CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Elnemo is running on a new server.
Should you encounter any unexpected behaviour,
please let us know.


***  CALCIUM BINDING/STRUCTURAL PROTEIN 16-APR-14 4Q57  ***

elNémo ID: 19080913321098883

Job options:

ID        	=	 19080913321098883
JOBID     	=	 CALCIUM BINDING/STRUCTURAL PROTEIN 16-APR-14 4Q57
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    CALCIUM BINDING/STRUCTURAL PROTEIN      16-APR-14   4Q57              
TITLE     CRYSTAL STRUCTURE OF THE PLECTIN 1A ACTIN-BINDING DOMAIN/N-TERMINAL   
TITLE    2 DOMAIN OF CALMODULIN COMPLEX                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALMODULIN;                                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN (UNP RESIDUES 10-74);                    
COMPND   5 SYNONYM: CAM;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PLECTIN;                                                   
COMPND   8 CHAIN: B;                                                            
COMPND   9 FRAGMENT: ACTIN-BINDING DOMAIN (UNP RESIDUES 23-263, SEE REMARK 999);
COMPND  10 SYNONYM: PCN, PLTN, PLECTIN-1, PLECTIN-6                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   7 ORGANISM_COMMON: MOUSE;                                              
SOURCE   8 ORGANISM_TAXID: 10090                                                
KEYWDS    EF-HAND MOTIF, CALPONIN HOMOLOGY DOMAIN, CALCIUM BINDING-STRUCTURAL   
KEYWDS   2 PROTEIN COMPLEX                                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-G.SONG,J.KOSTAN,I.GRISHKOVSKAYA,K.DJINOVIC-CARUGO                  
REVDAT   1   23-JUL-14 4Q57    0                                                
JRNL        AUTH   J.-G.SONG,J.KOSTAN,I.GRISHKOVSKAYA,K.DJINOVIC-CARUGO         
JRNL        TITL   CRYSTAL STRUCTURE OF THE PLECTIN 1A ACTIN-BINDING            
JRNL        TITL 2 DOMAIN/N-TERMINAL DOMAIN OF CALMODULIN COMPLEX               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.93                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31746                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.153                           
REMARK   3   R VALUE            (WORKING SET) : 0.151                           
REMARK   3   FREE R VALUE                     : 0.187                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1600                            
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 48.9468 -  4.0026    1.00     2938   150  0.1566 0.1860        
REMARK   3     2  4.0026 -  3.1771    1.00     2826   150  0.1341 0.1764        
REMARK   3     3  3.1771 -  2.7756    1.00     2766   163  0.1499 0.1734        
REMARK   3     4  2.7756 -  2.5218    1.00     2731   168  0.1482 0.1868        
REMARK   3     5  2.5218 -  2.3411    1.00     2734   156  0.1500 0.1859        
REMARK   3     6  2.3411 -  2.2030    1.00     2757   144  0.1379 0.1670        
REMARK   3     7  2.2030 -  2.0927    1.00     2723   150  0.1479 0.1982        
REMARK   3     8  2.0927 -  2.0016    1.00     2739   143  0.1521 0.2114        
REMARK   3     9  2.0016 -  1.9245    1.00     2750   119  0.1675 0.1940        
REMARK   3    10  1.9245 -  1.8581    1.00     2737   126  0.1775 0.2295        
REMARK   3    11  1.8581 -  1.8000    0.90     2445   131  0.2008 0.2202        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.010           
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      :  0.007           2621                                  
REMARK   3   ANGLE     :  0.963           3543                                  
REMARK   3   CHIRALITY :  0.042            394                                  
REMARK   3   PLANARITY :  0.005            466                                  
REMARK   3   DIHEDRAL  : 12.834           1005                                  
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 9 through 19 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  37.8721  17.4003   6.4633              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4739 T22:   0.2380                                     
REMARK   3      T33:   0.2416 T12:   0.0057                                     
REMARK   3      T13:  -0.0139 T23:  -0.0615                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0230 L22:   7.4311                                     
REMARK   3      L33:   2.0004 L12:  -0.2057                                     
REMARK   3      L13:  -2.0758 L23:   1.0740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0113 S12:  -0.6408 S13:   0.5859                       
REMARK   3      S21:   0.5414 S22:   0.0408 S23:  -0.0469                       
REMARK   3      S31:  -0.8797 S32:  -0.0497 S33:  -0.0237                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain 'A' and (resid 20 through 38 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  38.5259  12.7710  -5.1203              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2558 T22:   0.1626                                     
REMARK   3      T33:   0.2130 T12:   0.0207                                     
REMARK   3      T13:  -0.0476 T23:   0.0219                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3356 L22:   2.6090                                     
REMARK   3      L33:   3.1676 L12:   0.3257                                     
REMARK   3      L13:  -2.2557 L23:  -0.2435                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0183 S12:  -0.0019 S13:   0.0229                       
REMARK   3      S21:  -0.2580 S22:  -0.1284 S23:   0.1497                       
REMARK   3      S31:  -0.3946 S32:  -0.0150 S33:   0.1164                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain 'A' and (resid 39 through 44 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  50.2796   9.9945  -7.8213              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3877 T22:   0.3756                                     
REMARK   3      T33:   0.4218 T12:   0.0180                                     
REMARK   3      T13:   0.0775 T23:   0.1245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5794 L22:   3.3824                                     
REMARK   3      L33:   2.4442 L12:   1.7885                                     
REMARK   3      L13:   1.1458 L23:   2.7702                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1347 S12:  -0.0395 S13:  -0.2962                       
REMARK   3      S21:  -0.0259 S22:  -0.2256 S23:  -0.8010                       
REMARK   3      S31:   0.0230 S32:   0.5747 S33:   0.2633                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain 'A' and (resid 45 through 55 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  43.3726   1.7458  -2.9862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2752 T22:   0.1025                                     
REMARK   3      T33:   0.2650 T12:   0.0185                                     
REMARK   3      T13:  -0.0386 T23:   0.0242                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5016 L22:   4.5350                                     
REMARK   3      L33:   7.7769 L12:   1.2605                                     
REMARK   3      L13:  -3.7317 L23:  -1.6804                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0150 S12:   0.0289 S13:   0.1158                       
REMARK   3      S21:  -0.6220 S22:  -0.0937 S23:  -0.2829                       
REMARK   3      S31:   0.3764 S32:   0.0698 S33:   0.0670                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain 'A' and (resid 56 through 73 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  35.4243   5.6827   5.6961              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1461 T22:   0.1629                                     
REMARK   3      T33:   0.1409 T12:  -0.0067                                     
REMARK   3      T13:   0.0046 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5325 L22:   3.8520                                     
REMARK   3      L33:   3.0334 L12:  -0.2566                                     
REMARK   3      L13:  -0.4820 L23:   0.3355                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:  -0.3522 S13:  -0.0760                       
REMARK   3      S21:   0.1441 S22:  -0.0916 S23:   0.2939                       
REMARK   3      S31:   0.0364 S32:  -0.3810 S33:   0.0469                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain 'B' and (resid -3 through 59 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  49.4175  27.8550   8.9188              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1376 T22:   0.1418                                     
REMARK   3      T33:   0.1113 T12:   0.0215                                     
REMARK   3      T13:  -0.0200 T23:   0.0006                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4338 L22:   5.8374                                     
REMARK   3      L33:   0.6163 L12:   1.0501                                     
REMARK   3      L13:   0.2139 L23:   1.4538                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0744 S12:   0.0216 S13:  -0.1016                       
REMARK   3      S21:   0.0205 S22:  -0.1025 S23:  -0.1763                       
REMARK   3      S31:   0.1141 S32:   0.0028 S33:   0.0323                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain 'B' and (resid 60 through 144 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  52.2283  37.5029  25.4678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0641 T22:   0.0671                                     
REMARK   3      T33:   0.0623 T12:  -0.0037                                     
REMARK   3      T13:  -0.0054 T23:  -0.0037                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1774 L22:   1.9208                                     
REMARK   3      L33:   1.8707 L12:  -0.3399                                     
REMARK   3      L13:   0.1499 L23:  -0.1563                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0125 S12:  -0.0391 S13:  -0.0238                       
REMARK   3      S21:  -0.0055 S22:  -0.0400 S23:   0.0061                       
REMARK   3      S31:  -0.0902 S32:   0.0379 S33:   0.0189                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain 'B' and (resid 145 through 184 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  27.9754  43.5961   8.6848              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1077 T22:   0.2957                                     
REMARK   3      T33:   0.1759 T12:   0.0158                                     
REMARK   3      T13:   0.0259 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3820 L22:   3.4849                                     
REMARK   3      L33:   1.4104 L12:  -0.2624                                     
REMARK   3      L13:   0.1238 L23:  -0.3055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0890 S12:  -0.4129 S13:   0.0123                       
REMARK   3      S21:   0.3172 S22:   0.2034 S23:   0.3826                       
REMARK   3      S31:  -0.0618 S32:  -0.5755 S33:  -0.0330                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain 'B' and (resid 185 through 263 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  39.8213  46.2114  -0.4927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0601 T22:   0.0745                                     
REMARK   3      T33:   0.0818 T12:  -0.0121                                     
REMARK   3      T13:  -0.0228 T23:   0.0045                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2428 L22:   1.6830                                     
REMARK   3      L33:   1.9029 L12:  -0.3814                                     
REMARK   3      L13:   0.7319 L23:  -0.3462                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0667 S12:  -0.0455 S13:   0.1152                       
REMARK   3      S21:   0.0448 S22:   0.0014 S23:  -0.0736                       
REMARK   3      S31:  -0.0831 S32:  -0.0247 S33:   0.0488                       
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 4Q57 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-APR-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB085618.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : DIAMOND(001)                       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31749                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 9.400                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.50300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M BIS-TRIS, PH 6.5, 0.2 M            
REMARK 280  MAGNESIUM CHLORIDE, 13% PEG8000, VAPOR DIFFUSION, HANGING DROP,     
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       29.54000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.65000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       32.68950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       43.65000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       29.54000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       32.68950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2280 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 16210 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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   O    HOH B   713     O    HOH B   759              2.03            
REMARK 500   OD1  ASP B   237     O    HOH B   681              2.03            
REMARK 500   O    HOH B   718     O    HOH B   767              2.06            
REMARK 500   O    HOH B   678     O    HOH B   712              2.06            
REMARK 500   O    HOH A   224     O    HOH A   244              2.13            
REMARK 500   O    HOH B   712     O    HOH B   717              2.14            
REMARK 500   O    HOH B   554     O    HOH B   713              2.15            
REMARK 500   O    HOH B   596     O    HOH B   712              2.18            
REMARK 500   O    HOH B   744     O    HOH B   761              2.19            
REMARK 500   O    HOH B   716     O    HOH B   767              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU B   227     O    HOH B   712     4565     2.11            
REMARK 500   O    HOH B   622     O    HOH B   712     4565     2.12            
REMARK 500   O    HOH B   620     O    HOH B   639     2665     2.13            
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    ASP B 157       33.99    -96.74                                   
REMARK 500    THR B 184      -94.86   -130.78                                   
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                              MG B 301  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 123   OD1                                                    
REMARK 620 2 ASN B 122   OD1  82.3                                              
REMARK 620 3 HOH B 604   O    88.9  98.5                                        
REMARK 620 4 HOH B 601   O    96.5  81.6 174.6                                  
REMARK 620 5 HOH B 602   O   170.1  92.7  83.4  91.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 101  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A  31   OE2                                                    
REMARK 620 2 ASP A  20   OD1  94.2                                              
REMARK 620 3 THR A  26   O   107.7  85.5                                        
REMARK 620 4 ASP A  22   OD1  84.5  84.7 164.9                                  
REMARK 620 5 ASP A  24   OD1 165.0  87.9  87.3  80.9                            
REMARK 620 6 GLU A  31   OE1  49.4 124.6  72.7 122.3 138.8                      
REMARK 620 7 HOH A 204   O    95.8 166.2 100.3  86.9  80.0  69.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 102  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  56   OD1                                                    
REMARK 620 2 THR A  62   O    86.7                                              
REMARK 620 3 ASP A  58   OD1  82.2 151.2                                        
REMARK 620 4 GLU A  67   OE1 102.7  81.7 126.7                                  
REMARK 620 5 ASN A  60   OD1  89.8  75.7  77.7 153.5                            
REMARK 620 6 GLU A  67   OE2  92.5 133.7  73.6  53.3 150.6                      
REMARK 620 7 HOH A 239   O   167.5 104.3  85.3  84.9  87.4  84.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 102                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 304                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 305                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 306                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4Q58   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4Q59   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 PROTEIN IS ISOFORM PLEC-1A (Q9QXS1-3) OF MUS MUSCULUS PLECTIN.       
DBREF  4Q57 A    9    73  UNP    P62158   CALM_HUMAN      10     74             
DBREF  4Q57 B   23   263  UNP    Q9QXS1   PLEC_MOUSE      23    263             
SEQADV 4Q57 GLY B   -3  UNP  Q9QXS1              EXPRESSION TAG                 
SEQADV 4Q57 PRO B   -2  UNP  Q9QXS1              EXPRESSION TAG                 
SEQADV 4Q57 MET B   -1  UNP  Q9QXS1              EXPRESSION TAG                 
SEQRES   1 A   65  ILE ALA GLU PHE LYS GLU ALA PHE SER LEU PHE ASP LYS          
SEQRES   2 A   65  ASP GLY ASP GLY THR ILE THR THR LYS GLU LEU GLY THR          
SEQRES   3 A   65  VAL MET ARG SER LEU GLY GLN ASN PRO THR GLU ALA GLU          
SEQRES   4 A   65  LEU GLN ASP MET ILE ASN GLU VAL ASP ALA ASP GLY ASN          
SEQRES   5 A   65  GLY THR ILE ASP PHE PRO GLU PHE LEU THR MET MET ALA          
SEQRES   1 B  244  GLY PRO MET ASP ASN LEU TYR LEU ALA VAL LEU ARG ALA          
SEQRES   2 B  244  SER GLU GLY LYS LYS ASP GLU ARG ASP ARG VAL GLN LYS          
SEQRES   3 B  244  LYS THR PHE THR LYS TRP VAL ASN LYS HIS LEU ILE LYS          
SEQRES   4 B  244  ALA GLN ARG HIS ILE SER ASP LEU TYR GLU ASP LEU ARG          
SEQRES   5 B  244  ASP GLY HIS ASN LEU ILE SER LEU LEU GLU VAL LEU SER          
SEQRES   6 B  244  GLY ASP SER LEU PRO ARG GLU LYS GLY ARG MET ARG PHE          
SEQRES   7 B  244  HIS LYS LEU GLN ASN VAL GLN ILE ALA LEU ASP TYR LEU          
SEQRES   8 B  244  ARG HIS ARG GLN VAL LYS LEU VAL ASN ILE ARG ASN ASP          
SEQRES   9 B  244  ASP ILE ALA ASP GLY ASN PRO LYS LEU THR LEU GLY LEU          
SEQRES  10 B  244  ILE TRP THR ILE ILE LEU HIS PHE GLN ILE SER ASP ILE          
SEQRES  11 B  244  GLN VAL SER GLY GLN SER GLU ASP MET THR ALA LYS GLU          
SEQRES  12 B  244  LYS LEU LEU LEU TRP SER GLN ARG MET VAL GLU GLY TYR          
SEQRES  13 B  244  GLN GLY LEU ARG CYS ASP ASN PHE THR THR SER TRP ARG          
SEQRES  14 B  244  ASP GLY ARG LEU PHE ASN ALA ILE ILE HIS ARG HIS LYS          
SEQRES  15 B  244  PRO MET LEU ILE ASP MET ASN LYS VAL TYR ARG GLN THR          
SEQRES  16 B  244  ASN LEU GLU ASN LEU ASP GLN ALA PHE SER VAL ALA GLU          
SEQRES  17 B  244  ARG ASP LEU GLY VAL THR ARG LEU LEU ASP PRO GLU ASP          
SEQRES  18 B  244  VAL ASP VAL PRO GLN PRO ASP GLU LYS SER ILE ILE THR          
SEQRES  19 B  244  TYR VAL SER SER LEU TYR ASP ALA MET PRO                      
HET     CA  A 101       1                                                       
HET     CA  A 102       1                                                       
HET     MG  B 301       1                                                       
HET     CL  B 302       1                                                       
HET    EDO  B 303       4                                                       
HET    EDO  B 304       4                                                       
HET    EDO  B 305       4                                                       
HET    GOL  B 306       6                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     GOL GLYCEROL                                                         
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3   CA    2(CA 2+)                                                     
FORMUL   5   MG    MG 2+                                                        
FORMUL   6   CL    CL 1-                                                        
FORMUL   7  EDO    3(C2 H6 O2)                                                  
FORMUL  10  GOL    C3 H8 O3                                                     
FORMUL  11  HOH   *427(H2 O)                                                    
HELIX    1   1 ILE A    9  ASP A   20  1                                  12    
HELIX    2   2 THR A   28  LEU A   39  1                                  12    
HELIX    3   3 THR A   44  ASP A   56  1                                  13    
HELIX    4   4 PHE A   65  ALA A   73  1                                   9    
HELIX    5   5 ASP B   23  ILE B   57  1                                  35    
HELIX    6   6 LYS B   58  GLN B   60  5                                   3    
HELIX    7   7 GLY B   73  GLY B   85  1                                  13    
HELIX    8   8 MET B   95  ARG B  113  1                                  19    
HELIX    9   9 ARG B  121  ASP B  127  1                                   7    
HELIX   10  10 ASN B  129  GLN B  145  1                                  17    
HELIX   11  11 ILE B  146  ILE B  149  5                                   4    
HELIX   12  12 THR B  159  VAL B  172  1                                  14    
HELIX   13  13 THR B  184  ARG B  188  5                                   5    
HELIX   14  14 GLY B  190  LYS B  201  1                                  12    
HELIX   15  15 PRO B  202  ILE B  205  5                                   4    
HELIX   16  16 ASP B  206  GLN B  213  1                                   8    
HELIX   17  17 THR B  214  GLY B  231  1                                  18    
HELIX   18  18 ASP B  237  ASP B  242  1                                   6    
HELIX   19  19 ASP B  247  ALA B  261  1                                  15    
SHEET    1   A 2 THR A  26  ILE A  27  0                                        
SHEET    2   A 2 ILE A  63  ASP A  64 -1  O  ILE A  63   N  ILE A  27           
LINK         OD1 ASP B 123                MG    MG B 301     1555   1555  2.06  
LINK         OD1 ASN B 122                MG    MG B 301     1555   1555  2.14  
LINK         OE2 GLU A  31                CA    CA A 101     1555   1555  2.19  
LINK         OD1 ASP A  20                CA    CA A 101     1555   1555  2.22  
