
ANISOU 3354  C   PRO A 430     7536   4626   5933  -1083   1810   2147       C  
ATOM   3355  O   PRO A 430      52.937 133.197 -14.642  1.00 47.32           O  
ANISOU 3355  O   PRO A 430     7517   4747   5717  -1023   1924   2130       O  
ATOM   3356  CB  PRO A 430      52.811 136.210 -15.640  1.00 50.39           C  
ANISOU 3356  CB  PRO A 430     7868   4900   6377  -1311   1730   2486       C  
ATOM   3357  CG  PRO A 430      52.251 137.591 -15.535  1.00 51.17           C  
ANISOU 3357  CG  PRO A 430     7991   4795   6656  -1392   1571   2563       C  
ATOM   3358  CD  PRO A 430      51.849 137.761 -14.096  1.00 50.03           C  
ANISOU 3358  CD  PRO A 430     7863   4481   6663  -1325   1483   2393       C  
ATOM   3359  N   ARG A 431      53.359 134.469 -12.830  1.00 48.25           N  
ANISOU 3359  N   ARG A 431     7549   4643   6141  -1071   1762   2049       N  
ATOM   3360  CA  ARG A 431      54.056 133.384 -12.149  1.00 47.50           C  
ANISOU 3360  CA  ARG A 431     7411   4660   5977   -976   1838   1917       C  
ATOM   3361  C   ARG A 431      53.092 132.268 -11.770  1.00 45.82           C  
ANISOU 3361  C   ARG A 431     7311   4447   5650   -838   1858   1770       C  
ATOM   3362  O   ARG A 431      53.460 131.088 -11.786  1.00 45.31           O  
ANISOU 3362  O   ARG A 431     7250   4509   5455   -752   1954   1701       O  
ATOM   3363  CB  ARG A 431      54.768 133.908 -10.903  1.00 48.11           C  
ANISOU 3363  CB  ARG A 431     7399   4661   6218   -991   1763   1841       C  
ATOM   3364  CG  ARG A 431      55.386 135.284 -11.060  1.00 49.78           C  
ANISOU 3364  CG  ARG A 431     7518   4797   6600  -1141   1693   1970       C  
ATOM   3365  CD  ARG A 431      56.380 135.557  -9.945  1.00 51.07           C  
ANISOU 3365  CD  ARG A 431     7568   4942   6895  -1151   1648   1887       C  
ATOM   3366  NE  ARG A 431      57.660 134.909 -10.208  1.00 52.06           N  
ANISOU 3366  NE  ARG A 431     7580   5259   6941  -1152   1761   1906       N  
ATOM   3367  CZ  ARG A 431      58.492 134.483  -9.264  1.00 53.77           C  
ANISOU 3367  CZ  ARG A 431     7715   5529   7185  -1093   1763   1788       C  
ATOM   3368  NH1 ARG A 431      58.174 134.621  -7.984  1.00 54.52           N1+
ANISOU 3368  NH1 ARG A 431     7837   5507   7373  -1029   1660   1645       N1+
ATOM   3369  NH2 ARG A 431      59.637 133.907  -9.602  1.00 54.69           N  
ANISOU 3369  NH2 ARG A 431     7723   5828   7230  -1090   1866   1809       N  
ATOM   3370  N   PHE A 432      51.853 132.624 -11.420  1.00 47.32           N  
ANISOU 3370  N   PHE A 432     7592   4494   5895   -816   1768   1719       N  
ATOM   3371  CA  PHE A 432      50.860 131.615 -11.064  1.00 45.85           C  
ANISOU 3371  CA  PHE A 432     7509   4302   5608   -702   1787   1585       C  
ATOM   3372  C   PHE A 432      50.573 130.689 -12.239  1.00 45.74           C  
ANISOU 3372  C   PHE A 432     7554   4414   5410   -671   1889   1626       C  
ATOM   3373  O   PHE A 432      50.552 129.461 -12.089  1.00 44.93           O  
ANISOU 3373  O   PHE A 432     7492   4391   5188   -577   1964   1529       O  
ATOM   3374  CB  PHE A 432      49.576 132.292 -10.581  1.00 45.31           C  
ANISOU 3374  CB  PHE A 432     7509   4068   5639   -696   1671   1533       C  
ATOM   3375  CG  PHE A 432      48.415 131.352 -10.422  1.00 44.02           C  
ANISOU 3375  CG  PHE A 432     7450   3904   5372   -602   1694   1419       C  
ATOM   3376  CD1 PHE A 432      48.298 130.560  -9.292  1.00 43.05           C  
ANISOU 3376  CD1 PHE A 432     7352   3778   5227   -514   1709   1267       C  
ATOM   3377  CD2 PHE A 432      47.435 131.266 -11.399  1.00 43.97           C  
ANISOU 3377  CD2 PHE A 432     7517   3900   5291   -606   1697   1466       C  
ATOM   3378  CE1 PHE A 432      47.230 129.695  -9.142  1.00 41.93           C  
ANISOU 3378  CE1 PHE A 432     7304   3633   4996   -442   1734   1170       C  
ATOM   3379  CE2 PHE A 432      46.365 130.403 -11.256  1.00 42.91           C  
ANISOU 3379  CE2 PHE A 432     7468   3765   5070   -529   1716   1357       C  
ATOM   3380  CZ  PHE A 432      46.262 129.617 -10.125  1.00 41.89           C  
ANISOU 3380  CZ  PHE A 432     7362   3630   4926   -452   1738   1211       C  
ATOM   3381  N   TRP A 433      50.346 131.261 -13.421  1.00 44.84           N  
ANISOU 3381  N   TRP A 433     7451   4319   5269   -746   1888   1769       N  
ATOM   3382  CA  TRP A 433      50.108 130.449 -14.607  1.00 44.95           C  
ANISOU 3382  CA  TRP A 433     7510   4467   5101   -719   1974   1805       C  
ATOM   3383  C   TRP A 433      51.370 129.762 -15.108  1.00 45.64           C  
ANISOU 3383  C   TRP A 433     7520   4741   5082   -711   2092   1835       C  
ATOM   3384  O   TRP A 433      51.272 128.866 -15.953  1.00 45.66           O  
ANISOU 3384  O   TRP A 433     7532   4884   4932   -657   2143   1805       O  
ATOM   3385  CB  TRP A 433      49.487 131.310 -15.708  1.00 45.87           C  
ANISOU 3385  CB  TRP A 433     7629   4577   5222   -790   1892   1928       C  
ATOM   3386  CG  TRP A 433      48.176 131.895 -15.285  1.00 45.24           C  
ANISOU 3386  CG  TRP A 433     7627   4324   5238   -780   1779   1886       C  
ATOM   3387  CD1 TRP A 433      47.937 133.180 -14.895  1.00 45.75           C  
ANISOU 3387  CD1 TRP A 433     7688   4223   5473   -847   1671   1947       C  
ATOM   3388  CD2 TRP A 433      46.926 131.203 -15.174  1.00 44.08           C  
ANISOU 3388  CD2 TRP A 433     7571   4149   5028   -694   1763   1766       C  
ATOM   3389  NE1 TRP A 433      46.613 133.336 -14.562  1.00 44.99           N  
ANISOU 3389  NE1 TRP A 433     7672   4004   5419   -801   1589   1868       N  
ATOM   3390  CE2 TRP A 433      45.971 132.136 -14.724  1.00 43.96           C  
ANISOU 3390  CE2 TRP A 433     7599   3959   5145   -712   1650   1761       C  
ATOM   3391  CE3 TRP A 433      46.521 129.887 -15.418  1.00 43.25           C  
ANISOU 3391  CE3 TRP A 433     7513   4144   4775   -608   1831   1660       C  
ATOM   3392  CZ2 TRP A 433      44.637 131.796 -14.513  1.00 43.04           C  
ANISOU 3392  CZ2 TRP A 433     7566   3777   5009   -649   1614   1657       C  
ATOM   3393  CZ3 TRP A 433      45.196 129.552 -15.209  1.00 42.33           C  
ANISOU 3393  CZ3 TRP A 433     7482   3957   4645   -554   1793   1562       C  
ATOM   3394  CH2 TRP A 433      44.270 130.501 -14.760  1.00 42.23           C  
ANISOU 3394  CH2 TRP A 433     7507   3782   4758   -577   1691   1563       C  
ATOM   3395  N   ALA A 434      52.544 130.152 -14.608  1.00 46.23           N  
ANISOU 3395  N   ALA A 434     7491   4833   5242   -756   2110   1866       N  
ATOM   3396  CA  ALA A 434      53.752 129.381 -14.880  1.00 46.81           C  
ANISOU 3396  CA  ALA A 434     7482   5084   5219   -726   2226   1860       C  
ATOM   3397  C   ALA A 434      53.755 128.081 -14.086  1.00 45.58           C  
ANISOU 3397  C   ALA A 434     7366   4953   5000   -586   2263   1685       C  
ATOM   3398  O   ALA A 434      54.170 127.034 -14.596  1.00 45.71           O  
ANISOU 3398  O   ALA A 434     7382   5110   4875   -516   2362   1649       O  
ATOM   3399  CB  ALA A 434      54.992 130.213 -14.557  1.00 48.00           C  
ANISOU 3399  CB  ALA A 434     7489   5253   5495   -817   2215   1932       C  
ATOM   3400  N   LEU A 435      53.293 128.131 -12.833  1.00 45.86           N  
ANISOU 3400  N   LEU A 435     7438   4851   5134   -542   2182   1576       N  
ATOM   3401  CA  LEU A 435      53.180 126.916 -12.031  1.00 44.75           C  
ANISOU 3401  CA  LEU A 435     7354   4716   4932   -415   2208   1422       C  
ATOM   3402  C   LEU A 435      52.166 125.954 -12.635  1.00 44.01           C  
ANISOU 3402  C   LEU A 435     7383   4640   4700   -350   2252   1374       C  
ATOM   3403  O   LEU A 435      52.379 124.736 -12.640  1.00 43.70           O  
ANISOU 3403  O   LEU A 435     7378   4674   4552   -255   2322   1291       O  
ATOM   3404  CB  LEU A 435      52.795 127.274 -10.595  1.00 43.90           C  
ANISOU 3404  CB  LEU A 435     7266   4462   4952   -394   2110   1327       C  
ATOM   3405  CG  LEU A 435      53.858 128.000  -9.770  1.00 44.54           C  
ANISOU 3405  CG  LEU A 435     7229   4528   5167   -432   2061   1330       C  
ATOM   3406  CD1 LEU A 435      53.263 128.546  -8.481  1.00 43.83           C  
ANISOU 3406  CD1 LEU A 435     7168   4286   5200   -421   1951   1242       C  
ATOM   3407  CD2 LEU A 435      55.022 127.068  -9.470  1.00 44.79           C  
ANISOU 3407  CD2 LEU A 435     7198   4685   5136   -352   2132   1272       C  
ATOM   3408  N   VAL A 436      51.055 126.485 -13.148  1.00 43.92           N  
ANISOU 3408  N   VAL A 436     7437   4554   4695   -399   2204   1421       N  
ATOM   3409  CA  VAL A 436      50.071 125.644 -13.822  1.00 43.39           C  
ANISOU 3409  CA  VAL A 436     7458   4518   4509   -345   2217   1365       C  
ATOM   3410  C   VAL A 436      50.660 125.057 -15.098  1.00 44.30           C  
ANISOU 3410  C   VAL A 436     7522   4816   4494   -331   2280   1398       C  
ATOM   3411  O   VAL A 436      50.570 123.848 -15.344  1.00 43.98           O  
ANISOU 3411  O   VAL A 436     7517   4845   4349   -243   2322   1301       O  
ATOM   3412  CB  VAL A 436      48.790 126.444 -14.111  1.00 43.18           C  
ANISOU 3412  CB  VAL A 436     7477   4391   4537   -396   2119   1395       C  
ATOM   3413  CG1 VAL A 436      47.871 125.644 -15.009  1.00 42.93           C  
ANISOU 3413  CG1 VAL A 436     7500   4421   4389   -350   2117   1341       C  
ATOM   3414  CG2 VAL A 436      48.091 126.816 -12.813  1.00 42.24           C  
ANISOU 3414  CG2 VAL A 436     7417   4101   4532   -388   2062   1327       C  
ATOM   3415  N   ASP A 437      51.269 125.907 -15.932  1.00 44.29           N  
ANISOU 3415  N   ASP A 437     7436   4893   4500   -420   2285   1536       N  
ATOM   3416  CA  ASP A 437      51.895 125.424 -17.160  1.00 45.37           C  
ANISOU 3416  CA  ASP A 437     7513   5221   4505   -413   2350   1574       C  
ATOM   3417  C   ASP A 437      52.956 124.373 -16.863  1.00 45.48           C  
ANISOU 3417  C   ASP A 437     7489   5338   4452   -327   2450   1494       C  
ATOM   3418  O   ASP A 437      53.131 123.419 -17.631  1.00 45.84           O  
ANISOU 3418  O   ASP A 437     7531   5516   4372   -262   2498   1439       O  
ATOM   3419  CB  ASP A 437      52.507 126.590 -17.936  1.00 46.88           C  
ANISOU 3419  CB  ASP A 437     7611   5478   4724   -538   2344   1748       C  
ATOM   3420  CG  ASP A 437      51.469 127.403 -18.681  1.00 47.15           C  
ANISOU 3420  CG  ASP A 437     7686   5460   4770   -605   2251   1834       C  
ATOM   3421  OD1 ASP A 437      50.506 126.801 -19.201  1.00 46.66           O  
ANISOU 3421  OD1 ASP A 437     7696   5411   4621   -549   2228   1769       O  
ATOM   3422  OD2 ASP A 437      51.615 128.641 -18.746  1.00 47.96           O1+
ANISOU 3422  OD2 ASP A 437     7748   5502   4971   -713   2198   1968       O1+
ATOM   3423  N   ARG A 438      53.672 124.526 -15.748  1.00 47.76           N  
ANISOU 3423  N   ARG A 438     7753   5568   4827   -319   2480   1482       N  
ATOM   3424  CA  ARG A 438      54.703 123.558 -15.396  1.00 48.01           C  
ANISOU 3424  CA  ARG A 438     7749   5693   4800   -226   2574   1407       C  
ATOM   3425  C   ARG A 438      54.100 122.259 -14.878  1.00 46.75           C  
ANISOU 3425  C   ARG A 438     7696   5481   4584    -97   2566   1250       C  
ATOM   3426  O   ARG A 438      54.679 121.185 -15.081  1.00 46.94           O  
ANISOU 3426  O   ARG A 438     7710   5606   4518      0   2628   1173       O  
ATOM   3427  CB  ARG A 438      55.647 124.153 -14.351  1.00 48.47           C  
ANISOU 3427  CB  ARG A 438     7706   5716   4994   -253   2548   1415       C  
ATOM   3428  CG  ARG A 438      57.121 123.917 -14.626  1.00 49.97           C  
ANISOU 3428  CG  ARG A 438     7756   6079   5152   -237   2629   1431       C  
ATOM   3429  CD  ARG A 438      57.960 124.373 -13.444  1.00 50.57           C  
ANISOU 3429  CD  ARG A 438     7732   6110   5372   -245   2573   1401       C  
ATOM   3430  NE  ARG A 438      59.296 124.804 -13.844  1.00 52.74           N  
ANISOU 3430  NE  ARG A 438     7836   6535   5668   -305   2628   1475       N  
ATOM   3431  CZ  ARG A 438      60.218 125.258 -13.002  1.00 54.34           C  
ANISOU 3431  CZ  ARG A 438     7920   6733   5993   -326   2588   1461       C  
ATOM   3432  NH1 ARG A 438      61.407 125.631 -13.455  1.00 56.35           N1+
ANISOU 3432  NH1 ARG A 438     8011   7136   6263   -390   2647   1530       N1+
ATOM   3433  NH2 ARG A 438      59.953 125.337 -11.705  1.00 54.19           N  
ANISOU 3433  NH2 ARG A 438     7941   6571   6077   -286   2491   1373       N  
ATOM   3434  N   GLU A 439      52.947 122.334 -14.209  1.00 43.34           N  
ANISOU 3434  N   GLU A 439     7366   4894   4210    -95   2490   1199       N  
ATOM   3435  CA  GLU A 439      52.329 121.128 -13.665  1.00 42.35           C  
ANISOU 3435  CA  GLU A 439     7342   4708   4042     10   2480   1060       C  
ATOM   3436  C   GLU A 439      51.677 120.295 -14.762  1.00 42.44           C  
ANISOU 3436  C   GLU A 439     7390   4784   3953     47   2472   1007       C  
ATOM   3437  O   GLU A 439      51.805 119.065 -14.772  1.00 42.37           O  
ANISOU 3437  O   GLU A 439     7420   4803   3875    144   2501    907       O  
ATOM   3438  CB  GLU A 439      51.309 121.500 -12.591  1.00 41.20           C  
ANISOU 3438  CB  GLU A 439     7279   4389   3985     -9   2410   1024       C  
ATOM   3439  CG  GLU A 439      51.721 121.076 -11.197  1.00 40.67           C  
ANISOU 3439  CG  GLU A 439     7232   4258   3962     58   2407    946       C  
ATOM   3440  CD  GLU A 439      51.831 119.570 -11.061  1.00 40.46           C  
ANISOU 3440  CD  GLU A 439     7283   4257   3835    176   2461    844       C  
ATOM   3441  OE1 GLU A 439      50.791 118.883 -11.156  1.00 39.84           O  
ANISOU 3441  OE1 GLU A 439     7285   4122   3730    201   2424    770       O  
ATOM   3442  OE2 GLU A 439      52.959 119.072 -10.869  1.00 41.03           O1+
ANISOU 3442  OE2 GLU A 439     7297   4406   3887    244   2496    819       O1+
ATOM   3443  N   ARG A 440      50.974 120.946 -15.693  1.00 41.05           N  
ANISOU 3443  N   ARG A 440     7206   4624   3766    -28   2429   1073       N  
ATOM   3444  CA  ARG A 440      50.376 120.223 -16.810  1.00 41.30           C  
ANISOU 3444  CA  ARG A 440     7270   4727   3695      2   2426   1030       C  
ATOM   3445  C   ARG A 440      51.431 119.493 -17.631  1.00 42.41           C  
ANISOU 3445  C   ARG A 440     7347   5040   3727     55   2502   1017       C  
ATOM   3446  O   ARG A 440      51.172 118.397 -18.140  1.00 42.49           O  
ANISOU 3446  O   ARG A 440     7400   5089   3653    128   2514    924       O  
ATOM   3447  CB  ARG A 440      49.577 121.185 -17.691  1.00 41.63           C  
ANISOU 3447  CB  ARG A 440     7307   4773   3737    -88   2371   1125       C  
ATOM   3448  CG  ARG A 440      49.069 120.566 -18.982  1.00 42.16           C  
ANISOU 3448  CG  ARG A 440     7398   4940   3682    -66   2374   1099       C  
ATOM   3449  CD  ARG A 440      48.199 121.516 -19.788  1.00 42.51           C  
ANISOU 3449  CD  ARG A 440     7451   4979   3722   -147   2314   1195       C  
ATOM   3450  NE  ARG A 440      48.719 122.880 -19.791  1.00 43.16           N  
ANISOU 3450  NE  ARG A 440     7461   5063   3875   -244   2295   1345       N  
ATOM   3451  CZ  ARG A 440      48.051 123.932 -19.331  1.00 42.76           C  
ANISOU 3451  CZ  ARG A 440     7434   4881   3933   -308   2222   1406       C  
ATOM   3452  NH1 ARG A 440      48.599 125.138 -19.369  1.00 43.54           N1+
ANISOU 3452  NH1 ARG A 440     7466   4973   4104   -399   2201   1546       N1+
ATOM   3453  NH2 ARG A 440      46.827 123.779 -18.843  1.00 41.71           N  
ANISOU 3453  NH2 ARG A 440     7389   4620   3839   -283   2169   1328       N  
ATOM   3454  N   GLU A 441      52.629 120.073 -17.755  1.00 43.83           N  
ANISOU 3454  N   GLU A 441     7421   5323   3911     20   2556   1104       N  
ATOM   3455  CA  GLU A 441      53.727 119.371 -18.414  1.00 44.99           C  
ANISOU 3455  CA  GLU A 441     7493   5645   3956     78   2638   1079       C  
ATOM   3456  C   GLU A 441      54.049 118.065 -17.702  1.00 44.54           C  
ANISOU 3456  C   GLU A 441     7486   5557   3882    212   2668    939       C  
ATOM   3457  O   GLU A 441      54.251 117.030 -18.349  1.00 45.11           O  
ANISOU 3457  O   GLU A 441     7563   5718   3858    293   2699    857       O  
ATOM   3458  CB  GLU A 441      54.967 120.263 -18.471  1.00 46.10           C  
ANISOU 3458  CB  GLU A 441     7504   5891   4123     10   2698   1196       C  
ATOM   3459  CG  GLU A 441      55.012 121.201 -19.664  1.00 47.30           C  
ANISOU 3459  CG  GLU A 441     7582   6157   4233   -106   2695   1334       C  
ATOM   3460  CD  GLU A 441      56.318 121.966 -19.747  1.00 48.62           C  
ANISOU 3460  CD  GLU A 441     7610   6439   4423   -180   2765   1447       C  
ATOM   3461  OE1 GLU A 441      56.878 122.308 -18.681  1.00 48.29           O  
ANISOU 3461  OE1 GLU A 441     7540   6323   4487   -186   2784   1458       O  
ATOM   3462  OE2 GLU A 441      56.789 122.219 -20.877  1.00 50.07           O1+
ANISOU 3462  OE2 GLU A 441     7711   6796   4519   -236   2805   1524       O1+
ATOM   3463  N   HIS A 442      54.110 118.095 -16.367  1.00 44.44           N  
ANISOU 3463  N   HIS A 442     7513   5414   3958    237   2655    911       N  
ATOM   3464  CA  HIS A 442      54.328 116.868 -15.608  1.00 44.04           C  
ANISOU 3464  CA  HIS A 442     7526   5313   3894    363   2669    787       C  
ATOM   3465  C   HIS A 442      53.215 115.861 -15.866  1.00 43.44           C  
ANISOU 3465  C   HIS A 442     7563   5159   3781    410   2620    688       C  
ATOM   3466  O   HIS A 442      53.478 114.665 -16.046  1.00 43.80           O  
ANISOU 3466  O   HIS A 442     7640   5233   3767    512   2641    593       O  
ATOM   3467  CB  HIS A 442      54.432 117.179 -14.114  1.00 43.21           C  
ANISOU 3467  CB  HIS A 442     7456   5078   3882    370   2655    785       C  
ATOM   3468  CG  HIS A 442      55.705 117.863 -13.722  1.00 43.93           C  
ANISOU 3468  CG  HIS A 442     7440   5246   4006    355   2719    856       C  
ATOM   3469  ND1 HIS A 442      56.921 117.560 -14.297  1.00 45.21           N  
ANISOU 3469  ND1 HIS A 442     7496   5577   4105    404   2801    857       N  
ATOM   3470  CD2 HIS A 442      55.951 118.831 -12.808  1.00 43.67           C  
ANISOU 3470  CD2 HIS A 442     7352   5146   4094    291   2669    905       C  
ATOM   3471  CE1 HIS A 442      57.861 118.313 -13.754  1.00 45.70           C  
ANISOU 3471  CE1 HIS A 442     7430   5674   4259    364   2788    905       C  
ATOM   3472  NE2 HIS A 442      57.299 119.094 -12.848  1.00 44.78           N  
ANISOU 3472  NE2 HIS A 442     7343   5412   4259    295   2701    933       N  
ATOM   3473  N   HIS A 443      51.963 116.328 -15.885  1.00 41.54           N  
ANISOU 3473  N   HIS A 443     7384   4818   3581    338   2555    707       N  
ATOM   3474  CA  HIS A 443      50.839 115.443 -16.179  1.00 41.06           C  
ANISOU 3474  CA  HIS A 443     7423   4688   3491    367   2515    620       C  
ATOM   3475  C   HIS A 443      51.013 114.768 -17.533  1.00 42.10           C  
ANISOU 3475  C   HIS A 443     7531   4954   3510    403   2544    587       C  
ATOM   3476  O   HIS A 443      50.836 113.551 -17.660  1.00 42.20           O  
ANISOU 3476  O   HIS A 443     7608   4945   3481    484   2546    484       O  
ATOM   3477  CB  HIS A 443      49.524 116.224 -16.139  1.00 40.26           C  
ANISOU 3477  CB  HIS A 443     7364   4488   3443    277   2449    656       C  
ATOM   3478  CG  HIS A 443      49.000 116.463 -14.757  1.00 39.15           C  
ANISOU 3478  CG  HIS A 443     7282   4193   3400    264   2412    635       C  
ATOM   3479  ND1 HIS A 443      47.751 116.995 -14.521  1.00 38.39           N  
ANISOU 3479  ND1 HIS A 443     7233   3996   3356    201   2355    638       N  
ATOM   3480  CD2 HIS A 443      49.551 116.241 -13.540  1.00 38.78           C  
ANISOU 3480  CD2 HIS A 443     7253   4085   3399    309   2425    608       C  
ATOM   3481  CE1 HIS A 443      47.556 117.092 -13.218  1.00 37.61           C  
ANISOU 3481  CE1 HIS A 443     7174   3787   3331    205   2337    610       C  
ATOM   3482  NE2 HIS A 443      48.633 116.641 -12.600  1.00 37.83           N  
ANISOU 3482  NE2 HIS A 443     7188   3834   3353    269   2377    595       N  
ATOM   3483  N   LEU A 444      51.365 115.547 -18.560  1.00 42.83           N  
ANISOU 3483  N   LEU A 444     7534   5188   3551    343   2566    676       N  
ATOM   3484  CA  LEU A 444      51.553 114.982 -19.892  1.00 43.97           C  
ANISOU 3484  CA  LEU A 444     7649   5485   3573    374   2596    647       C  
ATOM   3485  C   LEU A 444      52.699 113.982 -19.944  1.00 44.85           C  
ANISOU 3485  C   LEU A 444     7722   5692   3627    484   2660    567       C  
ATOM   3486  O   LEU A 444      52.734 113.145 -20.854  1.00 45.69           O  
ANISOU 3486  O   LEU A 444     7832   5890   3637    541   2678    493       O  
ATOM   3487  CB  LEU A 444      51.791 116.096 -20.915  1.00 44.93           C  
ANISOU 3487  CB  LEU A 444     7676   5749   3645    279   2610    776       C  
ATOM   3488  CG  LEU A 444      50.578 116.615 -21.697  1.00 44.81           C  
ANISOU 3488  CG  LEU A 444     7705   5717   3603    206   2553    822       C  
ATOM   3489  CD1 LEU A 444      49.421 115.631 -21.629  1.00 44.04           C  
ANISOU 3489  CD1 LEU A 444     7726   5508   3498    259   2511    701       C  
ATOM   3490  CD2 LEU A 444      50.144 117.980 -21.199  1.00 44.20           C  
ANISOU 3490  CD2 LEU A 444     7621   5545   3628    103   2504    941       C  
ATOM   3491  N   ARG A 445      53.638 114.049 -19.000  1.00 44.77           N  
ANISOU 3491  N   ARG A 445     7674   5667   3672    520   2693    573       N  
ATOM   3492  CA  ARG A 445      54.723 113.082 -18.900  1.00 45.60           C  
ANISOU 3492  CA  ARG A 445     7746   5848   3733    641   2748    488       C  
ATOM   3493  C   ARG A 445      54.431 111.989 -17.878  1.00 44.82           C  
ANISOU 3493  C   ARG A 445     7764   5584   3681    739   2714    380       C  
ATOM   3494  O   ARG A 445      55.348 111.269 -17.466  1.00 45.36           O  
ANISOU 3494  O   ARG A 445     7818   5678   3740    848   2748    316       O  
ATOM   3495  CB  ARG A 445      56.035 113.793 -18.565  1.00 46.28           C  
ANISOU 3495  CB  ARG A 445     7706   6040   3838    631   2813    559       C  
ATOM   3496  CG  ARG A 445      56.802 114.269 -19.789  1.00 47.82           C  
ANISOU 3496  CG  ARG A 445     7766   6460   3943    586   2878    622       C  
ATOM   3497  CD  ARG A 445      57.979 115.164 -19.421  1.00 48.48           C  
ANISOU 3497  CD  ARG A 445     7718   6637   4065    542   2943    716       C  
ATOM   3498  NE  ARG A 445      58.983 114.481 -18.608  1.00 48.76           N  
ANISOU 3498  NE  ARG A 445     7724   6683   4119    666   2988    635       N  
ATOM   3499  CZ  ARG A 445      59.103 114.623 -17.292  1.00 47.86           C  
ANISOU 3499  CZ  ARG A 445     7649   6437   4100    692   2973    634       C  
ATOM   3500  NH1 ARG A 445      58.279 115.426 -16.631  1.00 46.63           N1+
ANISOU 3500  NH1 ARG A 445     7558   6127   4030    598   2916    706       N1+
ATOM   3501  NH2 ARG A 445      60.048 113.964 -16.633  1.00 48.30           N  
ANISOU 3501  NH2 ARG A 445     7674   6519   4159    819   3013    557       N  
ATOM   3502  N   GLY A 446      53.175 111.857 -17.458  1.00 43.67           N  
ANISOU 3502  N   GLY A 446     7732   5274   3587    703   2649    363       N  
ATOM   3503  CA  GLY A 446      52.790 110.792 -16.555  1.00 43.07           C  
ANISOU 3503  CA  GLY A 446     7774   5039   3549    778   2616    273       C  
ATOM   3504  C   GLY A 446      53.207 110.979 -15.117  1.00 42.42           C  
ANISOU 3504  C   GLY A 446     7713   4861   3545    802   2612    290       C  
ATOM   3505  O   GLY A 446      53.318 109.990 -14.386  1.00 42.36           O  
ANISOU 3505  O   GLY A 446     7786   4760   3550    892   2599    220       O  
ATOM   3506  N   GLU A 447      53.438 112.214 -14.681  1.00 44.21           N  
ANISOU 3506  N   GLU A 447     7874   5104   3821    725   2620    384       N  
ATOM   3507  CA  GLU A 447      53.829 112.487 -13.307  1.00 43.67           C  
ANISOU 3507  CA  GLU A 447     7822   4953   3819    745   2617    399       C  
ATOM   3508  C   GLU A 447      52.877 113.506 -12.694  1.00 42.56           C  
ANISOU 3508  C   GLU A 447     7710   4704   3756    633   2569    460       C  
ATOM   3509  O   GLU A 447      52.059 114.127 -13.379  1.00 42.31           O  
ANISOU 3509  O   GLU A 447     7668   4676   3731    542   2542    501       O  
ATOM   3510  CB  GLU A 447      55.274 112.998 -13.219  1.00 44.55           C  
ANISOU 3510  CB  GLU A 447     7810   5197   3919    776   2684    442       C  
ATOM   3511  CG  GLU A 447      56.333 112.000 -13.659  1.00 45.77           C  
ANISOU 3511  CG  GLU A 447     7922   5465   4002    906   2734    367       C  
ATOM   3512  CD  GLU A 447      57.702 112.332 -13.096  1.00 46.47           C  
ANISOU 3512  CD  GLU A 447     7911   5646   4101    964   2794    386       C  
ATOM   3513  OE1 GLU A 447      57.856 112.307 -11.854  1.00 46.25           O  
ANISOU 3513  OE1 GLU A 447     7932   5521   4121   1007   2777    374       O  
ATOM   3514  OE2 GLU A 447      58.617 112.633 -13.893  1.00 47.62           O1+
ANISOU 3514  OE2 GLU A 447     7922   5968   4202    964   2862    412       O1+
ATOM   3515  N   CYS A 448      52.996 113.669 -11.379  1.00 40.54           N  
ANISOU 3515  N   CYS A 448     7492   4357   3555    649   2556    459       N  
ATOM   3516  CA  CYS A 448      52.222 114.651 -10.633  1.00 39.61           C  
ANISOU 3516  CA  CYS A 448     7396   4141   3512    557   2513    505       C  
ATOM   3517  C   CYS A 448      53.085 115.142  -9.481  1.00 39.62           C  
ANISOU 3517  C   CYS A 448     7372   4135   3548    581   2535    531       C  
ATOM   3518  O   CYS A 448      53.634 114.329  -8.732  1.00 39.80           O  
ANISOU 3518  O   CYS A 448     7436   4135   3550    683   2544    475       O  
ATOM   3519  CB  CYS A 448      50.912 114.045 -10.116  1.00 38.73           C  
ANISOU 3519  CB  CYS A 448     7403   3888   3424    549   2455    444       C  
ATOM   3520  SG  CYS A 448      49.830 115.201  -9.255  1.00 37.69           S  
ANISOU 3520  SG  CYS A 448     7293   3649   3379    443   2402    478       S  
ATOM   3521  N   HIS A 449      53.214 116.464  -9.350  1.00 40.80           N  
ANISOU 3521  N   HIS A 449     7435   4296   3769    488   2515    610       N  
ATOM   3522  CA  HIS A 449      54.155 117.054  -8.407  1.00 41.03           C  
ANISOU 3522  CA  HIS A 449     7367   4338   3886    494   2471    621       C  
ATOM   3523  C   HIS A 449      53.527 117.983  -7.376  1.00 40.28           C  
ANISOU 3523  C   HIS A 449     7281   4132   3892    424   2391    632       C  
ATOM   3524  O   HIS A 449      54.039 118.058  -6.257  1.00 40.27           O  
ANISOU 3524  O   HIS A 449     7255   4104   3943    462   2343    599       O  
ATOM   3525  CB  HIS A 449      55.255 117.828  -9.158  1.00 42.07           C  
ANISOU 3525  CB  HIS A 449     7338   4607   4040    449   2500    695       C  
ATOM   3526  CG  HIS A 449      56.271 116.946  -9.815  1.00 43.08           C  
ANISOU 3526  CG  HIS A 449     7416   4868   4083    543   2573    665       C  
ATOM   3527  ND1 HIS A 449      56.078 115.592  -9.988  1.00 43.06           N  
ANISOU 3527  ND1 HIS A 449     7520   4856   3987    655   2608    582       N  
ATOM   3528  CD2 HIS A 449      57.491 117.221 -10.332  1.00 44.24           C  
ANISOU 3528  CD2 HIS A 449     7417   5165   4230    545   2615    699       C  
ATOM   3529  CE1 HIS A 449      57.133 115.072 -10.589  1.00 44.17           C  
ANISOU 3529  CE1 HIS A 449     7580   5132   4070    732   2666    559       C  
ATOM   3530  NE2 HIS A 449      58.005 116.039 -10.808  1.00 44.90           N  
ANISOU 3530  NE2 HIS A 449     7514   5332   4214    666   2676    629       N  
ATOM   3531  N   SER A 450      52.444 118.692  -7.705  1.00 41.06           N  
ANISOU 3531  N   SER A 450     7412   4170   4019    330   2369    669       N  
ATOM   3532  CA  SER A 450      51.911 119.708  -6.805  1.00 40.60           C  
ANISOU 3532  CA  SER A 450     7342   4018   4066    265   2289    674       C  
ATOM   3533  C   SER A 450      50.520 119.411  -6.265  1.00 40.09           C  
ANISOU 3533  C   SER A 450     7401   3842   3990    260   2266    619       C  
ATOM   3534  O   SER A 450      50.127 120.017  -5.264  1.00 40.29           O  
ANISOU 3534  O   SER A 450     7426   3793   4088    236   2203    594       O  
ATOM   3535  CB  SER A 450      51.868 121.073  -7.506  1.00 41.26           C  
ANISOU 3535  CB  SER A 450     7336   4116   4225    151   2262    769       C  
ATOM   3536  OG  SER A 450      50.659 121.226  -8.227  1.00 40.92           O  
ANISOU 3536  OG  SER A 450     7362   4030   4156     99   2264    791       O  
ATOM   3537  N   CYS A 451      49.771 118.507  -6.891  1.00 38.58           N  
ANISOU 3537  N   CYS A 451     7307   3641   3710    280   2315    594       N  
ATOM   3538  CA  CYS A 451      48.358 118.304  -6.570  1.00 37.81           C  
ANISOU 3538  CA  CYS A 451     7311   3449   3606    254   2299    549       C  
ATOM   3539  C   CYS A 451      48.229 117.513  -5.274  1.00 37.46           C  
ANISOU 3539  C   CYS A 451     7346   3341   3545    316   2290    476       C  
ATOM   3540  O   CYS A 451      48.284 116.282  -5.273  1.00 37.50           O  
ANISOU 3540  O   CYS A 451     7416   3342   3491    383   2312    430       O  
ATOM   3541  CB  CYS A 451      47.656 117.597  -7.722  1.00 37.76           C  
ANISOU 3541  CB  CYS A 451     7327   3466   3554    252   2299    522       C  
ATOM   3542  SG  CYS A 451      47.874 118.426  -9.311  1.00 38.39           S  
ANISOU 3542  SG  CYS A 451     7313   3644   3628    189   2304    610       S  
ATOM   3543  N   VAL A 452      48.030 118.225  -4.164  1.00 36.60           N  
ANISOU 3543  N   VAL A 452     7215   3182   3507    294   2231    458       N  
ATOM   3544  CA  VAL A 452      47.852 117.632  -2.844  1.00 36.37           C  
ANISOU 3544  CA  VAL A 452     7260   3102   3459    344   2218    397       C  
ATOM   3545  C   VAL A 452      46.639 118.281  -2.188  1.00 35.85           C  
ANISOU 3545  C   VAL A 452     7215   2969   3439    282   2179    364       C  
ATOM   3546  O   VAL A 452      46.340 119.456  -2.424  1.00 35.77           O  
ANISOU 3546  O   VAL A 452     7132   2951   3510    218   2134    385       O  
ATOM   3547  CB  VAL A 452      49.123 117.800  -1.973  1.00 36.82           C  
ANISOU 3547  CB  VAL A 452     7253   3193   3543    404   2182    394       C  
ATOM   3548  CG1 VAL A 452      48.916 117.242  -0.573  1.00 36.70           C  
ANISOU 3548  CG1 VAL A 452     7319   3130   3496    455   2161    339       C  
ATOM   3549  CG2 VAL A 452      50.318 117.128  -2.637  1.00 37.46           C  
ANISOU 3549  CG2 VAL A 452     7301   3351   3579    473   2222    416       C  
ATOM   3550  N   TYR A 453      45.931 117.505  -1.367  1.00 34.69           N  
ANISOU 3550  N   TYR A 453     7167   2772   3240    302   2196    312       N  
ATOM   3551  CA  TYR A 453      44.694 117.959  -0.741  1.00 34.30           C  
ANISOU 3551  CA  TYR A 453     7139   2674   3218    248   2173    269       C  
ATOM   3552  C   TYR A 453      44.946 118.647   0.597  1.00 34.38           C  
ANISOU 3552  C   TYR A 453     7111   2680   3273    263   2115    233       C  
ATOM   3553  O   TYR A 453      45.838 118.259   1.359  1.00 34.70           O  
ANISOU 3553  O   TYR A 453     7161   2739   3284    328   2106    228       O  
ATOM   3554  CB  TYR A 453      43.736 116.784  -0.532  1.00 34.15           C  
ANISOU 3554  CB  TYR A 453     7224   2615   3137    247   2210    226       C  
ATOM   3555  CG  TYR A 453      42.911 116.435  -1.749  1.00 34.00           C  
ANISOU 3555  CG  TYR A 453     7193   2589   3135    205   2206    217       C  
ATOM   3556  CD1 TYR A 453      43.247 115.355  -2.556  1.00 34.23           C  
ANISOU 3556  CD1 TYR A 453     7240   2627   3138    241   2213    220       C  
ATOM   3557  CD2 TYR A 453      41.792 117.184  -2.089  1.00 33.72           C  
ANISOU 3557  CD2 TYR A 453     7137   2540   3134    135   2198    202       C  
ATOM   3558  CE1 TYR A 453      42.493 115.033  -3.667  1.00 34.18           C  
ANISOU 3558  CE1 TYR A 453     7232   2620   3136    204   2211    206       C  
ATOM   3559  CE2 TYR A 453      41.032 116.869  -3.198  1.00 33.66           C  
ANISOU 3559  CE2 TYR A 453     7125   2535   3130    101   2194    191       C  
ATOM   3560  CZ  TYR A 453      41.387 115.793  -3.983  1.00 33.89           C  
ANISOU 3560  CZ  TYR A 453     7172   2576   3129    134   2200    191       C  
ATOM   3561  OH  TYR A 453      40.633 115.476  -5.090  1.00 33.92           O  
ANISOU 3561  OH  TYR A 453     7179   2584   3126    102   2198    177       O  
ATOM   3562  N   ASN A 454      44.141 119.673   0.872  1.00 34.49           N  
ANISOU 3562  N   ASN A 454     7079   2670   3357    208   2069    202       N  
ATOM   3563  CA  ASN A 454      44.071 120.316   2.179  1.00 34.61           C  
ANISOU 3563  CA  ASN A 454     7067   2678   3406    219   2015    144       C  
ATOM   3564  C   ASN A 454      42.781 119.888   2.864  1.00 34.43           C  
ANISOU 3564  C   ASN A 454     7117   2633   3331    199   2046     83       C  
ATOM   3565  O   ASN A 454      41.701 119.998   2.277  1.00 34.18           O  
ANISOU 3565  O   ASN A 454     7091   2580   3314    145   2064     70       O  
ATOM   3566  CB  ASN A 454      44.104 121.843   2.061  1.00 34.72           C  
ANISOU 3566  CB  ASN A 454     6969   2678   3546    177   1933    139       C  
ATOM   3567  CG  ASN A 454      45.402 122.365   1.481  1.00 35.08           C  
ANISOU 3567  CG  ASN A 454     6929   2748   3651    181   1901    204       C  
ATOM   3568  OD1 ASN A 454      46.408 122.478   2.181  1.00 35.67           O  
ANISOU 3568  OD1 ASN A 454     6966   2849   3739    223   1868    195       O  
ATOM   3569  ND2 ASN A 454      45.378 122.716   0.200  1.00 35.08           N  
ANISOU 3569  ND2 ASN A 454     6893   2748   3687    134   1910    271       N  
ATOM   3570  N   MET A 455      42.890 119.410   4.099  1.00 34.76           N  
ANISOU 3570  N   MET A 455     7211   2688   3310    240   2052     46       N  
ATOM   3571  CA  MET A 455      41.733 118.941   4.845  1.00 34.77           C  
ANISOU 3571  CA  MET A 455     7282   2682   3248    217   2092     -6       C  
ATOM   3572  C   MET A 455      41.593 119.737   6.134  1.00 35.08           C  
ANISOU 3572  C   MET A 455     7278   2746   3303    231   2040    -78       C  
ATOM   3573  O   MET A 455      42.584 120.173   6.730  1.00 35.56           O  
ANISOU 3573  O   MET A 455     7298   2829   3384    280   1983    -84       O  
ATOM   3574  CB  MET A 455      41.826 117.442   5.161  1.00 34.98           C  
ANISOU 3574  CB  MET A 455     7434   2699   3156    247   2162     23       C  
ATOM   3575  CG  MET A 455      40.459 116.762   5.268  1.00 34.96           C  
ANISOU 3575  CG  MET A 455     7461   2678   3145    182   2183      6       C  
ATOM   3576  SD  MET A 455      40.538 114.960   5.220  1.00 35.29           S  
ANISOU 3576  SD  MET A 455     7581   2676   3151    195   2188     56       S  
ATOM   3577  CE  MET A 455      41.133 114.597   6.867  1.00 35.95           C  
ANISOU 3577  CE  MET A 455     7722   2785   3152    256   2174     61       C  
ATOM   3578  N   MET A 456      40.348 119.906   6.563  1.00 35.15           N  
ANISOU 3578  N   MET A 456     7294   2760   3302    189   2060   -141       N  
ATOM   3579  CA  MET A 456      40.025 120.735   7.713  1.00 35.52           C  
ANISOU 3579  CA  MET A 456     7292   2840   3364    200   2013   -228       C  
ATOM   3580  C   MET A 456      38.550 120.530   8.031  1.00 35.62           C  
ANISOU 3580  C   MET A 456     7328   2869   3336    149   2068   -288       C  
ATOM   3581  O   MET A 456      37.825 119.829   7.316  1.00 35.37           O  
ANISOU 3581  O   MET A 456     7342   2817   3280    101   2132   -260       O  
ATOM   3582  CB  MET A 456      40.336 122.209   7.434  1.00 35.73           C  
ANISOU 3582  CB  MET A 456     7198   2847   3529    200   1914   -260       C  
ATOM   3583  CG  MET A 456      39.724 122.706   6.130  1.00 35.53           C  
ANISOU 3583  CG  MET A 456     7127   2777   3595    145   1906   -235       C  
ATOM   3584  SD  MET A 456      40.612 124.114   5.442  1.00 37.85           S  
ANISOU 3584  SD  MET A 456     7307   3028   4044    142   1798   -204       S  
ATOM   3585  CE  MET A 456      40.184 125.405   6.606  1.00 39.17           C  
ANISOU 3585  CE  MET A 456     7398   3193   4293    159   1705   -332       C  
ATOM   3586  N   GLY A 457      38.107 121.171   9.106  1.00 34.65           N  
ANISOU 3586  N   GLY A 457     7165   2791   3209    161   2040   -380       N  
ATOM   3587  CA  GLY A 457      36.724 121.075   9.518  1.00 34.91           C  
ANISOU 3587  CA  GLY A 457     7200   2861   3204    116   2093   -450       C  
ATOM   3588  C   GLY A 457      35.903 122.219   8.951  1.00 34.79           C  
ANISOU 3588  C   GLY A 457     7079   2827   3314     89   2039   -520       C  
ATOM   3589  O   GLY A 457      36.334 123.369   8.947  1.00 34.85           O  
ANISOU 3589  O   GLY A 457     7005   2813   3425    120   1944   -557       O  
ATOM   3590  N   LYS A 458      34.714 121.880   8.466  1.00 35.84           N  
ANISOU 3590  N   LYS A 458     7214   2962   3440     31   2096   -538       N  
ATOM   3591  CA  LYS A 458      33.785 122.880   7.965  1.00 35.86           C  
ANISOU 3591  CA  LYS A 458     7120   2952   3553     11   2046   -611       C  
ATOM   3592  C   LYS A 458      33.075 123.554   9.130  1.00 36.56           C  
ANISOU 3592  C   LYS A 458     7146   3108   3639     31   2029   -744       C  
ATOM   3593  O   LYS A 458      32.742 122.913  10.130  1.00 37.09           O  
ANISOU 3593  O   LYS A 458     7249   3251   3593     23   2096   -771       O  
ATOM   3594  CB  LYS A 458      32.761 122.245   7.021  1.00 35.63           C  
ANISOU 3594  CB  LYS A 458     7110   2911   3518    -54   2108   -591       C  
ATOM   3595  CG  LYS A 458      31.960 123.246   6.213  1.00 35.62           C  
ANISOU 3595  CG  LYS A 458     7012   2882   3639    -66   2040   -642       C  
ATOM   3596  CD  LYS A 458      30.768 122.603   5.514  1.00 35.60           C  
ANISOU 3596  CD  LYS A 458     7018   2891   3619   -130   2102   -652       C  
ATOM   3597  CE  LYS A 458      29.994 123.612   4.666  1.00 35.67           C  
ANISOU 3597  CE  LYS A 458     6932   2872   3750   -131   2021   -699       C  
ATOM   3598  NZ  LYS A 458      30.670 123.913   3.370  1.00 35.29           N1+
ANISOU 3598  NZ  LYS A 458     6892   2750   3765   -125   1961   -599       N1+
ATOM   3599  N   ARG A 459      32.851 124.856   8.996  1.00 35.63           N  
ANISOU 3599  N   ARG A 459     6927   2964   3646     58   1932   -821       N  
ATOM   3600  CA  ARG A 459      32.294 125.681  10.062  1.00 36.40           C  
ANISOU 3600  CA  ARG A 459     6951   3119   3760     95   1894   -965       C  
ATOM   3601  C   ARG A 459      30.805 125.867   9.789  1.00 36.70           C  
ANISOU 3601  C   ARG A 459     6927   3188   3831     62   1918  -1051       C  
ATOM   3602  O   ARG A 459      30.412 126.684   8.953  1.00 36.63           O  
ANISOU 3602  O   ARG A 459     6850   3117   3950     66   1842  -1071       O  
ATOM   3603  CB  ARG A 459      33.030 127.013  10.131  1.00 36.59           C  
ANISOU 3603  CB  ARG A 459     6903   3084   3915    151   1759  -1005       C  
ATOM   3604  CG  ARG A 459      32.817 127.758  11.426  1.00 37.48           C  
ANISOU 3604  CG  ARG A 459     6958   3259   4024    206   1715  -1156       C  
ATOM   3605  CD  ARG A 459      34.033 127.695  12.335  1.00 37.69           C  
ANISOU 3605  CD  ARG A 459     7020   3310   3990    252   1689  -1144       C  
ATOM   3606  NE  ARG A 459      33.712 128.139  13.689  1.00 38.65           N  
ANISOU 3606  NE  ARG A 459     7103   3523   4060    303   1672  -1293       N  
ATOM   3607  CZ  ARG A 459      33.551 129.410  14.042  1.00 39.32           C  
ANISOU 3607  CZ  ARG A 459     7094   3587   4258    352   1563  -1427       C  
ATOM   3608  NH1 ARG A 459      33.256 129.716  15.297  1.00 40.28           N1+
ANISOU 3608  NH1 ARG A 459     7184   3808   4312    403   1557  -1570       N1+
ATOM   3609  NH2 ARG A 459      33.680 130.377  13.141  1.00 39.13           N  
ANISOU 3609  NH2 ARG A 459     7011   3444   4413    352   1458  -1418       N  
ATOM   3610  N   GLU A 460      29.977 125.115  10.508  1.00 37.17           N  
ANISOU 3610  N   GLU A 460     7006   3344   3773     30   2022  -1099       N  
ATOM   3611  CA  GLU A 460      28.538 125.090  10.297  1.00 37.56           C  
ANISOU 3611  CA  GLU A 460     6990   3443   3838    -11   2062  -1177       C  
ATOM   3612  C   GLU A 460      27.800 125.482  11.571  1.00 38.61           C  
ANISOU 3612  C   GLU A 460     7035   3704   3933     13   2066  -1313       C  
ATOM   3613  O   GLU A 460      28.393 125.657  12.637  1.00 39.04           O  
ANISOU 3613  O   GLU A 460     7094   3810   3928     59   2047  -1342       O  
ATOM   3614  CB  GLU A 460      28.075 123.701   9.840  1.00 37.30           C  
ANISOU 3614  CB  GLU A 460     7009   3438   3727   -100   2157  -1071       C  
ATOM   3615  CG  GLU A 460      28.416 123.366   8.401  1.00 36.44           C  
ANISOU 3615  CG  GLU A 460     6963   3220   3664   -127   2156   -970       C  
ATOM   3616  CD  GLU A 460      28.402 121.876   8.138  1.00 36.22           C  
ANISOU 3616  CD  GLU A 460     7010   3202   3549   -200   2234   -851       C  
ATOM   3617  OE1 GLU A 460      28.504 121.104   9.116  1.00 36.63           O  
ANISOU 3617  OE1 GLU A 460     7090   3318   3509   -221   2277   -816       O  
ATOM   3618  OE2 GLU A 460      28.290 121.477   6.958  1.00 35.73           O1+
ANISOU 3618  OE2 GLU A 460     6983   3080   3515   -235   2246   -794       O1+
ATOM   3619  N   LYS A 461      26.482 125.616  11.435  1.00 39.13           N  
ANISOU 3619  N   LYS A 461     7015   3827   4027    -14   2090  -1403       N  
ATOM   3620  CA  LYS A 461      25.564 125.823  12.552  1.00 40.28           C  
ANISOU 3620  CA  LYS A 461     7064   4119   4122     -3   2115  -1534       C  
ATOM   3621  C   LYS A 461      24.748 124.543  12.705  1.00 40.60           C  
ANISOU 3621  C   LYS A 461     7114   4255   4057   -102   2231  -1472       C  
ATOM   3622  O   LYS A 461      23.817 124.299  11.931  1.00 40.58           O  
ANISOU 3622  O   LYS A 461     7077   4247   4096   -156   2266  -1485       O  
ATOM   3623  CB  LYS A 461      24.661 127.029  12.305  1.00 40.84           C  
ANISOU 3623  CB  LYS A 461     7015   4183   4320     50   2047  -1702       C  
ATOM   3624  CG  LYS A 461      25.402 128.326  12.043  1.00 40.66           C  
ANISOU 3624  CG  LYS A 461     6981   4034   4434    139   1914  -1756       C  
ATOM   3625  CD  LYS A 461      24.444 129.467  11.746  1.00 41.34           C  
ANISOU 3625  CD  LYS A 461     6936   4107   4666    193   1818  -1901       C  
ATOM   3626  CE  LYS A 461      25.190 130.781  11.594  1.00 41.38           C  
ANISOU 3626  CE  LYS A 461     6909   3989   4824    277   1651  -1931       C  
ATOM   3627  NZ  LYS A 461      24.250 131.914  11.377  1.00 42.23           N1+
ANISOU 3627  NZ  LYS A 461     6894   4074   5079    341   1546  -2080       N1+
ATOM   3628  N   LYS A 462      25.098 123.726  13.697  1.00 40.99           N  
ANISOU 3628  N   LYS A 462     7214   4384   3975   -127   2286  -1405       N  
ATOM   3629  CA  LYS A 462      24.436 122.449  13.926  1.00 41.44           C  
ANISOU 3629  CA  LYS A 462     7296   4512   3936   -227   2391  -1330       C  
ATOM   3630  C   LYS A 462      24.047 122.324  15.393  1.00 42.74           C  
ANISOU 3630  C   LYS A 462     7415   4839   3984   -224   2435  -1387       C  
ATOM   3631  O   LYS A 462      24.484 123.101  16.246  1.00 43.17           O  
ANISOU 3631  O   LYS A 462     7439   4948   4016   -139   2382  -1469       O  
ATOM   3632  CB  LYS A 462      25.327 121.271  13.507  1.00 40.66           C  
ANISOU 3632  CB  LYS A 462     7337   4320   3793   -275   2417  -1147       C  
ATOM   3633  CG  LYS A 462      25.560 121.178  12.007  1.00 39.55           C  
ANISOU 3633  CG  LYS A 462     7241   4041   3746   -293   2394  -1082       C  
ATOM   3634  CD  LYS A 462      25.248 119.784  11.483  1.00 39.45           C  
ANISOU 3634  CD  LYS A 462     7300   3993   3697   -394   2466   -969       C  
ATOM   3635  CE  LYS A 462      26.511 118.954  11.305  1.00 38.80           C  
ANISOU 3635  CE  LYS A 462     7347   3817   3579   -385   2454   -820       C  
ATOM   3636  NZ  LYS A 462      26.197 117.532  10.988  1.00 38.96           N1+
ANISOU 3636  NZ  LYS A 462     7442   3797   3564   -477   2517   -725       N1+
ATOM   3637  N   GLN A 463      23.206 121.332  15.678  1.00 43.48           N  
ANISOU 3637  N   GLN A 463     7506   5011   4003   -320   2531  -1346       N  
ATOM   3638  CA  GLN A 463      22.822 121.053  17.054  1.00 44.86           C  
ANISOU 3638  CA  GLN A 463     7649   5347   4050   -331   2586  -1376       C  
ATOM   3639  C   GLN A 463      24.023 120.542  17.841  1.00 44.83           C  
ANISOU 3639  C   GLN A 463     7759   5332   3943   -302   2571  -1266       C  
ATOM   3640  O   GLN A 463      24.863 119.807  17.316  1.00 43.96           O  
ANISOU 3640  O   GLN A 463     7766   5098   3839   -323   2562  -1126       O  
ATOM   3641  CB  GLN A 463      21.686 120.031  17.095  1.00 45.73           C  
ANISOU 3641  CB  GLN A 463     7740   5526   4111   -455   2696  -1339       C  
ATOM   3642  CG  GLN A 463      20.334 120.606  17.505  1.00 46.99           C  
ANISOU 3642  CG  GLN A 463     7742   5841   4272   -462   2737  -1499       C  
ATOM   3643  CD  GLN A 463      20.254 120.918  18.991  1.00 48.39           C  
ANISOU 3643  CD  GLN A 463     7867   6191   4327   -410   2753  -1569       C  
ATOM   3644  OE1 GLN A 463      21.166 120.599  19.754  1.00 48.48           O  
ANISOU 3644  OE1 GLN A 463     7967   6212   4242   -381   2740  -1488       O  
ATOM   3645  NE2 GLN A 463      19.157 121.541  19.408  1.00 49.58           N  
ANISOU 3645  NE2 GLN A 463     7873   6488   4478   -392   2778  -1723       N  
ATOM   3646  N   GLY A 464      24.103 120.943  19.105  1.00 45.89           N  
ANISOU 3646  N   GLY A 464     7854   5601   3980   -244   2565  -1337       N  
ATOM   3647  CA  GLY A 464      25.241 120.599  19.931  1.00 46.02           C  
ANISOU 3647  CA  GLY A 464     7968   5622   3894   -200   2541  -1256       C  
ATOM   3648  C   GLY A 464      25.278 119.130  20.305  1.00 46.54           C  
ANISOU 3648  C   GLY A 464     8137   5693   3853   -289   2618  -1096       C  
ATOM   3649  O   GLY A 464      24.343 118.360  20.082  1.00 47.02           O  
ANISOU 3649  O   GLY A 464     8189   5771   3906   -392   2698  -1055       O  
ATOM   3650  N   GLU A 465      26.406 118.739  20.892  1.00 46.55           N  
ANISOU 3650  N   GLU A 465     8242   5672   3773   -245   2587  -1008       N  
ATOM   3651  CA  GLU A 465      26.641 117.371  21.332  1.00 47.15           C  
ANISOU 3651  CA  GLU A 465     8433   5735   3747   -308   2639   -852       C  
ATOM   3652  C   GLU A 465      27.166 117.410  22.758  1.00 48.34           C  
ANISOU 3652  C   GLU A 465     8608   6015   3744   -246   2629   -857       C  
ATOM   3653  O   GLU A 465      28.128 118.130  23.043  1.00 47.98           O  
ANISOU 3653  O   GLU A 465     8572   5965   3693   -144   2550   -904       O  
ATOM   3654  CB  GLU A 465      27.631 116.659  20.408  1.00 45.90           C  
ANISOU 3654  CB  GLU A 465     8401   5386   3653   -310   2604   -717       C  
ATOM   3655  CG  GLU A 465      27.726 115.164  20.630  1.00 46.52           C  
ANISOU 3655  CG  GLU A 465     8600   5415   3660   -382   2655   -564       C  
ATOM   3656  CD  GLU A 465      28.757 114.512  19.734  1.00 45.38           C  
ANISOU 3656  CD  GLU A 465     8574   5087   3581   -363   2611   -452       C  
ATOM   3657  OE1 GLU A 465      29.291 115.204  18.838  1.00 44.07           O  
ANISOU 3657  OE1 GLU A 465     8388   4838   3519   -310   2553   -486       O  
ATOM   3658  OE2 GLU A 465      29.036 113.310  19.926  1.00 45.90           O1+
ANISOU 3658  OE2 GLU A 465     8752   5092   3594   -397   2634   -332       O1+
ATOM   3659  N   PHE A 466      26.541 116.631  23.639  1.00 49.85           N  
ANISOU 3659  N   PHE A 466     8811   6321   3809   -311   2707   -807       N  
ATOM   3660  CA  PHE A 466      26.781 116.699  25.086  1.00 51.34           C  
ANISOU 3660  CA  PHE A 466     9003   6674   3829   -260   2711   -824       C  
ATOM   3661  C   PHE A 466      26.486 118.141  25.494  1.00 51.60           C  
ANISOU 3661  C   PHE A 466     8897   6839   3870   -171   2671  -1024       C  
ATOM   3662  O   PHE A 466      25.425 118.669  25.125  1.00 51.68           O  
ANISOU 3662  O   PHE A 466     8790   6897   3950   -197   2702  -1132       O  
ATOM   3663  CB  PHE A 466      28.180 116.189  25.420  1.00 51.12           C  
ANISOU 3663  CB  PHE A 466     9116   6569   3740   -202   2654   -711       C  
ATOM   3664  CG  PHE A 466      28.652 115.079  24.525  1.00 50.23           C  
ANISOU 3664  CG  PHE A 466     9129   6261   3695   -256   2656   -552       C  
ATOM   3665  CD1 PHE A 466      27.982 113.868  24.483  1.00 50.99           C  
ANISOU 3665  CD1 PHE A 466     9281   6331   3763   -369   2736   -441       C  
ATOM   3666  CD2 PHE A 466      29.769 115.248  23.725  1.00 48.74           C  
ANISOU 3666  CD2 PHE A 466     9002   5917   3601   -191   2578   -522       C  
ATOM   3667  CE1 PHE A 466      28.414 112.847  23.655  1.00 50.28           C  
ANISOU 3667  CE1 PHE A 466     9307   6056   3741   -408   2731   -313       C  
ATOM   3668  CE2 PHE A 466      30.206 114.228  22.899  1.00 48.03           C  
ANISOU 3668  CE2 PHE A 466     9023   5655   3571   -227   2579   -390       C  
ATOM   3669  CZ  PHE A 466      29.527 113.028  22.864  1.00 48.79           C  
ANISOU 3669  CZ  PHE A 466     9175   5721   3642   -333   2651   -292       C  
ATOM   3670  N   GLY A 467      27.367 118.812  26.226  1.00 51.82           N  
ANISOU 3670  N   GLY A 467     8932   6923   3836    -61   2598  -1090       N  
ATOM   3671  CA  GLY A 467      27.127 120.197  26.574  1.00 52.13           C  
ANISOU 3671  CA  GLY A 467     8843   7066   3898     32   2546  -1295       C  
ATOM   3672  C   GLY A 467      27.719 121.166  25.573  1.00 50.51           C  
ANISOU 3672  C   GLY A 467     8617   6708   3868     95   2451  -1372       C  
ATOM   3673  O   GLY A 467      27.307 122.328  25.502  1.00 50.57           O  
ANISOU 3673  O   GLY A 467     8511   6752   3951    156   2406  -1546       O  
ATOM   3674  N   LYS A 468      28.671 120.691  24.775  1.00 49.18           N  
ANISOU 3674  N   LYS A 468     8557   6361   3767     84   2418  -1244       N  
ATOM   3675  CA  LYS A 468      29.499 121.548  23.943  1.00 47.80           C  
ANISOU 3675  CA  LYS A 468     8385   6044   3735    150   2324  -1293       C  
ATOM   3676  C   LYS A 468      29.052 121.495  22.483  1.00 46.49           C  
ANISOU 3676  C   LYS A 468     8204   5732   3728     87   2338  -1254       C  
ATOM   3677  O   LYS A 468      28.062 120.852  22.122  1.00 46.64           O  
ANISOU 3677  O   LYS A 468     8204   5764   3753     -6   2417  -1208       O  
ATOM   3678  CB  LYS A 468      30.969 121.144  24.071  1.00 47.35           C  
ANISOU 3678  CB  LYS A 468     8452   5902   3635    198   2271  -1187       C  
ATOM   3679  CG  LYS A 468      31.400 120.803  25.491  1.00 48.76           C  
ANISOU 3679  CG  LYS A 468     8676   6221   3629    240   2272  -1176       C  
ATOM   3680  CD  LYS A 468      31.292 122.005  26.409  1.00 49.75           C  
ANISOU 3680  CD  LYS A 468     8700   6488   3714    330   2218  -1376       C  
ATOM   3681  CE  LYS A 468      32.435 122.023  27.409  1.00 50.47           C  
ANISOU 3681  CE  LYS A 468     8861   6634   3680    414   2157  -1378       C  
ATOM   3682  NZ  LYS A 468      32.436 123.263  28.231  1.00 51.40           N1+
ANISOU 3682  NZ  LYS A 468     8882   6873   3776    509   2088  -1591       N1+
ATOM   3683  N   ALA A 469      29.816 122.180  21.634  1.00 45.28           N  
ANISOU 3683  N   ALA A 469     8061   5442   3702    136   2260  -1274       N  
ATOM   3684  CA  ALA A 469      29.543 122.233  20.209  1.00 44.05           C  