LINK         O   THR A  26                CA    CA A 101     1555   1555  2.22  
LINK         OD1 ASP A  22                CA    CA A 101     1555   1555  2.26  
LINK         OD1 ASP A  56                CA    CA A 102     1555   1555  2.29  
LINK         OD1 ASP A  24                CA    CA A 101     1555   1555  2.31  
LINK         O   THR A  62                CA    CA A 102     1555   1555  2.34  
LINK         OD1 ASP A  58                CA    CA A 102     1555   1555  2.37  
LINK         OE1 GLU A  67                CA    CA A 102     1555   1555  2.41  
LINK         OD1 ASN A  60                CA    CA A 102     1555   1555  2.46  
LINK         OE2 GLU A  67                CA    CA A 102     1555   1555  2.51  
LINK         OE1 GLU A  31                CA    CA A 101     1555   1555  2.85  
LINK        MG    MG B 301                 O   HOH B 604     1555   1555  2.07  
LINK        MG    MG B 301                 O   HOH B 601     1555   1555  2.09  
LINK        MG    MG B 301                 O   HOH B 602     1555   1555  2.10  
LINK        CA    CA A 101                 O   HOH A 204     1555   1555  2.29  
LINK        CA    CA A 102                 O   HOH A 239     1555   1555  2.42  
SITE     1 AC1  6 ASP A  20  ASP A  22  ASP A  24  THR A  26                    
SITE     2 AC1  6 GLU A  31  HOH A 204                                          
SITE     1 AC2  6 ASP A  56  ASP A  58  ASN A  60  THR A  62                    
SITE     2 AC2  6 GLU A  67  HOH A 239                                          
SITE     1 AC3  6 ASN B 122  ASP B 123  HOH B 601  HOH B 602                    
SITE     2 AC3  6 HOH B 604  HOH B 605                                          
SITE     1 AC4  1 ASN B 215                                                     
SITE     1 AC5  3 HIS B  55  LYS B  58  VAL B  82                               
SITE     1 AC6  3 GLN B 169  CYS B 180  HOH B 470                               
SITE     1 AC7  2 ARG B 170  HOH B 711                                          
SITE     1 AC8  5 ASN B 119  ARG B 212  GLU B 217  HOH B 445                    
SITE     2 AC8  5 HOH B 520                                                     
CRYST1   59.080   65.379   87.300  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016926  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015295  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011455        0.00000                         
ATOM      1  N   ILE A   9      34.010  16.098  14.077  1.00 62.65           N  
ANISOU    1  N   ILE A   9    10285   7902   5618    644    841  -1087       N  
ATOM      2  CA  ILE A   9      34.680  17.370  14.314  1.00 61.07           C  
ANISOU    2  CA  ILE A   9    10230   7603   5369    526    646  -1343       C  
ATOM      3  C   ILE A   9      34.833  18.160  13.014  1.00 58.22           C  
ANISOU    3  C   ILE A   9     9777   6984   5361    508    546  -1400       C  
ATOM      4  O   ILE A   9      34.799  17.597  11.914  1.00 59.30           O  
ANISOU    4  O   ILE A   9     9649   7108   5774    519    485  -1177       O  
ATOM      5  CB  ILE A   9      36.066  17.166  14.966  1.00 59.05           C  
ANISOU    5  CB  ILE A   9    10061   7550   4826    358    297  -1349       C  
ATOM      6  CG1 ILE A   9      37.163  17.030  13.907  1.00 56.77           C  
ANISOU    6  CG1 ILE A   9     9640   7206   4724    232    -14  -1272       C  
ATOM      7  CG2 ILE A   9      36.046  15.959  15.890  1.00 64.65           C  
ANISOU    7  CG2 ILE A   9    10808   8527   5229    404    339  -1135       C  
ATOM      8  CD1 ILE A   9      38.554  17.210  14.461  1.00 61.85           C  
ANISOU    8  CD1 ILE A   9    10299   7969   5230     55   -379  -1368       C  
ATOM      9  N   ALA A  10      34.996  19.470  13.153  1.00 52.65           N  
ANISOU    9  N   ALA A  10     9173   6093   4738    453    523  -1642       N  
ATOM     10  CA  ALA A  10      35.039  20.372  12.012  1.00 47.94           C  
ANISOU   10  CA  ALA A  10     8525   5197   4492    458    487  -1676       C  
ATOM     11  C   ALA A  10      36.347  20.260  11.246  1.00 39.93           C  
ANISOU   11  C   ALA A  10     7424   4174   3573    271    192  -1584       C  
ATOM     12  O   ALA A  10      36.365  20.398  10.026  1.00 38.59           O  
ANISOU   12  O   ALA A  10     7113   3852   3696    283    164  -1429       O  
ATOM     13  CB  ALA A  10      34.821  21.809  12.473  1.00 49.54           C  
ANISOU   13  CB  ALA A  10     8818   5193   4810    450    595  -1940       C  
ATOM     14  N   GLU A  11      37.442  20.032  11.965  1.00 41.11           N  
ANISOU   14  N   GLU A  11     7648   4485   3488    101    -30  -1677       N  
ATOM     15  CA  GLU A  11      38.745  19.880  11.327  1.00 44.72           C  
ANISOU   15  CA  GLU A  11     7964   4924   4102    -91   -292  -1607       C  
ATOM     16  C   GLU A  11      38.724  18.706  10.356  1.00 38.52           C  
ANISOU   16  C   GLU A  11     6924   4243   3470    -61   -301  -1262       C  
ATOM     17  O   GLU A  11      39.186  18.820   9.219  1.00 31.06           O  
ANISOU   17  O   GLU A  11     5854   3147   2800   -138   -336  -1156       O  
ATOM     18  CB  GLU A  11      39.848  19.679  12.369  1.00 55.99           C  
ANISOU   18  CB  GLU A  11     9422   6562   5291   -246   -565  -1740       C  
ATOM     19  CG  GLU A  11      41.150  19.119  11.804  1.00 69.14           C  
ANISOU   19  CG  GLU A  11    10890   8252   7127   -421   -838  -1628       C  
ATOM     20  CD  GLU A  11      42.124  18.688  12.887  1.00 84.50           C  
ANISOU   20  CD  GLU A  11    12795  10464   8848   -512  -1145  -1694       C  
ATOM     21  OE1 GLU A  11      41.731  17.874  13.750  1.00 90.14           O  
ANISOU   21  OE1 GLU A  11    13586  11450   9214   -392  -1150  -1570       O  
ATOM     22  OE2 GLU A  11      43.282  19.158  12.875  1.00 89.03           O  
ANISOU   22  OE2 GLU A  11    13229  10973   9624   -692  -1361  -1851       O  
ATOM     23  N   PHE A  12      38.181  17.580  10.806  1.00 31.98           N  
ANISOU   23  N   PHE A  12     6037   3653   2460     45   -232  -1097       N  
ATOM     24  CA  PHE A  12      38.121  16.390   9.954  1.00 28.89           C  
ANISOU   24  CA  PHE A  12     5393   3355   2230     62   -214   -808       C  
ATOM     25  C   PHE A  12      37.183  16.610   8.769  1.00 27.12           C  
ANISOU   25  C   PHE A  12     5068   2972   2264    174    -59   -727       C  
ATOM     26  O   PHE A  12      37.407  16.069   7.687  1.00 24.91           O  
ANISOU   26  O   PHE A  12     4617   2679   2169    129    -93   -563       O  
ATOM     27  CB  PHE A  12      37.679  15.156  10.755  1.00 29.00           C  
ANISOU   27  CB  PHE A  12     5371   3615   2032    156   -123   -654       C  
ATOM     28  CG  PHE A  12      38.749  14.593  11.647  1.00 30.52           C  
ANISOU   28  CG  PHE A  12     5608   3998   1991     63   -348   -612       C  
ATOM     29  CD1 PHE A  12      40.084  14.714  11.312  1.00 30.45           C  
ANISOU   29  CD1 PHE A  12     5495   3955   2120   -113   -626   -632       C  
ATOM     30  CD2 PHE A  12      38.419  13.951  12.828  1.00 32.85           C  
ANISOU   30  CD2 PHE A  12     6049   4494   1939    163   -277   -544       C  
ATOM     31  CE1 PHE A  12      41.070  14.202  12.131  1.00 36.23           C  
ANISOU   31  CE1 PHE A  12     6225   4865   2678   -176   -891   -591       C  
ATOM     32  CE2 PHE A  12      39.403  13.441  13.652  1.00 40.25           C  
ANISOU   32  CE2 PHE A  12     7046   5619   2629    110   -539   -473       C  
ATOM     33  CZ  PHE A  12      40.731  13.565  13.299  1.00 40.68           C  
ANISOU   33  CZ  PHE A  12     6952   5652   2854    -54   -876   -500       C  
ATOM     34  N   LYS A  13      36.137  17.405   8.962  1.00 28.53           N  
ANISOU   34  N   LYS A  13     5354   3029   2457    326    102   -850       N  
ATOM     35  CA  LYS A  13      35.207  17.664   7.873  1.00 33.94           C  
ANISOU   35  CA  LYS A  13     5932   3572   3390    467    187   -767       C  
ATOM     36  C   LYS A  13      35.872  18.546   6.805  1.00 27.37           C  
ANISOU   36  C   LYS A  13     5163   2509   2725    385     76   -750       C  
ATOM     37  O   LYS A  13      35.663  18.340   5.609  1.00 26.00           O  
ANISOU   37  O   LYS A  13     4893   2293   2693    424     44   -588       O  
ATOM     38  CB  LYS A  13      33.916  18.310   8.388  1.00 41.96           C  
ANISOU   38  CB  LYS A  13     7009   4485   4450    671    394   -900       C  
ATOM     39  CG  LYS A  13      32.711  18.174   7.434  1.00 53.10           C  
ANISOU   39  CG  LYS A  13     8213   5834   6130    865    453   -787       C  
ATOM     40  CD  LYS A  13      32.887  17.016   6.435  1.00 64.24           C  
ANISOU   40  CD  LYS A  13     9402   7399   7608    808    332   -582       C  
ATOM     41  CE  LYS A  13      31.556  16.447   5.928  1.00 68.01           C  
ANISOU   41  CE  LYS A  13     9616   7923   8304    987    400   -529       C  
ATOM     42  NZ  LYS A  13      30.627  17.489   5.405  1.00 70.71           N  
ANISOU   42  NZ  LYS A  13     9948   8060   8859   1195    379   -570       N  
ATOM     43  N   GLU A  14      36.685  19.510   7.231  1.00 29.12           N  
ANISOU   43  N   GLU A  14     5562   2579   2925    264     30   -923       N  
ATOM     44  CA  GLU A  14      37.451  20.327   6.289  1.00 29.35           C  
ANISOU   44  CA  GLU A  14     5661   2351   3141    157    -17   -903       C  
ATOM     45  C   GLU A  14      38.403  19.445   5.479  1.00 27.15           C  
ANISOU   45  C   GLU A  14     5241   2161   2914     -7   -116   -728       C  
ATOM     46  O   GLU A  14      38.517  19.592   4.260  1.00 26.48           O  
ANISOU   46  O   GLU A  14     5166   1935   2959    -14    -88   -581       O  
ATOM     47  CB  GLU A  14      38.226  21.430   7.027  1.00 37.22           C  
ANISOU   47  CB  GLU A  14     6828   3162   4153     18    -31  -1173       C  
ATOM     48  CG  GLU A  14      39.452  21.964   6.272  1.00 45.44           C  
ANISOU   48  CG  GLU A  14     7887   3971   5408   -186    -74  -1171       C  
ATOM     49  CD  GLU A  14      40.146  23.114   7.000  1.00 55.24           C  
ANISOU   49  CD  GLU A  14     9208   5033   6748   -327    -75  -1469       C  
ATOM     50  OE1 GLU A  14      39.438  24.012   7.506  1.00 58.00           O  
ANISOU   50  OE1 GLU A  14     9650   5276   7112   -210     41  -1616       O  
ATOM     51  OE2 GLU A  14      41.397  23.120   7.072  1.00 51.28           O  
ANISOU   51  OE2 GLU A  14     8584   4532   6367   -545   -187  -1552       O  
ATOM     52  N   ALA A  15      39.066  18.515   6.158  1.00 26.45           N  
ANISOU   52  N   ALA A  15     5035   2297   2716   -125   -216   -735       N  
ATOM     53  CA  ALA A  15      40.009  17.619   5.495  1.00 24.71           C  
ANISOU   53  CA  ALA A  15     4646   2143   2600   -282   -282   -588       C  
ATOM     54  C   ALA A  15      39.297  16.714   4.490  1.00 24.85           C  
ANISOU   54  C   ALA A  15     4538   2252   2652   -187   -203   -379       C  
ATOM     55  O   ALA A  15      39.810  16.457   3.401  1.00 21.51           O  
ANISOU   55  O   ALA A  15     4069   1753   2351   -285   -176   -269       O  
ATOM     56  CB  ALA A  15      40.765  16.785   6.531  1.00 24.99           C  
ANISOU   56  CB  ALA A  15     4566   2399   2530   -380   -428   -615       C  
ATOM     57  N   PHE A  16      38.117  16.230   4.866  1.00 22.07           N  
ANISOU   57  N   PHE A  16     4131   2053   2202     -9   -147   -351       N  
ATOM     58  CA  PHE A  16      37.309  15.381   3.992  1.00 20.52           C  
ANISOU   58  CA  PHE A  16     3782   1950   2065     83    -93   -212       C  
ATOM     59  C   PHE A  16      36.904  16.147   2.737  1.00 20.95           C  
ANISOU   59  C   PHE A  16     3943   1828   2190    159   -102   -162       C  
ATOM     60  O   PHE A  16      36.933  15.615   1.626  1.00 20.03           O  
ANISOU   60  O   PHE A  16     3769   1735   2106    126   -113    -54       O  
ATOM     61  CB  PHE A  16      36.071  14.884   4.744  1.00 20.78           C  
ANISOU   61  CB  PHE A  16     3718   2131   2048    260     -1   -236       C  
ATOM     62  CG  PHE A  16      35.234  13.897   3.974  1.00 21.74           C  
ANISOU   62  CG  PHE A  16     3620   2359   2282    333     45   -144       C  
ATOM     63  CD1 PHE A  16      35.512  12.542   4.030  1.00 18.28           C  
ANISOU   63  CD1 PHE A  16     2988   2074   1885    243     99    -59       C  
ATOM     64  CD2 PHE A  16      34.150  14.324   3.219  1.00 20.34           C  
ANISOU   64  CD2 PHE A  16     3412   2118   2199    498     23   -157       C  
ATOM     65  CE1 PHE A  16      34.744  11.625   3.338  1.00 18.43           C  
ANISOU   65  CE1 PHE A  16     2786   2173   2043    285    155    -27       C  
ATOM     66  CE2 PHE A  16      33.377  13.417   2.523  1.00 19.81           C  
ANISOU   66  CE2 PHE A  16     3117   2162   2250    552     22   -124       C  
ATOM     67  CZ  PHE A  16      33.675  12.059   2.580  1.00 19.90           C  
ANISOU   67  CZ  PHE A  16     2935   2319   2309    430    102    -79       C  
ATOM     68  N   SER A  17      36.544  17.415   2.920  1.00 22.81           N  
ANISOU   68  N   SER A  17     4358   1873   2437    267    -91   -240       N  
ATOM     69  CA  SER A  17      36.046  18.223   1.811  1.00 23.95           C  
ANISOU   69  CA  SER A  17     4631   1830   2638    395   -110   -150       C  
ATOM     70  C   SER A  17      37.144  18.544   0.802  1.00 25.52           C  
ANISOU   70  C   SER A  17     4982   1858   2855    229    -95    -52       C  
ATOM     71  O   SER A  17      36.853  18.895  -0.340  1.00 24.95           O  
ANISOU   71  O   SER A  17     5040   1678   2761    317   -112     88       O  
ATOM     72  CB  SER A  17      35.418  19.520   2.332  1.00 33.80           C  
ANISOU   72  CB  SER A  17     6023   2868   3951    562    -63   -249       C  
ATOM     73  OG  SER A  17      36.412  20.385   2.856  1.00 37.69           O  
ANISOU   73  OG  SER A  17     6682   3167   4471    409     -9   -374       O  
ATOM     74  N   LEU A  18      38.401  18.432   1.222  1.00 23.62           N  
ANISOU   74  N   LEU A  18     4729   1586   2659     -3    -60   -123       N  
ATOM     75  CA  LEU A  18      39.521  18.616   0.308  1.00 23.91           C  
ANISOU   75  CA  LEU A  18     4865   1443   2778   -192     19    -49       C  
ATOM     76  C   LEU A  18      39.474  17.542  -0.774  1.00 22.48           C  
ANISOU   76  C   LEU A  18     4607   1404   2530   -225     34     97       C  
ATOM     77  O   LEU A  18      39.874  17.776  -1.917  1.00 26.81           O  
ANISOU   77  O   LEU A  18     5324   1800   3062   -286    129    208       O  
ATOM     78  CB  LEU A  18      40.865  18.557   1.048  1.00 27.54           C  
ANISOU   78  CB  LEU A  18     5228   1860   3374   -436     26   -184       C  
ATOM     79  CG  LEU A  18      41.170  19.645   2.090  1.00 26.09           C  
ANISOU   79  CG  LEU A  18     5130   1521   3262   -471     -1   -395       C  
ATOM     80  CD1 LEU A  18      42.517  19.410   2.757  1.00 28.75           C  
ANISOU   80  CD1 LEU A  18     5314   1869   3739   -715    -75   -541       C  
ATOM     81  CD2 LEU A  18      41.138  21.021   1.447  1.00 28.38           C  
ANISOU   81  CD2 LEU A  18     5601   1513   3668   -420    132   -370       C  
ATOM     82  N   PHE A  19      38.964  16.373  -0.402  1.00 20.73           N  
ANISOU   82  N   PHE A  19     4153   1459   2265   -188    -29     84       N  
ATOM     83  CA  PHE A  19      38.922  15.222  -1.303  1.00 19.53           C  
ANISOU   83  CA  PHE A  19     3886   1451   2082   -245     -2    163       C  
ATOM     84  C   PHE A  19      37.582  15.081  -2.002  1.00 22.73           C  
ANISOU   84  C   PHE A  19     4301   1967   2369    -38   -100    209       C  
ATOM     85  O   PHE A  19      37.508  14.635  -3.145  1.00 22.21           O  
ANISOU   85  O   PHE A  19     4284   1942   2213    -65   -101    267       O  
ATOM     86  CB  PHE A  19      39.232  13.941  -0.530  1.00 23.16           C  
ANISOU   86  CB  PHE A  19     4057   2112   2630   -343     12    125       C  
ATOM     87  CG  PHE A  19      40.653  13.851  -0.069  1.00 17.73           C  
ANISOU   87  CG  PHE A  19     3305   1341   2091   -554     56     99       C  
ATOM     88  CD1 PHE A  19      41.070  14.513   1.080  1.00 19.47           C  
ANISOU   88  CD1 PHE A  19     3548   1517   2333   -567    -27      5       C  
ATOM     89  CD2 PHE A  19      41.579  13.113  -0.791  1.00 19.81           C  
ANISOU   89  CD2 PHE A  19     3472   1562   2492   -742    176    143       C  
ATOM     90  CE1 PHE A  19      42.384  14.433   1.502  1.00 19.15           C  
ANISOU   90  CE1 PHE A  19     3405   1410   2461   -756    -48    -42       C  
ATOM     91  CE2 PHE A  19      42.902  13.037  -0.382  1.00 17.70           C  
ANISOU   91  CE2 PHE A  19     3046   1239   2442   -887    193    109       C  
ATOM     92  CZ  PHE A  19      43.306  13.698   0.771  1.00 18.69           C  
ANISOU   92  CZ  PHE A  19     3205   1297   2600   -930     61     21       C  
ATOM     93  N   ASP A  20      36.518  15.444  -1.304  1.00 18.09           N  
ANISOU   93  N   ASP A  20     2782   1721   2372    227   -386     48       N  
ATOM     94  CA  ASP A  20      35.177  15.212  -1.813  1.00 18.31           C  
ANISOU   94  CA  ASP A  20     2753   1713   2490    380   -437     37       C  
ATOM     95  C   ASP A  20      34.774  16.322  -2.784  1.00 19.35           C  
ANISOU   95  C   ASP A  20     3014   1718   2621    487   -467     61       C  
ATOM     96  O   ASP A  20      33.980  17.194  -2.448  1.00 24.35           O  
ANISOU   96  O   ASP A  20     3690   2257   3306    578   -425     39       O  
ATOM     97  CB  ASP A  20      34.186  15.114  -0.652  1.00 18.63           C  
ANISOU   97  CB  ASP A  20     2706   1770   2601    418   -383    -22       C  
ATOM     98  CG  ASP A  20      32.788  14.787  -1.109  1.00 21.92           C  
ANISOU   98  CG  ASP A  20     3013   2183   3131    562   -435    -38       C  
ATOM     99  OD1 ASP A  20      32.630  14.294  -2.245  1.00 18.99           O  
ANISOU   99  OD1 ASP A  20     2604   1845   2768    604   -530    -12       O  
ATOM    100  OD2 ASP A  20      31.842  15.043  -0.339  1.00 24.77           O  
ANISOU  100  OD2 ASP A  20     3321   2522   3568    623   -377    -84       O  
ATOM    101  N   LYS A  21      35.313  16.255  -3.997  1.00 25.20           N  
ANISOU  101  N   LYS A  21     3818   2455   3302    491   -523    121       N  
ATOM    102  CA  LYS A  21      35.168  17.329  -4.974  1.00 28.12           C  
ANISOU  102  CA  LYS A  21     4338   2710   3637    590   -538    183       C  
ATOM    103  C   LYS A  21      33.719  17.644  -5.335  1.00 27.96           C  
ANISOU  103  C   LYS A  21     4266   2678   3681    788   -605    208       C  
ATOM    104  O   LYS A  21      33.354  18.818  -5.465  1.00 26.58           O  
ANISOU  104  O   LYS A  21     4205   2369   3527    902   -557    261       O  
ATOM    105  CB  LYS A  21      35.952  16.982  -6.239  1.00 27.46           C  
ANISOU  105  CB  LYS A  21     4317   2659   3457    557   -587    245       C  
ATOM    106  CG  LYS A  21      37.449  16.881  -6.011  1.00 23.71           C  
ANISOU  106  CG  LYS A  21     3891   2186   2932    381   -506    246       C  
ATOM    107  CD  LYS A  21      37.989  18.173  -5.393  1.00 27.44           C  
ANISOU  107  CD  LYS A  21     4500   2528   3399    303   -394    231       C  
ATOM    108  CE  LYS A  21      39.487  18.088  -5.158  1.00 23.56           C  
ANISOU  108  CE  LYS A  21     4016   2079   2856    107   -329    225       C  
ATOM    109  NZ  LYS A  21      39.985  19.279  -4.407  1.00 28.94           N  
ANISOU  109  NZ  LYS A  21     4807   2656   3531    -20   -216    165       N  
ATOM    110  N   ASP A  22      32.893  16.611  -5.497  1.00 26.57           N  
ANISOU  110  N   ASP A  22     3910   2639   3547    831   -702    174       N  
ATOM    111  CA  ASP A  22      31.511  16.829  -5.904  1.00 25.95           C  
ANISOU  111  CA  ASP A  22     3730   2602   3527   1012   -790    199       C  
ATOM    112  C   ASP A  22      30.563  16.949  -4.713  1.00 34.56           C  
ANISOU  112  C   ASP A  22     4702   3670   4759   1067   -719    140       C  
ATOM    113  O   ASP A  22      29.353  17.111  -4.885  1.00 36.73           O  
ANISOU  113  O   ASP A  22     4851   3990   5116   1222   -776    158       O  
ATOM    114  CB  ASP A  22      31.040  15.717  -6.846  1.00 28.54           C  
ANISOU  114  CB  ASP A  22     3916   3110   3819   1009   -938    171       C  
ATOM    115  CG  ASP A  22      31.145  14.341  -6.232  1.00 28.51           C  
ANISOU  115  CG  ASP A  22     3774   3183   3877    864   -904     61       C  
ATOM    116  OD1 ASP A  22      31.511  14.243  -5.045  1.00 21.39           O  
ANISOU  116  OD1 ASP A  22     2869   2224   3035    791   -787     32       O  
ATOM    117  OD2 ASP A  22      30.848  13.355  -6.937  1.00 32.55           O  
ANISOU  117  OD2 ASP A  22     4184   3813   4371    820   -985      5       O  
ATOM    118  N   GLY A  23      31.119  16.878  -3.508  1.00 33.45           N  
ANISOU  118  N   GLY A  23     4593   3479   4639    941   -594     73       N  
ATOM    119  CA  GLY A  23      30.345  17.073  -2.296  1.00 29.61           C  
ANISOU  119  CA  GLY A  23     4034   2958   4259    974   -491     11       C  
ATOM    120  C   GLY A  23      29.205  16.089  -2.093  1.00 30.92           C  
ANISOU  120  C   GLY A  23     3964   3248   4535   1021   -537    -35       C  
ATOM    121  O   GLY A  23      28.183  16.436  -1.493  1.00 33.08           O  
ANISOU  121  O   GLY A  23     4152   3495   4923   1125   -474    -60       O  
ATOM    122  N   ASP A  24      29.367  14.864  -2.585  1.00 23.23           N  
ANISOU  122  N   ASP A  24     2886   2398   3541    937   -622    -56       N  
ATOM    123  CA  ASP A  24      28.318  13.864  -2.436  1.00 24.66           C  
ANISOU  123  CA  ASP A  24     2843   2687   3838    944   -646   -120       C  
ATOM    124  C   ASP A  24      28.519  13.013  -1.183  1.00 23.38           C  
ANISOU  124  C   ASP A  24     2630   2531   3723    826   -512   -171       C  
ATOM    125  O   ASP A  24      27.838  12.008  -0.985  1.00 24.49           O  
ANISOU  125  O   ASP A  24     2602   2738   3965    794   -491   -225       O  
ATOM    126  CB  ASP A  24      28.228  12.982  -3.690  1.00 27.99           C  
ANISOU  126  CB  ASP A  24     3182   3229   4224    908   -787   -140       C  
ATOM    127  CG  ASP A  24      29.436  12.078  -3.878  1.00 28.57           C  
ANISOU  127  CG  ASP A  24     3336   3302   4218    751   -755   -149       C  
ATOM    128  OD1 ASP A  24      30.440  12.230  -3.154  1.00 30.03           O  
ANISOU  128  OD1 ASP A  24     3634   3417   4358    685   -656   -112       O  
ATOM    129  OD2 ASP A  24      29.384  11.217  -4.775  1.00 32.90           O  
ANISOU  129  OD2 ASP A  24     3827   3929   4746    692   -824   -196       O  
ATOM    130  N   GLY A  25      29.459  13.426  -0.338  1.00 23.74           N  
ANISOU  130  N   GLY A  25     2818   2516   3688    756   -415   -151       N  
ATOM    131  CA  GLY A  25      29.713  12.739   0.916  1.00 21.07           C  
ANISOU  131  CA  GLY A  25     2444   2210   3352    661   -293   -167       C  
ATOM    132  C   GLY A  25      30.540  11.472   0.778  1.00 19.48           C  
ANISOU  132  C   GLY A  25     2209   2073   3120    555   -291   -130       C  
ATOM    133  O   GLY A  25      30.642  10.684   1.724  1.00 21.30           O  
ANISOU  133  O   GLY A  25     2383   2342   3367    502   -187   -111       O  
ATOM    134  N   THR A  26      31.134  11.260  -0.396  1.00 19.37           N  
ANISOU  134  N   THR A  26     2234   2063   3061    536   -384   -105       N  
ATOM    135  CA  THR A  26      31.995  10.090  -0.595  1.00 19.48           C  
ANISOU  135  CA  THR A  26     2229   2111   3061    450   -350    -65       C  
ATOM    136  C   THR A  26      33.273  10.443  -1.351  1.00 21.04           C  
ANISOU  136  C   THR A  26     2554   2299   3140    409   -400     -8       C  
ATOM    137  O   THR A  26      33.281  11.349  -2.177  1.00 18.98           O  
ANISOU  137  O   THR A  26     2385   2003   2823    448   -486    -14       O  
ATOM    138  CB  THR A  26      31.289   8.970  -1.388  1.00 21.25           C  
ANISOU  138  CB  THR A  26     2333   2348   3392    438   -364   -129       C  
ATOM    139  OG1 THR A  26      31.227   9.332  -2.772  1.00 29.84           O  
ANISOU  139  OG1 THR A  26     3466   3447   4425    461   -498   -161       O  
ATOM    140  CG2 THR A  26      29.884   8.696  -0.848  1.00 20.60           C  
ANISOU  140  CG2 THR A  26     2099   2280   3449    471   -324   -203       C  
ATOM    141  N   ILE A  27      34.347   9.717  -1.077  1.00 18.05           N  
ANISOU  141  N   ILE A  27     2174   1952   2732    341   -333     64       N  
ATOM    142  CA  ILE A  27      35.591   9.872  -1.824  1.00 16.10           C  
ANISOU  142  CA  ILE A  27     2015   1704   2397    297   -357    120       C  
ATOM    143  C   ILE A  27      35.800   8.656  -2.727  1.00 16.06           C  
ANISOU  143  C   ILE A  27     1970   1682   2448    281   -321    119       C  
ATOM    144  O   ILE A  27      35.841   7.523  -2.244  1.00 16.09           O  
ANISOU  144  O   ILE A  27     1885   1690   2538    269   -213    152       O  
ATOM    145  CB  ILE A  27      36.814  10.021  -0.887  1.00 15.88           C  
ANISOU  145  CB  ILE A  27     1996   1749   2288    231   -304    213       C  
ATOM    146  CG1 ILE A  27      36.650  11.229   0.046  1.00 17.18           C  
ANISOU  146  CG1 ILE A  27     2221   1928   2379    207   -318    175       C  
ATOM    147  CG2 ILE A  27      38.110  10.114  -1.701  1.00 16.51           C  
ANISOU  147  CG2 ILE A  27     2135   1835   2305    182   -313    272       C  
ATOM    148  CD1 ILE A  27      37.614  11.217   1.226  1.00 16.50           C  
ANISOU  148  CD1 ILE A  27     2101   1973   2194    121   -275    242       C  
ATOM    149  N   THR A  28      35.949   8.904  -4.026  1.00 16.95           N  
ANISOU  149  N   THR A  28     2164   1767   2508    280   -388     85       N  
ATOM    150  CA  THR A  28      36.227   7.861  -5.014  1.00 18.47           C  
ANISOU  150  CA  THR A  28     2355   1936   2726    244   -340     56       C  
ATOM    151  C   THR A  28      37.716   7.774  -5.313  1.00 23.19           C  
ANISOU  151  C   THR A  28     3016   2525   3270    208   -270    151       C  
ATOM    152  O   THR A  28      38.486   8.620  -4.870  1.00 15.87           O  
ANISOU  152  O   THR A  28     2129   1627   2274    198   -288    227       O  
ATOM    153  CB  THR A  28      35.506   8.139  -6.343  1.00 20.66           C  
ANISOU  153  CB  THR A  28     2685   2223   2941    256   -457    -44       C  
ATOM    154  OG1 THR A  28      36.014   9.365  -6.891  1.00 17.30           O  
ANISOU  154  OG1 THR A  28     2394   1792   2385    286   -537     12       O  
ATOM    155  CG2 THR A  28      33.999   8.260  -6.132  1.00 18.67           C  
ANISOU  155  CG2 THR A  28     2330   2011   2751    300   -542   -131       C  
ATOM    156  N   THR A  29      38.124   6.776  -6.093  1.00 16.56           N  
ANISOU  156  N   THR A  29     2183   1644   2465    179   -176    133       N  
ATOM    157  CA  THR A  29      39.522   6.702  -6.511  1.00 16.54           C  
ANISOU  157  CA  THR A  29     2231   1630   2424    157    -94    223       C  
ATOM    158  C   THR A  29      39.911   7.927  -7.337  1.00 16.59           C  
ANISOU  158  C   THR A  29     2372   1644   2286    144   -193    222       C  
ATOM    159  O   THR A  29      41.018   8.430  -7.196  1.00 18.79           O  
ANISOU  159  O   THR A  29     2674   1941   2525    119   -161    315       O  
ATOM    160  CB  THR A  29      39.837   5.422  -7.325  1.00 18.15           C  
ANISOU  160  CB  THR A  29     2442   1757   2698    133     60    185       C  
ATOM    161  OG1 THR A  29      38.931   5.317  -8.429  1.00 19.75           O  
ANISOU  161  OG1 THR A  29     2716   1942   2847     94     -6     21       O  
ATOM    162  CG2 THR A  29      39.737   4.186  -6.451  1.00 17.87           C  
ANISOU  162  CG2 THR A  29     2286   1677   2827    156    219    232       C  
ATOM    163  N   LYS A  30      38.998   8.426  -8.171  1.00 17.05           N  
ANISOU  163  N   LYS A  30     2510   1699   2268    161   -309    130       N  
ATOM    164  CA  LYS A  30      39.316   9.576  -9.027  1.00 17.43           C  
ANISOU  164  CA  LYS A  30     2708   1738   2177    170   -383    156       C  
ATOM    165  C   LYS A  30      39.545  10.817  -8.175  1.00 17.43           C  
ANISOU  165  C   LYS A  30     2733   1730   2161    181   -421    225       C  
ATOM    166  O   LYS A  30      40.472  11.590  -8.427  1.00 17.21           O  
ANISOU  166  O   LYS A  30     2799   1673   2068    144   -390    286       O  
ATOM    167  CB  LYS A  30      38.210   9.836 -10.055  1.00 19.55           C  
ANISOU  167  CB  LYS A  30     3039   2037   2352    213   -512     75       C  
ATOM    168  CG  LYS A  30      38.536  10.985 -11.026  1.00 23.79           C  
ANISOU  168  CG  LYS A  30     3750   2558   2730    246   -569    136       C  
ATOM    169  CD  LYS A  30      38.076  10.678 -12.448  1.00 38.97           C  
ANISOU  169  CD  LYS A  30     5751   4546   4510    250   -636     71       C  
ATOM    170  CE  LYS A  30      36.588  10.901 -12.622  1.00 49.57           C  
ANISOU  170  CE  LYS A  30     7026   5987   5822    329   -810     19       C  
ATOM    171  NZ  LYS A  30      36.204  12.325 -12.404  1.00 62.13           N  
ANISOU  171  NZ  LYS A  30     8674   7550   7383    454   -895    132       N  
ATOM    172  N   GLU A  31      38.705  10.995  -7.156  1.00 19.76           N  
ANISOU  172  N   GLU A  31     2947   2042   2520    216   -465    200       N  
ATOM    173  CA  GLU A  31      38.838  12.127  -6.245  1.00 17.24           C  
ANISOU  173  CA  GLU A  31     2658   1705   2186    208   -475    230       C  
ATOM    174  C   GLU A  31      40.159  12.048  -5.494  1.00 16.86           C  
ANISOU  174  C   GLU A  31     2567   1704   2136    112   -392    295       C  
ATOM    175  O   GLU A  31      40.870  13.052  -5.367  1.00 16.67           O  
ANISOU  175  O   GLU A  31     2620   1659   2053     47   -377    317       O  
ATOM    176  CB  GLU A  31      37.656  12.177  -5.273  1.00 17.70           C  
ANISOU  176  CB  GLU A  31     2631   1777   2316    263   -509    180       C  
ATOM    177  CG  GLU A  31      36.406  12.804  -5.891  1.00 18.51           C  
ANISOU  177  CG  GLU A  31     2774   1846   2414    372   -606    139       C  
ATOM    178  CD  GLU A  31      35.150  12.515  -5.092  1.00 24.27           C  
ANISOU  178  CD  GLU A  31     3372   2604   3245    430   -623     81       C  
ATOM    179  OE1 GLU A  31      34.915  11.339  -4.753  1.00 32.36           O  
ANISOU  179  OE1 GLU A  31     4272   3678   4346    397   -586     46       O  
ATOM    180  OE2 GLU A  31      34.391  13.463  -4.825  1.00 23.14           O  
ANISOU  180  OE2 GLU A  31     3254   2419   3120    513   -651     74       O  
ATOM    181  N   LEU A  32      40.497  10.851  -5.017  1.00 15.96           N  
ANISOU  181  N   LEU A  32     2320   1656   2088    101   -328    332       N  
ATOM    182  CA  LEU A  32      41.768  10.642  -4.338  1.00 16.00           C  
ANISOU  182  CA  LEU A  32     2241   1752   2087     33   -261    426       C  
ATOM    183  C   LEU A  32      42.948  10.963  -5.257  1.00 17.15           C  
ANISOU  183  C   LEU A  32     2450   1880   2185    -23   -218    471       C  
ATOM    184  O   LEU A  32      43.873  11.666  -4.863  1.00 16.80           O  
ANISOU  184  O   LEU A  32     2395   1894   2093   -113   -210    507       O  
ATOM    185  CB  LEU A  32      41.876   9.194  -3.832  1.00 17.34           C  
ANISOU  185  CB  LEU A  32     2261   1976   2351     76   -177    496       C  
ATOM    186  CG  LEU A  32      43.208   8.848  -3.171  1.00 16.34           C  
ANISOU  186  CG  LEU A  32     2010   1978   2221     43   -113    637       C  
ATOM    187  CD1 LEU A  32      43.465   9.785  -1.984  1.00 16.65           C  
ANISOU  187  CD1 LEU A  32     2015   2150   2162    -36   -184    643       C  
ATOM    188  CD2 LEU A  32      43.221   7.385  -2.735  1.00 16.57           C  
ANISOU  188  CD2 LEU A  32     1908   2028   2362    126      0    738       C  
ATOM    189  N   GLY A  33      42.905  10.449  -6.486  1.00 16.49           N  
ANISOU  189  N   GLY A  33     2433   1724   2110     13   -182    453       N  
ATOM    190  CA  GLY A  33      43.990  10.648  -7.437  1.00 17.02           C  
ANISOU  190  CA  GLY A  33     2568   1765   2134    -34   -112    496       C  
ATOM    191  C   GLY A  33      44.134  12.121  -7.789  1.00 17.45           C  
ANISOU  191  C   GLY A  33     2772   1765   2093    -86   -157    479       C  
ATOM    192  O   GLY A  33      45.238  12.631  -8.007  1.00 18.02           O  
ANISOU  192  O   GLY A  33     2866   1842   2138   -170    -92    527       O  
ATOM    193  N   THR A  34      42.999  12.805  -7.836  1.00 17.43           N  
ANISOU  193  N   THR A  34     2866   1702   2055    -31   -250    419       N  
ATOM    194  CA  THR A  34      42.974  14.228  -8.152  1.00 18.14           C  
ANISOU  194  CA  THR A  34     3119   1700   2075    -49   -266    417       C  
ATOM    195  C   THR A  34      43.773  15.008  -7.113  1.00 18.42           C  
ANISOU  195  C   THR A  34     3119   1760   2120   -177   -224    419       C  
ATOM    196  O   THR A  34      44.618  15.834  -7.462  1.00 19.25           O  
ANISOU  196  O   THR A  34     3314   1810   2189   -271   -155    439       O  
ATOM    197  CB  THR A  34      41.530  14.772  -8.214  1.00 18.35           C  
ANISOU  197  CB  THR A  34     3218   1665   2090     66   -363    375       C  
ATOM    198  OG1 THR A  34      40.840  14.186  -9.330  1.00 18.61           O  
ANISOU  198  OG1 THR A  34     3284   1709   2077    158   -422    364       O  
ATOM    199  CG2 THR A  34      41.519  16.292  -8.359  1.00 19.39           C  
ANISOU  199  CG2 THR A  34     3521   1668   2178     66   -340    396       C  
ATOM    200  N   VAL A  35      43.506  14.735  -5.840  1.00 17.98           N  
ANISOU  200  N   VAL A  35     2933   1795   2102   -195   -256    390       N  
ATOM    201  CA  VAL A  35      44.202  15.443  -4.769  1.00 18.57           C  
ANISOU  201  CA  VAL A  35     2966   1936   2153   -341   -232    365       C  
ATOM    202  C   VAL A  35      45.684  15.110  -4.802  1.00 19.02           C  
ANISOU  202  C   VAL A  35     2906   2116   2204   -457   -175    433       C  
ATOM    203  O   VAL A  35      46.530  16.011  -4.738  1.00 22.53           O  
ANISOU  203  O   VAL A  35     3387   2559   2615   -607   -128    409       O  
ATOM    204  CB  VAL A  35      43.614  15.106  -3.379  1.00 18.24           C  
ANISOU  204  CB  VAL A  35     2806   2003   2120   -334   -277    328       C  
ATOM    205  CG1 VAL A  35      44.481  15.724  -2.268  1.00 20.27           C  
ANISOU  205  CG1 VAL A  35     3003   2388   2311   -517   -261    291       C  
ATOM    206  CG2 VAL A  35      42.181  15.624  -3.285  1.00 19.24           C  
ANISOU  206  CG2 VAL A  35     3038   2002   2269   -229   -310    255       C  
ATOM    207  N   MET A  36      45.998  13.825  -4.952  1.00 18.50           N  
ANISOU  207  N   MET A  36     2699   2143   2187   -388   -160    516       N  
ATOM    208  CA  MET A  36      47.389  13.386  -4.916  1.00 22.33           C  
ANISOU  208  CA  MET A  36     3029   2764   2690   -462    -98    608       C  
ATOM    209  C   MET A  36      48.202  13.965  -6.065  1.00 25.23           C  
ANISOU  209  C   MET A  36     3503   3038   3046   -530    -12    618       C  
ATOM    210  O   MET A  36      49.342  14.368  -5.871  1.00 24.23           O  
ANISOU  210  O   MET A  36     3287   3006   2913   -668     33    644       O  
ATOM    211  CB  MET A  36      47.463  11.867  -4.914  1.00 18.72           C  
ANISOU  211  CB  MET A  36     2423   2376   2315   -339    -57    709       C  
ATOM    212  CG  MET A  36      47.010  11.306  -3.571  1.00 23.23           C  
ANISOU  212  CG  MET A  36     2852   3081   2893   -298   -113    741       C  
ATOM    213  SD  MET A  36      47.007   9.520  -3.558  1.00 29.67           S  
ANISOU  213  SD  MET A  36     3521   3921   3832   -137    -19    874       S  
ATOM    214  CE  MET A  36      48.768   9.195  -3.440  1.00 25.77           C  
ANISOU  214  CE  MET A  36     2814   3613   3365   -172     58   1047       C  
ATOM    215  N   ARG A  37      47.608  14.029  -7.249  1.00 19.58           N  
ANISOU  215  N   ARG A  37     2970   2153   2314   -443     10    596       N  
ATOM    216  CA  ARG A  37      48.273  14.673  -8.377  1.00 20.46           C  
ANISOU  216  CA  ARG A  37     3224   2161   2391   -499    104    612       C  
ATOM    217  C   ARG A  37      48.434  16.175  -8.129  1.00 29.84           C  
ANISOU  217  C   ARG A  37     4533   3268   3537   -632    118    558       C  
ATOM    218  O   ARG A  37      49.442  16.766  -8.523  1.00 29.36           O  
ANISOU  218  O   ARG A  37     4500   3183   3474   -759    221    576       O  
ATOM    219  CB  ARG A  37      47.503  14.413  -9.679  1.00 20.24           C  
ANISOU  219  CB  ARG A  37     3375   2002   2313   -372    108    604       C  
ATOM    220  CG  ARG A  37      47.629  12.971 -10.155  1.00 19.88           C  
ANISOU  220  CG  ARG A  37     3240   2002   2311   -293    161    632       C  
ATOM    221  CD  ARG A  37      46.991  12.751 -11.526  1.00 20.18           C  
ANISOU  221  CD  ARG A  37     3462   1944   2261   -212    169    596       C  
ATOM    222  NE  ARG A  37      45.532  12.801 -11.482  1.00 21.54           N  
ANISOU  222  NE  ARG A  37     3695   2096   2392   -121     26    529       N  
ATOM    223  CZ  ARG A  37      44.742  11.769 -11.195  1.00 19.01           C  
ANISOU  223  CZ  ARG A  37     3279   1818   2127    -59    -21    475       C  
ATOM    224  NH1 ARG A  37      45.261  10.573 -10.916  1.00 18.79           N  
ANISOU  224  NH1 ARG A  37     3110   1830   2200    -64     78    490       N  
ATOM    225  NH2 ARG A  37      43.426  11.935 -11.188  1.00 18.85           N  
ANISOU  225  NH2 ARG A  37     3296   1794   2073     13   -152    412       N  
ATOM    226  N   SER A  38      47.462  16.794  -7.459  1.00 21.24           N  
ANISOU  226  N   SER A  38     3517   2125   2431   -610     42    486       N  
ATOM    227  CA  SER A  38      47.553  18.236  -7.184  1.00 22.39           C  
ANISOU  227  CA  SER A  38     3802   2151   2555   -737     94    419       C  
ATOM    228  C   SER A  38      48.683  18.523  -6.197  1.00 31.27           C  
ANISOU  228  C   SER A  38     4767   3429   3685   -964    125    371       C  
ATOM    229  O   SER A  38      49.153  19.661  -6.092  1.00 30.23           O  
ANISOU  229  O   SER A  38     4732   3209   3546  -1136    214    301       O  
ATOM    230  CB  SER A  38      46.235  18.789  -6.633  1.00 30.23           C  
ANISOU  230  CB  SER A  38     4899   3042   3545   -648     33    350       C  
ATOM    231  OG  SER A  38      46.076  18.481  -5.251  1.00 26.50           O  
ANISOU  231  OG  SER A  38     4269   2722   3079   -705    -32    285       O  
ATOM    232  N   LEU A  39      49.112  17.489  -5.476  1.00 29.16           N  
ANISOU  232  N   LEU A  39     3974   3609   3496   -540   -352   1054       N  
ATOM    233  CA  LEU A  39      50.197  17.611  -4.507  1.00 30.10           C  
ANISOU  233  CA  LEU A  39     3905   3840   3693   -606   -415   1231       C  
ATOM    234  C   LEU A  39      51.498  17.007  -5.033  1.00 31.78           C  
ANISOU  234  C   LEU A  39     3948   4099   4028   -572   -243   1408       C  
ATOM    235  O   LEU A  39      52.381  16.641  -4.254  1.00 35.08           O  
ANISOU  235  O   LEU A  39     4180   4597   4553   -562   -273   1537       O  
ATOM    236  CB  LEU A  39      49.812  16.942  -3.187  1.00 31.28           C  
ANISOU  236  CB  LEU A  39     4011   4040   3833   -591   -474   1209       C  
ATOM    237  CG  LEU A  39      48.616  17.571  -2.464  1.00 34.27           C  
ANISOU  237  CG  LEU A  39     4501   4412   4107   -668   -630    989       C  
ATOM    238  CD1 LEU A  39      48.223  16.726  -1.257  1.00 38.41           C  
ANISOU  238  CD1 LEU A  39     5023   4990   4583   -699   -629    958       C  
ATOM    239  CD2 LEU A  39      48.914  19.014  -2.056  1.00 32.08           C  
ANISOU  239  CD2 LEU A  39     4198   4165   3824   -796   -840    990       C  
ATOM    240  N   GLY A  40      51.598  16.881  -6.352  1.00 31.81           N  
ANISOU  240  N   GLY A  40     4013   4050   4022   -557    -74   1388       N  
ATOM    241  CA  GLY A  40      52.827  16.440  -6.991  1.00 33.45           C  
ANISOU  241  CA  GLY A  40     4044   4315   4351   -559    114   1493       C  
ATOM    242  C   GLY A  40      53.067  14.941  -7.044  1.00 37.29           C  
ANISOU  242  C   GLY A  40     4390   4807   4970   -392    281   1512       C  
ATOM    243  O   GLY A  40      54.125  14.501  -7.495  1.00 39.67           O  
ANISOU  243  O   GLY A  40     4494   5162   5417   -376    427   1560       O  
ATOM    244  N   GLN A  41      52.101  14.147  -6.589  1.00 36.39           N  
ANISOU  244  N   GLN A  41     4374   4638   4816   -277    260   1453       N  
ATOM    245  CA  GLN A  41      52.240  12.689  -6.625  1.00 38.72           C  
ANISOU  245  CA  GLN A  41     4580   4906   5226   -118    396   1472       C  
ATOM    246  C   GLN A  41      51.607  12.123  -7.897  1.00 40.76           C  
ANISOU  246  C   GLN A  41     4956   5094   5437    -50    615   1358       C  
ATOM    247  O   GLN A  41      50.851  12.809  -8.580  1.00 36.25           O  
ANISOU  247  O   GLN A  41     4573   4479   4722   -114    619   1256       O  
ATOM    248  CB  GLN A  41      51.605  12.046  -5.385  1.00 40.85           C  
ANISOU  248  CB  GLN A  41     4918   5146   5457    -67    265   1481       C  
ATOM    249  CG  GLN A  41      51.652  12.907  -4.129  1.00 45.06           C  
ANISOU  249  CG  GLN A  41     5454   5738   5929   -189     23   1531       C  
ATOM    250  CD  GLN A  41      53.058  13.092  -3.588  1.00 52.67           C  
ANISOU  250  CD  GLN A  41     6190   6775   7048   -204    -83   1693       C  
ATOM    251  OE1 GLN A  41      53.773  12.119  -3.350  1.00 56.70           O  
ANISOU  251  OE1 GLN A  41     6567   7265   7710    -89    -81   1782       O  
ATOM    252  NE2 GLN A  41      53.464  14.345  -3.398  1.00 48.48           N  
ANISOU  252  NE2 GLN A  41     5610   6317   6494   -338   -195   1717       N  
ATOM    253  N   ASN A  42      51.912  10.874  -8.224  1.00 33.13           N  
ANISOU  253  N   ASN A  42     3887   4103   4599     86    776   1366       N  
ATOM    254  CA  ASN A  42      51.324  10.270  -9.414  1.00 32.60           C  
ANISOU  254  CA  ASN A  42     3923   3975   4490    150    995   1253       C  
ATOM    255  C   ASN A  42      50.960   8.803  -9.209  1.00 34.77           C  
ANISOU  255  C   ASN A  42     4190   4181   4840    317   1081   1232       C  
ATOM    256  O   ASN A  42      51.594   7.915  -9.779  1.00 36.48           O  
ANISOU  256  O   ASN A  42     4260   4387   5215    417   1244   1235       O  
ATOM    257  CB  ASN A  42      52.274  10.408 -10.611  1.00 43.87           C  
ANISOU  257  CB  ASN A  42     5226   5450   5992     91   1195   1247       C  
ATOM    258  CG  ASN A  42      51.600  10.072 -11.933  1.00 50.79           C  
ANISOU  258  CG  ASN A  42     6264   6267   6767    103   1404   1125       C  
ATOM    259  OD1 ASN A  42      50.403  10.307 -12.111  1.00 48.01           O  
ANISOU  259  OD1 ASN A  42     6154   5841   6247    107   1346   1038       O  
ATOM    260  ND2 ASN A  42      52.367   9.516 -12.866  1.00 56.19           N  
ANISOU  260  ND2 ASN A  42     6802   6986   7561    105   1643   1092       N  
ATOM    261  N   PRO A  43      49.922   8.545  -8.397  1.00 31.19           N  
ANISOU  261  N   PRO A  43     3899   3677   4274    332    978   1187       N  
ATOM    262  CA  PRO A  43      49.526   7.170  -8.088  1.00 33.86           C  
ANISOU  262  CA  PRO A  43     4280   3934   4651    453   1045   1174       C  
ATOM    263  C   PRO A  43      48.881   6.477  -9.279  1.00 33.36           C  
ANISOU  263  C   PRO A  43     4295   3814   4565    537   1281   1038       C  
ATOM    264  O   PRO A  43      48.234   7.126 -10.098  1.00 29.54           O  
ANISOU  264  O   PRO A  43     3925   3337   3961    486   1340    917       O  
ATOM    265  CB  PRO A  43      48.508   7.347  -6.960  1.00 30.13           C  