ANISOU 3684  CA  ALA A 469     7897   5147   3694     90   2261  -1239       C  
ATOM   3685  C   ALA A 469      29.953 120.931  19.532  1.00 43.32           C  
ANISOU 3685  C   ALA A 469     7922   4948   3589     21   2306  -1049       C  
ATOM   3686  O   ALA A 469      30.903 120.262  19.946  1.00 43.38           O  
ANISOU 3686  O   ALA A 469     8029   4935   3517     43   2298   -948       O  
ATOM   3687  CB  ALA A 469      30.282 123.407  19.573  1.00 43.20           C  
ANISOU 3687  CB  ALA A 469     7766   4928   3720    167   2162  -1316       C  
ATOM   3688  N   LYS A 470      29.230 120.586  18.471  1.00 42.71           N  
ANISOU 3688  N   LYS A 470     7831   4801   3595    -54   2346  -1011       N  
ATOM   3689  CA  LYS A 470      29.466 119.332  17.772  1.00 42.14           C  
ANISOU 3689  CA  LYS A 470     7863   4627   3524   -122   2386   -852       C  
ATOM   3690  C   LYS A 470      30.780 119.375  17.000  1.00 41.00           C  
ANISOU 3690  C   LYS A 470     7794   4345   3439    -69   2326   -777       C  
ATOM   3691  O   LYS A 470      31.275 120.442  16.625  1.00 40.43           O  
ANISOU 3691  O   LYS A 470     7683   4234   3446     -6   2261   -847       O  
ATOM   3692  CB  LYS A 470      28.314 119.038  16.811  1.00 41.88           C  
ANISOU 3692  CB  LYS A 470     7787   4561   3566   -212   2439   -853       C  
ATOM   3693  CG  LYS A 470      28.267 117.607  16.302  1.00 41.73           C  
ANISOU 3693  CG  LYS A 470     7866   4459   3531   -296   2492   -712       C  
ATOM   3694  CD  LYS A 470      27.276 117.467  15.162  1.00 41.32           C  
ANISOU 3694  CD  LYS A 470     7772   4358   3571   -374   2527   -728       C  
ATOM   3695  CE  LYS A 470      26.704 116.065  15.113  1.00 41.89           C  
ANISOU 3695  CE  LYS A 470     7908   4407   3602   -478   2601   -639       C  
ATOM   3696  NZ  LYS A 470      26.000 115.750  16.388  1.00 43.36           N1+
ANISOU 3696  NZ  LYS A 470     8066   4732   3679   -520   2663   -661       N1+
ATOM   3697  N   GLY A 471      31.346 118.192  16.768  1.00 40.79           N  
ANISOU 3697  N   GLY A 471     7877   4244   3377    -95   2347   -637       N  
ATOM   3698  CA  GLY A 471      32.492 118.084  15.890  1.00 39.77           C  
ANISOU 3698  CA  GLY A 471     7815   3989   3305    -53   2302   -561       C  
ATOM   3699  C   GLY A 471      32.156 118.499  14.470  1.00 38.78           C  
ANISOU 3699  C   GLY A 471     7648   3779   3306    -82   2296   -575       C  
ATOM   3700  O   GLY A 471      30.994 118.590  14.070  1.00 38.85           O  
ANISOU 3700  O   GLY A 471     7596   3808   3357   -145   2332   -622       O  
ATOM   3701  N   SER A 472      33.202 118.751  13.693  1.00 37.94           N  
ANISOU 3701  N   SER A 472     7576   3582   3256    -33   2251   -534       N  
ATOM   3702  CA  SER A 472      33.061 119.354  12.376  1.00 37.08           C  
ANISOU 3702  CA  SER A 472     7429   3399   3260    -44   2234   -552       C  
ATOM   3703  C   SER A 472      33.229 118.325  11.266  1.00 36.50           C  
ANISOU 3703  C   SER A 472     7424   3236   3210    -85   2260   -441       C  
ATOM   3704  O   SER A 472      34.051 117.407  11.366  1.00 36.52           O  
ANISOU 3704  O   SER A 472     7510   3199   3166    -65   2261   -350       O  
ATOM   3705  CB  SER A 472      34.077 120.483  12.186  1.00 36.67           C  
ANISOU 3705  CB  SER A 472     7360   3309   3265     36   2167   -595       C  
ATOM   3706  OG  SER A 472      35.353 120.105  12.677  1.00 36.75           O  
ANISOU 3706  OG  SER A 472     7439   3309   3213     95   2146   -534       O  
ATOM   3707  N   ARG A 473      32.435 118.489  10.212  1.00 39.93           N  
ANISOU 3707  N   ARG A 473     7819   3636   3716   -136   2275   -460       N  
ATOM   3708  CA  ARG A 473      32.589 117.700   9.001  1.00 39.31           C  
ANISOU 3708  CA  ARG A 473     7794   3474   3669   -167   2289   -377       C  
ATOM   3709  C   ARG A 473      33.861 118.115   8.269  1.00 38.61           C  
ANISOU 3709  C   ARG A 473     7731   3324   3614   -102   2248   -333       C  
ATOM   3710  O   ARG A 473      34.341 119.243   8.403  1.00 38.55           O  
ANISOU 3710  O   ARG A 473     7684   3324   3638    -50   2210   -385       O  
ATOM   3711  CB  ARG A 473      31.369 117.888   8.099  1.00 39.29           C  
ANISOU 3711  CB  ARG A 473     7738   3466   3725   -232   2313   -424       C  
ATOM   3712  CG  ARG A 473      31.258 116.926   6.929  1.00 39.39           C  
ANISOU 3712  CG  ARG A 473     7803   3407   3758   -277   2333   -357       C  
ATOM   3713  CD  ARG A 473      29.952 117.157   6.188  1.00 39.64           C  
ANISOU 3713  CD  ARG A 473     7777   3451   3835   -342   2357   -420       C  
ATOM   3714  NE  ARG A 473      28.831 117.256   7.120  1.00 40.44           N  
ANISOU 3714  NE  ARG A 473     7818   3636   3914   -387   2393   -498       N  
ATOM   3715  CZ  ARG A 473      28.111 116.220   7.537  1.00 41.19           C  
ANISOU 3715  CZ  ARG A 473     7936   3748   3966   -461   2449   -487       C  
ATOM   3716  NH1 ARG A 473      28.388 114.999   7.099  1.00 41.13           N1+
ANISOU 3716  NH1 ARG A 473     8018   3666   3943   -493   2467   -408       N1+
ATOM   3717  NH2 ARG A 473      27.113 116.404   8.392  1.00 42.14           N  
ANISOU 3717  NH2 ARG A 473     7990   3961   4061   -502   2488   -562       N  
ATOM   3718  N   ALA A 474      34.407 117.188   7.489  1.00 36.31           N  
ANISOU 3718  N   ALA A 474     7504   2970   3322   -104   2256   -246       N  
ATOM   3719  CA  ALA A 474      35.639 117.432   6.755  1.00 35.82           C  
ANISOU 3719  CA  ALA A 474     7464   2863   3282    -45   2229   -198       C  
ATOM   3720  C   ALA A 474      35.346 117.954   5.354  1.00 35.31           C  
ANISOU 3720  C   ALA A 474     7369   2764   3282    -69   2230   -202       C  
ATOM   3721  O   ALA A 474      34.467 117.442   4.655  1.00 35.26           O  
ANISOU 3721  O   ALA A 474     7363   2742   3292   -126   2252   -201       O  
ATOM   3722  CB  ALA A 474      36.476 116.154   6.667  1.00 35.91           C  
ANISOU 3722  CB  ALA A 474     7556   2832   3256    -17   2231   -114       C  
ATOM   3723  N   ILE A 475      36.087 118.985   4.956  1.00 34.15           N  
ANISOU 3723  N   ILE A 475     7202   2602   3169    -23   2207   -214       N  
ATOM   3724  CA  ILE A 475      36.099 119.484   3.588  1.00 33.77           C  
ANISOU 3724  CA  ILE A 475     7117   2521   3192    -37   2183   -187       C  
ATOM   3725  C   ILE A 475      37.536 119.440   3.090  1.00 33.60           C  
ANISOU 3725  C   ILE A 475     7103   2486   3179     11   2157   -107       C  
ATOM   3726  O   ILE A 475      38.468 119.775   3.829  1.00 33.76           O  
ANISOU 3726  O   ILE A 475     7104   2520   3203     59   2121   -103       O  
ATOM   3727  CB  ILE A 475      35.524 120.912   3.477  1.00 33.80           C  
ANISOU 3727  CB  ILE A 475     7010   2525   3308    -48   2104   -246       C  
ATOM   3728  CG1 ILE A 475      36.207 121.852   4.475  1.00 34.05           C  
ANISOU 3728  CG1 ILE A 475     6986   2568   3382      0   2036   -283       C  
ATOM   3729  CG2 ILE A 475      34.018 120.901   3.681  1.00 34.02           C  
ANISOU 3729  CG2 ILE A 475     7018   2574   3334    -95   2132   -330       C  
ATOM   3730  CD1 ILE A 475      35.829 123.309   4.308  1.00 34.19           C  
ANISOU 3730  CD1 ILE A 475     6899   2565   3528     -1   1941   -336       C  
ATOM   3731  N   TRP A 476      37.719 119.012   1.844  1.00 33.87           N  
ANISOU 3731  N   TRP A 476     7157   2502   3210     -1   2177    -49       N  
ATOM   3732  CA  TRP A 476      39.058 118.907   1.283  1.00 33.83           C  
ANISOU 3732  CA  TRP A 476     7150   2500   3204     42   2165     24       C  
ATOM   3733  C   TRP A 476      39.084 119.471  -0.128  1.00 33.69           C  
ANISOU 3733  C   TRP A 476     7079   2480   3244     17   2138     70       C  
ATOM   3734  O   TRP A 476      38.223 119.151  -0.951  1.00 33.61           O  
ANISOU 3734  O   TRP A 476     7090   2460   3219    -22   2163     65       O  
ATOM   3735  CB  TRP A 476      39.610 117.464   1.278  1.00 33.95           C  
ANISOU 3735  CB  TRP A 476     7248   2509   3142     78   2209     57       C  
ATOM   3736  CG  TRP A 476      38.669 116.284   1.490  1.00 34.07           C  
ANISOU 3736  CG  TRP A 476     7300   2500   3146     46   2211     30       C  
ATOM   3737  CD1 TRP A 476      37.417 116.284   2.041  1.00 34.15           C  
ANISOU 3737  CD1 TRP A 476     7309   2508   3159    -12   2222    -18       C  
ATOM   3738  CD2 TRP A 476      38.956 114.918   1.165  1.00 34.27           C  
ANISOU 3738  CD2 TRP A 476     7374   2497   3152     68   2211     51       C  
ATOM   3739  NE1 TRP A 476      36.907 115.011   2.064  1.00 34.40           N  
ANISOU 3739  NE1 TRP A 476     7386   2510   3176    -37   2233    -19       N  
ATOM   3740  CE2 TRP A 476      37.833 114.153   1.532  1.00 34.48           C  
ANISOU 3740  CE2 TRP A 476     7436   2494   3172     14   2226     20       C  
ATOM   3741  CE3 TRP A 476      40.054 114.270   0.591  1.00 34.41           C  
ANISOU 3741  CE3 TRP A 476     7410   2510   3153    130   2207     89       C  
ATOM   3742  CZ2 TRP A 476      37.776 112.774   1.345  1.00 34.83           C  
ANISOU 3742  CZ2 TRP A 476     7549   2490   3195     17   2238     27       C  
ATOM   3743  CZ3 TRP A 476      39.996 112.904   0.406  1.00 34.74           C  
ANISOU 3743  CZ3 TRP A 476     7519   2507   3172    143   2217     90       C  
ATOM   3744  CH2 TRP A 476      38.865 112.169   0.782  1.00 34.95           C  
ANISOU 3744  CH2 TRP A 476     7594   2490   3194     85   2232     60       C  
ATOM   3745  N   TYR A 477      40.084 120.310  -0.391  1.00 33.35           N  
ANISOU 3745  N   TYR A 477     6964   2446   3261     36   2086    117       N  
ATOM   3746  CA  TYR A 477      40.302 120.927  -1.690  1.00 33.40           C  
ANISOU 3746  CA  TYR A 477     6917   2457   3315     10   2058    180       C  
ATOM   3747  C   TYR A 477      41.801 121.006  -1.936  1.00 33.64           C  
ANISOU 3747  C   TYR A 477     6912   2519   3349     44   2054    248       C  
ATOM   3748  O   TYR A 477      42.603 120.993  -0.998  1.00 33.77           O  
ANISOU 3748  O   TYR A 477     6917   2545   3368     85   2041    235       O  
ATOM   3749  CB  TYR A 477      39.676 122.327  -1.759  1.00 33.49           C  
ANISOU 3749  CB  TYR A 477     6848   2438   3437    -28   1977    164       C  
ATOM   3750  CG  TYR A 477      40.109 123.232  -0.625  1.00 33.68           C  
ANISOU 3750  CG  TYR A 477     6814   2446   3536     -9   1912    126       C  
ATOM   3751  CD1 TYR A 477      41.312 123.925  -0.681  1.00 33.98           C  
ANISOU 3751  CD1 TYR A 477     6789   2486   3635      0   1866    180       C  
ATOM   3752  CD2 TYR A 477      39.316 123.390   0.504  1.00 33.67           C  
ANISOU 3752  CD2 TYR A 477     6817   2435   3543     -3   1898     30       C  
ATOM   3753  CE1 TYR A 477      41.713 124.746   0.352  1.00 34.25           C  
ANISOU 3753  CE1 TYR A 477     6768   2503   3742     16   1798    134       C  
ATOM   3754  CE2 TYR A 477      39.709 124.212   1.544  1.00 33.95           C  
ANISOU 3754  CE2 TYR A 477     6799   2461   3639     21   1834    -18       C  
ATOM   3755  CZ  TYR A 477      40.909 124.888   1.462  1.00 34.22           C  
ANISOU 3755  CZ  TYR A 477     6775   2488   3741     31   1780     32       C  
ATOM   3756  OH  TYR A 477      41.314 125.710   2.488  1.00 34.59           O  
ANISOU 3756  OH  TYR A 477     6767   2522   3854     53   1708    -25       O  
ATOM   3757  N   MET A 478      42.175 121.102  -3.207  1.00 34.40           N  
ANISOU 3757  N   MET A 478     6985   2642   3443     28   2064    319       N  
ATOM   3758  CA  MET A 478      43.574 121.223  -3.586  1.00 34.77           C  
ANISOU 3758  CA  MET A 478     6982   2736   3495     51   2067    387       C  
ATOM   3759  C   MET A 478      43.934 122.683  -3.829  1.00 35.12           C  
ANISOU 3759  C   MET A 478     6923   2769   3651      6   1993    439       C  
ATOM   3760  O   MET A 478      43.079 123.571  -3.846  1.00 35.08           O  
ANISOU 3760  O   MET A 478     6894   2714   3719    -37   1936    426       O  
ATOM   3761  CB  MET A 478      43.870 120.389  -4.831  1.00 34.94           C  
ANISOU 3761  CB  MET A 478     7036   2808   3431     63   2132    433       C  
ATOM   3762  CG  MET A 478      42.896 119.259  -5.052  1.00 34.66           C  
ANISOU 3762  CG  MET A 478     7089   2758   3321     72   2173    376       C  
ATOM   3763  SD  MET A 478      43.476 118.158  -6.342  1.00 35.02           S  
ANISOU 3763  SD  MET A 478     7124   2878   3304    115   2194    383       S  
ATOM   3764  CE  MET A 478      44.799 117.314  -5.481  1.00 35.26           C  
ANISOU 3764  CE  MET A 478     7176   2922   3298    202   2225    373       C  
ATOM   3765  N   TRP A 479      45.229 122.920  -4.025  1.00 36.71           N  
ANISOU 3765  N   TRP A 479     7061   3015   3872     15   1992    497       N  
ATOM   3766  CA  TRP A 479      45.722 124.270  -4.240  1.00 37.22           C  
ANISOU 3766  CA  TRP A 479     7026   3065   4050    -38   1923    557       C  
ATOM   3767  C   TRP A 479      45.193 124.824  -5.562  1.00 37.46           C  
ANISOU 3767  C   TRP A 479     7046   3092   4094   -100   1915    636       C  
ATOM   3768  O   TRP A 479      44.787 124.081  -6.460  1.00 37.33           O  
ANISOU 3768  O   TRP A 479     7084   3115   3985    -95   1973    653       O  
ATOM   3769  CB  TRP A 479      47.253 124.284  -4.183  1.00 37.78           C  
ANISOU 3769  CB  TRP A 479     7025   3198   4131    -20   1935    601       C  
ATOM   3770  CG  TRP A 479      47.960 124.711  -5.426  1.00 38.45           C  
ANISOU 3770  CG  TRP A 479     7044   3341   4226    -69   1955    712       C  
ATOM   3771  CD1 TRP A 479      48.305 123.923  -6.483  1.00 38.66           C  
ANISOU 3771  CD1 TRP A 479     7088   3452   4150    -53   2036    759       C  
ATOM   3772  CD2 TRP A 479      48.450 126.024  -5.726  1.00 39.17           C  
ANISOU 3772  CD2 TRP A 479     7038   3413   4433   -145   1894    791       C  
ATOM   3773  NE1 TRP A 479      48.964 124.666  -7.432  1.00 39.47           N  
ANISOU 3773  NE1 TRP A 479     7108   3604   4285   -116   2037    866       N  
ATOM   3774  CE2 TRP A 479      49.066 125.959  -6.991  1.00 39.81           C  
ANISOU 3774  CE2 TRP A 479     7082   3579   4465   -178   1950    895       C  
ATOM   3775  CE3 TRP A 479      48.419 127.249  -5.053  1.00 39.45           C  
ANISOU 3775  CE3 TRP A 479     7016   3365   4609   -189   1795    782       C  
ATOM   3776  CZ2 TRP A 479      49.644 127.072  -7.598  1.00 40.73           C  
ANISOU 3776  CZ2 TRP A 479     7108   3701   4667   -264   1917   1004       C  
ATOM   3777  CZ3 TRP A 479      48.995 128.353  -5.657  1.00 40.35           C  
ANISOU 3777  CZ3 TRP A 479     7044   3468   4821   -272   1753    884       C  
ATOM   3778  CH2 TRP A 479      49.599 128.257  -6.916  1.00 40.99           C  
ANISOU 3778  CH2 TRP A 479     7092   3636   4848   -313   1816   1001       C  
ATOM   3779  N   LEU A 480      45.188 126.157  -5.659  1.00 37.30           N  
ANISOU 3779  N   LEU A 480     6958   3020   4193   -157   1834    681       N  
ATOM   3780  CA  LEU A 480      44.452 126.836  -6.724  1.00 37.58           C  
ANISOU 3780  CA  LEU A 480     6994   3029   4256   -214   1800    750       C  
ATOM   3781  C   LEU A 480      44.934 126.408  -8.106  1.00 38.00           C  
ANISOU 3781  C   LEU A 480     7051   3172   4216   -232   1868    851       C  
ATOM   3782  O   LEU A 480      44.122 126.184  -9.013  1.00 37.96           O  
ANISOU 3782  O   LEU A 480     7093   3179   4151   -243   1883    872       O  
ATOM   3783  CB  LEU A 480      44.573 128.350  -6.553  1.00 38.21           C  
ANISOU 3783  CB  LEU A 480     7001   3027   4490   -270   1695    793       C  
ATOM   3784  CG  LEU A 480      43.667 129.219  -7.426  1.00 38.60           C  
ANISOU 3784  CG  LEU A 480     7056   3017   4593   -320   1630    853       C  
ATOM   3785  CD1 LEU A 480      42.209 128.900  -7.149  1.00 37.95           C  
ANISOU 3785  CD1 LEU A 480     7036   2896   4488   -286   1615    751       C  
ATOM   3786  CD2 LEU A 480      43.950 130.696  -7.195  1.00 39.39           C  
ANISOU 3786  CD2 LEU A 480     7087   3022   4859   -374   1520    899       C  
ATOM   3787  N   GLY A 481      46.251 126.291  -8.287  1.00 37.10           N  
ANISOU 3787  N   GLY A 481     6880   3130   4085   -233   1910    909       N  
ATOM   3788  CA  GLY A 481      46.776 125.836  -9.563  1.00 37.62           C  
ANISOU 3788  CA  GLY A 481     6941   3304   4050   -243   1985    994       C  
ATOM   3789  C   GLY A 481      46.348 124.425  -9.917  1.00 37.12           C  
ANISOU 3789  C   GLY A 481     6964   3295   3844   -179   2066    931       C  
ATOM   3790  O   GLY A 481      46.118 124.118 -11.089  1.00 37.43           O  
ANISOU 3790  O   GLY A 481     7021   3401   3799   -187   2098    972       O  
ATOM   3791  N   ALA A 482      46.235 123.548  -8.916  1.00 37.14           N  
ANISOU 3791  N   ALA A 482     7016   3273   3821   -112   2086    825       N  
ATOM   3792  CA  ALA A 482      45.740 122.200  -9.174  1.00 36.65           C  
ANISOU 3792  CA  ALA A 482     7044   3239   3641    -57   2151    759       C  
ATOM   3793  C   ALA A 482      44.237 122.194  -9.408  1.00 36.41           C  
ANISOU 3793  C   ALA A 482     7067   3157   3612    -78   2111    710       C  
ATOM   3794  O   ALA A 482      43.732 121.355 -10.163  1.00 36.56           O  
ANISOU 3794  O   ALA A 482     7114   3220   3558    -56   2125    669       O  
ATOM   3795  CB  ALA A 482      46.097 121.272  -8.013  1.00 36.32           C  
ANISOU 3795  CB  ALA A 482     7044   3180   3576     16   2179    673       C  
ATOM   3796  N   ARG A 483      43.508 123.112  -8.769  1.00 36.48           N  
ANISOU 3796  N   ARG A 483     7075   3074   3714   -117   2050    701       N  
ATOM   3797  CA  ARG A 483      42.072 123.205  -8.992  1.00 36.19           C  
ANISOU 3797  CA  ARG A 483     7082   2987   3681   -139   2017    660       C  
ATOM   3798  C   ARG A 483      41.741 123.741 -10.379  1.00 36.73           C  
ANISOU 3798  C   ARG A 483     7139   3086   3732   -182   1995    746       C  
ATOM   3799  O   ARG A 483      40.620 123.533 -10.859  1.00 36.61           O  
ANISOU 3799  O   ARG A 483     7168   3059   3685   -190   1983    713       O  
ATOM   3800  CB  ARG A 483      41.427 124.076  -7.910  1.00 35.92           C  
ANISOU 3800  CB  ARG A 483     7022   2864   3763   -153   1939    605       C  
ATOM   3801  CG  ARG A 483      40.370 123.344  -7.097  1.00 35.32           C  
ANISOU 3801  CG  ARG A 483     7008   2754   3660   -130   1957    488       C  
ATOM   3802  CD  ARG A 483      40.335 123.792  -5.640  1.00 35.11           C  
ANISOU 3802  CD  ARG A 483     6955   2676   3709   -115   1917    418       C  
ATOM   3803  NE  ARG A 483      39.747 125.117  -5.460  1.00 35.34           N  
ANISOU 3803  NE  ARG A 483     6926   2643   3857   -145   1821    409       N  
ATOM   3804  CZ  ARG A 483      40.411 126.176  -5.006  1.00 35.69           C  
ANISOU 3804  CZ  ARG A 483     6904   2652   4005   -154   1753    434       C  
ATOM   3805  NH1 ARG A 483      39.793 127.340  -4.871  1.00 36.00           N1+
ANISOU 3805  NH1 ARG A 483     6898   2621   4157   -175   1659    417       N1+
ATOM   3806  NH2 ARG A 483      41.692 126.068  -4.680  1.00 35.83           N  
ANISOU 3806  NH2 ARG A 483     6896   2700   4019   -140   1773    469       N  
ATOM   3807  N   PHE A 484      42.688 124.416 -11.035  1.00 35.73           N  
ANISOU 3807  N   PHE A 484     6947   3007   3623   -212   1985    855       N  
ATOM   3808  CA  PHE A 484      42.468 124.849 -12.411  1.00 36.42           C  
ANISOU 3808  CA  PHE A 484     7013   3149   3677   -249   1957    941       C  
ATOM   3809  C   PHE A 484      42.647 123.693 -13.388  1.00 36.60           C  
ANISOU 3809  C   PHE A 484     7044   3295   3568   -209   2012    915       C  
ATOM   3810  O   PHE A 484      41.849 123.530 -14.317  1.00 36.81           O  
ANISOU 3810  O   PHE A 484     7102   3350   3534   -216   1998    917       O  
ATOM   3811  CB  PHE A 484      43.407 126.000 -12.770  1.00 37.30           C  
ANISOU 3811  CB  PHE A 484     7047   3270   3855   -308   1927   1075       C  
ATOM   3812  CG  PHE A 484      43.418 126.327 -14.236  1.00 38.21           C  
ANISOU 3812  CG  PHE A 484     7136   3471   3912   -344   1911   1180       C  
ATOM   3813  CD1 PHE A 484      42.322 126.921 -14.837  1.00 38.45           C  
ANISOU 3813  CD1 PHE A 484     7204   3451   3956   -373   1845   1216       C  
ATOM   3814  CD2 PHE A 484      44.520 126.033 -15.016  1.00 38.95           C  
ANISOU 3814  CD2 PHE A 484     7169   3699   3930   -348   1964   1244       C  
ATOM   3815  CE1 PHE A 484      42.329 127.216 -16.186  1.00 39.41           C  
ANISOU 3815  CE1 PHE A 484     7309   3655   4009   -405   1829   1321       C  
ATOM   3816  CE2 PHE A 484      44.535 126.328 -16.365  1.00 39.92           C  
ANISOU 3816  CE2 PHE A 484     7269   3914   3985   -384   1954   1344       C  
ATOM   3817  CZ  PHE A 484      43.437 126.920 -16.951  1.00 40.15           C  
ANISOU 3817  CZ  PHE A 484     7342   3892   4022   -413   1884   1386       C  
ATOM   3818  N   LEU A 485      43.703 122.892 -13.203  1.00 36.62           N  
ANISOU 3818  N   LEU A 485     7022   3367   3524   -164   2072    888       N  
ATOM   3819  CA  LEU A 485      43.856 121.670 -13.989  1.00 36.80           C  
ANISOU 3819  CA  LEU A 485     7061   3488   3434   -112   2119    838       C  
ATOM   3820  C   LEU A 485      42.611 120.803 -13.885  1.00 36.20           C  
ANISOU 3820  C   LEU A 485     7069   3360   3324    -86   2114    729       C  
ATOM   3821  O   LEU A 485      42.154 120.229 -14.881  1.00 36.50           O  
ANISOU 3821  O   LEU A 485     7134   3452   3283    -76   2121    708       O  
ATOM   3822  CB  LEU A 485      45.088 120.891 -13.521  1.00 36.86           C  
ANISOU 3822  CB  LEU A 485     7044   3545   3417    -54   2178    807       C  
ATOM   3823  CG  LEU A 485      46.445 121.166 -14.177  1.00 37.82           C  
ANISOU 3823  CG  LEU A 485     7078   3784   3507    -61   2217    896       C  
ATOM   3824  CD1 LEU A 485      46.365 122.300 -15.188  1.00 38.60           C  
ANISOU 3824  CD1 LEU A 485     7126   3928   3613   -142   2184   1021       C  
ATOM   3825  CD2 LEU A 485      47.512 121.444 -13.125  1.00 37.79           C  
ANISOU 3825  CD2 LEU A 485     7036   3757   3564    -52   2244    915       C  
ATOM   3826  N   GLU A 486      42.049 120.702 -12.679  1.00 37.59           N  
ANISOU 3826  N   GLU A 486     7288   3435   3557    -80   2106    658       N  
ATOM   3827  CA  GLU A 486      40.747 120.067 -12.507  1.00 37.27           C  
ANISOU 3827  CA  GLU A 486     7323   3338   3500    -77   2102    566       C  
ATOM   3828  C   GLU A 486      39.691 120.735 -13.378  1.00 37.55           C  
ANISOU 3828  C   GLU A 486     7374   3366   3525   -126   2064    604       C  
ATOM   3829  O   GLU A 486      38.857 120.057 -13.989  1.00 37.58           O  
ANISOU 3829  O   GLU A 486     7429   3384   3467   -122   2072    552       O  
ATOM   3830  CB  GLU A 486      40.334 120.133 -11.038  1.00 36.79           C  
ANISOU 3830  CB  GLU A 486     7292   3181   3505    -78   2099    506       C  
ATOM   3831  CG  GLU A 486      40.397 118.825 -10.282  1.00 36.57           C  
ANISOU 3831  CG  GLU A 486     7312   3133   3449    -29   2135    412       C  
ATOM   3832  CD  GLU A 486      39.869 118.966  -8.867  1.00 36.17           C  
ANISOU 3832  CD  GLU A 486     7292   3000   3449    -39   2134    360       C  
ATOM   3833  OE1 GLU A 486      40.132 120.015  -8.238  1.00 35.85           O  
ANISOU 3833  OE1 GLU A 486     7223   2931   3470    -59   2115    402       O  
ATOM   3834  OE2 GLU A 486      39.178 118.042  -8.388  1.00 36.14           O1+
ANISOU 3834  OE2 GLU A 486     7344   2960   3426    -32   2151    280       O1+
ATOM   3835  N   PHE A 487      39.724 122.067 -13.458  1.00 36.21           N  
ANISOU 3835  N   PHE A 487     7168   3170   3421   -171   2017    699       N  
ATOM   3836  CA  PHE A 487      38.655 122.803 -14.125  1.00 36.51           C  
ANISOU 3836  CA  PHE A 487     7234   3174   3466   -213   1968    741       C  
ATOM   3837  C   PHE A 487      38.742 122.678 -15.642  1.00 37.31           C  
ANISOU 3837  C   PHE A 487     7330   3378   3468   -216   1967    803       C  
ATOM   3838  O   PHE A 487      37.720 122.493 -16.313  1.00 37.48           O  
ANISOU 3838  O   PHE A 487     7408   3401   3433   -224   1955    783       O  
ATOM   3839  CB  PHE A 487      38.692 124.273 -13.702  1.00 36.71           C  
ANISOU 3839  CB  PHE A 487     7214   3117   3615   -253   1894    818       C  
ATOM   3840  CG  PHE A 487      37.661 125.126 -14.384  1.00 37.17           C  
ANISOU 3840  CG  PHE A 487     7268   3144   3712   -281   1802    852       C  
ATOM   3841  CD1 PHE A 487      36.329 125.053 -14.014  1.00 36.82           C  
ANISOU 3841  CD1 PHE A 487     7240   3045   3706   -271   1756    748       C  
ATOM   3842  CD2 PHE A 487      38.024 126.003 -15.391  1.00 38.10           C  
ANISOU 3842  CD2 PHE A 487     7362   3288   3825   -316   1759    991       C  
ATOM   3843  CE1 PHE A 487      35.377 125.836 -14.640  1.00 37.64           C  
ANISOU 3843  CE1 PHE A 487     7333   3120   3847   -285   1661    773       C  
ATOM   3844  CE2 PHE A 487      37.077 126.790 -16.020  1.00 38.64           C  
ANISOU 3844  CE2 PHE A 487     7433   3321   3928   -333   1663   1029       C  
ATOM   3845  CZ  PHE A 487      35.752 126.705 -15.645  1.00 38.51           C  
ANISOU 3845  CZ  PHE A 487     7429   3249   3953   -312   1610    915       C  
ATOM   3846  N   GLU A 488      39.945 122.782 -16.207  1.00 37.19           N  
ANISOU 3846  N   GLU A 488     7250   3457   3423   -213   1983    879       N  
ATOM   3847  CA  GLU A 488      40.080 122.719 -17.657  1.00 38.11           C  
ANISOU 3847  CA  GLU A 488     7356   3688   3435   -218   1984    944       C  
ATOM   3848  C   GLU A 488      39.908 121.312 -18.216  1.00 38.11           C  
ANISOU 3848  C   GLU A 488     7397   3762   3321   -166   2033    844       C  
ATOM   3849  O   GLU A 488      39.761 121.166 -19.434  1.00 38.88           O  
ANISOU 3849  O   GLU A 488     7503   3952   3318   -166   2033    876       O  
ATOM   3850  CB  GLU A 488      41.434 123.285 -18.094  1.00 38.91           C  
ANISOU 3850  CB  GLU A 488     7369   3880   3537   -240   1995   1060       C  
ATOM   3851  CG  GLU A 488      42.574 122.283 -18.114  1.00 39.01           C  
ANISOU 3851  CG  GLU A 488     7341   3991   3489   -189   2067   1014       C  
ATOM   3852  CD  GLU A 488      43.807 122.840 -18.798  1.00 40.08           C  
ANISOU 3852  CD  GLU A 488     7386   4242   3599   -221   2087   1136       C  
ATOM   3853  OE1 GLU A 488      43.765 124.012 -19.223  1.00 40.73           O  
ANISOU 3853  OE1 GLU A 488     7440   4319   3718   -289   2040   1262       O  
ATOM   3854  OE2 GLU A 488      44.815 122.110 -18.915  1.00 40.37           O1+
ANISOU 3854  OE2 GLU A 488     7383   4375   3581   -180   2150   1108       O1+
ATOM   3855  N   ALA A 489      39.904 120.285 -17.367  1.00 37.39           N  
ANISOU 3855  N   ALA A 489     7334   3627   3244   -124   2070    726       N  
ATOM   3856  CA  ALA A 489      39.694 118.916 -17.817  1.00 37.46           C  
ANISOU 3856  CA  ALA A 489     7389   3676   3167    -77   2106    625       C  
ATOM   3857  C   ALA A 489      38.268 118.427 -17.619  1.00 37.03           C  
ANISOU 3857  C   ALA A 489     7419   3542   3107    -89   2096    532       C  
ATOM   3858  O   ALA A 489      37.794 117.607 -18.411  1.00 37.41           O  
ANISOU 3858  O   ALA A 489     7511   3630   3071    -73   2107    474       O  
ATOM   3859  CB  ALA A 489      40.648 117.961 -17.090  1.00 37.17           C  
ANISOU 3859  CB  ALA A 489     7339   3636   3146    -22   2149    562       C  
ATOM   3860  N   LEU A 490      37.572 118.907 -16.584  1.00 36.35           N  
ANISOU 3860  N   LEU A 490     7354   3350   3107   -119   2078    512       N  
ATOM   3861  CA  LEU A 490      36.241 118.417 -16.256  1.00 35.99           C  
ANISOU 3861  CA  LEU A 490     7381   3234   3060   -139   2082    419       C  
ATOM   3862  C   LEU A 490      35.227 119.522 -15.995  1.00 35.87           C  
ANISOU 3862  C   LEU A 490     7374   3152   3101   -188   2037    450       C  
ATOM   3863  O   LEU A 490      34.045 119.217 -15.803  1.00 35.71           O  
ANISOU 3863  O   LEU A 490     7370   3094   3104   -204   2012    358       O  
ATOM   3864  CB  LEU A 490      36.301 117.497 -15.027  1.00 35.34           C  
ANISOU 3864  CB  LEU A 490     7318   3082   3027   -119   2114    323       C  
ATOM   3865  CG  LEU A 490      37.239 116.291 -15.131  1.00 35.50           C  
ANISOU 3865  CG  LEU A 490     7339   3137   3014    -63   2144    283       C  
ATOM   3866  CD1 LEU A 490      37.488 115.688 -13.763  1.00 34.93           C  
ANISOU 3866  CD1 LEU A 490     7282   2986   3005    -44   2163    229       C  
ATOM   3867  CD2 LEU A 490      36.670 115.252 -16.082  1.00 36.00           C  
ANISOU 3867  CD2 LEU A 490     7456   3228   2996    -55   2155    216       C  
ATOM   3868  N   GLY A 491      35.647 120.788 -15.981  1.00 36.04           N  
ANISOU 3868  N   GLY A 491     7337   3166   3191   -204   1984    553       N  
ATOM   3869  CA  GLY A 491      34.733 121.882 -15.699  1.00 36.04           C  
ANISOU 3869  CA  GLY A 491     7294   3100   3298   -231   1887    557       C  
ATOM   3870  C   GLY A 491      33.600 122.021 -16.693  1.00 36.59           C  
ANISOU 3870  C   GLY A 491     7374   3195   3334   -240   1823    542       C  
ATOM   3871  O   GLY A 491      32.589 122.657 -16.378  1.00 36.58           O  
ANISOU 3871  O   GLY A 491     7341   3137   3420   -251   1744    503       O  
ATOM   3872  N   PHE A 492      33.739 121.431 -17.885  1.00 37.17           N  
ANISOU 3872  N   PHE A 492     7485   3359   3279   -230   1850    564       N  
ATOM   3873  CA  PHE A 492      32.666 121.490 -18.872  1.00 37.80           C  
ANISOU 3873  CA  PHE A 492     7576   3474   3312   -234   1784    542       C  
ATOM   3874  C   PHE A 492      31.368 120.908 -18.326  1.00 37.41           C  
ANISOU 3874  C   PHE A 492     7533   3375   3308   -241   1767    394       C  
ATOM   3875  O   PHE A 492      30.282 121.283 -18.782  1.00 37.85           O  
ANISOU 3875  O   PHE A 492     7570   3431   3381   -247   1685    364       O  
ATOM   3876  CB  PHE A 492      33.079 120.753 -20.150  1.00 38.50           C  
ANISOU 3876  CB  PHE A 492     7711   3679   3240   -215   1829    565       C  
ATOM   3877  CG  PHE A 492      33.103 119.254 -20.008  1.00 38.20           C  
ANISOU 3877  CG  PHE A 492     7727   3657   3131   -194   1915    443       C  
ATOM   3878  CD1 PHE A 492      31.980 118.497 -20.306  1.00 38.36           C  
ANISOU 3878  CD1 PHE A 492     7777   3677   3121   -198   1895    323       C  
ATOM   3879  CD2 PHE A 492      34.249 118.603 -19.583  1.00 37.88           C  
ANISOU 3879  CD2 PHE A 492     7705   3627   3061   -170   2008    446       C  
ATOM   3880  CE1 PHE A 492      31.996 117.124 -20.175  1.00 38.22           C  
ANISOU 3880  CE1 PHE A 492     7815   3656   3051   -185   1967    213       C  
ATOM   3881  CE2 PHE A 492      34.272 117.226 -19.453  1.00 37.74           C  
ANISOU 3881  CE2 PHE A 492     7737   3608   2994   -145   2070    334       C  
ATOM   3882  CZ  PHE A 492      33.143 116.486 -19.749  1.00 37.92           C  
ANISOU 3882  CZ  PHE A 492     7805   3618   2985   -157   2056    222       C  
ATOM   3883  N   LEU A 493      31.460 119.990 -17.360  1.00 36.72           N  
ANISOU 3883  N   LEU A 493     7468   3248   3236   -242   1844    302       N  
ATOM   3884  CA  LEU A 493      30.261 119.389 -16.783  1.00 36.47           C  
ANISOU 3884  CA  LEU A 493     7439   3173   3245   -263   1842    167       C  
ATOM   3885  C   LEU A 493      29.403 120.425 -16.069  1.00 36.33           C  
ANISOU 3885  C   LEU A 493     7353   3096   3356   -278   1763    144       C  
ATOM   3886  O   LEU A 493      28.172 120.313 -16.059  1.00 36.54           O  
ANISOU 3886  O   LEU A 493     7355   3115   3412   -295   1723     51       O  
ATOM   3887  CB  LEU A 493      30.653 118.267 -15.821  1.00 35.87           C  
ANISOU 3887  CB  LEU A 493     7409   3060   3161   -266   1940     99       C  
ATOM   3888  CG  LEU A 493      31.333 117.055 -16.459  1.00 36.11           C  
ANISOU 3888  CG  LEU A 493     7512   3135   3073   -243   2015     86       C  
ATOM   3889  CD1 LEU A 493      32.099 116.252 -15.421  1.00 35.57           C  
ANISOU 3889  CD1 LEU A 493     7486   3019   3012   -229   2100     64       C  
ATOM   3890  CD2 LEU A 493      30.308 116.181 -17.162  1.00 36.62           C  
ANISOU 3890  CD2 LEU A 493     7610   3219   3084   -261   2005    -16       C  
ATOM   3891  N   ASN A 494      30.028 121.435 -15.466  1.00 36.09           N  
ANISOU 3891  N   ASN A 494     7284   3024   3405   -269   1737    219       N  
ATOM   3892  CA  ASN A 494      29.299 122.465 -14.737  1.00 36.06           C  
ANISOU 3892  CA  ASN A 494     7213   2958   3528   -272   1658    189       C  
ATOM   3893  C   ASN A 494      28.923 123.648 -15.622  1.00 36.83           C  
ANISOU 3893  C   ASN A 494     7275   3056   3662   -261   1539    265       C  
ATOM   3894  O   ASN A 494      27.801 124.157 -15.531  1.00 38.86           O  
ANISOU 3894  O   ASN A 494     7486   3288   3992   -255   1458    201       O  
ATOM   3895  CB  ASN A 494      30.129 122.956 -13.546  1.00 35.51           C  
ANISOU 3895  CB  ASN A 494     7122   2834   3537   -266   1681    215       C  
ATOM   3896  CG  ASN A 494      30.474 121.843 -12.574  1.00 34.86           C  
ANISOU 3896  CG  ASN A 494     7078   2746   3420   -271   1788    147       C  
ATOM   3897  OD1 ASN A 494      29.615 121.051 -12.185  1.00 34.74           O  
ANISOU 3897  OD1 ASN A 494     7076   2730   3393   -290   1824     41       O  
ATOM   3898  ND2 ASN A 494      31.740 121.775 -12.179  1.00 34.54           N  
ANISOU 3898  ND2 ASN A 494     7056   2703   3366   -257   1837    210       N  
ATOM   3899  N   GLU A 495      29.840 124.093 -16.482  1.00 37.25           N  
ANISOU 3899  N   GLU A 495     7347   3139   3665   -256   1526    403       N  
ATOM   3900  CA  GLU A 495      29.613 125.278 -17.301  1.00 38.16           C  
ANISOU 3900  CA  GLU A 495     7439   3244   3814   -250   1411    502       C  
ATOM   3901  C   GLU A 495      28.730 125.008 -18.512  1.00 39.70           C  
ANISOU 3901  C   GLU A 495     7655   3506   3924   -241   1360    487       C  
ATOM   3902  O   GLU A 495      28.230 125.965 -19.116  1.00 42.11           O  
ANISOU 3902  O   GLU A 495     7939   3795   4265   -229   1246    547       O  
ATOM   3903  CB  GLU A 495      30.951 125.863 -17.762  1.00 38.45           C  
ANISOU 3903  CB  GLU A 495     7489   3296   3825   -261   1424    668       C  
ATOM   3904  CG  GLU A 495      32.073 125.741 -16.739  1.00 37.73           C  
ANISOU 3904  CG  GLU A 495     7388   3175   3774   -270   1503    678       C  
ATOM   3905  CD  GLU A 495      31.753 126.419 -15.422  1.00 37.29           C  
ANISOU 3905  CD  GLU A 495     7282   3017   3869   -265   1458    612       C  
ATOM   3906  OE1 GLU A 495      31.364 127.606 -15.440  1.00 37.82           O  
ANISOU 3906  OE1 GLU A 495     7312   3017   4042   -263   1347    651       O  
ATOM   3907  OE2 GLU A 495      31.889 125.761 -14.367  1.00 36.50           O1+
ANISOU 3907  OE2 GLU A 495     7183   2904   3782   -261   1529    520       O1+
ATOM   3908  N   ASP A 496      28.531 123.744 -18.886  1.00 38.73           N  
ANISOU 3908  N   ASP A 496     7572   3452   3690   -244   1433    408       N  
ATOM   3909  CA  ASP A 496      27.612 123.385 -19.957  1.00 39.47           C  
ANISOU 3909  CA  ASP A 496     7681   3611   3704   -236   1381    365       C  
ATOM   3910  C   ASP A 496      26.343 122.719 -19.444  1.00 39.24           C  
ANISOU 3910  C   ASP A 496     7626   3566   3718   -246   1378    193       C  
ATOM   3911  O   ASP A 496      25.523 122.272 -20.254  1.00 39.85           O  
ANISOU 3911  O   ASP A 496     7710   3699   3733   -243   1340    132       O  
ATOM   3912  CB  ASP A 496      28.311 122.478 -20.976  1.00 39.80           C  
ANISOU 3912  CB  ASP A 496     7788   3754   3580   -233   1454    401       C  
ATOM   3913  CG  ASP A 496      29.500 123.153 -21.629  1.00 40.28           C  
ANISOU 3913  CG  ASP A 496     7865   3856   3584   -230   1459    575       C  
ATOM   3914  OD1 ASP A 496      29.624 124.389 -21.490  1.00 40.55           O  
ANISOU 3914  OD1 ASP A 496     7865   3834   3707   -235   1384    678       O  
ATOM   3915  OD2 ASP A 496      30.306 122.455 -22.280  1.00 40.50           O1+
ANISOU 3915  OD2 ASP A 496     7936   3972   3482   -223   1537    608       O1+
ATOM   3916  N   HIS A 497      26.169 122.634 -18.122  1.00 38.48           N  
ANISOU 3916  N   HIS A 497     7496   3403   3721   -260   1419    114       N  
ATOM   3917  CA  HIS A 497      24.904 122.238 -17.499  1.00 38.41           C  
ANISOU 3917  CA  HIS A 497     7441   3377   3774   -278   1410    -40       C  
ATOM   3918  C   HIS A 497      24.485 120.826 -17.908  1.00 38.51           C  
ANISOU 3918  C   HIS A 497     7497   3442   3694   -306   1475   -138       C  
ATOM   3919  O   HIS A 497      23.363 120.592 -18.362  1.00 39.10           O  
ANISOU 3919  O   HIS A 497     7542   3548   3767   -316   1422   -229       O  
ATOM   3920  CB  HIS A 497      23.806 123.256 -17.815  1.00 39.16           C  
ANISOU 3920  CB  HIS A 497     7466   3464   3949   -253   1273    -63       C  
ATOM   3921  CG  HIS A 497      24.196 124.668 -17.511  1.00 39.26           C  
ANISOU 3921  CG  HIS A 497     7446   3411   4062   -222   1194     34       C  
ATOM   3922  ND1 HIS A 497      24.311 125.147 -16.224  1.00 38.71           N  
ANISOU 3922  ND1 HIS A 497     7332   3271   4106   -221   1209     -2       N  
ATOM   3923  CD2 HIS A 497      24.510 125.702 -18.327  1.00 39.97           C  
ANISOU 3923  CD2 HIS A 497     7542   3489   4155   -194   1096    167       C  
ATOM   3924  CE1 HIS A 497      24.675 126.417 -16.260  1.00 39.07           C  
ANISOU 3924  CE1 HIS A 497     7357   3257   4229   -192   1119     95       C  
ATOM   3925  NE2 HIS A 497      24.802 126.778 -17.524  1.00 39.84           N  
ANISOU 3925  NE2 HIS A 497     7487   3384   4266   -180   1050    205       N  
ATOM   3926  N   TRP A 498      25.401 119.873 -17.721  1.00 38.02           N  
ANISOU 3926  N   TRP A 498     7502   3382   3560   -319   1585   -126       N  
ATOM   3927  CA  TRP A 498      25.107 118.481 -18.046  1.00 38.18           C  
ANISOU 3927  CA  TRP A 498     7573   3431   3502   -345   1647   -220       C  
ATOM   3928  C   TRP A 498      24.057 117.891 -17.113  1.00 38.03           C  
ANISOU 3928  C   TRP A 498     7521   3375   3555   -396   1677   -357       C  
ATOM   3929  O   TRP A 498      23.261 117.044 -17.534  1.00 38.54           O  
ANISOU 3929  O   TRP A 498     7593   3462   3588   -428   1679   -456       O  
ATOM   3930  CB  TRP A 498      26.386 117.646 -17.987  1.00 37.77           C  
ANISOU 3930  CB  TRP A 498     7601   3380   3369   -335   1751   -175       C  
ATOM   3931  CG  TRP A 498      27.236 117.741 -19.217  1.00 38.26           C  
ANISOU 3931  CG  TRP A 498     7703   3516   3318   -296   1742    -79       C  
ATOM   3932  CD1 TRP A 498      27.780 118.871 -19.754  1.00 38.52           C  
ANISOU 3932  CD1 TRP A 498     7713   3580   3343   -269   1686     52       C  
ATOM   3933  CD2 TRP A 498      27.653 116.658 -20.057  1.00 38.68           C  
ANISOU 3933  CD2 TRP A 498     7825   3625   3247   -282   1792   -107       C  
ATOM   3934  NE1 TRP A 498      28.502 118.560 -20.880  1.00 39.09           N  
ANISOU 3934  NE1 TRP A 498     7832   3738   3284   -243   1707    112       N  
ATOM   3935  CE2 TRP A 498      28.440 117.208 -21.087  1.00 39.19           C  
ANISOU 3935  CE2 TRP A 498     7899   3770   3221   -245   1770      9       C  
ATOM   3936  CE3 TRP A 498      27.434 115.278 -20.040  1.00 38.79           C  
ANISOU 3936  CE3 TRP A 498     7894   3626   3219   -298   1852   -221       C  
ATOM   3937  CZ2 TRP A 498      29.009 116.426 -22.090  1.00 39.80           C  
ANISOU 3937  CZ2 TRP A 498     8032   3930   3159   -215   1810      5       C  
ATOM   3938  CZ3 TRP A 498      27.998 114.504 -21.036  1.00 39.38           C  
ANISOU 3938  CZ3 TRP A 498     8030   3765   3167   -266   1882   -230       C  
ATOM   3939  CH2 TRP A 498      28.776 115.079 -22.047  1.00 39.87           C  
ANISOU 3939  CH2 TRP A 498     8093   3923   3132   -221   1863   -122       C  
ATOM   3940  N   MET A 499      24.037 118.321 -15.854  1.00 37.47           N  
ANISOU 3940  N   MET A 499     7409   3250   3577   -406   1701   -367       N  
ATOM   3941  CA  MET A 499      23.147 117.752 -14.852  1.00 37.39           C  
ANISOU 3941  CA  MET A 499     7367   3215   3626   -461   1749   -485       C  
ATOM   3942  C   MET A 499      21.834 118.510 -14.719  1.00 37.89           C  
ANISOU 3942  C   MET A 499     7323   3295   3780   -467   1664   -565       C  
ATOM   3943  O   MET A 499      21.005 118.138 -13.882  1.00 37.98           O  
ANISOU 3943  O   MET A 499     7288   3300   3842   -516   1703   -668       O  
ATOM   3944  CB  MET A 499      23.858 117.691 -13.497  1.00 36.63           C  
ANISOU 3944  CB  MET A 499     7289   3065   3563   -467   1831   -461       C  
ATOM   3945  CG  MET A 499      25.115 116.842 -13.528  1.00 36.22           C  
ANISOU 3945  CG  MET A 499     7338   2996   3429   -455   1916   -397       C  
ATOM   3946  SD  MET A 499      24.831 115.242 -14.313  1.00 36.75           S  
ANISOU 3946  SD  MET A 499     7485   3073   3405   -493   1966   -470       S  
ATOM   3947  CE  MET A 499      26.501 114.799 -14.780  1.00 36.46           C  
ANISOU 3947  CE  MET A 499     7543   3038   3271   -435   2018   -368       C  
ATOM   3948  N   GLY A 500      21.624 119.551 -15.521  1.00 38.34           N  
ANISOU 3948  N   GLY A 500     7338   3375   3855   -419   1549   -519       N  
ATOM   3949  CA  GLY A 500      20.336 120.215 -15.540  1.00 39.00           C  
ANISOU 3949  CA  GLY A 500     7319   3478   4022   -412   1455   -604       C  
ATOM   3950  C   GLY A 500      19.221 119.279 -15.963  1.00 39.67           C  
ANISOU 3950  C   GLY A 500     7380   3610   4083   -463   1458   -730       C  
ATOM   3951  O   GLY A 500      19.441 118.235 -16.582  1.00 39.79           O  
ANISOU 3951  O   GLY A 500     7466   3643   4008   -492   1504   -739       O  
ATOM   3952  N   ARG A 501      17.993 119.668 -15.618  1.00 40.23           N  
ANISOU 3952  N   ARG A 501     7341   3702   4242   -472   1404   -838       N  
ATOM   3953  CA  ARG A 501      16.859 118.781 -15.852  1.00 40.95           C  
ANISOU 3953  CA  ARG A 501     7390   3840   4330   -534   1413   -973       C  
ATOM   3954  C   ARG A 501      16.567 118.608 -17.338  1.00 41.74           C  
ANISOU 3954  C   ARG A 501     7510   3991   4358   -512   1323   -973       C  
ATOM   3955  O   ARG A 501      16.072 117.553 -17.750  1.00 42.23           O  
ANISOU 3955  O   ARG A 501     7586   4081   4378   -569   1350  -1059       O  
ATOM   3956  CB  ARG A 501      15.623 119.301 -15.120  1.00 41.49           C  
ANISOU 3956  CB  ARG A 501     7319   3933   4511   -545   1377  -1093       C  
ATOM   3957  CG  ARG A 501      14.500 118.283 -15.032  1.00 42.21           C  
ANISOU 3957  CG  ARG A 501     7354   4070   4613   -634   1420  -1238       C  
ATOM   3958  CD  ARG A 501      13.551 118.592 -13.890  1.00 42.54           C  
ANISOU 3958  CD  ARG A 501     7268   4139   4758   -665   1446  -1350       C  
ATOM   3959  NE  ARG A 501      12.597 117.510 -13.671  1.00 43.25           N  
ANISOU 3959  NE  ARG A 501     7308   4268   4855   -773   1515  -1475       N  
ATOM   3960  CZ  ARG A 501      12.839 116.443 -12.916  1.00 42.96           C  
ANISOU 3960  CZ  ARG A 501     7331   4203   4790   -868   1654  -1481       C  
ATOM   3961  NH1 ARG A 501      11.910 115.507 -12.771  1.00 43.80           N1+
ANISOU 3961  NH1 ARG A 501     7387   4341   4913   -976   1708  -1592       N1+
ATOM   3962  NH2 ARG A 501      14.008 116.311 -12.304  1.00 41.95           N  
ANISOU 3962  NH2 ARG A 501     7310   4011   4619   -857   1736  -1375       N  
ATOM   3963  N   GLU A 502      16.869 119.620 -18.154  1.00 41.98           N  
ANISOU 3963  N   GLU A 502     7546   4033   4372   -433   1213   -877       N  
ATOM   3964  CA  GLU A 502      16.645 119.499 -19.591  1.00 42.83           C  
ANISOU 3964  CA  GLU A 502     7680   4201   4393   -406   1123   -866       C  
ATOM   3965  C   GLU A 502      17.499 118.397 -20.202  1.00 42.62           C  
ANISOU 3965  C   GLU A 502     7770   4186   4236   -431   1205   -830       C  
ATOM   3966  O   GLU A 502      17.062 117.723 -21.141  1.00 43.39           O  
ANISOU 3966  O   GLU A 502     7885   4339   4260   -443   1172   -892       O  
ATOM   3967  CB  GLU A 502      16.938 120.828 -20.285  1.00 43.19           C  
ANISOU 3967  CB  GLU A 502     7724   4249   4437   -320    997   -743       C  
ATOM   3968  CG  GLU A 502      16.451 120.891 -21.726  1.00 44.34           C  
ANISOU 3968  CG  GLU A 502     7877   4470   4501   -283    879   -740       C  
ATOM   3969  CD  GLU A 502      17.233 121.877 -22.572  1.00 44.62           C  
ANISOU 3969  CD  GLU A 502     7969   4509   4477   -214    798   -565       C  
ATOM   3970  OE1 GLU A 502      17.710 121.480 -23.657  1.00 45.04           O  
ANISOU 3970  OE1 GLU A 502     8100   4622   4392   -204    794   -505       O  
ATOM   3971  OE2 GLU A 502      17.375 123.047 -22.154  1.00 44.53           O1+
ANISOU 3971  OE2 GLU A 502     7925   4440   4556   -172    738   -489       O1+
ATOM   3972  N   ASN A 503      18.706 118.190 -19.678  1.00 41.67           N  
ANISOU 3972  N   ASN A 503     7728   4019   4087   -434   1306   -740       N  
ATOM   3973  CA  ASN A 503      19.658 117.256 -20.267  1.00 41.52           C  
ANISOU 3973  CA  ASN A 503     7818   4012   3946   -438   1378   -697       C  
ATOM   3974  C   ASN A 503      19.590 115.871 -19.636  1.00 41.27           C  
ANISOU 3974  C   ASN A 503     7826   3942   3912   -510   1493   -795       C  
ATOM   3975  O   ASN A 503      19.712 114.865 -20.343  1.00 41.70           O  
ANISOU 3975  O   ASN A 503     7945   4017   3881   -525   1518   -838       O  
ATOM   3976  CB  ASN A 503      21.078 117.814 -20.136  1.00 40.79           C  
ANISOU 3976  CB  ASN A 503     7784   3895   3821   -394   1417   -541       C  
ATOM   3977  CG  ASN A 503      22.038 117.217 -21.147  1.00 41.00           C  
ANISOU 3977  CG  ASN A 503     7905   3970   3705   -369   1451   -479       C  
ATOM   3978  OD1 ASN A 503      22.174 117.723 -22.260  1.00 41.67           O  
ANISOU 3978  OD1 ASN A 503     8001   4121   3712   -326   1376   -409       O  
ATOM   3979  ND2 ASN A 503      22.712 116.141 -20.761  1.00 40.54           N  
ANISOU 3979  ND2 ASN A 503     7915   3882   3607   -392   1563   -503       N  
ATOM   3980  N   SER A 504      19.394 115.797 -18.319  1.00 40.70           N  
ANISOU 3980  N   SER A 504     7720   3813   3932   -555   1562   -831       N  
ATOM   3981  CA  SER A 504      19.450 114.536 -17.593  1.00 40.49           C  
ANISOU 3981  CA  SER A 504     7744   3735   3906   -626   1677   -895       C  
ATOM   3982  C   SER A 504      18.081 113.970 -17.241  1.00 41.18           C  
ANISOU 3982  C   SER A 504     7759   3827   4059   -711   1680  -1040       C  
ATOM   3983  O   SER A 504      17.993 112.790 -16.883  1.00 41.33           O  
ANISOU 3983  O   SER A 504     7828   3804   4071   -783   1763  -1099       O  
ATOM   3984  CB  SER A 504      20.271 114.705 -16.308  1.00 39.50           C  
ANISOU 3984  CB  SER A 504     7643   3548   3818   -626   1765   -827       C  
ATOM   3985  OG  SER A 504      19.822 115.821 -15.556  1.00 39.30           O  
ANISOU 3985  OG  SER A 504     7521   3524   3886   -612   1726   -824       O  
ATOM   3986  N   GLY A 505      17.021 114.772 -17.312  1.00 41.69           N  
ANISOU 3986  N   GLY A 505     7708   3940   4194   -706   1592  -1098       N  
ATOM   3987  CA  GLY A 505      15.697 114.295 -16.966  1.00 42.46           C  
ANISOU 3987  CA  GLY A 505     7717   4057   4360   -789   1596  -1240       C  
ATOM   3988  C   GLY A 505      15.470 114.133 -15.476  1.00 42.10           C  
ANISOU 3988  C   GLY A 505     7633   3975   4390   -855   1698  -1270       C  
ATOM   3989  O   GLY A 505      14.358 114.348 -14.986  1.00 42.68           O  
ANISOU 3989  O   GLY A 505     7588   4086   4543   -899   1686  -1368       O  
ATOM   3990  N   GLY A 506      16.515 113.756 -14.743  1.00 41.26           N  
ANISOU 3990  N   GLY A 506     7621   3803   4252   -859   1798  -1189       N  
ATOM   3991  CA  GLY A 506      16.401 113.532 -13.316  1.00 40.98           C  
ANISOU 3991  CA  GLY A 506     7568   3737   4267   -920   1900  -1205       C  
ATOM   3992  C   GLY A 506      17.179 114.524 -12.476  1.00 40.07           C  
ANISOU 3992  C   GLY A 506     7449   3606   4172   -852   1912  -1115       C  
ATOM   3993  O   GLY A 506      16.955 114.631 -11.268  1.00 39.95           O  
ANISOU 3993  O   GLY A 506     7392   3587   4201   -887   1976  -1138       O  
ATOM   3994  N   GLY A 507      18.098 115.251 -13.098  1.00 39.54           N  
ANISOU 3994  N   GLY A 507     7422   3532   4070   -760   1851  -1014       N  
ATOM   3995  CA  GLY A 507      18.865 116.249 -12.386  1.00 38.78           C  
ANISOU 3995  CA  GLY A 507     7318   3415   4002   -697   1848   -931       C  
ATOM   3996  C   GLY A 507      18.038 117.479 -12.058  1.00 39.08           C  
ANISOU 3996  C   GLY A 507     7226   3489   4135   -664   1766   -981       C  
ATOM   3997  O   GLY A 507      16.891 117.637 -12.480  1.00 39.89           O  
ANISOU 3997  O   GLY A 507     7238   3640   4278   -678   1702  -1074       O  
ATOM   3998  N   VAL A 508      18.645 118.371 -11.273  1.00 38.51           N  
ANISOU 3998  N   VAL A 508     7140   3392   4102   -613   1763   -925       N  
ATOM   3999  CA  VAL A 508      18.004 119.618 -10.864  1.00 38.82           C  
ANISOU 3999  CA  VAL A 508     7062   3450   4238   -566   1681   -972       C  
ATOM   4000  C   VAL A 508      19.038 120.735 -10.813  1.00 38.27           C  
ANISOU 4000  C   VAL A 508     7015   3333   4191   -484   1624   -861       C  
ATOM   4001  O   VAL A 508      18.775 121.807 -10.256  1.00 38.42           O  
ANISOU 4001  O   VAL A 508     6955   3345   4297   -438   1563   -889       O  
ATOM   4002  CB  VAL A 508      17.313 119.481  -9.494  1.00 39.01           C  
ANISOU 4002  CB  VAL A 508     7011   3500   4311   -614   1757  -1076       C  
ATOM   4003  CG1 VAL A 508      16.096 118.568  -9.570  1.00 39.83           C  
ANISOU 4003  CG1 VAL A 508     7061   3659   4415   -703   1799  -1195       C  
ATOM   4004  CG2 VAL A 508      18.301 118.976  -8.466  1.00 38.26           C  
ANISOU 4004  CG2 VAL A 508     7002   3366   4170   -636   1872  -1016       C  
ATOM   4005  N   GLU A 509      20.216 120.492 -11.388  1.00 37.74           N  
ANISOU 4005  N   GLU A 509     7052   3234   4052   -467   1641   -741       N  
ATOM   4006  CA  GLU A 509      21.331 121.422 -11.255  1.00 37.24           C  
ANISOU 4006  CA  GLU A 509     7015   3126   4008   -408   1606   -627       C  
ATOM   4007  C   GLU A 509      20.959 122.809 -11.766  1.00 38.82           C  
ANISOU 4007  C   GLU A 509     7145   3316   4290   -345   1463   -608       C  
ATOM   4008  O   GLU A 509      20.313 122.956 -12.807  1.00 40.92           O  
ANISOU 4008  O   GLU A 509     7389   3610   4548   -332   1381   -617       O  
ATOM   4009  CB  GLU A 509      22.551 120.889 -12.011  1.00 36.82           C  
ANISOU 4009  CB  GLU A 509     7071   3062   3858   -403   1644   -508       C  
ATOM   4010  CG  GLU A 509      23.799 121.762 -11.911  1.00 36.39           C  
ANISOU 4010  CG  GLU A 509     7041   2967   3819   -355   1619   -384       C  
ATOM   4011  CD  GLU A 509      23.893 122.789 -13.026  1.00 38.80           C  
ANISOU 4011  CD  GLU A 509     7331   3272   4141   -312   1500   -297       C  
ATOM   4012  OE1 GLU A 509      24.945 123.456 -13.137  1.00 39.45           O  
ANISOU 4012  OE1 GLU A 509     7436   3323   4230   -285   1480   -181       O  
ATOM   4013  OE2 GLU A 509      22.917 122.928 -13.794  1.00 40.45           O1+
ANISOU 4013  OE2 GLU A 509     7502   3511   4354   -307   1426   -341       O1+
ATOM   4014  N   GLY A 510      21.375 123.833 -11.018  1.00 38.00           N  
ANISOU 4014  N   GLY A 510     7008   3165   4266   -303   1427   -582       N  