ANISOU  265  CB  PRO A  43     3989   3450   4011    365    893   1120       C  
ATOM    266  CG  PRO A  43      47.901   8.694  -7.236  1.00 28.87           C  
ANISOU  266  CG  PRO A  43     3911   3340   3720    252    825   1001       C  
ATOM    267  CD  PRO A  43      49.019   9.535  -7.782  1.00 29.80           C  
ANISOU  267  CD  PRO A  43     3882   3515   3924    215    808   1110       C  
ATOM    268  N  ATHR A  44      49.063   5.167  -9.386  0.11 32.45           N  
ANISOU  268  N  ATHR A  44     4131   3629   4570    669   1394   1055       N  
ATOM    269  N  BTHR A  44      49.067   5.162  -9.360  0.89 33.57           N  
ANISOU  269  N  BTHR A  44     4273   3771   4712    669   1391   1058       N  
ATOM    270  CA ATHR A  44      48.397   4.413 -10.438  0.11 30.82           C  
ANISOU  270  CA ATHR A  44     4001   3367   4340    751   1623    919       C  
ATOM    271  CA BTHR A  44      48.407   4.340 -10.368  0.89 30.87           C  
ANISOU  271  CA BTHR A  44     4007   3369   4353    756   1618    925       C  
ATOM    272  C  ATHR A  44      47.009   4.007  -9.954  0.11 30.12           C  
ANISOU  272  C  ATHR A  44     4139   3219   4088    734   1613    797       C  
ATOM    273  C  BTHR A  44      46.980   4.023  -9.936  0.89 31.78           C  
ANISOU  273  C  BTHR A  44     4353   3429   4293    731   1610    794       C  
ATOM    274  O  ATHR A  44      46.714   4.084  -8.759  0.11 29.25           O  
ANISOU  274  O  ATHR A  44     4109   3103   3901    659   1452    831       O  
ATOM    275  O  BTHR A  44      46.630   4.157  -8.754  0.89 29.12           O  
ANISOU  275  O  BTHR A  44     4103   3090   3870    650   1448    819       O  
ATOM    276  CB ATHR A  44      49.203   3.167 -10.858  0.11 32.53           C  
ANISOU  276  CB ATHR A  44     4051   3528   4779    904   1763    959       C  
ATOM    277  CB BTHR A  44      49.160   3.020 -10.603  0.89 32.58           C  
ANISOU  277  CB BTHR A  44     4073   3517   4788    913   1730    976       C  
ATOM    278  OG1ATHR A  44      48.702   2.664 -12.104  0.11 32.02           O  
ANISOU  278  OG1ATHR A  44     4034   3440   4693    957   2011    818       O  
ATOM    279  OG1BTHR A  44      48.968   2.164  -9.474  0.89 33.06           O  
ANISOU  279  OG1BTHR A  44     4221   3480   4862    958   1597   1051       O  
ATOM    280  CG2ATHR A  44      49.107   2.084  -9.804  0.11 33.24           C  
ANISOU  280  CG2ATHR A  44     4200   3506   4922    984   1651   1036       C  
ATOM    281  CG2BTHR A  44      50.646   3.275 -10.783  0.89 34.60           C  
ANISOU  281  CG2BTHR A  44     4048   3839   5261    933   1712   1065       C  
ATOM    282  N   GLU A  45      46.159   3.591 -10.886  1.00 25.91           N  
ANISOU  282  N   GLU A  45     5018   1712   3114    412    546    592       N  
ATOM    283  CA  GLU A  45      44.790   3.197 -10.571  1.00 26.05           C  
ANISOU  283  CA  GLU A  45     5054   1842   3003    315    246    542       C  
ATOM    284  C   GLU A  45      44.741   2.074  -9.531  1.00 27.12           C  
ANISOU  284  C   GLU A  45     5111   1961   3231    290    196    417       C  
ATOM    285  O   GLU A  45      43.960   2.131  -8.579  1.00 26.10           O  
ANISOU  285  O   GLU A  45     4796   1925   3195    241    -13    391       O  
ATOM    286  CB  GLU A  45      44.053   2.773 -11.845  1.00 32.03           C  
ANISOU  286  CB  GLU A  45     6143   2668   3360    202    170    543       C  
ATOM    287  CG  GLU A  45      42.644   2.232 -11.622  1.00 41.37           C  
ANISOU  287  CG  GLU A  45     7315   4032   4370     33   -143    486       C  
ATOM    288  CD  GLU A  45      41.688   3.253 -11.024  1.00 53.43           C  
ANISOU  288  CD  GLU A  45     8527   5732   6040     89   -384    623       C  
ATOM    289  OE1 GLU A  45      41.986   4.467 -11.076  1.00 52.69           O  
ANISOU  289  OE1 GLU A  45     8326   5593   6101    245   -304    776       O  
ATOM    290  OE2 GLU A  45      40.630   2.836 -10.500  1.00 55.55           O  
ANISOU  290  OE2 GLU A  45     8671   6162   6273    -24   -613    581       O  
ATOM    291  N   ALA A  46      45.586   1.061  -9.705  1.00 25.84           N  
ANISOU  291  N   ALA A  46     5104   1665   3048    353    430    363       N  
ATOM    292  CA  ALA A  46      45.642  -0.044  -8.755  1.00 27.29           C  
ANISOU  292  CA  ALA A  46     5254   1793   3321    384    443    299       C  
ATOM    293  C   ALA A  46      46.074   0.445  -7.363  1.00 23.76           C  
ANISOU  293  C   ALA A  46     4395   1461   3174    467    360    359       C  
ATOM    294  O   ALA A  46      45.527   0.006  -6.342  1.00 23.19           O  
ANISOU  294  O   ALA A  46     4222   1437   3152    428    208    325       O  
ATOM    295  CB  ALA A  46      46.578  -1.125  -9.264  1.00 31.14           C  
ANISOU  295  CB  ALA A  46     5977   2098   3756    509    785    280       C  
ATOM    296  N   GLU A  47      47.046   1.351  -7.324  1.00 22.63           N  
ANISOU  296  N   GLU A  47     4027   1374   3196    538    467    439       N  
ATOM    297  CA  GLU A  47      47.475   1.956  -6.065  1.00 22.60           C  
ANISOU  297  CA  GLU A  47     3645   1525   3417    526    377    466       C  
ATOM    298  C   GLU A  47      46.322   2.702  -5.385  1.00 21.47           C  
ANISOU  298  C   GLU A  47     3423   1444   3289    386    127    401       C  
ATOM    299  O   GLU A  47      46.098   2.543  -4.183  1.00 19.29           O  
ANISOU  299  O   GLU A  47     2975   1268   3088    348     -3    366       O  
ATOM    300  CB  GLU A  47      48.655   2.907  -6.295  1.00 25.75           C  
ANISOU  300  CB  GLU A  47     3844   1983   3957    526    548    533       C  
ATOM    301  CG  GLU A  47      50.015   2.205  -6.350  1.00 27.91           C  
ANISOU  301  CG  GLU A  47     3971   2317   4317    696    785    639       C  
ATOM    302  CD  GLU A  47      51.153   3.127  -6.772  1.00 37.86           C  
ANISOU  302  CD  GLU A  47     5027   3659   5699    652    983    706       C  
ATOM    303  OE1 GLU A  47      50.882   4.261  -7.222  1.00 34.06           O  
ANISOU  303  OE1 GLU A  47     4626   3106   5210    496    984    664       O  
ATOM    304  OE2 GLU A  47      52.328   2.712  -6.657  1.00 42.86           O  
ANISOU  304  OE2 GLU A  47     5409   4433   6442    783   1163    825       O  
ATOM    305  N   LEU A  48      45.596   3.511  -6.150  1.00 19.97           N  
ANISOU  305  N   LEU A  48     3362   1206   3022    338     83    412       N  
ATOM    306  CA  LEU A  48      44.434   4.231  -5.623  1.00 19.07           C  
ANISOU  306  CA  LEU A  48     3173   1136   2935    274    -98    395       C  
ATOM    307  C   LEU A  48      43.390   3.275  -5.043  1.00 18.88           C  
ANISOU  307  C   LEU A  48     3161   1186   2827    226   -285    335       C  
ATOM    308  O   LEU A  48      42.856   3.503  -3.962  1.00 17.31           O  
ANISOU  308  O   LEU A  48     2802   1053   2723    183   -388    292       O  
ATOM    309  CB  LEU A  48      43.802   5.094  -6.720  1.00 20.16           C  
ANISOU  309  CB  LEU A  48     3453   1233   2973    306    -98    497       C  
ATOM    310  CG  LEU A  48      44.677   6.262  -7.165  1.00 21.24           C  
ANISOU  310  CG  LEU A  48     3597   1255   3219    331    116    568       C  
ATOM    311  CD1 LEU A  48      44.128   6.970  -8.413  1.00 22.94           C  
ANISOU  311  CD1 LEU A  48     4007   1423   3287    411    143    732       C  
ATOM    312  CD2 LEU A  48      44.811   7.231  -5.997  1.00 20.83           C  
ANISOU  312  CD2 LEU A  48     3354   1166   3394    258    156    505       C  
ATOM    313  N   GLN A  49      43.094   2.202  -5.769  1.00 19.09           N  
ANISOU  313  N   GLN A  49     3409   1186   2659    198   -297    315       N  
ATOM    314  CA  GLN A  49      42.087   1.257  -5.300  1.00 18.77           C  
ANISOU  314  CA  GLN A  49     3410   1198   2524     87   -444    245       C  
ATOM    315  C   GLN A  49      42.523   0.553  -4.008  1.00 17.89           C  
ANISOU  315  C   GLN A  49     3191   1066   2539    117   -411    210       C  
ATOM    316  O   GLN A  49      41.713   0.369  -3.108  1.00 19.07           O  
ANISOU  316  O   GLN A  49     3241   1292   2712     38   -538    174       O  
ATOM    317  CB  GLN A  49      41.766   0.223  -6.384  1.00 22.91           C  
ANISOU  317  CB  GLN A  49     4259   1666   2780    -27   -418    190       C  
ATOM    318  CG  GLN A  49      40.513  -0.596  -6.085  1.00 33.39           C  
ANISOU  318  CG  GLN A  49     5634   3079   3974   -239   -584    107       C  
ATOM    319  CD  GLN A  49      39.253   0.251  -6.018  1.00 35.24           C  
ANISOU  319  CD  GLN A  49     5629   3563   4196   -306   -828    175       C  
ATOM    320  OE1 GLN A  49      38.836   0.846  -7.013  1.00 43.77           O  
ANISOU  320  OE1 GLN A  49     6723   4779   5128   -319   -920    262       O  
ATOM    321  NE2 GLN A  49      38.640   0.307  -4.845  1.00 26.54           N  
ANISOU  321  NE2 GLN A  49     4301   2539   3242   -323   -915    165       N  
ATOM    322  N   ASP A  50      43.798   0.169  -3.927  1.00 18.35           N  
ANISOU  322  N   ASP A  50     3250   1053   2670    248   -233    253       N  
ATOM    323  CA  ASP A  50      44.369  -0.397  -2.706  1.00 18.18           C  
ANISOU  323  CA  ASP A  50     3076   1078   2755    327   -211    294       C  
ATOM    324  C   ASP A  50      44.191   0.540  -1.509  1.00 17.00           C  
ANISOU  324  C   ASP A  50     2636   1104   2719    255   -359    275       C  
ATOM    325  O   ASP A  50      43.860   0.095  -0.399  1.00 16.68           O  
ANISOU  325  O   ASP A  50     2520   1137   2678    224   -441    270       O  
ATOM    326  CB  ASP A  50      45.865  -0.686  -2.873  1.00 19.57           C  
ANISOU  326  CB  ASP A  50     3184   1239   3011    522     -1    408       C  
ATOM    327  CG  ASP A  50      46.139  -1.935  -3.676  1.00 29.45           C  
ANISOU  327  CG  ASP A  50     4760   2265   4165    645    231    434       C  
ATOM    328  OD1 ASP A  50      45.208  -2.743  -3.863  1.00 27.64           O  
ANISOU  328  OD1 ASP A  50     4775   1935   3792    516    205    334       O  
ATOM    329  OD2 ASP A  50      47.299  -2.112  -4.104  1.00 27.82           O  
ANISOU  329  OD2 ASP A  50     4507   2045   4017    825    452    530       O  
ATOM    330  N   MET A  51      44.441   1.827  -1.736  1.00 16.80           N  
ANISOU  330  N   MET A  51     2493   1118   2774    214   -351    258       N  
ATOM    331  CA  MET A  51      44.360   2.814  -0.667  1.00 16.37           C  
ANISOU  331  CA  MET A  51     2235   1175   2812    107   -420    198       C  
ATOM    332  C   MET A  51      42.932   2.915  -0.143  1.00 18.91           C  
ANISOU  332  C   MET A  51     2584   1498   3104     38   -539    134       C  
ATOM    333  O   MET A  51      42.702   2.932   1.069  1.00 15.35           O  
ANISOU  333  O   MET A  51     2025   1143   2663    -35   -596     81       O  
ATOM    334  CB  MET A  51      44.850   4.185  -1.156  1.00 16.97           C  
ANISOU  334  CB  MET A  51     2267   1202   2978     55   -314    181       C  
ATOM    335  CG  MET A  51      46.320   4.196  -1.562  1.00 18.23           C  
ANISOU  335  CG  MET A  51     2327   1412   3187     82   -177    245       C  
ATOM    336  SD  MET A  51      46.830   5.752  -2.350  1.00 24.23           S  
ANISOU  336  SD  MET A  51     3111   2053   4043    -19      4    231       S  
ATOM    337  CE  MET A  51      46.607   6.848  -0.968  1.00 19.76           C  
ANISOU  337  CE  MET A  51     2422   1536   3550   -260    -31     74       C  
ATOM    338  N   ILE A  52      41.975   2.983  -1.063  1.00 15.57           N  
ANISOU  338  N   ILE A  52     2283   1008   2623     55   -574    154       N  
ATOM    339  CA  ILE A  52      40.572   3.052  -0.691  1.00 15.42           C  
ANISOU  339  CA  ILE A  52     2226   1046   2586      7   -680    134       C  
ATOM    340  C   ILE A  52      40.129   1.747  -0.015  1.00 15.19           C  
ANISOU  340  C   ILE A  52     2229   1068   2475    -69   -752    101       C  
ATOM    341  O   ILE A  52      39.476   1.781   1.034  1.00 19.57           O  
ANISOU  341  O   ILE A  52     2681   1697   3059   -128   -791     61       O  
ATOM    342  CB  ILE A  52      39.680   3.332  -1.918  1.00 16.30           C  
ANISOU  342  CB  ILE A  52     2404   1174   2617     38   -738    216       C  
ATOM    343  CG1 ILE A  52      40.009   4.703  -2.516  1.00 24.83           C  
ANISOU  343  CG1 ILE A  52     3481   2169   3785    146   -630    292       C  
ATOM    344  CG2 ILE A  52      38.215   3.263  -1.542  1.00 18.66           C  
ANISOU  344  CG2 ILE A  52     2581   1611   2897     -9   -857    232       C  
ATOM    345  CD1 ILE A  52      39.606   5.850  -1.639  1.00 26.73           C  
ANISOU  345  CD1 ILE A  52     3601   2366   4190    184   -545    275       C  
ATOM    346  N   ASN A  53      40.504   0.608  -0.596  1.00 16.76           N  
ANISOU  346  N   ASN A  53     2607   1192   2570    -68   -721    118       N  
ATOM    347  CA  ASN A  53      40.057  -0.683  -0.075  1.00 17.34           C  
ANISOU  347  CA  ASN A  53     2789   1238   2561   -152   -731     96       C  
ATOM    348  C   ASN A  53      40.414  -0.851   1.398  1.00 15.98           C  
ANISOU  348  C   ASN A  53     2493   1128   2450   -121   -722    115       C  
ATOM    349  O   ASN A  53      39.628  -1.380   2.178  1.00 16.68           O  
ANISOU  349  O   ASN A  53     2586   1251   2502   -218   -757     95       O  
ATOM    350  CB  ASN A  53      40.661  -1.844  -0.876  1.00 17.21           C  
ANISOU  350  CB  ASN A  53     3054   1043   2441   -122   -598    109       C  
ATOM    351  CG  ASN A  53      40.083  -1.964  -2.284  1.00 20.52           C  
ANISOU  351  CG  ASN A  53     3672   1428   2698   -249   -621     54       C  
ATOM    352  OD1 ASN A  53      39.033  -1.391  -2.605  1.00 20.38           O  
ANISOU  352  OD1 ASN A  53     3546   1569   2628   -370   -781     40       O  
ATOM    353  ND2 ASN A  53      40.767  -2.733  -3.130  1.00 20.25           N  
ANISOU  353  ND2 ASN A  53     3926   1206   2564   -215   -447     39       N  
ATOM    354  N   GLU A  54      41.608  -0.403   1.770  1.00 15.56           N  
ANISOU  354  N   GLU A  54     2319   1128   2466    -13   -679    163       N  
ATOM    355  CA  GLU A  54      42.102  -0.618   3.124  1.00 15.92           C  
ANISOU  355  CA  GLU A  54     2236   1307   2505      4   -700    211       C  
ATOM    356  C   GLU A  54      41.157  -0.098   4.207  1.00 21.72           C  
ANISOU  356  C   GLU A  54     2878   2148   3226   -138   -774    120       C  
ATOM    357  O   GLU A  54      40.987  -0.730   5.252  1.00 17.47           O  
ANISOU  357  O   GLU A  54     2343   1683   2612   -166   -792    158       O  
ATOM    358  CB  GLU A  54      43.476   0.027   3.312  1.00 16.51           C  
ANISOU  358  CB  GLU A  54     2117   1523   2633     65   -683    262       C  
ATOM    359  CG  GLU A  54      43.985  -0.113   4.746  1.00 17.56           C  
ANISOU  359  CG  GLU A  54     2078   1899   2696     38   -756    325       C  
ATOM    360  CD  GLU A  54      45.455   0.210   4.890  1.00 26.41           C  
ANISOU  360  CD  GLU A  54     2955   3246   3833     82   -762    425       C  
ATOM    361  OE1 GLU A  54      46.258  -0.281   4.065  1.00 26.58           O  
ANISOU  361  OE1 GLU A  54     2972   3213   3916    271   -658    560       O  
ATOM    362  OE2 GLU A  54      45.803   0.959   5.826  1.00 25.07           O  
ANISOU  362  OE2 GLU A  54     2597   3326   3601    -97   -854    363       O  
ATOM    363  N   VAL A  55      40.526   1.041   3.957  1.00 15.00           N  
ANISOU  363  N   VAL A  55     1965   1290   2444   -201   -781     23       N  
ATOM    364  CA  VAL A  55      39.679   1.639   4.979  1.00 19.10           C  
ANISOU  364  CA  VAL A  55     2406   1882   2969   -300   -778    -66       C  
ATOM    365  C   VAL A  55      38.208   1.657   4.566  1.00 18.18           C  
ANISOU  365  C   VAL A  55     2288   1734   2885   -319   -785    -75       C  
ATOM    366  O   VAL A  55      37.377   2.285   5.228  1.00 17.68           O  
ANISOU  366  O   VAL A  55     2141   1713   2865   -352   -732   -131       O  
ATOM    367  CB  VAL A  55      40.156   3.061   5.318  1.00 22.80           C  
ANISOU  367  CB  VAL A  55     2799   2364   3502   -352   -708   -167       C  
ATOM    368  CG1 VAL A  55      41.597   3.012   5.827  1.00 22.83           C  
ANISOU  368  CG1 VAL A  55     2728   2508   3439   -406   -739   -154       C  
ATOM    369  CG2 VAL A  55      40.057   3.966   4.105  1.00 20.48           C  
ANISOU  369  CG2 VAL A  55     2531   1926   3326   -272   -642   -156       C  
ATOM    370  N   ASP A  56      37.893   0.964   3.469  1.00 15.92           N  
ANISOU  370  N   ASP A  56     2247   1701   2102   -227    -30    285       N  
ATOM    371  CA  ASP A  56      36.522   0.885   2.959  1.00 13.03           C  
ANISOU  371  CA  ASP A  56     1817   1366   1766   -288    -45    220       C  
ATOM    372  C   ASP A  56      35.739  -0.189   3.717  1.00 15.90           C  
ANISOU  372  C   ASP A  56     2142   1738   2162   -410     13    281       C  
ATOM    373  O   ASP A  56      35.487  -1.271   3.193  1.00 20.32           O  
ANISOU  373  O   ASP A  56     2738   2191   2790   -492     10    287       O  
ATOM    374  CB  ASP A  56      36.532   0.584   1.460  1.00 14.09           C  
ANISOU  374  CB  ASP A  56     2019   1397   1937   -278   -103    155       C  
ATOM    375  CG  ASP A  56      35.133   0.463   0.871  1.00 18.53           C  
ANISOU  375  CG  ASP A  56     2502   2003   2535   -344   -163     76       C  
ATOM    376  OD1 ASP A  56      34.167   0.985   1.461  1.00 17.08           O  
ANISOU  376  OD1 ASP A  56     2182   1945   2362   -360   -156     56       O  
ATOM    377  OD2 ASP A  56      35.005  -0.154  -0.196  1.00 17.61           O  
ANISOU  377  OD2 ASP A  56     2453   1800   2439   -374   -220     23       O  
ATOM    378  N   ALA A  57      35.359   0.133   4.951  1.00 16.30           N  
ANISOU  378  N   ALA A  57     2131   1905   2156   -429     79    322       N  
ATOM    379  CA  ALA A  57      34.769  -0.827   5.869  1.00 22.02           C  
ANISOU  379  CA  ALA A  57     2843   2638   2884   -545    173    412       C  
ATOM    380  C   ALA A  57      33.538  -1.546   5.319  1.00 22.26           C  
ANISOU  380  C   ALA A  57     2784   2641   3032   -680    190    369       C  
ATOM    381  O   ALA A  57      33.366  -2.735   5.574  1.00 25.41           O  
ANISOU  381  O   ALA A  57     3229   2942   3482   -798    252    448       O  
ATOM    382  CB  ALA A  57      34.409  -0.141   7.180  1.00 21.39           C  
ANISOU  382  CB  ALA A  57     2714   2716   2698   -534    257    434       C  
ATOM    383  N   ASP A  58      32.669  -0.848   4.595  1.00 16.16           N  
ANISOU  383  N   ASP A  58     1882   1948   2311   -668    131    247       N  
ATOM    384  CA  ASP A  58      31.451  -1.521   4.138  1.00 21.16           C  
ANISOU  384  CA  ASP A  58     2390   2580   3069   -810    126    192       C  
ATOM    385  C   ASP A  58      31.615  -2.109   2.741  1.00 20.20           C  
ANISOU  385  C   ASP A  58     2344   2323   3008   -835     -1    119       C  
ATOM    386  O   ASP A  58      30.682  -2.695   2.183  1.00 20.12           O  
ANISOU  386  O   ASP A  58     2242   2298   3104   -962    -48     46       O  
ATOM    387  CB  ASP A  58      30.242  -0.572   4.203  1.00 25.27           C  
ANISOU  387  CB  ASP A  58     2690   3279   3631   -787    123     99       C  
ATOM    388  CG  ASP A  58      30.276   0.531   3.158  1.00 23.30           C  
ANISOU  388  CG  ASP A  58     2424   3066   3362   -633    -27     -6       C  
ATOM    389  OD1 ASP A  58      31.274   0.661   2.420  1.00 18.24           O  
ANISOU  389  OD1 ASP A  58     1948   2323   2660   -551   -107     -6       O  
ATOM    390  OD2 ASP A  58      29.283   1.289   3.087  1.00 23.95           O  
ANISOU  390  OD2 ASP A  58     2326   3279   3495   -586    -53    -82       O  
ATOM    391  N   GLY A  59      32.810  -1.959   2.180  1.00 20.29           N  
ANISOU  391  N   GLY A  59     2520   2239   2951   -721    -53    128       N  
ATOM    392  CA  GLY A  59      33.133  -2.594   0.913  1.00 19.15           C  
ANISOU  392  CA  GLY A  59     2494   1951   2831   -733   -140     62       C  
ATOM    393  C   GLY A  59      32.445  -2.030  -0.315  1.00 20.54           C  
ANISOU  393  C   GLY A  59     2619   2183   3002   -703   -284    -74       C  
ATOM    394  O   GLY A  59      32.523  -2.620  -1.399  1.00 18.51           O  
ANISOU  394  O   GLY A  59     2467   1820   2746   -734   -365   -150       O  
ATOM    395  N   ASN A  60      31.793  -0.880  -0.183  1.00 20.53           N  
ANISOU  395  N   ASN A  60     2475   2343   2982   -628   -325   -109       N  
ATOM    396  CA  ASN A  60      31.039  -0.362  -1.321  1.00 23.38           C  
ANISOU  396  CA  ASN A  60     2782   2766   3337   -583   -487   -223       C  
ATOM    397  C   ASN A  60      31.913   0.384  -2.354  1.00 16.21           C  
ANISOU  397  C   ASN A  60     2056   1803   2300   -424   -557   -240       C  
ATOM    398  O   ASN A  60      31.406   0.842  -3.384  1.00 25.01           O  
ANISOU  398  O   ASN A  60     3177   2957   3368   -362   -703   -317       O  
ATOM    399  CB  ASN A  60      29.882   0.524  -0.829  1.00 24.69           C  
ANISOU  399  CB  ASN A  60     2708   3115   3558   -548   -506   -253       C  
ATOM    400  CG  ASN A  60      30.323   1.927  -0.446  1.00 24.91           C  
ANISOU  400  CG  ASN A  60     2755   3205   3506   -366   -468   -218       C  
ATOM    401  OD1 ASN A  60      31.502   2.185  -0.191  1.00 20.70           O  
ANISOU  401  OD1 ASN A  60     2378   2596   2892   -304   -395   -155       O  
ATOM    402  ND2 ASN A  60      29.360   2.841  -0.381  1.00 26.41           N  
ANISOU  402  ND2 ASN A  60     2771   3529   3735   -282   -516   -267       N  
ATOM    403  N   GLY A  61      33.217   0.476  -2.094  1.00 17.57           N  
ANISOU  403  N   GLY A  61     2373   1887   2416   -360   -454   -165       N  
ATOM    404  CA  GLY A  61      34.166   0.986  -3.073  1.00 17.32           C  
ANISOU  404  CA  GLY A  61     2521   1778   2280   -243   -472   -173       C  
ATOM    405  C   GLY A  61      34.540   2.451  -2.926  1.00 17.63           C  
ANISOU  405  C   GLY A  61     2564   1873   2263   -104   -451   -140       C  
ATOM    406  O   GLY A  61      35.434   2.942  -3.622  1.00 16.33           O  
ANISOU  406  O   GLY A  61     2547   1635   2022    -18   -427   -127       O  
ATOM    407  N   THR A  62      33.853   3.153  -2.033  1.00 14.37           N  
ANISOU  407  N   THR A  62     1994   1576   1891    -85   -443   -133       N  
ATOM    408  CA  THR A  62      34.145   4.570  -1.779  1.00 13.88           C  
ANISOU  408  CA  THR A  62     1939   1544   1790     40   -415   -115       C  
ATOM    409  C   THR A  62      34.226   4.800  -0.280  1.00 14.98           C  
ANISOU  409  C   THR A  62     1974   1751   1967     13   -312    -81       C  
ATOM    410  O   THR A  62      33.735   3.981   0.494  1.00 17.36           O  
ANISOU  410  O   THR A  62     2176   2104   2317    -88   -273    -67       O  
ATOM    411  CB  THR A  62      33.066   5.516  -2.363  1.00 17.76           C  
ANISOU  411  CB  THR A  62     2367   2110   2271    145   -531   -166       C  
ATOM    412  OG1 THR A  62      31.824   5.304  -1.680  1.00 20.43           O  
ANISOU  412  OG1 THR A  62     2486   2575   2701     97   -552   -203       O  
ATOM    413  CG2 THR A  62      32.882   5.290  -3.853  1.00 20.78           C  
ANISOU  413  CG2 THR A  62     2869   2447   2579    177   -665   -201       C  
ATOM    414  N   ILE A  63      34.814   5.920   0.125  1.00 14.90           N  
ANISOU  414  N   ILE A  63     2001   1734   1926     96   -265    -72       N  
ATOM    415  CA  ILE A  63      34.966   6.246   1.545  1.00 11.11           C  
ANISOU  415  CA  ILE A  63     1455   1320   1446     78   -179    -60       C  
ATOM    416  C   ILE A  63      33.969   7.326   1.954  1.00 14.76           C  
ANISOU  416  C   ILE A  63     1817   1869   1920    161   -176   -120       C  
ATOM    417  O   ILE A  63      33.981   8.412   1.381  1.00 17.48           O  
ANISOU  417  O   ILE A  63     2217   2168   2257    273   -210   -149       O  
ATOM    418  CB  ILE A  63      36.397   6.740   1.846  1.00 12.81           C  
ANISOU  418  CB  ILE A  63     1773   1465   1629     97   -132    -34       C  
ATOM    419  CG1 ILE A  63      37.433   5.702   1.387  1.00 12.77           C  
ANISOU  419  CG1 ILE A  63     1847   1372   1635     45   -124     23       C  
ATOM    420  CG2 ILE A  63      36.557   7.103   3.317  1.00 11.25           C  
ANISOU  420  CG2 ILE A  63     1528   1346   1401     78    -73    -40       C  
ATOM    421  CD1 ILE A  63      37.165   4.268   1.910  1.00 11.43           C  
ANISOU  421  CD1 ILE A  63     1635   1222   1485    -49   -112     72       C  
ATOM    422  N   ASP A  64      33.099   7.034   2.922  1.00 12.71           N  
ANISOU  422  N   ASP A  64     1419   1726   1684    115   -118   -134       N  
ATOM    423  CA  ASP A  64      32.189   8.063   3.427  1.00 16.05           C  
ANISOU  423  CA  ASP A  64     1736   2234   2128    210    -83   -201       C  
ATOM    424  C   ASP A  64      32.797   8.714   4.672  1.00 15.83           C  
ANISOU  424  C   ASP A  64     1765   2223   2028    222     20   -218       C  
ATOM    425  O   ASP A  64      33.886   8.345   5.098  1.00 16.84           O  
ANISOU  425  O   ASP A  64     1992   2310   2095    155     37   -172       O  
ATOM    426  CB  ASP A  64      30.790   7.500   3.722  1.00 18.24           C  
ANISOU  426  CB  ASP A  64     1806   2642   2484    163    -57   -225       C  
ATOM    427  CG  ASP A  64      30.805   6.312   4.683  1.00 21.05           C  
ANISOU  427  CG  ASP A  64     2127   3046   2824      1     50   -166       C  
ATOM    428  OD1 ASP A  64      31.722   6.186   5.515  1.00 20.25           O  
ANISOU  428  OD1 ASP A  64     2143   2922   2630    -35    118   -118       O  
ATOM    429  OD2 ASP A  64      29.861   5.501   4.624  1.00 26.82           O  
ANISOU  429  OD2 ASP A  64     2713   3840   3640    -94     62   -165       O  
ATOM    430  N   PHE A  65      32.114   9.692   5.249  1.00 18.61           N  
ANISOU  430  N   PHE A  65     2054   2633   2386    316     80   -294       N  
ATOM    431  CA  PHE A  65      32.703  10.395   6.386  1.00 16.39           C  
ANISOU  431  CA  PHE A  65     1855   2357   2016    327    165   -340       C  
ATOM    432  C   PHE A  65      32.906   9.493   7.615  1.00 14.95           C  
ANISOU  432  C   PHE A  65     1672   2273   1738    205    251   -296       C  
ATOM    433  O   PHE A  65      33.964   9.568   8.241  1.00 19.24           O  
ANISOU  433  O   PHE A  65     2333   2793   2186    167    246   -286       O  
ATOM    434  CB  PHE A  65      31.868  11.627   6.762  1.00 19.16           C  
ANISOU  434  CB  PHE A  65     2153   2734   2391    466    230   -448       C  
ATOM    435  CG  PHE A  65      32.578  12.567   7.709  1.00 20.45           C  
ANISOU  435  CG  PHE A  65     2447   2859   2464    488    292   -529       C  
ATOM    436  CD1 PHE A  65      33.798  13.128   7.363  1.00 18.81           C  
ANISOU  436  CD1 PHE A  65     2393   2511   2241    475    226   -532       C  
ATOM    437  CD2 PHE A  65      32.032  12.881   8.942  1.00 19.17           C  
ANISOU  437  CD2 PHE A  65     2254   2800   2229    509    423   -612       C  
ATOM    438  CE1 PHE A  65      34.463  13.992   8.229  1.00 20.80           C  
ANISOU  438  CE1 PHE A  65     2757   2723   2423    471    263   -627       C  
ATOM    439  CE2 PHE A  65      32.692  13.752   9.812  1.00 21.64           C  
ANISOU  439  CE2 PHE A  65     2708   3075   2440    521    464   -712       C  
ATOM    440  CZ  PHE A  65      33.904  14.306   9.453  1.00 22.51           C  
ANISOU  440  CZ  PHE A  65     2961   3040   2550    495    371   -724       C  
ATOM    441  N   PRO A  66      31.909   8.649   7.978  1.00 17.95           N  
ANISOU  441  N   PRO A  66     1920   2761   2141    142    327   -264       N  
ATOM    442  CA  PRO A  66      32.173   7.736   9.102  1.00 22.66           C  
ANISOU  442  CA  PRO A  66     2559   3426   2626     25    416   -189       C  
ATOM    443  C   PRO A  66      33.414   6.850   8.915  1.00 20.71           C  
ANISOU  443  C   PRO A  66     2436   3092   2340    -53    328    -82       C  
ATOM    444  O   PRO A  66      34.180   6.658   9.866  1.00 21.71           O  
ANISOU  444  O   PRO A  66     2667   3244   2339    -86    344    -40       O  
ATOM    445  CB  PRO A  66      30.905   6.878   9.158  1.00 20.07           C  
ANISOU  445  CB  PRO A  66     2061   3186   2379    -53    508   -155       C  
ATOM    446  CG  PRO A  66      29.843   7.758   8.616  1.00 25.07           C  
ANISOU  446  CG  PRO A  66     2533   3860   3131     61    506   -261       C  
ATOM    447  CD  PRO A  66      30.504   8.559   7.530  1.00 19.39           C  
ANISOU  447  CD  PRO A  66     1905   3015   2446    171    348   -296       C  
ATOM    448  N   GLU A  67      33.619   6.327   7.710  1.00 16.74           N  
ANISOU  448  N   GLU A  67     1927   2491   1941    -70    232    -45       N  
ATOM    449  CA  GLU A  67      34.809   5.515   7.434  1.00 14.42           C  
ANISOU  449  CA  GLU A  67     1741   2102   1635   -118    164     44       C  
ATOM    450  C   GLU A  67      36.063   6.385   7.542  1.00 14.34           C  
ANISOU  450  C   GLU A  67     1828   2045   1575    -58    107     11       C  
ATOM    451  O   GLU A  67      37.103   5.955   8.036  1.00 16.22           O  
ANISOU  451  O   GLU A  67     2134   2268   1759    -85     76     72       O  
ATOM    452  CB  GLU A  67      34.702   4.853   6.049  1.00 14.44           C  
ANISOU  452  CB  GLU A  67     1731   2006   1750   -139     91     62       C  
ATOM    453  CG  GLU A  67      33.633   3.751   5.977  1.00 16.53           C  
ANISOU  453  CG  GLU A  67     1902   2297   2082   -244    130     96       C  
ATOM    454  CD  GLU A  67      33.382   3.235   4.572  1.00 18.49           C  
ANISOU  454  CD  GLU A  67     2140   2458   2427   -265     37     72       C  
ATOM    455  OE1 GLU A  67      33.747   3.939   3.602  1.00 15.37           O  
ANISOU  455  OE1 GLU A  67     1796   2011   2034   -174    -47     22       O  
ATOM    456  OE2 GLU A  67      32.797   2.129   4.436  1.00 18.52           O  
ANISOU  456  OE2 GLU A  67     2100   2441   2497   -381     51     99       O  
ATOM    457  N   PHE A  68      35.936   7.625   7.095  1.00 15.80           N  
ANISOU  457  N   PHE A  68     2010   2204   1790     25     91    -86       N  
ATOM    458  CA  PHE A  68      37.013   8.602   7.168  1.00 15.12           C  
ANISOU  458  CA  PHE A  68     2005   2057   1683     61     53   -137       C  
ATOM    459  C   PHE A  68      37.387   8.865   8.637  1.00 15.74           C  
ANISOU  459  C   PHE A  68     2121   2225   1633     36     77   -170       C  
ATOM    460  O   PHE A  68      38.562   8.834   9.018  1.00 16.68           O  
ANISOU  460  O   PHE A  68     2292   2331   1715      4     15   -155       O  
ATOM    461  CB  PHE A  68      36.564   9.875   6.446  1.00 14.91           C  
ANISOU  461  CB  PHE A  68     1984   1964   1715    156     53   -226       C  
ATOM    462  CG  PHE A  68      37.617  10.930   6.320  1.00 17.64           C  
ANISOU  462  CG  PHE A  68     2420   2207   2074    173     30   -279       C  
ATOM    463  CD1 PHE A  68      38.485  10.943   5.236  1.00 19.89           C  
ANISOU  463  CD1 PHE A  68     2757   2372   2427    166     -6   -237       C  
ATOM    464  CD2 PHE A  68      37.718  11.938   7.270  1.00 20.79           C  
ANISOU  464  CD2 PHE A  68     2857   2622   2420    189     59   -383       C  
ATOM    465  CE1 PHE A  68      39.450  11.939   5.113  1.00 21.20           C  
ANISOU  465  CE1 PHE A  68     2993   2435   2629    158     -3   -284       C  
ATOM    466  CE2 PHE A  68      38.677  12.935   7.151  1.00 20.43           C  
ANISOU  466  CE2 PHE A  68     2891   2462   2409    178     39   -446       C  
ATOM    467  CZ  PHE A  68      39.546  12.932   6.079  1.00 15.74           C  
ANISOU  467  CZ  PHE A  68     2328   1749   1904    155     12   -390       C  
ATOM    468  N   LEU A  69      36.375   9.087   9.465  1.00 17.01           N  
ANISOU  468  N   LEU A  69     2250   2490   1722     51    166   -217       N  
ATOM    469  CA  LEU A  69      36.594   9.328  10.886  1.00 16.41           C  
ANISOU  469  CA  LEU A  69     2239   2513   1481     32    202   -258       C  
ATOM    470  C   LEU A  69      37.323   8.158  11.555  1.00 19.62           C  
ANISOU  470  C   LEU A  69     2696   2970   1788    -42    158   -130       C  
ATOM    471  O   LEU A  69      38.263   8.360  12.326  1.00 20.23           O  
ANISOU  471  O   LEU A  69     2851   3080   1754    -56     84   -148       O  
ATOM    472  CB  LEU A  69      35.261   9.590  11.579  1.00 23.07           C  
ANISOU  472  CB  LEU A  69     3035   3465   2266     64    347   -317       C  
ATOM    473  CG  LEU A  69      34.648  10.958  11.281  1.00 25.96           C  
ANISOU  473  CG  LEU A  69     3375   3789   2701    174    390   -464       C  
ATOM    474  CD1 LEU A  69      33.280  11.077  11.936  1.00 31.48           C  
ANISOU  474  CD1 LEU A  69     3986   4607   3369    219    554   -518       C  
ATOM    475  CD2 LEU A  69      35.574  12.060  11.778  1.00 26.71           C  
ANISOU  475  CD2 LEU A  69     3599   3827   2722    192    341   -584       C  
ATOM    476  N   THR A  70      36.883   6.940  11.258  1.00 18.33           N  
ANISOU  476  N   THR A  70     2492   2804   1670    -88    191     -5       N  
ATOM    477  CA  THR A  70      37.528   5.742  11.790  1.00 22.82           C  
ANISOU  477  CA  THR A  70     3122   3384   2165   -140    155    140       C  
ATOM    478  C   THR A  70      39.007   5.707  11.423  1.00 22.43           C  
ANISOU  478  C   THR A  70     3103   3258   2162   -120      9    164       C  
ATOM    479  O   THR A  70      39.855   5.434  12.266  1.00 18.23           O  
ANISOU  479  O   THR A  70     2633   2775   1518   -120    -69    216       O  
ATOM    480  CB  THR A  70      36.844   4.468  11.276  1.00 21.65           C  
ANISOU  480  CB  THR A  70     2930   3188   2108   -200    215    258       C  
ATOM    481  OG1 THR A  70      35.470   4.475  11.684  1.00 24.77           O  
ANISOU  481  OG1 THR A  70     3260   3670   2481   -236    362    235       O  
ATOM    482  CG2 THR A  70      37.533   3.222  11.828  1.00 20.87           C  
ANISOU  482  CG2 THR A  70     2922   3064   1942   -236    183    423       C  
ATOM    483  N   MET A  71      39.306   6.001  10.162  1.00 17.42           N  
ANISOU  483  N   MET A  71     2420   2512   1688    -97    -28    126       N  
ATOM    484  CA  MET A  71      40.689   6.053   9.690  1.00 17.05           C  
ANISOU  484  CA  MET A  71     2371   2389   1717    -81   -129    136       C  
ATOM    485  C   MET A  71      41.535   7.065  10.463  1.00 19.40           C  
ANISOU  485  C   MET A  71     2687   2741   1944    -78   -206     41       C  
ATOM    486  O   MET A  71      42.664   6.770  10.856  1.00 20.13           O  
ANISOU  486  O   MET A  71     2770   2851   2026    -81   -310     81       O  
ATOM    487  CB  MET A  71      40.726   6.394   8.195  1.00 14.77           C  
ANISOU  487  CB  MET A  71     2051   1976   1585    -58   -115     96       C  
ATOM    488  CG  MET A  71      42.104   6.786   7.679  1.00 14.17           C  
ANISOU  488  CG  MET A  71     1960   1826   1599    -48   -174     77       C  
ATOM    489  SD  MET A  71      42.125   7.051   5.903  1.00 16.30           S  
ANISOU  489  SD  MET A  71     2238   1949   2008    -21   -123     58       S  
ATOM    490  CE  MET A  71      41.083   8.504   5.710  1.00 17.31           C  
ANISOU  490  CE  MET A  71     2396   2071   2112      9    -83    -55       C  
ATOM    491  N   MET A  72      40.988   8.259  10.675  1.00 17.47           N  
ANISOU  491  N   MET A  72     2460   2515   1662    -70   -162    -93       N  
ATOM    492  CA  MET A  72      41.778   9.358  11.220  1.00 22.61           C  
ANISOU  492  CA  MET A  72     3136   3177   2277    -86   -233   -219       C  
ATOM    493  C   MET A  72      41.870   9.309  12.745  1.00 32.15           C  
ANISOU  493  C   MET A  72     4415   4532   3270   -104   -283   -243       C  
ATOM    494  O   MET A  72      42.695  10.005  13.335  1.00 32.42           O  
ANISOU  494  O   MET A  72     4471   4594   3253   -133   -385   -345       O  
ATOM    495  CB  MET A  72      41.212  10.716  10.783  1.00 22.73           C  
ANISOU  495  CB  MET A  72     3172   3114   2350    -61   -163   -361       C  
ATOM    496  CG  MET A  72      41.128  10.915   9.274  1.00 19.67           C  
ANISOU  496  CG  MET A  72     2753   2583   2138    -32   -124   -336       C  
ATOM    497  SD  MET A  72      42.700  10.681   8.432  1.00 22.41           S  
ANISOU  497  SD  MET A  72     3054   2831   2629    -77   -193   -282       S  
ATOM    498  CE  MET A  72      43.720  11.892   9.267  1.00 26.49           C  
ANISOU  498  CE  MET A  72     3582   3345   3138   -146   -267   -430       C  
ATOM    499  N   ALA A  73      41.037   8.488  13.381  1.00 29.28           N  
ANISOU  499  N   ALA A  73     4093   4260   2773    -96   -211   -152       N  
ATOM    500  CA  ALA A  73      41.061   8.374  14.845  1.00 35.44           C  
ANISOU  500  CA  ALA A  73     4977   5186   3303   -106   -239   -155       C  
ATOM    501  C   ALA A  73      42.363   7.744  15.334  1.00 39.76           C  
ANISOU  501  C   ALA A  73     5537   5778   3792   -113   -424    -66       C  
ATOM    502  O   ALA A  73      42.899   6.831  14.701  1.00 37.61           O  
ANISOU  502  O   ALA A  73     5201   5440   3650    -98   -473     70       O  
ATOM    503  CB  ALA A  73      39.874   7.566  15.339  1.00 33.80           C  
ANISOU  503  CB  ALA A  73     4812   5052   2979   -108    -85    -51       C  
TER     504      ALA A  73                                                      
ATOM    505  N   GLY B  -3      49.498  -6.679   5.604  1.00 49.46           N  
ANISOU  505  N   GLY B  -3     7231   4541   7020    380   -795   -335       N  
ATOM    506  CA  GLY B  -3      48.714  -5.898   6.541  1.00 42.89           C  
ANISOU  506  CA  GLY B  -3     6563   3772   5961    288   -807   -267       C  
ATOM    507  C   GLY B  -3      48.473  -4.496   6.017  1.00 46.76           C  
ANISOU  507  C   GLY B  -3     6923   4443   6402    291   -664   -288       C  
ATOM    508  O   GLY B  -3      48.919  -4.156   4.920  1.00 40.49           O  
ANISOU  508  O   GLY B  -3     5946   3715   5724    356   -556   -351       O  
ATOM    509  N   PRO B  -2      47.762  -3.673   6.802  1.00 49.83           N  
ANISOU  509  N   PRO B  -2     7426   4893   6613    210   -649   -243       N  
ATOM    510  CA  PRO B  -2      47.462  -2.288   6.424  1.00 39.67           C  
ANISOU  510  CA  PRO B  -2     6032   3766   5276    208   -537   -259       C  
ATOM    511  C   PRO B  -2      48.720  -1.422   6.380  1.00 36.10           C  
ANISOU  511  C   PRO B  -2     5444   3298   4974    291   -617   -247       C  
ATOM    512  O   PRO B  -2      49.645  -1.612   7.179  1.00 32.80           O  
ANISOU  512  O   PRO B  -2     5066   2734   4663    323   -810   -205       O  
ATOM    513  CB  PRO B  -2      46.510  -1.818   7.530  1.00 43.67           C  
ANISOU  513  CB  PRO B  -2     6715   4284   5594     91   -518   -220       C  
ATOM    514  CG  PRO B  -2      46.813  -2.705   8.701  1.00 45.49           C  
ANISOU  514  CG  PRO B  -2     7183   4325   5778     42   -675   -158       C  
ATOM    515  CD  PRO B  -2      47.186  -4.031   8.111  1.00 51.62           C  
ANISOU  515  CD  PRO B  -2     7922   5019   6673    100   -721   -184       C  
ATOM    516  N   MET B  -1      48.746  -0.467   5.457  1.00 29.12           N  
ANISOU  516  N   MET B  -1     4415   2542   4108    323   -486   -289       N  
ATOM    517  CA  MET B  -1      49.930   0.351   5.260  1.00 28.33           C  
ANISOU  517  CA  MET B  -1     4169   2423   4172    393   -511   -300       C  
ATOM    518  C   MET B  -1      49.663   1.840   5.433  1.00 21.48           C  
ANISOU  518  C   MET B  -1     3285   1675   3201    369   -467   -275       C  
ATOM    519  O   MET B  -1      50.572   2.640   5.245  1.00 22.25           O  
ANISOU  519  O   MET B  -1     3263   1768   3424    417   -466   -289       O  
ATOM    520  CB  MET B  -1      50.528   0.096   3.872  1.00 28.05           C  
ANISOU  520  CB  MET B  -1     3988   2384   4287    450   -364   -392       C  
ATOM    521  CG  MET B  -1      51.179  -1.276   3.714  1.00 41.02           C  
ANISOU  521  CG  MET B  -1     5592   3873   6120    493   -413   -433       C  
ATOM    522  SD  MET B  -1      52.683  -1.464   4.700  1.00 35.89           S  
ANISOU  522  SD  MET B  -1     4842   3008   5786    567   -662   -422       S  
ATOM    523  CE  MET B  -1      53.794  -0.401   3.780  1.00 46.36           C  
ANISOU  523  CE  MET B  -1     5926   4340   7350    618   -489   -521       C  
ATOM    524  N   ASP B  23      48.428   2.215   5.778  1.00 18.97           N  
ANISOU  524  N   ASP B  23     3071   1451   2686    292   -420   -253       N  
ATOM    525  CA  ASP B  23      48.135   3.609   6.095  1.00 18.18           C  
ANISOU  525  CA  ASP B  23     2961   1446   2501    265   -395   -231       C  
ATOM    526  C   ASP B  23      48.323   4.598   4.946  1.00 17.53           C  
ANISOU  526  C   ASP B  23     2752   1464   2444    309   -283   -274       C  
ATOM    527  O   ASP B  23      48.551   5.778   5.189  1.00 17.19           O  
ANISOU  527  O   ASP B  23     2672   1470   2388    311   -287   -253       O  
ATOM    528  CB  ASP B  23      49.008   4.078   7.272  1.00 24.40           C  
ANISOU  528  CB  ASP B  23     3789   2148   3335    271   -552   -166       C  
ATOM    529  CG  ASP B  23      48.218   4.366   8.527  1.00 24.92           C  
ANISOU  529  CG  ASP B  23     4044   2200   3225    170   -587   -116       C  
ATOM    530  OD1 ASP B  23      46.973   4.223   8.540  1.00 29.17           O  
ANISOU  530  OD1 ASP B  23     4651   2793   3640     91   -466   -143       O  
ATOM    531  OD2 ASP B  23      48.862   4.777   9.501  1.00 19.64           O  
ANISOU  531  OD2 ASP B  23     3457   1447   2557    162   -730    -60       O  
ATOM    532  N   ASN B  24      48.221   4.154   3.702  1.00 17.58           N  
ANISOU  532  N   ASN B  24     2726   1486   2467    332   -182   -335       N  
ATOM    533  CA  ASN B  24      48.569   5.086   2.630  1.00 17.37           C  
ANISOU  533  CA  ASN B  24     2646   1511   2443    358    -76   -374       C  
ATOM    534  C   ASN B  24      47.500   6.164   2.381  1.00 20.77           C  
ANISOU  534  C   ASN B  24     3118   2050   2723    323    -59   -372       C  
ATOM    535  O   ASN B  24      47.851   7.316   2.105  1.00 16.27           O  
ANISOU  535  O   ASN B  24     2523   1519   2140    334    -25   -369       O  
ATOM    536  CB  ASN B  24      48.906   4.309   1.363  1.00 21.05           C  
ANISOU  536  CB  ASN B  24     3119   1924   2956    378     37   -445       C  
ATOM    537  CG  ASN B  24      50.308   3.715   1.417  1.00 25.98           C  
ANISOU  537  CG  ASN B  24     3638   2423   3809    425     56   -476       C  
ATOM    538  OD1 ASN B  24      51.240   4.349   1.917  1.00 28.53           O  
ANISOU  538  OD1 ASN B  24     3862   2708   4271    454     23   -466       O  
ATOM    539  ND2 ASN B  24      50.454   2.483   0.949  1.00 23.93           N  
ANISOU  539  ND2 ASN B  24     3385   2084   3623    436     95   -523       N  
ATOM    540  N   LEU B  25      46.213   5.847   2.533  1.00 16.25           N  
ANISOU  540  N   LEU B  25     2597   1509   2068    279    -87   -383       N  
ATOM    541  CA  LEU B  25      45.202   6.917   2.442  1.00 15.72           C  
ANISOU  541  CA  LEU B  25     2532   1515   1927    251   -101   -397       C  
ATOM    542  C   LEU B  25      45.355   7.892   3.603  1.00 15.29           C  
ANISOU  542  C   LEU B  25     2444   1494   1872    230   -128   -348       C  
ATOM    543  O   LEU B  25      45.296   9.114   3.424  1.00 14.90           O  
ANISOU  543  O   LEU B  25     2367   1497   1796    238   -127   -345       O  
ATOM    544  CB  LEU B  25      43.780   6.358   2.425  1.00 15.86           C  
ANISOU  544  CB  LEU B  25     2567   1529   1929    205   -122   -448       C  
ATOM    545  CG  LEU B  25      42.675   7.431   2.412  1.00 16.92           C  