ATOM   4015  CA  GLY A 510      21.145 125.211 -11.382  1.00 38.57           C  
ANISOU 4015  CA  GLY A 510     7023   3201   4430   -240   1287   -554       C  
ATOM   4016  C   GLY A 510      19.894 125.829 -10.796  1.00 39.23           C  
ANISOU 4016  C   GLY A 510     6989   3296   4619   -213   1222   -693       C  
ATOM   4017  O   GLY A 510      19.802 127.058 -10.727  1.00 39.68           O  
ANISOU 4017  O   GLY A 510     6996   3303   4776   -150   1110   -685       O  
ATOM   4018  N   LEU A 511      18.931 125.018 -10.370  1.00 38.99           N  
ANISOU 4018  N   LEU A 511     6911   3331   4575   -258   1289   -823       N  
ATOM   4019  CA  LEU A 511      17.680 125.541  -9.851  1.00 39.77           C  
ANISOU 4019  CA  LEU A 511     6882   3462   4767   -233   1236   -969       C  
ATOM   4020  C   LEU A 511      17.831 125.985  -8.399  1.00 39.56           C  
ANISOU 4020  C   LEU A 511     6810   3422   4800   -217   1279  -1032       C  
ATOM   4021  O   LEU A 511      18.749 125.575  -7.683  1.00 38.80           O  
ANISOU 4021  O   LEU A 511     6780   3307   4655   -245   1376   -983       O  
ATOM   4022  CB  LEU A 511      16.573 124.493  -9.962  1.00 40.21           C  
ANISOU 4022  CB  LEU A 511     6892   3602   4785   -300   1296  -1086       C  
ATOM   4023  CG  LEU A 511      16.011 124.242 -11.362  1.00 40.82           C  
ANISOU 4023  CG  LEU A 511     6971   3709   4828   -300   1219  -1078       C  
ATOM   4024  CD1 LEU A 511      15.056 123.066 -11.344  1.00 41.22           C  
ANISOU 4024  CD1 LEU A 511     6983   3836   4841   -384   1297  -1194       C  
ATOM   4025  CD2 LEU A 511      15.315 125.486 -11.890  1.00 41.75           C  
ANISOU 4025  CD2 LEU A 511     7002   3817   5042   -212   1050  -1104       C  
ATOM   4026  N   GLY A 512      16.905 126.841  -7.969  1.00 40.37           N  
ANISOU 4026  N   GLY A 512     6793   3539   5006   -163   1200  -1150       N  
ATOM   4027  CA  GLY A 512      16.838 127.298  -6.602  1.00 40.43           C  
ANISOU 4027  CA  GLY A 512     6738   3555   5070   -140   1233  -1243       C  
ATOM   4028  C   GLY A 512      15.666 126.683  -5.851  1.00 41.00           C  
ANISOU 4028  C   GLY A 512     6709   3734   5134   -185   1318  -1406       C  
ATOM   4029  O   GLY A 512      14.840 125.959  -6.400  1.00 41.40           O  
ANISOU 4029  O   GLY A 512     6730   3847   5154   -237   1341  -1455       O  
ATOM   4030  N   LEU A 513      15.615 126.999  -4.553  1.00 41.13           N  
ANISOU 4030  N   LEU A 513     6671   3778   5179   -168   1365  -1494       N  
ATOM   4031  CA  LEU A 513      14.538 126.506  -3.698  1.00 41.82           C  
ANISOU 4031  CA  LEU A 513     6653   3980   5255   -213   1456  -1650       C  
ATOM   4032  C   LEU A 513      13.169 126.929  -4.206  1.00 43.00           C  
ANISOU 4032  C   LEU A 513     6662   4187   5487   -178   1364  -1778       C  
ATOM   4033  O   LEU A 513      12.174 126.245  -3.943  1.00 43.64           O  
ANISOU 4033  O   LEU A 513     6660   4375   5547   -242   1441  -1888       O  
ATOM   4034  CB  LEU A 513      14.737 127.000  -2.264  1.00 41.94           C  
ANISOU 4034  CB  LEU A 513     6626   4021   5289   -179   1499  -1727       C  
ATOM   4035  CG  LEU A 513      15.696 126.208  -1.372  1.00 41.11           C  
ANISOU 4035  CG  LEU A 513     6625   3919   5075   -242   1640  -1655       C  
ATOM   4036  CD1 LEU A 513      15.910 126.934  -0.055  1.00 41.38           C  
ANISOU 4036  CD1 LEU A 513     6612   3974   5135   -184   1647  -1736       C  
ATOM   4037  CD2 LEU A 513      15.163 124.802  -1.135  1.00 41.22           C  
ANISOU 4037  CD2 LEU A 513     6652   4020   4990   -362   1792  -1677       C  
ATOM   4038  N   GLN A 514      13.098 128.037  -4.931  1.00 43.40           N  
ANISOU 4038  N   GLN A 514     6686   4170   5635    -78   1197  -1764       N  
ATOM   4039  CA  GLN A 514      11.860 128.601  -5.452  1.00 44.63           C  
ANISOU 4039  CA  GLN A 514     6709   4367   5882    -18   1079  -1882       C  
ATOM   4040  C   GLN A 514      11.308 127.838  -6.647  1.00 44.84           C  
ANISOU 4040  C   GLN A 514     6745   4428   5862    -73   1065  -1857       C  
ATOM   4041  O   GLN A 514      10.396 128.355  -7.306  1.00 45.85           O  
ANISOU 4041  O   GLN A 514     6780   4578   6065    -13    940  -1929       O  
ATOM   4042  CB  GLN A 514      12.086 130.064  -5.834  1.00 45.06           C  
ANISOU 4042  CB  GLN A 514     6753   4314   6055    112    894  -1853       C  
ATOM   4043  CG  GLN A 514      13.176 130.754  -5.022  1.00 44.49           C  
ANISOU 4043  CG  GLN A 514     6741   4153   6010    153    892  -1798       C  
ATOM   4044  CD  GLN A 514      14.548 130.664  -5.671  1.00 43.40           C  
ANISOU 4044  CD  GLN A 514     6764   3909   5818    126    887  -1589       C  
ATOM   4045  OE1 GLN A 514      14.669 130.648  -6.896  1.00 43.38           O  
ANISOU 4045  OE1 GLN A 514     6818   3865   5801    125    815  -1480       O  
ATOM   4046  NE2 GLN A 514      15.589 130.608  -4.848  1.00 42.59           N  
ANISOU 4046  NE2 GLN A 514     6730   3772   5682    106    964  -1535       N  
ATOM   4047  N   ARG A 515      11.805 126.641  -6.954  1.00 44.02           N  
ANISOU 4047  N   ARG A 515     6749   4332   5645   -177   1179  -1766       N  
ATOM   4048  CA  ARG A 515      11.392 125.948  -8.167  1.00 44.24           C  
ANISOU 4048  CA  ARG A 515     6799   4384   5628   -222   1152  -1739       C  
ATOM   4049  C   ARG A 515      11.378 124.436  -7.975  1.00 43.86           C  
ANISOU 4049  C   ARG A 515     6801   4389   5476   -358   1316  -1740       C  
ATOM   4050  O   ARG A 515      10.839 123.705  -8.813  1.00 44.25           O  
ANISOU 4050  O   ARG A 515     6847   4474   5490   -412   1312  -1759       O  
ATOM   4051  CB  ARG A 515      12.319 126.323  -9.326  1.00 43.72           C  
ANISOU 4051  CB  ARG A 515     6856   4220   5535   -176   1053  -1570       C  
ATOM   4052  CG  ARG A 515      11.612 126.541 -10.650  1.00 44.58           C  
ANISOU 4052  CG  ARG A 515     6932   4344   5662   -137    916  -1575       C  
ATOM   4053  CD  ARG A 515      11.866 127.946 -11.172  1.00 44.98           C  
ANISOU 4053  CD  ARG A 515     6987   4310   5795    -17    740  -1504       C  
ATOM   4054  NE  ARG A 515      11.297 128.967 -10.296  1.00 45.70           N  
ANISOU 4054  NE  ARG A 515     6956   4394   6012     65    676  -1624       N  
ATOM   4055  CZ  ARG A 515      11.501 130.273 -10.439  1.00 46.16           C  
ANISOU 4055  CZ  ARG A 515     7009   4361   6169    173    528  -1584       C  
ATOM   4056  NH1 ARG A 515      10.940 131.130  -9.597  1.00 46.90           N1+
ANISOU 4056  NH1 ARG A 515     6988   4453   6381    250    472  -1715       N1+
ATOM   4057  NH2 ARG A 515      12.271 130.722 -11.421  1.00 45.99           N  
ANISOU 4057  NH2 ARG A 515     7097   4249   6128    202    435  -1413       N  
ATOM   4058  N   LEU A 516      11.965 123.954  -6.877  1.00 43.22           N  
ANISOU 4058  N   LEU A 516     6769   4306   5345   -412   1454  -1721       N  
ATOM   4059  CA  LEU A 516      12.037 122.512  -6.656  1.00 42.93           C  
ANISOU 4059  CA  LEU A 516     6798   4299   5212   -540   1606  -1706       C  
ATOM   4060  C   LEU A 516      10.666 121.914  -6.366  1.00 44.06           C  
ANISOU 4060  C   LEU A 516     6811   4553   5375   -622   1665  -1858       C  
ATOM   4061  O   LEU A 516      10.399 120.768  -6.747  1.00 44.21           O  
ANISOU 4061  O   LEU A 516     6866   4592   5341   -726   1735  -1858       O  
ATOM   4062  CB  LEU A 516      12.999 122.198  -5.511  1.00 42.10           C  
ANISOU 4062  CB  LEU A 516     6781   4166   5050   -569   1729  -1643       C  
ATOM   4063  CG  LEU A 516      14.466 122.568  -5.719  1.00 40.98           C  
ANISOU 4063  CG  LEU A 516     6773   3920   4877   -510   1698  -1488       C  
ATOM   4064  CD1 LEU A 516      15.329 121.955  -4.625  1.00 40.29           C  
ANISOU 4064  CD1 LEU A 516     6774   3819   4717   -556   1831  -1435       C  
ATOM   4065  CD2 LEU A 516      14.943 122.128  -7.094  1.00 40.59           C  
ANISOU 4065  CD2 LEU A 516     6823   3820   4780   -518   1652  -1381       C  
ATOM   4066  N   GLY A 517       9.787 122.668  -5.705  1.00 44.96           N  
ANISOU 4066  N   GLY A 517     6769   4744   5569   -577   1636  -1994       N  
ATOM   4067  CA  GLY A 517       8.475 122.140  -5.378  1.00 46.18           C  
ANISOU 4067  CA  GLY A 517     6780   5020   5744   -659   1699  -2144       C  
ATOM   4068  C   GLY A 517       7.630 121.835  -6.597  1.00 46.93           C  
ANISOU 4068  C   GLY A 517     6820   5144   5867   -680   1614  -2194       C  
ATOM   4069  O   GLY A 517       6.806 120.918  -6.570  1.00 47.71           O  
ANISOU 4069  O   GLY A 517     6856   5319   5953   -794   1692  -2274       O  
ATOM   4070  N   TYR A 518       7.810 122.600  -7.677  1.00 46.82           N  
ANISOU 4070  N   TYR A 518     6828   5071   5891   -574   1451  -2146       N  
ATOM   4071  CA  TYR A 518       7.084 122.328  -8.913  1.00 47.56           C  
ANISOU 4071  CA  TYR A 518     6881   5193   5996   -583   1357  -2184       C  
ATOM   4072  C   TYR A 518       7.525 121.025  -9.566  1.00 47.05           C  
ANISOU 4072  C   TYR A 518     6949   5094   5833   -692   1431  -2101       C  
ATOM   4073  O   TYR A 518       6.761 120.447 -10.346  1.00 47.85           O  
ANISOU 4073  O   TYR A 518     7004   5242   5935   -743   1398  -2167       O  
ATOM   4074  CB  TYR A 518       7.260 123.486  -9.896  1.00 47.64           C  
ANISOU 4074  CB  TYR A 518     6900   5144   6055   -439   1163  -2133       C  
ATOM   4075  CG  TYR A 518       6.690 124.798  -9.406  1.00 48.42           C  
ANISOU 4075  CG  TYR A 518     6862   5266   6271   -319   1059  -2232       C  
ATOM   4076  CD1 TYR A 518       5.348 125.106  -9.589  1.00 49.90           C  
ANISOU 4076  CD1 TYR A 518     6869   5549   6541   -286    978  -2395       C  
ATOM   4077  CD2 TYR A 518       7.494 125.730  -8.764  1.00 47.80           C  
ANISOU 4077  CD2 TYR A 518     6827   5111   6224   -235   1038  -2171       C  
ATOM   4078  CE1 TYR A 518       4.822 126.305  -9.145  1.00 50.74           C  
ANISOU 4078  CE1 TYR A 518     6847   5674   6759   -163    876  -2497       C  
ATOM   4079  CE2 TYR A 518       6.977 126.931  -8.316  1.00 48.64           C  
ANISOU 4079  CE2 TYR A 518     6810   5227   6444   -118    935  -2273       C  
ATOM   4080  CZ  TYR A 518       5.642 127.213  -8.509  1.00 50.11           C  
ANISOU 4080  CZ  TYR A 518     6822   5508   6711    -79    855  -2437       C  
ATOM   4081  OH  TYR A 518       5.124 128.408  -8.065  1.00 51.06           O  
ANISOU 4081  OH  TYR A 518     6817   5635   6949     49    747  -2548       O  
ATOM   4082  N   ILE A 519       8.736 120.554  -9.269  1.00 45.83           N  
ANISOU 4082  N   ILE A 519     6955   4859   5599   -723   1522  -1967       N  
ATOM   4083  CA  ILE A 519       9.203 119.288  -9.822  1.00 45.41           C  
ANISOU 4083  CA  ILE A 519     7033   4766   5456   -818   1595  -1896       C  
ATOM   4084  C   ILE A 519       8.568 118.113  -9.089  1.00 46.00           C  
ANISOU 4084  C   ILE A 519     7071   4893   5515   -968   1743  -1977       C  
ATOM   4085  O   ILE A 519       8.216 117.100  -9.704  1.00 46.47           O  
ANISOU 4085  O   ILE A 519     7154   4956   5546  -1059   1766  -2002       O  
ATOM   4086  CB  ILE A 519      10.741 119.229  -9.775  1.00 44.02           C  
ANISOU 4086  CB  ILE A 519     7034   4488   5205   -787   1633  -1729       C  
ATOM   4087  CG1 ILE A 519      11.341 120.355 -10.619  1.00 43.64           C  
ANISOU 4087  CG1 ILE A 519     7020   4389   5171   -656   1487  -1639       C  
ATOM   4088  CG2 ILE A 519      11.244 117.877 -10.252  1.00 43.69           C  
ANISOU 4088  CG2 ILE A 519     7125   4403   5072   -878   1714  -1668       C  
ATOM   4089  CD1 ILE A 519      12.850 120.344 -10.657  1.00 42.41           C  
ANISOU 4089  CD1 ILE A 519     7022   4145   4946   -627   1520  -1478       C  
ATOM   4090  N   LEU A 520       8.407 118.228  -7.768  1.00 46.12           N  
ANISOU 4090  N   LEU A 520     7026   4949   5547   -999   1844  -2019       N  
ATOM   4091  CA  LEU A 520       7.753 117.165  -7.010  1.00 46.88           C  
ANISOU 4091  CA  LEU A 520     7081   5103   5628  -1150   1990  -2087       C  
ATOM   4092  C   LEU A 520       6.265 117.095  -7.329  1.00 48.41           C  
ANISOU 4092  C   LEU A 520     7092   5408   5894  -1201   1953  -2249       C  
ATOM   4093  O   LEU A 520       5.695 116.002  -7.418  1.00 49.18           O  
ANISOU 4093  O   LEU A 520     7177   5530   5981  -1340   2028  -2294       O  
ATOM   4094  CB  LEU A 520       7.975 117.376  -5.512  1.00 46.74           C  
ANISOU 4094  CB  LEU A 520     7045   5117   5595  -1163   2105  -2087       C  
ATOM   4095  CG  LEU A 520       9.393 117.121  -5.002  1.00 45.42           C  
ANISOU 4095  CG  LEU A 520     7060   4852   5346  -1149   2175  -1935       C  
ATOM   4096  CD1 LEU A 520       9.527 117.542  -3.549  1.00 45.43           C  
ANISOU 4096  CD1 LEU A 520     7024   4903   5336  -1138   2262  -1952       C  
ATOM   4097  CD2 LEU A 520       9.759 115.655  -5.169  1.00 45.30           C  
ANISOU 4097  CD2 LEU A 520     7182   4772   5257  -1274   2276  -1861       C  
ATOM   4098  N   GLU A 521       5.621 118.252  -7.502  1.00 48.97           N  
ANISOU 4098  N   GLU A 521     7018   5543   6047  -1090   1832  -2341       N  
ATOM   4099  CA  GLU A 521       4.208 118.269  -7.868  1.00 50.52           C  
ANISOU 4099  CA  GLU A 521     7026   5850   6317  -1121   1779  -2503       C  
ATOM   4100  C   GLU A 521       3.984 117.624  -9.229  1.00 50.82           C  
ANISOU 4100  C   GLU A 521     7105   5862   6342  -1156   1698  -2501       C  
ATOM   4101  O   GLU A 521       3.034 116.852  -9.411  1.00 51.99           O  
ANISOU 4101  O   GLU A 521     7162   6079   6515  -1271   1731  -2605       O  
ATOM   4102  CB  GLU A 521       3.684 119.705  -7.857  1.00 51.05           C  
ANISOU 4102  CB  GLU A 521     6946   5973   6476   -968   1643  -2594       C  
ATOM   4103  CG  GLU A 521       2.470 119.928  -8.740  1.00 52.44           C  
ANISOU 4103  CG  GLU A 521     6963   6233   6729   -942   1515  -2729       C  
ATOM   4104  CD  GLU A 521       1.927 121.336  -8.633  1.00 53.13           C  
ANISOU 4104  CD  GLU A 521     6902   6370   6914   -784   1380  -2826       C  
ATOM   4105  OE1 GLU A 521       1.015 121.557  -7.810  1.00 54.26           O  
ANISOU 4105  OE1 GLU A 521     6865   6632   7117   -798   1428  -2974       O  
ATOM   4106  OE2 GLU A 521       2.416 122.224  -9.362  1.00 52.64           O1+
ANISOU 4106  OE2 GLU A 521     6903   6228   6870   -645   1227  -2753       O1+
ATOM   4107  N   GLU A 522       4.850 117.928 -10.200  1.00 51.64           N  
ANISOU 4107  N   GLU A 522     7343   5872   6405  -1062   1593  -2386       N  
ATOM   4108  CA  GLU A 522       4.756 117.280 -11.504  1.00 52.60           C  
ANISOU 4108  CA  GLU A 522     7522   5971   6493  -1090   1520  -2378       C  
ATOM   4109  C   GLU A 522       5.025 115.785 -11.399  1.00 51.77           C  
ANISOU 4109  C   GLU A 522     7525   5821   6323  -1246   1657  -2346       C  
ATOM   4110  O   GLU A 522       4.372 114.983 -12.076  1.00 52.99           O  
ANISOU 4110  O   GLU A 522     7650   6001   6483  -1331   1640  -2421       O  
ATOM   4111  CB  GLU A 522       5.727 117.931 -12.488  1.00 52.19           C  
ANISOU 4111  CB  GLU A 522     7598   5837   6393   -958   1396  -2247       C  
ATOM   4112  CG  GLU A 522       5.272 119.286 -13.002  1.00 54.17           C  
ANISOU 4112  CG  GLU A 522     7746   6123   6712   -810   1220  -2284       C  
ATOM   4113  CD  GLU A 522       6.378 120.043 -13.714  1.00 53.82           C  
ANISOU 4113  CD  GLU A 522     7838   5989   6620   -689   1121  -2126       C  
ATOM   4114  OE1 GLU A 522       7.294 119.391 -14.257  1.00 52.36           O  
ANISOU 4114  OE1 GLU A 522     7812   5743   6341   -718   1158  -2013       O  
ATOM   4115  OE2 GLU A 522       6.335 121.291 -13.720  1.00 54.96           O1+
ANISOU 4115  OE2 GLU A 522     7930   6127   6827   -565   1006  -2116       O1+
ATOM   4116  N   MET A 523       5.976 115.390 -10.548  1.00 52.74           N  
ANISOU 4116  N   MET A 523     7775   5873   6391  -1284   1786  -2240       N  
ATOM   4117  CA  MET A 523       6.295 113.973 -10.401  1.00 51.97           C  
ANISOU 4117  CA  MET A 523     7796   5715   6237  -1425   1910  -2200       C  
ATOM   4118  C   MET A 523       5.128 113.186  -9.818  1.00 53.72           C  
ANISOU 4118  C   MET A 523     7893   6010   6507  -1586   2006  -2323       C  
ATOM   4119  O   MET A 523       5.020 111.977 -10.051  1.00 54.36           O  
ANISOU 4119  O   MET A 523     8038   6048   6568  -1714   2067  -2329       O  
ATOM   4120  CB  MET A 523       7.539 113.801  -9.527  1.00 49.52           C  
ANISOU 4120  CB  MET A 523     7637   5317   5860  -1419   2020  -2061       C  
ATOM   4121  CG  MET A 523       8.844 113.710 -10.303  1.00 47.78           C  
ANISOU 4121  CG  MET A 523     7599   4992   5564  -1340   1975  -1925       C  
ATOM   4122  SD  MET A 523      10.303 113.791  -9.242  1.00 45.66           S  
ANISOU 4122  SD  MET A 523     7477   4639   5232  -1301   2078  -1773       S  
ATOM   4123  CE  MET A 523       9.943 112.509  -8.045  1.00 46.30           C  
ANISOU 4123  CE  MET A 523     7579   4715   5299  -1477   2259  -1796       C  
ATOM   4124  N   ASN A 524       4.249 113.844  -9.063  1.00 51.44           N  
ANISOU 4124  N   ASN A 524     7426   5835   6285  -1584   2022  -2425       N  
ATOM   4125  CA  ASN A 524       3.108 113.154  -8.475  1.00 52.96           C  
ANISOU 4125  CA  ASN A 524     7481   6118   6524  -1744   2122  -2543       C  
ATOM   4126  C   ASN A 524       1.988 112.899  -9.476  1.00 54.48           C  
ANISOU 4126  C   ASN A 524     7543   6376   6780  -1788   2025  -2679       C  
ATOM   4127  O   ASN A 524       1.085 112.109  -9.179  1.00 56.16           O  
ANISOU 4127  O   ASN A 524     7658   6648   7031  -1946   2106  -2772       O  
ATOM   4128  CB  ASN A 524       2.563 113.951  -7.287  1.00 53.45           C  
ANISOU 4128  CB  ASN A 524     7385   6296   6627  -1722   2180  -2615       C  
ATOM   4129  CG  ASN A 524       1.700 113.107  -6.364  1.00 54.85           C  
ANISOU 4129  CG  ASN A 524     7462   6560   6820  -1909   2339  -2690       C  
ATOM   4130  OD1 ASN A 524       1.955 111.918  -6.175  1.00 54.98           O  
ANISOU 4130  OD1 ASN A 524     7592   6506   6792  -2055   2449  -2624       O  
ATOM   4131  ND2 ASN A 524       0.668 113.718  -5.790  1.00 56.04           N  
ANISOU 4131  ND2 ASN A 524     7397   6863   7034  -1907   2351  -2828       N  
ATOM   4132  N   ARG A 525       2.021 113.537 -10.650  1.00 54.53           N  
ANISOU 4132  N   ARG A 525     7547   6376   6796  -1657   1853  -2692       N  
ATOM   4133  CA  ARG A 525       0.961 113.332 -11.632  1.00 56.07           C  
ANISOU 4133  CA  ARG A 525     7618   6641   7047  -1686   1746  -2826       C  
ATOM   4134  C   ARG A 525       1.121 112.018 -12.388  1.00 56.30           C  
ANISOU 4134  C   ARG A 525     7765   6592   7035  -1804   1764  -2810       C  
ATOM   4135  O   ARG A 525       0.116 111.408 -12.770  1.00 58.13           O  
ANISOU 4135  O   ARG A 525     7886   6882   7320  -1911   1746  -2937       O  
ATOM   4136  CB  ARG A 525       0.912 114.502 -12.617  1.00 56.21           C  
ANISOU 4136  CB  ARG A 525     7593   6684   7082  -1500   1547  -2840       C  
ATOM   4137  CG  ARG A 525       0.348 115.790 -12.033  1.00 56.84           C  
ANISOU 4137  CG  ARG A 525     7502   6857   7237  -1388   1493  -2914       C  
ATOM   4138  CD  ARG A 525       0.150 116.842 -13.115  1.00 57.48           C  
ANISOU 4138  CD  ARG A 525     7538   6957   7346  -1216   1281  -2936       C  
ATOM   4139  NE  ARG A 525      -1.221 116.880 -13.622  1.00 59.78           N  
ANISOU 4139  NE  ARG A 525     7627   7369   7717  -1230   1184  -3112       N  
ATOM   4140  CZ  ARG A 525      -2.088 117.851 -13.351  1.00 61.06           C  
ANISOU 4140  CZ  ARG A 525     7595   7633   7972  -1139   1104  -3232       C  
ATOM   4141  NH1 ARG A 525      -1.724 118.868 -12.581  1.00 60.24           N1+
ANISOU 4141  NH1 ARG A 525     7479   7517   7893  -1029   1108  -3196       N1+
ATOM   4142  NH2 ARG A 525      -3.315 117.812 -13.853  1.00 63.32           N  
ANISOU 4142  NH2 ARG A 525     7697   8033   8330  -1153   1013  -3395       N  
ATOM   4143  N   ALA A 526       2.353 111.573 -12.617  1.00 56.01           N  
ANISOU 4143  N   ALA A 526     7946   6425   6910  -1783   1793  -2667       N  
ATOM   4144  CA  ALA A 526       2.563 110.280 -13.245  1.00 56.18           C  
ANISOU 4144  CA  ALA A 526     8089   6361   6894  -1890   1818  -2658       C  
ATOM   4145  C   ALA A 526       2.151 109.162 -12.287  1.00 57.07           C  
ANISOU 4145  C   ALA A 526     8190   6456   7038  -2093   1984  -2685       C  
ATOM   4146  O   ALA A 526       2.322 109.283 -11.071  1.00 56.70           O  
ANISOU 4146  O   ALA A 526     8137   6417   6989  -2130   2109  -2634       O  
ATOM   4147  CB  ALA A 526       4.024 110.109 -13.650  1.00 54.13           C  
ANISOU 4147  CB  ALA A 526     8058   5975   6533  -1808   1815  -2502       C  
ATOM   4148  N   PRO A 527       1.600 108.061 -12.809  1.00 56.68           N  
ANISOU 4148  N   PRO A 527     8139   6382   7016  -2230   1987  -2764       N  
ATOM   4149  CA  PRO A 527       1.155 106.975 -11.924  1.00 57.75           C  
ANISOU 4149  CA  PRO A 527     8262   6491   7189  -2440   2142  -2782       C  
ATOM   4150  C   PRO A 527       2.319 106.240 -11.277  1.00 56.75           C  
ANISOU 4150  C   PRO A 527     8355   6216   6991  -2480   2266  -2625       C  
ATOM   4151  O   PRO A 527       3.484 106.526 -11.570  1.00 55.23           O  
ANISOU 4151  O   PRO A 527     8319   5944   6721  -2346   2230  -2512       O  
ATOM   4152  CB  PRO A 527       0.364 106.061 -12.867  1.00 59.31           C  
ANISOU 4152  CB  PRO A 527     8416   6682   7438  -2555   2079  -2908       C  
ATOM   4153  CG  PRO A 527       0.991 106.284 -14.199  1.00 58.54           C  
ANISOU 4153  CG  PRO A 527     8424   6538   7278  -2406   1926  -2890       C  
ATOM   4154  CD  PRO A 527       1.379 107.740 -14.231  1.00 57.27           C  
ANISOU 4154  CD  PRO A 527     8229   6446   7085  -2205   1846  -2837       C  
ATOM   4155  N   GLY A 528       2.013 105.293 -10.390  1.00 57.71           N  
ANISOU 4155  N   GLY A 528     8487   6302   7137  -2665   2411  -2614       N  
ATOM   4156  CA  GLY A 528       3.015 104.500  -9.718  1.00 57.06           C  
ANISOU 4156  CA  GLY A 528     8610   6076   6993  -2716   2528  -2469       C  
ATOM   4157  C   GLY A 528       2.723 104.410  -8.239  1.00 57.58           C  
ANISOU 4157  C   GLY A 528     8624   6189   7065  -2832   2691  -2427       C  
ATOM   4158  O   GLY A 528       1.594 104.644  -7.794  1.00 58.85           O  
ANISOU 4158  O   GLY A 528     8587   6486   7288  -2922   2730  -2530       O  
ATOM   4159  N   GLY A 529       3.754 104.071  -7.473  1.00 56.69           N  
ANISOU 4159  N   GLY A 529     8687   5972   6879  -2825   2785  -2278       N  
ATOM   4160  CA  GLY A 529       3.638 103.910  -6.040  1.00 57.17           C  
ANISOU 4160  CA  GLY A 529     8735   6067   6919  -2930   2944  -2214       C  
ATOM   4161  C   GLY A 529       3.995 105.169  -5.278  1.00 56.01           C  
ANISOU 4161  C   GLY A 529     8531   6024   6726  -2786   2957  -2178       C  
ATOM   4162  O   GLY A 529       4.023 106.276  -5.821  1.00 55.15           O  
ANISOU 4162  O   GLY A 529     8340   5986   6628  -2624   2841  -2230       O  
ATOM   4163  N   LYS A 530       4.273 104.984  -3.991  1.00 56.11           N  
ANISOU 4163  N   LYS A 530     8593   6041   6685  -2847   3096  -2087       N  
ATOM   4164  CA  LYS A 530       4.632 106.085  -3.114  1.00 55.19           C  
ANISOU 4164  CA  LYS A 530     8430   6020   6519  -2724   3122  -2055       C  
ATOM   4165  C   LYS A 530       5.978 106.681  -3.526  1.00 53.16           C  
ANISOU 4165  C   LYS A 530     8320   5672   6206  -2524   3029  -1959       C  
ATOM   4166  O   LYS A 530       6.735 106.108  -4.315  1.00 52.50           O  
ANISOU 4166  O   LYS A 530     8394   5449   6103  -2493   2975  -1896       O  
ATOM   4167  CB  LYS A 530       4.680 105.608  -1.662  1.00 55.90           C  
ANISOU 4167  CB  LYS A 530     8561   6131   6548  -2843   3294  -1971       C  
ATOM   4168  CG  LYS A 530       3.422 104.871  -1.220  1.00 58.09           C  
ANISOU 4168  CG  LYS A 530     8710   6489   6872  -3068   3405  -2042       C  
ATOM   4169  CD  LYS A 530       3.724 103.833  -0.149  1.00 58.92           C  
ANISOU 4169  CD  LYS A 530     8955   6522   6909  -3223   3565  -1907       C  
ATOM   4170  CE  LYS A 530       4.239 104.474   1.128  1.00 58.36           C  
ANISOU 4170  CE  LYS A 530     8903   6534   6739  -3150   3651  -1830       C  
ATOM   4171  NZ  LYS A 530       4.502 103.464   2.192  1.00 59.34           N1+
ANISOU 4171  NZ  LYS A 530     9165   6597   6785  -3302   3804  -1691       N1+
ATOM   4172  N   MET A 531       6.268 107.859  -2.983  1.00 52.28           N  
ANISOU 4172  N   MET A 531     8148   5644   6071  -2389   3011  -1955       N  
ATOM   4173  CA  MET A 531       7.547 108.516  -3.203  1.00 50.48           C  
ANISOU 4173  CA  MET A 531     8044   5342   5793  -2210   2936  -1859       C  
ATOM   4174  C   MET A 531       8.541 108.081  -2.137  1.00 49.95           C  
ANISOU 4174  C   MET A 531     8138   5204   5637  -2222   3044  -1719       C  
ATOM   4175  O   MET A 531       8.187 107.924  -0.968  1.00 50.77           O  
ANISOU 4175  O   MET A 531     8203   5377   5710  -2310   3164  -1711       O  
ATOM   4176  CB  MET A 531       7.389 110.036  -3.182  1.00 49.89           C  
ANISOU 4176  CB  MET A 531     7828   5378   5749  -2055   2848  -1927       C  
ATOM   4177  CG  MET A 531       6.546 110.580  -4.318  1.00 50.30           C  
ANISOU 4177  CG  MET A 531     7737   5491   5885  -2009   2714  -2052       C  
ATOM   4178  SD  MET A 531       6.824 112.335  -4.600  1.00 49.26           S  
ANISOU 4178  SD  MET A 531     7520   5412   5783  -1787   2568  -2080       S  
ATOM   4179  CE  MET A 531       6.625 112.403  -6.375  1.00 49.20           C  
ANISOU 4179  CE  MET A 531     7509   5366   5819  -1726   2399  -2120       C  
ATOM   4180  N   TYR A 532       9.792 107.895  -2.546  1.00 48.68           N  
ANISOU 4180  N   TYR A 532     8155   4914   5429  -2130   3000  -1608       N  
ATOM   4181  CA  TYR A 532      10.834 107.406  -1.655  1.00 48.19           C  
ANISOU 4181  CA  TYR A 532     8260   4769   5282  -2129   3085  -1471       C  
ATOM   4182  C   TYR A 532      12.009 108.371  -1.679  1.00 46.55           C  
ANISOU 4182  C   TYR A 532     8109   4540   5036  -1943   3012  -1405       C  
ATOM   4183  O   TYR A 532      12.478 108.757  -2.755  1.00 45.65           O  
ANISOU 4183  O   TYR A 532     8019   4384   4943  -1838   2900  -1404       O  
ATOM   4184  CB  TYR A 532      11.277 105.995  -2.056  1.00 48.53           C  
ANISOU 4184  CB  TYR A 532     8480   4654   5305  -2216   3114  -1396       C  
ATOM   4185  CG  TYR A 532      10.160 104.978  -1.972  1.00 50.31           C  
ANISOU 4185  CG  TYR A 532     8660   4880   5574  -2417   3190  -1452       C  
ATOM   4186  CD1 TYR A 532       9.345 104.719  -3.066  1.00 51.00           C  
ANISOU 4186  CD1 TYR A 532     8667   4970   5739  -2471   3121  -1561       C  
ATOM   4187  CD2 TYR A 532       9.916 104.283  -0.796  1.00 51.42           C  
ANISOU 4187  CD2 TYR A 532     8838   5022   5678  -2557   3328  -1394       C  
ATOM   4188  CE1 TYR A 532       8.322 103.793  -2.992  1.00 52.73           C  
ANISOU 4188  CE1 TYR A 532     8838   5189   6009  -2664   3187  -1617       C  
ATOM   4189  CE2 TYR A 532       8.895 103.357  -0.712  1.00 53.19           C  
ANISOU 4189  CE2 TYR A 532     9018   5245   5948  -2755   3401  -1437       C  
ATOM   4190  CZ  TYR A 532       8.102 103.115  -1.813  1.00 53.84           C  
ANISOU 4190  CZ  TYR A 532     9014   5324   6118  -2811   3330  -1552       C  
ATOM   4191  OH  TYR A 532       7.084 102.192  -1.732  1.00 55.71           O  
ANISOU 4191  OH  TYR A 532     9199   5557   6410  -3017   3399  -1599       O  
ATOM   4192  N   ALA A 533      12.478 108.756  -0.495  1.00 46.26           N  
ANISOU 4192  N   ALA A 533     8092   4541   4943  -1909   3076  -1349       N  
ATOM   4193  CA  ALA A 533      13.530 109.753  -0.341  1.00 44.87           C  
ANISOU 4193  CA  ALA A 533     7949   4360   4740  -1743   3012  -1296       C  
ATOM   4194  C   ALA A 533      14.619 109.256   0.597  1.00 44.49           C  
ANISOU 4194  C   ALA A 533     8061   4243   4601  -1732   3086  -1168       C  
ATOM   4195  O   ALA A 533      15.090 109.986   1.473  1.00 44.05           O  
ANISOU 4195  O   ALA A 533     7992   4238   4507  -1656   3097  -1145       O  
ATOM   4196  CB  ALA A 533      12.954 111.075   0.159  1.00 44.93           C  
ANISOU 4196  CB  ALA A 533     7782   4506   4783  -1676   2983  -1392       C  
ATOM   4197  N   ASP A 534      15.041 108.005   0.424  1.00 46.17           N  
ANISOU 4197  N   ASP A 534     8428   4336   4780  -1802   3129  -1087       N  
ATOM   4198  CA  ASP A 534      16.110 107.460   1.250  1.00 45.91           C  
ANISOU 4198  CA  ASP A 534     8557   4226   4662  -1783   3187   -960       C  
ATOM   4199  C   ASP A 534      17.411 108.217   1.006  1.00 44.40           C  
ANISOU 4199  C   ASP A 534     8405   3996   4469  -1603   3076   -898       C  
ATOM   4200  O   ASP A 534      17.682 108.696  -0.098  1.00 43.60           O  
ANISOU 4200  O   ASP A 534     8297   3876   4394  -1526   3003   -926       O  
ATOM   4201  CB  ASP A 534      16.307 105.971   0.958  1.00 46.58           C  
ANISOU 4201  CB  ASP A 534     8795   4169   4735  -1877   3223   -893       C  
ATOM   4202  CG  ASP A 534      15.041 105.165   1.159  1.00 48.22           C  
ANISOU 4202  CG  ASP A 534     8955   4398   4968  -2068   3313   -943       C  
ATOM   4203  OD1 ASP A 534      14.094 105.689   1.784  1.00 48.91           O  
ANISOU 4203  OD1 ASP A 534     8895   4623   5067  -2127   3363  -1013       O  
ATOM   4204  OD2 ASP A 534      14.994 104.004   0.697  1.00 48.92           O1+
ANISOU 4204  OD2 ASP A 534     9148   4366   5073  -2157   3328   -916       O1+
ATOM   4205  N   ASP A 535      18.221 108.324   2.056  1.00 49.72           N  
ANISOU 4205  N   ASP A 535     9109   4664   5118  -1535   3047   -812       N  
ATOM   4206  CA  ASP A 535      19.485 109.046   2.008  1.00 48.54           C  
ANISOU 4206  CA  ASP A 535     8984   4489   4970  -1379   2951   -748       C  
ATOM   4207  C   ASP A 535      20.625 108.106   2.368  1.00 48.34           C  
ANISOU 4207  C   ASP A 535     9104   4352   4912  -1339   2929   -637       C  
ATOM   4208  O   ASP A 535      20.522 107.338   3.330  1.00 49.30           O  
ANISOU 4208  O   ASP A 535     9271   4461   4998  -1395   2973   -601       O  
ATOM   4209  CB  ASP A 535      19.473 110.248   2.959  1.00 48.49           C  
ANISOU 4209  CB  ASP A 535     8862   4596   4966  -1312   2927   -774       C  
ATOM   4210  CG  ASP A 535      18.645 111.402   2.430  1.00 48.42           C  
ANISOU 4210  CG  ASP A 535     8714   4683   5002  -1293   2910   -895       C  
ATOM   4211  OD1 ASP A 535      18.734 111.692   1.217  1.00 47.81           O  
ANISOU 4211  OD1 ASP A 535     8640   4568   4956  -1253   2861   -921       O  
ATOM   4212  OD2 ASP A 535      17.906 112.018   3.226  1.00 48.89           O1+
ANISOU 4212  OD2 ASP A 535     8657   4855   5064  -1311   2941   -970       O1+
ATOM   4213  N   THR A 536      21.706 108.168   1.595  1.00 46.45           N  
ANISOU 4213  N   THR A 536     8930   4038   4680  -1237   2858   -588       N  
ATOM   4214  CA  THR A 536      22.904 107.408   1.918  1.00 46.35           C  
ANISOU 4214  CA  THR A 536     9040   3931   4640  -1169   2826   -500       C  
ATOM   4215  C   THR A 536      23.601 108.026   3.125  1.00 46.53           C  
ANISOU 4215  C   THR A 536     9030   4006   4644  -1088   2791   -454       C  
ATOM   4216  O   THR A 536      23.762 109.248   3.205  1.00 46.14           O  
ANISOU 4216  O   THR A 536     8885   4031   4614  -1024   2749   -471       O  
ATOM   4217  CB  THR A 536      23.848 107.370   0.715  1.00 45.60           C  
ANISOU 4217  CB  THR A 536     9004   3763   4558  -1080   2766   -473       C  
ATOM   4218  OG1 THR A 536      23.288 106.542  -0.313  1.00 46.04           O  
ANISOU 4218  OG1 THR A 536     9122   3758   4612  -1158   2805   -512       O  
ATOM   4219  CG2 THR A 536      25.216 106.825   1.111  1.00 45.19           C  
ANISOU 4219  CG2 THR A 536     9051   3640   4480   -981   2724   -396       C  
ATOM   4220  N   ALA A 537      24.003 107.183   4.073  1.00 48.09           N  
ANISOU 4220  N   ALA A 537     9309   4167   4797  -1090   2807   -400       N  
ATOM   4221  CA  ALA A 537      24.711 107.645   5.262  1.00 47.76           C  
ANISOU 4221  CA  ALA A 537     9251   4175   4722  -1015   2776   -355       C  
ATOM   4222  C   ALA A 537      26.154 107.960   4.889  1.00 46.79           C  
ANISOU 4222  C   ALA A 537     9166   4002   4609   -879   2696   -305       C  
ATOM   4223  O   ALA A 537      26.949 107.050   4.631  1.00 46.96           O  
ANISOU 4223  O   ALA A 537     9296   3932   4614   -837   2681   -262       O  
ATOM   4224  CB  ALA A 537      24.645 106.594   6.365  1.00 49.09           C  
ANISOU 4224  CB  ALA A 537     9498   4326   4829  -1063   2820   -308       C  
ATOM   4225  N   GLY A 538      26.497 109.247   4.864  1.00 43.87           N  
ANISOU 4225  N   GLY A 538     8705   3698   4265   -811   2649   -317       N  
ATOM   4226  CA  GLY A 538      27.837 109.666   4.497  1.00 42.95           C  
ANISOU 4226  CA  GLY A 538     8608   3550   4162   -693   2578   -271       C  
ATOM   4227  C   GLY A 538      28.201 109.271   3.081  1.00 42.50           C  
ANISOU 4227  C   GLY A 538     8596   3416   4134   -671   2557   -265       C  
ATOM   4228  O   GLY A 538      29.005 108.360   2.871  1.00 42.61           O  
ANISOU 4228  O   GLY A 538     8708   3353   4129   -627   2547   -227       O  
ATOM   4229  N   TRP A 539      27.620 109.970   2.103  1.00 38.61           N  
ANISOU 4229  N   TRP A 539     8035   2955   3681   -695   2550   -306       N  
ATOM   4230  CA  TRP A 539      27.734 109.558   0.706  1.00 38.39           C  
ANISOU 4230  CA  TRP A 539     8047   2871   3668   -692   2539   -307       C  
ATOM   4231  C   TRP A 539      29.174 109.632   0.210  1.00 37.75           C  
ANISOU 4231  C   TRP A 539     8000   2756   3588   -581   2482   -250       C  
ATOM   4232  O   TRP A 539      29.664 108.697  -0.433  1.00 37.92           O  
ANISOU 4232  O   TRP A 539     8106   2708   3595   -559   2483   -234       O  
ATOM   4233  CB  TRP A 539      26.820 110.423  -0.162  1.00 38.15           C  
ANISOU 4233  CB  TRP A 539     7927   2900   3669   -732   2539   -363       C  
ATOM   4234  CG  TRP A 539      27.008 110.238  -1.642  1.00 37.89           C  
ANISOU 4234  CG  TRP A 539     7921   2836   3641   -715   2515   -360       C  
ATOM   4235  CD1 TRP A 539      27.922 110.869  -2.437  1.00 37.21           C  
ANISOU 4235  CD1 TRP A 539     7818   2759   3561   -628   2458   -322       C  
ATOM   4236  CD2 TRP A 539      26.253 109.379  -2.506  1.00 38.44           C  
ANISOU 4236  CD2 TRP A 539     8038   2870   3699   -789   2553   -400       C  
ATOM   4237  NE1 TRP A 539      27.789 110.449  -3.738  1.00 37.31           N  
ANISOU 4237  NE1 TRP A 539     7861   2754   3562   -638   2453   -334       N  
ATOM   4238  CE2 TRP A 539      26.771 109.535  -3.807  1.00 38.05           C  
ANISOU 4238  CE2 TRP A 539     7994   2818   3644   -734   2508   -385       C  
ATOM   4239  CE3 TRP A 539      25.192 108.491  -2.306  1.00 39.34           C  
ANISOU 4239  CE3 TRP A 539     8189   2957   3801   -903   2624   -451       C  
ATOM   4240  CZ2 TRP A 539      26.266 108.837  -4.901  1.00 38.50           C  
ANISOU 4240  CZ2 TRP A 539     8092   2852   3683   -779   2523   -423       C  
ATOM   4241  CZ3 TRP A 539      24.692 107.799  -3.393  1.00 39.78           C  
ANISOU 4241  CZ3 TRP A 539     8291   2978   3845   -957   2647   -491       C  
ATOM   4242  CH2 TRP A 539      25.229 107.975  -4.673  1.00 39.34           C  
ANISOU 4242  CH2 TRP A 539     8238   2927   3783   -889   2590   -480       C  
ATOM   4243  N   ASP A 540      29.869 110.737   0.497  1.00 39.24           N  
ANISOU 4243  N   ASP A 540     8124   2996   3791   -510   2437   -227       N  
ATOM   4244  CA  ASP A 540      31.206 110.954  -0.048  1.00 38.65           C  
ANISOU 4244  CA  ASP A 540     8060   2906   3719   -413   2388   -178       C  
ATOM   4245  C   ASP A 540      32.228 109.937   0.442  1.00 39.20           C  
ANISOU 4245  C   ASP A 540     8221   2918   3757   -354   2387   -138       C  
ATOM   4246  O   ASP A 540      33.352 109.921  -0.071  1.00 39.10           O  
ANISOU 4246  O   ASP A 540     8221   2893   3741   -274   2356   -103       O  
ATOM   4247  CB  ASP A 540      31.690 112.367   0.286  1.00 38.14           C  
ANISOU 4247  CB  ASP A 540     7915   2904   3673   -362   2352   -167       C  
ATOM   4248  CG  ASP A 540      30.931 113.439  -0.471  1.00 37.74           C  
ANISOU 4248  CG  ASP A 540     7790   2898   3650   -392   2347   -204       C  
ATOM   4249  OD1 ASP A 540      30.228 113.098  -1.446  1.00 37.85           O  
ANISOU 4249  OD1 ASP A 540     7811   2902   3666   -437   2360   -229       O  
ATOM   4250  OD2 ASP A 540      31.044 114.626  -0.097  1.00 37.43           O1+
ANISOU 4250  OD2 ASP A 540     7694   2902   3626   -367   2330   -215       O1+
ATOM   4251  N   THR A 541      31.875 109.098   1.415  1.00 38.46           N  
ANISOU 4251  N   THR A 541     8188   2793   3632   -390   2423   -142       N  
ATOM   4252  CA  THR A 541      32.765 108.054   1.901  1.00 38.92           C  
ANISOU 4252  CA  THR A 541     8350   2790   3648   -333   2427   -108       C  
ATOM   4253  C   THR A 541      32.462 106.686   1.306  1.00 39.60           C  
ANISOU 4253  C   THR A 541     8547   2788   3711   -367   2468   -126       C  
ATOM   4254  O   THR A 541      33.211 105.737   1.563  1.00 40.09           O  
ANISOU 4254  O   THR A 541     8711   2790   3732   -312   2476   -102       O  
ATOM   4255  CB  THR A 541      32.695 107.971   3.431  1.00 39.42           C  
ANISOU 4255  CB  THR A 541     8428   2877   3674   -342   2440    -92       C  
ATOM   4256  OG1 THR A 541      31.358 107.645   3.830  1.00 40.06           O  
ANISOU 4256  OG1 THR A 541     8508   2966   3746   -453   2492   -127       O  
ATOM   4257  CG2 THR A 541      33.088 109.306   4.051  1.00 38.86           C  
ANISOU 4257  CG2 THR A 541     8262   2888   3615   -301   2402    -81       C  
ATOM   4258  N   ARG A 542      31.390 106.562   0.524  1.00 40.50           N  
ANISOU 4258  N   ARG A 542     8651   2894   3844   -454   2498   -171       N  
ATOM   4259  CA  ARG A 542      31.015 105.299  -0.097  1.00 41.01           C  
ANISOU 4259  CA  ARG A 542     8827   2874   3881   -498   2544   -200       C  
ATOM   4260  C   ARG A 542      31.337 105.247  -1.582  1.00 40.79           C  
ANISOU 4260  C   ARG A 542     8797   2836   3865   -468   2522   -198       C  
ATOM   4261  O   ARG A 542      31.185 104.184  -2.193  1.00 41.74           O  
ANISOU 4261  O   ARG A 542     8988   2917   3953   -490   2544   -209       O  
ATOM   4262  CB  ARG A 542      29.516 105.029   0.100  1.00 41.59           C  
ANISOU 4262  CB  ARG A 542     8893   2953   3956   -633   2602   -249       C  
ATOM   4263  CG  ARG A 542      28.937 105.628   1.374  1.00 41.76           C  
ANISOU 4263  CG  ARG A 542     8839   3047   3982   -680   2611   -244       C  
ATOM   4264  CD  ARG A 542      29.516 104.969   2.614  1.00 42.34           C  
ANISOU 4264  CD  ARG A 542     8982   3098   4005   -645   2616   -197       C  
ATOM   4265  NE  ARG A 542      29.013 103.610   2.780  1.00 43.58           N  
ANISOU 4265  NE  ARG A 542     9248   3188   4121   -718   2672   -201       N  
ATOM   4266  CZ  ARG A 542      29.602 102.679   3.522  1.00 44.36           C  
ANISOU 4266  CZ  ARG A 542     9448   3239   4168   -683   2676   -152       C  
ATOM   4267  NH1 ARG A 542      30.729 102.955   4.164  1.00 43.98           N1+
ANISOU 4267  NH1 ARG A 542     9408   3203   4100   -575   2631   -102       N1+
ATOM   4268  NH2 ARG A 542      29.069 101.469   3.615  1.00 45.74           N  
ANISOU 4268  NH2 ARG A 542     9715   3353   4312   -761   2721   -146       N  
ATOM   4269  N   ILE A 543      31.762 106.361  -2.176  1.00 36.52           N  
ANISOU 4269  N   ILE A 543     8168   2349   3360   -422   2476   -178       N  
ATOM   4270  CA  ILE A 543      32.196 106.386  -3.567  1.00 36.30           C  
ANISOU 4270  CA  ILE A 543     8134   2327   3332   -387   2454   -163       C  
ATOM   4271  C   ILE A 543      33.409 105.478  -3.698  1.00 36.64           C  
ANISOU 4271  C   ILE A 543     8249   2335   3336   -296   2444   -122       C  
ATOM   4272  O   ILE A 543      34.533 105.870  -3.368  1.00 36.28           O  
ANISOU 4272  O   ILE A 543     8187   2305   3293   -205   2415    -84       O  
ATOM   4273  CB  ILE A 543      32.514 107.818  -4.031  1.00 35.45           C  
ANISOU 4273  CB  ILE A 543     7895   2323   3252   -344   2399   -147       C  
ATOM   4274  CG1 ILE A 543      31.280 108.712  -3.896  1.00 35.25           C  
ANISOU 4274  CG1 ILE A 543     7786   2354   3253   -425   2404   -188       C  
ATOM   4275  CG2 ILE A 543      33.006 107.818  -5.470  1.00 35.38           C  
ANISOU 4275  CG2 ILE A 543     7876   2341   3225   -301   2376   -137       C  
ATOM   4276  CD1 ILE A 543      30.168 108.367  -4.861  1.00 35.64           C  
ANISOU 4276  CD1 ILE A 543     7845   2403   3294   -506   2430   -235       C  
ATOM   4277  N   SER A 544      33.186 104.257  -4.171  1.00 38.02           N  
ANISOU 4277  N   SER A 544     8513   2461   3472   -323   2474   -130       N  
ATOM   4278  CA  SER A 544      34.244 103.265  -4.249  1.00 38.56           C  
ANISOU 4278  CA  SER A 544     8670   2487   3493   -241   2475    -91       C  
ATOM   4279  C   SER A 544      35.165 103.546  -5.435  1.00 38.27           C  
ANISOU 4279  C   SER A 544     8626   2466   3448   -163   2458    -63       C  
ATOM   4280  O   SER A 544      34.913 104.423  -6.265  1.00 37.74           O  
ANISOU 4280  O   SER A 544     8471   2462   3406   -176   2434    -83       O  
ATOM   4281  CB  SER A 544      33.647 101.862  -4.357  1.00 39.66           C  
ANISOU 4281  CB  SER A 544     8926   2573   3569   -303   2530   -103       C  
ATOM   4282  OG  SER A 544      32.694 101.796  -5.405  1.00 39.82           O  
ANISOU 4282  OG  SER A 544     8951   2590   3590   -387   2557   -146       O  
ATOM   4283  N   LYS A 545      36.258 102.782  -5.501  1.00 41.70           N  
ANISOU 4283  N   LYS A 545     9140   2868   3838    -72   2464    -26       N  
ATOM   4284  CA  LYS A 545      37.161 102.878  -6.641  1.00 41.63           C  
ANISOU 4284  CA  LYS A 545     9088   2914   3814     17   2435    -32       C  
ATOM   4285  C   LYS A 545      36.505 102.404  -7.930  1.00 42.06           C  
ANISOU 4285  C   LYS A 545     9142   2988   3851    -20   2432    -96       C  
ATOM   4286  O   LYS A 545      36.980 102.752  -9.016  1.00 42.01           O  
ANISOU 4286  O   LYS A 545     9063   3062   3837     36   2399   -121       O  
ATOM   4287  CB  LYS A 545      38.439 102.082  -6.366  1.00 42.08           C  
ANISOU 4287  CB  LYS A 545     9221   2942   3827    132   2436     -1       C  
ATOM   4288  CG  LYS A 545      38.208 100.622  -6.010  1.00 43.49           C  
ANISOU 4288  CG  LYS A 545     9549   3024   3950    121   2471     -5       C  
ATOM   4289  CD  LYS A 545      39.383 100.054  -5.222  1.00 44.28           C  
ANISOU 4289  CD  LYS A 545     9726   3090   4009    232   2469     37       C  
ATOM   4290  CE  LYS A 545      40.701 100.255  -5.955  1.00 44.37           C  
ANISOU 4290  CE  LYS A 545     9667   3166   4027    365   2428     24       C  
ATOM   4291  NZ  LYS A 545      40.753  99.496  -7.235  1.00 45.04           N1+
ANISOU 4291  NZ  LYS A 545     9753   3255   4103    401   2408    -48       N1+
ATOM   4292  N   PHE A 546      35.424 101.626  -7.836  1.00 41.01           N  
ANISOU 4292  N   PHE A 546     9084   2791   3707   -114   2465   -129       N  
ATOM   4293  CA  PHE A 546      34.665 101.259  -9.025  1.00 41.48           C  
ANISOU 4293  CA  PHE A 546     9131   2867   3762   -157   2451   -208       C  
ATOM   4294  C   PHE A 546      33.711 102.373  -9.435  1.00 40.79           C  
ANISOU 4294  C   PHE A 546     8940   2852   3707   -232   2438   -234       C  
ATOM   4295  O   PHE A 546      33.508 102.610 -10.630  1.00 40.86           O  
ANISOU 4295  O   PHE A 546     8895   2926   3705   -222   2405   -285       O  
ATOM   4296  CB  PHE A 546      33.901  99.958  -8.783  1.00 42.55           C  
ANISOU 4296  CB  PHE A 546     9376   2905   3884   -227   2481   -248       C  
ATOM   4297  CG  PHE A 546      34.780  98.805  -8.397  1.00 43.41           C  
ANISOU 4297  CG  PHE A 546     9593   2936   3965   -148   2481   -230       C  
ATOM   4298  CD1 PHE A 546      34.679  98.230  -7.143  1.00 43.84           C  
ANISOU 4298  CD1 PHE A 546     9738   2919   3999   -179   2520   -188       C  
ATOM   4299  CD2 PHE A 546      35.717  98.304  -9.284  1.00 43.92           C  
ANISOU 4299  CD2 PHE A 546     9661   3008   4016    -35   2439   -263       C  
ATOM   4300  CE1 PHE A 546      35.489  97.171  -6.784  1.00 44.75           C  
ANISOU 4300  CE1 PHE A 546     9951   2959   4093    -98   2505   -175       C  
ATOM   4301  CE2 PHE A 546      36.532  97.245  -8.929  1.00 44.82           C  
ANISOU 4301  CE2 PHE A 546     9870   3046   4114     49   2428   -256       C  
ATOM   4302  CZ  PHE A 546      36.417  96.678  -7.679  1.00 45.24           C  
ANISOU 4302  CZ  PHE A 546    10018   3015   4157     18   2456   -208       C  
ATOM   4303  N   ASP A 547      33.110 103.059  -8.458  1.00 40.84           N  
ANISOU 4303  N   ASP A 547     8919   2853   3747   -301   2459   -207       N  
ATOM   4304  CA  ASP A 547      32.323 104.249  -8.770  1.00 40.20           C  
ANISOU 4304  CA  ASP A 547     8727   2847   3699   -351   2437   -233       C  
ATOM   4305  C   ASP A 547      33.164 105.273  -9.519  1.00 39.58           C  
ANISOU 4305  C   ASP A 547     8553   2865   3621   -263   2385   -212       C  
ATOM   4306  O   ASP A 547      32.680 105.925 -10.451  1.00 39.45           O  
ANISOU 4306  O   ASP A 547     8470   2921   3597   -279   2359   -245       O  
ATOM   4307  CB  ASP A 547      31.755 104.863  -7.487  1.00 39.76           C  
ANISOU 4307  CB  ASP A 547     8647   2776   3686   -413   2460   -213       C  
ATOM   4308  CG  ASP A 547      30.586 104.075  -6.923  1.00 40.62           C  
ANISOU 4308  CG  ASP A 547     8826   2818   3788   -532   2523   -247       C  
ATOM   4309  OD1 ASP A 547      30.381 104.111  -5.690  1.00 40.90           O  
ANISOU 4309  OD1 ASP A 547     8873   2825   3842   -564   2548   -234       O  
ATOM   4310  OD2 ASP A 547      29.870 103.424  -7.712  1.00 41.25           O1+
ANISOU 4310  OD2 ASP A 547     8930   2893   3849   -586   2533   -308       O1+
ATOM   4311  N   LEU A 548      34.433 105.419  -9.132  1.00 38.81           N  
ANISOU 4311  N   LEU A 548     8449   2773   3524   -173   2373   -158       N  
ATOM   4312  CA  LEU A 548      35.318 106.358  -9.812  1.00 38.38           C  
ANISOU 4312  CA  LEU A 548     8303   2816   3463    -97   2335   -134       C  
ATOM   4313  C   LEU A 548      35.665 105.880 -11.216  1.00 38.96           C  
ANISOU 4313  C   LEU A 548     8382   2940   3482    -49   2325   -166       C  
ATOM   4314  O   LEU A 548      35.790 106.694 -12.138  1.00 38.80           O  
ANISOU 4314  O   LEU A 548     8286   3015   3442    -31   2301   -165       O  
ATOM   4315  CB  LEU A 548      36.589 106.566  -8.991  1.00 38.10           C  
ANISOU 4315  CB  LEU A 548     8256   2779   3441    -16   2330    -78       C  
ATOM   4316  CG  LEU A 548      36.407 107.144  -7.584  1.00 37.57           C  
ANISOU 4316  CG  LEU A 548     8172   2682   3422    -44   2329    -55       C  
ATOM   4317  CD1 LEU A 548      37.722 107.120  -6.823  1.00 37.52           C  
ANISOU 4317  CD1 LEU A 548     8170   2671   3413     45   2324    -11       C  
ATOM   4318  CD2 LEU A 548      35.851 108.558  -7.653  1.00 36.92           C  
ANISOU 4318  CD2 LEU A 548     7983   2670   3374    -84   2303    -60       C  
ATOM   4319  N   GLU A 549      35.831 104.568 -11.399  1.00 41.33           N  
ANISOU 4319  N   GLU A 549     8774   3179   3752    -27   2342   -197       N  
ATOM   4320  CA  GLU A 549      36.112 104.040 -12.731  1.00 41.89           C  
ANISOU 4320  CA  GLU A 549     8847   3301   3768     24   2328   -248       C  
ATOM   4321  C   GLU A 549      34.961 104.320 -13.689  1.00 41.98           C  
ANISOU 4321  C   GLU A 549     8831   3357   3762    -44   2312   -307       C  
ATOM   4322  O   GLU A 549      35.181 104.611 -14.871  1.00 42.19           O  
ANISOU 4322  O   GLU A 549     8812   3480   3739     -5   2290   -331       O  
ATOM   4323  CB  GLU A 549      36.388 102.538 -12.660  1.00 42.68           C  
ANISOU 4323  CB  GLU A 549     9056   3314   3848     59   2342   -285       C  
ATOM   4324  CG  GLU A 549      37.738 102.166 -12.070  1.00 42.92           C  
ANISOU 4324  CG  GLU A 549     9114   3324   3871    161   2350   -240       C  
ATOM   4325  CD  GLU A 549      37.964 100.666 -12.043  1.00 44.51           C  
ANISOU 4325  CD  GLU A 549     9428   3432   4051    203   2355   -284       C  
ATOM   4326  OE1 GLU A 549      39.127 100.238 -11.870  1.00 44.98           O  
ANISOU 4326  OE1 GLU A 549     9508   3489   4093    310   2353   -270       O  
ATOM   4327  OE2 GLU A 549      36.979  99.912 -12.199  1.00 45.21           O1+
ANISOU 4327  OE2 GLU A 549     9582   3451   4146    131   2358   -338       O1+
ATOM   4328  N   ASN A 550      33.724 104.239 -13.194  1.00 38.61           N  
ANISOU 4328  N   ASN A 550     8430   2871   3369   -147   2325   -334       N  
ATOM   4329  CA  ASN A 550      32.567 104.484 -14.048  1.00 38.84           C  
ANISOU 4329  CA  ASN A 550     8433   2941   3383   -211   2307   -402       C  
ATOM   4330  C   ASN A 550      32.421 105.966 -14.375  1.00 38.14           C  
ANISOU 4330  C   ASN A 550     8249   2950   3291   -213   2284   -368       C  
ATOM   4331  O   ASN A 550      32.003 106.324 -15.483  1.00 38.42           O  
ANISOU 4331  O   ASN A 550     8256   3062   3279   -214   2258   -407       O  
ATOM   4332  CB  ASN A 550      31.302 103.948 -13.378  1.00 39.10           C  
ANISOU 4332  CB  ASN A 550     8512   2889   3456   -324   2333   -447       C  
ATOM   4333  CG  ASN A 550      31.221 102.432 -13.413  1.00 40.12           C  
ANISOU 4333  CG  ASN A 550     8740   2926   3579   -336   2347   -498       C  
ATOM   4334  OD1 ASN A 550      31.648 101.798 -14.377  1.00 40.81           O  
ANISOU 4334  OD1 ASN A 550     8851   3029   3628   -275   2321   -546       O  
ATOM   4335  ND2 ASN A 550      30.670 101.844 -12.357  1.00 40.35           N  
ANISOU 4335  ND2 ASN A 550     8828   2859   3643   -414   2388   -491       N  
ATOM   4336  N   GLU A 551      32.758 106.843 -13.426  1.00 38.89           N  
ANISOU 4336  N   GLU A 551     8301   3044   3431   -211   2289   -299       N  
ATOM   4337  CA  GLU A 551      32.735 108.275 -13.707  1.00 38.33           C  
ANISOU 4337  CA  GLU A 551     8146   3057   3360   -205   2265   -261       C  
ATOM   4338  C   GLU A 551      33.767 108.652 -14.760  1.00 38.51           C  
ANISOU 4338  C   GLU A 551     8131   3176   3325   -124   2245   -224       C  
ATOM   4339  O   GLU A 551      33.553 109.595 -15.532  1.00 38.49           O  
ANISOU 4339  O   GLU A 551     8082   3256   3286   -127   2224   -206       O  
ATOM   4340  CB  GLU A 551      32.979 109.068 -12.425  1.00 37.56           C  
ANISOU 4340  CB  GLU A 551     8011   2933   3327   -212   2270   -205       C  
ATOM   4341  CG  GLU A 551      31.925 108.862 -11.357  1.00 37.44           C  
ANISOU 4341  CG  GLU A 551     8018   2849   3361   -295   2294   -238       C  
ATOM   4342  CD  GLU A 551      32.325 109.471 -10.031  1.00 36.84           C  
ANISOU 4342  CD  GLU A 551     7910   2749   3337   -286   2297   -191       C  
ATOM   4343  OE1 GLU A 551      33.438 110.032  -9.947  1.00 36.49           O  
ANISOU 4343  OE1 GLU A 551     7829   2738   3297   -215   2277   -138       O  
ATOM   4344  OE2 GLU A 551      31.530 109.389  -9.071  1.00 36.80           O1+
ANISOU 4344  OE2 GLU A 551     7913   2703   3365   -350   2321   -214       O1+