ANISOU  545  CG  LEU B  25     2662   1704   2061    179   -157   -487       C  
ATOM    546  CD1 LEU B  25      42.865   8.418   1.267  1.00 15.96           C  
ANISOU  546  CD1 LEU B  25     2571   1604   1890    223   -196   -496       C  
ATOM    547  CD2 LEU B  25      41.305   6.784   2.310  1.00 21.06           C  
ANISOU  547  CD2 LEU B  25     3165   2191   2645    136   -178   -568       C  
ATOM    548  N   TYR B  26      45.549   7.353   4.802  1.00 15.52           N  
ANISOU  548  N   TYR B  26     2506   1474   1916    198   -161   -308       N  
ATOM    549  CA  TYR B  26      45.822   8.193   5.962  1.00 15.37           C  
ANISOU  549  CA  TYR B  26     2504   1458   1878    169   -197   -257       C  
ATOM    550  C   TYR B  26      46.963   9.187   5.662  1.00 15.14           C  
ANISOU  550  C   TYR B  26     2401   1455   1899    231   -213   -230       C  
ATOM    551  O   TYR B  26      46.842  10.393   5.937  1.00 14.98           O  
ANISOU  551  O   TYR B  26     2357   1489   1845    220   -209   -216       O  
ATOM    552  CB  TYR B  26      46.157   7.317   7.179  1.00 16.09           C  
ANISOU  552  CB  TYR B  26     2711   1444   1959    127   -265   -209       C  
ATOM    553  CG  TYR B  26      46.717   8.105   8.334  1.00 16.53           C  
ANISOU  553  CG  TYR B  26     2829   1466   1986    102   -341   -148       C  
ATOM    554  CD1 TYR B  26      45.879   8.832   9.170  1.00 20.12           C  
ANISOU  554  CD1 TYR B  26     3361   1940   2343     13   -286   -150       C  
ATOM    555  CD2 TYR B  26      48.088   8.124   8.587  1.00 16.75           C  
ANISOU  555  CD2 TYR B  26     2834   1422   2109    165   -469   -103       C  
ATOM    556  CE1 TYR B  26      46.386   9.562  10.230  1.00 22.08           C  
ANISOU  556  CE1 TYR B  26     3702   2146   2543    -20   -356    -95       C  
ATOM    557  CE2 TYR B  26      48.608   8.854   9.642  1.00 24.46           C  
ANISOU  557  CE2 TYR B  26     3881   2349   3062    144   -573    -48       C  
ATOM    558  CZ  TYR B  26      47.748   9.571  10.457  1.00 27.13           C  
ANISOU  558  CZ  TYR B  26     4335   2717   3256     49   -516    -37       C  
ATOM    559  OH  TYR B  26      48.255  10.298  11.502  1.00 23.52           O  
ANISOU  559  OH  TYR B  26     3981   2201   2754     18   -619     17       O  
ATOM    560  N   LEU B  27      48.055   8.703   5.074  1.00 15.61           N  
ANISOU  560  N   LEU B  27     2411   1461   2059    291   -212   -237       N  
ATOM    561  CA  LEU B  27      49.199   9.586   4.800  1.00 15.71           C  
ANISOU  561  CA  LEU B  27     2336   1470   2164    338   -195   -235       C  
ATOM    562  C   LEU B  27      48.869  10.635   3.725  1.00 17.91           C  
ANISOU  562  C   LEU B  27     2609   1829   2367    340    -93   -268       C  
ATOM    563  O   LEU B  27      49.359  11.768   3.786  1.00 16.60           O  
ANISOU  563  O   LEU B  27     2402   1690   2215    350    -77   -255       O  
ATOM    564  CB  LEU B  27      50.436   8.763   4.405  1.00 16.72           C  
ANISOU  564  CB  LEU B  27     2388   1487   2477    391   -185   -269       C  
ATOM    565  CG  LEU B  27      51.029   7.956   5.568  1.00 17.53           C  
ANISOU  565  CG  LEU B  27     2497   1471   2693    404   -354   -230       C  
ATOM    566  CD1 LEU B  27      52.071   6.956   5.102  1.00 21.27           C  
ANISOU  566  CD1 LEU B  27     2873   1814   3395    461   -356   -285       C  
ATOM    567  CD2 LEU B  27      51.608   8.906   6.625  1.00 17.64           C  
ANISOU  567  CD2 LEU B  27     2497   1459   2745    406   -479   -178       C  
ATOM    568  N   ALA B  28      48.017  10.284   2.764  1.00 15.55           N  
ANISOU  568  N   ALA B  28     2373   1551   1982    327    -47   -310       N  
ATOM    569  CA  ALA B  28      47.611  11.264   1.751  1.00 15.03           C  
ANISOU  569  CA  ALA B  28     2363   1527   1820    323     -3   -336       C  
ATOM    570  C   ALA B  28      46.726  12.336   2.372  1.00 15.20           C  
ANISOU  570  C   ALA B  28     2370   1620   1786    300    -74   -313       C  
ATOM    571  O   ALA B  28      46.852  13.516   2.043  1.00 16.02           O  
ANISOU  571  O   ALA B  28     2484   1752   1850    306    -64   -308       O  
ATOM    572  CB  ALA B  28      46.896  10.580   0.577  1.00 15.47           C  
ANISOU  572  CB  ALA B  28     2526   1554   1799    314     12   -388       C  
ATOM    573  N   VAL B  29      45.838  11.937   3.281  1.00 16.32           N  
ANISOU  573  N   VAL B  29     2494   1774   1934    265   -127   -309       N  
ATOM    574  CA  VAL B  29      44.996  12.905   3.980  1.00 18.35           C  
ANISOU  574  CA  VAL B  29     2720   2076   2176    230   -158   -310       C  
ATOM    575  C   VAL B  29      45.841  13.810   4.876  1.00 17.31           C  
ANISOU  575  C   VAL B  29     2559   1965   2052    230   -158   -253       C  
ATOM    576  O   VAL B  29      45.604  15.019   4.953  1.00 17.41           O  
ANISOU  576  O   VAL B  29     2547   2022   2047    226   -164   -251       O  
ATOM    577  CB  VAL B  29      43.898  12.208   4.824  1.00 14.39           C  
ANISOU  577  CB  VAL B  29     2218   1550   1698    165   -154   -343       C  
ATOM    578  CG1 VAL B  29      43.180  13.213   5.709  1.00 17.41           C  
ANISOU  578  CG1 VAL B  29     2564   1954   2097    112   -138   -359       C  
ATOM    579  CG2 VAL B  29      42.892  11.497   3.905  1.00 14.35           C  
ANISOU  579  CG2 VAL B  29     2215   1519   1720    166   -175   -416       C  
ATOM    580  N   LEU B  30      46.830  13.222   5.544  1.00 18.18           N  
ANISOU  580  N   LEU B  30     2675   2029   2205    238   -174   -211       N  
ATOM    581  CA  LEU B  30      47.752  13.976   6.392  1.00 20.14           C  
ANISOU  581  CA  LEU B  30     2900   2268   2483    245   -214   -159       C  
ATOM    582  C   LEU B  30      48.500  15.024   5.580  1.00 19.93           C  
ANISOU  582  C   LEU B  30     2811   2274   2489    290   -170   -166       C  
ATOM    583  O   LEU B  30      48.622  16.173   6.002  1.00 22.63           O  
ANISOU  583  O   LEU B  30     3131   2653   2815    283   -182   -142       O  
ATOM    584  CB  LEU B  30      48.747  13.038   7.064  1.00 17.84           C  
ANISOU  584  CB  LEU B  30     2626   1878   2275    260   -293   -126       C  
ATOM    585  CG  LEU B  30      49.157  13.366   8.494  1.00 31.45           C  
ANISOU  585  CG  LEU B  30     4416   3544   3989    227   -405    -68       C  
ATOM    586  CD1 LEU B  30      47.915  13.575   9.346  1.00 34.97           C  
ANISOU  586  CD1 LEU B  30     4982   4012   4293    131   -369    -65       C  
ATOM    587  CD2 LEU B  30      50.017  12.232   9.058  1.00 27.38           C  
ANISOU  587  CD2 LEU B  30     3949   2890   3565    247   -541    -41       C  
ATOM    588  N   ARG B  31      48.999  14.621   4.415  1.00 17.64           N  
ANISOU  588  N   ARG B  31     2512   1955   2235    324    -99   -203       N  
ATOM    589  CA  ARG B  31      49.714  15.543   3.526  1.00 16.46           C  
ANISOU  589  CA  ARG B  31     2348   1806   2100    344     -8   -225       C  
ATOM    590  C   ARG B  31      48.820  16.700   3.066  1.00 18.43           C  
ANISOU  590  C   ARG B  31     2662   2121   2219    325    -13   -226       C  
ATOM    591  O   ARG B  31      49.223  17.863   3.111  1.00 17.93           O  
ANISOU  591  O   ARG B  31     2582   2080   2151    327      8   -211       O  
ATOM    592  CB  ARG B  31      50.261  14.798   2.304  1.00 24.88           C  
ANISOU  592  CB  ARG B  31     3449   2801   3203    355    111   -284       C  
ATOM    593  CG  ARG B  31      51.007  15.695   1.318  1.00 26.02           C  
ANISOU  593  CG  ARG B  31     3631   2911   3344    346    259   -323       C  
ATOM    594  CD  ARG B  31      51.296  14.978   0.006  1.00 33.81           C  
ANISOU  594  CD  ARG B  31     4723   3810   4312    326    413   -395       C  
ATOM    595  NE  ARG B  31      52.140  13.800   0.199  1.00 44.80           N  
ANISOU  595  NE  ARG B  31     5998   5119   5904    349    461   -435       N  
ATOM    596  CZ  ARG B  31      53.463  13.802   0.069  1.00 52.94           C  
ANISOU  596  CZ  ARG B  31     6913   6048   7155    355    599   -500       C  
ATOM    597  NH1 ARG B  31      54.096  14.919  -0.260  1.00 52.67           N  
ANISOU  597  NH1 ARG B  31     6876   5989   7146    329    728   -530       N  
ATOM    598  NH2 ARG B  31      54.151  12.686   0.263  1.00 61.02           N  
ANISOU  598  NH2 ARG B  31     7812   6975   8397    383    608   -548       N  
ATOM    599  N   ALA B  32      47.612  16.386   2.612  1.00 14.67           N  
ANISOU  599  N   ALA B  32     2254   1660   1660    311    -57   -251       N  
ATOM    600  CA  ALA B  32      46.710  17.439   2.134  1.00 20.44           C  
ANISOU  600  CA  ALA B  32     3040   2418   2310    303   -112   -264       C  
ATOM    601  C   ALA B  32      46.281  18.360   3.277  1.00 17.11           C  
ANISOU  601  C   ALA B  32     2532   2052   1918    287   -162   -240       C  
ATOM    602  O   ALA B  32      46.265  19.584   3.133  1.00 17.61           O  
ANISOU  602  O   ALA B  32     2603   2136   1952    291   -178   -232       O  
ATOM    603  CB  ALA B  32      45.494  16.835   1.460  1.00 16.21           C  
ANISOU  603  CB  ALA B  32     2568   1852   1737    297   -190   -313       C  
ATOM    604  N   SER B  33      45.931  17.756   4.408  1.00 15.33           N  
ANISOU  604  N   SER B  33     2252   1833   1738    258   -175   -233       N  
ATOM    605  CA  SER B  33      45.443  18.498   5.563  1.00 24.53           C  
ANISOU  605  CA  SER B  33     3373   3027   2920    218   -187   -224       C  
ATOM    606  C   SER B  33      46.534  19.383   6.157  1.00 21.25           C  
ANISOU  606  C   SER B  33     2938   2632   2504    227   -178   -167       C  
ATOM    607  O   SER B  33      46.282  20.558   6.482  1.00 19.76           O  
ANISOU  607  O   SER B  33     2726   2478   2306    215   -185   -164       O  
ATOM    608  CB  SER B  33      44.897  17.535   6.623  1.00 25.20           C  
ANISOU  608  CB  SER B  33     3472   3080   3024    158   -168   -235       C  
ATOM    609  OG  SER B  33      44.440  18.242   7.762  1.00 37.39           O  
ANISOU  609  OG  SER B  33     5013   4626   4568     95   -139   -239       O  
ATOM    610  N   GLU B  34      47.741  18.832   6.301  1.00 17.49           N  
ANISOU  610  N   GLU B  34     2458   2120   2067    252   -175   -133       N  
ATOM    611  CA  GLU B  34      48.866  19.611   6.824  1.00 24.19           C  
ANISOU  611  CA  GLU B  34     3266   2962   2962    267   -189    -93       C  
ATOM    612  C   GLU B  34      49.236  20.730   5.862  1.00 21.16           C  
ANISOU  612  C   GLU B  34     2862   2608   2570    294   -130   -106       C  
ATOM    613  O   GLU B  34      49.637  21.815   6.284  1.00 21.02           O  
ANISOU  613  O   GLU B  34     2812   2611   2562    292   -137    -83       O  
ATOM    614  CB  GLU B  34      50.089  18.727   7.086  1.00 28.23           C  
ANISOU  614  CB  GLU B  34     3746   3391   3587    296   -226    -78       C  
ATOM    615  CG  GLU B  34      49.968  17.819   8.299  1.00 37.49           C  
ANISOU  615  CG  GLU B  34     4990   4502   4754    262   -328    -45       C  
ATOM    616  CD  GLU B  34      51.151  16.869   8.437  1.00 55.71           C  
ANISOU  616  CD  GLU B  34     7260   6696   7210    305   -411    -40       C  
ATOM    617  OE1 GLU B  34      52.003  16.835   7.521  1.00 62.08           O  
ANISOU  617  OE1 GLU B  34     7959   7478   8152    356   -347    -82       O  
ATOM    618  OE2 GLU B  34      51.227  16.152   9.459  1.00 57.69           O  
ANISOU  618  OE2 GLU B  34     7605   6861   7455    279   -538     -4       O  
ATOM    619  N   GLY B  35      49.102  20.469   4.563  1.00 18.56           N  
ANISOU  619  N   GLY B  35     2584   2264   2205    309    -71   -144       N  
ATOM    620  CA  GLY B  35      49.377  21.489   3.572  1.00 16.58           C  
ANISOU  620  CA  GLY B  35     2389   2010   1903    314     -7   -158       C  
ATOM    621  C   GLY B  35      48.431  22.661   3.757  1.00 16.63           C  
ANISOU  621  C   GLY B  35     2414   2066   1837    303    -79   -148       C  
ATOM    622  O   GLY B  35      48.846  23.819   3.725  1.00 18.95           O  
ANISOU  622  O   GLY B  35     2709   2373   2118    302    -57   -133       O  
ATOM    623  N   LYS B  36      47.155  22.355   3.970  1.00 15.54           N  
ANISOU  623  N   LYS B  36     2275   1944   1684    291   -160   -169       N  
ATOM    624  CA  LYS B  36      46.136  23.385   4.109  1.00 18.60           C  
ANISOU  624  CA  LYS B  36     2649   2352   2065    283   -236   -187       C  
ATOM    625  C   LYS B  36      46.343  24.169   5.410  1.00 17.60           C  
ANISOU  625  C   LYS B  36     2438   2272   1979    260   -220   -158       C  
ATOM    626  O   LYS B  36      46.220  25.398   5.448  1.00 14.77           O  
ANISOU  626  O   LYS B  36     2069   1931   1613    261   -241   -154       O  
ATOM    627  CB  LYS B  36      44.743  22.757   4.077  1.00 26.10           C  
ANISOU  627  CB  LYS B  36     3577   3277   3062    271   -310   -247       C  
ATOM    628  CG  LYS B  36      43.609  23.696   4.446  1.00 35.01           C  
ANISOU  628  CG  LYS B  36     4631   4400   4269    257   -382   -297       C  
ATOM    629  CD  LYS B  36      43.240  24.609   3.293  1.00 42.10           C  
ANISOU  629  CD  LYS B  36     5611   5247   5137    294   -508   -316       C  
ATOM    630  CE  LYS B  36      42.162  25.602   3.716  1.00 43.58           C  
ANISOU  630  CE  LYS B  36     5690   5410   5459    290   -597   -378       C  
ATOM    631  NZ  LYS B  36      41.923  26.664   2.696  1.00 45.20           N  
ANISOU  631  NZ  LYS B  36     5997   5546   5630    329   -758   -384       N  
ATOM    632  N   LYS B  37      46.665  23.455   6.479  1.00 13.49           N  
ANISOU  632  N   LYS B  37     1887   1752   1488    233   -194   -135       N  
ATOM    633  CA  LYS B  37      46.836  24.111   7.769  1.00 18.33           C  
ANISOU  633  CA  LYS B  37     2475   2381   2109    195   -191   -107       C  
ATOM    634  C   LYS B  37      48.102  24.957   7.766  1.00 18.47           C  
ANISOU  634  C   LYS B  37     2475   2410   2134    223   -188    -60       C  
ATOM    635  O   LYS B  37      48.135  26.028   8.369  1.00 15.68           O  
ANISOU  635  O   LYS B  37     2104   2079   1774    206   -194    -45       O  
ATOM    636  CB  LYS B  37      46.855  23.076   8.909  1.00 22.73           C  
ANISOU  636  CB  LYS B  37     3078   2896   2662    144   -190    -92       C  
ATOM    637  CG  LYS B  37      45.487  22.428   9.109  1.00 29.64           C  
ANISOU  637  CG  LYS B  37     3966   3750   3548     89   -150   -156       C  
ATOM    638  CD  LYS B  37      45.385  21.677  10.418  1.00 41.23           C  
ANISOU  638  CD  LYS B  37     5537   5154   4975      5   -118   -146       C  
ATOM    639  CE  LYS B  37      46.013  20.314  10.311  1.00 44.93           C  
ANISOU  639  CE  LYS B  37     6064   5577   5431     26   -164   -111       C  
ATOM    640  NZ  LYS B  37      45.798  19.527  11.556  1.00 47.79           N  
ANISOU  640  NZ  LYS B  37     6584   5849   5726    -70   -147   -101       N  
ATOM    641  N   ASP B  38      49.131  24.504   7.059  1.00 16.63           N  
ANISOU  641  N   ASP B  38     2236   2147   1936    262   -161    -53       N  
ATOM    642  CA  ASP B  38      50.377  25.269   6.991  1.00 16.95           C  
ANISOU  642  CA  ASP B  38     2231   2174   2036    283   -131    -34       C  
ATOM    643  C   ASP B  38      50.183  26.536   6.173  1.00 19.77           C  
ANISOU  643  C   ASP B  38     2620   2559   2332    287    -85    -45       C  
ATOM    644  O   ASP B  38      50.760  27.576   6.478  1.00 17.53           O  
ANISOU  644  O   ASP B  38     2302   2285   2072    285    -73    -28       O  
ATOM    645  CB  ASP B  38      51.507  24.446   6.382  1.00 17.47           C  
ANISOU  645  CB  ASP B  38     2260   2169   2208    312    -74    -57       C  
ATOM    646  CG  ASP B  38      52.041  23.379   7.326  1.00 24.90           C  
ANISOU  646  CG  ASP B  38     3158   3050   3253    319   -164    -40       C  
ATOM    647  OD1 ASP B  38      51.727  23.411   8.537  1.00 25.36           O  
ANISOU  647  OD1 ASP B  38     3251   3110   3275    291   -269      0       O  
ATOM    648  OD2 ASP B  38      52.783  22.504   6.844  1.00 27.45           O  
ANISOU  648  OD2 ASP B  38     3435   3301   3693    345   -130    -73       O  
ATOM    649  N   GLU B  39      49.382  26.443   5.117  1.00 14.09           N  
ANISOU  649  N   GLU B  39     1988   1835   1533    290    -80    -74       N  
ATOM    650  CA  GLU B  39      49.096  27.622   4.315  1.00 13.84           C  
ANISOU  650  CA  GLU B  39     2039   1797   1422    290    -81    -81       C  
ATOM    651  C   GLU B  39      48.295  28.644   5.110  1.00 15.74           C  
ANISOU  651  C   GLU B  39     2228   2085   1669    282   -162    -73       C  
ATOM    652  O   GLU B  39      48.549  29.850   5.018  1.00 16.06           O  
ANISOU  652  O   GLU B  39     2284   2132   1687    282   -156    -59       O  
ATOM    653  CB  GLU B  39      48.350  27.248   3.040  1.00 13.68           C  
ANISOU  653  CB  GLU B  39     2165   1724   1308    294   -117   -114       C  
ATOM    654  CG  GLU B  39      48.030  28.436   2.164  1.00 24.49           C  
ANISOU  654  CG  GLU B  39     3681   3048   2576    290   -165   -117       C  
ATOM    655  CD  GLU B  39      49.270  29.114   1.583  1.00 30.41           C  
ANISOU  655  CD  GLU B  39     4526   3753   3274    265    -14   -108       C  
ATOM    656  OE1 GLU B  39      50.399  28.604   1.763  1.00 27.14           O  
ANISOU  656  OE1 GLU B  39     4036   3333   2942    256    134   -115       O  
ATOM    657  OE2 GLU B  39      49.108  30.170   0.938  1.00 30.95           O  
ANISOU  657  OE2 GLU B  39     4748   3773   3239    251    -44   -103       O  
ATOM    658  N   ARG B  40      47.325  28.161   5.882  1.00 14.52           N  
ANISOU  658  N   ARG B  40     2013   1949   1554    266   -215    -93       N  
ATOM    659  CA  ARG B  40      46.544  29.037   6.753  1.00 15.86           C  
ANISOU  659  CA  ARG B  40     2120   2143   1762    241   -248   -109       C  
ATOM    660  C   ARG B  40      47.447  29.746   7.748  1.00 15.53           C  
ANISOU  660  C   ARG B  40     2044   2132   1723    222   -208    -62       C  
ATOM    661  O   ARG B  40      47.324  30.961   7.950  1.00 14.17           O  
ANISOU  661  O   ARG B  40     1854   1977   1553    218   -218    -61       O  
ATOM    662  CB  ARG B  40      45.468  28.254   7.511  1.00 14.77           C  
ANISOU  662  CB  ARG B  40     1933   1992   1686    201   -247   -159       C  
ATOM    663  CG  ARG B  40      44.642  29.120   8.472  1.00 15.09           C  
ANISOU  663  CG  ARG B  40     1908   2030   1794    153   -226   -204       C  
ATOM    664  CD  ARG B  40      43.894  28.279   9.505  1.00 28.01           C  
ANISOU  664  CD  ARG B  40     3531   3633   3479     76   -147   -256       C  
ATOM    665  NE  ARG B  40      43.140  27.194   8.894  1.00 48.66           N  
ANISOU  665  NE  ARG B  40     6128   6210   6150     84   -167   -312       N  
ATOM    666  CZ  ARG B  40      43.056  25.967   9.402  1.00 55.00           C  
ANISOU  666  CZ  ARG B  40     6973   6988   6936     37   -105   -318       C  
ATOM    667  NH1 ARG B  40      42.351  25.036   8.771  1.00 54.55           N  
ANISOU  667  NH1 ARG B  40     6890   6895   6940     48   -127   -374       N  
ATOM    668  NH2 ARG B  40      43.676  25.671  10.540  1.00 51.53           N  
ANISOU  668  NH2 ARG B  40     6626   6541   6413    -24    -40   -268       N  
ATOM    669  N   ASP B  41      48.342  28.985   8.378  1.00 18.44           N  
ANISOU  669  N   ASP B  41     2409   2491   2105    213   -189    -27       N  
ATOM    670  CA  ASP B  41      49.273  29.558   9.352  1.00 14.48           C  
ANISOU  670  CA  ASP B  41     1888   1989   1624    198   -198     15       C  
ATOM    671  C   ASP B  41      50.135  30.632   8.709  1.00 11.48           C  
ANISOU  671  C   ASP B  41     1482   1618   1262    230   -169     28       C  
ATOM    672  O   ASP B  41      50.359  31.685   9.297  1.00 10.85           O  
ANISOU  672  O   ASP B  41     1382   1556   1186    216   -179     46       O  
ATOM    673  CB  ASP B  41      50.175  28.479   9.962  1.00 12.56           C  
ANISOU  673  CB  ASP B  41     1654   1693   1426    197   -240     43       C  
ATOM    674  CG  ASP B  41      49.439  27.574  10.933  1.00 20.31           C  
ANISOU  674  CG  ASP B  41     2714   2643   2360    140   -267     42       C  
ATOM    675  OD1 ASP B  41      48.301  27.903  11.318  1.00 19.35           O  
ANISOU  675  OD1 ASP B  41     2620   2539   2192     89   -221      9       O  
ATOM    676  OD2 ASP B  41      50.004  26.522  11.302  1.00 21.81           O  
ANISOU  676  OD2 ASP B  41     2943   2771   2574    141   -326     63       O  
ATOM    677  N   ARG B  42      50.608  30.357   7.490  1.00 12.24           N  
ANISOU  677  N   ARG B  42     1597   1688   1363    260   -112     12       N  
ATOM    678  CA  ARG B  42      51.487  31.271   6.778  1.00 10.56           C  
ANISOU  678  CA  ARG B  42     1393   1456   1165    268    -35      9       C  
ATOM    679  C   ARG B  42      50.803  32.616   6.520  1.00 10.31           C  
ANISOU  679  C   ARG B  42     1415   1453   1051    261    -55     13       C  
ATOM    680  O   ARG B  42      51.385  33.682   6.737  1.00 11.59           O  
ANISOU  680  O   ARG B  42     1553   1618   1231    255    -28     27       O  
ATOM    681  CB  ARG B  42      51.942  30.647   5.457  1.00 14.80           C  
ANISOU  681  CB  ARG B  42     1999   1931   1694    274     71    -26       C  
ATOM    682  CG  ARG B  42      52.913  31.506   4.672  1.00 21.37           C  
ANISOU  682  CG  ARG B  42     2871   2707   2540    257    210    -49       C  
ATOM    683  CD  ARG B  42      53.203  30.894   3.301  1.00 28.88           C  
ANISOU  683  CD  ARG B  42     3957   3572   3444    235    353    -98       C  
ATOM    684  NE  ARG B  42      52.082  31.031   2.370  1.00 25.62           N  
ANISOU  684  NE  ARG B  42     3754   3147   2835    225    293    -92       N  
ATOM    685  CZ  ARG B  42      51.769  32.158   1.730  1.00 23.60           C  