ATOM   4345  N   ALA A 552      34.888 107.927 -14.811  1.00 37.25           N  
ANISOU 4345  N   ALA A 552     7991   3014   3147    -52   2255   -210       N  
ATOM   4346  CA  ALA A 552      35.930 108.204 -15.790  1.00 37.58           C  
ANISOU 4346  CA  ALA A 552     7987   3163   3129     23   2247   -180       C  
ATOM   4347  C   ALA A 552      35.512 107.866 -17.215  1.00 38.40           C  
ANISOU 4347  C   ALA A 552     8102   3339   3148     29   2234   -237       C  
ATOM   4348  O   ALA A 552      36.249 108.198 -18.149  1.00 38.80           O  
ANISOU 4348  O   ALA A 552     8107   3503   3133     83   2229   -210       O  
ATOM   4349  CB  ALA A 552      37.205 107.437 -15.432  1.00 37.83           C  
ANISOU 4349  CB  ALA A 552     8036   3177   3161    104   2265   -166       C  
ATOM   4350  N   LEU A 553      34.357 107.225 -17.407  1.00 38.75           N  
ANISOU 4350  N   LEU A 553     8203   3332   3188    -27   2228   -318       N  
ATOM   4351  CA  LEU A 553      33.911 106.862 -18.748  1.00 39.62           C  
ANISOU 4351  CA  LEU A 553     8328   3513   3215    -19   2208   -388       C  
ATOM   4352  C   LEU A 553      33.473 108.064 -19.574  1.00 39.59           C  
ANISOU 4352  C   LEU A 553     8273   3614   3153    -37   2184   -356       C  
ATOM   4353  O   LEU A 553      33.189 107.900 -20.766  1.00 40.38           O  
ANISOU 4353  O   LEU A 553     8382   3797   3165    -22   2164   -405       O  
ATOM   4354  CB  LEU A 553      32.771 105.844 -18.671  1.00 40.11           C  
ANISOU 4354  CB  LEU A 553     8459   3483   3297    -81   2204   -492       C  
ATOM   4355  CG  LEU A 553      33.137 104.485 -18.072  1.00 40.51           C  
ANISOU 4355  CG  LEU A 553     8580   3426   3385    -65   2225   -527       C  
ATOM   4356  CD1 LEU A 553      32.023 103.475 -18.300  1.00 41.29           C  
ANISOU 4356  CD1 LEU A 553     8742   3453   3494   -129   2214   -636       C  
ATOM   4357  CD2 LEU A 553      34.455 103.983 -18.643  1.00 41.07           C  
ANISOU 4357  CD2 LEU A 553     8650   3551   3403     45   2227   -524       C  
ATOM   4358  N   ILE A 554      33.409 109.258 -18.979  1.00 38.79           N  
ANISOU 4358  N   ILE A 554     8128   3515   3096    -66   2184   -277       N  
ATOM   4359  CA  ILE A 554      33.127 110.456 -19.762  1.00 38.88           C  
ANISOU 4359  CA  ILE A 554     8102   3622   3048    -76   2160   -224       C  
ATOM   4360  C   ILE A 554      34.259 110.727 -20.744  1.00 39.43           C  
ANISOU 4360  C   ILE A 554     8127   3818   3035     -9   2158   -160       C  
ATOM   4361  O   ILE A 554      34.046 111.342 -21.796  1.00 39.98           O  
ANISOU 4361  O   ILE A 554     8184   3990   3016     -8   2137   -129       O  
ATOM   4362  CB  ILE A 554      32.879 111.657 -18.828  1.00 38.01           C  
ANISOU 4362  CB  ILE A 554     7957   3473   3011   -117   2159   -153       C  
ATOM   4363  CG1 ILE A 554      32.515 112.911 -19.629  1.00 38.23           C  
ANISOU 4363  CG1 ILE A 554     7965   3583   2976   -131   2131    -87       C  
ATOM   4364  CG2 ILE A 554      34.102 111.922 -17.960  1.00 37.43           C  
ANISOU 4364  CG2 ILE A 554     7839   3380   3004    -81   2174    -77       C  
ATOM   4365  CD1 ILE A 554      31.355 112.720 -20.578  1.00 38.92           C  
ANISOU 4365  CD1 ILE A 554     8102   3708   2979   -157   2108   -165       C  
ATOM   4366  N   THR A 555      35.469 110.253 -20.437  1.00 39.42           N  
ANISOU 4366  N   THR A 555     8102   3820   3055     47   2182   -139       N  
ATOM   4367  CA  THR A 555      36.626 110.495 -21.290  1.00 40.03           C  
ANISOU 4367  CA  THR A 555     8121   4030   3058    108   2191    -82       C  
ATOM   4368  C   THR A 555      36.561 109.740 -22.612  1.00 41.19           C  
ANISOU 4368  C   THR A 555     8289   4273   3087    147   2186   -154       C  
ATOM   4369  O   THR A 555      37.414 109.972 -23.475  1.00 41.90           O  
ANISOU 4369  O   THR A 555     8325   4499   3095    192   2195   -111       O  
ATOM   4370  CB  THR A 555      37.911 110.126 -20.546  1.00 39.80           C  
ANISOU 4370  CB  THR A 555     8061   3980   3081    161   2220    -58       C  
ATOM   4371  OG1 THR A 555      37.947 108.713 -20.316  1.00 40.11           O  
ANISOU 4371  OG1 THR A 555     8165   3946   3129    197   2233   -155       O  
ATOM   4372  CG2 THR A 555      37.973 110.853 -19.209  1.00 38.74           C  
ANISOU 4372  CG2 THR A 555     7907   3755   3057    126   2220      1       C  
ATOM   4373  N   ASN A 556      35.585 108.847 -22.793  1.00 41.51           N  
ANISOU 4373  N   ASN A 556     8400   4254   3116    129   2171   -267       N  
ATOM   4374  CA  ASN A 556      35.405 108.214 -24.096  1.00 42.70           C  
ANISOU 4374  CA  ASN A 556     8572   4502   3151    164   2155   -348       C  
ATOM   4375  C   ASN A 556      34.882 109.212 -25.123  1.00 43.15           C  
ANISOU 4375  C   ASN A 556     8609   4679   3106    142   2127   -299       C  
ATOM   4376  O   ASN A 556      35.280 109.173 -26.293  1.00 44.19           O  
ANISOU 4376  O   ASN A 556     8718   4955   3117    187   2122   -301       O  
ATOM   4377  CB  ASN A 556      34.460 107.018 -23.981  1.00 43.01           C  
ANISOU 4377  CB  ASN A 556     8690   4436   3217    141   2140   -486       C  
ATOM   4378  CG  ASN A 556      35.140 105.785 -23.413  1.00 43.18           C  
ANISOU 4378  CG  ASN A 556     8743   4370   3292    188   2162   -541       C  
ATOM   4379  OD1 ASN A 556      36.352 105.614 -23.546  1.00 43.47           O  
ANISOU 4379  OD1 ASN A 556     8744   4468   3303    262   2185   -512       O  
ATOM   4380  ND2 ASN A 556      34.358 104.915 -22.782  1.00 43.12           N  
ANISOU 4380  ND2 ASN A 556     8804   4222   3356    142   2156   -619       N  
ATOM   4381  N   GLN A 557      33.995 110.115 -24.704  1.00 42.48           N  
ANISOU 4381  N   GLN A 557     8537   4543   3062     75   2107   -254       N  
ATOM   4382  CA  GLN A 557      33.415 111.121 -25.586  1.00 42.93           C  
ANISOU 4382  CA  GLN A 557     8593   4695   3024     52   2073   -196       C  
ATOM   4383  C   GLN A 557      34.290 112.358 -25.737  1.00 42.86           C  
ANISOU 4383  C   GLN A 557     8516   4770   3000     57   2079    -32       C  
ATOM   4384  O   GLN A 557      33.774 113.422 -26.098  1.00 42.99           O  
ANISOU 4384  O   GLN A 557     8539   4821   2976     23   2047     52       O  
ATOM   4385  CB  GLN A 557      32.034 111.537 -25.074  1.00 42.41           C  
ANISOU 4385  CB  GLN A 557     8575   4533   3004    -18   2047   -230       C  
ATOM   4386  CG  GLN A 557      31.061 110.392 -24.902  1.00 42.58           C  
ANISOU 4386  CG  GLN A 557     8654   4471   3054    -44   2038   -393       C  
ATOM   4387  CD  GLN A 557      29.781 110.824 -24.218  1.00 42.04           C  
ANISOU 4387  CD  GLN A 557     8602   4311   3059   -119   2015   -429       C  
ATOM   4388  OE1 GLN A 557      29.278 111.924 -24.450  1.00 42.02           O  
ANISOU 4388  OE1 GLN A 557     8540   4348   3076   -139   1946   -358       O  
ATOM   4389  NE2 GLN A 557      29.253 109.962 -23.359  1.00 41.71           N  
ANISOU 4389  NE2 GLN A 557     8589   4149   3108   -161   2038   -530       N  
ATOM   4390  N   MET A 558      35.587 112.255 -25.474  1.00 42.77           N  
ANISOU 4390  N   MET A 558     8442   4790   3020     96   2115     18       N  
ATOM   4391  CA  MET A 558      36.480 113.400 -25.520  1.00 42.76           C  
ANISOU 4391  CA  MET A 558     8364   4860   3024     88   2122    170       C  
ATOM   4392  C   MET A 558      37.428 113.297 -26.705  1.00 44.01           C  
ANISOU 4392  C   MET A 558     8466   5198   3057    135   2140    205       C  
ATOM   4393  O   MET A 558      37.808 112.201 -27.128  1.00 44.63           O  
ANISOU 4393  O   MET A 558     8550   5328   3080    192   2162    105       O  
ATOM   4394  CB  MET A 558      37.302 113.517 -24.232  1.00 41.78           C  
ANISOU 4394  CB  MET A 558     8195   4645   3034     89   2150    204       C  
ATOM   4395  CG  MET A 558      36.501 113.862 -22.993  1.00 40.62           C  
ANISOU 4395  CG  MET A 558     8083   4341   3009     39   2135    194       C  
ATOM   4396  SD  MET A 558      37.573 114.162 -21.574  1.00 39.67           S  
ANISOU 4396  SD  MET A 558     7904   4144   3024     45   2160    246       S  
ATOM   4397  CE  MET A 558      36.368 114.451 -20.282  1.00 38.56           C  
ANISOU 4397  CE  MET A 558     7815   3841   2996    -13   2142    209       C  
ATOM   4398  N   GLU A 559      37.794 114.461 -27.240  1.00 44.49           N  
ANISOU 4398  N   GLU A 559     8474   5356   3073    107   2129    350       N  
ATOM   4399  CA  GLU A 559      38.956 114.558 -28.108  1.00 45.61           C  
ANISOU 4399  CA  GLU A 559     8536   5673   3120    136   2160    414       C  
ATOM   4400  C   GLU A 559      40.145 113.904 -27.418  1.00 45.29           C  
ANISOU 4400  C   GLU A 559     8441   5621   3146    180   2213    374       C  
ATOM   4401  O   GLU A 559      40.292 113.993 -26.196  1.00 44.15           O  
ANISOU 4401  O   GLU A 559     8297   5343   3136    167   2219    375       O  
ATOM   4402  CB  GLU A 559      39.252 116.028 -28.418  1.00 45.98           C  
ANISOU 4402  CB  GLU A 559     8528   5785   3159     77   2141    600       C  
ATOM   4403  CG  GLU A 559      39.482 116.336 -29.886  1.00 47.61           C  
ANISOU 4403  CG  GLU A 559     8705   6189   3197     78   2138    674       C  
ATOM   4404  CD  GLU A 559      39.201 117.790 -30.221  1.00 48.01           C  
ANISOU 4404  CD  GLU A 559     8748   6255   3241      9   2090    855       C  
ATOM   4405  OE1 GLU A 559      38.820 118.550 -29.305  1.00 47.00           O  
ANISOU 4405  OE1 GLU A 559     8637   5977   3245    -36   2058    912       O  
ATOM   4406  OE2 GLU A 559      39.354 118.173 -31.401  1.00 49.44           O1+
ANISOU 4406  OE2 GLU A 559     8907   6596   3283     -2   2081    941       O1+
ATOM   4407  N   GLU A 560      40.984 113.225 -28.206  1.00 46.40           N  
ANISOU 4407  N   GLU A 560     8539   5907   3184    237   2252    331       N  
ATOM   4408  CA  GLU A 560      42.016 112.365 -27.629  1.00 46.28           C  
ANISOU 4408  CA  GLU A 560     8491   5878   3215    298   2299    261       C  
ATOM   4409  C   GLU A 560      42.874 113.112 -26.614  1.00 45.51           C  
ANISOU 4409  C   GLU A 560     8329   5731   3231    271   2320    361       C  
ATOM   4410  O   GLU A 560      43.142 112.607 -25.518  1.00 44.64           O  
ANISOU 4410  O   GLU A 560     8237   5498   3225    298   2331    308       O  
ATOM   4411  CB  GLU A 560      42.894 111.772 -28.729  1.00 47.82           C  
ANISOU 4411  CB  GLU A 560     8630   6269   3270    360   2340    219       C  
ATOM   4412  CG  GLU A 560      44.206 111.215 -28.202  1.00 47.92           C  
ANISOU 4412  CG  GLU A 560     8584   6302   3320    420   2395    186       C  
ATOM   4413  CD  GLU A 560      44.669 109.988 -28.952  1.00 49.16           C  
ANISOU 4413  CD  GLU A 560     8739   6566   3374    511   2423     50       C  
ATOM   4414  OE1 GLU A 560      44.596 108.882 -28.377  1.00 48.82           O  
ANISOU 4414  OE1 GLU A 560     8756   6404   3389    571   2419    -73       O  
ATOM   4415  OE2 GLU A 560      45.100 110.127 -30.117  1.00 50.59           O1+
ANISOU 4415  OE2 GLU A 560     8858   6949   3414    520   2448     66       O1+
ATOM   4416  N   GLY A 561      43.307 114.325 -26.960  1.00 45.92           N  
ANISOU 4416  N   GLY A 561     8308   5874   3264    215   2321    508       N  
ATOM   4417  CA  GLY A 561      44.119 115.094 -26.031  1.00 45.32           C  
ANISOU 4417  CA  GLY A 561     8168   5753   3297    182   2336    601       C  
ATOM   4418  C   GLY A 561      43.367 115.480 -24.771  1.00 43.82           C  
ANISOU 4418  C   GLY A 561     8032   5363   3254    146   2295    601       C  
ATOM   4419  O   GLY A 561      43.935 115.489 -23.676  1.00 43.07           O  
ANISOU 4419  O   GLY A 561     7917   5186   3261    154   2310    598       O  
ATOM   4420  N   HIS A 562      42.082 115.816 -24.910  1.00 43.47           N  
ANISOU 4420  N   HIS A 562     8056   5246   3213    107   2245    602       N  
ATOM   4421  CA  HIS A 562      41.265 116.118 -23.738  1.00 42.16           C  
ANISOU 4421  CA  HIS A 562     7943   4900   3175     74   2211    585       C  
ATOM   4422  C   HIS A 562      41.116 114.892 -22.846  1.00 41.40           C  
ANISOU 4422  C   HIS A 562     7903   4692   3135    123   2228    447       C  
ATOM   4423  O   HIS A 562      41.108 115.007 -21.614  1.00 40.42           O  
ANISOU 4423  O   HIS A 562     7787   4446   3124    112   2225    438       O  
ATOM   4424  CB  HIS A 562      39.894 116.639 -24.171  1.00 42.14           C  
ANISOU 4424  CB  HIS A 562     8007   4860   3147     29   2159    601       C  
ATOM   4425  CG  HIS A 562      39.058 117.156 -23.041  1.00 41.00           C  
ANISOU 4425  CG  HIS A 562     7902   4551   3124    -13   2127    597       C  
ATOM   4426  ND1 HIS A 562      37.728 117.485 -23.190  1.00 40.86           N  
ANISOU 4426  ND1 HIS A 562     7955   4474   3096    -47   2086    586       N  
ATOM   4427  CD2 HIS A 562      39.364 117.407 -21.746  1.00 40.05           C  
ANISOU 4427  CD2 HIS A 562     7762   4324   3130    -23   2131    599       C  
ATOM   4428  CE1 HIS A 562      37.250 117.913 -22.036  1.00 39.88           C  
ANISOU 4428  CE1 HIS A 562     7849   4216   3089    -77   2071    579       C  
ATOM   4429  NE2 HIS A 562      38.222 117.876 -21.143  1.00 39.37           N  
ANISOU 4429  NE2 HIS A 562     7729   4122   3108    -63   2096    586       N  
ATOM   4430  N   ARG A 563      40.989 113.708 -23.452  1.00 41.96           N  
ANISOU 4430  N   ARG A 563     8015   4802   3126    175   2244    341       N  
ATOM   4431  CA  ARG A 563      40.961 112.476 -22.672  1.00 41.49           C  
ANISOU 4431  CA  ARG A 563     8011   4634   3118    221   2259    223       C  
ATOM   4432  C   ARG A 563      42.251 112.289 -21.885  1.00 41.30           C  
ANISOU 4432  C   ARG A 563     7937   4605   3150    265   2294    239       C  
ATOM   4433  O   ARG A 563      42.226 111.765 -20.767  1.00 40.56           O  
ANISOU 4433  O   ARG A 563     7885   4383   3141    280   2296    192       O  
ATOM   4434  CB  ARG A 563      40.710 111.280 -23.595  1.00 42.39           C  
ANISOU 4434  CB  ARG A 563     8173   4800   3134    271   2265    110       C  
ATOM   4435  CG  ARG A 563      40.946 109.915 -22.959  1.00 42.29           C  
ANISOU 4435  CG  ARG A 563     8213   4691   3162    329   2282     -1       C  
ATOM   4436  CD  ARG A 563      40.387 108.780 -23.815  1.00 43.16           C  
ANISOU 4436  CD  ARG A 563     8387   4820   3193    363   2273   -124       C  
ATOM   4437  NE  ARG A 563      40.830 108.841 -25.206  1.00 44.44           N  
ANISOU 4437  NE  ARG A 563     8497   5170   3216    399   2283   -124       N  
ATOM   4438  CZ  ARG A 563      40.071 109.260 -26.215  1.00 44.99           C  
ANISOU 4438  CZ  ARG A 563     8575   5324   3195    368   2257   -116       C  
ATOM   4439  NH1 ARG A 563      40.556 109.282 -27.449  1.00 46.27           N1+
ANISOU 4439  NH1 ARG A 563     8689   5671   3222    404   2269   -113       N1+
ATOM   4440  NH2 ARG A 563      38.826 109.656 -25.991  1.00 44.36           N  
ANISOU 4440  NH2 ARG A 563     8552   5154   3150    302   2219   -114       N  
ATOM   4441  N   THR A 564      43.381 112.730 -22.439  1.00 42.05           N  
ANISOU 4441  N   THR A 564     7944   4843   3192    282   2324    309       N  
ATOM   4442  CA  THR A 564      44.656 112.574 -21.747  1.00 42.03           C  
ANISOU 4442  CA  THR A 564     7888   4850   3230    327   2363    321       C  
ATOM   4443  C   THR A 564      44.711 113.433 -20.488  1.00 40.96           C  
ANISOU 4443  C   THR A 564     7739   4608   3218    282   2347    387       C  
ATOM   4444  O   THR A 564      45.136 112.967 -19.424  1.00 40.44           O  
ANISOU 4444  O   THR A 564     7692   4455   3218    320   2358    350       O  
ATOM   4445  CB  THR A 564      45.810 112.925 -22.687  1.00 43.24           C  
ANISOU 4445  CB  THR A 564     7939   5198   3291    343   2405    383       C  
ATOM   4446  OG1 THR A 564      45.863 111.972 -23.757  1.00 44.32           O  
ANISOU 4446  OG1 THR A 564     8088   5441   3311    402   2424    298       O  
ATOM   4447  CG2 THR A 564      47.127 112.906 -21.937  1.00 43.25           C  
ANISOU 4447  CG2 THR A 564     7878   5218   3338    383   2448    402       C  
ATOM   4448  N   LEU A 565      44.285 114.694 -20.591  1.00 40.74           N  
ANISOU 4448  N   LEU A 565     7680   4583   3217    205   2317    484       N  
ATOM   4449  CA  LEU A 565      44.324 115.586 -19.436  1.00 39.87           C  
ANISOU 4449  CA  LEU A 565     7552   4375   3221    162   2298    541       C  
ATOM   4450  C   LEU A 565      43.368 115.123 -18.346  1.00 38.80           C  
ANISOU 4450  C   LEU A 565     7502   4075   3164    161   2272    460       C  
ATOM   4451  O   LEU A 565      43.710 115.155 -17.158  1.00 38.16           O  
ANISOU 4451  O   LEU A 565     7422   3913   3162    171   2275    452       O  
ATOM   4452  CB  LEU A 565      43.991 117.015 -19.865  1.00 40.04           C  
ANISOU 4452  CB  LEU A 565     7532   4425   3255     80   2264    662       C  
ATOM   4453  CG  LEU A 565      44.881 117.623 -20.949  1.00 41.24           C  
ANISOU 4453  CG  LEU A 565     7597   4742   3331     58   2287    768       C  
ATOM   4454  CD1 LEU A 565      44.424 119.033 -21.292  1.00 41.46           C  
ANISOU 4454  CD1 LEU A 565     7601   4765   3385    -28   2239    898       C  
ATOM   4455  CD2 LEU A 565      46.337 117.617 -20.511  1.00 41.55           C  
ANISOU 4455  CD2 LEU A 565     7557   4840   3391     83   2338    796       C  
ATOM   4456  N   ALA A 566      42.163 114.694 -18.730  1.00 38.69           N  
ANISOU 4456  N   ALA A 566     7560   4018   3123    146   2250    399       N  
ATOM   4457  CA  ALA A 566      41.196 114.228 -17.743  1.00 37.84           C  
ANISOU 4457  CA  ALA A 566     7529   3766   3083    133   2233    324       C  
ATOM   4458  C   ALA A 566      41.707 112.994 -17.011  1.00 37.72           C  
ANISOU 4458  C   ALA A 566     7555   3690   3087    194   2259    248       C  
ATOM   4459  O   ALA A 566      41.545 112.877 -15.791  1.00 37.02           O  
ANISOU 4459  O   ALA A 566     7497   3495   3074    188   2254    228       O  
ATOM   4460  CB  ALA A 566      39.856 113.937 -18.417  1.00 37.97           C  
ANISOU 4460  CB  ALA A 566     7610   3763   3054    101   2212    271       C  
ATOM   4461  N   LEU A 567      42.335 112.065 -17.735  1.00 38.51           N  
ANISOU 4461  N   LEU A 567     7659   3859   3113    256   2286    208       N  
ATOM   4462  CA  LEU A 567      42.837 110.856 -17.093  1.00 38.57           C  
ANISOU 4462  CA  LEU A 567     7718   3802   3136    322   2306    142       C  
ATOM   4463  C   LEU A 567      44.005 111.155 -16.162  1.00 38.35           C  
ANISOU 4463  C   LEU A 567     7643   3773   3154    358   2325    187       C  
ATOM   4464  O   LEU A 567      44.183 110.460 -15.157  1.00 38.07           O  
ANISOU 4464  O   LEU A 567     7662   3642   3160    393   2330    153       O  
ATOM   4465  CB  LEU A 567      43.239 109.822 -18.145  1.00 39.63           C  
ANISOU 4465  CB  LEU A 567     7865   4015   3176    387   2328     80       C  
ATOM   4466  CG  LEU A 567      42.079 109.217 -18.940  1.00 39.96           C  
ANISOU 4466  CG  LEU A 567     7974   4038   3171    363   2309      8       C  
ATOM   4467  CD1 LEU A 567      42.517 107.973 -19.699  1.00 41.03           C  
ANISOU 4467  CD1 LEU A 567     8139   4220   3230    442   2326    -78       C  
ATOM   4468  CD2 LEU A 567      40.897 108.914 -18.031  1.00 39.19           C  
ANISOU 4468  CD2 LEU A 567     7961   3782   3149    307   2287    -29       C  
ATOM   4469  N   ALA A 568      44.806 112.176 -16.471  1.00 38.57           N  
ANISOU 4469  N   ALA A 568     7575   3908   3172    347   2337    269       N  
ATOM   4470  CA  ALA A 568      45.857 112.582 -15.544  1.00 38.38           C  
ANISOU 4470  CA  ALA A 568     7503   3883   3195    371   2355    312       C  
ATOM   4471  C   ALA A 568      45.264 113.182 -14.275  1.00 37.37           C  
ANISOU 4471  C   ALA A 568     7402   3634   3161    323   2324    327       C  
ATOM   4472  O   ALA A 568      45.742 112.907 -13.168  1.00 37.07           O  
ANISOU 4472  O   ALA A 568     7386   3535   3164    359   2331    314       O  
ATOM   4473  CB  ALA A 568      46.802 113.573 -16.223  1.00 39.00           C  
ANISOU 4473  CB  ALA A 568     7470   4105   3243    353   2379    403       C  
ATOM   4474  N   VAL A 569      44.217 113.998 -14.417  1.00 36.93           N  
ANISOU 4474  N   VAL A 569     7347   3550   3134    246   2290    351       N  
ATOM   4475  CA  VAL A 569      43.529 114.560 -13.261  1.00 36.08           C  
ANISOU 4475  CA  VAL A 569     7263   3336   3108    202   2261    349       C  
ATOM   4476  C   VAL A 569      42.733 113.494 -12.511  1.00 35.68           C  
ANISOU 4476  C   VAL A 569     7308   3173   3076    214   2256    265       C  
ATOM   4477  O   VAL A 569      42.497 113.631 -11.307  1.00 35.12           O  
ANISOU 4477  O   VAL A 569     7261   3022   3062    202   2246    252       O  
ATOM   4478  CB  VAL A 569      42.647 115.742 -13.723  1.00 35.91           C  
ANISOU 4478  CB  VAL A 569     7216   3323   3106    125   2227    398       C  
ATOM   4479  CG1 VAL A 569      41.537 116.054 -12.726  1.00 35.15           C  
ANISOU 4479  CG1 VAL A 569     7163   3116   3076     82   2200    362       C  
ATOM   4480  CG2 VAL A 569      43.504 116.981 -13.954  1.00 36.23           C  
ANISOU 4480  CG2 VAL A 569     7167   3435   3164     98   2226    504       C  
ATOM   4481  N   ILE A 570      42.341 112.412 -13.176  1.00 36.07           N  
ANISOU 4481  N   ILE A 570     7415   3215   3076    233   2266    208       N  
ATOM   4482  CA  ILE A 570      41.591 111.347 -12.512  1.00 35.88           C  
ANISOU 4482  CA  ILE A 570     7486   3077   3070    231   2265    141       C  
ATOM   4483  C   ILE A 570      42.520 110.302 -11.904  1.00 36.19           C  
ANISOU 4483  C   ILE A 570     7570   3080   3102    308   2287    122       C  
ATOM   4484  O   ILE A 570      42.369 109.926 -10.739  1.00 35.88           O  
ANISOU 4484  O   ILE A 570     7585   2947   3101    309   2286    111       O  
ATOM   4485  CB  ILE A 570      40.589 110.712 -13.501  1.00 36.25           C  
ANISOU 4485  CB  ILE A 570     7582   3120   3072    202   2262     88       C  
ATOM   4486  CG1 ILE A 570      39.448 111.687 -13.799  1.00 35.90           C  
ANISOU 4486  CG1 ILE A 570     7516   3083   3041    124   2238     99       C  
ATOM   4487  CG2 ILE A 570      40.036 109.408 -12.949  1.00 36.36           C  
ANISOU 4487  CG2 ILE A 570     7699   3022   3095    202   2272     25       C  
ATOM   4488  CD1 ILE A 570      38.609 111.298 -14.997  1.00 36.41           C  
ANISOU 4488  CD1 ILE A 570     7612   3180   3042    101   2234     56       C  
ATOM   4489  N   LYS A 571      43.500 109.823 -12.676  1.00 36.92           N  
ANISOU 4489  N   LYS A 571     7641   3250   3136    378   2310    120       N  
ATOM   4490  CA  LYS A 571      44.387 108.770 -12.185  1.00 37.38           C  
ANISOU 4490  CA  LYS A 571     7750   3275   3179    465   2331     96       C  
ATOM   4491  C   LYS A 571      45.269 109.248 -11.037  1.00 37.07           C  
ANISOU 4491  C   LYS A 571     7682   3228   3176    498   2335    139       C  
ATOM   4492  O   LYS A 571      45.602 108.458 -10.146  1.00 37.21           O  
ANISOU 4492  O   LYS A 571     7770   3169   3198    550   2340    125       O  
ATOM   4493  CB  LYS A 571      45.253 108.237 -13.331  1.00 38.36           C  
ANISOU 4493  CB  LYS A 571     7842   3505   3227    540   2355     73       C  
ATOM   4494  CG  LYS A 571      46.236 107.146 -12.939  1.00 39.03           C  
ANISOU 4494  CG  LYS A 571     7974   3566   3289    647   2375     39       C  
ATOM   4495  CD  LYS A 571      46.957 106.590 -14.158  1.00 40.12           C  
ANISOU 4495  CD  LYS A 571     8075   3818   3349    722   2398     -6       C  
ATOM   4496  CE  LYS A 571      47.873 105.437 -13.781  1.00 40.91           C  
ANISOU 4496  CE  LYS A 571     8228   3887   3431    841   2411    -55       C  
ATOM   4497  NZ  LYS A 571      48.418 104.749 -14.984  1.00 42.11           N1+
ANISOU 4497  NZ  LYS A 571     8350   4141   3507    918   2428   -124       N1+
ATOM   4498  N   TYR A 572      45.645 110.527 -11.027  1.00 36.76           N  
ANISOU 4498  N   TYR A 572     7547   3263   3159    467   2332    195       N  
ATOM   4499  CA  TYR A 572      46.605 111.040 -10.058  1.00 36.63           C  
ANISOU 4499  CA  TYR A 572     7493   3258   3168    500   2341    233       C  
ATOM   4500  C   TYR A 572      45.969 111.834  -8.924  1.00 35.82           C  
ANISOU 4500  C   TYR A 572     7397   3084   3130    440   2313    250       C  
ATOM   4501  O   TYR A 572      46.662 112.143  -7.949  1.00 35.73           O  
ANISOU 4501  O   TYR A 572     7374   3066   3137    470   2316    271       O  
ATOM   4502  CB  TYR A 572      47.643 111.930 -10.756  1.00 37.07           C  
ANISOU 4502  CB  TYR A 572     7432   3450   3201    507   2367    289       C  
ATOM   4503  CG  TYR A 572      48.345 111.278 -11.926  1.00 38.01           C  
ANISOU 4503  CG  TYR A 572     7523   3673   3247    568   2401    270       C  
ATOM   4504  CD1 TYR A 572      48.543 109.905 -11.965  1.00 38.53           C  
ANISOU 4504  CD1 TYR A 572     7663   3703   3275    652   2411    203       C  
ATOM   4505  CD2 TYR A 572      48.811 112.037 -12.992  1.00 38.52           C  
ANISOU 4505  CD2 TYR A 572     7486   3874   3275    541   2423    320       C  
ATOM   4506  CE1 TYR A 572      49.182 109.306 -13.030  1.00 39.51           C  
ANISOU 4506  CE1 TYR A 572     7756   3928   3328    715   2441    170       C  
ATOM   4507  CE2 TYR A 572      49.453 111.447 -14.063  1.00 39.51           C  
ANISOU 4507  CE2 TYR A 572     7577   4113   3322    597   2458    295       C  
ATOM   4508  CZ  TYR A 572      49.635 110.081 -14.076  1.00 39.99           C  
ANISOU 4508  CZ  TYR A 572     7708   4140   3347    689   2466    212       C  
ATOM   4509  OH  TYR A 572      50.272 109.482 -15.137  1.00 41.08           O  
ANISOU 4509  OH  TYR A 572     7808   4397   3405    753   2499    172       O  
ATOM   4510  N   THR A 573      44.684 112.171  -9.020  1.00 35.33           N  
ANISOU 4510  N   THR A 573     7351   2975   3097    361   2287    235       N  
ATOM   4511  CA  THR A 573      44.087 113.100  -8.068  1.00 34.67           C  
ANISOU 4511  CA  THR A 573     7255   2848   3071    304   2262    246       C  
ATOM   4512  C   THR A 573      42.793 112.555  -7.470  1.00 34.33           C  
ANISOU 4512  C   THR A 573     7288   2706   3048    261   2248    194       C  
ATOM   4513  O   THR A 573      42.517 112.766  -6.283  1.00 33.99           O  
ANISOU 4513  O   THR A 573     7265   2613   3036    247   2238    185       O  
ATOM   4514  CB  THR A 573      43.856 114.452  -8.754  1.00 34.53           C  
ANISOU 4514  CB  THR A 573     7156   2891   3074    242   2249    293       C  
ATOM   4515  OG1 THR A 573      45.092 115.174  -8.833  1.00 34.84           O  
ANISOU 4515  OG1 THR A 573     7120   3005   3113    264   2265    357       O  
ATOM   4516  CG2 THR A 573      42.826 115.282  -8.019  1.00 33.95           C  
ANISOU 4516  CG2 THR A 573     7086   2759   3053    178   2221    283       C  
ATOM   4517  N   TYR A 574      41.999 111.843  -8.270  1.00 36.70           N  
ANISOU 4517  N   TYR A 574     7632   2987   3326    238   2251    159       N  
ATOM   4518  CA  TYR A 574      40.744 111.271  -7.793  1.00 36.31           C  
ANISOU 4518  CA  TYR A 574     7653   2849   3293    184   2248    113       C  
ATOM   4519  C   TYR A 574      40.883 109.825  -7.342  1.00 36.79           C  
ANISOU 4519  C   TYR A 574     7817   2832   3331    221   2268     92       C  
ATOM   4520  O   TYR A 574      40.316 109.444  -6.313  1.00 36.99           O  
ANISOU 4520  O   TYR A 574     7899   2781   3374    192   2271     78       O  
ATOM   4521  CB  TYR A 574      39.667 111.356  -8.881  1.00 36.23           C  
ANISOU 4521  CB  TYR A 574     7640   2854   3270    125   2243     87       C  
ATOM   4522  CG  TYR A 574      39.243 112.765  -9.232  1.00 35.87           C  
ANISOU 4522  CG  TYR A 574     7519   2863   3245     79   2222    112       C  
ATOM   4523  CD1 TYR A 574      39.691 113.854  -8.495  1.00 35.55           C  
ANISOU 4523  CD1 TYR A 574     7424   2840   3244     80   2210    149       C  
ATOM   4524  CD2 TYR A 574      38.385 113.005 -10.296  1.00 36.02           C  
ANISOU 4524  CD2 TYR A 574     7533   2912   3241     36   2215    100       C  
ATOM   4525  CE1 TYR A 574      39.307 115.142  -8.816  1.00 35.55           C  
ANISOU 4525  CE1 TYR A 574     7369   2873   3264     37   2192    181       C  
ATOM   4526  CE2 TYR A 574      37.993 114.287 -10.620  1.00 35.89           C  
ANISOU 4526  CE2 TYR A 574     7463   2935   3238     -3   2196    134       C  
ATOM   4527  CZ  TYR A 574      38.456 115.352  -9.878  1.00 35.83           C  
ANISOU 4527  CZ  TYR A 574     7405   2931   3276     -3   2184    178       C  
ATOM   4528  OH  TYR A 574      38.063 116.630 -10.202  1.00 35.63           O  
ANISOU 4528  OH  TYR A 574     7339   2927   3270    -44   2163    223       O  
ATOM   4529  N   GLN A 575      41.623 109.009  -8.088  1.00 36.88           N  
ANISOU 4529  N   GLN A 575     7854   2861   3296    284   2284     90       N  
ATOM   4530  CA  GLN A 575      41.850 107.618  -7.725  1.00 37.49           C  
ANISOU 4530  CA  GLN A 575     8042   2857   3344    328   2305     75       C  
ATOM   4531  C   GLN A 575      43.056 107.436  -6.813  1.00 37.91           C  
ANISOU 4531  C   GLN A 575     8112   2905   3387    415   2310    107       C  
ATOM   4532  O   GLN A 575      43.221 106.356  -6.233  1.00 38.39           O  
ANISOU 4532  O   GLN A 575     8281   2884   3423    454   2324    105       O  
ATOM   4533  CB  GLN A 575      42.008 106.774  -8.993  1.00 38.17           C  
ANISOU 4533  CB  GLN A 575     8156   2967   3379    363   2318     44       C  
ATOM   4534  CG  GLN A 575      40.804 106.870  -9.921  1.00 38.12           C  
ANISOU 4534  CG  GLN A 575     8144   2969   3370    283   2312      7       C  
ATOM   4535  CD  GLN A 575      41.034 106.202 -11.261  1.00 39.03           C  
ANISOU 4535  CD  GLN A 575     8267   3135   3426    324   2318    -33       C  
ATOM   4536  OE1 GLN A 575      42.173 106.001 -11.682  1.00 39.38           O  
ANISOU 4536  OE1 GLN A 575     8284   3245   3435    412   2327    -29       O  
ATOM   4537  NE2 GLN A 575      39.947 105.853 -11.941  1.00 39.48           N  
ANISOU 4537  NE2 GLN A 575     8359   3173   3470    263   2316    -79       N  
ATOM   4538  N   ASN A 576      43.898 108.458  -6.679  1.00 37.83           N  
ANISOU 4538  N   ASN A 576     8006   2978   3389    444   2301    137       N  
ATOM   4539  CA  ASN A 576      44.946 108.501  -5.668  1.00 37.72           C  
ANISOU 4539  CA  ASN A 576     7997   2966   3367    516   2302    164       C  
ATOM   4540  C   ASN A 576      44.940 109.891  -5.054  1.00 37.00           C  
ANISOU 4540  C   ASN A 576     7819   2920   3318    474   2284    189       C  
ATOM   4541  O   ASN A 576      45.013 110.887  -5.779  1.00 36.67           O  
ANISOU 4541  O   ASN A 576     7684   2956   3293    442   2281    204       O  
ATOM   4542  CB  ASN A 576      46.325 108.186  -6.262  1.00 38.22           C  
ANISOU 4542  CB  ASN A 576     8030   3105   3387    620   2323    170       C  
ATOM   4543  CG  ASN A 576      46.411 106.781  -6.824  1.00 39.02           C  
ANISOU 4543  CG  ASN A 576     8221   3162   3442    678   2338    135       C  
ATOM   4544  OD1 ASN A 576      46.657 105.822  -6.092  1.00 39.49           O  
ANISOU 4544  OD1 ASN A 576     8385   3141   3480    736   2340    132       O  
ATOM   4545  ND2 ASN A 576      46.217 106.653  -8.131  1.00 39.28           N  
ANISOU 4545  ND2 ASN A 576     8219   3249   3455    665   2345    107       N  
ATOM   4546  N   LYS A 577      44.840 109.959  -3.730  1.00 35.89           N  
ANISOU 4546  N   LYS A 577     7717   2732   3189    474   2273    194       N  
ATOM   4547  CA  LYS A 577      44.762 111.227  -3.019  1.00 35.38           C  
ANISOU 4547  CA  LYS A 577     7584   2700   3158    436   2254    206       C  
ATOM   4548  C   LYS A 577      45.897 111.316  -2.010  1.00 35.65           C  
ANISOU 4548  C   LYS A 577     7626   2752   3166    512   2256    229       C  
ATOM   4549  O   LYS A 577      46.151 110.360  -1.274  1.00 36.07           O  
ANISOU 4549  O   LYS A 577     7769   2753   3182    569   2258    228       O  
ATOM   4550  CB  LYS A 577      43.416 111.381  -2.304  1.00 34.98           C  
ANISOU 4550  CB  LYS A 577     7561   2592   3137    355   2239    178       C  
ATOM   4551  CG  LYS A 577      42.212 111.474  -3.225  1.00 34.72           C  
ANISOU 4551  CG  LYS A 577     7513   2551   3129    276   2238    150       C  
ATOM   4552  CD  LYS A 577      41.248 110.323  -2.983  1.00 34.97           C  
ANISOU 4552  CD  LYS A 577     7639   2497   3150    241   2251    119       C  
ATOM   4553  CE  LYS A 577      39.806 110.762  -3.177  1.00 34.64           C  
ANISOU 4553  CE  LYS A 577     7573   2447   3140    145   2247     82       C  
ATOM   4554  NZ  LYS A 577      39.580 111.365  -4.517  1.00 34.45           N1+
ANISOU 4554  NZ  LYS A 577     7487   2477   3125    121   2240     80       N1+
ATOM   4555  N   VAL A 578      46.576 112.459  -1.984  1.00 34.79           N  
ANISOU 4555  N   VAL A 578     7432   2715   3072    515   2257    254       N  
ATOM   4556  CA  VAL A 578      47.535 112.795  -0.937  1.00 35.02           C  
ANISOU 4556  CA  VAL A 578     7460   2769   3077    575   2258    269       C  
ATOM   4557  C   VAL A 578      46.913 113.907  -0.105  1.00 34.55           C  
ANISOU 4557  C   VAL A 578     7377   2703   3049    509   2239    263       C  
ATOM   4558  O   VAL A 578      46.672 115.009  -0.612  1.00 34.24           O  
ANISOU 4558  O   VAL A 578     7266   2692   3051    446   2242    278       O  
ATOM   4559  CB  VAL A 578      48.892 113.222  -1.516  1.00 35.44           C  
ANISOU 4559  CB  VAL A 578     7438   2913   3115    630   2288    299       C  
ATOM   4560  CG1 VAL A 578      49.818 113.680  -0.402  1.00 35.72           C  
ANISOU 4560  CG1 VAL A 578     7439   2976   3156    683   2258    302       C  
ATOM   4561  CG2 VAL A 578      49.521 112.077  -2.291  1.00 36.04           C  
ANISOU 4561  CG2 VAL A 578     7539   3006   3151    710   2310    290       C  
ATOM   4562  N   VAL A 579      46.641 113.620   1.164  1.00 34.62           N  
ANISOU 4562  N   VAL A 579     7449   2672   3033    524   2222    243       N  
ATOM   4563  CA  VAL A 579      45.866 114.508   2.021  1.00 34.28           C  
ANISOU 4563  CA  VAL A 579     7395   2621   3009    465   2206    220       C  
ATOM   4564  C   VAL A 579      46.755 115.042   3.136  1.00 34.59           C  
ANISOU 4564  C   VAL A 579     7414   2695   3034    521   2176    214       C  
ATOM   4565  O   VAL A 579      47.577 114.310   3.700  1.00 35.11           O  
ANISOU 4565  O   VAL A 579     7525   2765   3048    607   2168    222       O  
ATOM   4566  CB  VAL A 579      44.628 113.789   2.591  1.00 34.21           C  
ANISOU 4566  CB  VAL A 579     7450   2553   2997    420   2194    191       C  
ATOM   4567  CG1 VAL A 579      43.826 114.718   3.489  1.00 33.99           C  
ANISOU 4567  CG1 VAL A 579     7402   2533   2979    366   2185    157       C  
ATOM   4568  CG2 VAL A 579      43.760 113.269   1.457  1.00 33.99           C  
ANISOU 4568  CG2 VAL A 579     7421   2492   3003    366   2203    182       C  
ATOM   4569  N   LYS A 580      46.587 116.325   3.444  1.00 34.38           N  
ANISOU 4569  N   LYS A 580     7291   2689   3082    475   2126    193       N  
ATOM   4570  CA  LYS A 580      47.280 116.998   4.533  1.00 34.71           C  
ANISOU 4570  CA  LYS A 580     7273   2763   3151    512   2057    168       C  
ATOM   4571  C   LYS A 580      46.247 117.406   5.576  1.00 34.59           C  
ANISOU 4571  C   LYS A 580     7286   2732   3125    474   2041    114       C  
ATOM   4572  O   LYS A 580      45.230 118.019   5.234  1.00 34.19           O  
ANISOU 4572  O   LYS A 580     7210   2662   3119    400   2048     92       O  
ATOM   4573  CB  LYS A 580      48.035 118.223   4.010  1.00 34.76           C  
ANISOU 4573  CB  LYS A 580     7134   2806   3267    489   2002    181       C  
ATOM   4574  CG  LYS A 580      49.285 118.582   4.786  1.00 35.34           C  
ANISOU 4574  CG  LYS A 580     7137   2925   3367    551   1936    167       C  
ATOM   4575  CD  LYS A 580      49.856 119.912   4.323  1.00 35.48           C  
ANISOU 4575  CD  LYS A 580     7008   2966   3509    502   1880    179       C  
ATOM   4576  CE  LYS A 580      48.828 121.024   4.460  1.00 35.14           C  
ANISOU 4576  CE  LYS A 580     6933   2879   3541    421   1843    145       C  
ATOM   4577  NZ  LYS A 580      49.456 122.370   4.370  1.00 35.51           N1+
ANISOU 4577  NZ  LYS A 580     6846   2931   3717    381   1765    146       N1+
ATOM   4578  N   VAL A 581      46.493 117.059   6.841  1.00 35.04           N  
ANISOU 4578  N   VAL A 581     7394   2804   3116    529   2020     90       N  
ATOM   4579  CA  VAL A 581      45.521 117.322   7.899  1.00 35.10           C  
ANISOU 4579  CA  VAL A 581     7435   2815   3089    499   2017     35       C  
ATOM   4580  C   VAL A 581      46.248 117.399   9.233  1.00 35.76           C  
ANISOU 4580  C   VAL A 581     7522   2941   3124    572   1959      6       C  
ATOM   4581  O   VAL A 581      47.298 116.780   9.423  1.00 36.20           O  
ANISOU 4581  O   VAL A 581     7604   3010   3140    651   1941     39       O  
ATOM   4582  CB  VAL A 581      44.405 116.244   7.914  1.00 35.04           C  
ANISOU 4582  CB  VAL A 581     7553   2768   2991    461   2102     49       C  
ATOM   4583  CG1 VAL A 581      44.967 114.889   8.323  1.00 35.58           C  
ANISOU 4583  CG1 VAL A 581     7732   2819   2967    529   2119     99       C  
ATOM   4584  CG2 VAL A 581      43.261 116.663   8.829  1.00 35.13           C  
ANISOU 4584  CG2 VAL A 581     7572   2798   2976    412   2110    -12       C  
ATOM   4585  N   LEU A 582      45.679 118.168  10.161  1.00 35.92           N  
ANISOU 4585  N   LEU A 582     7512   2989   3147    551   1925    -63       N  
ATOM   4586  CA  LEU A 582      46.209 118.340  11.505  1.00 36.63           C  
ANISOU 4586  CA  LEU A 582     7604   3131   3182    616   1865   -106       C  
ATOM   4587  C   LEU A 582      45.652 117.277  12.447  1.00 37.11           C  
ANISOU 4587  C   LEU A 582     7805   3204   3091    634   1920    -91       C  
ATOM   4588  O   LEU A 582      44.588 116.702  12.219  1.00 36.89           O  
ANISOU 4588  O   LEU A 582     7851   3147   3020    574   2000    -73       O  
ATOM   4589  CB  LEU A 582      45.868 119.729  12.046  1.00 36.72           C  
ANISOU 4589  CB  LEU A 582     7511   3171   3269    588   1798   -200       C  
ATOM   4590  CG  LEU A 582      46.343 120.957  11.267  1.00 36.45           C  
ANISOU 4590  CG  LEU A 582     7337   3115   3396    558   1730   -216       C  
ATOM   4591  CD1 LEU A 582      45.671 122.208  11.807  1.00 36.60           C  
ANISOU 4591  CD1 LEU A 582     7280   3140   3486    525   1672   -317       C  
ATOM   4592  CD2 LEU A 582      47.855 121.094  11.329  1.00 36.89           C  
ANISOU 4592  CD2 LEU A 582     7331   3195   3489    620   1662   -197       C  
ATOM   4593  N   ARG A 583      46.387 117.035  13.530  1.00 37.89           N  
ANISOU 4593  N   ARG A 583     7939   3349   3110    715   1872    -97       N  
ATOM   4594  CA  ARG A 583      45.986 116.099  14.570  1.00 38.60           C  
ANISOU 4594  CA  ARG A 583     8164   3459   3044    739   1911    -74       C  
ATOM   4595  C   ARG A 583      46.601 116.535  15.891  1.00 39.47           C  
ANISOU 4595  C   ARG A 583     8254   3649   3093    813   1828   -127       C  
ATOM   4596  O   ARG A 583      47.763 116.970  15.912  1.00 39.66           O  
ANISOU 4596  O   ARG A 583     8201   3695   3174    880   1742   -144       O  
ATOM   4597  CB  ARG A 583      46.415 114.661  14.246  1.00 38.85           C  
ANISOU 4597  CB  ARG A 583     8322   3434   3005    782   1954     25       C  
ATOM   4598  CG  ARG A 583      46.158 113.657  15.363  1.00 39.81           C  
ANISOU 4598  CG  ARG A 583     8580   3565   2980    808   1971     71       C  
ATOM   4599  CD  ARG A 583      46.556 112.254  14.946  1.00 40.12           C  
ANISOU 4599  CD  ARG A 583     8723   3524   2997    846   1987    168       C  
ATOM   4600  NE  ARG A 583      47.955 112.179  14.535  1.00 40.21           N  
ANISOU 4600  NE  ARG A 583     8727   3532   3021    957   1945    179       N  
ATOM   4601  CZ  ARG A 583      48.921 111.624  15.259  1.00 41.16           C  
ANISOU 4601  CZ  ARG A 583     8904   3667   3067   1070   1884    210       C  
ATOM   4602  NH1 ARG A 583      48.645 111.082  16.437  1.00 42.10           N1+
ANISOU 4602  NH1 ARG A 583     9144   3803   3049   1093   1884    242       N1+
ATOM   4603  NH2 ARG A 583      50.165 111.604  14.801  1.00 41.26           N  
ANISOU 4603  NH2 ARG A 583     8851   3685   3140   1160   1822    211       N  
ATOM   4604  N   PRO A 584      45.857 116.457  16.991  1.00 40.09           N  
ANISOU 4604  N   PRO A 584     8395   3782   3056    802   1851   -158       N  
ATOM   4605  CA  PRO A 584      46.462 116.698  18.305  1.00 41.10           C  
ANISOU 4605  CA  PRO A 584     8526   3996   3095    883   1774   -203       C  
ATOM   4606  C   PRO A 584      47.415 115.577  18.687  1.00 41.85           C  
ANISOU 4606  C   PRO A 584     8731   4083   3087    978   1751   -115       C  
ATOM   4607  O   PRO A 584      47.196 114.404  18.369  1.00 41.90           O  
ANISOU 4607  O   PRO A 584     8861   4026   3033    969   1821    -18       O  
ATOM   4608  CB  PRO A 584      45.255 116.751  19.248  1.00 41.63           C  
ANISOU 4608  CB  PRO A 584     8643   4127   3047    834   1830   -246       C  
ATOM   4609  CG  PRO A 584      44.191 115.975  18.540  1.00 41.13           C  
ANISOU 4609  CG  PRO A 584     8617   4000   3009    733   1923   -171       C  
ATOM   4610  CD  PRO A 584      44.404 116.238  17.080  1.00 39.99           C  
ANISOU 4610  CD  PRO A 584     8425   3770   2999    708   1941   -162       C  
ATOM   4611  N   ALA A 585      48.485 115.952  19.379  1.00 42.54           N  
ANISOU 4611  N   ALA A 585     8771   4230   3162   1072   1645   -154       N  
ATOM   4612  CA  ALA A 585      49.536 115.026  19.775  1.00 43.38           C  
ANISOU 4612  CA  ALA A 585     8961   4337   3184   1183   1598    -84       C  
ATOM   4613  C   ALA A 585      49.582 114.911  21.295  1.00 44.68           C  
ANISOU 4613  C   ALA A 585     9199   4595   3182   1246   1552   -104       C  
ATOM   4614  O   ALA A 585      48.772 115.501  22.014  1.00 44.92           O  
ANISOU 4614  O   ALA A 585     9217   4695   3158   1201   1568   -173       O  
ATOM   4615  CB  ALA A 585      50.889 115.471  19.217  1.00 43.24           C  
ANISOU 4615  CB  ALA A 585     8818   4318   3292   1250   1506   -107       C  
ATOM   4616  N   GLU A 586      50.550 114.137  21.780  1.00 47.16           N  
ANISOU 4616  N   GLU A 586     9589   4918   3412   1358   1491    -46       N  
ATOM   4617  CA  GLU A 586      50.730 113.965  23.216  1.00 48.56           C  
ANISOU 4617  CA  GLU A 586     9844   5189   3419   1433   1435    -54       C  
ATOM   4618  C   GLU A 586      51.346 115.225  23.812  1.00 48.90           C  
ANISOU 4618  C   GLU A 586     9738   5332   3508   1479   1317   -188       C  
ATOM   4619  O   GLU A 586      52.485 115.581  23.489  1.00 48.88           O  
ANISOU 4619  O   GLU A 586     9630   5330   3611   1544   1224   -221       O  
ATOM   4620  CB  GLU A 586      51.616 112.753  23.503  1.00 49.57           C  
ANISOU 4620  CB  GLU A 586    10098   5286   3449   1549   1392     52       C  
ATOM   4621  CG  GLU A 586      51.436 111.583  22.543  1.00 49.13           C  
ANISOU 4621  CG  GLU A 586    10150   5098   3419   1526   1475    170       C  
ATOM   4622  CD  GLU A 586      52.073 110.302  23.059  1.00 50.44           C  
ANISOU 4622  CD  GLU A 586    10477   5227   3460   1639   1437    279       C  
ATOM   4623  OE1 GLU A 586      51.406 109.566  23.817  1.00 51.34           O  
ANISOU 4623  OE1 GLU A 586    10754   5336   3417   1619   1484    359       O  
ATOM   4624  OE2 GLU A 586      53.245 110.033  22.717  1.00 50.68           O1+
ANISOU 4624  OE2 GLU A 586    10472   5236   3549   1749   1356    287       O1+
ATOM   4625  N   GLY A 587      50.595 115.904  24.678  1.00 47.77           N  
ANISOU 4625  N   GLY A 587     9580   5277   3292   1443   1321   -273       N  
ATOM   4626  CA  GLY A 587      51.098 117.056  25.401  1.00 48.33           C  
ANISOU 4626  CA  GLY A 587     9528   5446   3390   1490   1204   -412       C  
ATOM   4627  C   GLY A 587      50.482 118.385  25.027  1.00 47.52           C  
ANISOU 4627  C   GLY A 587     9279   5344   3433   1403   1206   -538       C  
ATOM   4628  O   GLY A 587      50.915 119.415  25.559  1.00 48.02           O  
ANISOU 4628  O   GLY A 587     9230   5472   3542   1438   1100   -666       O  
ATOM   4629  N   GLY A 588      49.488 118.407  24.140  1.00 50.58           N  
ANISOU 4629  N   GLY A 588     9664   5659   3897   1295   1314   -512       N  
ATOM   4630  CA  GLY A 588      48.860 119.633  23.711  1.00 50.01           C  
ANISOU 4630  CA  GLY A 588     9459   5572   3969   1217   1313   -623       C  
ATOM   4631  C   GLY A 588      49.392 120.194  22.409  1.00 49.68           C  
ANISOU 4631  C   GLY A 588     9295   5434   4146   1179   1285   -618       C  
ATOM   4632  O   GLY A 588      48.698 120.991  21.765  1.00 49.07           O  
ANISOU 4632  O   GLY A 588     9137   5312   4195   1097   1310   -669       O  
ATOM   4633  N   LYS A 589      50.603 119.810  22.013  1.00 49.30           N  
ANISOU 4633  N   LYS A 589     9229   5358   4143   1239   1232   -558       N  
ATOM   4634  CA  LYS A 589      51.114 120.199  20.708  1.00 49.45           C  
ANISOU 4634  CA  LYS A 589     9142   5296   4352   1197   1225   -533       C  
ATOM   4635  C   LYS A 589      50.270 119.563  19.610  1.00 47.12           C  
ANISOU 4635  C   LYS A 589     8911   4916   4078   1116   1353   -439       C  
ATOM   4636  O   LYS A 589      49.756 118.451  19.756  1.00 46.45           O  
ANISOU 4636  O   LYS A 589     8966   4819   3863   1119   1436   -359       O  
ATOM   4637  CB  LYS A 589      52.576 119.775  20.561  1.00 51.57           C  
ANISOU 4637  CB  LYS A 589     9382   5572   4642   1285   1154   -488       C  
ATOM   4638  CG  LYS A 589      53.510 120.388  21.593  1.00 53.69           C  
ANISOU 4638  CG  LYS A 589     9575   5926   4899   1368   1015   -584       C  
ATOM   4639  CD  LYS A 589      54.859 119.686  21.612  1.00 56.10           C  
ANISOU 4639  CD  LYS A 589     9879   6253   5182   1473    954   -531       C  
ATOM   4640  CE  LYS A 589      55.746 120.231  22.722  1.00 59.09           C  
ANISOU 4640  CE  LYS A 589    10189   6727   5534   1560    810   -632       C  
ATOM   4641  NZ  LYS A 589      56.987 119.426  22.893  1.00 60.43           N1+
ANISOU 4641  NZ  LYS A 589    10373   6931   5656   1679    747   -582       N1+
ATOM   4642  N   THR A 590      50.115 120.288  18.508  1.00 42.69           N  
ANISOU 4642  N   THR A 590     8247   4293   3683   1040   1364   -449       N  
ATOM   4643  CA  THR A 590      49.390 119.796  17.348  1.00 41.69           C  
ANISOU 4643  CA  THR A 590     8162   4088   3592    964   1471   -370       C  
ATOM   4644  C   THR A 590      50.371 119.506  16.221  1.00 41.30           C  
ANISOU 4644  C   THR A 590     8065   3993   3634    977   1468   -296       C  
ATOM   4645  O   THR A 590      51.433 120.130  16.124  1.00 41.60           O  
ANISOU 4645  O   THR A 590     7990   4050   3765   1008   1384   -324       O  
ATOM   4646  CB  THR A 590      48.329 120.800  16.888  1.00 41.04           C  
ANISOU 4646  CB  THR A 590     8007   3974   3613    867   1492   -431       C  
ATOM   4647  OG1 THR A 590      48.962 121.903  16.229  1.00 40.82           O  
ANISOU 4647  OG1 THR A 590     7833   3915   3760    843   1417   -465       O  
ATOM   4648  CG2 THR A 590      47.539 121.315  18.083  1.00 41.65           C  
ANISOU 4648  CG2 THR A 590     8092   4117   3616    869   1474   -536       C  
ATOM   4649  N   VAL A 591      50.010 118.545  15.369  1.00 39.76           N  
ANISOU 4649  N   VAL A 591     7954   3742   3412    953   1563   -206       N  
ATOM   4650  CA  VAL A 591      50.925 118.000  14.377  1.00 39.58           C  
ANISOU 4650  CA  VAL A 591     7912   3689   3437    984   1574   -135       C  
ATOM   4651  C   VAL A 591      50.179 117.798  13.064  1.00 38.63           C  
ANISOU 4651  C   VAL A 591     7804   3502   3371    899   1666    -85       C  
ATOM   4652  O   VAL A 591      48.955 117.650  13.032  1.00 38.22           O  
ANISOU 4652  O   VAL A 591     7818   3420   3283    834   1732    -86       O  
ATOM   4653  CB  VAL A 591      51.559 116.674  14.864  1.00 40.30           C  
ANISOU 4653  CB  VAL A 591     8122   3788   3401   1089   1577    -76       C  
ATOM   4654  CG1 VAL A 591      50.734 115.472  14.419  1.00 39.98           C  
ANISOU 4654  CG1 VAL A 591     8230   3680   3281   1062   1682      0       C  
ATOM   4655  CG2 VAL A 591      53.000 116.556  14.408  1.00 40.67           C  
ANISOU 4655  CG2 VAL A 591     8088   3856   3509   1166   1522    -58       C  
ATOM   4656  N   MET A 592      50.937 117.808  11.971  1.00 38.38           N  
ANISOU 4656  N   MET A 592     7702   3457   3425    902   1668    -45       N  
ATOM   4657  CA  MET A 592      50.391 117.629  10.633  1.00 37.60           C  
ANISOU 4657  CA  MET A 592     7607   3307   3375    831   1747      3       C  
ATOM   4658  C   MET A 592      50.665 116.209  10.160  1.00 37.73           C  
ANISOU 4658  C   MET A 592     7729   3294   3312    887   1807     69       C  
ATOM   4659  O   MET A 592      51.808 115.747  10.210  1.00 38.31           O  
ANISOU 4659  O   MET A 592     7788   3395   3372    977   1774     87       O  
ATOM   4660  CB  MET A 592      51.004 118.634   9.656  1.00 37.38           C  
ANISOU 4660  CB  MET A 592     7426   3288   3488    788   1715      5       C  
ATOM   4661  CG  MET A 592      50.389 118.602   8.268  1.00 36.66           C  
ANISOU 4661  CG  MET A 592     7332   3154   3442    712   1788     53       C  
ATOM   4662  SD  MET A 592      48.921 119.638   8.141  1.00 36.02           S  
ANISOU 4662  SD  MET A 592     7229   3032   3425    600   1793     12       S  
ATOM   4663  CE  MET A 592      49.664 121.267   8.160  1.00 36.34           C  
ANISOU 4663  CE  MET A 592     7099   3090   3619    569   1689    -23       C  
ATOM   4664  N   ASP A 593      49.622 115.521   9.706  1.00 37.28           N  
ANISOU 4664  N   ASP A 593     7774   3182   3210    837   1889     99       N  
ATOM   4665  CA  ASP A 593      49.737 114.162   9.197  1.00 37.45           C  
ANISOU 4665  CA  ASP A 593     7906   3157   3165    880   1946    154       C  
ATOM   4666  C   ASP A 593      49.604 114.158   7.681  1.00 36.86           C  
ANISOU 4666  C   ASP A 593     7789   3060   3157    831   1999    178       C  
ATOM   4667  O   ASP A 593      48.760 114.865   7.121  1.00 36.21           O  
ANISOU 4667  O   ASP A 593     7661   2968   3131    737   2022    165       O  
ATOM   4668  CB  ASP A 593      48.671 113.248   9.808  1.00 37.59           C  
ANISOU 4668  CB  ASP A 593     8083   3122   3077    856   2001    172       C  
ATOM   4669  CG  ASP A 593      48.909 112.970  11.277  1.00 38.42           C  
ANISOU 4669  CG  ASP A 593     8258   3254   3085    921   1958    169       C  
ATOM   4670  OD1 ASP A 593      50.084 112.965  11.702  1.00 39.02           O  
ANISOU 4670  OD1 ASP A 593     8300   3370   3155   1019   1888    166       O  
ATOM   4671  OD2 ASP A 593      47.919 112.749  12.006  1.00 38.56           O1+
ANISOU 4671  OD2 ASP A 593     8363   3261   3027    873   1994    168       O1+
ATOM   4672  N   ILE A 594      50.439 113.360   7.023  1.00 37.20           N  
ANISOU 4672  N   ILE A 594     7846   3099   3188    902   2013    208       N  
ATOM   4673  CA  ILE A 594      50.346 113.130   5.586  1.00 36.84           C  
ANISOU 4673  CA  ILE A 594     7780   3040   3176    871   2069    229       C  
ATOM   4674  C   ILE A 594      49.791 111.727   5.392  1.00 37.01           C  
ANISOU 4674  C   ILE A 594     7960   2985   3118    891   2128    250       C  
ATOM   4675  O   ILE A 594      50.462 110.733   5.700  1.00 37.73           O  