ANISOU  685  CZ  ARG B  42     3664   2858   2446    202    282    -83       C  
ATOM    686  NH1 ARG B  42      52.486  33.267   1.917  1.00 25.96           N  
ANISOU  686  NH1 ARG B  42     3939   3150   2776    182    364    -78       N  
ATOM    687  NH2 ARG B  42      50.736  32.181   0.897  1.00 23.63           N  
ANISOU  687  NH2 ARG B  42     3868   2816   2295    201    167    -82       N  
ATOM    688  N   VAL B  43      49.555  32.564   6.076  1.00 10.35           N  
ANISOU  688  N   VAL B  43     1482   1460    990    266   -122     -7       N  
ATOM    689  CA  VAL B  43      48.823  33.778   5.757  1.00 12.21           C  
ANISOU  689  CA  VAL B  43     1766   1691   1180    269   -184    -15       C  
ATOM    690  C   VAL B  43      48.460  34.551   7.042  1.00 12.94           C  
ANISOU  690  C   VAL B  43     1752   1833   1331    251   -214    -10       C  
ATOM    691  O   VAL B  43      48.626  35.781   7.114  1.00 11.91           O  
ANISOU  691  O   VAL B  43     1625   1709   1192    250   -217      2       O  
ATOM    692  CB  VAL B  43      47.568  33.445   4.922  1.00 11.27           C  
ANISOU  692  CB  VAL B  43     1727   1525   1031    285   -294    -55       C  
ATOM    693  CG1 VAL B  43      46.668  34.646   4.796  1.00 16.74           C  
ANISOU  693  CG1 VAL B  43     2434   2189   1739    297   -412    -77       C  
ATOM    694  CG2 VAL B  43      47.999  32.963   3.531  1.00 12.06           C  
ANISOU  694  CG2 VAL B  43     2006   1551   1024    287   -261    -56       C  
ATOM    695  N   GLN B  44      47.989  33.840   8.062  1.00  9.62           N  
ANISOU  695  N   GLN B  44     1264   1432    957    226   -219    -23       N  
ATOM    696  CA  GLN B  44      47.694  34.487   9.342  1.00 13.33           C  
ANISOU  696  CA  GLN B  44     1680   1924   1460    184   -210    -28       C  
ATOM    697  C   GLN B  44      48.940  35.115   9.956  1.00  9.16           C  
ANISOU  697  C   GLN B  44     1146   1412    922    176   -188     26       C  
ATOM    698  O   GLN B  44      48.870  36.173  10.590  1.00  9.69           O  
ANISOU  698  O   GLN B  44     1196   1492    993    153   -187     29       O  
ATOM    699  CB  GLN B  44      47.087  33.480  10.317  1.00 12.70           C  
ANISOU  699  CB  GLN B  44     1595   1830   1401    132   -185    -55       C  
ATOM    700  CG  GLN B  44      45.656  33.119   9.963  1.00 11.39           C  
ANISOU  700  CG  GLN B  44     1391   1634   1304    125   -194   -137       C  
ATOM    701  CD  GLN B  44      45.018  32.146  10.947  1.00 14.70           C  
ANISOU  701  CD  GLN B  44     1819   2020   1748     51   -121   -180       C  
ATOM    702  OE1 GLN B  44      45.561  31.878  12.027  1.00 10.25           O  
ANISOU  702  OE1 GLN B  44     1329   1447   1118     -6    -75   -143       O  
ATOM    703  NE2 GLN B  44      43.848  31.620  10.578  1.00 11.58           N  
ANISOU  703  NE2 GLN B  44     1368   1583   1451     45   -118   -266       N  
ATOM    704  N   LYS B  45      50.078  34.461   9.772  1.00  9.30           N  
ANISOU  704  N   LYS B  45     1164   1413    957    194   -176     56       N  
ATOM    705  CA  LYS B  45      51.320  34.972  10.342  1.00 12.24           C  
ANISOU  705  CA  LYS B  45     1500   1771   1378    192   -182     89       C  
ATOM    706  C   LYS B  45      51.626  36.343   9.764  1.00 12.45           C  
ANISOU  706  C   LYS B  45     1518   1811   1399    204   -139     90       C  
ATOM    707  O   LYS B  45      52.030  37.245  10.482  1.00 10.70           O  
ANISOU  707  O   LYS B  45     1270   1597   1200    188   -156    108       O  
ATOM    708  CB  LYS B  45      52.495  34.020  10.085  1.00  9.94           C  
ANISOU  708  CB  LYS B  45     1171   1427   1181    218   -178     92       C  
ATOM    709  CG  LYS B  45      53.726  34.341  10.936  1.00 12.42           C  
ANISOU  709  CG  LYS B  45     1422   1689   1609    217   -241    111       C  
ATOM    710  CD  LYS B  45      54.946  33.508  10.525  1.00 13.75           C  
ANISOU  710  CD  LYS B  45     1500   1773   1951    251   -235     83       C  
ATOM    711  CE  LYS B  45      56.134  33.826  11.435  1.00 12.59           C  
ANISOU  711  CE  LYS B  45     1268   1542   1972    257   -351     87       C  
ATOM    712  NZ  LYS B  45      57.396  33.164  10.993  1.00 13.90           N  
ANISOU  712  NZ  LYS B  45     1292   1594   2394    294   -339     29       N  
ATOM    713  N   LYS B  46      51.433  36.496   8.459  1.00  9.55           N  
ANISOU  713  N   LYS B  46     1208   1432    990    225    -91     72       N  
ATOM    714  CA  LYS B  46      51.682  37.778   7.818  1.00  9.87           C  
ANISOU  714  CA  LYS B  46     1294   1460    996    225    -49     74       C  
ATOM    715  C   LYS B  46      50.705  38.828   8.334  1.00  9.47           C  
ANISOU  715  C   LYS B  46     1240   1444    917    218   -121     74       C  
ATOM    716  O   LYS B  46      51.106  39.936   8.709  1.00 10.88           O  
ANISOU  716  O   LYS B  46     1396   1632   1106    208   -108     89       O  
ATOM    717  CB  LYS B  46      51.582  37.648   6.291  1.00 10.36           C  
ANISOU  717  CB  LYS B  46     1498   1465    973    231      3     54       C  
ATOM    718  CG  LYS B  46      52.666  36.769   5.698  1.00 13.50           C  
ANISOU  718  CG  LYS B  46     1901   1807   1419    222    130     33       C  
ATOM    719  CD  LYS B  46      52.351  36.318   4.259  1.00 16.45           C  
ANISOU  719  CD  LYS B  46     2467   2109   1673    211    182      8       C  
ATOM    720  CE  LYS B  46      52.187  37.496   3.325  1.00 17.72           C  
ANISOU  720  CE  LYS B  46     2828   2206   1697    184    201     11       C  
ATOM    721  NZ  LYS B  46      52.085  37.014   1.904  1.00 18.62           N  
ANISOU  721  NZ  LYS B  46     3197   2210   1667    152    261    -14       N  
ATOM    722  N   THR B  47      49.422  38.479   8.357  1.00  9.80           N  
ANISOU  722  N   THR B  47     1285   1488    951    222   -189     44       N  
ATOM    723  CA  THR B  47      48.396  39.420   8.795  1.00 10.87           C  
ANISOU  723  CA  THR B  47     1386   1627   1118    215   -245     14       C  
ATOM    724  C   THR B  47      48.664  39.902  10.213  1.00 13.44           C  
ANISOU  724  C   THR B  47     1645   1987   1474    172   -207     25       C  
ATOM    725  O   THR B  47      48.677  41.106  10.508  1.00 11.10           O  
ANISOU  725  O   THR B  47     1334   1697   1188    164   -209     27       O  
ATOM    726  CB  THR B  47      46.992  38.784   8.754  1.00 11.32           C  
ANISOU  726  CB  THR B  47     1409   1655   1236    217   -306    -51       C  
ATOM    727  OG1 THR B  47      46.693  38.381   7.408  1.00 14.13           O  
ANISOU  727  OG1 THR B  47     1856   1958   1554    257   -382    -61       O  
ATOM    728  CG2 THR B  47      45.948  39.804   9.211  1.00 15.02           C  
ANISOU  728  CG2 THR B  47     1803   2098   1805    206   -347   -111       C  
ATOM    729  N   PHE B  48      48.889  38.941  11.099  1.00  9.53           N  
ANISOU  729  N   PHE B  48     1140   1498    981    138   -184     33       N  
ATOM    730  CA  PHE B  48      49.017  39.238  12.515  1.00  8.83           C  
ANISOU  730  CA  PHE B  48     1059   1409    888     78   -165     41       C  
ATOM    731  C   PHE B  48      50.329  39.960  12.836  1.00  9.65           C  
ANISOU  731  C   PHE B  48     1161   1517    988     83   -184     94       C  
ATOM    732  O   PHE B  48      50.388  40.778  13.758  1.00  8.82           O  
ANISOU  732  O   PHE B  48     1072   1409    871     42   -184     99       O  
ATOM    733  CB  PHE B  48      48.912  37.942  13.327  1.00  9.10           C  
ANISOU  733  CB  PHE B  48     1149   1413    896     30   -159     40       C  
ATOM    734  CG  PHE B  48      47.538  37.302  13.289  1.00  9.35           C  
ANISOU  734  CG  PHE B  48     1172   1425    956      1   -110    -32       C  
ATOM    735  CD1 PHE B  48      46.466  37.931  12.661  1.00 11.55           C  
ANISOU  735  CD1 PHE B  48     1372   1700   1318     22   -104   -100       C  
ATOM    736  CD2 PHE B  48      47.323  36.067  13.881  1.00 10.71           C  
ANISOU  736  CD2 PHE B  48     1414   1558   1096    -50    -84    -41       C  
ATOM    737  CE1 PHE B  48      45.211  37.338  12.627  1.00  9.98           C  
ANISOU  737  CE1 PHE B  48     1127   1457   1206     -3    -68   -189       C  
ATOM    738  CE2 PHE B  48      46.065  35.464  13.853  1.00 12.24           C  
ANISOU  738  CE2 PHE B  48     1586   1721   1345    -87    -15   -123       C  
ATOM    739  CZ  PHE B  48      45.010  36.102  13.228  1.00 11.90           C  
ANISOU  739  CZ  PHE B  48     1427   1672   1422    -62     -4   -205       C  
ATOM    740  N   THR B  49      51.385  39.651  12.091  1.00 10.27           N  
ANISOU  740  N   THR B  49     1216   1586   1098    127   -188    120       N  
ATOM    741  CA  THR B  49      52.649  40.361  12.279  1.00  9.06           C  
ANISOU  741  CA  THR B  49     1024   1416   1002    133   -195    145       C  
ATOM    742  C   THR B  49      52.466  41.845  11.950  1.00 12.93           C  
ANISOU  742  C   THR B  49     1511   1931   1471    134   -158    142       C  
ATOM    743  O   THR B  49      52.899  42.727  12.711  1.00  8.88           O  
ANISOU  743  O   THR B  49      982   1417    976    112   -178    156       O  
ATOM    744  CB  THR B  49      53.775  39.753  11.420  1.00 10.02           C  
ANISOU  744  CB  THR B  49     1097   1496   1215    169   -157    140       C  
ATOM    745  OG1 THR B  49      54.045  38.410  11.867  1.00 11.17           O  
ANISOU  745  OG1 THR B  49     1234   1603   1408    172   -221    143       O  
ATOM    746  CG2 THR B  49      55.047  40.609  11.529  1.00 15.12           C  
ANISOU  746  CG2 THR B  49     1668   2102   1976    170   -140    138       C  
ATOM    747  N   LYS B  50      51.814  42.124  10.824  1.00 10.04           N  
ANISOU  747  N   LYS B  50     1183   1571   1062    159   -127    124       N  
ATOM    748  CA  LYS B  50      51.611  43.506  10.401  1.00  9.19           C  
ANISOU  748  CA  LYS B  50     1103   1462    928    163   -118    122       C  
ATOM    749  C   LYS B  50      50.709  44.239  11.389  1.00  8.71           C  
ANISOU  749  C   LYS B  50     1011   1423    876    138   -156    104       C  
ATOM    750  O   LYS B  50      50.927  45.416  11.678  1.00 11.37           O  
ANISOU  750  O   LYS B  50     1338   1764   1218    127   -151    112       O  
ATOM    751  CB  LYS B  50      51.027  43.558   8.992  1.00 12.44           C  
ANISOU  751  CB  LYS B  50     1615   1834   1276    191   -128    107       C  
ATOM    752  CG  LYS B  50      52.085  43.252   7.921  1.00 14.18           C  
ANISOU  752  CG  LYS B  50     1914   2005   1467    189    -29    114       C  
ATOM    753  CD  LYS B  50      51.477  42.781   6.597  1.00 25.12           C  
ANISOU  753  CD  LYS B  50     3458   3330   2755    202    -50    100       C  
ATOM    754  CE  LYS B  50      52.576  42.356   5.609  1.00 32.91           C  
ANISOU  754  CE  LYS B  50     4546   4249   3711    174    106     89       C  
ATOM    755  NZ  LYS B  50      52.010  41.930   4.288  1.00 27.64           N  
ANISOU  755  NZ  LYS B  50     4098   3497   2906    170     85     78       N  
ATOM    756  N   TRP B  51      49.715  43.537  11.930  1.00  8.97           N  
ANISOU  756  N   TRP B  51     1029   1457    923    117   -171     68       N  
ATOM    757  CA  TRP B  51      48.799  44.154  12.889  1.00 11.15           C  
ANISOU  757  CA  TRP B  51     1276   1726   1233     72   -155     22       C  
ATOM    758  C   TRP B  51      49.538  44.478  14.179  1.00 11.10           C  
ANISOU  758  C   TRP B  51     1299   1724   1194     14   -130     52       C  
ATOM    759  O   TRP B  51      49.404  45.564  14.724  1.00  8.76           O  
ANISOU  759  O   TRP B  51      996   1425    906    -14   -110     39       O  
ATOM    760  CB  TRP B  51      47.602  43.247  13.172  1.00 10.07           C  
ANISOU  760  CB  TRP B  51     1119   1563   1145     43   -131    -46       C  
ATOM    761  CG  TRP B  51      46.555  43.880  14.036  1.00  9.44           C  
ANISOU  761  CG  TRP B  51      996   1445   1147    -17    -65   -130       C  
ATOM    762  CD1 TRP B  51      45.493  44.617  13.614  1.00 10.04           C  
ANISOU  762  CD1 TRP B  51      980   1476   1358      6    -90   -211       C  
ATOM    763  CD2 TRP B  51      46.467  43.831  15.474  1.00 13.32           C  
ANISOU  763  CD2 TRP B  51     1548   1910   1604   -120     42   -155       C  
ATOM    764  NE1 TRP B  51      44.749  45.041  14.687  1.00 10.52           N  
ANISOU  764  NE1 TRP B  51     1001   1489   1507    -75     26   -300       N  
ATOM    765  CE2 TRP B  51      45.319  44.560  15.841  1.00 12.78           C  
ANISOU  765  CE2 TRP B  51     1404   1786   1666   -164    126   -265       C  
ATOM    766  CE3 TRP B  51      47.233  43.222  16.477  1.00 12.11           C  
ANISOU  766  CE3 TRP B  51     1529   1745   1326   -187     62   -101       C  
ATOM    767  CZ2 TRP B  51      44.921  44.716  17.169  1.00 14.50           C  
ANISOU  767  CZ2 TRP B  51     1691   1943   1874   -287    282   -328       C  
ATOM    768  CZ3 TRP B  51      46.835  43.376  17.806  1.00 10.65           C  
ANISOU  768  CZ3 TRP B  51     1456   1495   1097   -308    176   -148       C  
ATOM    769  CH2 TRP B  51      45.691  44.116  18.136  1.00 17.76           C  
ANISOU  769  CH2 TRP B  51     2292   2346   2109   -364    311   -263       C  
ATOM    770  N   VAL B  52      50.327  43.530  14.667  1.00 10.66           N  
ANISOU  770  N   VAL B  52     1288   1658   1105     -3   -155     91       N  
ATOM    771  CA  VAL B  52      51.065  43.759  15.896  1.00  9.04           C  
ANISOU  771  CA  VAL B  52     1150   1421    865    -57   -190    122       C  
ATOM    772  C   VAL B  52      52.030  44.940  15.695  1.00 11.27           C  
ANISOU  772  C   VAL B  52     1380   1716   1186    -27   -217    152       C  
ATOM    773  O   VAL B  52      52.166  45.799  16.570  1.00  9.11           O  
ANISOU  773  O   VAL B  52     1145   1427    890    -73   -226    156       O  
ATOM    774  CB  VAL B  52      51.831  42.487  16.339  1.00 12.88           C  
ANISOU  774  CB  VAL B  52     1700   1858   1337    -66   -273    159       C  
ATOM    775  CG1 VAL B  52      52.872  42.815  17.401  1.00 14.11           C  
ANISOU  775  CG1 VAL B  52     1928   1948   1484   -100   -384    198       C  
ATOM    776  CG2 VAL B  52      50.851  41.433  16.864  1.00 10.43           C  
ANISOU  776  CG2 VAL B  52     1489   1515    959   -126   -231    128       C  
ATOM    777  N   ASN B  53      52.660  45.014  14.527  1.00  8.77           N  
ANISOU  777  N   ASN B  53      992   1416    924     36   -206    165       N  
ATOM    778  CA  ASN B  53      53.664  46.053  14.306  1.00 10.20           C  
ANISOU  778  CA  ASN B  53     1126   1590   1159     52   -200    181       C  
ATOM    779  C   ASN B  53      53.050  47.432  14.176  1.00 12.48           C  
ANISOU  779  C   ASN B  53     1421   1906   1416     45   -161    169       C  
ATOM    780  O   ASN B  53      53.693  48.442  14.496  1.00 12.87           O  
ANISOU  780  O   ASN B  53     1451   1947   1491     33   -163    181       O  
ATOM    781  CB  ASN B  53      54.515  45.734  13.073  1.00 11.27           C  
ANISOU  781  CB  ASN B  53     1212   1705   1363     95   -145    177       C  
ATOM    782  CG  ASN B  53      55.621  44.768  13.394  1.00 12.74           C  
ANISOU  782  CG  ASN B  53     1339   1834   1667    103   -196    177       C  
ATOM    783  OD1 ASN B  53      56.018  44.638  14.553  1.00 12.46           O  
ANISOU  783  OD1 ASN B  53     1308   1761   1666     81   -313    193       O  
ATOM    784  ND2 ASN B  53      56.109  44.064  12.385  1.00 11.16           N  
ANISOU  784  ND2 ASN B  53     1101   1605   1536    131   -123    153       N  
ATOM    785  N   LYS B  54      51.800  47.477  13.730  1.00 12.48           N  
ANISOU  785  N   LYS B  54     1437   1920   1384     55   -143    137       N  
ATOM    786  CA  LYS B  54      51.066  48.737  13.666  1.00 13.46           C  
ANISOU  786  CA  LYS B  54     1555   2044   1514     54   -137    111       C  
ATOM    787  C   LYS B  54      50.996  49.375  15.042  1.00 16.23           C  
ANISOU  787  C   LYS B  54     1910   2393   1864     -8   -122     99       C  
ATOM    788  O   LYS B  54      51.010  50.600  15.168  1.00 16.00           O  
ANISOU  788  O   LYS B  54     1868   2362   1847    -14   -113     95       O  
ATOM    789  CB  LYS B  54      49.648  48.523  13.121  1.00 16.77           C  
ANISOU  789  CB  LYS B  54     1965   2444   1964     75   -160     55       C  
ATOM    790  CG  LYS B  54      48.809  49.796  13.086  1.00 24.19           C  
ANISOU  790  CG  LYS B  54     2874   3352   2964     81   -184      9       C  
ATOM    791  CD  LYS B  54      47.343  49.546  12.722  1.00 30.14           C  
ANISOU  791  CD  LYS B  54     3574   4049   3827    103   -236    -75       C  
ATOM    792  CE  LYS B  54      46.602  48.839  13.839  1.00 35.46           C  
ANISOU  792  CE  LYS B  54     4190   4715   4568     36   -144   -146       C  
ATOM    793  NZ  LYS B  54      45.109  48.915  13.686  1.00 30.10           N  
ANISOU  793  NZ  LYS B  54     3403   3953   4081     44   -165   -268       N  
ATOM    794  N   HIS B  55      50.912  48.539  16.073  1.00 10.69           N  
ANISOU  794  N   HIS B  55     1258   1675   1130    -64   -117     94       N  
ATOM    795  CA  HIS B  55      50.823  49.034  17.441  1.00  9.09           C  
ANISOU  795  CA  HIS B  55     1128   1439    885   -148    -92     79       C  
ATOM    796  C   HIS B  55      52.186  49.127  18.117  1.00 15.03           C  
ANISOU  796  C   HIS B  55     1937   2165   1608   -165   -182    140       C  
ATOM    797  O   HIS B  55      52.462  50.100  18.816  1.00 12.52           O  
ANISOU  797  O   HIS B  55     1656   1828   1271   -205   -189    143       O  
ATOM    798  CB  HIS B  55      49.877  48.148  18.252  1.00 12.21           C  
ANISOU  798  CB  HIS B  55     1610   1789   1241   -228    -22     27       C  
ATOM    799  CG  HIS B  55      48.463  48.196  17.765  1.00 17.58           C  
ANISOU  799  CG  HIS B  55     2201   2463   2017   -221     66    -64       C  
ATOM    800  ND1 HIS B  55      47.638  49.277  17.990  1.00 14.69           N  
ANISOU  800  ND1 HIS B  55     1777   2069   1736   -248    141   -140       N  
ATOM    801  CD2 HIS B  55      47.731  47.302  17.061  1.00 19.33           C  
ANISOU  801  CD2 HIS B  55     2364   2684   2298   -188     72   -102       C  
ATOM    802  CE1 HIS B  55      46.456  49.045  17.447  1.00 18.30           C  
ANISOU  802  CE1 HIS B  55     2128   2495   2329   -227    176   -230       C  
ATOM    803  NE2 HIS B  55      46.485  47.853  16.878  1.00 20.55           N  
ANISOU  803  NE2 HIS B  55     2417   2798   2592   -191    131   -206       N  
ATOM    804  N   LEU B  56      53.051  48.136  17.902  1.00 10.01           N  
ANISOU  804  N   LEU B  56     1296   1513    994   -133   -265    178       N  
ATOM    805  CA  LEU B  56      54.353  48.148  18.575  1.00 10.06           C  
ANISOU  805  CA  LEU B  56     1332   1457   1033   -142   -396    217       C  
ATOM    806  C   LEU B  56      55.209  49.350  18.176  1.00  9.98           C  
ANISOU  806  C   LEU B  56     1215   1460   1117   -107   -398    224       C  
ATOM    807  O   LEU B  56      56.057  49.777  18.951  1.00 12.73           O  
ANISOU  807  O   LEU B  56     1589   1748   1502   -130   -504    240       O  
ATOM    808  CB  LEU B  56      55.126  46.862  18.301  1.00 12.96           C  
ANISOU  808  CB  LEU B  56     1671   1781   1473   -102   -492    236       C  
ATOM    809  CG  LEU B  56      54.695  45.632  19.114  1.00 12.51           C  
ANISOU  809  CG  LEU B  56     1774   1662   1316   -156   -556    244       C  
ATOM    810  CD1 LEU B  56      55.638  44.463  18.825  1.00 13.18           C  
ANISOU  810  CD1 LEU B  56     1807   1687   1514   -103   -684    262       C  
ATOM    811  CD2 LEU B  56      54.657  45.925  20.637  1.00 11.88           C  
ANISOU  811  CD2 LEU B  56     1919   1487   1108   -258   -641    258       C  
ATOM    812  N   ILE B  57      54.986  49.894  16.981  1.00 11.41           N  
ANISOU  812  N   ILE B  57     1301   1699   1333    -58   -293    210       N  
ATOM    813  CA  ILE B  57      55.782  51.044  16.540  1.00 12.08           C  
ANISOU  813  CA  ILE B  57     1312   1784   1496    -38   -264    212       C  
ATOM    814  C   ILE B  57      55.616  52.211  17.520  1.00 13.74           C  
ANISOU  814  C   ILE B  57     1570   1988   1661    -87   -286    213       C  
ATOM    815  O   ILE B  57      56.544  53.000  17.729  1.00 14.56           O  
ANISOU  815  O   ILE B  57     1631   2063   1840    -90   -319    219       O  
ATOM    816  CB  ILE B  57      55.394  51.496  15.104  1.00 18.62           C  
ANISOU  816  CB  ILE B  57     2114   2648   2313      3   -148    200       C  
ATOM    817  CG1 ILE B  57      56.444  52.447  14.532  1.00 28.32           C  
ANISOU  817  CG1 ILE B  57     3290   3846   3625      9    -87    196       C  
ATOM    818  CG2 ILE B  57      54.022  52.127  15.076  1.00 13.69           C  
ANISOU  818  CG2 ILE B  57     1538   2057   1604     -4   -125    184       C  
ATOM    819  CD1 ILE B  57      57.733  51.757  14.125  1.00 39.87           C  
ANISOU  819  CD1 ILE B  57     4664   5246   5240     21    -60    175       C  
ATOM    820  N   LYS B  58      54.443  52.292  18.151  1.00 14.64           N  
ANISOU  820  N   LYS B  58     1773   2118   1673   -133   -253    195       N  
ATOM    821  CA  LYS B  58      54.160  53.359  19.112  1.00 17.70           C  
ANISOU  821  CA  LYS B  58     2225   2488   2012   -194   -240    181       C  
ATOM    822  C   LYS B  58      54.970  53.204  20.399  1.00 19.59           C  
ANISOU  822  C   LYS B  58     2582   2647   2214   -255   -366    206       C  
ATOM    823  O   LYS B  58      55.046  54.135  21.210  1.00 17.84           O  
ANISOU  823  O   LYS B  58     2433   2393   1951   -309   -378    202       O  
ATOM    824  CB  LYS B  58      52.665  53.401  19.428  1.00 16.61           C  
ANISOU  824  CB  LYS B  58     2137   2355   1818   -240   -134    124       C  
ATOM    825  CG  LYS B  58      51.798  53.498  18.185  1.00 19.73           C  