ANISOU 4675  O   ILE A 594     8127   3054   3155    991   2116    264       O  
ATOM   4676  CB  ILE A 594      51.701 113.289   4.886  1.00 37.23           C  
ANISOU 4676  CB  ILE A 594     7716   3155   3273    935   2048    238       C  
ATOM   4677  CG1 ILE A 594      52.373 114.593   5.314  1.00 37.32           C  
ANISOU 4677  CG1 ILE A 594     7579   3235   3365    919   1977    218       C  
ATOM   4678  CG2 ILE A 594      51.515 113.260   3.377  1.00 36.88           C  
ANISOU 4678  CG2 ILE A 594     7637   3118   3259    888   2108    257       C  
ATOM   4679  CD1 ILE A 594      51.602 115.826   4.930  1.00 36.64           C  
ANISOU 4679  CD1 ILE A 594     7416   3146   3360    799   1976    213       C  
ATOM   4680  N   ILE A 595      48.565 111.641   4.883  1.00 36.47           N  
ANISOU 4680  N   ILE A 595     7933   2869   3055    796   2177    250       N  
ATOM   4681  CA  ILE A 595      47.903 110.370   4.640  1.00 36.67           C  
ANISOU 4681  CA  ILE A 595     8052   2810   3072    782   2186    265       C  
ATOM   4682  C   ILE A 595      47.587 110.262   3.153  1.00 36.30           C  
ANISOU 4682  C   ILE A 595     7955   2755   3081    735   2210    260       C  
ATOM   4683  O   ILE A 595      47.730 111.219   2.392  1.00 35.85           O  
ANISOU 4683  O   ILE A 595     7793   2758   3070    700   2217    254       O  
ATOM   4684  CB  ILE A 595      46.627 110.204   5.488  1.00 36.58           C  
ANISOU 4684  CB  ILE A 595     8091   2750   3059    699   2177    257       C  
ATOM   4685  CG1 ILE A 595      45.634 111.329   5.190  1.00 35.79           C  
ANISOU 4685  CG1 ILE A 595     7891   2680   3029    588   2176    225       C  
ATOM   4686  CG2 ILE A 595      46.974 110.167   6.970  1.00 37.16           C  
ANISOU 4686  CG2 ILE A 595     8225   2838   3055    753   2152    266       C  
ATOM   4687  CD1 ILE A 595      44.470 111.397   6.158  1.00 35.80           C  
ANISOU 4687  CD1 ILE A 595     7915   2666   3022    515   2171    204       C  
ATOM   4688  N   SER A 596      47.158 109.070   2.743  1.00 36.60           N  
ANISOU 4688  N   SER A 596     8082   2717   3108    736   2225    263       N  
ATOM   4689  CA  SER A 596      46.785 108.843   1.356  1.00 36.38           C  
ANISOU 4689  CA  SER A 596     8022   2681   3119    696   2245    250       C  
ATOM   4690  C   SER A 596      45.678 107.802   1.296  1.00 36.56           C  
ANISOU 4690  C   SER A 596     8148   2602   3141    643   2259    239       C  
ATOM   4691  O   SER A 596      45.537 106.962   2.188  1.00 37.11           O  
ANISOU 4691  O   SER A 596     8337   2599   3167    667   2263    250       O  
ATOM   4692  CB  SER A 596      47.985 108.404   0.507  1.00 36.89           C  
ANISOU 4692  CB  SER A 596     8075   2785   3156    797   2263    255       C  
ATOM   4693  OG  SER A 596      48.373 107.077   0.813  1.00 37.72           O  
ANISOU 4693  OG  SER A 596     8312   2818   3203    887   2270    261       O  
ATOM   4694  N   ARG A 597      44.891 107.868   0.223  1.00 37.53           N  
ANISOU 4694  N   ARG A 597     8232   2721   3307    569   2269    215       N  
ATOM   4695  CA  ARG A 597      43.758 106.974   0.044  1.00 37.73           C  
ANISOU 4695  CA  ARG A 597     8345   2655   3334    504   2288    194       C  
ATOM   4696  C   ARG A 597      43.486 106.818  -1.445  1.00 37.63           C  
ANISOU 4696  C   ARG A 597     8301   2656   3341    477   2301    176       C  
ATOM   4697  O   ARG A 597      43.929 107.629  -2.263  1.00 38.24           O  
ANISOU 4697  O   ARG A 597     8268   2821   3438    485   2290    176       O  
ATOM   4698  CB  ARG A 597      42.515 107.497   0.773  1.00 37.32           C  
ANISOU 4698  CB  ARG A 597     8267   2597   3315    402   2281    168       C  
ATOM   4699  CG  ARG A 597      41.422 106.466   0.958  1.00 37.77           C  
ANISOU 4699  CG  ARG A 597     8430   2561   3359    339   2311    142       C  
ATOM   4700  CD  ARG A 597      40.148 107.093   1.480  1.00 37.39           C  
ANISOU 4700  CD  ARG A 597     8325   2538   3345    233   2308    108       C  
ATOM   4701  NE  ARG A 597      39.093 106.095   1.617  1.00 37.95           N  
ANISOU 4701  NE  ARG A 597     8488   2533   3398    164   2346     77       N  
ATOM   4702  CZ  ARG A 597      38.942 105.312   2.680  1.00 38.69           C  
ANISOU 4702  CZ  ARG A 597     8677   2583   3441    164   2366     82       C  
ATOM   4703  NH1 ARG A 597      39.781 105.413   3.702  1.00 38.93           N1+
ANISOU 4703  NH1 ARG A 597     8726   2632   3432    235   2345    121       N1+
ATOM   4704  NH2 ARG A 597      37.953 104.430   2.721  1.00 39.30           N  
ANISOU 4704  NH2 ARG A 597     8830   2604   3498     89   2406     50       N  
ATOM   4705  N   GLN A 598      42.745 105.761  -1.792  1.00 39.54           N  
ANISOU 4705  N   GLN A 598     8646   2810   3569    441   2327    161       N  
ATOM   4706  CA  GLN A 598      42.477 105.435  -3.187  1.00 39.36           C  
ANISOU 4706  CA  GLN A 598     8611   2798   3547    421   2338    140       C  
ATOM   4707  C   GLN A 598      40.992 105.296  -3.501  1.00 39.11           C  
ANISOU 4707  C   GLN A 598     8600   2721   3541    304   2351    105       C  
ATOM   4708  O   GLN A 598      40.646 104.879  -4.612  1.00 39.77           O  
ANISOU 4708  O   GLN A 598     8693   2806   3613    282   2361     84       O  
ATOM   4709  CB  GLN A 598      43.214 104.151  -3.581  1.00 40.27           C  
ANISOU 4709  CB  GLN A 598     8832   2867   3601    508   2358    148       C  
ATOM   4710  CG  GLN A 598      44.701 104.192  -3.283  1.00 40.55           C  
ANISOU 4710  CG  GLN A 598     8848   2954   3607    637   2347    169       C  
ATOM   4711  CD  GLN A 598      45.433 102.965  -3.781  1.00 41.93           C  
ANISOU 4711  CD  GLN A 598     9105   3098   3727    738   2356    153       C  
ATOM   4712  OE1 GLN A 598      45.751 102.063  -3.009  1.00 43.02           O  
ANISOU 4712  OE1 GLN A 598     9367   3157   3822    799   2359    171       O  
ATOM   4713  NE2 GLN A 598      45.708 102.928  -5.080  1.00 42.07           N  
ANISOU 4713  NE2 GLN A 598     9052   3186   3746    763   2354    113       N  
ATOM   4714  N   ASP A 599      40.108 105.623  -2.567  1.00 38.20           N  
ANISOU 4714  N   ASP A 599     8485   2578   3452    232   2351     90       N  
ATOM   4715  CA  ASP A 599      38.678 105.666  -2.854  1.00 38.07           C  
ANISOU 4715  CA  ASP A 599     8462   2541   3462    120   2365     47       C  
ATOM   4716  C   ASP A 599      38.119 106.934  -2.218  1.00 37.37           C  
ANISOU 4716  C   ASP A 599     8258   2523   3416     69   2338     31       C  
ATOM   4717  O   ASP A 599      38.855 107.891  -1.955  1.00 36.94           O  
ANISOU 4717  O   ASP A 599     8120   2541   3375    116   2307     54       O  
ATOM   4718  CB  ASP A 599      37.982 104.378  -2.385  1.00 38.89           C  
ANISOU 4718  CB  ASP A 599     8672   2574   3529     73   2395     29       C  
ATOM   4719  CG  ASP A 599      38.239 104.071  -0.927  1.00 39.62           C  
ANISOU 4719  CG  ASP A 599     8816   2645   3593    102   2397     37       C  
ATOM   4720  OD1 ASP A 599      39.398 104.217  -0.483  1.00 39.85           O  
ANISOU 4720  OD1 ASP A 599     8857   2680   3605    199   2381     75       O  
ATOM   4721  OD2 ASP A 599      37.281 103.683  -0.224  1.00 39.99           O1+
ANISOU 4721  OD2 ASP A 599     8902   2667   3626     28   2424      5       O1+
ATOM   4722  N   GLN A 600      36.804 106.949  -1.979  1.00 36.24           N  
ANISOU 4722  N   GLN A 600     8116   2364   3290    -28   2356     -8       N  
ATOM   4723  CA  GLN A 600      36.079 108.109  -1.465  1.00 35.71           C  
ANISOU 4723  CA  GLN A 600     7947   2364   3258    -84   2339    -26       C  
ATOM   4724  C   GLN A 600      36.131 109.292  -2.426  1.00 35.07           C  
ANISOU 4724  C   GLN A 600     7757   2361   3208    -82   2307    -25       C  
ATOM   4725  O   GLN A 600      36.833 109.257  -3.443  1.00 35.03           O  
ANISOU 4725  O   GLN A 600     7742   2375   3194    -34   2296     -7       O  
ATOM   4726  CB  GLN A 600      36.614 108.539  -0.095  1.00 35.64           C  
ANISOU 4726  CB  GLN A 600     7922   2380   3241    -45   2323     -4       C  
ATOM   4727  CG  GLN A 600      36.280 107.594   1.042  1.00 36.35           C  
ANISOU 4727  CG  GLN A 600     8105   2414   3291    -66   2354     -8       C  
ATOM   4728  CD  GLN A 600      36.619 108.181   2.398  1.00 36.32           C  
ANISOU 4728  CD  GLN A 600     8072   2457   3272    -40   2336     14       C  
ATOM   4729  OE1 GLN A 600      36.806 109.389   2.533  1.00 35.75           O  
ANISOU 4729  OE1 GLN A 600     7904   2453   3225    -30   2307     17       O  
ATOM   4730  NE2 GLN A 600      36.702 107.327   3.411  1.00 37.05           N  
ANISOU 4730  NE2 GLN A 600     8255   2511   3313    -30   2356     28       N  
ATOM   4731  N   ARG A 601      35.381 110.343  -2.108  1.00 34.05           N  
ANISOU 4731  N   ARG A 601     7551   2279   3107   -133   2297    -44       N  
ATOM   4732  CA  ARG A 601      35.322 111.553  -2.915  1.00 33.57           C  
ANISOU 4732  CA  ARG A 601     7403   2281   3070   -134   2273    -44       C  
ATOM   4733  C   ARG A 601      35.664 112.755  -2.048  1.00 33.20           C  
ANISOU 4733  C   ARG A 601     7296   2278   3042   -114   2255    -31       C  
ATOM   4734  O   ARG A 601      35.132 112.901  -0.942  1.00 33.29           O  
ANISOU 4734  O   ARG A 601     7305   2287   3055   -146   2266    -50       O  
ATOM   4735  CB  ARG A 601      33.936 111.732  -3.547  1.00 33.61           C  
ANISOU 4735  CB  ARG A 601     7391   2294   3086   -218   2288    -87       C  
ATOM   4736  CG  ARG A 601      33.587 113.176  -3.898  1.00 33.22           C  
ANISOU 4736  CG  ARG A 601     7262   2302   3058   -231   2270    -92       C  
ATOM   4737  CD  ARG A 601      33.355 113.370  -5.388  1.00 33.25           C  
ANISOU 4737  CD  ARG A 601     7254   2331   3048   -238   2261    -93       C  
ATOM   4738  NE  ARG A 601      32.361 112.440  -5.916  1.00 33.66           N  
ANISOU 4738  NE  ARG A 601     7350   2358   3083   -298   2285   -136       N  
ATOM   4739  CZ  ARG A 601      32.617 111.513  -6.833  1.00 33.99           C  
ANISOU 4739  CZ  ARG A 601     7440   2382   3093   -284   2288   -134       C  
ATOM   4740  NH1 ARG A 601      33.837 111.395  -7.342  1.00 33.95           N1+
ANISOU 4740  NH1 ARG A 601     7438   2393   3070   -209   2270    -92       N1+
ATOM   4741  NH2 ARG A 601      31.648 110.711  -7.249  1.00 34.45           N  
ANISOU 4741  NH2 ARG A 601     7541   2414   3135   -348   2314   -180       N  
ATOM   4742  N   GLY A 602      36.556 113.607  -2.547  1.00 34.98           N  
ANISOU 4742  N   GLY A 602     7473   2543   3274    -66   2234      1       N  
ATOM   4743  CA  GLY A 602      36.839 114.862  -1.875  1.00 34.72           C  
ANISOU 4743  CA  GLY A 602     7391   2542   3258    -55   2224     10       C  
ATOM   4744  C   GLY A 602      35.694 115.845  -2.061  1.00 34.80           C  
ANISOU 4744  C   GLY A 602     7366   2567   3292   -116   2231    -23       C  
ATOM   4745  O   GLY A 602      35.091 115.937  -3.130  1.00 35.24           O  
ANISOU 4745  O   GLY A 602     7413   2629   3350   -147   2232    -30       O  
ATOM   4746  N   SER A 603      35.400 116.592  -0.994  1.00 34.55           N  
ANISOU 4746  N   SER A 603     7316   2543   3267   -127   2238    -48       N  
ATOM   4747  CA  SER A 603      34.256 117.497  -1.019  1.00 34.56           C  
ANISOU 4747  CA  SER A 603     7286   2558   3287   -175   2253   -100       C  
ATOM   4748  C   SER A 603      34.494 118.689  -1.937  1.00 34.56           C  
ANISOU 4748  C   SER A 603     7226   2565   3341   -164   2202    -72       C  
ATOM   4749  O   SER A 603      33.544 119.200  -2.542  1.00 34.64           O  
ANISOU 4749  O   SER A 603     7188   2577   3396   -197   2168   -102       O  
ATOM   4750  CB  SER A 603      33.940 117.984   0.394  1.00 34.71           C  
ANISOU 4750  CB  SER A 603     7282   2594   3310   -175   2257   -156       C  
ATOM   4751  OG  SER A 603      34.724 119.118   0.721  1.00 34.83           O  
ANISOU 4751  OG  SER A 603     7245   2615   3374   -129   2203   -148       O  
ATOM   4752  N   GLY A 604      35.741 119.138  -2.061  1.00 35.93           N  
ANISOU 4752  N   GLY A 604     7379   2741   3533   -120   2171     -8       N  
ATOM   4753  CA  GLY A 604      36.036 120.352  -2.796  1.00 35.91           C  
ANISOU 4753  CA  GLY A 604     7296   2738   3610   -119   2096     35       C  
ATOM   4754  C   GLY A 604      36.577 120.149  -4.196  1.00 36.04           C  
ANISOU 4754  C   GLY A 604     7323   2772   3599   -118   2102    114       C  
ATOM   4755  O   GLY A 604      37.173 121.067  -4.768  1.00 36.70           O  
ANISOU 4755  O   GLY A 604     7348   2861   3735   -115   2050    177       O  
ATOM   4756  N   GLN A 605      36.388 118.960  -4.760  1.00 35.63           N  
ANISOU 4756  N   GLN A 605     7344   2730   3462   -122   2166    110       N  
ATOM   4757  CA  GLN A 605      36.711 118.759  -6.164  1.00 35.81           C  
ANISOU 4757  CA  GLN A 605     7367   2785   3453   -118   2164    163       C  
ATOM   4758  C   GLN A 605      35.743 119.552  -7.034  1.00 36.04           C  
ANISOU 4758  C   GLN A 605     7357   2815   3521   -159   2115    166       C  
ATOM   4759  O   GLN A 605      34.578 119.753  -6.680  1.00 36.07           O  
ANISOU 4759  O   GLN A 605     7345   2798   3561   -189   2093     98       O  
ATOM   4760  CB  GLN A 605      36.660 117.273  -6.523  1.00 35.88           C  
ANISOU 4760  CB  GLN A 605     7413   2805   3414    -98   2181    116       C  
ATOM   4761  CG  GLN A 605      37.477 116.389  -5.596  1.00 35.79           C  
ANISOU 4761  CG  GLN A 605     7425   2778   3397    -50   2191    102       C  
ATOM   4762  CD  GLN A 605      37.417 114.924  -5.978  1.00 35.93           C  
ANISOU 4762  CD  GLN A 605     7493   2776   3381    -36   2203     73       C  
ATOM   4763  OE1 GLN A 605      38.022 114.077  -5.321  1.00 36.02           O  
ANISOU 4763  OE1 GLN A 605     7541   2761   3383      4   2211     70       O  
ATOM   4764  NE2 GLN A 605      36.686 114.616  -7.044  1.00 36.21           N  
ANISOU 4764  NE2 GLN A 605     7544   2819   3396    -67   2205     55       N  
ATOM   4765  N   VAL A 606      36.242 120.016  -8.183  1.00 35.55           N  
ANISOU 4765  N   VAL A 606     7269   2786   3452   -158   2089    245       N  
ATOM   4766  CA  VAL A 606      35.461 120.928  -9.018  1.00 36.02           C  
ANISOU 4766  CA  VAL A 606     7283   2847   3557   -187   2017    265       C  
ATOM   4767  C   VAL A 606      34.185 120.262  -9.517  1.00 36.05           C  
ANISOU 4767  C   VAL A 606     7321   2857   3520   -211   2028    194       C  
ATOM   4768  O   VAL A 606      33.159 120.929  -9.700  1.00 36.73           O  
ANISOU 4768  O   VAL A 606     7366   2928   3660   -233   1964    163       O  
ATOM   4769  CB  VAL A 606      36.322 121.447 -10.187  1.00 36.48           C  
ANISOU 4769  CB  VAL A 606     7317   2950   3594   -185   1998    378       C  
ATOM   4770  CG1 VAL A 606      35.556 122.484 -10.998  1.00 37.14           C  
ANISOU 4770  CG1 VAL A 606     7359   3025   3727   -213   1912    415       C  
ATOM   4771  CG2 VAL A 606      37.622 122.033  -9.667  1.00 36.51           C  
ANISOU 4771  CG2 VAL A 606     7277   2951   3643   -171   1994    444       C  
ATOM   4772  N   VAL A 607      34.215 118.950  -9.728  1.00 34.38           N  
ANISOU 4772  N   VAL A 607     7182   2662   3219   -206   2100    160       N  
ATOM   4773  CA  VAL A 607      33.076 118.217 -10.260  1.00 34.53           C  
ANISOU 4773  CA  VAL A 607     7235   2685   3198   -235   2112     89       C  
ATOM   4774  C   VAL A 607      32.433 117.325  -9.197  1.00 34.27           C  
ANISOU 4774  C   VAL A 607     7244   2613   3165   -258   2165     -2       C  
ATOM   4775  O   VAL A 607      31.783 116.339  -9.535  1.00 34.45           O  
ANISOU 4775  O   VAL A 607     7317   2632   3141   -284   2199    -59       O  
ATOM   4776  CB  VAL A 607      33.471 117.405 -11.504  1.00 34.86           C  
ANISOU 4776  CB  VAL A 607     7330   2775   3140   -219   2144    112       C  
ATOM   4777  CG1 VAL A 607      33.571 118.313 -12.717  1.00 35.37           C  
ANISOU 4777  CG1 VAL A 607     7350   2892   3197   -216   2083    189       C  
ATOM   4778  CG2 VAL A 607      34.791 116.682 -11.267  1.00 34.73           C  
ANISOU 4778  CG2 VAL A 607     7309   2772   3114   -165   2162    129       C  
ATOM   4779  N   THR A 608      32.595 117.662  -7.914  1.00 34.07           N  
ANISOU 4779  N   THR A 608     7198   2558   3187   -254   2171    -15       N  
ATOM   4780  CA  THR A 608      32.013 116.846  -6.850  1.00 34.03           C  
ANISOU 4780  CA  THR A 608     7234   2524   3170   -281   2227    -88       C  
ATOM   4781  C   THR A 608      30.496 116.777  -6.975  1.00 34.30           C  
ANISOU 4781  C   THR A 608     7241   2563   3230   -339   2215   -172       C  
ATOM   4782  O   THR A 608      29.910 115.688  -6.971  1.00 34.55           O  
ANISOU 4782  O   THR A 608     7327   2581   3220   -379   2268   -222       O  
ATOM   4783  CB  THR A 608      32.408 117.400  -5.479  1.00 33.78           C  
ANISOU 4783  CB  THR A 608     7175   2479   3181   -263   2224    -89       C  
ATOM   4784  OG1 THR A 608      33.825 117.303  -5.311  1.00 33.61           O  
ANISOU 4784  OG1 THR A 608     7171   2458   3143   -209   2227    -23       O  
ATOM   4785  CG2 THR A 608      31.721 116.614  -4.368  1.00 33.89           C  
ANISOU 4785  CG2 THR A 608     7217   2476   3185   -298   2270   -155       C  
ATOM   4786  N   TYR A 609      29.841 117.937  -7.086  1.00 33.60           N  
ANISOU 4786  N   TYR A 609     7063   2488   3215   -343   2142   -191       N  
ATOM   4787  CA  TYR A 609      28.384 117.955  -7.192  1.00 33.96           C  
ANISOU 4787  CA  TYR A 609     7064   2548   3292   -390   2123   -280       C  
ATOM   4788  C   TYR A 609      27.908 117.223  -8.440  1.00 34.31           C  
ANISOU 4788  C   TYR A 609     7142   2608   3287   -415   2124   -294       C  
ATOM   4789  O   TYR A 609      26.906 116.498  -8.399  1.00 34.66           O  
ANISOU 4789  O   TYR A 609     7193   2656   3322   -468   2154   -373       O  
ATOM   4790  CB  TYR A 609      27.871 119.396  -7.196  1.00 34.09           C  
ANISOU 4790  CB  TYR A 609     6978   2572   3402   -372   2028   -295       C  
ATOM   4791  CG  TYR A 609      26.376 119.499  -7.409  1.00 34.58           C  
ANISOU 4791  CG  TYR A 609     6978   2658   3502   -408   1996   -391       C  
ATOM   4792  CD1 TYR A 609      25.495 119.410  -6.340  1.00 34.78           C  
ANISOU 4792  CD1 TYR A 609     6959   2697   3558   -440   2029   -488       C  
ATOM   4793  CD2 TYR A 609      25.846 119.678  -8.682  1.00 34.95           C  
ANISOU 4793  CD2 TYR A 609     7006   2725   3550   -409   1932   -387       C  
ATOM   4794  CE1 TYR A 609      24.129 119.497  -6.531  1.00 35.33           C  
ANISOU 4794  CE1 TYR A 609     6958   2800   3667   -474   2002   -584       C  
ATOM   4795  CE2 TYR A 609      24.483 119.764  -8.883  1.00 35.49           C  
ANISOU 4795  CE2 TYR A 609     7009   2820   3656   -437   1896   -482       C  
ATOM   4796  CZ  TYR A 609      23.629 119.674  -7.805  1.00 35.68           C  
ANISOU 4796  CZ  TYR A 609     6980   2858   3719   -470   1932   -583       C  
ATOM   4797  OH  TYR A 609      22.270 119.762  -8.007  1.00 36.32           O  
ANISOU 4797  OH  TYR A 609     6981   2977   3842   -498   1897   -684       O  
ATOM   4798  N   ALA A 610      28.610 117.402  -9.561  1.00 34.07           N  
ANISOU 4798  N   ALA A 610     7130   2594   3220   -380   2091   -220       N  
ATOM   4799  CA  ALA A 610      28.173 116.791 -10.812  1.00 34.51           C  
ANISOU 4799  CA  ALA A 610     7215   2678   3220   -394   2082   -239       C  
ATOM   4800  C   ALA A 610      28.336 115.277 -10.780  1.00 34.62           C  
ANISOU 4800  C   ALA A 610     7323   2670   3163   -415   2166   -274       C  
ATOM   4801  O   ALA A 610      27.433 114.541 -11.197  1.00 35.08           O  
ANISOU 4801  O   ALA A 610     7397   2729   3203   -460   2174   -349       O  
ATOM   4802  CB  ALA A 610      28.951 117.390 -11.983  1.00 34.63           C  
ANISOU 4802  CB  ALA A 610     7228   2731   3201   -350   2032   -145       C  
ATOM   4803  N   LEU A 611      29.479 114.793 -10.289  1.00 34.32           N  
ANISOU 4803  N   LEU A 611     7345   2606   3087   -382   2223   -225       N  
ATOM   4804  CA  LEU A 611      29.723 113.355 -10.276  1.00 34.54           C  
ANISOU 4804  CA  LEU A 611     7442   2600   3083   -390   2262   -245       C  
ATOM   4805  C   LEU A 611      28.876 112.658  -9.217  1.00 34.69           C  
ANISOU 4805  C   LEU A 611     7467   2572   3142   -457   2295   -304       C  
ATOM   4806  O   LEU A 611      28.419 111.528  -9.429  1.00 35.17           O  
ANISOU 4806  O   LEU A 611     7572   2602   3190   -499   2315   -345       O  
ATOM   4807  CB  LEU A 611      31.209 113.076 -10.057  1.00 34.29           C  
ANISOU 4807  CB  LEU A 611     7417   2556   3055   -322   2252   -171       C  
ATOM   4808  CG  LEU A 611      32.151 113.656 -11.116  1.00 34.31           C  
ANISOU 4808  CG  LEU A 611     7398   2618   3018   -262   2225   -106       C  
ATOM   4809  CD1 LEU A 611      33.580 113.192 -10.881  1.00 34.21           C  
ANISOU 4809  CD1 LEU A 611     7385   2603   3011   -195   2221    -59       C  
ATOM   4810  CD2 LEU A 611      31.685 113.302 -12.522  1.00 34.86           C  
ANISOU 4810  CD2 LEU A 611     7495   2731   3019   -271   2218   -134       C  
ATOM   4811  N   ASN A 612      28.659 113.310  -8.070  1.00 34.40           N  
ANISOU 4811  N   ASN A 612     7390   2533   3149   -470   2306   -308       N  
ATOM   4812  CA  ASN A 612      27.743 112.756  -7.077  1.00 34.70           C  
ANISOU 4812  CA  ASN A 612     7422   2548   3214   -542   2344   -362       C  
ATOM   4813  C   ASN A 612      26.336 112.630  -7.645  1.00 35.24           C  
ANISOU 4813  C   ASN A 612     7470   2637   3283   -612   2354   -459       C  
ATOM   4814  O   ASN A 612      25.636 111.647  -7.377  1.00 35.77           O  
ANISOU 4814  O   ASN A 612     7561   2678   3353   -686   2393   -504       O  
ATOM   4815  CB  ASN A 612      27.734 113.619  -5.815  1.00 34.40           C  
ANISOU 4815  CB  ASN A 612     7331   2525   3214   -535   2348   -361       C  
ATOM   4816  CG  ASN A 612      28.940 113.375  -4.930  1.00 34.08           C  
ANISOU 4816  CG  ASN A 612     7318   2455   3178   -485   2344   -289       C  
ATOM   4817  OD1 ASN A 612      29.640 112.373  -5.076  1.00 34.18           O  
ANISOU 4817  OD1 ASN A 612     7392   2424   3172   -465   2346   -252       O  
ATOM   4818  ND2 ASN A 612      29.182 114.288  -3.996  1.00 33.80           N  
ANISOU 4818  ND2 ASN A 612     7238   2440   3164   -459   2336   -282       N  
ATOM   4819  N   THR A 613      25.906 113.618  -8.433  1.00 35.22           N  
ANISOU 4819  N   THR A 613     7405   2680   3299   -592   2296   -485       N  
ATOM   4820  CA  THR A 613      24.616 113.520  -9.108  1.00 35.83           C  
ANISOU 4820  CA  THR A 613     7428   2785   3399   -646   2261   -569       C  
ATOM   4821  C   THR A 613      24.606 112.366 -10.102  1.00 36.29           C  
ANISOU 4821  C   THR A 613     7565   2823   3400   -667   2277   -592       C  
ATOM   4822  O   THR A 613      23.624 111.619 -10.189  1.00 36.93           O  
ANISOU 4822  O   THR A 613     7646   2895   3491   -743   2296   -674       O  
ATOM   4823  CB  THR A 613      24.291 114.838  -9.814  1.00 35.80           C  
ANISOU 4823  CB  THR A 613     7327   2833   3441   -604   2159   -564       C  
ATOM   4824  OG1 THR A 613      24.186 115.889  -8.845  1.00 35.52           O  
ANISOU 4824  OG1 THR A 613     7216   2807   3473   -585   2138   -564       O  
ATOM   4825  CG2 THR A 613      22.981 114.729 -10.582  1.00 36.51           C  
ANISOU 4825  CG2 THR A 613     7360   2960   3553   -649   2112   -654       C  
ATOM   4826  N   PHE A 614      25.698 112.197 -10.852  1.00 36.08           N  
ANISOU 4826  N   PHE A 614     7602   2793   3313   -602   2269   -527       N  
ATOM   4827  CA  PHE A 614      25.766 111.125 -11.840  1.00 36.61           C  
ANISOU 4827  CA  PHE A 614     7745   2846   3320   -607   2278   -558       C  
ATOM   4828  C   PHE A 614      25.667 109.757 -11.176  1.00 36.98           C  
ANISOU 4828  C   PHE A 614     7846   2823   3383   -665   2329   -575       C  
ATOM   4829  O   PHE A 614      24.847 108.920 -11.572  1.00 37.71           O  
ANISOU 4829  O   PHE A 614     7961   2894   3474   -729   2336   -655       O  
ATOM   4830  CB  PHE A 614      27.061 111.239 -12.647  1.00 36.38           C  
ANISOU 4830  CB  PHE A 614     7754   2842   3228   -519   2261   -478       C  
ATOM   4831  CG  PHE A 614      27.221 110.167 -13.688  1.00 37.01           C  
ANISOU 4831  CG  PHE A 614     7888   2922   3254   -509   2251   -508       C  
ATOM   4832  CD1 PHE A 614      27.952 109.021 -13.419  1.00 37.17           C  
ANISOU 4832  CD1 PHE A 614     7960   2886   3276   -494   2273   -484       C  
ATOM   4833  CD2 PHE A 614      26.634 110.304 -14.934  1.00 37.57           C  
ANISOU 4833  CD2 PHE A 614     7956   3047   3270   -509   2211   -566       C  
ATOM   4834  CE1 PHE A 614      28.095 108.033 -14.374  1.00 37.87           C  
ANISOU 4834  CE1 PHE A 614     8099   2972   3317   -477   2261   -525       C  
ATOM   4835  CE2 PHE A 614      26.775 109.321 -15.894  1.00 38.25           C  
ANISOU 4835  CE2 PHE A 614     8094   3140   3300   -494   2201   -609       C  
ATOM   4836  CZ  PHE A 614      27.504 108.183 -15.613  1.00 38.41           C  
ANISOU 4836  CZ  PHE A 614     8161   3102   3330   -478   2225   -590       C  
ATOM   4837  N   THR A 615      26.499 109.511 -10.160  1.00 36.60           N  
ANISOU 4837  N   THR A 615     7822   2733   3352   -644   2358   -500       N  
ATOM   4838  CA  THR A 615      26.505 108.208  -9.504  1.00 37.06           C  
ANISOU 4838  CA  THR A 615     7954   2713   3415   -693   2407   -499       C  
ATOM   4839  C   THR A 615      25.193 107.934  -8.778  1.00 37.58           C  
ANISOU 4839  C   THR A 615     8004   2762   3514   -807   2457   -571       C  
ATOM   4840  O   THR A 615      24.739 106.784  -8.736  1.00 38.35           O  
ANISOU 4840  O   THR A 615     8167   2798   3607   -878   2497   -610       O  
ATOM   4841  CB  THR A 615      27.686 108.117  -8.535  1.00 36.60           C  
ANISOU 4841  CB  THR A 615     7929   2615   3364   -636   2420   -406       C  
ATOM   4842  OG1 THR A 615      28.909 108.319  -9.255  1.00 36.27           O  
ANISOU 4842  OG1 THR A 615     7891   2593   3295   -535   2378   -352       O  
ATOM   4843  CG2 THR A 615      27.732 106.753  -7.857  1.00 37.22           C  
ANISOU 4843  CG2 THR A 615     8110   2599   3433   -681   2476   -398       C  
ATOM   4844  N   ASN A 616      24.562 108.969  -8.217  1.00 37.30           N  
ANISOU 4844  N   ASN A 616     7882   2780   3511   -827   2457   -597       N  
ATOM   4845  CA  ASN A 616      23.295 108.761  -7.522  1.00 37.91           C  
ANISOU 4845  CA  ASN A 616     7927   2859   3618   -935   2510   -677       C  
ATOM   4846  C   ASN A 616      22.184 108.396  -8.499  1.00 38.67           C  
ANISOU 4846  C   ASN A 616     8006   2964   3724  -1003   2496   -789       C  
ATOM   4847  O   ASN A 616      21.308 107.585  -8.176  1.00 39.51           O  
ANISOU 4847  O   ASN A 616     8128   3036   3848  -1111   2549   -853       O  
ATOM   4848  CB  ASN A 616      22.925 110.006  -6.718  1.00 37.52           C  
ANISOU 4848  CB  ASN A 616     7777   2876   3602   -925   2508   -691       C  
ATOM   4849  CG  ASN A 616      22.026 109.690  -5.539  1.00 38.11           C  
ANISOU 4849  CG  ASN A 616     7830   2957   3694  -1025   2586   -737       C  
ATOM   4850  OD1 ASN A 616      21.752 108.525  -5.249  1.00 38.81           O  
ANISOU 4850  OD1 ASN A 616     7994   2987   3766  -1109   2652   -745       O  
ATOM   4851  ND2 ASN A 616      21.570 110.728  -4.845  1.00 37.96           N  
ANISOU 4851  ND2 ASN A 616     7711   3008   3704  -1017   2585   -772       N  
ATOM   4852  N   LEU A 617      22.200 108.988  -9.696  1.00 38.51           N  
ANISOU 4852  N   LEU A 617     7949   2991   3693   -944   2419   -811       N  
ATOM   4853  CA  LEU A 617      21.268 108.577 -10.742  1.00 39.31           C  
ANISOU 4853  CA  LEU A 617     8020   3110   3805   -994   2374   -903       C  
ATOM   4854  C   LEU A 617      21.480 107.114 -11.111  1.00 39.97           C  
ANISOU 4854  C   LEU A 617     8224   3107   3856  -1033   2411   -927       C  
ATOM   4855  O   LEU A 617      20.521 106.342 -11.224  1.00 40.91           O  
ANISOU 4855  O   LEU A 617     8339   3198   4005  -1134   2424  -1012       O  
ATOM   4856  CB  LEU A 617      21.432 109.466 -11.976  1.00 39.07           C  
ANISOU 4856  CB  LEU A 617     7938   3151   3754   -909   2276   -896       C  
ATOM   4857  CG  LEU A 617      21.023 110.938 -11.897  1.00 38.70           C  
ANISOU 4857  CG  LEU A 617     7767   3183   3755   -871   2209   -887       C  
ATOM   4858  CD1 LEU A 617      21.473 111.674 -13.150  1.00 38.54           C  
ANISOU 4858  CD1 LEU A 617     7735   3214   3696   -782   2118   -845       C  
ATOM   4859  CD2 LEU A 617      19.524 111.075 -11.708  1.00 39.42           C  
ANISOU 4859  CD2 LEU A 617     7746   3316   3916   -951   2189   -995       C  
ATOM   4860  N   VAL A 618      22.742 106.719 -11.306  1.00 39.60           N  
ANISOU 4860  N   VAL A 618     8251   3030   3766   -952   2404   -836       N  
ATOM   4861  CA  VAL A 618      23.064 105.333 -11.633  1.00 40.29           C  
ANISOU 4861  CA  VAL A 618     8433   3041   3836   -968   2417   -840       C  
ATOM   4862  C   VAL A 618      22.576 104.392 -10.541  1.00 40.93           C  
ANISOU 4862  C   VAL A 618     8565   3034   3952  -1077   2494   -848       C  
ATOM   4863  O   VAL A 618      22.138 103.270 -10.824  1.00 41.93           O  
ANISOU 4863  O   VAL A 618     8746   3094   4091  -1146   2504   -903       O  
ATOM   4864  CB  VAL A 618      24.582 105.190 -11.870  1.00 39.78           C  
ANISOU 4864  CB  VAL A 618     8426   2966   3723   -850   2401   -741       C  
ATOM   4865  CG1 VAL A 618      24.963 103.733 -12.086  1.00 40.59           C  
ANISOU 4865  CG1 VAL A 618     8629   2982   3811   -854   2413   -750       C  
ATOM   4866  CG2 VAL A 618      25.013 106.036 -13.057  1.00 39.41           C  
ANISOU 4866  CG2 VAL A 618     8336   3006   3630   -758   2335   -738       C  
ATOM   4867  N   VAL A 619      22.618 104.837  -9.286  1.00 40.49           N  
ANISOU 4867  N   VAL A 619     8496   2979   3909  -1097   2551   -796       N  
ATOM   4868  CA  VAL A 619      22.186 103.991  -8.178  1.00 41.19           C  
ANISOU 4868  CA  VAL A 619     8648   2988   4014  -1205   2638   -794       C  
ATOM   4869  C   VAL A 619      20.677 103.774  -8.223  1.00 42.15           C  
ANISOU 4869  C   VAL A 619     8718   3112   4186  -1347   2665   -913       C  
ATOM   4870  O   VAL A 619      20.194 102.640  -8.128  1.00 43.24           O  
ANISOU 4870  O   VAL A 619     8917   3166   4345  -1450   2701   -944       O  
ATOM   4871  CB  VAL A 619      22.634 104.602  -6.839  1.00 40.54           C  
ANISOU 4871  CB  VAL A 619     8565   2921   3919  -1183   2691   -716       C  
ATOM   4872  CG1 VAL A 619      21.836 104.015  -5.699  1.00 41.40           C  
ANISOU 4872  CG1 VAL A 619     8718   2975   4036  -1317   2794   -741       C  
ATOM   4873  CG2 VAL A 619      24.118 104.363  -6.625  1.00 39.99           C  
ANISOU 4873  CG2 VAL A 619     8576   2811   3809  -1073   2678   -602       C  
ATOM   4874  N   GLN A 620      19.908 104.857  -8.376  1.00 41.88           N  
ANISOU 4874  N   GLN A 620     8549   3182   4181  -1353   2633   -972       N  
ATOM   4875  CA  GLN A 620      18.454 104.727  -8.380  1.00 42.86           C  
ANISOU 4875  CA  GLN A 620     8571   3347   4366  -1480   2639  -1072       C  
ATOM   4876  C   GLN A 620      17.950 104.081  -9.664  1.00 43.66           C  
ANISOU 4876  C   GLN A 620     8679   3426   4484  -1513   2579  -1165       C  
ATOM   4877  O   GLN A 620      16.865 103.487  -9.674  1.00 44.79           O  
ANISOU 4877  O   GLN A 620     8780   3560   4679  -1642   2595  -1247       O  
ATOM   4878  CB  GLN A 620      17.804 106.095  -8.176  1.00 42.43           C  
ANISOU 4878  CB  GLN A 620     8351   3424   4346  -1457   2604  -1105       C  
ATOM   4879  CG  GLN A 620      18.369 106.872  -7.005  1.00 41.62           C  
ANISOU 4879  CG  GLN A 620     8235   3353   4225  -1404   2646  -1026       C  
ATOM   4880  CD  GLN A 620      18.273 106.114  -5.694  1.00 42.19           C  
ANISOU 4880  CD  GLN A 620     8367   3378   4285  -1501   2757   -987       C  
ATOM   4881  OE1 GLN A 620      17.242 105.518  -5.381  1.00 43.29           O  
ANISOU 4881  OE1 GLN A 620     8470   3520   4459  -1635   2809  -1043       O  
ATOM   4882  NE2 GLN A 620      19.351 106.134  -4.920  1.00 41.55           N  
ANISOU 4882  NE2 GLN A 620     8377   3257   4153  -1436   2794   -886       N  
ATOM   4883  N   LEU A 621      18.712 104.194 -10.754  1.00 43.19           N  
ANISOU 4883  N   LEU A 621     8668   3366   4378  -1402   2509  -1158       N  
ATOM   4884  CA  LEU A 621      18.361 103.490 -11.982  1.00 44.04           C  
ANISOU 4884  CA  LEU A 621     8800   3451   4484  -1421   2451  -1249       C  
ATOM   4885  C   LEU A 621      18.502 101.982 -11.805  1.00 45.01           C  
ANISOU 4885  C   LEU A 621     9032   3450   4620  -1491   2489  -1242       C  
ATOM   4886  O   LEU A 621      17.711 101.207 -12.357  1.00 46.18           O  
ANISOU 4886  O   LEU A 621     9177   3564   4807  -1580   2466  -1340       O  
ATOM   4887  CB  LEU A 621      19.237 103.993 -13.130  1.00 43.39           C  
ANISOU 4887  CB  LEU A 621     8733   3420   4333  -1276   2371  -1223       C  
ATOM   4888  CG  LEU A 621      18.549 104.415 -14.431  1.00 43.82           C  
ANISOU 4888  CG  LEU A 621     8708   3563   4380  -1257   2273  -1318       C  
ATOM   4889  CD1 LEU A 621      17.181 105.024 -14.165  1.00 44.23           C  
ANISOU 4889  CD1 LEU A 621     8607   3692   4505  -1340   2250  -1388       C  
ATOM   4890  CD2 LEU A 621      19.433 105.382 -15.205  1.00 42.95           C  
ANISOU 4890  CD2 LEU A 621     8590   3532   4196  -1113   2212  -1252       C  
ATOM   4891  N   ILE A 622      19.495 101.551 -11.025  1.00 44.64           N  
ANISOU 4891  N   ILE A 622     9078   3338   4547  -1450   2539  -1126       N  
ATOM   4892  CA  ILE A 622      19.674 100.128 -10.758  1.00 45.66           C  
ANISOU 4892  CA  ILE A 622     9312   3347   4688  -1505   2569  -1104       C  
ATOM   4893  C   ILE A 622      18.623  99.633  -9.772  1.00 46.65           C  
ANISOU 4893  C   ILE A 622     9432   3421   4873  -1679   2650  -1129       C  
ATOM   4894  O   ILE A 622      18.091  98.525  -9.916  1.00 47.99           O  
ANISOU 4894  O   ILE A 622     9638   3512   5085  -1779   2652  -1173       O  
ATOM   4895  CB  ILE A 622      21.103  99.860 -10.250  1.00 45.03           C  
ANISOU 4895  CB  ILE A 622     9332   3223   4554  -1393   2588   -976       C  
ATOM   4896  CG1 ILE A 622      22.124 100.170 -11.347  1.00 44.36           C  
ANISOU 4896  CG1 ILE A 622     9249   3187   4417  -1238   2510   -961       C  
ATOM   4897  CG2 ILE A 622      21.245  98.420  -9.772  1.00 46.19           C  
ANISOU 4897  CG2 ILE A 622     9590   3246   4715  -1448   2620   -946       C  
ATOM   4898  CD1 ILE A 622      23.563 100.140 -10.875  1.00 43.64           C  
ANISOU 4898  CD1 ILE A 622     9227   3077   4277  -1119   2524   -842       C  
ATOM   4899  N   ARG A 623      18.301 100.443  -8.759  1.00 46.15           N  
ANISOU 4899  N   ARG A 623     9317   3402   4814  -1722   2717  -1104       N  
ATOM   4900  CA  ARG A 623      17.321 100.020  -7.764  1.00 47.18           C  
ANISOU 4900  CA  ARG A 623     9435   3499   4994  -1895   2807  -1120       C  
ATOM   4901  C   ARG A 623      15.939  99.841  -8.381  1.00 48.31           C  
ANISOU 4901  C   ARG A 623     9475   3670   5210  -2027   2785  -1258       C  
ATOM   4902  O   ARG A 623      15.154  99.009  -7.913  1.00 49.67           O  
ANISOU 4902  O   ARG A 623     9655   3783   5434  -2190   2843  -1280       O  
ATOM   4903  CB  ARG A 623      17.277 101.023  -6.610  1.00 46.44           C  
ANISOU 4903  CB  ARG A 623     9268   3496   4881  -1889   2868  -1063       C  
ATOM   4904  CG  ARG A 623      16.293 100.655  -5.511  1.00 47.58           C  
ANISOU 4904  CG  ARG A 623     9369   3650   5060  -2059   2965  -1061       C  
ATOM   4905  CD  ARG A 623      16.604 101.367  -4.207  1.00 46.96           C  
ANISOU 4905  CD  ARG A 623     9266   3642   4933  -2029   3032   -975       C  
ATOM   4906  NE  ARG A 623      15.399 101.583  -3.412  1.00 47.86           N  
ANISOU 4906  NE  ARG A 623     9251   3856   5079  -2166   3104  -1016       N  
ATOM   4907  CZ  ARG A 623      15.387 101.712  -2.090  1.00 48.09           C  
ANISOU 4907  CZ  ARG A 623     9280   3925   5067  -2208   3196   -947       C  
ATOM   4908  NH1 ARG A 623      16.518 101.630  -1.403  1.00 47.46           N1+
ANISOU 4908  NH1 ARG A 623     9329   3788   4916  -2124   3220   -830       N1+
ATOM   4909  NH2 ARG A 623      14.241 101.910  -1.453  1.00 49.05           N  
ANISOU 4909  NH2 ARG A 623     9270   4155   5214  -2333   3263   -999       N  
ATOM   4910  N   ASN A 624      15.623 100.601  -9.431  1.00 47.89           N  
ANISOU 4910  N   ASN A 624     9313   3721   5161  -1959   2693  -1343       N  
ATOM   4911  CA  ASN A 624      14.394 100.345 -10.175  1.00 49.06           C  
ANISOU 4911  CA  ASN A 624     9360   3905   5374  -2062   2647  -1478       C  
ATOM   4912  C   ASN A 624      14.444  99.001 -10.889  1.00 50.22           C  
ANISOU 4912  C   ASN A 624     9622   3917   5541  -2116   2621  -1528       C  
ATOM   4913  O   ASN A 624      13.418  98.322 -10.998  1.00 51.66           O  
ANISOU 4913  O   ASN A 624     9762   4071   5796  -2266   2626  -1616       O  
ATOM   4914  CB  ASN A 624      14.137 101.470 -11.178  1.00 48.39           C  
ANISOU 4914  CB  ASN A 624     9147   3961   5279  -1957   2541  -1546       C  
ATOM   4915  CG  ASN A 624      13.465 102.678 -10.546  1.00 47.97           C  
ANISOU 4915  CG  ASN A 624     8925   4048   5251  -1958   2552  -1552       C  
ATOM   4916  OD1 ASN A 624      12.624 102.540  -9.658  1.00 48.73           O  
ANISOU 4916  OD1 ASN A 624     8948   4171   5398  -2085   2625  -1572       O  
ATOM   4917  ND2 ASN A 624      13.826 103.867 -11.011  1.00 46.87           N  
ANISOU 4917  ND2 ASN A 624     8724   4003   5080  -1817   2477  -1535       N  
ATOM   4918  N   MET A 625      15.623  98.596 -11.366  1.00 49.73           N  
ANISOU 4918  N   MET A 625     9665   3807   5421  -1979   2575  -1456       N  
ATOM   4919  CA  MET A 625      15.740  97.314 -12.054  1.00 50.90           C  
ANISOU 4919  CA  MET A 625     9890   3862   5589  -1992   2525  -1488       C  
ATOM   4920  C   MET A 625      15.532  96.146 -11.099  1.00 52.14           C  
ANISOU 4920  C   MET A 625    10120   3900   5793  -2119   2597  -1432       C  
ATOM   4921  O   MET A 625      14.822  95.190 -11.430  1.00 53.70           O  
ANISOU 4921  O   MET A 625    10317   4030   6055  -2230   2575  -1506       O  
ATOM   4922  CB  MET A 625      17.099  97.207 -12.744  1.00 50.13           C  
ANISOU 4922  CB  MET A 625     9879   3753   5417  -1809   2465  -1431       C  
ATOM   4923  CG  MET A 625      17.076  97.617 -14.203  1.00 50.00           C  
ANISOU 4923  CG  MET A 625     9814   3817   5367  -1719   2361  -1529       C  
ATOM   4924  SD  MET A 625      18.688  97.487 -14.997  1.00 49.28           S  
ANISOU 4924  SD  MET A 625     9813   3728   5182  -1514   2304  -1464       S  
ATOM   4925  CE  MET A 625      19.580  98.781 -14.142  1.00 47.39           C  
ANISOU 4925  CE  MET A 625     9556   3563   4888  -1416   2359  -1321       C  
ATOM   4926  N   GLU A 626      16.146  96.199  -9.914  1.00 51.60           N  
ANISOU 4926  N   GLU A 626    10113   3805   5689  -2103   2677  -1301       N  
ATOM   4927  CA  GLU A 626      15.945  95.135  -8.935  1.00 52.88           C  
ANISOU 4927  CA  GLU A 626    10344   3868   5881  -2218   2743  -1234       C  
ATOM   4928  C   GLU A 626      14.494  95.063  -8.481  1.00 54.11           C  
ANISOU 4928  C   GLU A 626    10399   4048   6112  -2424   2803  -1300       C  
ATOM   4929  O   GLU A 626      13.981  93.972  -8.208  1.00 55.76           O  
ANISOU 4929  O   GLU A 626    10639   4173   6375  -2549   2822  -1297       O  
ATOM   4930  CB  GLU A 626      16.867  95.343  -7.733  1.00 52.05           C  
ANISOU 4930  CB  GLU A 626    10312   3758   5706  -2147   2810  -1086       C  
ATOM   4931  CG  GLU A 626      16.742  94.268  -6.663  1.00 53.43           C  
ANISOU 4931  CG  GLU A 626    10564   3845   5893  -2245   2867  -1003       C  
ATOM   4932  CD  GLU A 626      17.653  94.509  -5.476  1.00 52.67           C  
ANISOU 4932  CD  GLU A 626    10533   3762   5718  -2160   2917   -869       C  
ATOM   4933  OE1 GLU A 626      18.638  95.261  -5.627  1.00 51.13           O  
ANISOU 4933  OE1 GLU A 626    10353   3613   5463  -2005   2893   -835       O  
ATOM   4934  OE2 GLU A 626      17.381  93.949  -4.392  1.00 53.71           O1+
ANISOU 4934  OE2 GLU A 626    10696   3864   5848  -2248   2974   -801       O1+
ATOM   4935  N   ALA A 627      13.813  96.207  -8.412  1.00 53.45           N  
ANISOU 4935  N   ALA A 627    10189   4080   6039  -2463   2830  -1364       N  
ATOM   4936  CA  ALA A 627      12.422  96.242  -7.983  1.00 54.63           C  
ANISOU 4936  CA  ALA A 627    10218   4275   6263  -2661   2891  -1439       C  
ATOM   4937  C   ALA A 627      11.459  95.755  -9.054  1.00 55.92           C  
ANISOU 4937  C   ALA A 627    10307   4432   6507  -2752   2819  -1589       C  
ATOM   4938  O   ALA A 627      10.353  95.322  -8.717  1.00 57.43           O  
ANISOU 4938  O   ALA A 627    10418   4630   6774  -2936   2866  -1641       O  
ATOM   4939  CB  ALA A 627      12.039  97.661  -7.565  1.00 53.57           C  
ANISOU 4939  CB  ALA A 627     9956   4280   6118  -2653   2931  -1469       C  
ATOM   4940  N   GLU A 628      11.842  95.825 -10.328  1.00 55.46           N  
ANISOU 4940  N   GLU A 628    10265   4374   6432  -2629   2705  -1661       N  
ATOM   4941  CA  GLU A 628      10.995  95.378 -11.424  1.00 56.70           C  
ANISOU 4941  CA  GLU A 628    10354   4533   6655  -2696   2619  -1812       C  
ATOM   4942  C   GLU A 628      11.335  93.968 -11.889  1.00 57.95           C  
ANISOU 4942  C   GLU A 628    10626   4553   6838  -2698   2567  -1804       C  
ATOM   4943  O   GLU A 628      10.869  93.548 -12.953  1.00 58.90           O  
ANISOU 4943  O   GLU A 628    10714   4665   7001  -2715   2475  -1930       O  
ATOM   4944  CB  GLU A 628      11.090  96.358 -12.595  1.00 55.65           C  
ANISOU 4944  CB  GLU A 628    10158   4507   6481  -2559   2516  -1910       C  
ATOM   4945  CG  GLU A 628      10.592  97.754 -12.258  1.00 54.70           C  
ANISOU 4945  CG  GLU A 628     9890   4542   6352  -2544   2535  -1933       C  
ATOM   4946  CD  GLU A 628      10.857  98.756 -13.363  1.00 53.64           C  
ANISOU 4946  CD  GLU A 628     9692   4530   6159  -2369   2418  -1979       C  
ATOM   4947  OE1 GLU A 628      11.059  98.330 -14.519  1.00 54.01           O  
ANISOU 4947  OE1 GLU A 628     9795   4542   6185  -2317   2329  -2054       O  
ATOM   4948  OE2 GLU A 628      10.867  99.972 -13.072  1.00 52.53           O1+
ANISOU 4948  OE2 GLU A 628     9449   4518   5992  -2285   2413  -1938       O1+
ATOM   4949  N   GLU A 629      12.147  93.239 -11.119  1.00 58.05           N  
ANISOU 4949  N   GLU A 629    10770   4460   6825  -2672   2615  -1665       N  
ATOM   4950  CA  GLU A 629      12.469  91.834 -11.369  1.00 59.45           C  
ANISOU 4950  CA  GLU A 629    11061   4488   7037  -2681   2570  -1650       C  
ATOM   4951  C   GLU A 629      13.286  91.636 -12.642  1.00 59.05           C  
ANISOU 4951  C   GLU A 629    11073   4414   6950  -2512   2454  -1707       C  
ATOM   4952  O   GLU A 629      13.186  90.596 -13.297  1.00 60.48           O  
ANISOU 4952  O   GLU A 629    11300   4496   7183  -2532   2383  -1775       O  
ATOM   4953  CB  GLU A 629      11.204  90.971 -11.408  1.00 61.64           C  
ANISOU 4953  CB  GLU A 629    11277   4713   7428  -2886   2569  -1736       C  
ATOM   4954  CG  GLU A 629      10.376  91.056 -10.137  1.00 62.33           C  
ANISOU 4954  CG  GLU A 629    11297   4834   7550  -3063   2691  -1676       C  
ATOM   4955  CD  GLU A 629       9.128  90.203 -10.192  1.00 64.63           C  
ANISOU 4955  CD  GLU A 629    11515   5084   7958  -3272   2691  -1757       C  
ATOM   4956  OE1 GLU A 629       8.317  90.280  -9.244  1.00 65.43           O  
ANISOU 4956  OE1 GLU A 629    11536   5235   8091  -3432   2791  -1724       O  
ATOM   4957  OE2 GLU A 629       8.956  89.457 -11.180  1.00 65.74           O1+
ANISOU 4957  OE2 GLU A 629    11673   5148   8157  -3276   2591  -1857       O1+
ATOM   4958  N   VAL A 630      14.102  92.626 -13.007  1.00 57.24           N  
ANISOU 4958  N   VAL A 630    10842   4276   6631  -2345   2433  -1683       N  
ATOM   4959  CA  VAL A 630      15.080  92.419 -14.070  1.00 56.86           C  
ANISOU 4959  CA  VAL A 630    10863   4214   6528  -2172   2340  -1709       C  
ATOM   4960  C   VAL A 630      16.324  91.732 -13.519  1.00 56.70           C  
ANISOU 4960  C   VAL A 630    10983   4089   6471  -2075   2360  -1581       C  
ATOM   4961  O   VAL A 630      16.873  90.816 -14.143  1.00 57.52           O  
ANISOU 4961  O   VAL A 630    11169   4105   6582  -2005   2293  -1612       O  
ATOM   4962  CB  VAL A 630      15.426  93.756 -14.751  1.00 55.19           C  
ANISOU 4962  CB  VAL A 630    10583   4153   6234  -2038   2304  -1733       C  
ATOM   4963  CG1 VAL A 630      16.481  93.550 -15.830  1.00 54.90           C  
ANISOU 4963  CG1 VAL A 630    10613   4119   6128  -1861   2219  -1752       C  
ATOM   4964  CG2 VAL A 630      14.178  94.397 -15.336  1.00 55.53           C  
ANISOU 4964  CG2 VAL A 630    10488   4299   6312  -2125   2267  -1871       C  
ATOM   4965  N   LEU A 631      16.778  92.154 -12.344  1.00 55.75           N  
ANISOU 4965  N   LEU A 631    10891   3980   6313  -2065   2448  -1445       N  
ATOM   4966  CA  LEU A 631      17.918  91.552 -11.670  1.00 55.65           C  
ANISOU 4966  CA  LEU A 631    11004   3878   6263  -1977   2470  -1319       C  
ATOM   4967  C   LEU A 631      17.438  90.677 -10.519  1.00 57.02           C  
ANISOU 4967  C   LEU A 631    11228   3947   6491  -2122   2534  -1249       C  
ATOM   4968  O   LEU A 631      16.543  91.062  -9.760  1.00 57.18           O  
ANISOU 4968  O   LEU A 631    11177   4014   6534  -2259   2610  -1234       O  
ATOM   4969  CB  LEU A 631      18.873  92.628 -11.146  1.00 53.71           C  
ANISOU 4969  CB  LEU A 631    10759   3724   5926  -1848   2512  -1213       C  
ATOM   4970  CG  LEU A 631      19.372  93.645 -12.174  1.00 52.32           C  
ANISOU 4970  CG  LEU A 631    10525   3666   5690  -1708   2457  -1259       C  
ATOM   4971  CD1 LEU A 631      20.259  94.685 -11.508  1.00 50.59           C  
ANISOU 4971  CD1 LEU A 631    10301   3525   5397  -1603   2503  -1145       C  
ATOM   4972  CD2 LEU A 631      20.111  92.951 -13.310  1.00 52.82           C  
ANISOU 4972  CD2 LEU A 631    10647   3687   5736  -1589   2366  -1315       C  
ATOM   4973  N   GLU A 632      18.036  89.499 -10.399  1.00 58.14           N  
ANISOU 4973  N   GLU A 632    11488   3949   6652  -2088   2501  -1206       N  
ATOM   4974  CA  GLU A 632      17.709  88.530  -9.366  1.00 59.69           C  
ANISOU 4974  CA  GLU A 632    11750   4030   6897  -2209   2544  -1127       C  
ATOM   4975  C   GLU A 632      18.813  88.512  -8.311  1.00 59.03           C  
ANISOU 4975  C   GLU A 632    11763   3925   6740  -2107   2583   -976       C  
ATOM   4976  O   GLU A 632      19.658  89.412  -8.249  1.00 57.27           O  
ANISOU 4976  O   GLU A 632    11531   3795   6433  -1970   2596   -934       O  
ATOM   4977  CB  GLU A 632      17.495  87.153  -9.999  1.00 61.74           C  
ANISOU 4977  CB  GLU A 632    12075   4133   7249  -2254   2463  -1198       C  
ATOM   4978  CG  GLU A 632      16.357  87.117 -11.012  1.00 62.59           C  
ANISOU 4978  CG  GLU A 632    12084   4263   7434  -2362   2416  -1358       C  
ATOM   4979  CD  GLU A 632      16.593  86.120 -12.131  1.00 63.88           C  
ANISOU 4979  CD  GLU A 632    12305   4313   7653  -2305   2299  -1466       C  
ATOM   4980  OE1 GLU A 632      17.475  86.372 -12.980  1.00 62.95           O  
ANISOU 4980  OE1 GLU A 632    12209   4232   7476  -2131   2238  -1510       O  
ATOM   4981  OE2 GLU A 632      15.899  85.082 -12.160  1.00 65.93           O1+
ANISOU 4981  OE2 GLU A 632    12586   4449   8017  -2434   2269  -1509       O1+
ATOM   4982  N   MET A 633      18.808  87.478  -7.471  1.00 61.13           N  
ANISOU 4982  N   MET A 633    12118   4068   7039  -2174   2597   -895       N  
ATOM   4983  CA  MET A 633      19.831  87.365  -6.438  1.00 60.76           C  
ANISOU 4983  CA  MET A 633    12166   3995   6924  -2077   2621   -757       C  
ATOM   4984  C   MET A 633      21.084  86.652  -6.929  1.00 60.94           C  
ANISOU 4984  C   MET A 633    12301   3916   6938  -1909   2536   -748       C  
ATOM   4985  O   MET A 633      22.173  86.888  -6.391  1.00 60.04           O  
ANISOU 4985  O   MET A 633    12242   3822   6749  -1775   2542   -660       O  
ATOM   4986  CB  MET A 633      19.273  86.648  -5.206  1.00 62.39           C  
ANISOU 4986  CB  MET A 633    12416   4130   7160  -2221   2674   -660       C  
ATOM   4987  CG  MET A 633      18.775  85.239  -5.460  1.00 64.80           C  
ANISOU 4987  CG  MET A 633    12785   4261   7575  -2329   2621   -684       C  
ATOM   4988  SD  MET A 633      18.446  84.379  -3.911  1.00 66.75           S  
ANISOU 4988  SD  MET A 633    13108   4417   7839  -2463   2675   -531       S  
ATOM   4989  CE  MET A 633      17.604  85.662  -2.990  1.00 65.64           C  
ANISOU 4989  CE  MET A 633    12831   4480   7630  -2569   2802   -502       C  
ATOM   4990  N   GLN A 634      20.961  85.792  -7.942  1.00 61.61           N  
ANISOU 4990  N   GLN A 634    12415   3895   7098  -1909   2453   -846       N  
ATOM   4991  CA  GLN A 634      22.144  85.242  -8.593  1.00 61.71           C  
ANISOU 4991  CA  GLN A 634    12512   3832   7102  -1734   2368   -868       C  
ATOM   4992  C   GLN A 634      22.908  86.308  -9.366  1.00 59.68           C  
ANISOU 4992  C   GLN A 634    12197   3719   6762  -1575   2356   -910       C  
ATOM   4993  O   GLN A 634      24.111  86.149  -9.598  1.00 59.32           O  
ANISOU 4993  O   GLN A 634    12210   3655   6675  -1408   2313   -892       O  
ATOM   4994  CB  GLN A 634      21.737  84.098  -9.526  1.00 63.64           C  
ANISOU 4994  CB  GLN A 634    12791   3936   7454  -1776   2278   -983       C  
ATOM   4995  CG  GLN A 634      22.898  83.334 -10.149  1.00 64.21           C  
ANISOU 4995  CG  GLN A 634    12956   3908   7532  -1603   2185  -1018       C  
ATOM   4996  CD  GLN A 634      22.939  83.465 -11.661  1.00 64.01           C  
ANISOU 4996  CD  GLN A 634    12877   3930   7514  -1523   2111  -1181       C  
ATOM   4997  OE1 GLN A 634      22.737  84.550 -12.209  1.00 62.47           O  
ANISOU 4997  OE1 GLN A 634    12580   3896   7260  -1503   2135  -1229       O  
ATOM   4998  NE2 GLN A 634      23.198  82.355 -12.344  1.00 65.70           N  
ANISOU 4998  NE2 GLN A 634    13157   4004   7800  -1472   2015  -1271       N  
ATOM   4999  N   ASP A 635      22.239  87.402  -9.739  1.00 58.46           N  
ANISOU 4999  N   ASP A 635    11923   3706   6583  -1624   2393   -962       N  
ATOM   5000  CA  ASP A 635      22.857  88.417 -10.586  1.00 56.75           C  
ANISOU 5000  CA  ASP A 635    11644   3624   6297  -1486   2373  -1005       C  
ATOM   5001  C   ASP A 635      23.948  89.194  -9.860  1.00 55.16           C  
ANISOU 5001  C   ASP A 635    11457   3499   6003  -1362   2416   -888       C  
ATOM   5002  O   ASP A 635      24.856  89.724 -10.510  1.00 54.09           O  
ANISOU 5002  O   ASP A 635    11304   3436   5811  -1214   2386   -900       O  
ATOM   5003  CB  ASP A 635      21.788  89.375 -11.110  1.00 56.06           C  
ANISOU 5003  CB  ASP A 635    11427   3657   6215  -1578   2393  -1087       C  
ATOM   5004  CG  ASP A 635      21.069  88.832 -12.325  1.00 57.26           C  
ANISOU 5004  CG  ASP A 635    11548   3775   6433  -1626   2316  -1239       C  
ATOM   5005  OD1 ASP A 635      21.751  88.281 -13.213  1.00 57.73           O  
ANISOU 5005  OD1 ASP A 635    11654   3793   6489  -1509   2238  -1302       O  
ATOM   5006  OD2 ASP A 635      19.827  88.952 -12.395  1.00 57.82           O1+
ANISOU 5006  OD2 ASP A 635    11544   3865   6559  -1778   2332  -1304       O1+
ATOM   5007  N   LEU A 636      23.874  89.288  -8.530  1.00 55.08           N  
ANISOU 5007  N   LEU A 636    11472   3481   5974  -1420   2485   -778       N  
ATOM   5008  CA  LEU A 636      24.898  90.017  -7.786  1.00 53.67           C  
ANISOU 5008  CA  LEU A 636    11306   3376   5711  -1303   2520   -675       C  
ATOM   5009  C   LEU A 636      26.276  89.404  -7.994  1.00 53.88           C  
ANISOU 5009  C   LEU A 636    11424   3337   5712  -1136   2461   -647       C  
ATOM   5010  O   LEU A 636      27.278  90.122  -8.091  1.00 52.57           O  
ANISOU 5010  O   LEU A 636    11239   3254   5480   -999   2460   -615       O  
ATOM   5011  CB  LEU A 636      24.552  90.041  -6.296  1.00 53.91           C  
ANISOU 5011  CB  LEU A 636    11357   3401   5726  -1393   2593   -575       C  
ATOM   5012  CG  LEU A 636      23.505  91.033  -5.793  1.00 53.21           C  
ANISOU 5012  CG  LEU A 636    11163   3423   5631  -1517   2669   -581       C  
ATOM   5013  CD1 LEU A 636      23.133  90.692  -4.363  1.00 54.07           C  
ANISOU 5013  CD1 LEU A 636    11307   3503   5733  -1612   2728   -493       C  
ATOM   5014  CD2 LEU A 636      24.024  92.458  -5.875  1.00 51.18           C  
ANISOU 5014  CD2 LEU A 636    10830   3309   5308  -1417   2690   -571       C  
ATOM   5015  N   TRP A 637      26.344  88.075  -8.074  1.00 55.65           N  
ANISOU 5015  N   TRP A 637    11741   3408   5994  -1145   2409   -663       N  
ATOM   5016  CA  TRP A 637      27.625  87.386  -8.180  1.00 56.12           C  
ANISOU 5016  CA  TRP A 637    11892   3391   6041   -987   2349   -642       C  
ATOM   5017  C   TRP A 637      28.160  87.407  -9.609  1.00 55.92           C  
ANISOU 5017  C   TRP A 637    11836   3396   6015   -866   2283   -752       C  
ATOM   5018  O   TRP A 637      29.312  87.788  -9.843  1.00 55.06           O  
ANISOU 5018  O   TRP A 637    11724   3348   5847   -710   2267   -735       O  
ATOM   5019  CB  TRP A 637      27.474  85.952  -7.668  1.00 58.26           C  
ANISOU 5019  CB  TRP A 637    12278   3475   6385  -1042   2312   -616       C  
ATOM   5020  CG  TRP A 637      28.468  84.984  -8.219  1.00 59.34           C  
ANISOU 5020  CG  TRP A 637    12500   3498   6550   -901   2224   -655       C  
ATOM   5021  CD1 TRP A 637      29.808  84.952  -7.969  1.00 58.99           C  
ANISOU 5021  CD1 TRP A 637    12505   3454   6455   -732   2199   -604       C  
ATOM   5022  CD2 TRP A 637      28.197  83.886  -9.097  1.00 61.10           C  
ANISOU 5022  CD2 TRP A 637    12764   3587   6864   -913   2143   -763       C  
ATOM   5023  NE1 TRP A 637      30.391  83.909  -8.648  1.00 60.42           N  
ANISOU 5023  NE1 TRP A 637    12753   3513   6690   -634   2110   -676       N  
ATOM   5024  CE2 TRP A 637      29.423  83.239  -9.347  1.00 61.73           C  
ANISOU 5024  CE2 TRP A 637    12918   3594   6945   -741   2073   -776       C  
ATOM   5025  CE3 TRP A 637      27.037  83.391  -9.701  1.00 62.28           C  
ANISOU 5025  CE3 TRP A 637    12891   3674   7100  -1050   2120   -858       C  
ATOM   5026  CZ2 TRP A 637      29.522  82.124 -10.174  1.00 63.51           C  
ANISOU 5026  CZ2 TRP A 637    13195   3683   7253   -698   1980   -886       C  
ATOM   5027  CZ3 TRP A 637      27.138  82.284 -10.522  1.00 64.03           C  
ANISOU 5027  CZ3 TRP A 637    13166   3759   7405  -1012   2025   -964       C  
ATOM   5028  CH2 TRP A 637      28.372  81.663 -10.751  1.00 64.64           C  
ANISOU 5028  CH2 TRP A 637    13317   3762   7479   -835   1957   -979       C  
ATOM   5029  N   LEU A 638      27.338  87.003 -10.574  1.00 56.81           N  
ANISOU 5029  N   LEU A 638    11921   3476   6188   -937   2242   -871       N  
ATOM   5030  CA  LEU A 638      27.733  86.963 -11.977  1.00 56.86           C  
ANISOU 5030  CA  LEU A 638    11895   3521   6190   -829   2174   -993       C  
ATOM   5031  C   LEU A 638      26.548  87.394 -12.825  1.00 56.78           C  
ANISOU 5031  C   LEU A 638    11792   3579   6204   -938   2169  -1099       C  
ATOM   5032  O   LEU A 638      25.453  86.842 -12.684  1.00 57.94           O  
ANISOU 5032  O   LEU A 638    11945   3644   6427  -1088   2168  -1136       O  
ATOM   5033  CB  LEU A 638      28.200  85.559 -12.380  1.00 58.78           C  
ANISOU 5033  CB  LEU A 638    12234   3605   6495   -761   2089  -1058       C  
ATOM   5034  CG  LEU A 638      28.256  85.226 -13.873  1.00 59.49           C  
ANISOU 5034  CG  LEU A 638    12294   3709   6601   -687   2009  -1222       C  
ATOM   5035  CD1 LEU A 638      29.275  86.093 -14.600  1.00 58.12           C  
ANISOU 5035  CD1 LEU A 638    12057   3695   6330   -521   2007  -1241       C  
ATOM   5036  CD2 LEU A 638      28.557  83.747 -14.079  1.00 61.66           C  
ANISOU 5036  CD2 LEU A 638    12670   3800   6959   -643   1925  -1288       C  
ATOM   5037  N   LEU A 639      26.764  88.373 -13.700  1.00 55.53           N  
ANISOU 5037  N   LEU A 639    11545   3571   5982   -863   2163  -1148       N  
ATOM   5038  CA  LEU A 639      25.666  88.925 -14.486  1.00 55.35           C  
ANISOU 5038  CA  LEU A 639    11428   3632   5971   -954   2154  -1245       C  
ATOM   5039  C   LEU A 639      25.160  87.885 -15.479  1.00 57.15           C  
ANISOU 5039  C   LEU A 639    11677   3773   6264   -979   2070  -1394       C  
ATOM   5040  O   LEU A 639      25.890  87.472 -16.386  1.00 57.68           O  
ANISOU 5040  O   LEU A 639    11764   3842   6309   -848   2005  -1474       O  
ATOM   5041  CB  LEU A 639      26.104  90.196 -15.206  1.00 53.74           C  
ANISOU 5041  CB  LEU A 639    11132   3608   5680   -855   2156  -1253       C  
ATOM   5042  CG  LEU A 639      25.175  91.400 -15.008  1.00 52.57           C  
ANISOU 5042  CG  LEU A 639    10883   3571   5519   -957   2204  -1235       C  
ATOM   5043  CD1 LEU A 639      24.806  92.018 -16.344  1.00 52.35           C  
ANISOU 5043  CD1 LEU A 639    10768   3666   5456   -927   2151  -1347       C  
ATOM   5044  CD2 LEU A 639      23.915  91.023 -14.228  1.00 53.36           C  
ANISOU 5044  CD2 LEU A 639    10985   3589   5698  -1145   2243  -1234       C  
ATOM   5045  N   ARG A 640      23.904  87.473 -15.300  1.00 58.39           N  
ANISOU 5045  N   ARG A 640    11822   3861   6503  -1149   2073  -1438       N  
ATOM   5046  CA  ARG A 640      23.276  86.404 -16.068  1.00 60.34           C  
ANISOU 5046  CA  ARG A 640    12091   4001   6833  -1203   1993  -1578       C  
ATOM   5047  C   ARG A 640      23.318  86.666 -17.569  1.00 60.37           C  
ANISOU 5047  C   ARG A 640    12034   4109   6792  -1111   1919  -1729       C  
ATOM   5048  O   ARG A 640      24.258  86.253 -18.256  1.00 60.77           O  
ANISOU 5048  O   ARG A 640    12124   4156   6810   -960   1863  -1784       O  
ATOM   5049  CB  ARG A 640      21.825  86.226 -15.612  1.00 61.18           C  
ANISOU 5049  CB  ARG A 640    12162   4057   7026  -1417   2021  -1593       C  
ATOM   5050  CG  ARG A 640      21.174  84.946 -16.085  1.00 63.48           C  
ANISOU 5050  CG  ARG A 640    12493   4198   7429  -1500   1945  -1710       C  
ATOM   5051  CD  ARG A 640      21.919  83.742 -15.549  1.00 64.80           C  
ANISOU 5051  CD  ARG A 640    12789   4184   7647  -1452   1918  -1654       C  
ATOM   5052  NE  ARG A 640      21.391  82.494 -16.085  1.00 67.13           N  
ANISOU 5052  NE  ARG A 640    13126   4323   8059  -1515   1830  -1774       N  
ATOM   5053  CZ  ARG A 640      21.988  81.316 -15.949  1.00 68.70           C  
ANISOU 5053  CZ  ARG A 640    13435   4348   8322  -1460   1773  -1772       C  
ATOM   5054  NH1 ARG A 640      23.138  81.227 -15.295  1.00 68.16           N1+
ANISOU 5054  NH1 ARG A 640    13444   4248   8206  -1338   1795  -1657       N1+
ATOM   5055  NH2 ARG A 640      21.438  80.228 -16.471  1.00 70.91           N  
ANISOU 5055  NH2 ARG A 640    13744   4482   8717  -1524   1687  -1892       N  
ATOM   5056  N   LYS A 641      22.288  87.329 -18.089  1.00 59.87           N  
ANISOU 5056  N   LYS A 641    11875   4146   6727  -1200   1914  -1804       N  
ATOM   5057  CA  LYS A 641      22.238  87.736 -19.489  1.00 59.84           C  
ANISOU 5057  CA  LYS A 641    11806   4268   6661  -1119   1845  -1940       C  
ATOM   5058  C   LYS A 641      22.331  89.254 -19.539  1.00 57.84           C  
ANISOU 5058  C   LYS A 641    11465   4201   6311  -1081   1893  -1876       C  
ATOM   5059  O   LYS A 641      21.320  89.943 -19.332  1.00 57.37           O  
ANISOU 5059  O   LYS A 641    11329   4200   6270  -1200   1921  -1878       O  
ATOM   5060  CB  LYS A 641      20.946  87.251 -20.155  1.00 61.37           C  
ANISOU 5060  CB  LYS A 641    11959   4428   6931  -1244   1781  -2095       C  
ATOM   5061  CG  LYS A 641      20.696  85.754 -20.019  1.00 63.52           C  
ANISOU 5061  CG  LYS A 641    12314   4500   7323  -1310   1731  -2155       C  
ATOM   5062  CD  LYS A 641      21.157  84.989 -21.250  1.00 64.89           C  
ANISOU 5062  CD  LYS A 641    12518   4651   7485  -1185   1624  -2315       C  
ATOM   5063  CE  LYS A 641      21.108  83.487 -21.013  1.00 67.04           C  
ANISOU 5063  CE  LYS A 641    12885   4702   7885  -1229   1571  -2359       C  
ATOM   5064  NZ  LYS A 641      20.327  82.776 -22.063  1.00 68.97           N1+
ANISOU 5064  NZ  LYS A 641    13107   4904   8194  -1271   1464  -2560       N1+
ATOM   5065  N   PRO A 642      23.511  89.826 -19.797  1.00 56.72           N  
ANISOU 5065  N   PRO A 642    11324   4155   6072   -922   1903  -1819       N  
ATOM   5066  CA  PRO A 642      23.645  91.291 -19.734  1.00 54.88           C  
ANISOU 5066  CA  PRO A 642    11011   4083   5757   -891   1948  -1740       C  
ATOM   5067  C   PRO A 642      22.780  92.020 -20.742  1.00 54.84           C  
ANISOU 5067  C   PRO A 642    10913   4209   5713   -920   1903  -1845       C  
ATOM   5068  O   PRO A 642      22.485  93.205 -20.540  1.00 53.56           O  
ANISOU 5068  O   PRO A 642    10680   4153   5516   -943   1937  -1788       O  
ATOM   5069  CB  PRO A 642      25.138  91.524 -20.011  1.00 54.17           C  
ANISOU 5069  CB  PRO A 642    10944   4059   5579   -710   1951  -1682       C  
ATOM   5070  CG  PRO A 642      25.796  90.189 -19.803  1.00 55.44           C  
ANISOU 5070  CG  PRO A 642    11205   4072   5788   -659   1927  -1700       C  
ATOM   5071  CD  PRO A 642      24.770  89.171 -20.183  1.00 57.22           C  
ANISOU 5071  CD  PRO A 642    11454   4187   6100   -762   1869  -1832       C  
ATOM   5072  N   GLU A 643      22.361  91.347 -21.816  1.00 56.30           N  
ANISOU 5072  N   GLU A 643    11099   4389   5904   -914   1820  -2002       N  
ATOM   5073  CA  GLU A 643      21.488  91.976 -22.800  1.00 56.47           C  
ANISOU 5073  CA  GLU A 643    11038   4536   5882   -940   1766  -2113       C  
ATOM   5074  C   GLU A 643      20.167  92.417 -22.183  1.00 56.29           C  
ANISOU 5074  C   GLU A 643    10951   4503   5934  -1111   1793  -2113       C  
ATOM   5075  O   GLU A 643      19.545  93.369 -22.667  1.00 55.82           O  
ANISOU 5075  O   GLU A 643    10809   4570   5829  -1127   1771  -2152       O  
ATOM   5076  CB  GLU A 643      21.240  91.014 -23.963  1.00 58.32           C  
ANISOU 5076  CB  GLU A 643    11292   4750   6118   -911   1667  -2294       C  
ATOM   5077  CG  GLU A 643      20.646  89.677 -23.545  1.00 59.97           C  
ANISOU 5077  CG  GLU A 643    11555   4767   6464  -1025   1644  -2359       C  
ATOM   5078  CD  GLU A 643      21.619  88.523 -23.704  1.00 61.04           C  
ANISOU 5078  CD  GLU A 643    11785   4793   6616   -920   1613  -2388       C  
ATOM   5079  OE1 GLU A 643      21.182  87.357 -23.602  1.00 62.71           O  
ANISOU 5079  OE1 GLU A 643    12045   4846   6935   -994   1571  -2465       O  
ATOM   5080  OE2 GLU A 643      22.819  88.782 -23.937  1.00 60.34           O1+
ANISOU 5080  OE2 GLU A 643    11715   4774   6435   -765   1628  -2338       O1+
ATOM   5081  N   LYS A 644      19.727  91.751 -21.111  1.00 56.76           N  
ANISOU 5081  N   LYS A 644    11044   4418   6105  -1238   1841  -2069       N  
ATOM   5082  CA  LYS A 644      18.464  92.111 -20.474  1.00 56.77           C  
ANISOU 5082  CA  LYS A 644    10975   4415   6181  -1409   1877  -2074       C  
ATOM   5083  C   LYS A 644      18.537  93.451 -19.754  1.00 54.94           C  
ANISOU 5083  C   LYS A 644    10685   4284   5908  -1406   1950  -1954       C  
ATOM   5084  O   LYS A 644      17.490  94.035 -19.454  1.00 54.83           O  
ANISOU 5084  O   LYS A 644    10585   4313   5933  -1521   1969  -1981       O  
ATOM   5085  CB  LYS A 644      18.033  91.017 -19.494  1.00 57.92           C  
ANISOU 5085  CB  LYS A 644    11174   4387   6446  -1549   1917  -2046       C  
ATOM   5086  CG  LYS A 644      18.716  91.088 -18.137  1.00 56.96           C  
ANISOU 5086  CG  LYS A 644    11111   4204   6327  -1547   2016  -1870       C  
ATOM   5087  CD  LYS A 644      18.571  89.782 -17.371  1.00 58.42           C  
ANISOU 5087  CD  LYS A 644    11382   4208   6609  -1645   2036  -1841       C  
ATOM   5088  CE  LYS A 644      19.388  89.799 -16.089  1.00 57.58           C  
ANISOU 5088  CE  LYS A 644    11348   4049   6483  -1618   2121  -1668       C  
ATOM   5089  NZ  LYS A 644      19.367  88.478 -15.401  1.00 59.16           N1+
ANISOU 5089  NZ  LYS A 644    11646   4069   6765  -1693   2129  -1631       N1+
ATOM   5090  N   VAL A 645      19.741  93.949 -19.468  1.00 53.63           N  
ANISOU 5090  N   VAL A 645    10554   4153   5669  -1279   1988  -1832       N  
ATOM   5091  CA  VAL A 645      19.879  95.267 -18.857  1.00 51.95           C  
ANISOU 5091  CA  VAL A 645    10285   4036   5418  -1262   2045  -1725       C  
ATOM   5092  C   VAL A 645      19.841  96.356 -19.921  1.00 51.34           C  
ANISOU 5092  C   VAL A 645    10135   4119   5252  -1178   1990  -1773       C  
ATOM   5093  O   VAL A 645      19.127  97.356 -19.783  1.00 50.73           O  
ANISOU 5093  O   VAL A 645     9976   4123   5177  -1227   1997  -1777       O  
ATOM   5094  CB  VAL A 645      21.171  95.340 -18.022  1.00 50.90           C  
ANISOU 5094  CB  VAL A 645    10218   3871   5253  -1170   2107  -1572       C  
ATOM   5095  CG1 VAL A 645      21.472  96.781 -17.631  1.00 49.22           C  
ANISOU 5095  CG1 VAL A 645     9941   3770   4989  -1123   2145  -1475       C  
ATOM   5096  CG2 VAL A 645      21.052  94.467 -16.784  1.00 51.45           C  
ANISOU 5096  CG2 VAL A 645    10354   3795   5400  -1268   2170  -1508       C  
ATOM   5097  N   THR A 646      20.608  96.173 -21.000  1.00 51.62           N  
ANISOU 5097  N   THR A 646    10202   4206   5203  -1049   1933  -1811       N  
ATOM   5098  CA  THR A 646      20.627  97.152 -22.083  1.00 51.24           C  
ANISOU 5098  CA  THR A 646    10100   4318   5052   -965   1879  -1849       C  
ATOM   5099  C   THR A 646      19.239  97.362 -22.676  1.00 52.07           C  
ANISOU 5099  C   THR A 646    10134   4472   5177  -1058   1818  -1986       C  
ATOM   5100  O   THR A 646      18.924  98.461 -23.149  1.00 51.54           O  
ANISOU 5100  O   THR A 646    10008   4530   5046  -1032   1790  -1994       O  
ATOM   5101  CB  THR A 646      21.613  96.712 -23.169  1.00 51.79           C  
ANISOU 5101  CB  THR A 646    10216   4436   5026   -823   1832  -1886       C  
ATOM   5102  OG1 THR A 646      22.889  96.440 -22.575  1.00 51.17           O  
ANISOU 5102  OG1 THR A 646    10195   4307   4942   -740   1886  -1771       O  
ATOM   5103  CG2 THR A 646      21.780  97.798 -24.223  1.00 51.39           C  
ANISOU 5103  CG2 THR A 646    10119   4562   4845   -730   1791  -1894       C  
ATOM   5104  N   ARG A 647      18.389  96.335 -22.644  1.00 53.45           N  
ANISOU 5104  N   ARG A 647    10315   4549   5443  -1170   1794  -2094       N  
ATOM   5105  CA  ARG A 647      17.046  96.469 -23.194  1.00 54.39           C  
ANISOU 5105  CA  ARG A 647    10358   4716   5592  -1267   1730  -2237       C  
ATOM   5106  C   ARG A 647      16.097  97.186 -22.244  1.00 53.82           C  
ANISOU 5106  C   ARG A 647    10202   4650   5598  -1393   1781  -2209       C  
ATOM   5107  O   ARG A 647      15.215  97.922 -22.700  1.00 53.97           O  
ANISOU 5107  O   ARG A 647    10136   4767   5604  -1426   1732  -2292       O  
ATOM   5108  CB  ARG A 647      16.496  95.092 -23.563  1.00 56.25           C  
ANISOU 5108  CB  ARG A 647    10621   4847   5904  -1343   1677  -2372       C  
ATOM   5109  CG  ARG A 647      16.855  94.679 -24.977  1.00 57.25           C  
ANISOU 5109  CG  ARG A 647    10780   5035   5938  -1230   1581  -2487       C  
ATOM   5110  CD  ARG A 647      17.220  93.213 -25.078  1.00 58.61           C  
ANISOU 5110  CD  ARG A 647    11034   5068   6168  -1225   1559  -2544       C  
ATOM   5111  NE  ARG A 647      17.637  92.880 -26.436  1.00 59.57           N  
ANISOU 5111  NE  ARG A 647    11181   5265   6189  -1100   1470  -2662       N  
ATOM   5112  CZ  ARG A 647      17.741  91.643 -26.908  1.00 61.18           C  
ANISOU 5112  CZ  ARG A 647    11438   5377   6432  -1084   1412  -2774       C  
ATOM   5113  NH1 ARG A 647      18.127  91.443 -28.160  1.00 62.06           N1+
ANISOU 5113  NH1 ARG A 647    11562   5580   6437   -960   1334  -2888       N1+
ATOM   5114  NH2 ARG A 647      17.451  90.608 -26.131  1.00 62.04           N  
ANISOU 5114  NH2 ARG A 647    11588   5303   6682  -1192   1432  -2775       N  
ATOM   5115  N   TRP A 648      16.260  96.999 -20.932  1.00 53.27           N  
ANISOU 5115  N   TRP A 648    10153   4485   5602  -1460   1875  -2100       N  
ATOM   5116  CA  TRP A 648      15.418  97.723 -19.986  1.00 52.76           C  
ANISOU 5116  CA  TRP A 648    10004   4440   5601  -1572   1933  -2076       C  
ATOM   5117  C   TRP A 648      15.709  99.218 -20.009  1.00 51.28           C  
ANISOU 5117  C   TRP A 648     9766   4378   5340  -1479   1936  -2010       C  
ATOM   5118  O   TRP A 648      14.802 100.028 -19.783  1.00 51.14           O  
ANISOU 5118  O   TRP A 648     9652   4425   5354  -1543   1934  -2054       O  
ATOM   5119  CB  TRP A 648      15.609  97.167 -18.576  1.00 52.60           C  
ANISOU 5119  CB  TRP A 648    10030   4299   5656  -1656   2038  -1969       C  
ATOM   5120  CG  TRP A 648      14.755  97.842 -17.544  1.00 52.24           C  
ANISOU 5120  CG  TRP A 648     9897   4278   5673  -1774   2107  -1951       C  
ATOM   5121  CD1 TRP A 648      13.498  97.477 -17.153  1.00 53.39           C  
ANISOU 5121  CD1 TRP A 648     9972   4397   5917  -1948   2129  -2038       C  
ATOM   5122  CD2 TRP A 648      15.094  98.999 -16.769  1.00 50.74           C  
ANISOU 5122  CD2 TRP A 648     9674   4150   5453  -1727   2165  -1849       C  
ATOM   5123  NE1 TRP A 648      13.035  98.333 -16.184  1.00 52.71           N  
ANISOU 5123  NE1 TRP A 648     9809   4360   5859  -2010   2202  -2001       N  
ATOM   5124  CE2 TRP A 648      13.996  99.277 -15.931  1.00 51.08           C  
ANISOU 5124  CE2 TRP A 648     9627   4205   5575  -1872   2221  -1888       C  
ATOM   5125  CE3 TRP A 648      16.218  99.827 -16.705  1.00 49.24           C  
ANISOU 5125  CE3 TRP A 648     9516   4012   5183  -1579   2174  -1733       C  
ATOM   5126  CZ2 TRP A 648      13.990 100.345 -15.040  1.00 49.98           C  
ANISOU 5126  CZ2 TRP A 648     9416   4138   5436  -1856   2274  -1810       C  
ATOM   5127  CZ3 TRP A 648      16.210 100.886 -15.818  1.00 48.15           C  
ANISOU 5127  CZ3 TRP A 648     9324   3922   5047  -1575   2228  -1663       C  
ATOM   5128  CH2 TRP A 648      15.104 101.137 -14.998  1.00 48.52           C  
ANISOU 5128  CH2 TRP A 648     9271   3990   5173  -1705   2273  -1700       C  
ATOM   5129  N   LEU A 649      16.958  99.605 -20.275  1.00 50.28           N  
ANISOU 5129  N   LEU A 649     9697   4286   5119  -1330   1937  -1909       N  
ATOM   5130  CA  LEU A 649      17.292 101.023 -20.365  1.00 49.01           C  
ANISOU 5130  CA  LEU A 649     9496   4238   4888  -1241   1934  -1839       C  
ATOM   5131  C   LEU A 649      16.780 101.625 -21.668  1.00 49.51           C  
ANISOU 5131  C   LEU A 649     9501   4431   4881  -1192   1828  -1931       C  
ATOM   5132  O   LEU A 649      16.204 102.719 -21.676  1.00 49.12           O  
ANISOU 5132  O   LEU A 649     9331   4488   4844  -1184   1783  -1906       O  
ATOM   5133  CB  LEU A 649      18.804 101.215 -20.240  1.00 47.94           C  
ANISOU 5133  CB  LEU A 649     9429   4105   4681  -1108   1968  -1696       C  
ATOM   5134  CG  LEU A 649      19.427 100.916 -18.875  1.00 47.23           C  
ANISOU 5134  CG  LEU A 649     9378   3918   4647  -1130   2060  -1573       C  
ATOM   5135  CD1 LEU A 649      20.943 100.896 -18.974  1.00 46.51           C  
ANISOU 5135  CD1 LEU A 649     9353   3833   4487   -994   2075  -1461       C  
ATOM   5136  CD2 LEU A 649      18.970 101.942 -17.852  1.00 46.32           C  
ANISOU 5136  CD2 LEU A 649     9193   3829   4576  -1181   2110  -1520       C  
ATOM   5137  N   GLN A 650      16.980 100.916 -22.781  1.00 50.49           N  
ANISOU 5137  N   GLN A 650     9688   4562   4935  -1148   1771  -2023       N  
ATOM   5138  CA  GLN A 650      16.540 101.414 -24.079  1.00 51.14           C  
ANISOU 5138  CA  GLN A 650     9710   4785   4937  -1090   1658  -2098       C  
ATOM   5139  C   GLN A 650      15.028 101.576 -24.153  1.00 52.02           C  
ANISOU 5139  C   GLN A 650     9691   4940   5134  -1196   1589  -2206       C  
ATOM   5140  O   GLN A 650      14.542 102.381 -24.954  1.00 52.28           O  
ANISOU 5140  O   GLN A 650     9637   5108   5119  -1145   1491  -2229       O  
ATOM   5141  CB  GLN A 650      17.017 100.470 -25.184  1.00 52.23           C  
ANISOU 5141  CB  GLN A 650     9948   4915   4983  -1030   1618  -2198       C  
ATOM   5142  CG  GLN A 650      17.645 101.173 -26.374  1.00 52.17           C  
ANISOU 5142  CG  GLN A 650     9945   5063   4815   -886   1555  -2165       C  
ATOM   5143  CD  GLN A 650      19.015 101.740 -26.056  1.00 50.85           C  
ANISOU 5143  CD  GLN A 650     9830   4912   4577   -780   1629  -2000       C  
ATOM   5144  OE1 GLN A 650      19.990 100.999 -25.933  1.00 50.81           O  
ANISOU 5144  OE1 GLN A 650     9886   4851   4566   -728   1671  -1959       O  
ATOM   5145  NE2 GLN A 650      19.095 103.060 -25.914  1.00 49.86           N  
ANISOU 5145  NE2 GLN A 650     9627   4883   4433   -740   1617  -1872       N  
ATOM   5146  N   SER A 651      14.276 100.843 -23.334  1.00 52.58           N  
ANISOU 5146  N   SER A 651     9744   4904   5331  -1341   1637  -2270       N  
ATOM   5147  CA  SER A 651      12.819 100.904 -23.341  1.00 53.58           C  
ANISOU 5147  CA  SER A 651     9734   5073   5551  -1455   1580  -2384       C  
ATOM   5148  C   SER A 651      12.250 101.831 -22.277  1.00 52.78           C  
ANISOU 5148  C   SER A 651     9510   5010   5535  -1506   1623  -2312       C  
ATOM   5149  O   SER A 651      11.292 102.557 -22.553  1.00 53.17           O  
ANISOU 5149  O   SER A 651     9418   5169   5614  -1515   1545  -2366       O  
ATOM   5150  CB  SER A 651      12.225  99.505 -23.153  1.00 55.01           C  
ANISOU 5150  CB  SER A 651     9955   5122   5825  -1603   1604  -2511       C  
ATOM   5151  OG  SER A 651      12.409  98.706 -24.308  1.00 56.15           O  
ANISOU 5151  OG  SER A 651    10179   5253   5904  -1563   1530  -2629       O  
ATOM   5152  N   ASN A 652      12.811 101.826 -21.065  1.00 51.78           N  
ANISOU 5152  N   ASN A 652     9429   4799   5446  -1531   1739  -2197       N  
ATOM   5153  CA  ASN A 652      12.239 102.582 -19.958  1.00 51.21           C  
ANISOU 5153  CA  ASN A 652     9242   4759   5455  -1589   1790  -2146       C  
ATOM   5154  C   ASN A 652      13.204 103.545 -19.289  1.00 49.55           C  
ANISOU 5154  C   ASN A 652     9056   4567   5205  -1488   1841  -1984       C  
ATOM   5155  O   ASN A 652      12.778 104.279 -18.391  1.00 49.07           O  
ANISOU 5155  O   ASN A 652     8897   4542   5204  -1517   1876  -1945       O  
ATOM   5156  CB  ASN A 652      11.696 101.631 -18.880  1.00 51.90           C  
ANISOU 5156  CB  ASN A 652     9337   4734   5649  -1759   1890  -2176       C  
ATOM   5157  CG  ASN A 652      11.026 100.408 -19.464  1.00 53.60           C  
ANISOU 5157  CG  ASN A 652     9575   4882   5909  -1870   1857  -2322       C  
ATOM   5158  OD1 ASN A 652       9.811 100.384 -19.657  1.00 54.73           O  
ANISOU 5158  OD1 ASN A 652     9589   5082   6123  -1966   1809  -2440       O  
ATOM   5159  ND2 ASN A 652      11.816  99.378 -19.745  1.00 53.90           N  
ANISOU 5159  ND2 ASN A 652     9772   4796   5910  -1856   1877  -2323       N  
ATOM   5160  N   GLY A 653      14.477 103.571 -19.690  1.00 48.78           N  
ANISOU 5160  N   GLY A 653     9075   4449   5009  -1370   1847  -1897       N  
ATOM   5161  CA  GLY A 653      15.473 104.300 -18.918  1.00 47.32           C  
ANISOU 5161  CA  GLY A 653     8923   4257   4799  -1293   1910  -1745       C  
ATOM   5162  C   GLY A 653      15.176 105.782 -18.807  1.00 46.62           C  
ANISOU 5162  C   GLY A 653     8709   4280   4722  -1235   1860  -1693       C  
ATOM   5163  O   GLY A 653      15.294 106.373 -17.732  1.00 45.80           O  
ANISOU 5163  O   GLY A 653     8569   4168   4664  -1242   1918  -1618       O  
ATOM   5164  N   TRP A 654      14.783 106.405 -19.920  1.00 47.03           N  
ANISOU 5164  N   TRP A 654     8699   4437   4735  -1172   1745  -1734       N  
ATOM   5165  CA  TRP A 654      14.551 107.845 -19.911  1.00 46.50           C  
ANISOU 5165  CA  TRP A 654     8524   4463   4679  -1103   1680  -1678       C  
ATOM   5166  C   TRP A 654      13.317 108.215 -19.098  1.00 46.85           C  
ANISOU 5166  C   TRP A 654     8426   4534   4842  -1188   1682  -1747       C  
ATOM   5167  O   TRP A 654      13.235 109.331 -18.572  1.00 46.23           O  
ANISOU 5167  O   TRP A 654     8267   4497   4801  -1144   1668  -1691       O  
ATOM   5168  CB  TRP A 654      14.426 108.361 -21.344  1.00 47.06           C  
ANISOU 5168  CB  TRP A 654     8574   4636   4670  -1015   1550  -1698       C  
ATOM   5169  CG  TRP A 654      14.201 109.840 -21.445  1.00 46.70           C  
ANISOU 5169  CG  TRP A 654     8432   4674   4638   -938   1467  -1634       C  
ATOM   5170  CD1 TRP A 654      13.053 110.469 -21.829  1.00 47.50           C  
ANISOU 5170  CD1 TRP A 654     8406   4856   4786   -937   1359  -1710       C  
ATOM   5171  CD2 TRP A 654      15.149 110.876 -21.157  1.00 45.58           C  
ANISOU 5171  CD2 TRP A 654     8312   4534   4471   -848   1478  -1482       C  
ATOM   5172  NE1 TRP A 654      13.228 111.831 -21.802  1.00 46.96           N  
ANISOU 5172  NE1 TRP A 654     8287   4831   4725   -847   1298  -1613       N  
ATOM   5173  CE2 TRP A 654      14.506 112.107 -21.391  1.00 45.79           C  
ANISOU 5173  CE2 TRP A 654     8229   4633   4535   -797   1371  -1471       C  
ATOM   5174  CE3 TRP A 654      16.480 110.882 -20.726  1.00 44.51           C  
ANISOU 5174  CE3 TRP A 654     8275   4345   4292   -806   1562  -1358       C  
ATOM   5175  CZ2 TRP A 654      15.146 113.333 -21.207  1.00 44.99           C  
ANISOU 5175  CZ2 TRP A 654     8121   4540   4434   -713   1345  -1338       C  
ATOM   5176  CZ3 TRP A 654      17.114 112.099 -20.543  1.00 43.70           C  
ANISOU 5176  CZ3 TRP A 654     8156   4262   4186   -727   1540  -1229       C  
ATOM   5177  CH2 TRP A 654      16.447 113.307 -20.784  1.00 43.96           C  
ANISOU 5177  CH2 TRP A 654     8086   4355   4261   -684   1433  -1219       C  
ATOM   5178  N   ASP A 655      12.356 107.298 -18.974  1.00 47.95           N  
ANISOU 5178  N   ASP A 655     8526   4650   5043  -1312   1701  -1873       N  
ATOM   5179  CA  ASP A 655      11.150 107.595 -18.208  1.00 48.47           C  
ANISOU 5179  CA  ASP A 655     8442   4757   5218  -1401   1711  -1948       C  
ATOM   5180  C   ASP A 655      11.394 107.484 -16.708  1.00 47.82           C  
ANISOU 5180  C   ASP A 655     8372   4612   5185  -1465   1846  -1884       C  
ATOM   5181  O   ASP A 655      10.874 108.295 -15.932  1.00 47.64           O  
ANISOU 5181  O   ASP A 655     8233   4644   5224  -1471   1858  -1885       O  
ATOM   5182  CB  ASP A 655      10.012 106.668 -18.631  1.00 50.05           C  
ANISOU 5182  CB  ASP A 655     8583   4964   5469  -1521   1683  -2106       C  
ATOM   5183  CG  ASP A 655       8.719 106.967 -17.898  1.00 50.78           C  
ANISOU 5183  CG  ASP A 655     8502   5119   5675  -1616   1696  -2195       C  
ATOM   5184  OD1 ASP A 655       8.469 108.152 -17.597  1.00 50.34           O  
ANISOU 5184  OD1 ASP A 655     8339   5141   5646  -1547   1658  -2170       O  
ATOM   5185  OD2 ASP A 655       7.958 106.018 -17.617  1.00 51.91           O1+
ANISOU 5185  OD2 ASP A 655     8611   5231   5882  -1762   1744  -2291       O1+
ATOM   5186  N   ARG A 656      12.165 106.481 -16.278  1.00 47.58           N  
ANISOU 5186  N   ARG A 656     8481   4470   5127  -1510   1943  -1833       N  
ATOM   5187  CA  ARG A 656      12.550 106.406 -14.873  1.00 46.94           C  
ANISOU 5187  CA  ARG A 656     8432   4331   5071  -1554   2066  -1752       C  
ATOM   5188  C   ARG A 656      13.380 107.620 -14.475  1.00 45.56           C  
ANISOU 5188  C   ARG A 656     8254   4191   4865  -1428   2060  -1635       C  
ATOM   5189  O   ARG A 656      13.266 108.121 -13.350  1.00 45.16           O  
ANISOU 5189  O   ARG A 656     8149   4156   4855  -1447   2120  -1602       O  
ATOM   5190  CB  ARG A 656      13.326 105.117 -14.603  1.00 47.01           C  
ANISOU 5190  CB  ARG A 656     8607   4206   5048  -1603   2152  -1709       C  
ATOM   5191  CG  ARG A 656      12.602 103.849 -15.021  1.00 48.48           C  
ANISOU 5191  CG  ARG A 656     8815   4332   5271  -1730   2153  -1821       C  
ATOM   5192  CD  ARG A 656      11.303 103.668 -14.256  1.00 49.51           C  
ANISOU 5192  CD  ARG A 656     8820   4492   5500  -1885   2202  -1900       C  
ATOM   5193  NE  ARG A 656      10.168 103.481 -15.154  1.00 50.81           N  
ANISOU 5193  NE  ARG A 656     8878   4716   5711  -1945   2115  -2048       N  
ATOM   5194  CZ  ARG A 656       9.819 102.314 -15.686  1.00 52.06           C  
ANISOU 5194  CZ  ARG A 656     9088   4801   5893  -2042   2103  -2136       C  
ATOM   5195  NH1 ARG A 656      10.519 101.222 -15.412  1.00 52.21           N1+
ANISOU 5195  NH1 ARG A 656     9268   4672   5896  -2086   2172  -2088       N1+
ATOM   5196  NH2 ARG A 656       8.770 102.239 -16.494  1.00 53.27           N  
ANISOU 5196  NH2 ARG A 656     9129   5022   6089  -2090   2014  -2276       N  
ATOM   5197  N   LEU A 657      14.221 108.106 -15.392  1.00 44.93           N  
ANISOU 5197  N   LEU A 657     8231   4128   4713  -1303   1988  -1574       N  
ATOM   5198  CA  LEU A 657      14.976 109.328 -15.134  1.00 43.78           C  
ANISOU 5198  CA  LEU A 657     8074   4015   4548  -1190   1967  -1465       C  
ATOM   5199  C   LEU A 657      14.047 110.522 -14.958  1.00 43.94           C  
ANISOU 5199  C   LEU A 657     7934   4126   4637  -1169   1898  -1508       C  
ATOM   5200  O   LEU A 657      14.264 111.361 -14.076  1.00 43.26           O  
ANISOU 5200  O   LEU A 657     7806   4049   4584  -1134   1923  -1454       O  
ATOM   5201  CB  LEU A 657      15.969 109.579 -16.270  1.00 43.36           C  
ANISOU 5201  CB  LEU A 657     8102   3971   4401  -1075   1902  -1394       C  
ATOM   5202  CG  LEU A 657      17.302 108.833 -16.180  1.00 42.78           C  
ANISOU 5202  CG  LEU A 657     8182   3817   4256  -1044   1976  -1310       C  
ATOM   5203  CD1 LEU A 657      18.126 109.035 -17.441  1.00 42.67           C  
ANISOU 5203  CD1 LEU A 657     8229   3841   4144   -940   1912  -1262       C  
ATOM   5204  CD2 LEU A 657      18.079 109.286 -14.953  1.00 41.73           C  
ANISOU 5204  CD2 LEU A 657     8070   3646   4140  -1020   2053  -1206       C  
ATOM   5205  N   LYS A 658      13.002 110.614 -15.785  1.00 44.94           N  
ANISOU 5205  N   LYS A 658     7966   4319   4789  -1185   1806  -1614       N  
ATOM   5206  CA  LYS A 658      12.019 111.680 -15.626  1.00 45.31           C  
ANISOU 5206  CA  LYS A 658     7852   4451   4912  -1163   1733  -1672       C  
ATOM   5207  C   LYS A 658      11.263 111.577 -14.308  1.00 45.61           C  
ANISOU 5207  C   LYS A 658     7795   4501   5034  -1260   1824  -1733       C  
ATOM   5208  O   LYS A 658      10.684 112.572 -13.859  1.00 45.70           O  
ANISOU 5208  O   LYS A 658     7679   4576   5108  -1224   1786  -1766       O  
ATOM   5209  CB  LYS A 658      11.030 111.666 -16.793  1.00 46.49           C  
ANISOU 5209  CB  LYS A 658     7921   4673   5069  -1164   1612  -1783       C  
ATOM   5210  CG  LYS A 658      11.491 112.444 -18.016  1.00 46.34           C  
ANISOU 5210  CG  LYS A 658     7933   4692   4981  -1035   1484  -1720       C  
ATOM   5211  CD  LYS A 658      10.486 112.335 -19.152  1.00 47.65           C  
ANISOU 5211  CD  LYS A 658     8025   4935   5144  -1037   1363  -1836       C  
ATOM   5212  CE  LYS A 658      10.820 113.295 -20.281  1.00 47.66           C  
ANISOU 5212  CE  LYS A 658     8043   4989   5078   -905   1226  -1764       C  
ATOM   5213  NZ  LYS A 658      10.360 112.772 -21.599  1.00 48.81           N1+
ANISOU 5213  NZ  LYS A 658     8197   5191   5159   -903   1130  -1846       N1+
ATOM   5214  N   ARG A 659      11.258 110.405 -13.677  1.00 45.88           N  
ANISOU 5214  N   ARG A 659     7890   4476   5068  -1378   1941  -1749       N  
ATOM   5215  CA  ARG A 659      10.561 110.187 -12.416  1.00 46.34           C  
ANISOU 5215  CA  ARG A 659     7867   4552   5190  -1486   2043  -1797       C  
ATOM   5216  C   ARG A 659      11.418 110.500 -11.195  1.00 45.32           C  
ANISOU 5216  C   ARG A 659     7795   4384   5039  -1459   2138  -1691       C  
ATOM   5217  O   ARG A 659      10.975 110.256 -10.069  1.00 45.70           O  
ANISOU 5217  O   ARG A 659     7798   4448   5119  -1548   2237  -1714       O  
ATOM   5218  CB  ARG A 659      10.068 108.740 -12.321  1.00 47.39           C  
ANISOU 5218  CB  ARG A 659     8038   4634   5335  -1643   2122  -1859       C  
ATOM   5219  CG  ARG A 659       8.972 108.349 -13.297  1.00 48.73           C  
ANISOU 5219  CG  ARG A 659     8118   4851   5545  -1704   2041  -1995       C  
ATOM   5220  CD  ARG A 659       8.580 106.893 -13.070  1.00 49.81           C  
ANISOU 5220  CD  ARG A 659     8304   4916   5705  -1872   2128  -2045       C  
ATOM   5221  NE  ARG A 659       7.654 106.375 -14.072  1.00 51.15           N  
ANISOU 5221  NE  ARG A 659     8407   5115   5911  -1935   2047  -2179       N  
ATOM   5222  CZ  ARG A 659       6.341 106.271 -13.897  1.00 52.50           C  
ANISOU 5222  CZ  ARG A 659     8416   5363   6167  -2047   2047  -2304       C  
ATOM   5223  NH1 ARG A 659       5.787 106.655 -12.755  1.00 52.71           N1+
ANISOU 5223  NH1 ARG A 659     8328   5452   6245  -2106   2131  -2314       N1+
ATOM   5224  NH2 ARG A 659       5.580 105.781 -14.867  1.00 53.73           N  
ANISOU 5224  NH2 ARG A 659     8519   5544   6354  -2098   1963  -2427       N  
ATOM   5225  N   MET A 660      12.626 111.023 -11.384  1.00 44.13           N  
ANISOU 5225  N   MET A 660     7742   4193   4835  -1342   2110  -1576       N  
ATOM   5226  CA  MET A 660      13.545 111.279 -10.285  1.00 43.18           C  
ANISOU 5226  CA  MET A 660     7685   4033   4690  -1310   2190  -1476       C  
ATOM   5227  C   MET A 660      13.809 112.772 -10.130  1.00 42.48           C  
ANISOU 5227  C   MET A 660     7525   3991   4626  -1188   2117  -1441       C  
ATOM   5228  O   MET A 660      13.418 113.596 -10.962  1.00 42.66           O  
ANISOU 5228  O   MET A 660     7471   4063   4677  -1119   2000  -1473       O  
ATOM   5229  CB  MET A 660      14.868 110.534 -10.494  1.00 42.47           C  
ANISOU 5229  CB  MET A 660     7774   3842   4520  -1283   2231  -1368       C  
ATOM   5230  CG  MET A 660      14.749 109.024 -10.455  1.00 43.18           C  
ANISOU 5230  CG  MET A 660     7957   3858   4593  -1398   2309  -1391       C  
ATOM   5231  SD  MET A 660      16.291 108.212 -10.910  1.00 42.50           S  
ANISOU 5231  SD  MET A 660     8072   3660   4418  -1336   2331  -1284       S  
ATOM   5232  CE  MET A 660      15.738 106.520 -11.081  1.00 43.79           C  
ANISOU 5232  CE  MET A 660     8311   3737   4592  -1479   2386  -1355       C  
ATOM   5233  N   ALA A 661      14.488 113.103  -9.032  1.00 41.78           N  
ANISOU 5233  N   ALA A 661     7467   3880   4526  -1163   2183  -1373       N  
ATOM   5234  CA  ALA A 661      14.950 114.462  -8.760  1.00 41.08           C  
ANISOU 5234  CA  ALA A 661     7333   3812   4462  -1049   2121  -1329       C  
ATOM   5235  C   ALA A 661      16.167 114.325  -7.850  1.00 40.18           C  
ANISOU 5235  C   ALA A 661     7328   3639   4299  -1027   2202  -1223       C  
ATOM   5236  O   ALA A 661      16.019 114.055  -6.655  1.00 40.33           O  
ANISOU 5236  O   ALA A 661     7339   3669   4317  -1082   2296  -1237       O  
ATOM   5237  CB  ALA A 661      13.857 115.305  -8.117  1.00 41.71           C  
ANISOU 5237  CB  ALA A 661     7247   3977   4622  -1050   2099  -1433       C  
ATOM   5238  N   VAL A 662      17.356 114.507  -8.417  1.00 39.36           N  
ANISOU 5238  N   VAL A 662     7322   3482   4150   -947   2166  -1118       N  
ATOM   5239  CA  VAL A 662      18.610 114.206  -7.733  1.00 38.58           C  
ANISOU 5239  CA  VAL A 662     7338   3324   3998   -924   2236  -1016       C  
ATOM   5240  C   VAL A 662      19.482 115.454  -7.731  1.00 37.81           C  
ANISOU 5240  C   VAL A 662     7227   3223   3915   -813   2167   -942       C  
ATOM   5241  O   VAL A 662      19.811 115.991  -8.796  1.00 37.63           O  
ANISOU 5241  O   VAL A 662     7207   3199   3891   -750   2079   -900       O  
ATOM   5242  CB  VAL A 662      19.345 113.028  -8.390  1.00 38.47           C  
ANISOU 5242  CB  VAL A 662     7463   3244   3912   -942   2273   -961       C  
ATOM   5243  CG1 VAL A 662      20.695 112.803  -7.729  1.00 37.72           C  
ANISOU 5243  CG1 VAL A 662     7476   3092   3766   -899   2330   -857       C  
ATOM   5244  CG2 VAL A 662      18.497 111.771  -8.315  1.00 39.37           C  
ANISOU 5244  CG2 VAL A 662     7595   3341   4022  -1061   2339  -1034       C  
ATOM   5245  N   SER A 663      19.853 115.908  -6.536  1.00 38.23           N  
ANISOU 5245  N   SER A 663     7269   3276   3982   -794   2206   -924       N  
ATOM   5246  CA  SER A 663      20.834 116.972  -6.333  1.00 37.54           C  
ANISOU 5246  CA  SER A 663     7182   3170   3911   -700   2154   -850       C  
ATOM   5247  C   SER A 663      21.963 116.384  -5.497  1.00 37.00           C  
ANISOU 5247  C   SER A 663     7219   3058   3782   -697   2239   -773       C  
ATOM   5248  O   SER A 663      21.819 116.225  -4.280  1.00 37.13           O  
ANISOU 5248  O   SER A 663     7228   3088   3790   -727   2306   -801       O  
ATOM   5249  CB  SER A 663      20.214 118.185  -5.645  1.00 37.77           C  
ANISOU 5249  CB  SER A 663     7087   3242   4022   -665   2102   -918       C  
ATOM   5250  OG  SER A 663      21.216 119.090  -5.216  1.00 37.24           O  
ANISOU 5250  OG  SER A 663     7032   3145   3974   -588   2065   -851       O  
ATOM   5251  N   GLY A 664      23.080 116.065  -6.143  1.00 36.12           N  
ANISOU 5251  N   GLY A 664     7202   2901   3620   -658   2234   -680       N  
ATOM   5252  CA  GLY A 664      24.186 115.457  -5.422  1.00 35.70           C  
ANISOU 5252  CA  GLY A 664     7248   2806   3510   -646   2305   -610       C  
ATOM   5253  C   GLY A 664      23.766 114.136  -4.810  1.00 36.17           C  
ANISOU 5253  C   GLY A 664     7372   2845   3524   -729   2406   -640       C  
ATOM   5254  O   GLY A 664      23.258 113.240  -5.494  1.00 36.62           O  
ANISOU 5254  O   GLY A 664     7465   2886   3563   -785   2424   -671       O  
ATOM   5255  N   ASP A 665      23.962 114.013  -3.497  1.00 38.48           N  
ANISOU 5255  N   ASP A 665     7669   3143   3811   -742   2452   -622       N  
ATOM   5256  CA  ASP A 665      23.601 112.795  -2.785  1.00 38.95           C  
ANISOU 5256  CA  ASP A 665     7770   3181   3847   -826   2521   -618       C  
ATOM   5257  C   ASP A 665      22.136 112.751  -2.376  1.00 40.05           C  
ANISOU 5257  C   ASP A 665     7838   3376   4003   -920   2575   -727       C  
ATOM   5258  O   ASP A 665      21.668 111.695  -1.936  1.00 41.05           O  
ANISOU 5258  O   ASP A 665     8007   3483   4108  -1011   2646   -732       O  
ATOM   5259  CB  ASP A 665      24.479 112.631  -1.543  1.00 38.65           C  
ANISOU 5259  CB  ASP A 665     7765   3127   3794   -796   2531   -543       C  
ATOM   5260  CG  ASP A 665      24.319 113.774  -0.560  1.00 38.62           C  
ANISOU 5260  CG  ASP A 665     7672   3192   3811   -764   2520   -578       C  
ATOM   5261  OD1 ASP A 665      24.308 114.943  -1.000  1.00 38.15           O  
ANISOU 5261  OD1 ASP A 665     7553   3160   3784   -708   2472   -615       O  
ATOM   5262  OD2 ASP A 665      24.201 113.503   0.655  1.00 39.32           O1+
ANISOU 5262  OD2 ASP A 665     7756   3302   3881   -792   2557   -575       O1+
ATOM   5263  N   ASP A 666      21.406 113.856  -2.500  1.00 39.97           N  
ANISOU 5263  N   ASP A 666     7719   3430   4039   -899   2539   -814       N  
ATOM   5264  CA  ASP A 666      19.999 113.900  -2.127  1.00 40.89           C  
ANISOU 5264  CA  ASP A 666     7727   3618   4193   -978   2568   -920       C  
ATOM   5265  C   ASP A 666      19.138 113.542  -3.333  1.00 41.42           C  
ANISOU 5265  C   ASP A 666     7756   3687   4294  -1027   2529   -978       C  
ATOM   5266  O   ASP A 666      19.392 114.007  -4.449  1.00 40.85           O  
ANISOU 5266  O   ASP A 666     7676   3600   4245   -964   2437   -963       O  
ATOM   5267  CB  ASP A 666      19.632 115.287  -1.594  1.00 40.99           C  
ANISOU 5267  CB  ASP A 666     7607   3704   4263   -918   2514   -984       C  
ATOM   5268  CG  ASP A 666      18.487 115.248  -0.601  1.00 42.04           C  
ANISOU 5268  CG  ASP A 666     7644   3927   4404   -992   2584  -1082       C  
ATOM   5269  OD1 ASP A 666      17.496 114.531  -0.856  1.00 42.99           O  
ANISOU 5269  OD1 ASP A 666     7731   4072   4531  -1091   2627  -1139       O  
ATOM   5270  OD2 ASP A 666      18.582 115.932   0.442  1.00 41.96           O1+
ANISOU 5270  OD2 ASP A 666     7586   3967   4390   -953   2597  -1108       O1+
ATOM   5271  N   CYS A 667      18.122 112.709  -3.107  1.00 39.97           N  
ANISOU 5271  N   CYS A 667     7549   3526   4112  -1143   2597  -1041       N  
ATOM   5272  CA  CYS A 667      17.322 112.191  -4.207  1.00 40.55           C  
ANISOU 5272  CA  CYS A 667     7596   3597   4215  -1202   2565  -1101       C  
ATOM   5273  C   CYS A 667      15.903 111.902  -3.741  1.00 41.74           C  
ANISOU 5273  C   CYS A 667     7635   3820   4403  -1318   2620  -1209       C  
ATOM   5274  O   CYS A 667      15.661 111.623  -2.563  1.00 42.22           O  
ANISOU 5274  O   CYS A 667     7689   3912   4440  -1384   2717  -1212       O  
ATOM   5275  CB  CYS A 667      17.936 110.915  -4.795  1.00 40.54           C  
ANISOU 5275  CB  CYS A 667     7745   3496   4163  -1237   2596  -1040       C  
ATOM   5276  SG  CYS A 667      17.806 109.464  -3.723  1.00 41.38           S  
ANISOU 5276  SG  CYS A 667     7953   3546   4224  -1371   2737  -1012       S  
ATOM   5277  N   VAL A 668      14.969 111.975  -4.688  1.00 41.86           N  
ANISOU 5277  N   VAL A 668     7561   3873   4472  -1344   2556  -1297       N  
ATOM   5278  CA  VAL A 668      13.586 111.546  -4.496  1.00 43.15           C  
ANISOU 5278  CA  VAL A 668     7614   4104   4678  -1467   2601  -1407       C  
ATOM   5279  C   VAL A 668      13.170 110.778  -5.743  1.00 43.66           C  
ANISOU 5279  C   VAL A 668     7700   4130   4759  -1519   2554  -1446       C  
ATOM   5280  O   VAL A 668      13.373 111.256  -6.864  1.00 43.24           O  
ANISOU 5280  O   VAL A 668     7642   4070   4716  -1433   2443  -1449       O  
ATOM   5281  CB  VAL A 668      12.632 112.731  -4.246  1.00 43.57           C  
ANISOU 5281  CB  VAL A 668     7477   4279   4800  -1428   2550  -1516       C  
ATOM   5282  CG1 VAL A 668      11.191 112.250  -4.195  1.00 45.03           C  
ANISOU 5282  CG1 VAL A 668     7533   4543   5032  -1555   2591  -1639       C  
ATOM   5283  CG2 VAL A 668      12.998 113.454  -2.957  1.00 43.24           C  
ANISOU 5283  CG2 VAL A 668     7411   4279   4740  -1378   2598  -1495       C  
ATOM   5284  N   VAL A 669      12.599 109.590  -5.555  1.00 44.68           N  
ANISOU 5284  N   VAL A 669     7855   4233   4887  -1663   2637  -1475       N  
ATOM   5285  CA  VAL A 669      12.268 108.697  -6.660  1.00 45.29           C  
ANISOU 5285  CA  VAL A 669     7971   4259   4979  -1725   2600  -1516       C  
ATOM   5286  C   VAL A 669      10.797 108.311  -6.569  1.00 46.81           C  
ANISOU 5286  C   VAL A 669     8025   4523   5236  -1866   2630  -1640       C  
ATOM   5287  O   VAL A 669      10.321 107.903  -5.503  1.00 47.59           O  
ANISOU 5287  O   VAL A 669     8094   4649   5338  -1979   2743  -1647       O  
ATOM   5288  CB  VAL A 669      13.155 107.436  -6.661  1.00 45.19           C  
ANISOU 5288  CB  VAL A 669     8152   4109   4910  -1767   2660  -1425       C  
ATOM   5289  CG1 VAL A 669      12.742 106.493  -7.781  1.00 46.02           C  
ANISOU 5289  CG1 VAL A 669     8290   4159   5035  -1834   2619  -1488       C  
ATOM   5290  CG2 VAL A 669      14.621 107.819  -6.798  1.00 43.79           C  
ANISOU 5290  CG2 VAL A 669     8095   3873   4671  -1624   2628  -1311       C  
ATOM   5291  N   LYS A 670      10.082 108.444  -7.688  1.00 47.33           N  
ANISOU 5291  N   LYS A 670     8005   4628   5348  -1860   2530  -1738       N  
ATOM   5292  CA  LYS A 670       8.706 107.976  -7.832  1.00 48.88           C  
ANISOU 5292  CA  LYS A 670     8071   4888   5614  -1996   2541  -1866       C  
ATOM   5293  C   LYS A 670       8.722 106.727  -8.705  1.00 49.52           C  
ANISOU 5293  C   LYS A 670     8255   4868   5691  -2079   2528  -1881       C  
ATOM   5294  O   LYS A 670       8.676 106.823  -9.940  1.00 49.50           O  
ANISOU 5294  O   LYS A 670     8250   4865   5692  -2018   2413  -1929       O  
ATOM   5295  CB  LYS A 670       7.816 109.060  -8.447  1.00 49.20           C  
ANISOU 5295  CB  LYS A 670     7925   5052   5715  -1923   2424  -1981       C  
ATOM   5296  CG  LYS A 670       6.394 108.611  -8.767  1.00 50.88           C  
ANISOU 5296  CG  LYS A 670     7988   5340   6003  -2050   2414  -2128       C  
ATOM   5297  CD  LYS A 670       5.396 109.101  -7.732  1.00 51.77           C  
ANISOU 5297  CD  LYS A 670     7916   5585   6170  -2110   2482  -2211       C  
ATOM   5298  CE  LYS A 670       3.970 108.781  -8.155  1.00 53.50           C  
ANISOU 5298  CE  LYS A 670     7961   5896   6472  -2223   2456  -2368       C  
ATOM   5299  NZ  LYS A 670       2.959 109.407  -7.257  1.00 54.46           N1+
ANISOU 5299  NZ  LYS A 670     7874   6171   6649  -2257   2508  -2467       N1+
ATOM   5300  N   PRO A 671       8.794 105.533  -8.120  1.00 50.20           N  
ANISOU 5300  N   PRO A 671     8440   4865   5768  -2216   2638  -1842       N  
ATOM   5301  CA  PRO A 671       8.865 104.316  -8.941  1.00 50.89           C  
ANISOU 5301  CA  PRO A 671     8639   4837   5861  -2289   2619  -1861       C  
ATOM   5302  C   PRO A 671       7.532 103.964  -9.579  1.00 52.45           C  
ANISOU 5302  C   PRO A 671     8699   5092   6139  -2405   2575  -2011       C  
ATOM   5303  O   PRO A 671       6.575 104.741  -9.512  1.00 52.92           O  
ANISOU 5303  O   PRO A 671     8569   5289   6249  -2408   2545  -2104       O  
ATOM   5304  CB  PRO A 671       9.303 103.247  -7.935  1.00 51.28           C  
ANISOU 5304  CB  PRO A 671     8828   4770   5886  -2402   2752  -1764       C  
ATOM   5305  CG  PRO A 671       8.740 103.728  -6.638  1.00 51.62           C  
ANISOU 5305  CG  PRO A 671     8758   4916   5939  -2467   2852  -1756       C  
ATOM   5306  CD  PRO A 671       8.834 105.231  -6.679  1.00 50.48           C  
ANISOU 5306  CD  PRO A 671     8499   4895   5786  -2307   2781  -1775       C  
ATOM   5307  N   ILE A 672       7.460 102.786 -10.206  1.00 53.37           N  
ANISOU 5307  N   ILE A 672     8905   5102   6273  -2497   2564  -2045       N  
ATOM   5308  CA  ILE A 672       6.215 102.328 -10.818  1.00 55.02           C  
ANISOU 5308  CA  ILE A 672     8989   5353   6563  -2621   2520  -2194       C  
ATOM   5309  C   ILE A 672       5.380 101.475  -9.874  1.00 56.61           C  
ANISOU 5309  C   ILE A 672     9143   5538   6829  -2841   2647  -2215       C  
ATOM   5310  O   ILE A 672       4.204 101.212 -10.175  1.00 58.14           O  
ANISOU 5310  O   ILE A 672     9193   5794   7103  -2964   2626  -2344       O  
ATOM   5311  CB  ILE A 672       6.487 101.547 -12.121  1.00 55.39           C  
ANISOU 5311  CB  ILE A 672     9141   5302   6600  -2604   2423  -2246       C  
ATOM   5312  CG1 ILE A 672       7.169 100.212 -11.823  1.00 55.76           C  
ANISOU 5312  CG1 ILE A 672     9389   5163   6635  -2690   2501  -2171       C  
ATOM   5313  CG2 ILE A 672       7.342 102.375 -13.068  1.00 53.94           C  
ANISOU 5313  CG2 ILE A 672     9008   5148   6340  -2393   2308  -2214       C  
ATOM   5314  CD1 ILE A 672       7.401  99.366 -13.055  1.00 56.34           C  
ANISOU 5314  CD1 ILE A 672     9566   5137   6705  -2677   2409  -2240       C  
ATOM   5315  N   ASP A 673       5.941 101.038  -8.750  1.00 56.43           N  
ANISOU 5315  N   ASP A 673     9233   5437   6770  -2898   2774  -2089       N  
ATOM   5316  CA  ASP A 673       5.208 100.302  -7.724  1.00 57.98           C  
ANISOU 5316  CA  ASP A 673     9392   5627   7013  -3109   2909  -2081       C  
ATOM   5317  C   ASP A 673       6.061 100.295  -6.460  1.00 57.23           C  
ANISOU 5317  C   ASP A 673     9418   5486   6842  -3094   3029  -1920       C  
ATOM   5318  O   ASP A 673       7.203 100.767  -6.456  1.00 55.58           O  
ANISOU 5318  O   ASP A 673     9322   5239   6557  -2927   2999  -1827       O  
ATOM   5319  CB  ASP A 673       4.849  98.884  -8.180  1.00 59.62           C  
ANISOU 5319  CB  ASP A 673     9678   5693   7283  -3280   2914  -2123       C  
ATOM   5320  CG  ASP A 673       6.004  98.171  -8.857  1.00 58.94           C  
ANISOU 5320  CG  ASP A 673     9820   5421   7153  -3194   2857  -2060       C  
ATOM   5321  OD1 ASP A 673       7.171  98.472  -8.536  1.00 57.43           O  
ANISOU 5321  OD1 ASP A 673     9760   5182   6877  -3056   2872  -1937       O  
ATOM   5322  OD2 ASP A 673       5.739  97.304  -9.717  1.00 60.01           O1+
ANISOU 5322  OD2 ASP A 673     9997   5463   7341  -3264   2796  -2142       O1+
ATOM   5323  N   ASP A 674       5.499  99.742  -5.386  1.00 58.58           N  
ANISOU 5323  N   ASP A 674     9563   5665   7029  -3273   3164  -1885       N  
ATOM   5324  CA  ASP A 674       6.134  99.768  -4.075  1.00 58.16           C  
ANISOU 5324  CA  ASP A 674     9603   5599   6898  -3274   3284  -1739       C  
ATOM   5325  C   ASP A 674       7.111  98.618  -3.856  1.00 58.23           C  
ANISOU 5325  C   ASP A 674     9864   5394   6867  -3307   3323  -1602       C  
ATOM   5326  O   ASP A 674       7.531  98.389  -2.717  1.00 58.34           O  
ANISOU 5326  O   ASP A 674     9969   5380   6820  -3345   3431  -1476       O  
ATOM   5327  CB  ASP A 674       5.072  99.767  -2.974  1.00 59.71           C  
ANISOU 5327  CB  ASP A 674     9649   5925   7112  -3447   3417  -1759       C  
ATOM   5328  CG  ASP A 674       4.249 101.039  -2.962  1.00 59.54           C  
ANISOU 5328  CG  ASP A 674     9380   6125   7116  -3381   3387  -1884       C  
ATOM   5329  OD1 ASP A 674       3.047 100.971  -2.625  1.00 61.17           O  
ANISOU 5329  OD1 ASP A 674     9409   6454   7380  -3533   3451  -1975       O  
ATOM   5330  OD2 ASP A 674       4.805 102.108  -3.294  1.00 57.87           O1+
ANISOU 5330  OD2 ASP A 674     9150   5964   6872  -3178   3296  -1894       O1+
ATOM   5331  N   ARG A 675       7.480  97.887  -4.912  1.00 58.28           N  
ANISOU 5331  N   ARG A 675     9987   5252   6905  -3287   3235  -1629       N  
ATOM   5332  CA  ARG A 675       8.580  96.936  -4.788  1.00 58.12           C  
ANISOU 5332  CA  ARG A 675    10212   5027   6844  -3267   3250  -1505       C  
ATOM   5333  C   ARG A 675       9.911  97.659  -4.625  1.00 56.07           C  
ANISOU 5333  C   ARG A 675    10050   4768   6487  -3048   3220  -1406       C  
ATOM   5334  O   ARG A 675      10.860  97.096  -4.066  1.00 55.86           O  
ANISOU 5334  O   ARG A 675    10187   4637   6399  -2997   3248  -1274       O  
ATOM   5335  CB  ARG A 675       8.620  96.009  -6.001  1.00 58.79           C  
ANISOU 5335  CB  ARG A 675    10372   4982   6983  -3270   3146  -1574       C  
ATOM   5336  CG  ARG A 675       7.449  95.043  -6.086  1.00 61.06           C  
ANISOU 5336  CG  ARG A 675    10582   5254   7365  -3471   3161  -1643       C  
ATOM   5337  CD  ARG A 675       7.575  94.137  -7.299  1.00 61.73           C  
ANISOU 5337  CD  ARG A 675    10737   5221   7495  -3441   3040  -1709       C  
ATOM   5338  NE  ARG A 675       7.468  94.879  -8.551  1.00 60.82           N  
ANISOU 5338  NE  ARG A 675    10551   5162   7395  -3350   2931  -1857       N  
ATOM   5339  CZ  ARG A 675       7.675  94.351  -9.753  1.00 61.08           C  
ANISOU 5339  CZ  ARG A 675    10634   5128   7446  -3281   2811  -1930       C  
ATOM   5340  NH1 ARG A 675       8.008  93.073  -9.869  1.00 62.21           N1+
ANISOU 5340  NH1 ARG A 675    10897   5130   7608  -3298   2784  -1877       N1+
ATOM   5341  NH2 ARG A 675       7.556  95.102 -10.841  1.00 60.32           N  
ANISOU 5341  NH2 ARG A 675    10466   5109   7344  -3187   2710  -2058       N  
ATOM   5342  N   PHE A 676       9.989  98.904  -5.103  1.00 54.67           N  
ANISOU 5342  N   PHE A 676     9753   4730   6290  -2893   3143  -1465       N  
ATOM   5343  CA  PHE A 676      11.152  99.757  -4.885  1.00 52.81           C  
ANISOU 5343  CA  PHE A 676     9576   4518   5971  -2697   3118  -1378       C  
ATOM   5344  C   PHE A 676      11.481  99.910  -3.408  1.00 52.70           C  
ANISOU 5344  C   PHE A 676     9600   4530   5896  -2718   3232  -1259       C  
ATOM   5345  O   PHE A 676      12.631 100.203  -3.062  1.00 51.48           O  
ANISOU 5345  O   PHE A 676     9552   4339   5668  -2584   3228  -1159       O  
ATOM   5346  CB  PHE A 676      10.882 101.121  -5.531  1.00 51.75           C  
ANISOU 5346  CB  PHE A 676     9274   4542   5846  -2568   3025  -1467       C  
ATOM   5347  CG  PHE A 676      12.021 102.097  -5.434  1.00 49.92           C  
ANISOU 5347  CG  PHE A 676     9085   4339   5543  -2371   2985  -1389       C  
ATOM   5348  CD1 PHE A 676      12.979 102.164  -6.431  1.00 48.89           C  
ANISOU 5348  CD1 PHE A 676     9049   4144   5382  -2229   2892  -1370       C  
ATOM   5349  CD2 PHE A 676      12.110 102.975  -4.366  1.00 49.34           C  
ANISOU 5349  CD2 PHE A 676     8946   4366   5436  -2331   3040  -1344       C  
ATOM   5350  CE1 PHE A 676      14.017 103.075  -6.352  1.00 47.33           C  
ANISOU 5350  CE1 PHE A 676     8881   3976   5126  -2061   2858  -1297       C  
ATOM   5351  CE2 PHE A 676      13.148 103.883  -4.280  1.00 47.77           C  
ANISOU 5351  CE2 PHE A 676     8781   4188   5182  -2158   2997  -1278       C  
ATOM   5352  CZ  PHE A 676      14.102 103.933  -5.273  1.00 46.77           C  
ANISOU 5352  CZ  PHE A 676     8747   3991   5032  -2028   2907  -1251       C  
ATOM   5353  N   ALA A 677      10.498  99.706  -2.528  1.00 54.08           N  
ANISOU 5353  N   ALA A 677     9683   4773   6091  -2885   3336  -1271       N  
ATOM   5354  CA  ALA A 677      10.725  99.840  -1.097  1.00 54.20           C  
ANISOU 5354  CA  ALA A 677     9728   4833   6034  -2914   3450  -1163       C  
ATOM   5355  C   ALA A 677      11.609  98.734  -0.533  1.00 54.61           C  
ANISOU 5355  C   ALA A 677     9977   4743   6028  -2893   3459  -1025       C  
ATOM   5356  O   ALA A 677      12.167  98.907   0.555  1.00 54.34           O  
ANISOU 5356  O   ALA A 677     9979   4752   5915  -2816   3481   -930       O  
ATOM   5357  CB  ALA A 677       9.387  99.861  -0.357  1.00 55.81           C  
ANISOU 5357  CB  ALA A 677     9766   5171   6267  -3094   3554  -1220       C  
ATOM   5358  N   HIS A 678      11.756  97.611  -1.238  1.00 55.33           N  
ANISOU 5358  N   HIS A 678    10173   4693   6158  -2918   3402  -1023       N  
ATOM   5359  CA  HIS A 678      12.524  96.481  -0.719  1.00 55.99           C  
ANISOU 5359  CA  HIS A 678    10416   4663   6196  -2873   3380   -902       C  
ATOM   5360  C   HIS A 678      13.403  95.869  -1.805  1.00 55.47           C  
ANISOU 5360  C   HIS A 678    10480   4456   6142  -2763   3281   -900       C  
ATOM   5361  O   HIS A 678      13.532  94.644  -1.909  1.00 56.70           O  
ANISOU 5361  O   HIS A 678    10733   4493   6318  -2796   3251   -862       O  
ATOM   5362  CB  HIS A 678      11.603  95.424  -0.106  1.00 58.27           C  
ANISOU 5362  CB  HIS A 678    10687   4934   6519  -3055   3434   -880       C  
ATOM   5363  CG  HIS A 678      10.661  94.795  -1.085  1.00 59.52           C  
ANISOU 5363  CG  HIS A 678    10793   5040   6783  -3198   3414   -986       C  
ATOM   5364  ND1 HIS A 678      11.070  93.866  -2.018  1.00 59.86           N  
ANISOU 5364  ND1 HIS A 678    10946   4932   6867  -3165   3327   -996       N  
ATOM   5365  CD2 HIS A 678       9.330  94.955  -1.273  1.00 60.62           C  
ANISOU 5365  CD2 HIS A 678    10770   5264   6998  -3369   3460  -1095       C  
ATOM   5366  CE1 HIS A 678      10.032  93.484  -2.740  1.00 61.10           C  
ANISOU 5366  CE1 HIS A 678    11016   5079   7121  -3308   3314  -1107       C  
ATOM   5367  NE2 HIS A 678       8.964  94.129  -2.308  1.00 61.58           N  
ANISOU 5367  NE2 HIS A 678    10909   5281   7207  -3437   3394  -1170       N  
ATOM   5368  N   ALA A 679      14.027  96.713  -2.622  1.00 53.77           N  
ANISOU 5368  N   ALA A 679    10263   4253   5913  -2628   3225   -940       N  
ATOM   5369  CA  ALA A 679      15.026  96.291  -3.604  1.00 53.12           C  
ANISOU 5369  CA  ALA A 679    10292   4069   5820  -2489   3129   -933       C  
ATOM   5370  C   ALA A 679      16.375  96.788  -3.088  1.00 51.65           C  
ANISOU 5370  C   ALA A 679    10185   3896   5544  -2307   3116   -831       C  
ATOM   5371  O   ALA A 679      16.846  97.861  -3.469  1.00 50.11           O  
ANISOU 5371  O   ALA A 679     9955   3759   5326  -2199   3092   -848       O  
ATOM   5372  CB  ALA A 679      14.709  96.837  -4.991  1.00 52.50           C  
ANISOU 5372  CB  ALA A 679    10144   4010   5793  -2468   3060  -1061       C  
ATOM   5373  N   LEU A 680      16.998  95.994  -2.215  1.00 52.25           N  
ANISOU 5373  N   LEU A 680    10364   3915   5575  -2274   3124   -726       N  
ATOM   5374  CA  LEU A 680      18.109  96.465  -1.403  1.00 51.17           C  
ANISOU 5374  CA  LEU A 680    10276   3808   5357  -2127   3119   -634       C  
ATOM   5375  C   LEU A 680      19.402  95.683  -1.575  1.00 51.05           C  
ANISOU 5375  C   LEU A 680    10401   3692   5304  -1989   3054   -564       C  
ATOM   5376  O   LEU A 680      20.445  96.151  -1.105  1.00 50.00           O  
ANISOU 5376  O   LEU A 680    10301   3586   5110  -1848   3034   -505       O  
ATOM   5377  CB  LEU A 680      17.718  96.442   0.083  1.00 51.98           C  
ANISOU 5377  CB  LEU A 680    10353   3968   5430  -2200   3183   -572       C  
ATOM   5378  CG  LEU A 680      16.331  97.004   0.405  1.00 52.58           C  
ANISOU 5378  CG  LEU A 680    10282   4153   5544  -2359   3260   -638       C  
ATOM   5379  CD1 LEU A 680      15.993  96.816   1.876  1.00 53.67           C  
ANISOU 5379  CD1 LEU A 680    10400   4350   5644  -2427   3318   -567       C  
ATOM   5380  CD2 LEU A 680      16.244  98.470   0.014  1.00 51.01           C  
ANISOU 5380  CD2 LEU A 680     9971   4063   5348  -2304   3263   -707       C  
ATOM   5381  N   ARG A 681      19.373  94.512  -2.218  1.00 52.20           N  
ANISOU 5381  N   ARG A 681    10621   3721   5489  -2022   3015   -576       N  
ATOM   5382  CA  ARG A 681      20.590  93.716  -2.354  1.00 52.28           C  
ANISOU 5382  CA  ARG A 681    10761   3634   5470  -1892   2954   -513       C  
ATOM   5383  C   ARG A 681      21.660  94.472  -3.130  1.00 50.57           C  
ANISOU 5383  C   ARG A 681    10543   3458   5212  -1717   2904   -526       C  
ATOM   5384  O   ARG A 681      22.834  94.475  -2.743  1.00 49.99           O  
ANISOU 5384  O   ARG A 681    10534   3376   5082  -1581   2880   -457       O  
ATOM   5385  CB  ARG A 681      20.274  92.386  -3.038  1.00 53.90           C  
ANISOU 5385  CB  ARG A 681    11032   3706   5743  -1961   2911   -543       C  
ATOM   5386  CG  ARG A 681      18.922  91.808  -2.674  1.00 55.62           C  
ANISOU 5386  CG  ARG A 681    11210   3898   6026  -2167   2959   -565       C  
ATOM   5387  CD  ARG A 681      18.692  90.472  -3.356  1.00 57.32           C  
ANISOU 5387  CD  ARG A 681    11495   3966   6318  -2228   2904   -596       C  
ATOM   5388  NE  ARG A 681      18.587  89.389  -2.384  1.00 59.13           N  
ANISOU 5388  NE  ARG A 681    11809   4095   6561  -2308   2920   -502       N  
ATOM   5389  CZ  ARG A 681      19.565  88.534  -2.104  1.00 59.72           C  
ANISOU 5389  CZ  ARG A 681    12016   4057   6619  -2213   2870   -421       C  
ATOM   5390  NH1 ARG A 681      19.373  87.583  -1.200  1.00 61.52           N1+
ANISOU 5390  NH1 ARG A 681    12317   4193   6866  -2300   2883   -330       N1+
ATOM   5391  NH2 ARG A 681      20.730  88.622  -2.732  1.00 58.64           N  
ANISOU 5391  NH2 ARG A 681    11934   3898   6449  -2034   2806   -430       N  
ATOM   5392  N   PHE A 682      21.272  95.122  -4.230  1.00 49.85           N  
ANISOU 5392  N   PHE A 682    10373   3416   5150  -1721   2884   -614       N  
ATOM   5393  CA  PHE A 682      22.214  95.942  -4.984  1.00 48.31           C  
ANISOU 5393  CA  PHE A 682    10162   3274   4917  -1567   2838   -618       C  
ATOM   5394  C   PHE A 682      22.491  97.263  -4.279  1.00 46.90           C  
ANISOU 5394  C   PHE A 682     9923   3204   4694  -1513   2875   -583       C  
ATOM   5395  O   PHE A 682      23.619  97.767  -4.320  1.00 45.81           O  
ANISOU 5395  O   PHE A 682     9803   3096   4506  -1369   2848   -536       O  
ATOM   5396  CB  PHE A 682      21.680  96.195  -6.393  1.00 48.18           C  
ANISOU 5396  CB  PHE A 682    10079   3279   4947  -1585   2789   -724       C  
ATOM   5397  CG  PHE A 682      21.902  95.052  -7.338  1.00 49.20           C  
ANISOU 5397  CG  PHE A 682    10275   3313   5104  -1562   2721   -765       C  
ATOM   5398  CD1 PHE A 682      21.116  93.914  -7.268  1.00 50.90           C  
ANISOU 5398  CD1 PHE A 682    10527   3432   5382  -1690   2724   -799       C  
ATOM   5399  CD2 PHE A 682      22.896  95.117  -8.300  1.00 48.57           C  
ANISOU 5399  CD2 PHE A 682    10217   3243   4995  -1414   2653   -774       C  
ATOM   5400  CE1 PHE A 682      21.321  92.862  -8.137  1.00 51.95           C  
ANISOU 5400  CE1 PHE A 682    10722   3468   5550  -1665   2653   -848       C  
ATOM   5401  CE2 PHE A 682      23.105  94.069  -9.172  1.00 49.62           C  
ANISOU 5401  CE2 PHE A 682    10408   3291   5153  -1386   2588   -827       C  
ATOM   5402  CZ  PHE A 682      22.316  92.940  -9.091  1.00 51.30           C  
ANISOU 5402  CZ  PHE A 682    10662   3397   5433  -1509   2585   -867       C  
ATOM   5403  N   LEU A 683      21.471  97.832  -3.634  1.00 47.03           N  
ANISOU 5403  N   LEU A 683     9856   3278   4732  -1628   2935   -609       N  
ATOM   5404  CA  LEU A 683      21.650  99.078  -2.897  1.00 45.88           C  
ANISOU 5404  CA  LEU A 683     9645   3230   4557  -1581   2963   -586       C  
ATOM   5405  C   LEU A 683      22.712  98.930  -1.813  1.00 45.66           C  
ANISOU 5405  C   LEU A 683     9682   3196   4472  -1475   2953   -498       C  
ATOM   5406  O   LEU A 683      23.570  99.805  -1.651  1.00 44.44           O  
ANISOU 5406  O   LEU A 683     9506   3090   4288  -1351   2926   -473       O  
ATOM   5407  CB  LEU A 683      20.312  99.512  -2.297  1.00 46.42           C  
ANISOU 5407  CB  LEU A 683     9612   3361   4665  -1734   3029   -632       C  
ATOM   5408  CG  LEU A 683      20.007 101.003  -2.129  1.00 45.34           C  
ANISOU 5408  CG  LEU A 683     9358   3334   4535  -1722   3049   -663       C  
ATOM   5409  CD1 LEU A 683      20.400 101.501  -0.753  1.00 45.03           C  
ANISOU 5409  CD1 LEU A 683     9289   3361   4459  -1666   3057   -603       C  
ATOM   5410  CD2 LEU A 683      20.674 101.821  -3.217  1.00 44.02           C  
ANISOU 5410  CD2 LEU A 683     9186   3172   4367  -1607   2991   -680       C  
ATOM   5411  N   ASN A 684      22.687  97.815  -1.076  1.00 46.94           N  
ANISOU 5411  N   ASN A 684     9920   3290   4626  -1521   2965   -449       N  
ATOM   5412  CA  ASN A 684      23.677  97.605  -0.024  1.00 46.93           C  
ANISOU 5412  CA  ASN A 684     9981   3275   4574  -1422   2945   -365       C  
ATOM   5413  C   ASN A 684      25.018  97.168  -0.599  1.00 46.52           C  
ANISOU 5413  C   ASN A 684    10021   3163   4490  -1274   2887   -332       C  
ATOM   5414  O   ASN A 684      26.073  97.612  -0.131  1.00 45.72           O  
ANISOU 5414  O   ASN A 684     9932   3089   4350  -1146   2858   -289       O  
ATOM   5415  CB  ASN A 684      23.178  96.567   0.982  1.00 48.61           C  
ANISOU 5415  CB  ASN A 684    10248   3435   4788  -1527   2975   -312       C  
ATOM   5416  CG  ASN A 684      22.232  97.151   2.015  1.00 48.94           C  
ANISOU 5416  CG  ASN A 684    10194   3569   4834  -1632   3031   -314       C  
ATOM   5417  OD1 ASN A 684      22.223  98.359   2.257  1.00 47.82           O  
ANISOU 5417  OD1 ASN A 684     9955   3527   4688  -1591   3033   -339       O  
ATOM   5418  ND2 ASN A 684      21.436  96.290   2.638  1.00 50.62           N  
ANISOU 5418  ND2 ASN A 684    10428   3749   5056  -1769   3074   -283       N  
ATOM   5419  N   ASP A 685      25.002  96.294  -1.610  1.00 47.16           N  
ANISOU 5419  N   ASP A 685    10160   3165   4594  -1288   2865   -354       N  
ATOM   5420  CA  ASP A 685      26.253  95.730  -2.110  1.00 47.08           C  
ANISOU 5420  CA  ASP A 685    10237   3095   4555  -1152   2810   -320       C  
ATOM   5421  C   ASP A 685      27.115  96.784  -2.795  1.00 45.48           C  
ANISOU 5421  C   ASP A 685     9985   2973   4323  -1022   2785   -330       C  
ATOM   5422  O   ASP A 685      28.340  96.632  -2.863  1.00 45.17           O  
ANISOU 5422  O   ASP A 685     9998   2919   4247   -890   2750   -287       O  
ATOM   5423  CB  ASP A 685      25.966  94.567  -3.060  1.00 48.28           C  
ANISOU 5423  CB  ASP A 685    10448   3141   4754  -1199   2778   -355       C  
ATOM   5424  CG  ASP A 685      27.205  93.762  -3.386  1.00 48.62           C  
ANISOU 5424  CG  ASP A 685    10590   3104   4778  -1066   2720   -320       C  
ATOM   5425  OD1 ASP A 685      27.678  93.012  -2.506  1.00 49.49           O  
ANISOU 5425  OD1 ASP A 685    10787   3144   4871  -1041   2711   -253       O  
ATOM   5426  OD2 ASP A 685      27.700  93.879  -4.525  1.00 48.12           O1+
ANISOU 5426  OD2 ASP A 685    10515   3051   4719   -986   2678   -359       O1+
ATOM   5427  N   MET A 686      26.503  97.850  -3.308  1.00 45.11           N  
ANISOU 5427  N   MET A 686     9837   3008   4295  -1061   2802   -380       N  
ATOM   5428  CA  MET A 686      27.264  98.964  -3.861  1.00 43.69           C  
ANISOU 5428  CA  MET A 686     9602   2907   4090   -950   2779   -373       C  
ATOM   5429  C   MET A 686      27.862  99.863  -2.785  1.00 42.82           C  
ANISOU 5429  C   MET A 686     9460   2854   3954   -875   2784   -344       C  
ATOM   5430  O   MET A 686      28.564 100.826  -3.120  1.00 41.70           O  
ANISOU 5430  O   MET A 686     9254   2773   3819   -781   2743   -328       O  
ATOM   5431  CB  MET A 686      26.382  99.794  -4.798  1.00 43.18           C  
ANISOU 5431  CB  MET A 686     9439   2899   4067  -1017   2778   -432       C  
ATOM   5432  CG  MET A 686      25.955  99.068  -6.065  1.00 43.90           C  
ANISOU 5432  CG  MET A 686     9537   2943   4200  -1054   2735   -492       C  
ATOM   5433  SD  MET A 686      24.977 100.115  -7.159  1.00 43.36           S  
ANISOU 5433  SD  MET A 686     9336   2957   4181  -1104   2702   -581       S  
ATOM   5434  CE  MET A 686      23.581 100.497  -6.104  1.00 43.71           C  
ANISOU 5434  CE  MET A 686     9328   3018   4260  -1264   2782   -619       C  
ATOM   5435  N   GLY A 687      27.609  99.568  -1.510  1.00 43.57           N  
ANISOU 5435  N   GLY A 687     9570   2928   4055   -915   2798   -323       N  
ATOM   5436  CA  GLY A 687      28.080 100.381  -0.412  1.00 42.93           C  
ANISOU 5436  CA  GLY A 687     9440   2892   3980   -854   2776   -295       C  
ATOM   5437  C   GLY A 687      27.211 101.570  -0.076  1.00 42.34           C  
ANISOU 5437  C   GLY A 687     9237   2894   3957   -919   2782   -328       C  
ATOM   5438  O   GLY A 687      27.557 102.330   0.839  1.00 41.85           O  
ANISOU 5438  O   GLY A 687     9112   2880   3907   -873   2753   -296       O  
ATOM   5439  N   LYS A 688      26.094 101.754  -0.775  1.00 41.81           N  
ANISOU 5439  N   LYS A 688     9123   2844   3917  -1026   2818   -388       N  
ATOM   5440  CA  LYS A 688      25.242 102.918  -0.568  1.00 41.32           C  
ANISOU 5440  CA  LYS A 688     8932   2863   3905  -1085   2824   -420       C  
ATOM   5441  C   LYS A 688      24.230 102.658   0.538  1.00 42.31           C  
ANISOU 5441  C   LYS A 688     9023   3022   4032  -1205   2878   -422       C  
ATOM   5442  O   LYS A 688      23.023 102.800   0.323  1.00 42.77           O  
ANISOU 5442  O   LYS A 688     9020   3116   4117  -1328   2928   -477       O  
ATOM   5443  CB  LYS A 688      24.524 103.290  -1.868  1.00 41.08           C  
ANISOU 5443  CB  LYS A 688     8866   2843   3901  -1143   2839   -484       C  
ATOM   5444  CG  LYS A 688      25.459 103.479  -3.055  1.00 40.31           C  
ANISOU 5444  CG  LYS A 688     8792   2727   3799  -1036   2782   -465       C  
ATOM   5445  CD  LYS A 688      26.318 104.714  -2.876  1.00 39.13           C  
ANISOU 5445  CD  LYS A 688     8557   2623   3686   -927   2709   -412       C  
ATOM   5446  CE  LYS A 688      27.515 104.697  -3.813  1.00 38.58           C  
ANISOU 5446  CE  LYS A 688     8500   2552   3605   -812   2644   -355       C  
ATOM   5447  NZ  LYS A 688      28.531 103.690  -3.399  1.00 38.96           N1+
ANISOU 5447  NZ  LYS A 688     8638   2554   3612   -734   2635   -319       N1+
ATOM   5448  N   VAL A 689      24.713 102.290   1.727  1.00 43.69           N  
ANISOU 5448  N   VAL A 689     9234   3192   4175  -1173   2871   -361       N  
ATOM   5449  CA  VAL A 689      23.811 101.964   2.824  1.00 44.84           C  
ANISOU 5449  CA  VAL A 689     9355   3372   4308  -1288   2926   -349       C  
ATOM   5450  C   VAL A 689      22.993 103.189   3.213  1.00 44.46           C  
ANISOU 5450  C   VAL A 689     9159   3446   4289  -1333   2944   -391       C  
ATOM   5451  O   VAL A 689      23.481 104.326   3.183  1.00 43.32           O  
ANISOU 5451  O   VAL A 689     8939   3360   4162  -1241   2894   -393       O  
ATOM   5452  CB  VAL A 689      24.601 101.410   4.022  1.00 45.39           C  
ANISOU 5452  CB  VAL A 689     9498   3420   4327  -1231   2908   -264       C  
ATOM   5453  CG1 VAL A 689      25.208 100.056   3.678  1.00 46.13           C  
ANISOU 5453  CG1 VAL A 689     9738   3395   4393  -1206   2899   -226       C  
ATOM   5454  CG2 VAL A 689      25.681 102.389   4.446  1.00 44.22           C  
ANISOU 5454  CG2 VAL A 689     9309   3319   4172  -1090   2844   -234       C  
ATOM   5455  N   ARG A 690      21.739 102.955   3.593  1.00 45.12           N  
ANISOU 5455  N   ARG A 690     9191   3575   4376  -1478   3016   -424       N  
ATOM   5456  CA  ARG A 690      20.815 104.046   3.856  1.00 44.98           C  
ANISOU 5456  CA  ARG A 690     9023   3685   4382  -1530   3046   -483       C  
ATOM   5457  C   ARG A 690      20.999 104.593   5.269  1.00 45.13           C  
ANISOU 5457  C   ARG A 690     8986   3798   4362  -1492   3042   -444       C  
ATOM   5458  O   ARG A 690      21.621 103.969   6.133  1.00 45.64           O  
ANISOU 5458  O   ARG A 690     9132   3829   4379  -1461   3033   -368       O  
ATOM   5459  CB  ARG A 690      19.373 103.586   3.654  1.00 46.21           C  
ANISOU 5459  CB  ARG A 690     9131   3868   4558  -1705   3133   -547       C  
ATOM   5460  CG  ARG A 690      19.070 103.109   2.247  1.00 46.19           C  
ANISOU 5460  CG  ARG A 690     9172   3784   4592  -1757   3141   -597       C  
ATOM   5461  CD  ARG A 690      17.744 102.377   2.197  1.00 47.71           C  
ANISOU 5461  CD  ARG A 690     9336   3984   4810  -1944   3225   -646       C  
ATOM   5462  NE  ARG A 690      17.708 101.273   3.150  1.00 49.09           N  
ANISOU 5462  NE  ARG A 690     9585   4116   4953  -2007   3252   -576       N  
ATOM   5463  CZ  ARG A 690      16.639 100.518   3.378  1.00 50.71           C  
ANISOU 5463  CZ  ARG A 690     9767   4325   5176  -2174   3321   -594       C  
ATOM   5464  NH1 ARG A 690      16.697  99.536   4.267  1.00 52.03           N1+
ANISOU 5464  NH1 ARG A 690    10010   4451   5309  -2222   3339   -512       N1+
ATOM   5465  NH2 ARG A 690      15.512 100.745   2.720  1.00 51.12           N  
ANISOU 5465  NH2 ARG A 690     9716   4424   5282  -2298   3370   -691       N  
ATOM   5466  N   LYS A 691      20.431 105.775   5.499  1.00 51.43           N  
ANISOU 5466  N   LYS A 691     9643   4721   5178  -1493   3050   -503       N  
ATOM   5467  CA  LYS A 691      20.643 106.506   6.740  1.00 51.46           C  
ANISOU 5467  CA  LYS A 691     9580   4830   5143  -1439   3039   -483       C  
ATOM   5468  C   LYS A 691      19.524 106.235   7.737  1.00 52.99           C  
ANISOU 5468  C   LYS A 691     9710   5124   5298  -1564   3127   -504       C  
ATOM   5469  O   LYS A 691      18.354 106.115   7.360  1.00 53.71           O  
ANISOU 5469  O   LYS A 691     9733   5256   5417  -1683   3192   -574       O  
ATOM   5470  CB  LYS A 691      20.735 108.010   6.470  1.00 50.32           C  
ANISOU 5470  CB  LYS A 691     9315   4770   5033  -1352   2991   -542       C  
ATOM   5471  CG  LYS A 691      21.403 108.801   7.587  1.00 50.03           C  
ANISOU 5471  CG  LYS A 691     9241   4811   4959  -1255   2952   -514       C  
ATOM   5472  CD  LYS A 691      21.165 110.296   7.429  1.00 49.32           C  
ANISOU 5472  CD  LYS A 691     9013   4822   4905  -1194   2920   -597       C  
ATOM   5473  CE  LYS A 691      22.076 111.109   8.340  1.00 48.89           C  
ANISOU 5473  CE  LYS A 691     8941   4818   4819  -1080   2865   -571       C  
ATOM   5474  NZ  LYS A 691      23.497 111.081   7.870  1.00 48.53           N1+
ANISOU 5474  NZ  LYS A 691     8986   4666   4787   -974   2786   -493       N1+
ATOM   5475  N   ASP A 692      19.904 106.140   9.011  1.00 54.45           N  
ANISOU 5475  N   ASP A 692     9916   5357   5415  -1536   3128   -442       N  
ATOM   5476  CA  ASP A 692      18.982 106.039  10.143  1.00 55.98           C  
ANISOU 5476  CA  ASP A 692    10039   5676   5554  -1632   3207   -450       C  
ATOM   5477  C   ASP A 692      17.904 104.983   9.902  1.00 57.40           C  
ANISOU 5477  C   ASP A 692    10234   5830   5745  -1801   3291   -459       C  
ATOM   5478  O   ASP A 692      16.702 105.245   9.961  1.00 57.93           O  
ANISOU 5478  O   ASP A 692    10179   6006   5826  -1906   3362   -538       O  
ATOM   5479  CB  ASP A 692      18.362 107.402  10.458  1.00 55.68           C  
ANISOU 5479  CB  ASP A 692     9829   5803   5522  -1608   3218   -550       C  
ATOM   5480  CG  ASP A 692      19.389 108.408  10.935  1.00 54.65           C  
ANISOU 5480  CG  ASP A 692     9684   5710   5372  -1454   3139   -537       C  
ATOM   5481  OD1 ASP A 692      19.834 108.299  12.098  1.00 55.21           O  
ANISOU 5481  OD1 ASP A 692     9785   5830   5364  -1421   3139   -479       O  
ATOM   5482  OD2 ASP A 692      19.752 109.307  10.149  1.00 53.45           O1+
ANISOU 5482  OD2 ASP A 692     9490   5540   5279  -1368   3078   -585       O1+
ATOM   5483  N   THR A 693      18.369 103.768   9.630  1.00 56.14           N  
ANISOU 5483  N   THR A 693    10224   5526   5582  -1824   3281   -382       N  
ATOM   5484  CA  THR A 693      17.505 102.616   9.423  1.00 57.65           C  
ANISOU 5484  CA  THR A 693    10454   5665   5784  -1982   3350   -374       C  
ATOM   5485  C   THR A 693      18.372 101.369   9.474  1.00 57.83           C  
ANISOU 5485  C   THR A 693    10657   5535   5781  -1957   3317   -267       C  
ATOM   5486  O   THR A 693      19.601 101.441   9.375  1.00 56.56           O  
ANISOU 5486  O   THR A 693    10579   5302   5609  -1816   3240   -222       O  
ATOM   5487  CB  THR A 693      16.755 102.689   8.088  1.00 57.18           C  
ANISOU 5487  CB  THR A 693    10344   5575   5807  -2056   3371   -473       C  
ATOM   5488  OG1 THR A 693      15.888 101.556   7.961  1.00 58.54           O  
ANISOU 5488  OG1 THR A 693    10548   5702   5995  -2221   3438   -467       O  
ATOM   5489  CG2 THR A 693      17.738 102.701   6.929  1.00 55.58           C  
ANISOU 5489  CG2 THR A 693    10233   5242   5643  -1942   3290   -472       C  
ATOM   5490  N   GLN A 694      17.715 100.225   9.631  1.00 54.42           N  
ANISOU 5490  N   GLN A 694    10277   5057   5345  -2096   3374   -229       N  
ATOM   5491  CA  GLN A 694      18.413  98.951   9.646  1.00 55.13           C  
ANISOU 5491  CA  GLN A 694    10535   4996   5417  -2084   3344   -131       C  
ATOM   5492  C   GLN A 694      18.704  98.501   8.218  1.00 54.37           C  
ANISOU 5492  C   GLN A 694    10511   4760   5388  -2061   3303   -175       C  
ATOM   5493  O   GLN A 694      17.955  98.801   7.285  1.00 54.04           O  
ANISOU 5493  O   GLN A 694    10394   4732   5406  -2128   3327   -270       O  
ATOM   5494  CB  GLN A 694      17.582  97.916  10.402  1.00 57.45           C  
ANISOU 5494  CB  GLN A 694    10853   5293   5682  -2247   3417    -64       C  
ATOM   5495  CG  GLN A 694      17.099  98.443  11.750  1.00 58.36           C  
ANISOU 5495  CG  GLN A 694    10872   5580   5723  -2286   3473    -35       C  
ATOM   5496  CD  GLN A 694      16.058  97.560  12.405  1.00 60.77           C  
ANISOU 5496  CD  GLN A 694    11167   5919   6006  -2470   3561     20       C  
ATOM   5497  OE1 GLN A 694      16.050  96.344  12.220  1.00 61.99           O  
ANISOU 5497  OE1 GLN A 694    11435   5941   6178  -2544   3562     89       O  
ATOM   5498  NE2 GLN A 694      15.167  98.173  13.177  1.00 61.60           N  
ANISOU 5498  NE2 GLN A 694    11130   6204   6070  -2544   3636    -12       N  
ATOM   5499  N   GLU A 695      19.813  97.776   8.055  1.00 53.98           N  
ANISOU 5499  N   GLU A 695    10604   4583   5321  -1962   3241   -108       N  
ATOM   5500  CA  GLU A 695      20.393  97.564   6.731  1.00 52.95           C  
ANISOU 5500  CA  GLU A 695    10538   4343   5237  -1888   3189   -151       C  
ATOM   5501  C   GLU A 695      19.522  96.720   5.806  1.00 53.93           C  
ANISOU 5501  C   GLU A 695    10681   4390   5420  -2024   3222   -197       C  
ATOM   5502  O   GLU A 695      19.842  96.617   4.616  1.00 53.15           O  
ANISOU 5502  O   GLU A 695    10617   4220   5358  -1975   3184   -247       O  
ATOM   5503  CB  GLU A 695      21.776  96.922   6.863  1.00 52.78           C  
ANISOU 5503  CB  GLU A 695    10659   4217   5179  -1751   3120    -70       C  
ATOM   5504  CG  GLU A 695      22.697  97.198   5.680  1.00 51.22           C  
ANISOU 5504  CG  GLU A 695    10494   3963   5006  -1616   3057   -117       C  
ATOM   5505  CD  GLU A 695      24.016  96.461   5.772  1.00 51.29           C  
ANISOU 5505  CD  GLU A 695    10637   3872   4979  -1489   2997    -44       C  
ATOM   5506  OE1 GLU A 695      24.446  96.150   6.903  1.00 52.03           O  
ANISOU 5506  OE1 GLU A 695    10782   3966   5023  -1463   2989     42       O  
ATOM   5507  OE2 GLU A 695      24.620  96.190   4.711  1.00 50.70           O1+
ANISOU 5507  OE2 GLU A 695    10616   3726   4922  -1413   2958    -73       O1+
ATOM   5508  N   TRP A 696      18.439  96.121   6.300  1.00 60.17           N  
ANISOU 5508  N   TRP A 696    14439   4158   4266  -1291   1781   -472       N  
ATOM   5509  CA  TRP A 696      17.574  95.331   5.435  1.00 61.47           C  
ANISOU 5509  CA  TRP A 696    14711   4282   4365  -1507   1823   -507       C  
ATOM   5510  C   TRP A 696      16.087  95.553   5.673  1.00 62.11           C  
ANISOU 5510  C   TRP A 696    14733   4400   4465  -1864   1986   -571       C  
ATOM   5511  O   TRP A 696      15.276  94.923   4.987  1.00 63.39           O  
ANISOU 5511  O   TRP A 696    14966   4542   4577  -2067   2020   -619       O  
ATOM   5512  CB  TRP A 696      17.899  93.836   5.576  1.00 63.65           C  
ANISOU 5512  CB  TRP A 696    15373   4359   4450  -1470   1788   -435       C  
ATOM   5513  CG  TRP A 696      19.259  93.497   5.054  1.00 63.34           C  
ANISOU 5513  CG  TRP A 696    15379   4295   4392  -1138   1628   -399       C  
ATOM   5514  CD1 TRP A 696      20.385  93.265   5.788  1.00 63.55           C  
ANISOU 5514  CD1 TRP A 696    15529   4250   4365   -879   1541   -336       C  
ATOM   5515  CD2 TRP A 696      19.644  93.376   3.679  1.00 62.94           C  
ANISOU 5515  CD2 TRP A 696    15244   4298   4371  -1025   1540   -432       C  
ATOM   5516  NE1 TRP A 696      21.445  92.996   4.956  1.00 63.35           N  
ANISOU 5516  NE1 TRP A 696    15488   4240   4341   -617   1414   -337       N  
ATOM   5517  CE2 TRP A 696      21.016  93.059   3.656  1.00 62.96           C  
ANISOU 5517  CE2 TRP A 696    15319   4262   4339   -702   1420   -390       C  
ATOM   5518  CE3 TRP A 696      18.960  93.500   2.465  1.00 62.73           C  
ANISOU 5518  CE3 TRP A 696    15098   4348   4389  -1162   1548   -498       C  
ATOM   5519  CZ2 TRP A 696      21.718  92.864   2.468  1.00 62.77           C  
ANISOU 5519  CZ2 TRP A 696    15252   4273   4325   -519   1334   -407       C  
ATOM   5520  CZ3 TRP A 696      19.658  93.306   1.287  1.00 62.51           C  
ANISOU 5520  CZ3 TRP A 696    15045   4344   4362   -973   1449   -507       C  
ATOM   5521  CH2 TRP A 696      21.022  92.992   1.297  1.00 62.53           C  
ANISOU 5521  CH2 TRP A 696    15122   4306   4331   -658   1356   -460       C  
ATOM   5522  N   LYS A 697      15.703  96.416   6.603  1.00 61.41           N  
ANISOU 5522  N   LYS A 697    14514   4371   4448  -1945   2088   -583       N  
ATOM   5523  CA  LYS A 697      14.295  96.758   6.755  1.00 61.98           C  
ANISOU 5523  CA  LYS A 697    14474   4514   4564  -2275   2254   -668       C  
ATOM   5524  C   LYS A 697      13.831  97.516   5.516  1.00 60.78           C  
ANISOU 5524  C   LYS A 697    14006   4530   4557  -2336   2206   -773       C  
ATOM   5525  O   LYS A 697      14.518  98.445   5.074  1.00 58.76           O  
ANISOU 5525  O   LYS A 697    13527   4387   4413  -2130   2108   -777       O  
ATOM   5526  CB  LYS A 697      14.079  97.602   8.012  1.00 61.43           C  
ANISOU 5526  CB  LYS A 697    14323   4473   4544  -2316   2374   -657       C  
ATOM   5527  CG  LYS A 697      12.615  97.810   8.384  1.00 62.53           C  
ANISOU 5527  CG  LYS A 697    14383   4674   4703  -2661   2584   -752       C  
ATOM   5528  CD  LYS A 697      12.439  98.999   9.323  1.00 61.38           C  
ANISOU 5528  CD  LYS A 697    14054   4609   4660  -2667   2683   -763       C  
ATOM   5529  CE  LYS A 697      12.944  98.707  10.729  1.00 62.13           C  
ANISOU 5529  CE  LYS A 697    14398   4564   4643  -2559   2721   -662       C  
ATOM   5530  NZ  LYS A 697      12.002  97.852  11.506  1.00 64.76           N1+
ANISOU 5530  NZ  LYS A 697    14903   4832   4870  -2769   2878   -722       N1+
ATOM   5531  N   PRO A 698      12.701  97.142   4.915  1.00 62.11           N  
ANISOU 5531  N   PRO A 698    14150   4721   4727  -2605   2262   -865       N  
ATOM   5532  CA  PRO A 698      12.205  97.889   3.752  1.00 61.16           C  
ANISOU 5532  CA  PRO A 698    13734   4753   4749  -2664   2195   -971       C  
ATOM   5533  C   PRO A 698      11.970  99.353   4.095  1.00 59.37           C  
ANISOU 5533  C   PRO A 698    13187   4685   4687  -2669   2246  -1021       C  
ATOM   5534  O   PRO A 698      11.644  99.705   5.230  1.00 59.49           O  
ANISOU 5534  O   PRO A 698    13186   4697   4720  -2758   2383  -1014       O  
ATOM   5535  CB  PRO A 698      10.894  97.176   3.404  1.00 63.41           C  
ANISOU 5535  CB  PRO A 698    14051   5017   5025  -2989   2258  -1068       C  
ATOM   5536  CG  PRO A 698      11.064  95.796   3.948  1.00 65.44           C  
ANISOU 5536  CG  PRO A 698    14686   5093   5085  -3019   2308   -993       C  
ATOM   5537  CD  PRO A 698      11.881  95.952   5.200  1.00 64.76           C  
ANISOU 5537  CD  PRO A 698    14735   4941   4929  -2850   2368   -882       C  
ATOM   5538  N   SER A 699      12.153 100.213   3.095  1.00 57.81           N  
ANISOU 5538  N   SER A 699    12749   4623   4595  -2564   2138  -1071       N  
ATOM   5539  CA  SER A 699      12.055 101.648   3.306  1.00 56.02           C  
ANISOU 5539  CA  SER A 699    12221   4552   4514  -2532   2168  -1115       C  
ATOM   5540  C   SER A 699      10.594 102.093   3.352  1.00 56.86           C  
ANISOU 5540  C   SER A 699    12115   4738   4753  -2851   2266  -1242       C  
ATOM   5541  O   SER A 699       9.675 101.370   2.959  1.00 58.73           O  
ANISOU 5541  O   SER A 699    12382   4937   4997  -3082   2276  -1307       O  
ATOM   5542  CB  SER A 699      12.806 102.411   2.213  1.00 54.23           C  
ANISOU 5542  CB  SER A 699    11825   4446   4332  -2293   2029  -1118       C  
ATOM   5543  OG  SER A 699      12.320 102.081   0.924  1.00 54.97           O  
ANISOU 5543  OG  SER A 699    11905   4561   4422  -2374   1936  -1189       O  
ATOM   5544  N   THR A 700      10.393 103.309   3.850  1.00 55.58           N  
ANISOU 5544  N   THR A 700    11710   4691   4718  -2857   2331  -1278       N  
ATOM   5545  CA  THR A 700       9.076 103.909   3.989  1.00 56.27           C  
ANISOU 5545  CA  THR A 700    11508   4882   4988  -3124   2417  -1375       C  
ATOM   5546  C   THR A 700       8.936 105.066   3.009  1.00 54.84           C  
ANISOU 5546  C   THR A 700    10921   4946   4970  -3006   2279  -1384       C  
ATOM   5547  O   THR A 700       9.873 105.848   2.818  1.00 52.86           O  
ANISOU 5547  O   THR A 700    10583   4787   4714  -2734   2204  -1313       O  
ATOM   5548  CB  THR A 700       8.851 104.401   5.424  1.00 56.20           C  
ANISOU 5548  CB  THR A 700    11463   4869   5021  -3185   2598  -1347       C  
ATOM   5549  OG1 THR A 700       8.885 103.283   6.321  1.00 57.85           O  
ANISOU 5549  OG1 THR A 700    12001   4912   5069  -3252   2713  -1294       O  
ATOM   5550  CG2 THR A 700       7.513 105.109   5.556  1.00 56.93           C  
ANISOU 5550  CG2 THR A 700    11173   5122   5337  -3412   2683  -1418       C  
ATOM   5551  N   GLY A 701       7.761 105.163   2.379  1.00 56.04           N  
ANISOU 5551  N   GLY A 701    10832   5194   5267  -3211   2241  -1477       N  
ATOM   5552  CA  GLY A 701       7.471 106.218   1.438  1.00 55.09           C  
ANISOU 5552  CA  GLY A 701    10347   5289   5294  -3117   2100  -1499       C  
ATOM   5553  C   GLY A 701       6.354 107.128   1.929  1.00 55.46           C  
ANISOU 5553  C   GLY A 701    10014   5499   5560  -3270   2176  -1555       C  
ATOM   5554  O   GLY A 701       5.677 106.850   2.926  1.00 56.76           O  
ANISOU 5554  O   GLY A 701    10187   5607   5773  -3486   2352  -1589       O  
ATOM   5555  N   TRP A 702       6.172 108.229   1.206  1.00 54.45           N  
ANISOU 5555  N   TRP A 702     9562   5567   5558  -3147   2049  -1565       N  
ATOM   5556  CA  TRP A 702       5.134 109.209   1.497  1.00 54.77           C  
ANISOU 5556  CA  TRP A 702     9212   5784   5814  -3247   2085  -1624       C  
ATOM   5557  C   TRP A 702       4.052 109.138   0.429  1.00 56.44           C  
ANISOU 5557  C   TRP A 702     9208   6079   6155  -3386   1935  -1750       C  
ATOM   5558  O   TRP A 702       4.355 109.168  -0.769  1.00 56.07           O  
ANISOU 5558  O   TRP A 702     9189   6058   6057  -3251   1742  -1754       O  
ATOM   5559  CB  TRP A 702       5.712 110.626   1.558  1.00 52.47           C  
ANISOU 5559  CB  TRP A 702     8711   5653   5573  -2990   2044  -1546       C  
ATOM   5560  CG  TRP A 702       6.608 110.871   2.731  1.00 51.06           C  
ANISOU 5560  CG  TRP A 702     8674   5414   5312  -2869   2183  -1442       C  
ATOM   5561  CD1 TRP A 702       6.263 111.448   3.919  1.00 50.97           C  
ANISOU 5561  CD1 TRP A 702     8544   5441   5380  -2926   2339  -1430       C  
ATOM   5562  CD2 TRP A 702       8.000 110.549   2.831  1.00 49.71           C  
ANISOU 5562  CD2 TRP A 702     8792   5129   4965  -2662   2167  -1343       C  
ATOM   5563  NE1 TRP A 702       7.355 111.505   4.752  1.00 49.64           N  
ANISOU 5563  NE1 TRP A 702     8589   5183   5088  -2767   2406  -1330       N  
ATOM   5564  CE2 TRP A 702       8.433 110.959   4.108  1.00 48.87           C  
ANISOU 5564  CE2 TRP A 702     8730   4997   4843  -2602   2298  -1279       C  
ATOM   5565  CE3 TRP A 702       8.921 109.954   1.965  1.00 49.27           C  
ANISOU 5565  CE3 TRP A 702     8962   4991   4768  -2513   2055  -1308       C  
ATOM   5566  CZ2 TRP A 702       9.746 110.792   4.539  1.00 47.69           C  
ANISOU 5566  CZ2 TRP A 702     8824   4742   4553  -2400   2298  -1191       C  
ATOM   5567  CZ3 TRP A 702      10.225 109.789   2.395  1.00 48.09           C  
ANISOU 5567  CZ3 TRP A 702     9041   4745   4487  -2313   2075  -1220       C  
ATOM   5568  CH2 TRP A 702      10.625 110.207   3.670  1.00 47.33           C  
ANISOU 5568  CH2 TRP A 702     8968   4627   4390  -2258   2186  -1166       C  
ATOM   5569  N   SER A 703       2.795 109.046   0.863  1.00 58.43           N  
ANISOU 5569  N   SER A 703     9251   6371   6580  -3652   2024  -1859       N  
ATOM   5570  CA  SER A 703       1.675 109.129  -0.065  1.00 60.21           C  
ANISOU 5570  CA  SER A 703     9205   6699   6972  -3780   1867  -1998       C  
ATOM   5571  C   SER A 703       1.369 110.563  -0.477  1.00 59.21           C  
ANISOU 5571  C   SER A 703     8705   6798   6996  -3612   1743  -2014       C  
ATOM   5572  O   SER A 703       0.705 110.774  -1.498  1.00 60.27           O  
ANISOU 5572  O   SER A 703     8649   7022   7230  -3619   1541  -2113       O  
ATOM   5573  CB  SER A 703       0.426 108.493   0.553  1.00 63.02           C  
ANISOU 5573  CB  SER A 703     9445   7015   7484  -4137   2016  -2124       C  
ATOM   5574  OG  SER A 703       0.608 107.105   0.775  1.00 64.31           O  
ANISOU 5574  OG  SER A 703     9973   6955   7506  -4312   2108  -2125       O  
ATOM   5575  N   ASN A 704       1.846 111.545   0.284  1.00 57.33           N  
ANISOU 5575  N   ASN A 704     8376   6639   6766  -3455   1846  -1921       N  
ATOM   5576  CA  ASN A 704       1.571 112.957   0.050  1.00 56.39           C  
ANISOU 5576  CA  ASN A 704     7922   6722   6782  -3296   1754  -1928       C  
ATOM   5577  C   ASN A 704       2.863 113.645  -0.368  1.00 53.74           C  
ANISOU 5577  C   ASN A 704     7715   6404   6301  -2978   1667  -1792       C  
ATOM   5578  O   ASN A 704       3.854 113.611   0.371  1.00 52.19           O  
ANISOU 5578  O   ASN A 704     7718   6129   5985  -2880   1792  -1678       O  
ATOM   5579  CB  ASN A 704       0.986 113.602   1.308  1.00 56.61           C  
ANISOU 5579  CB  ASN A 704     7725   6830   6955  -3385   1957  -1940       C  
ATOM   5580  CG  ASN A 704       0.545 115.033   1.084  1.00 56.01           C  
ANISOU 5580  CG  ASN A 704     7289   6961   7033  -3239   1861  -1966       C  
ATOM   5581  OD1 ASN A 704       1.008 115.951   1.762  1.00 54.34           O  
ANISOU 5581  OD1 ASN A 704     7027   6806   6814  -3090   1945  -1879       O  
ATOM   5582  ND2 ASN A 704      -0.354 115.232   0.127  1.00 57.51           N  
ANISOU 5582  ND2 ASN A 704     7238   7254   7359  -3274   1671  -2090       N  
ATOM   5583  N   TRP A 705       2.855 114.259  -1.555  1.00 53.42           N  
ANISOU 5583  N   TRP A 705     7567   6456   6272  -2820   1452  -1811       N  
ATOM   5584  CA  TRP A 705       4.073 114.880  -2.066  1.00 51.19           C  
ANISOU 5584  CA  TRP A 705     7414   6181   5856  -2534   1382  -1689       C  
ATOM   5585  C   TRP A 705       4.434 116.153  -1.317  1.00 49.42           C  
ANISOU 5585  C   TRP A 705     7026   6063   5689  -2385   1468  -1610       C  
ATOM   5586  O   TRP A 705       5.602 116.556  -1.338  1.00 47.53           O  
ANISOU 5586  O   TRP A 705     6919   5799   5341  -2182   1482  -1494       O  
ATOM   5587  CB  TRP A 705       3.944 115.172  -3.563  1.00 51.57           C  
ANISOU 5587  CB  TRP A 705     7435   6279   5881  -2409   1142  -1731       C  
ATOM   5588  CG  TRP A 705       2.998 116.287  -3.923  1.00 52.17           C  
ANISOU 5588  CG  TRP A 705     7172   6526   6124  -2371   1015  -1811       C  
ATOM   5589  CD1 TRP A 705       1.683 116.167  -4.266  1.00 54.43           C  
ANISOU 5589  CD1 TRP A 705     7236   6880   6566  -2528    898  -1964       C  
ATOM   5590  CD2 TRP A 705       3.305 117.687  -3.999  1.00 50.66           C  
ANISOU 5590  CD2 TRP A 705     6832   6454   5961  -2154    979  -1748       C  
ATOM   5591  NE1 TRP A 705       1.150 117.403  -4.544  1.00 54.42           N  
ANISOU 5591  NE1 TRP A 705     6957   7035   6685  -2406    784  -2004       N  
ATOM   5592  CE2 TRP A 705       2.125 118.353  -4.386  1.00 52.15           C  
ANISOU 5592  CE2 TRP A 705     6724   6777   6314  -2178    836  -1868       C  
ATOM   5593  CE3 TRP A 705       4.461 118.440  -3.773  1.00 48.81           C  
ANISOU 5593  CE3 TRP A 705     6686   6222   5637  -1944   1052  -1609       C  
ATOM   5594  CZ2 TRP A 705       2.068 119.736  -4.551  1.00 52.11           C  
ANISOU 5594  CZ2 TRP A 705     6535   6899   6365  -1992    764  -1846       C  
ATOM   5595  CZ3 TRP A 705       4.402 119.812  -3.937  1.00 48.85           C  
ANISOU 5595  CZ3 TRP A 705     6504   6351   5706  -1779    990  -1586       C  
ATOM   5596  CH2 TRP A 705       3.215 120.446  -4.322  1.00 50.65           C  
ANISOU 5596  CH2 TRP A 705     6464   6703   6077  -1800    849  -1700       C  
ATOM   5597  N   GLU A 706       3.472 116.786  -0.652  1.00 51.02           N  
ANISOU 5597  N   GLU A 706     6942   6378   6064  -2483   1530  -1673       N  
ATOM   5598  CA  GLU A 706       3.748 117.959   0.165  1.00 50.25           C  
ANISOU 5598  CA  GLU A 706     6703   6370   6020  -2357   1621  -1603       C  
ATOM   5599  C   GLU A 706       4.399 117.608   1.500  1.00 48.31           C  
ANISOU 5599  C   GLU A 706     6635   6020   5702  -2395   1835  -1521       C  
ATOM   5600  O   GLU A 706       4.494 118.473   2.375  1.00 46.88           O  
ANISOU 5600  O   GLU A 706     6344   5897   5572  -2330   1932  -1476       O  
ATOM   5601  CB  GLU A 706       2.456 118.748   0.384  1.00 51.01           C  
ANISOU 5601  CB  GLU A 706     6436   6621   6323  -2435   1611  -1709       C  
ATOM   5602  CG  GLU A 706       2.004 119.542  -0.836  1.00 52.70           C  
ANISOU 5602  CG  GLU A 706     6464   6958   6602  -2304   1375  -1769       C  
ATOM   5603  CD  GLU A 706       0.602 120.094  -0.689  1.00 53.45           C  
ANISOU 5603  CD  GLU A 706     6195   7197   6917  -2402   1342  -1906       C  
ATOM   5604  OE1 GLU A 706      -0.354 119.290  -0.633  1.00 54.24           O  
ANISOU 5604  OE1 GLU A 706     6199   7285   7124  -2631   1361  -2030       O  
ATOM   5605  OE2 GLU A 706       0.455 121.334  -0.631  1.00 53.08           O1+
ANISOU 5605  OE2 GLU A 706     5956   7272   6942  -2249   1299  -1895       O1+
ATOM   5606  N   GLU A 707       4.848 116.363   1.668  1.00 48.72           N  
ANISOU 5606  N   GLU A 707     6976   5909   5627  -2487   1899  -1502       N  
ATOM   5607  CA  GLU A 707       5.571 115.939   2.856  1.00 47.54           C  
ANISOU 5607  CA  GLU A 707     7053   5633   5375  -2495   2072  -1423       C  
ATOM   5608  C   GLU A 707       6.939 115.346   2.558  1.00 46.91           C  
ANISOU 5608  C   GLU A 707     7290   5423   5110  -2342   2031  -1331       C  
ATOM   5609  O   GLU A 707       7.726 115.162   3.494  1.00 45.58           O  
ANISOU 5609  O   GLU A 707     7308   5157   4853  -2286   2136  -1259       O  
ATOM   5610  CB  GLU A 707       4.748 114.906   3.645  1.00 49.57           C  
ANISOU 5610  CB  GLU A 707     7394   5789   5653  -2776   2234  -1495       C  
ATOM   5611  CG  GLU A 707       3.402 115.406   4.128  1.00 51.05           C  
ANISOU 5611  CG  GLU A 707     7266   6094   6039  -2947   2325  -1593       C  
ATOM   5612  CD  GLU A 707       2.763 114.457   5.121  1.00 53.00           C  
ANISOU 5612  CD  GLU A 707     7628   6219   6292  -3217   2543  -1643       C  
ATOM   5613  OE1 GLU A 707       3.371 113.405   5.412  1.00 53.16           O  
ANISOU 5613  OE1 GLU A 707     7995   6056   6149  -3265   2608  -1599       O  
ATOM   5614  OE2 GLU A 707       1.657 114.763   5.613  1.00 54.51           O1+
ANISOU 5614  OE2 GLU A 707     7570   6491   6651  -3379   2659  -1729       O1+
ATOM   5615  N   VAL A 708       7.245 115.043   1.300  1.00 46.33           N  
ANISOU 5615  N   VAL A 708     7288   5340   4974  -2264   1880  -1338       N  
ATOM   5616  CA  VAL A 708       8.506 114.400   0.929  1.00 45.50           C  
ANISOU 5616  CA  VAL A 708     7477   5111   4699  -2120   1848  -1264       C  
ATOM   5617  C   VAL A 708       9.663 115.355   1.190  1.00 43.44           C  
ANISOU 5617  C   VAL A 708     7196   4891   4420  -1875   1855  -1160       C  
ATOM   5618  O   VAL A 708       9.672 116.476   0.661  1.00 42.58           O  
ANISOU 5618  O   VAL A 708     6881   4912   4385  -1752   1780  -1143       O  
ATOM   5619  CB  VAL A 708       8.495 113.952  -0.542  1.00 46.11           C  
ANISOU 5619  CB  VAL A 708     7626   5176   4718  -2086   1690  -1300       C  
ATOM   5620  CG1 VAL A 708       9.804 113.268  -0.904  1.00 45.41           C  
ANISOU 5620  CG1 VAL A 708     7841   4957   4457  -1930   1678  -1228       C  
ATOM   5621  CG2 VAL A 708       7.316 113.036  -0.817  1.00 48.32           C  
ANISOU 5621  CG2 VAL A 708     7910   5416   5035  -2338   1662  -1416       C  
ATOM   5622  N   PRO A 709      10.644 114.965   1.999  1.00 42.77           N  
ANISOU 5622  N   PRO A 709     7320   4692   4241  -1800   1935  -1094       N  
ATOM   5623  CA  PRO A 709      11.821 115.819   2.188  1.00 41.02           C  
ANISOU 5623  CA  PRO A 709     7072   4500   4014  -1567   1926  -1006       C  
ATOM   5624  C   PRO A 709      12.746 115.755   0.983  1.00 40.46           C  
ANISOU 5624  C   PRO A 709     7080   4418   3873  -1391   1830   -971       C  
ATOM   5625  O   PRO A 709      12.999 114.686   0.421  1.00 41.22           O  
ANISOU 5625  O   PRO A 709     7393   4409   3858  -1405   1802   -987       O  
ATOM   5626  CB  PRO A 709      12.486 115.233   3.439  1.00 40.95           C  
ANISOU 5626  CB  PRO A 709     7284   4352   3922  -1557   2023   -969       C  
ATOM   5627  CG  PRO A 709      12.064 113.802   3.436  1.00 42.54           C  
ANISOU 5627  CG  PRO A 709     7729   4413   4023  -1726   2057  -1019       C  
ATOM   5628  CD  PRO A 709      10.674 113.775   2.866  1.00 43.77           C  
ANISOU 5628  CD  PRO A 709     7712   4651   4269  -1927   2038  -1104       C  
ATOM   5629  N   PHE A 710      13.240 116.921   0.579  1.00 39.34           N  
ANISOU 5629  N   PHE A 710     6773   4382   3794  -1227   1791   -923       N  
ATOM   5630  CA  PHE A 710      14.172 117.019  -0.538  1.00 38.86           C  
ANISOU 5630  CA  PHE A 710     6775   4314   3675  -1051   1732   -884       C  
ATOM   5631  C   PHE A 710      14.998 118.280  -0.353  1.00 37.44           C  
ANISOU 5631  C   PHE A 710     6444   4209   3571   -879   1749   -815       C  
ATOM   5632  O   PHE A 710      14.437 119.377  -0.254  1.00 37.00           O  
ANISOU 5632  O   PHE A 710     6173   4269   3616   -889   1736   -815       O  
ATOM   5633  CB  PHE A 710      13.438 117.042  -1.881  1.00 39.94           C  
ANISOU 5633  CB  PHE A 710     6870   4504   3802  -1086   1632   -931       C  
ATOM   5634  CG  PHE A 710      14.352 117.125  -3.071  1.00 39.38           C  
ANISOU 5634  CG  PHE A 710     6897   4413   3653   -908   1591   -890       C  
ATOM   5635  CD1 PHE A 710      15.422 116.254  -3.200  1.00 39.43           C  
ANISOU 5635  CD1 PHE A 710     7130   4299   3552   -814   1629   -860       C  
ATOM   5636  CD2 PHE A 710      14.135 118.063  -4.067  1.00 40.02           C  
ANISOU 5636  CD2 PHE A 710     6859   4585   3762   -829   1522   -885       C  
ATOM   5637  CE1 PHE A 710      16.265 116.324  -4.294  1.00 39.37           C  
ANISOU 5637  CE1 PHE A 710     7211   4270   3477   -651   1619   -826       C  
ATOM   5638  CE2 PHE A 710      14.975 118.136  -5.164  1.00 39.40           C  
ANISOU 5638  CE2 PHE A 710     6896   4473   3601   -670   1512   -846       C  
ATOM   5639  CZ  PHE A 710      16.041 117.264  -5.278  1.00 39.26           C  
ANISOU 5639  CZ  PHE A 710     7088   4342   3487   -584   1570   -816       C  
ATOM   5640  N   CYS A 711      16.321 118.116  -0.305  1.00 39.62           N  
ANISOU 5640  N   CYS A 711     6832   4417   3806   -724   1777   -764       N  
ATOM   5641  CA  CYS A 711      17.250 119.225  -0.084  1.00 37.91           C  
ANISOU 5641  CA  CYS A 711     6480   4252   3671   -567   1799   -705       C  
ATOM   5642  C   CYS A 711      16.937 119.953   1.221  1.00 37.30           C  
ANISOU 5642  C   CYS A 711     6269   4219   3685   -612   1830   -697       C  
ATOM   5643  O   CYS A 711      16.981 121.183   1.292  1.00 36.57           O  
ANISOU 5643  O   CYS A 711     5989   4218   3686   -554   1826   -668       O  
ATOM   5644  CB  CYS A 711      17.249 120.195  -1.268  1.00 38.21           C  
ANISOU 5644  CB  CYS A 711     6391   4383   3744   -485   1767   -683       C  
ATOM   5645  SG  CYS A 711      17.681 119.438  -2.851  1.00 39.00           S  
ANISOU 5645  SG  CYS A 711     6677   4421   3720   -408   1743   -687       S  
ATOM   5646  N   SER A 712      16.600 119.177   2.255  1.00 38.10           N  
ANISOU 5646  N   SER A 712     6489   4241   3746   -718   1865   -723       N  
ATOM   5647  CA  SER A 712      16.330 119.635   3.616  1.00 37.44           C  
ANISOU 5647  CA  SER A 712     6348   4163   3715   -764   1910   -719       C  
ATOM   5648  C   SER A 712      15.017 120.392   3.753  1.00 38.20           C  
ANISOU 5648  C   SER A 712     6242   4375   3896   -891   1924   -750       C  
ATOM   5649  O   SER A 712      14.747 120.955   4.822  1.00 37.50           O  
ANISOU 5649  O   SER A 712     6084   4305   3859   -918   1971   -745       O  
ATOM   5650  CB  SER A 712      17.476 120.494   4.164  1.00 35.98           C  
ANISOU 5650  CB  SER A 712     6096   3982   3593   -594   1902   -667       C  
ATOM   5651  OG  SER A 712      18.649 119.719   4.336  1.00 35.63           O  
ANISOU 5651  OG  SER A 712     6233   3821   3485   -481   1889   -655       O  
ATOM   5652  N   HIS A 713      14.183 120.414   2.718  1.00 36.71           N  
ANISOU 5652  N   HIS A 713     5965   4260   3723   -961   1879   -789       N  
ATOM   5653  CA  HIS A 713      12.874 121.042   2.789  1.00 37.71           C  
ANISOU 5653  CA  HIS A 713     5888   4498   3940  -1077   1878   -837       C  
ATOM   5654  C   HIS A 713      11.809 120.081   2.275  1.00 40.49           C  
ANISOU 5654  C   HIS A 713     6280   4837   4268  -1254   1861   -917       C  
ATOM   5655  O   HIS A 713      12.100 119.064   1.638  1.00 41.53           O  
ANISOU 5655  O   HIS A 713     6593   4883   4305  -1269   1831   -928       O  
ATOM   5656  CB  HIS A 713      12.813 122.340   1.969  1.00 37.79           C  
ANISOU 5656  CB  HIS A 713     5697   4635   4025   -966   1805   -818       C  
ATOM   5657  CG  HIS A 713      13.764 123.405   2.419  1.00 35.54           C  
ANISOU 5657  CG  HIS A 713     5349   4371   3786   -812   1822   -746       C  
ATOM   5658  ND1 HIS A 713      15.079 123.448   2.011  1.00 34.49           N  
ANISOU 5658  ND1 HIS A 713     5301   4185   3617   -663   1813   -688       N  
ATOM   5659  CD2 HIS A 713      13.582 124.482   3.219  1.00 34.60           C  
ANISOU 5659  CD2 HIS A 713     5083   4315   3751   -786   1846   -729       C  
ATOM   5660  CE1 HIS A 713      15.671 124.499   2.549  1.00 33.57           C  
ANISOU 5660  CE1 HIS A 713     5085   4098   3571   -564   1827   -642       C  
ATOM   5661  NE2 HIS A 713      14.785 125.143   3.288  1.00 33.57           N  
ANISOU 5661  NE2 HIS A 713     4956   4165   3636   -633   1842   -663       N  
ATOM   5662  N   HIS A 714      10.562 120.418   2.584  1.00 39.05           N  
ANISOU 5662  N   HIS A 714     5918   4739   4180  -1389   1880   -980       N  
ATOM   5663  CA  HIS A 714       9.392 119.937   1.871  1.00 40.55           C  
ANISOU 5663  CA  HIS A 714     6034   4968   4405  -1540   1825  -1073       C  
ATOM   5664  C   HIS A 714       8.670 121.143   1.285  1.00 41.27           C  
ANISOU 5664  C   HIS A 714     5854   5215   4610  -1488   1734  -1105       C  
ATOM   5665  O   HIS A 714       9.018 122.295   1.558  1.00 39.41           O  
ANISOU 5665  O   HIS A 714     5504   5048   4420  -1357   1738  -1053       O  
ATOM   5666  CB  HIS A 714       8.467 119.120   2.781  1.00 41.99           C  
ANISOU 5666  CB  HIS A 714     6240   5100   4615  -1770   1940  -1140       C  
ATOM   5667  CG  HIS A 714       8.084 119.820   4.048  1.00 41.83           C  
ANISOU 5667  CG  HIS A 714     6093   5124   4677  -1806   2061  -1135       C  
ATOM   5668  ND1 HIS A 714       8.912 119.873   5.149  1.00 40.94           N  
ANISOU 5668  ND1 HIS A 714     6127   4926   4502  -1738   2158  -1063       N  
ATOM   5669  CD2 HIS A 714       6.955 120.482   4.393  1.00 42.61           C  
ANISOU 5669  CD2 HIS A 714     5940   5336   4913  -1895   2100  -1199       C  
ATOM   5670  CE1 HIS A 714       8.312 120.545   6.115  1.00 41.12           C  
ANISOU 5670  CE1 HIS A 714     6014   5004   4608  -1786   2255  -1077       C  
ATOM   5671  NE2 HIS A 714       7.124 120.926   5.682  1.00 42.13           N  
ANISOU 5671  NE2 HIS A 714     5891   5254   4860  -1881   2232  -1159       N  
ATOM   5672  N   PHE A 715       7.659 120.879   0.463  1.00 41.73           N  
ANISOU 5672  N   PHE A 715     5818   5324   4713  -1585   1638  -1198       N  
ATOM   5673  CA  PHE A 715       7.055 121.935  -0.337  1.00 41.91           C  
ANISOU 5673  CA  PHE A 715     5627   5479   4818  -1501   1508  -1235       C  
ATOM   5674  C   PHE A 715       5.539 121.847  -0.270  1.00 43.77           C  
ANISOU 5674  C   PHE A 715     5641   5798   5191  -1672   1477  -1365       C  
ATOM   5675  O   PHE A 715       4.963 120.781  -0.503  1.00 45.27           O  
ANISOU 5675  O   PHE A 715     5882   5937   5381  -1839   1462  -1444       O  
ATOM   5676  CB  PHE A 715       7.538 121.851  -1.789  1.00 41.85           C  
ANISOU 5676  CB  PHE A 715     5742   5446   4712  -1376   1362  -1219       C  
ATOM   5677  CG  PHE A 715       9.038 121.852  -1.927  1.00 40.33           C  
ANISOU 5677  CG  PHE A 715     5753   5170   4400  -1216   1409  -1103       C  
ATOM   5678  CD1 PHE A 715       9.757 120.672  -1.831  1.00 40.33           C  
ANISOU 5678  CD1 PHE A 715     5992   5039   4291  -1251   1468  -1076       C  
ATOM   5679  CD2 PHE A 715       9.728 123.034  -2.146  1.00 39.08           C  
ANISOU 5679  CD2 PHE A 715     5543   5058   4245  -1033   1398  -1027       C  
ATOM   5680  CE1 PHE A 715      11.133 120.671  -1.952  1.00 39.15           C  
ANISOU 5680  CE1 PHE A 715     6001   4819   4054  -1096   1511   -984       C  
ATOM   5681  CE2 PHE A 715      11.105 123.038  -2.269  1.00 37.92           C  
ANISOU 5681  CE2 PHE A 715     5554   4838   4016   -898   1453   -933       C  
ATOM   5682  CZ  PHE A 715      11.808 121.855  -2.172  1.00 37.98           C  
ANISOU 5682  CZ  PHE A 715     5774   4727   3930   -925   1507   -915       C  
ATOM   5683  N   ASN A 716       4.902 122.972   0.044  1.00 45.64           N  
ANISOU 5683  N   ASN A 716     5628   6161   5551  -1629   1467  -1393       N  
ATOM   5684  CA  ASN A 716       3.454 123.074   0.124  1.00 47.89           C  
ANISOU 5684  CA  ASN A 716     5651   6547   5997  -1765   1437  -1527       C  
ATOM   5685  C   ASN A 716       2.922 123.928  -1.020  1.00 50.77           C  
ANISOU 5685  C   ASN A 716     5857   7021   6413  -1634   1222  -1585       C  
ATOM   5686  O   ASN A 716       3.596 124.842  -1.505  1.00 50.10           O  
ANISOU 5686  O   ASN A 716     5817   6955   6263  -1430   1148  -1506       O  
ATOM   5687  CB  ASN A 716       3.019 123.673   1.464  1.00 45.40           C  
ANISOU 5687  CB  ASN A 716     5167   6290   5790  -1816   1603  -1531       C  
ATOM   5688  CG  ASN A 716       3.365 122.780   2.639  1.00 45.30           C  
ANISOU 5688  CG  ASN A 716     5328   6158   5724  -1959   1814  -1492       C  
ATOM   5689  OD1 ASN A 716       4.440 122.894   3.228  1.00 43.67           O  
ANISOU 5689  OD1 ASN A 716     5304   5877   5414  -1863   1894  -1380       O  
ATOM   5690  ND2 ASN A 716       2.449 121.885   2.989  1.00 47.21           N  
ANISOU 5690  ND2 ASN A 716     5523   6376   6039  -2192   1903  -1590       N  
ATOM   5691  N   LYS A 717       1.699 123.618  -1.444  1.00 49.48           N  
ANISOU 5691  N   LYS A 717     5512   6920   6370  -1756   1118  -1729       N  
ATOM   5692  CA  LYS A 717       1.026 124.334  -2.520  1.00 50.51           C  
ANISOU 5692  CA  LYS A 717     5487   7147   6558  -1640    885  -1812       C  
ATOM   5693  C   LYS A 717       0.139 125.412  -1.912  1.00 51.12           C  
ANISOU 5693  C   LYS A 717     5247   7367   6808  -1610    900  -1877       C  
ATOM   5694  O   LYS A 717      -0.820 125.102  -1.195  1.00 52.65           O  
ANISOU 5694  O   LYS A 717     5231   7613   7161  -1788    996  -1980       O  
ATOM   5695  CB  LYS A 717       0.198 123.375  -3.375  1.00 52.76           C  
ANISOU 5695  CB  LYS A 717     5748   7414   6884  -1777    729  -1949       C  
ATOM   5696  CG  LYS A 717      -0.023 123.838  -4.808  1.00 53.52           C  
ANISOU 5696  CG  LYS A 717     5855   7542   6939  -1611    447  -2000       C  
ATOM   5697  CD  LYS A 717      -1.418 123.473  -5.297  1.00 56.39           C  
ANISOU 5697  CD  LYS A 717     5988   7971   7465  -1737    269  -2195       C  
ATOM   5698  CE  LYS A 717      -1.441 123.229  -6.799  1.00 57.41           C  
ANISOU 5698  CE  LYS A 717     6275   8049   7487  -1636     -8  -2244       C  
ATOM   5699  NZ  LYS A 717      -0.747 124.298  -7.570  1.00 56.09           N1+
ANISOU 5699  NZ  LYS A 717     6253   7882   7175  -1351   -123  -2148       N1+
ATOM   5700  N   LEU A 718       0.457 126.670  -2.195  1.00 55.01           N  
ANISOU 5700  N   LEU A 718     5712   7917   7271  -1387    819  -1819       N  
ATOM   5701  CA  LEU A 718      -0.304 127.803  -1.696  1.00 54.01           C  
ANISOU 5701  CA  LEU A 718     5311   7921   7289  -1318    816  -1873       C  
ATOM   5702  C   LEU A 718      -1.005 128.514  -2.845  1.00 56.89           C  
ANISOU 5702  C   LEU A 718     5551   8370   7697  -1168    543  -1969       C  
ATOM   5703  O   LEU A 718      -0.612 128.402  -4.009  1.00 59.29           O  
ANISOU 5703  O   LEU A 718     6039   8616   7874  -1065    371  -1949       O  
ATOM   5704  CB  LEU A 718       0.599 128.788  -0.946  1.00 50.91           C  
ANISOU 5704  CB  LEU A 718     4992   7521   6831  -1175    946  -1732       C  
ATOM   5705  CG  LEU A 718       1.355 128.220   0.255  1.00 47.44           C  
ANISOU 5705  CG  LEU A 718     4693   6993   6341  -1286   1194  -1636       C  
ATOM   5706  CD1 LEU A 718       2.004 129.337   1.057  1.00 43.99           C  
ANISOU 5706  CD1 LEU A 718     4267   6567   5879  -1146   1292  -1529       C  
ATOM   5707  CD2 LEU A 718       0.427 127.393   1.127  1.00 47.32           C  
ANISOU 5707  CD2 LEU A 718     4536   6992   6453  -1525   1341  -1736       C  
ATOM   5708  N   TYR A 719      -2.055 129.252  -2.500  1.00 56.94           N  
ANISOU 5708  N   TYR A 719     5253   8504   7876  -1146    505  -2078       N  
ATOM   5709  CA  TYR A 719      -2.851 129.997  -3.465  1.00 59.12           C  
ANISOU 5709  CA  TYR A 719     5381   8869   8215   -990    233  -2190       C  
ATOM   5710  C   TYR A 719      -2.851 131.465  -3.070  1.00 57.97           C  
ANISOU 5710  C   TYR A 719     5135   8800   8092   -791    240  -2148       C  
ATOM   5711  O   TYR A 719      -3.213 131.807  -1.938  1.00 55.81           O  
ANISOU 5711  O   TYR A 719     4674   8593   7939   -848    414  -2162       O  
ATOM   5712  CB  TYR A 719      -4.281 129.456  -3.532  1.00 59.73           C  
ANISOU 5712  CB  TYR A 719     5146   9037   8511  -1145    140  -2399       C  
ATOM   5713  CG  TYR A 719      -4.383 128.070  -4.126  1.00 60.89           C  
ANISOU 5713  CG  TYR A 719     5397   9102   8636  -1328     78  -2460       C  
ATOM   5714  CD1 TYR A 719      -4.191 126.940  -3.342  1.00 59.60           C  
ANISOU 5714  CD1 TYR A 719     5294   8868   8484  -1576    310  -2435       C  
ATOM   5715  CD2 TYR A 719      -4.676 127.891  -5.471  1.00 62.91           C  
ANISOU 5715  CD2 TYR A 719     5717   9340   8848  -1247   -220  -2544       C  
ATOM   5716  CE1 TYR A 719      -4.285 125.671  -3.880  1.00 60.43           C  
ANISOU 5716  CE1 TYR A 719     5512   8888   8562  -1745    252  -2492       C  
ATOM   5717  CE2 TYR A 719      -4.772 126.627  -6.020  1.00 63.64           C  
ANISOU 5717  CE2 TYR A 719     5918   9349   8914  -1412   -286  -2603       C  
ATOM   5718  CZ  TYR A 719      -4.576 125.520  -5.219  1.00 62.48           C  
ANISOU 5718  CZ  TYR A 719     5821   9134   8784  -1664    -47  -2576       C  
ATOM   5719  OH  TYR A 719      -4.670 124.257  -5.758  1.00 63.03           O  
ANISOU 5719  OH  TYR A 719     6017   9110   8821  -1831   -113  -2635       O  
ATOM   5720  N   LEU A 720      -2.440 132.325  -3.998  1.00 58.53           N  
ANISOU 5720  N   LEU A 720     5353   8849   8036   -560     58  -2096       N  
ATOM   5721  CA  LEU A 720      -2.462 133.758  -3.753  1.00 57.26           C  
ANISOU 5721  CA  LEU A 720     5124   8748   7883   -358     35  -2062       C  
ATOM   5722  C   LEU A 720      -3.895 134.236  -3.549  1.00 57.54           C  
ANISOU 5722  C   LEU A 720     4796   8931   8135   -337    -71  -2242       C  
ATOM   5723  O   LEU A 720      -4.858 133.608  -4.000  1.00 59.82           O  
ANISOU 5723  O   LEU A 720     4907   9273   8551   -427   -212  -2403       O  
ATOM   5724  CB  LEU A 720      -1.820 134.514  -4.917  1.00 59.32           C  
ANISOU 5724  CB  LEU A 720     5639   8941   7960   -124   -148  -1984       C  
ATOM   5725  CG  LEU A 720      -0.306 134.367  -5.092  1.00 58.49           C  
ANISOU 5725  CG  LEU A 720     5876   8698   7650    -99    -23  -1797       C  
ATOM   5726  CD1 LEU A 720       0.164 135.079  -6.351  1.00 60.82           C  
ANISOU 5726  CD1 LEU A 720     6414   8921   7772    119   -202  -1743       C  
ATOM   5727  CD2 LEU A 720       0.422 134.901  -3.872  1.00 54.55           C  
ANISOU 5727  CD2 LEU A 720     5379   8191   7155   -110    218  -1674       C  
ATOM   5728  N   LYS A 721      -4.030 135.363  -2.849  1.00 62.78           N  
ANISOU 5728  N   LYS A 721     5343   9660   8850   -216     -4  -2220       N  
ATOM   5729  CA  LYS A 721      -5.341 135.969  -2.654  1.00 62.94           C  
ANISOU 5729  CA  LYS A 721     5017   9824   9074   -156   -104  -2389       C  
ATOM   5730  C   LYS A 721      -5.947 136.294  -4.012  1.00 65.88           C  
ANISOU 5730  C   LYS A 721     5373  10222   9437     17   -457  -2506       C  
ATOM   5731  O   LYS A 721      -5.411 137.127  -4.751  1.00 66.68           O  
ANISOU 5731  O   LYS A 721     5699  10264   9371    238   -603  -2426       O  
ATOM   5732  CB  LYS A 721      -5.249 137.226  -1.789  1.00 60.51           C  
ANISOU 5732  CB  LYS A 721     4649   9562   8780    -13      9  -2329       C  
ATOM   5733  CG  LYS A 721      -6.477 137.451  -0.921  1.00 59.35           C  
ANISOU 5733  CG  LYS A 721     4115   9557   8877    -64     87  -2482       C  
ATOM   5734  CD  LYS A 721      -6.676 138.918  -0.585  1.00 57.87           C  
ANISOU 5734  CD  LYS A 721     3856   9429   8702    170     54  -2475       C  
ATOM   5735  CE  LYS A 721      -7.104 139.705  -1.814  1.00 59.69           C  
ANISOU 5735  CE  LYS A 721     4093   9687   8899    421   -291  -2554       C  
ATOM   5736  NZ  LYS A 721      -7.509 141.100  -1.480  1.00 59.43           N1+
ANISOU 5736  NZ  LYS A 721     3954   9723   8904    650   -340  -2581       N1+
ATOM   5737  N   ASP A 722      -7.050 135.620  -4.345  1.00 64.48           N  
ANISOU 5737  N   ASP A 722     4943  10120   9437    -87   -595  -2698       N  
ATOM   5738  CA  ASP A 722      -7.682 135.695  -5.659  1.00 66.88           C  
ANISOU 5738  CA  ASP A 722     5232  10437   9742     51   -957  -2832       C  
ATOM   5739  C   ASP A 722      -6.775 135.146  -6.754  1.00 67.82           C  
ANISOU 5739  C   ASP A 722     5743  10407   9620     76  -1071  -2731       C  
ATOM   5740  O   ASP A 722      -5.927 135.869  -7.289  1.00 67.50           O  
ANISOU 5740  O   ASP A 722     6004  10278   9366    269  -1122  -2596       O  
ATOM   5741  CB  ASP A 722      -8.096 137.134  -5.988  1.00 67.77           C  
ANISOU 5741  CB  ASP A 722     5287  10609   9852    352  -1160  -2876       C  
ATOM   5742  CG  ASP A 722      -9.559 137.395  -5.717  1.00 68.75           C  
ANISOU 5742  CG  ASP A 722     4962  10899  10262    369  -1276  -3106       C  
ATOM   5743  OD1 ASP A 722     -10.404 136.658  -6.268  1.00 70.69           O  
ANISOU 5743  OD1 ASP A 722     5021  11189  10651    280  -1462  -3284       O  
ATOM   5744  OD2 ASP A 722      -9.862 138.334  -4.950  1.00 67.55           O1+
ANISOU 5744  OD2 ASP A 722     4639  10830  10196    473  -1183  -3114       O1+
ATOM   5745  N   GLY A 723      -6.936 133.865  -7.084  1.00 62.99           N  
ANISOU 5745  N   GLY A 723     5137   9757   9040   -123  -1096  -2796       N  
ATOM   5746  CA  GLY A 723      -6.362 133.333  -8.304  1.00 62.84           C  
ANISOU 5746  CA  GLY A 723     5452   9609   8816    -76  -1269  -2752       C  
ATOM   5747  C   GLY A 723      -5.216 132.346  -8.194  1.00 60.67           C  
ANISOU 5747  C   GLY A 723     5469   9203   8380   -234  -1057  -2595       C  
ATOM   5748  O   GLY A 723      -5.419 131.165  -7.900  1.00 61.21           O  
ANISOU 5748  O   GLY A 723     5468   9259   8530   -475   -964  -2646       O  
ATOM   5749  N   ARG A 724      -4.002 132.837  -8.430  1.00 59.03           N  
ANISOU 5749  N   ARG A 724     5589   8893   7945    -98   -976  -2407       N  
ATOM   5750  CA  ARG A 724      -2.874 132.004  -8.820  1.00 59.34           C  
ANISOU 5750  CA  ARG A 724     5969   8790   7790   -165   -875  -2275       C  
ATOM   5751  C   ARG A 724      -2.359 131.157  -7.655  1.00 58.21           C  
ANISOU 5751  C   ARG A 724     5796   8629   7694   -399   -561  -2196       C  
ATOM   5752  O   ARG A 724      -2.770 131.303  -6.501  1.00 57.28           O  
ANISOU 5752  O   ARG A 724     5428   8598   7737   -502   -396  -2222       O  
ATOM   5753  CB  ARG A 724      -1.757 132.879  -9.381  1.00 59.28           C  
ANISOU 5753  CB  ARG A 724     6286   8685   7552     53   -865  -2108       C  
ATOM   5754  CG  ARG A 724      -2.153 133.615 -10.649  1.00 60.25           C  
ANISOU 5754  CG  ARG A 724     6533   8785   7576    291  -1174  -2172       C  
ATOM   5755  CD  ARG A 724      -1.330 134.874 -10.842  1.00 60.18           C  
ANISOU 5755  CD  ARG A 724     6740   8718   7407    508  -1128  -2027       C  
ATOM   5756  NE  ARG A 724      -1.718 135.926  -9.906  1.00 60.31           N  
ANISOU 5756  NE  ARG A 724     6514   8843   7558    567  -1062  -2035       N  
ATOM   5757  CZ  ARG A 724      -1.094 137.094  -9.797  1.00 60.26           C  
ANISOU 5757  CZ  ARG A 724     6638   8803   7455    729   -994  -1916       C  
ATOM   5758  NH1 ARG A 724      -0.045 137.360 -10.563  1.00 59.36           N1+
ANISOU 5758  NH1 ARG A 724     6884   8551   7119    837   -967  -1781       N1+
ATOM   5759  NH2 ARG A 724      -1.515 137.994  -8.919  1.00 59.81           N  
ANISOU 5759  NH2 ARG A 724     6358   8843   7524    778   -942  -1935       N  
ATOM   5760  N   SER A 725      -1.430 130.257  -7.986  1.00 56.91           N  
ANISOU 5760  N   SER A 725     5912   8339   7373   -470   -480  -2100       N  
ATOM   5761  CA  SER A 725      -0.885 129.284  -7.052  1.00 55.28           C  
ANISOU 5761  CA  SER A 725     5741   8085   7176   -680   -219  -2031       C  
ATOM   5762  C   SER A 725       0.631 129.231  -7.174  1.00 54.00           C  
ANISOU 5762  C   SER A 725     5911   7799   6807   -607    -78  -1843       C  
ATOM   5763  O   SER A 725       1.177 129.262  -8.282  1.00 54.01           O  
ANISOU 5763  O   SER A 725     6164   7717   6642   -477   -195  -1797       O  
ATOM   5764  CB  SER A 725      -1.465 127.885  -7.303  1.00 55.54           C  
ANISOU 5764  CB  SER A 725     5750   8086   7265   -892   -274  -2147       C  
ATOM   5765  OG  SER A 725      -1.022 127.367  -8.546  1.00 56.08           O  
ANISOU 5765  OG  SER A 725     6105   8045   7159   -825   -432  -2131       O  
ATOM   5766  N   ILE A 726       1.305 129.147  -6.029  1.00 51.00           N  
ANISOU 5766  N   ILE A 726     5533   7405   6441   -687    174  -1742       N  
ATOM   5767  CA  ILE A 726       2.751 128.982  -5.969  1.00 48.90           C  
ANISOU 5767  CA  ILE A 726     5538   7027   6015   -642    325  -1579       C  
ATOM   5768  C   ILE A 726       3.065 127.791  -5.075  1.00 48.37           C  
ANISOU 5768  C   ILE A 726     5509   6905   5966   -845    516  -1557       C  
ATOM   5769  O   ILE A 726       2.284 127.431  -4.188  1.00 49.16           O  
ANISOU 5769  O   ILE A 726     5413   7061   6206  -1008    595  -1636       O  
ATOM   5770  CB  ILE A 726       3.469 130.249  -5.451  1.00 47.17           C  
ANISOU 5770  CB  ILE A 726     5322   6824   5775   -493    427  -1461       C  
ATOM   5771  CG1 ILE A 726       2.907 130.667  -4.090  1.00 47.01           C  
ANISOU 5771  CG1 ILE A 726     5048   6898   5916   -571    552  -1491       C  
ATOM   5772  CG2 ILE A 726       3.351 131.383  -6.455  1.00 47.65           C  
ANISOU 5772  CG2 ILE A 726     5430   6902   5773   -279    248  -1461       C  
ATOM   5773  CD1 ILE A 726       3.603 131.870  -3.490  1.00 45.38           C  
ANISOU 5773  CD1 ILE A 726     4851   6699   5692   -438    650  -1380       C  
ATOM   5774  N   VAL A 727       4.219 127.177  -5.317  1.00 48.93           N  
ANISOU 5774  N   VAL A 727     5844   6858   5889   -831    597  -1454       N  
ATOM   5775  CA  VAL A 727       4.685 126.028  -4.547  1.00 47.18           C  
ANISOU 5775  CA  VAL A 727     5720   6559   5649   -991    765  -1422       C  
ATOM   5776  C   VAL A 727       5.948 126.460  -3.814  1.00 43.00           C  
ANISOU 5776  C   VAL A 727     5293   5983   5062   -907    936  -1279       C  
ATOM   5777  O   VAL A 727       7.009 126.620  -4.431  1.00 41.17           O  
ANISOU 5777  O   VAL A 727     5252   5683   4710   -775    939  -1187       O  
ATOM   5778  CB  VAL A 727       4.942 124.801  -5.431  1.00 47.60           C  
ANISOU 5778  CB  VAL A 727     5997   6505   5583  -1046    701  -1440       C  
ATOM   5779  CG1 VAL A 727       5.317 123.607  -4.573  1.00 46.08           C  
ANISOU 5779  CG1 VAL A 727     5908   6227   5374  -1213    868  -1418       C  
ATOM   5780  CG2 VAL A 727       3.713 124.490  -6.272  1.00 50.56           C  
ANISOU 5780  CG2 VAL A 727     6273   6921   6016  -1108    492  -1589       C  
ATOM   5781  N   VAL A 728       5.839 126.636  -2.501  1.00 42.38           N  
ANISOU 5781  N   VAL A 728     5092   5937   5074   -983   1080  -1267       N  
ATOM   5782  CA  VAL A 728       6.890 127.256  -1.697  1.00 40.57           C  
ANISOU 5782  CA  VAL A 728     4916   5679   4819   -893   1213  -1150       C  
ATOM   5783  C   VAL A 728       7.641 126.199  -0.895  1.00 39.94           C  
ANISOU 5783  C   VAL A 728     4997   5493   4685   -990   1360  -1102       C  
ATOM   5784  O   VAL A 728       7.092 125.119  -0.630  1.00 40.98           O  
ANISOU 5784  O   VAL A 728     5151   5590   4828  -1157   1394  -1167       O  
ATOM   5785  CB  VAL A 728       6.298 128.326  -0.768  1.00 40.44           C  
ANISOU 5785  CB  VAL A 728     4679   5761   4925   -876   1257  -1166       C  
ATOM   5786  CG1 VAL A 728       5.453 129.300  -1.565  1.00 41.36           C  
ANISOU 5786  CG1 VAL A 728     4639   5979   5095   -775   1094  -1231       C  
ATOM   5787  CG2 VAL A 728       5.464 127.675   0.323  1.00 41.35           C  
ANISOU 5787  CG2 VAL A 728     4681   5896   5135  -1068   1370  -1240       C  
ATOM   5788  N   PRO A 729       8.888 126.452  -0.504  1.00 40.45           N  
ANISOU 5788  N   PRO A 729     5181   5494   4692   -890   1443   -995       N  
ATOM   5789  CA  PRO A 729       9.599 125.525   0.381  1.00 39.29           C  
ANISOU 5789  CA  PRO A 729     5186   5245   4498   -959   1567   -957       C  
ATOM   5790  C   PRO A 729       9.345 125.824   1.849  1.00 39.04           C  
ANISOU 5790  C   PRO A 729     5067   5228   4537  -1022   1683   -955       C  
ATOM   5791  O   PRO A 729       9.077 126.958   2.248  1.00 38.66           O  
ANISOU 5791  O   PRO A 729     4864   5259   4565   -960   1685   -946       O  
ATOM   5792  CB  PRO A 729      11.070 125.775   0.022  1.00 38.01           C  
ANISOU 5792  CB  PRO A 729     5167   5017   4259   -799   1580   -856       C  
ATOM   5793  CG  PRO A 729      11.101 127.216  -0.348  1.00 37.46           C  
ANISOU 5793  CG  PRO A 729     4969   5028   4237   -666   1528   -824       C  
ATOM   5794  CD  PRO A 729       9.777 127.511  -1.018  1.00 38.88           C  
ANISOU 5794  CD  PRO A 729     5010   5301   4461   -705   1414   -912       C  
ATOM   5795  N   CYS A 730       9.448 124.774   2.663  1.00 42.01           N  
ANISOU 5795  N   CYS A 730     5574   5513   4875  -1140   1783   -962       N  
ATOM   5796  CA  CYS A 730       9.183 124.890   4.090  1.00 40.52           C  
ANISOU 5796  CA  CYS A 730     5356   5311   4728  -1212   1908   -963       C  
ATOM   5797  C   CYS A 730      10.007 123.860   4.848  1.00 39.28           C  
ANISOU 5797  C   CYS A 730     5447   5006   4470  -1246   1996   -923       C  
ATOM   5798  O   CYS A 730      10.259 122.760   4.351  1.00 40.15           O  
ANISOU 5798  O   CYS A 730     5722   5034   4500  -1295   1979   -934       O  
ATOM   5799  CB  CYS A 730       7.692 124.697   4.396  1.00 42.68           C  
ANISOU 5799  CB  CYS A 730     5469   5652   5095  -1388   1955  -1066       C  
ATOM   5800  SG  CYS A 730       7.301 124.572   6.155  1.00 41.57           S  
ANISOU 5800  SG  CYS A 730     5351   5465   4980  -1507   2154  -1075       S  
ATOM   5801  N   ARG A 731      10.421 124.231   6.059  1.00 42.92           N  
ANISOU 5801  N   ARG A 731     5953   5426   4930  -1209   2078   -881       N  
ATOM   5802  CA  ARG A 731      11.114 123.322   6.961  1.00 41.74           C  
ANISOU 5802  CA  ARG A 731     6051   5128   4682  -1232   2154   -852       C  
ATOM   5803  C   ARG A 731      10.740 123.700   8.390  1.00 40.86           C  
ANISOU 5803  C   ARG A 731     5939   4995   4591  -1277   2269   -854       C  
ATOM   5804  O   ARG A 731       9.935 124.607   8.622  1.00 40.73           O  
ANISOU 5804  O   ARG A 731     5720   5085   4669  -1295   2297   -880       O  
ATOM   5805  CB  ARG A 731      12.628 123.354   6.729  1.00 40.07           C  
ANISOU 5805  CB  ARG A 731     5967   4847   4410  -1054   2086   -779       C  
ATOM   5806  CG  ARG A 731      13.282 124.691   7.017  1.00 38.61           C  
ANISOU 5806  CG  ARG A 731     5665   4715   4289   -897   2051   -725       C  
ATOM   5807  CD  ARG A 731      14.749 124.672   6.617  1.00 38.03           C  
ANISOU 5807  CD  ARG A 731     5682   4584   4186   -737   1987   -668       C  
ATOM   5808  NE  ARG A 731      15.514 123.676   7.362  1.00 37.99           N  
ANISOU 5808  NE  ARG A 731     5909   4433   4091   -722   2009   -660       N  
ATOM   5809  CZ  ARG A 731      16.783 123.370   7.111  1.00 37.85           C  
ANISOU 5809  CZ  ARG A 731     5990   4345   4044   -592   1960   -629       C  
ATOM   5810  NH1 ARG A 731      17.431 123.980   6.128  1.00 37.68           N1+
ANISOU 5810  NH1 ARG A 731     5856   4384   4078   -482   1910   -600       N1+
ATOM   5811  NH2 ARG A 731      17.404 122.451   7.839  1.00 37.89           N  
ANISOU 5811  NH2 ARG A 731     6216   4214   3967   -568   1965   -632       N  
ATOM   5812  N   HIS A 732      11.324 122.991   9.355  1.00 42.58           N  
ANISOU 5812  N   HIS A 732     6402   5067   4710  -1284   2335   -829       N  
ATOM   5813  CA  HIS A 732      10.949 123.196  10.748  1.00 41.61           C  
ANISOU 5813  CA  HIS A 732     6340   4894   4576  -1335   2459   -832       C  
ATOM   5814  C   HIS A 732      11.503 124.522  11.250  1.00 40.35           C  
ANISOU 5814  C   HIS A 732     6086   4782   4464  -1169   2413   -783       C  
ATOM   5815  O   HIS A 732      12.693 124.812  11.098  1.00 40.20           O  
ANISOU 5815  O   HIS A 732     6119   4729   4426  -1010   2311   -729       O  
ATOM   5816  CB  HIS A 732      11.440 122.049  11.626  1.00 41.65           C  
ANISOU 5816  CB  HIS A 732     6680   4707   4437  -1375   2528   -820       C  
ATOM   5817  CG  HIS A 732      10.781 122.003  12.970  1.00 42.45           C  
ANISOU 5817  CG  HIS A 732     6886   4738   4505  -1478   2691   -838       C  
ATOM   5818  ND1 HIS A 732      11.157 122.822  14.013  1.00 42.02           N  
ANISOU 5818  ND1 HIS A 732     6874   4655   4438  -1367   2707   -801       N  
ATOM   5819  CD2 HIS A 732       9.756 121.250  13.435  1.00 44.23           C  
ANISOU 5819  CD2 HIS A 732     7190   4910   4707  -1687   2858   -891       C  
ATOM   5820  CE1 HIS A 732      10.399 122.568  15.065  1.00 43.34           C  
ANISOU 5820  CE1 HIS A 732     7144   4744   4578  -1480   2844   -823       C  
ATOM   5821  NE2 HIS A 732       9.541 121.618  14.741  1.00 44.83           N  
ANISOU 5821  NE2 HIS A 732     7344   4915   4773  -1671   2928   -877       N  
ATOM   5822  N   GLN A 733      10.628 125.314  11.874  1.00 40.95           N  
ANISOU 5822  N   GLN A 733     6021   4929   4608  -1212   2495   -807       N  
ATOM   5823  CA  GLN A 733      10.940 126.707  12.174  1.00 39.95           C  
ANISOU 5823  CA  GLN A 733     5764   4871   4544  -1066   2443   -770       C  
ATOM   5824  C   GLN A 733      12.049 126.836  13.213  1.00 39.47           C  
ANISOU 5824  C   GLN A 733     5912   4680   4405   -945   2422   -715       C  
ATOM   5825  O   GLN A 733      12.751 127.853  13.249  1.00 38.65           O  
ANISOU 5825  O   GLN A 733     5736   4606   4345   -798   2331   -674       O  
ATOM   5826  CB  GLN A 733       9.661 127.408  12.639  1.00 40.54           C  
ANISOU 5826  CB  GLN A 733     5657   5044   4703  -1144   2549   -819       C  
ATOM   5827  CG  GLN A 733       9.800 128.840  13.090  1.00 39.89           C  
ANISOU 5827  CG  GLN A 733     5459   5023   4676  -1008   2516   -789       C  
ATOM   5828  CD  GLN A 733       8.486 129.380  13.612  1.00 41.21           C  
ANISOU 5828  CD  GLN A 733     5465   5273   4921  -1080   2622   -843       C  
ATOM   5829  OE1 GLN A 733       7.586 129.705  12.837  1.00 41.88           O  
ANISOU 5829  OE1 GLN A 733     5311   5494   5107  -1123   2610   -899       O  
ATOM   5830  NE2 GLN A 733       8.353 129.443  14.932  1.00 41.70           N  
ANISOU 5830  NE2 GLN A 733     5662   5240   4940  -1080   2695   -827       N  
ATOM   5831  N   ASP A 734      12.232 125.817  14.056  1.00 40.77           N  
ANISOU 5831  N   ASP A 734     6347   4691   4453  -1003   2496   -718       N  
ATOM   5832  CA  ASP A 734      13.183 125.929  15.159  1.00 40.35           C  
ANISOU 5832  CA  ASP A 734     6512   4500   4317   -882   2463   -680       C  
ATOM   5833  C   ASP A 734      14.623 126.051  14.672  1.00 39.49           C  
ANISOU 5833  C   ASP A 734     6423   4363   4217   -711   2292   -639       C  
ATOM   5834  O   ASP A 734      15.428 126.753  15.295  1.00 39.40           O  
ANISOU 5834  O   ASP A 734     6445   4309   4214   -573   2212   -611       O  
ATOM   5835  CB  ASP A 734      13.040 124.732  16.099  1.00 41.54           C  
ANISOU 5835  CB  ASP A 734     6986   4477   4322   -977   2575   -696       C  
ATOM   5836  CG  ASP A 734      11.785 124.805  16.945  1.00 42.81           C  
ANISOU 5836  CG  ASP A 734     7147   4633   4488  -1117   2742   -726       C  
ATOM   5837  OD1 ASP A 734      11.154 125.883  16.985  1.00 42.50           O  
ANISOU 5837  OD1 ASP A 734     6872   4718   4558  -1105   2757   -733       O  
ATOM   5838  OD2 ASP A 734      11.433 123.787  17.577  1.00 44.25           O1+
ANISOU 5838  OD2 ASP A 734     7552   4675   4586  -1225   2824   -739       O1+
ATOM   5839  N   GLU A 735      14.970 125.390  13.568  1.00 40.41           N  
ANISOU 5839  N   GLU A 735     6516   4500   4337   -716   2236   -641       N  
ATOM   5840  CA  GLU A 735      16.326 125.503  13.044  1.00 40.44           C  
ANISOU 5840  CA  GLU A 735     6516   4485   4366   -557   2098   -609       C  
ATOM   5841  C   GLU A 735      16.514 126.749  12.191  1.00 40.11           C  
ANISOU 5841  C   GLU A 735     6201   4585   4455   -478   2031   -585       C  
ATOM   5842  O   GLU A 735      17.640 127.243  12.075  1.00 40.35           O  
ANISOU 5842  O   GLU A 735     6197   4601   4535   -339   1936   -557       O  
ATOM   5843  CB  GLU A 735      16.695 124.254  12.242  1.00 41.27           C  
ANISOU 5843  CB  GLU A 735     6739   4535   4408   -579   2077   -620       C  
ATOM   5844  CG  GLU A 735      17.247 123.124  13.101  1.00 42.12           C  
ANISOU 5844  CG  GLU A 735     7165   4458   4380   -558   2075   -629       C  
ATOM   5845  CD  GLU A 735      17.851 122.004  12.280  1.00 42.71           C  
ANISOU 5845  CD  GLU A 735     7357   4475   4398   -534   2030   -637       C  
ATOM   5846  OE1 GLU A 735      17.764 122.066  11.034  1.00 42.76           O  
ANISOU 5846  OE1 GLU A 735     7203   4583   4462   -548   2013   -635       O  
ATOM   5847  OE2 GLU A 735      18.415 121.064  12.881  1.00 43.00           O1+
ANISOU 5847  OE2 GLU A 735     7664   4355   4321   -490   2007   -646       O1+
ATOM   5848  N   LEU A 736      15.443 127.271  11.591  1.00 36.08           N  
ANISOU 5848  N   LEU A 736     5499   4206   4005   -562   2078   -600       N  
ATOM   5849  CA  LEU A 736      15.546 128.554  10.903  1.00 35.23           C  
ANISOU 5849  CA  LEU A 736     5166   4216   4002   -480   2018   -576       C  
ATOM   5850  C   LEU A 736      15.846 129.674  11.891  1.00 34.82           C  
ANISOU 5850  C   LEU A 736     5087   4153   3992   -393   1997   -553       C  
ATOM   5851  O   LEU A 736      16.775 130.466  11.689  1.00 34.09           O  
ANISOU 5851  O   LEU A 736     4927   4066   3962   -275   1915   -520       O  
ATOM   5852  CB  LEU A 736      14.260 128.842  10.130  1.00 35.56           C  
ANISOU 5852  CB  LEU A 736     5030   4391   4091   -576   2054   -610       C  
ATOM   5853  CG  LEU A 736      14.025 127.952   8.913  1.00 35.92           C  
ANISOU 5853  CG  LEU A 736     5077   4461   4111   -641   2037   -634       C  
ATOM   5854  CD1 LEU A 736      12.749 128.341   8.186  1.00 36.44           C  
ANISOU 5854  CD1 LEU A 736     4953   4657   4234   -718   2040   -679       C  
ATOM   5855  CD2 LEU A 736      15.221 128.019   7.974  1.00 35.18           C  
ANISOU 5855  CD2 LEU A 736     4995   4352   4021   -520   1955   -591       C  
ATOM   5856  N   ILE A 737      15.069 129.750  12.974  1.00 34.34           N  
ANISOU 5856  N   ILE A 737     5084   4067   3896   -455   2079   -575       N  
ATOM   5857  CA  ILE A 737      15.334 130.742  14.011  1.00 34.12           C  
ANISOU 5857  CA  ILE A 737     5070   4007   3886   -369   2059   -556       C  
ATOM   5858  C   ILE A 737      16.672 130.457  14.680  1.00 33.97           C  
ANISOU 5858  C   ILE A 737     5233   3847   3826   -260   1969   -536       C  
ATOM   5859  O   ILE A 737      17.509 131.353  14.839  1.00 33.39           O  
ANISOU 5859  O   ILE A 737     5105   3765   3817   -144   1872   -513       O  
ATOM   5860  CB  ILE A 737      14.188 130.769  15.038  1.00 35.05           C  
ANISOU 5860  CB  ILE A 737     5242   4116   3960   -460   2189   -587       C  
ATOM   5861  CG1 ILE A 737      12.867 131.138  14.361  1.00 35.39           C  
ANISOU 5861  CG1 ILE A 737     5060   4311   4075   -553   2261   -623       C  
ATOM   5862  CG2 ILE A 737      14.508 131.735  16.173  1.00 34.94           C  
ANISOU 5862  CG2 ILE A 737     5287   4046   3941   -361   2165   -569       C  
ATOM   5863  CD1 ILE A 737      11.709 131.293  15.322  1.00 36.47           C  
ANISOU 5863  CD1 ILE A 737     5201   4457   4200   -638   2408   -662       C  
ATOM   5864  N   GLY A 738      16.898 129.196  15.059  1.00 35.06           N  
ANISOU 5864  N   GLY A 738     5592   3869   3861   -295   1990   -552       N  
ATOM   5865  CA  GLY A 738      18.097 128.852  15.810  1.00 35.22           C  
ANISOU 5865  CA  GLY A 738     5807   3743   3833   -179   1890   -547       C  
ATOM   5866  C   GLY A 738      19.381 129.231  15.098  1.00 34.48           C  
ANISOU 5866  C   GLY A 738     5592   3667   3840    -51   1756   -530       C  
ATOM   5867  O   GLY A 738      20.316 129.745  15.717  1.00 34.41           O  
ANISOU 5867  O   GLY A 738     5613   3593   3870     68   1647   -528       O  
ATOM   5868  N   ARG A 739      19.449 128.978  13.788  1.00 35.12           N  
ANISOU 5868  N   ARG A 739     5542   3834   3970    -76   1764   -523       N  
ATOM   5869  CA  ARG A 739      20.619 129.392  13.019  1.00 35.52           C  
ANISOU 5869  CA  ARG A 739     5461   3908   4125     33   1673   -507       C  
ATOM   5870  C   ARG A 739      20.760 130.907  12.979  1.00 35.27           C  
ANISOU 5870  C   ARG A 739     5239   3950   4211     83   1638   -482       C  
ATOM   5871  O   ARG A 739      21.881 131.426  12.940  1.00 35.93           O  
ANISOU 5871  O   ARG A 739     5254   4008   4389    185   1552   -476       O  
ATOM   5872  CB  ARG A 739      20.543 128.857  11.590  1.00 35.08           C  
ANISOU 5872  CB  ARG A 739     5327   3924   4078     -7   1712   -501       C  
ATOM   5873  CG  ARG A 739      20.736 127.360  11.430  1.00 35.38           C  
ANISOU 5873  CG  ARG A 739     5550   3878   4014    -29   1723   -524       C  
ATOM   5874  CD  ARG A 739      20.920 127.042   9.957  1.00 35.30           C  
ANISOU 5874  CD  ARG A 739     5452   3932   4028    -32   1740   -516       C  
ATOM   5875  NE  ARG A 739      20.794 125.621   9.655  1.00 35.91           N  
ANISOU 5875  NE  ARG A 739     5704   3945   3995    -81   1766   -539       N  
ATOM   5876  CZ  ARG A 739      21.000 125.103   8.450  1.00 36.46           C  
ANISOU 5876  CZ  ARG A 739     5758   4041   4055    -77   1778   -538       C  
ATOM   5877  NH1 ARG A 739      20.862 123.800   8.252  1.00 37.02           N1+
ANISOU 5877  NH1 ARG A 739     6011   4040   4017   -122   1797   -562       N1+
ATOM   5878  NH2 ARG A 739      21.350 125.890   7.442  1.00 36.30           N  
ANISOU 5878  NH2 ARG A 739     5562   4107   4124    -25   1777   -513       N  
ATOM   5879  N   ALA A 740      19.640 131.632  12.981  1.00 33.83           N  
ANISOU 5879  N   ALA A 740     4965   3856   4031     13   1704   -474       N  
ATOM   5880  CA  ALA A 740      19.700 133.076  12.789  1.00 33.28           C  
ANISOU 5880  CA  ALA A 740     4725   3858   4063     60   1674   -449       C  
ATOM   5881  C   ALA A 740      20.296 133.790  13.994  1.00 33.37           C  
ANISOU 5881  C   ALA A 740     4793   3786   4101    142   1596   -450       C  
ATOM   5882  O   ALA A 740      20.897 134.858  13.838  1.00 33.03           O  
ANISOU 5882  O   ALA A 740     4631   3760   4160    206   1536   -432       O  
ATOM   5883  CB  ALA A 740      18.307 133.625  12.487  1.00 33.23           C  
ANISOU 5883  CB  ALA A 740     4613   3965   4047    -19   1753   -450       C  
ATOM   5884  N   ARG A 741      20.145 133.231  15.195  1.00 32.90           N  
ANISOU 5884  N   ARG A 741     4930   3625   3947    141   1596   -473       N  
ATOM   5885  CA  ARG A 741      20.618 133.892  16.404  1.00 33.16           C  
ANISOU 5885  CA  ARG A 741     5051   3565   3984    224   1511   -480       C  
ATOM   5886  C   ARG A 741      21.997 133.422  16.847  1.00 33.57           C  
ANISOU 5886  C   ARG A 741     5208   3491   4056    330   1373   -502       C  
ATOM   5887  O   ARG A 741      22.435 133.784  17.942  1.00 34.03           O  
ANISOU 5887  O   ARG A 741     5382   3447   4101    408   1277   -520       O  
ATOM   5888  CB  ARG A 741      19.617 133.717  17.552  1.00 33.80           C  
ANISOU 5888  CB  ARG A 741     5308   3594   3940    175   1593   -493       C  
ATOM   5889  CG  ARG A 741      18.616 132.594  17.393  1.00 34.26           C  
ANISOU 5889  CG  ARG A 741     5454   3668   3896     51   1733   -507       C  
ATOM   5890  CD  ARG A 741      17.553 132.685  18.479  1.00 35.03           C  
ANISOU 5890  CD  ARG A 741     5682   3729   3897     -7   1848   -521       C  
ATOM   5891  NE  ARG A 741      18.130 132.514  19.809  1.00 35.74           N  
ANISOU 5891  NE  ARG A 741     6039   3650   3892     75   1786   -530       N  
ATOM   5892  CZ  ARG A 741      17.526 132.858  20.941  1.00 36.47           C  
ANISOU 5892  CZ  ARG A 741     6280   3678   3900     72   1857   -537       C  
ATOM   5893  NH1 ARG A 741      18.133 132.660  22.104  1.00 37.23           N1+
ANISOU 5893  NH1 ARG A 741     6651   3602   3895    161   1779   -548       N1+
ATOM   5894  NH2 ARG A 741      16.319 133.407  20.913  1.00 36.59           N  
ANISOU 5894  NH2 ARG A 741     6175   3795   3931     -9   2002   -539       N  
ATOM   5895  N   VAL A 742      22.696 132.637  16.034  1.00 34.86           N  
ANISOU 5895  N   VAL A 742     5338   3656   4252    347   1351   -509       N  
ATOM   5896  CA  VAL A 742      24.094 132.307  16.290  1.00 36.11           C  
ANISOU 5896  CA  VAL A 742     5535   3714   4469    466   1210   -542       C  
ATOM   5897  C   VAL A 742      24.943 133.026  15.249  1.00 36.29           C  
ANISOU 5897  C   VAL A 742     5306   3815   4669    500   1182   -530       C  
ATOM   5898  O   VAL A 742      24.733 132.862  14.040  1.00 35.45           O  
ANISOU 5898  O   VAL A 742     5081   3801   4586    446   1275   -506       O  
ATOM   5899  CB  VAL A 742      24.350 130.790  16.281  1.00 36.26           C  
ANISOU 5899  CB  VAL A 742     5737   3653   4386    479   1206   -568       C  
ATOM   5900  CG1 VAL A 742      23.560 130.108  15.189  1.00 35.22           C  
ANISOU 5900  CG1 VAL A 742     5568   3613   4203    367   1346   -546       C  
ATOM   5901  CG2 VAL A 742      25.838 130.510  16.121  1.00 37.30           C  
ANISOU 5901  CG2 VAL A 742     5824   3724   4623    610   1069   -607       C  
ATOM   5902  N   SER A 743      25.889 133.837  15.722  1.00 37.69           N  
ANISOU 5902  N   SER A 743     5409   3944   4969    585   1059   -551       N  
ATOM   5903  CA  SER A 743      26.781 134.622  14.877  1.00 37.58           C  
ANISOU 5903  CA  SER A 743     5158   3982   5140    610   1041   -546       C  
ATOM   5904  C   SER A 743      28.128 133.934  14.763  1.00 38.42           C  
ANISOU 5904  C   SER A 743     5233   4022   5342    706    947   -599       C  
ATOM   5905  O   SER A 743      28.747 133.625  15.792  1.00 39.24           O  
ANISOU 5905  O   SER A 743     5453   4014   5444    799    798   -653       O  
ATOM   5906  CB  SER A 743      26.964 136.023  15.448  1.00 37.58           C  
ANISOU 5906  CB  SER A 743     5076   3968   5235    629    969   -543       C  
ATOM   5907  OG  SER A 743      28.081 136.661  14.856  1.00 37.89           O  
ANISOU 5907  OG  SER A 743     4911   4018   5468    660    931   -556       O  
ATOM   5908  N   PRO A 744      28.619 133.683  13.546  1.00 42.63           N  
ANISOU 5908  N   PRO A 744     5621   4617   5958    698   1025   -591       N  
ATOM   5909  CA  PRO A 744      29.898 132.971  13.399  1.00 43.70           C  
ANISOU 5909  CA  PRO A 744     5712   4696   6194    799    950   -650       C  
ATOM   5910  C   PRO A 744      31.111 133.786  13.811  1.00 44.90           C  
ANISOU 5910  C   PRO A 744     5701   4803   6557    875    820   -703       C  
ATOM   5911  O   PRO A 744      32.204 133.216  13.921  1.00 45.71           O  
ANISOU 5911  O   PRO A 744     5762   4847   6759    978    723   -772       O  
ATOM   5912  CB  PRO A 744      29.946 132.652  11.901  1.00 42.94           C  
ANISOU 5912  CB  PRO A 744     5502   4688   6125    755   1105   -619       C  
ATOM   5913  CG  PRO A 744      29.147 133.751  11.272  1.00 41.44           C  
ANISOU 5913  CG  PRO A 744     5213   4593   5939    653   1219   -552       C  
ATOM   5914  CD  PRO A 744      28.034 134.050  12.244  1.00 41.04           C  
ANISOU 5914  CD  PRO A 744     5301   4534   5760    608   1185   -533       C  
ATOM   5915  N   GLY A 745      30.952 135.082  14.051  1.00 46.76           N  
ANISOU 5915  N   GLY A 745     5842   5057   6867    831    808   -680       N  
ATOM   5916  CA  GLY A 745      32.086 135.982  14.150  1.00 47.47           C  
ANISOU 5916  CA  GLY A 745     5731   5119   7187    869    720   -725       C  
ATOM   5917  C   GLY A 745      33.006 135.675  15.316  1.00 48.77           C  
ANISOU 5917  C   GLY A 745     5948   5163   7419    994    491   -819       C  
ATOM   5918  O   GLY A 745      32.714 134.891  16.219  1.00 48.79           O  
ANISOU 5918  O   GLY A 745     6183   5087   7268   1059    388   -844       O  
ATOM   5919  N   ALA A 746      34.168 136.327  15.272  1.00 51.49           N  
ANISOU 5919  N   ALA A 746     6072   5486   8007   1028    409   -879       N  
ATOM   5920  CA  ALA A 746      35.157 136.236  16.336  1.00 52.31           C  
ANISOU 5920  CA  ALA A 746     6178   5476   8223   1153    160   -985       C  
ATOM   5921  C   ALA A 746      35.307 137.589  17.020  1.00 52.76           C  
ANISOU 5921  C   ALA A 746     6167   5490   8388   1126     49   -999       C  
ATOM   5922  O   ALA A 746      36.413 138.134  17.101  1.00 53.47           O  
ANISOU 5922  O   ALA A 746     6048   5546   8723   1155    -61  -1076       O  
ATOM   5923  CB  ALA A 746      36.502 135.758  15.784  1.00 52.47           C  
ANISOU 5923  CB  ALA A 746     5975   5496   8465   1230    128  -1071       C  
ATOM   5924  N   GLY A 747      34.198 138.143  17.506  1.00 50.64           N  
ANISOU 5924  N   GLY A 747     6070   5222   7948   1068     80   -931       N  
ATOM   5925  CA  GLY A 747      34.216 139.430  18.173  1.00 51.16           C  
ANISOU 5925  CA  GLY A 747     6112   5242   8085   1044    -19   -937       C  
ATOM   5926  C   GLY A 747      33.746 140.567  17.288  1.00 50.53           C  
ANISOU 5926  C   GLY A 747     5888   5255   8057    911    165   -856       C  
ATOM   5927  O   GLY A 747      34.409 141.605  17.194  1.00 50.61           O  
ANISOU 5927  O   GLY A 747     5722   5246   8263    875    127   -880       O  
ATOM   5928  N   TRP A 748      32.600 140.383  16.638  1.00 50.44           N  
ANISOU 5928  N   TRP A 748     5957   5335   7872    839    358   -765       N  
ATOM   5929  CA  TRP A 748      32.080 141.385  15.721  1.00 49.06           C  
ANISOU 5929  CA  TRP A 748     5674   5245   7720    730    528   -688       C  
ATOM   5930  C   TRP A 748      31.545 142.600  16.475  1.00 49.12           C  
ANISOU 5930  C   TRP A 748     5757   5215   7691    710    464   -666       C  
ATOM   5931  O   TRP A 748      31.322 142.570  17.689  1.00 50.11           O  
ANISOU 5931  O   TRP A 748     6053   5260   7727    773    319   -696       O  
ATOM   5932  CB  TRP A 748      30.969 140.794  14.853  1.00 47.75           C  
ANISOU 5932  CB  TRP A 748     5583   5184   7376    676    720   -611       C  
ATOM   5933  CG  TRP A 748      31.463 139.967  13.708  1.00 47.10           C  
ANISOU 5933  CG  TRP A 748     5392   5155   7348    667    836   -611       C  
ATOM   5934  CD1 TRP A 748      32.742 139.898  13.237  1.00 47.45           C  
ANISOU 5934  CD1 TRP A 748     5250   5180   7599    689    830   -663       C  
ATOM   5935  CD2 TRP A 748      30.685 139.088  12.887  1.00 45.85           C  
ANISOU 5935  CD2 TRP A 748     5307   5074   7039    636    980   -564       C  
ATOM   5936  NE1 TRP A 748      32.809 139.031  12.173  1.00 46.65           N  
ANISOU 5936  NE1 TRP A 748     5115   5138   7472    681    971   -645       N  
ATOM   5937  CE2 TRP A 748      31.559 138.521  11.938  1.00 45.83           C  
ANISOU 5937  CE2 TRP A 748     5178   5091   7145    649   1055   -584       C  
ATOM   5938  CE3 TRP A 748      29.335 138.726  12.861  1.00 44.98           C  
ANISOU 5938  CE3 TRP A 748     5351   5018   6722    596   1052   -514       C  
ATOM   5939  CZ2 TRP A 748      31.126 137.610  10.976  1.00 45.21           C  
ANISOU 5939  CZ2 TRP A 748     5147   5075   6957    629   1189   -551       C  
ATOM   5940  CZ3 TRP A 748      28.907 137.822  11.906  1.00 44.29           C  
ANISOU 5940  CZ3 TRP A 748     5291   4995   6542    567   1175   -487       C  
ATOM   5941  CH2 TRP A 748      29.800 137.275  10.976  1.00 44.46           C  
ANISOU 5941  CH2 TRP A 748     5209   5026   6657    586   1237   -503       C  
ATOM   5942  N   SER A 749      31.339 143.680  15.729  1.00 43.08           N  
ANISOU 5942  N   SER A 749     4885   4499   6986    627    579   -612       N  
ATOM   5943  CA  SER A 749      30.736 144.891  16.260  1.00 42.83           C  
ANISOU 5943  CA  SER A 749     4925   4440   6908    606    546   -582       C  
ATOM   5944  C   SER A 749      29.218 144.830  16.112  1.00 41.66           C  
ANISOU 5944  C   SER A 749     4919   4374   6537    586    668   -510       C  
ATOM   5945  O   SER A 749      28.666 143.953  15.443  1.00 40.66           O  
ANISOU 5945  O   SER A 749     4809   4327   6311    568    787   -480       O  
ATOM   5946  CB  SER A 749      31.293 146.125  15.551  1.00 42.73           C  
ANISOU 5946  CB  SER A 749     4743   4422   7069    531    603   -565       C  
ATOM   5947  OG  SER A 749      30.781 146.225  14.235  1.00 41.09           O  
ANISOU 5947  OG  SER A 749     4485   4311   6817    463    810   -491       O  
ATOM   5948  N   ILE A 750      28.538 145.786  16.749  1.00 39.53           N  
ANISOU 5948  N   ILE A 750     4747   4080   6195    591    633   -489       N  
ATOM   5949  CA  ILE A 750      27.077 145.798  16.726  1.00 38.21           C  
ANISOU 5949  CA  ILE A 750     4696   3988   5835    582    738   -436       C  
ATOM   5950  C   ILE A 750      26.565 146.044  15.311  1.00 37.02           C  
ANISOU 5950  C   ILE A 750     4441   3948   5676    518    908   -375       C  
ATOM   5951  O   ILE A 750      25.595 145.416  14.866  1.00 35.96           O  
ANISOU 5951  O   ILE A 750     4346   3903   5414    502   1011   -347       O  
ATOM   5952  CB  ILE A 750      26.537 146.843  17.720  1.00 38.45           C  
ANISOU 5952  CB  ILE A 750     4847   3962   5802    616    665   -433       C  
ATOM   5953  CG1 ILE A 750      26.863 146.427  19.156  1.00 39.91           C  
ANISOU 5953  CG1 ILE A 750     5192   4029   5941    692    503   -493       C  
ATOM   5954  CG2 ILE A 750      25.036 147.028  17.544  1.00 37.41           C  
ANISOU 5954  CG2 ILE A 750     4786   3923   5506    606    791   -385       C  
ATOM   5955  CD1 ILE A 750      26.415 147.428  20.196  1.00 40.48           C  
ANISOU 5955  CD1 ILE A 750     5409   4027   5944    737    424   -496       C  
ATOM   5956  N   ARG A 751      27.213 146.953  14.579  1.00 40.16           N  
ANISOU 5956  N   ARG A 751     4717   4332   6208    478    936   -357       N  
ATOM   5957  CA  ARG A 751      26.810 147.227  13.203  1.00 39.02           C  
ANISOU 5957  CA  ARG A 751     4508   4271   6045    428   1091   -300       C  
ATOM   5958  C   ARG A 751      26.934 145.988  12.323  1.00 38.14           C  
ANISOU 5958  C   ARG A 751     4351   4225   5917    410   1185   -297       C  
ATOM   5959  O   ARG A 751      26.102 145.771  11.434  1.00 36.99           O  
ANISOU 5959  O   ARG A 751     4223   4164   5668    391   1294   -256       O  
ATOM   5960  CB  ARG A 751      27.648 148.376  12.632  1.00 39.69           C  
ANISOU 5960  CB  ARG A 751     4496   4301   6283    381   1116   -285       C  
ATOM   5961  CG  ARG A 751      29.077 147.985  12.270  1.00 40.10           C  
ANISOU 5961  CG  ARG A 751     4401   4307   6527    349   1121   -324       C  
ATOM   5962  CD  ARG A 751      29.941 149.166  11.877  1.00 41.61           C  
ANISOU 5962  CD  ARG A 751     4495   4426   6890    286   1150   -320       C  
ATOM   5963  NE  ARG A 751      31.308 148.734  11.593  1.00 42.50           N  
ANISOU 5963  NE  ARG A 751     4439   4501   7208    255   1163   -373       N  
ATOM   5964  CZ  ARG A 751      32.308 148.786  12.467  1.00 44.03           C  
ANISOU 5964  CZ  ARG A 751     4544   4612   7573    268   1013   -453       C  
ATOM   5965  NH1 ARG A 751      33.514 148.363  12.119  1.00 44.73           N1+
ANISOU 5965  NH1 ARG A 751     4455   4679   7863    246   1036   -509       N1+
ATOM   5966  NH2 ARG A 751      32.105 149.268  13.686  1.00 44.80           N  
ANISOU 5966  NH2 ARG A 751     4733   4646   7643    310    836   -482       N  
ATOM   5967  N   GLU A 752      27.940 145.147  12.576  1.00 41.80           N  
ANISOU 5967  N   GLU A 752     4762   4644   6475    427   1131   -347       N  
ATOM   5968  CA  GLU A 752      28.225 144.037  11.677  1.00 40.95           C  
ANISOU 5968  CA  GLU A 752     4607   4584   6367    417   1222   -347       C  
ATOM   5969  C   GLU A 752      27.306 142.849  11.926  1.00 40.83           C  
ANISOU 5969  C   GLU A 752     4714   4620   6180    437   1230   -350       C  
ATOM   5970  O   GLU A 752      27.008 142.100  10.990  1.00 40.34           O  
ANISOU 5970  O   GLU A 752     4651   4621   6056    415   1332   -329       O  
ATOM   5971  CB  GLU A 752      29.688 143.615  11.817  1.00 42.21           C  
ANISOU 5971  CB  GLU A 752     4652   4677   6707    439   1162   -409       C  
ATOM   5972  CG  GLU A 752      30.257 142.919  10.592  1.00 41.83           C  
ANISOU 5972  CG  GLU A 752     4509   4668   6715    420   1295   -403       C  
ATOM   5973  CD  GLU A 752      31.695 142.477  10.788  1.00 43.56           C  
ANISOU 5973  CD  GLU A 752     4594   4827   7129    456   1233   -478       C  
ATOM   5974  OE1 GLU A 752      32.154 141.594  10.031  1.00 43.03           O  
ANISOU 5974  OE1 GLU A 752     4475   4787   7088    469   1320   -490       O  
ATOM   5975  OE2 GLU A 752      32.363 143.008  11.702  1.00 45.20           O1+
ANISOU 5975  OE2 GLU A 752     4748   4960   7467    478   1090   -532       O1+
ATOM   5976  N   THR A 753      26.854 142.654  13.167  1.00 37.12           N  
ANISOU 5976  N   THR A 753     4364   4112   5627    473   1129   -376       N  
ATOM   5977  CA  THR A 753      25.893 141.589  13.436  1.00 36.80           C  
ANISOU 5977  CA  THR A 753     4451   4110   5421    472   1161   -377       C  
ATOM   5978  C   THR A 753      24.486 141.999  13.020  1.00 35.35           C  
ANISOU 5978  C   THR A 753     4292   4019   5120    430   1257   -334       C  
ATOM   5979  O   THR A 753      23.709 141.164  12.542  1.00 34.66           O  
ANISOU 5979  O   THR A 753     4238   3998   4932    397   1334   -326       O  
ATOM   5980  CB  THR A 753      25.912 141.206  14.916  1.00 38.22           C  
ANISOU 5980  CB  THR A 753     4779   4200   5542    524   1040   -421       C  
ATOM   5981  OG1 THR A 753      25.234 142.210  15.680  1.00 38.29           O  
ANISOU 5981  OG1 THR A 753     4850   4194   5504    532   1011   -409       O  
ATOM   5982  CG2 THR A 753      27.340 141.074  15.414  1.00 39.86           C  
ANISOU 5982  CG2 THR A 753     4951   4306   5889    586    901   -477       C  
ATOM   5983  N   ALA A 754      24.142 143.277  13.200  1.00 33.86           N  
ANISOU 5983  N   ALA A 754     4085   3832   4948    435   1243   -312       N  
ATOM   5984  CA  ALA A 754      22.851 143.767  12.734  1.00 33.45           C  
ANISOU 5984  CA  ALA A 754     4036   3870   4803    415   1320   -280       C  
ATOM   5985  C   ALA A 754      22.706 143.604  11.227  1.00 33.27           C  
ANISOU 5985  C   ALA A 754     3939   3924   4778    381   1416   -248       C  
ATOM   5986  O   ALA A 754      21.588 143.454  10.723  1.00 33.03           O  
ANISOU 5986  O   ALA A 754     3916   3979   4654    365   1472   -239       O  
ATOM   5987  CB  ALA A 754      22.669 145.232  13.131  1.00 33.59           C  
ANISOU 5987  CB  ALA A 754     4055   3862   4847    444   1279   -264       C  
ATOM   5988  N   CYS A 755      23.821 143.631  10.494  1.00 33.75           N  
ANISOU 5988  N   CYS A 755     3929   3951   4944    373   1437   -238       N  
ATOM   5989  CA  CYS A 755      23.767 143.354   9.063  1.00 32.77           C  
ANISOU 5989  CA  CYS A 755     3769   3881   4801    347   1537   -209       C  
ATOM   5990  C   CYS A 755      23.542 141.869   8.800  1.00 32.76           C  
ANISOU 5990  C   CYS A 755     3804   3917   4726    331   1568   -230       C  
ATOM   5991  O   CYS A 755      22.789 141.504   7.890  1.00 32.47           O  
ANISOU 5991  O   CYS A 755     3785   3949   4603    311   1629   -215       O  
ATOM   5992  CB  CYS A 755      25.048 143.836   8.382  1.00 33.02           C  
ANISOU 5992  CB  CYS A 755     3721   3857   4970    338   1579   -194       C  
ATOM   5993  SG  CYS A 755      25.221 145.634   8.282  1.00 33.53           S  
ANISOU 5993  SG  CYS A 755     3762   3873   5105    333   1579   -158       S  
ATOM   5994  N   LEU A 756      24.185 140.998   9.585  1.00 32.37           N  
ANISOU 5994  N   LEU A 756     3782   3813   4705    346   1515   -268       N  
ATOM   5995  CA  LEU A 756      23.938 139.566   9.451  1.00 32.39           C  
ANISOU 5995  CA  LEU A 756     3849   3835   4624    331   1539   -289       C  
ATOM