ANISOU  825  CG  LYS B  58     2425   2793   2277   -173    -76     92       C  
ATOM    826  CD  LYS B  58      50.327  53.616  18.529  1.00 21.39           C  
ANISOU  826  CD  LYS B  58     2633   2977   2516   -216     17      6       C  
ATOM    827  CE  LYS B  58      49.505  53.770  17.250  1.00 30.08           C  
ANISOU  827  CE  LYS B  58     3628   4088   3714   -136      3    -28       C  
ATOM    828  NZ  LYS B  58      48.069  54.062  17.520  1.00 35.52           N  
ANISOU  828  NZ  LYS B  58     4256   4722   4520   -165     75   -140       N  
ATOM    829  N   ALA B  59      55.571  52.030  20.576  1.00 15.34           N  
ANISOU  829  N   ALA B  59     2079   2058   1693   -247   -481    230       N  
ATOM    830  CA  ALA B  59      56.447  51.750  21.706  1.00 16.49           C  
ANISOU  830  CA  ALA B  59     2355   2087   1823   -293   -674    257       C  
ATOM    831  C   ALA B  59      57.874  51.532  21.216  1.00 12.48           C  
ANISOU  831  C   ALA B  59     1683   1532   1525   -217   -813    268       C  
ATOM    832  O   ALA B  59      58.695  50.949  21.920  1.00 13.64           O  
ANISOU  832  O   ALA B  59     1897   1557   1729   -226  -1029    282       O  
ATOM    833  CB  ALA B  59      55.951  50.523  22.494  1.00 17.05           C  
ANISOU  833  CB  ALA B  59     2639   2083   1755   -359   -729    265       C  
ATOM    834  N   GLN B  60      58.153  52.014  20.007  1.00 13.28           N  
ANISOU  834  N   GLN B  60     2407   1012   1628   -657     42    285       N  
ATOM    835  CA  GLN B  60      59.462  51.879  19.375  1.00 14.01           C  
ANISOU  835  CA  GLN B  60     2403   1167   1753   -748    112    351       C  
ATOM    836  C   GLN B  60      59.925  50.427  19.327  1.00 15.86           C  
ANISOU  836  C   GLN B  60     2495   1544   1989   -729    148    348       C  
ATOM    837  O   GLN B  60      61.112  50.133  19.482  1.00 16.82           O  
ANISOU  837  O   GLN B  60     2495   1732   2163   -818    179    372       O  
ATOM    838  CB  GLN B  60      60.509  52.755  20.087  1.00 15.18           C  
ANISOU  838  CB  GLN B  60     2503   1283   1981   -864     85    344       C  
ATOM    839  CG  GLN B  60      60.211  54.247  19.997  1.00 22.35           C  
ANISOU  839  CG  GLN B  60     3541   2057   2893   -876     61    350       C  
ATOM    840  CD  GLN B  60      59.157  54.665  21.000  1.00 20.04           C  
ANISOU  840  CD  GLN B  60     3346   1690   2577   -808    -23    266       C  
ATOM    841  OE1 GLN B  60      59.229  54.290  22.158  1.00 18.97           O  
ANISOU  841  OE1 GLN B  60     3163   1587   2458   -819    -77    198       O  
ATOM    842  NE2 GLN B  60      58.161  55.411  20.552  1.00 22.32           N  
ANISOU  842  NE2 GLN B  60     3768   1890   2825   -724    -31    270       N  
ATOM    843  N   ARG B  61      58.983  49.521  19.079  1.00 12.33           N  
ANISOU  843  N   ARG B  61     2048   1147   1490   -600    142    313       N  
ATOM    844  CA  ARG B  61      59.316  48.114  18.929  1.00 11.43           C  
ANISOU  844  CA  ARG B  61     1813   1158   1373   -553    174    302       C  
ATOM    845  C   ARG B  61      58.801  47.601  17.581  1.00 12.07           C  
ANISOU  845  C   ARG B  61     1942   1266   1379   -461    225    329       C  
ATOM    846  O   ARG B  61      57.965  48.236  16.943  1.00 13.77           O  
ANISOU  846  O   ARG B  61     2278   1412   1542   -415    214    345       O  
ATOM    847  CB  ARG B  61      58.746  47.310  20.106  1.00 13.07           C  
ANISOU  847  CB  ARG B  61     1968   1403   1595   -498    106    225       C  
ATOM    848  CG  ARG B  61      59.499  47.602  21.438  1.00 14.37           C  
ANISOU  848  CG  ARG B  61     2072   1567   1819   -588     55    198       C  
ATOM    849  CD  ARG B  61      58.756  47.074  22.652  1.00 24.62           C  
ANISOU  849  CD  ARG B  61     3363   2880   3109   -529    -12    128       C  
ATOM    850  NE  ARG B  61      59.591  47.096  23.858  1.00 27.42           N  
ANISOU  850  NE  ARG B  61     3655   3259   3504   -603    -64    104       N  
ATOM    851  CZ  ARG B  61      60.277  46.046  24.310  1.00 27.72           C  
ANISOU  851  CZ  ARG B  61     3574   3392   3565   -601    -71    102       C  
ATOM    852  NH1 ARG B  61      60.225  44.893  23.655  1.00 27.49           N  
ANISOU  852  NH1 ARG B  61     3485   3432   3527   -528    -22    120       N  
ATOM    853  NH2 ARG B  61      61.015  46.146  25.417  1.00 23.68           N  
ANISOU  853  NH2 ARG B  61     3013   2902   3083   -665   -135     81       N  
ATOM    854  N   HIS B  62      59.310  46.454  17.153  1.00 11.09           N  
ANISOU  854  N   HIS B  62     1729   1239   1245   -428    276    332       N  
ATOM    855  CA  HIS B  62      58.972  45.903  15.845  1.00 11.17           C  
ANISOU  855  CA  HIS B  62     1791   1280   1175   -344    325    350       C  
ATOM    856  C   HIS B  62      59.289  44.407  15.824  1.00 17.34           C  
ANISOU  856  C   HIS B  62     2474   2158   1958   -286    347    315       C  
ATOM    857  O   HIS B  62      60.357  43.990  16.274  1.00 15.65           O  
ANISOU  857  O   HIS B  62     2142   2003   1800   -329    382    324       O  
ATOM    858  CB  HIS B  62      59.750  46.634  14.745  1.00 16.05           C  
ANISOU  858  CB  HIS B  62     2457   1886   1757   -397    421    438       C  
ATOM    859  CG  HIS B  62      59.468  46.129  13.365  1.00 17.69           C  
ANISOU  859  CG  HIS B  62     2737   2126   1858   -308    475    458       C  
ATOM    860  ND1 HIS B  62      58.418  46.595  12.605  1.00 22.27           N  
ANISOU  860  ND1 HIS B  62     3462   2645   2354   -242    437    467       N  
ATOM    861  CD2 HIS B  62      60.094  45.193  12.612  1.00 16.25           C  
ANISOU  861  CD2 HIS B  62     2510   2030   1634   -265    558    467       C  
ATOM    862  CE1 HIS B  62      58.420  45.983  11.431  1.00 22.05           C  
ANISOU  862  CE1 HIS B  62     3483   2665   2229   -171    489    479       C  
ATOM    863  NE2 HIS B  62      59.427  45.129  11.411  1.00 18.22           N  
ANISOU  863  NE2 HIS B  62     2890   2268   1766   -182    569    477       N  
ATOM    864  N   ILE B  63      58.352  43.617  15.309  1.00 10.89           N  
ANISOU  864  N   ILE B  63     1705   1349   1084   -187    319    274       N  
ATOM    865  CA  ILE B  63      58.506  42.173  15.151  1.00 13.84           C  
ANISOU  865  CA  ILE B  63     2019   1789   1450   -121    334    235       C  
ATOM    866  C   ILE B  63      59.008  41.820  13.765  1.00 10.67           C  
ANISOU  866  C   ILE B  63     1659   1427    969    -76    423    264       C  
ATOM    867  O   ILE B  63      58.444  42.293  12.774  1.00 14.58           O  
ANISOU  867  O   ILE B  63     2271   1890   1379    -44    426    283       O  
ATOM    868  CB  ILE B  63      57.149  41.438  15.357  1.00 16.74           C  
ANISOU  868  CB  ILE B  63     2420   2136   1805    -47    246    167       C  
ATOM    869  CG1 ILE B  63      56.574  41.733  16.733  1.00 31.77           C  
ANISOU  869  CG1 ILE B  63     4288   4010   3775    -78    173    139       C  
ATOM    870  CG2 ILE B  63      57.303  39.936  15.135  1.00 27.38           C  
ANISOU  870  CG2 ILE B  63     3727   3531   3145     15    258    126       C  
ATOM    871  CD1 ILE B  63      57.525  41.428  17.844  1.00 17.10           C  
ANISOU  871  CD1 ILE B  63     2323   2187   1986   -130    183    139       C  
ATOM    872  N   SER B  64      60.040  40.977  13.670  1.00 13.19           N  
ANISOU  872  N   SER B  64     1890   1817   1306    -61    495    267       N  
ATOM    873  CA  SER B  64      60.455  40.443  12.367  1.00 16.29           C  
ANISOU  873  CA  SER B  64     2327   2252   1609      7    588    279       C  
ATOM    874  C   SER B  64      59.887  39.050  12.128  1.00 17.39           C  
ANISOU  874  C   SER B  64     2494   2400   1713    110    548    201       C  
ATOM    875  O   SER B  64      59.476  38.721  11.024  1.00 19.82           O  
ANISOU  875  O   SER B  64     2909   2703   1918    180    561    181       O  
ATOM    876  CB  SER B  64      61.981  40.387  12.240  1.00 21.48           C  
ANISOU  876  CB  SER B  64     2872   2987   2302    -24    711    332       C  
ATOM    877  OG  SER B  64      62.540  41.680  12.150  1.00 26.99           O  
ANISOU  877  OG  SER B  64     3563   3674   3020   -127    764    413       O  
ATOM    878  N   ASP B  65      59.882  38.230  13.172  1.00 11.17           N  
ANISOU  878  N   ASP B  65     1618   1619   1008    115    496    157       N  
ATOM    879  CA  ASP B  65      59.411  36.858  13.075  1.00 13.75           C  
ANISOU  879  CA  ASP B  65     1967   1938   1321    199    456     87       C  
ATOM    880  C   ASP B  65      58.478  36.593  14.241  1.00 14.80           C  
ANISOU  880  C   ASP B  65     2073   2027   1524    174    345     49       C  
ATOM    881  O   ASP B  65      58.926  36.473  15.377  1.00 14.45           O  
ANISOU  881  O   ASP B  65     1932   1997   1561    138    332     58       O  
ATOM    882  CB  ASP B  65      60.588  35.877  13.086  1.00 18.59           C  
ANISOU  882  CB  ASP B  65     2496   2607   1960    250    535     84       C  
ATOM    883  CG  ASP B  65      60.154  34.410  12.972  1.00 20.90           C  
ANISOU  883  CG  ASP B  65     2830   2872   2240    339    495      9       C  
ATOM    884  OD1 ASP B  65      58.951  34.093  13.076  1.00 14.08           O  
ANISOU  884  OD1 ASP B  65     2034   1947   1367    341    398    -40       O  
ATOM    885  OD2 ASP B  65      61.036  33.554  12.789  1.00 21.83           O  
ANISOU  885  OD2 ASP B  65     2907   3025   2364    407    562     -1       O  
ATOM    886  N   LEU B  66      57.186  36.479  13.954  1.00 11.86           N  
ANISOU  886  N   LEU B  66     1782   1606   1116    195    265      7       N  
ATOM    887  CA  LEU B  66      56.185  36.296  15.005  1.00  9.52           C  
ANISOU  887  CA  LEU B  66     1458   1274    885    170    173    -22       C  
ATOM    888  C   LEU B  66      56.407  35.062  15.895  1.00  9.30           C  
ANISOU  888  C   LEU B  66     1362   1248    924    183    158    -49       C  
ATOM    889  O   LEU B  66      55.965  35.053  17.049  1.00 10.58           O  
ANISOU  889  O   LEU B  66     1477   1397   1147    147    112    -50       O  
ATOM    890  CB  LEU B  66      54.790  36.221  14.381  1.00 11.36           C  
ANISOU  890  CB  LEU B  66     1774   1468   1075    198     93    -64       C  
ATOM    891  CG  LEU B  66      53.633  36.366  15.374  1.00 14.57           C  
ANISOU  891  CG  LEU B  66     2144   1847   1547    167     11    -80       C  
ATOM    892  CD1 LEU B  66      53.534  37.810  15.843  1.00 12.67           C  
ANISOU  892  CD1 LEU B  66     1898   1600   1317    126     13    -39       C  
ATOM    893  CD2 LEU B  66      52.334  35.894  14.744  1.00 18.69           C  
ANISOU  893  CD2 LEU B  66     2716   2341   2045    198    -73   -130       C  
ATOM    894  N   TYR B  67      57.093  34.042  15.377  1.00 11.17           N  
ANISOU  894  N   TYR B  67     1603   1498   1142    242    203    -68       N  
ATOM    895  CA  TYR B  67      57.316  32.801  16.135  1.00 10.56           C  
ANISOU  895  CA  TYR B  67     1480   1407   1124    268    187    -90       C  
ATOM    896  C   TYR B  67      58.612  32.827  16.924  1.00 11.28           C  
ANISOU  896  C   TYR B  67     1467   1551   1270    261    238    -46       C  
ATOM    897  O   TYR B  67      58.936  31.845  17.600  1.00 14.40           O  
ANISOU  897  O   TYR B  67     1822   1937   1712    292    225    -53       O  
ATOM    898  CB  TYR B  67      57.355  31.563  15.223  1.00  9.57           C  
ANISOU  898  CB  TYR B  67     1426   1253    957    350    198   -143       C  
ATOM    899  CG  TYR B  67      56.133  31.367  14.355  1.00 11.14           C  
ANISOU  899  CG  TYR B  67     1731   1401   1100    360    132   -198       C  
ATOM    900  CD1 TYR B  67      54.910  31.924  14.707  1.00 12.39           C  
ANISOU  900  CD1 TYR B  67     1891   1536   1279    302     52   -200       C  
ATOM    901  CD2 TYR B  67      56.215  30.635  13.174  1.00 14.47           C  
ANISOU  901  CD2 TYR B  67     2250   1802   1445    432    146   -251       C  
ATOM    902  CE1 TYR B  67      53.792  31.747  13.910  1.00 10.34           C  
ANISOU  902  CE1 TYR B  67     1711   1240    977    310    -23   -250       C  
ATOM    903  CE2 TYR B  67      55.106  30.461  12.363  1.00 15.01           C  
ANISOU  903  CE2 TYR B  67     2418   1827   1457    437     66   -306       C  
ATOM    904  CZ  TYR B  67      53.899  31.026  12.742  1.00 15.50           C  
ANISOU  904  CZ  TYR B  67     2463   1873   1554    373    -24   -303       C  
ATOM    905  OH  TYR B  67      52.797  30.859  11.953  1.00 14.32           O  
ANISOU  905  OH  TYR B  67     2394   1689   1359    377   -117   -356       O  
ATOM    906  N   GLU B  68      59.364  33.917  16.814  1.00 10.42           N  
ANISOU  906  N   GLU B  68     1313   1490   1156    220    289      1       N  
ATOM    907  CA  GLU B  68      60.572  34.089  17.630  1.00 13.94           C  
ANISOU  907  CA  GLU B  68     1640   1992   1664    195    318     44       C  
ATOM    908  C   GLU B  68      60.463  35.282  18.571  1.00 18.26           C  
ANISOU  908  C   GLU B  68     2151   2541   2246     98    276     75       C  
ATOM    909  O   GLU B  68      60.909  35.221  19.717  1.00 11.71           O  
ANISOU  909  O   GLU B  68     1246   1732   1472     70    240     89       O  
ATOM    910  CB  GLU B  68      61.811  34.273  16.744  1.00 12.80           C  
ANISOU  910  CB  GLU B  68     1449   1913   1501    221    425     77       C  
ATOM    911  CG  GLU B  68      62.328  33.008  16.084  1.00 36.20           C  
ANISOU  911  CG  GLU B  68     4419   4892   4445    333    481     49       C  
ATOM    912  CD  GLU B  68      63.042  32.088  17.057  1.00 46.65           C  
ANISOU  912  CD  GLU B  68     5643   6236   5845    376    461     52       C  
ATOM    913  OE1 GLU B  68      63.379  30.955  16.655  1.00 57.68           O  
ANISOU  913  OE1 GLU B  68     7056   7626   7234    481    495     23       O  
ATOM    914  OE2 GLU B  68      63.269  32.496  18.221  1.00 35.85           O  
ANISOU  914  OE2 GLU B  68     4193   4886   4541    312    408     83       O  
ATOM    915  N   ASP B  69      59.871  36.369  18.082  1.00 10.61           N  
ANISOU  915  N   ASP B  69     1247   1545   1238     54    274     83       N  
ATOM    916  CA  ASP B  69      60.032  37.666  18.739  1.00 10.88           C  
ANISOU  916  CA  ASP B  69     1259   1576   1300    -36    254    114       C  
ATOM    917  C   ASP B  69      59.005  37.959  19.826  1.00 10.30           C  
ANISOU  917  C   ASP B  69     1213   1457   1242    -63    170     89       C  
ATOM    918  O   ASP B  69      59.029  39.047  20.414  1.00  9.13           O  
ANISOU  918  O   ASP B  69     1068   1292   1109   -129    146    102       O  
ATOM    919  CB  ASP B  69      60.011  38.782  17.684  1.00 10.83           C  
ANISOU  919  CB  ASP B  69     1317   1553   1243    -67    301    146       C  
ATOM    920  CG  ASP B  69      61.205  38.710  16.742  1.00 19.40           C  
ANISOU  920  CG  ASP B  69     2361   2697   2315    -57    406    187       C  
ATOM    921  OD1 ASP B  69      62.226  38.102  17.124  1.00 15.55           O  
ANISOU  921  OD1 ASP B  69     1763   2268   1878    -47    436    197       O  
ATOM    922  OD2 ASP B  69      61.130  39.258  15.622  1.00 17.77           O  
ANISOU  922  OD2 ASP B  69     2230   2480   2042    -54    462    213       O  
ATOM    923  N   LEU B  70      58.120  36.997  20.096  1.00 10.73           N  
ANISOU  923  N   LEU B  70     1291   1489   1295    -14    131     52       N  
ATOM    924  CA  LEU B  70      57.195  37.069  21.237  1.00  8.96           C  
ANISOU  924  CA  LEU B  70     1076   1237   1090    -32     70     33       C  
ATOM    925  C   LEU B  70      57.589  36.100  22.358  1.00  6.26           C  
ANISOU  925  C   LEU B  70      677    917    785    -21     47     35       C  
ATOM    926  O   LEU B  70      56.994  36.122  23.433  1.00 11.65           O  
ANISOU  926  O   LEU B  70     1366   1586   1476    -37      8     28       O  
ATOM    927  CB  LEU B  70      55.758  36.767  20.804  1.00  8.86           C  
ANISOU  927  CB  LEU B  70     1126   1184   1056      1     40      0       C  
ATOM    928  CG  LEU B  70      55.179  37.674  19.713  1.00 11.31           C  
ANISOU  928  CG  LEU B  70     1506   1471   1322      7     43     -1       C  
ATOM    929  CD1 LEU B  70      53.756  37.250  19.377  1.00 13.74           C  
ANISOU  929  CD1 LEU B  70     1850   1750   1621     42     -5    -37       C  
ATOM    930  CD2 LEU B  70      55.201  39.101  20.189  1.00 10.18           C  
ANISOU  930  CD2 LEU B  70     1377   1310   1180    -41     36     18       C  
ATOM    931  N   ARG B  71      58.593  35.258  22.117  1.00  7.53           N  
ANISOU  931  N   ARG B  71      788   1110    963     15     76     48       N  
ATOM    932  CA  ARG B  71      58.922  34.196  23.062  1.00  6.72           C  
ANISOU  932  CA  ARG B  71      645   1018    891     45     50     54       C  
ATOM    933  C   ARG B  71      59.286  34.680  24.461  1.00  8.97           C  
ANISOU  933  C   ARG B  71      890   1327   1191     -1      4     73       C  
ATOM    934  O   ARG B  71      58.999  33.989  25.425  1.00 10.62           O  
ANISOU  934  O   ARG B  71     1105   1526   1405     15    -31     78       O  
ATOM    935  CB  ARG B  71      60.072  33.330  22.535  1.00  9.72           C  
ANISOU  935  CB  ARG B  71      971   1433   1290    105     91     66       C  
ATOM    936  CG  ARG B  71      59.663  32.459  21.362  1.00  7.52           C  
ANISOU  936  CG  ARG B  71      753   1117    986    172    126     35       C  
ATOM    937  CD  ARG B  71      60.822  31.528  20.954  1.00 10.47           C  
ANISOU  937  CD  ARG B  71     1079   1523   1377    253    172     42       C  
ATOM    938  NE  ARG B  71      60.525  30.864  19.689  1.00 16.19           N  
ANISOU  938  NE  ARG B  71     1879   2212   2060    318    212      2       N  
ATOM    939  CZ  ARG B  71      61.206  29.835  19.192  1.00 27.49           C  
ANISOU  939  CZ  ARG B  71     3309   3643   3493    411    254    -12       C  
ATOM    940  NH1 ARG B  71      62.236  29.330  19.857  1.00 31.37           N  
ANISOU  940  NH1 ARG B  71     3712   4172   4035    457    261     18       N  
ATOM    941  NH2 ARG B  71      60.845  29.302  18.031  1.00 29.75           N  
ANISOU  941  NH2 ARG B  71     3687   3890   3727    468    283    -59       N  
ATOM    942  N   ASP B  72      59.898  35.858  24.583  1.00  9.50           N  
ANISOU  942  N   ASP B  72      927   1420   1262    -63      0     85       N  
ATOM    943  CA  ASP B  72      60.413  36.240  25.901  1.00 10.15           C  
ANISOU  943  CA  ASP B  72      973   1528   1355   -105    -58     96       C  
ATOM    944  C   ASP B  72      59.464  37.157  26.666  1.00 10.15           C  
ANISOU  944  C   ASP B  72     1046   1489   1321   -149    -94     72       C  
ATOM    945  O   ASP B  72      59.792  37.636  27.764  1.00  9.26           O  
ANISOU  945  O   ASP B  72      929   1389   1199   -187   -147     70       O  
ATOM    946  CB  ASP B  72      61.819  36.859  25.785  1.00 12.14           C  
ANISOU  946  CB  ASP B  72     1133   1835   1645   -153    -57    120       C  
ATOM    947  CG  ASP B  72      61.834  38.271  25.196  1.00 13.48           C  
ANISOU  947  CG  ASP B  72     1328   1982   1812   -232    -35    121       C  
ATOM    948  OD1 ASP B  72      60.788  38.916  25.020  1.00 11.33           O  
ANISOU  948  OD1 ASP B  72     1149   1651   1504   -245    -33     99       O  
ATOM    949  OD2 ASP B  72      62.947  38.748  24.904  1.00 16.73           O  
ANISOU  949  OD2 ASP B  72     1659   2435   2263   -282    -18    148       O  
ATOM    950  N   GLY B  73      58.287  37.365  26.086  1.00  8.67           N  
ANISOU  950  N   GLY B  73      926   1256   1113   -134    -68     52       N  
ATOM    951  CA  GLY B  73      57.213  38.093  26.739  1.00  8.29           C  
ANISOU  951  CA  GLY B  73      944   1171   1035   -149    -89     27       C  
ATOM    952  C   GLY B  73      57.241  39.613  26.608  1.00  8.93           C  
ANISOU  952  C   GLY B  73     1066   1221   1104   -201    -96     15       C  
ATOM    953  O   GLY B  73      56.205  40.260  26.809  1.00  9.56           O  
ANISOU  953  O   GLY B  73     1210   1262   1161   -192    -99     -9       O  
ATOM    954  N   HIS B  74      58.396  40.195  26.290  1.00 10.72           N  
ANISOU  954  N   HIS B  74     1256   1463   1355   -255    -97     34       N  
ATOM    955  CA  HIS B  74      58.533  41.654  26.342  1.00  9.70           C  
ANISOU  955  CA  HIS B  74     1175   1290   1222   -321   -114     25       C  
ATOM    956  C   HIS B  74      57.700  42.384  25.295  1.00 11.68           C  
ANISOU  956  C   HIS B  74     1500   1483   1456   -306    -79     24       C  
ATOM    957  O   HIS B  74      57.064  43.394  25.599  1.00  8.19           O  
ANISOU  957  O   HIS B  74     1136    981    995   -316    -98      1       O  
ATOM    958  CB  HIS B  74      59.998  42.053  26.220  1.00 11.08           C  
ANISOU  958  CB  HIS B  74     1277   1495   1439   -399   -121     53       C  
ATOM    959  CG  HIS B  74      60.772  41.822  27.473  1.00 12.14           C  
ANISOU  959  CG  HIS B  74     1357   1672   1585   -429   -190     46       C  
ATOM    960  ND1 HIS B  74      60.492  42.488  28.649  1.00 11.72           N  
ANISOU  960  ND1 HIS B  74     1369   1587   1499   -459   -257      7       N  
ATOM    961  CD2 HIS B  74      61.776  40.960  27.768  1.00 14.21           C  
ANISOU  961  CD2 HIS B  74     1513   2008   1879   -421   -209     69       C  
ATOM    962  CE1 HIS B  74      61.308  42.073  29.597  1.00 14.91           C  
ANISOU  962  CE1 HIS B  74     1713   2043   1907   -476   -321      8       C  
ATOM    963  NE2 HIS B  74      62.094  41.140  29.090  1.00 13.36           N  
ANISOU  963  NE2 HIS B  74     1407   1914   1756   -452   -296     48       N  
ATOM    964  N   ASN B  75      57.685  41.883  24.066  1.00  7.03           N  
ANISOU  964  N   ASN B  75      897    908    867   -273    -30     47       N  
ATOM    965  CA  ASN B  75      56.884  42.529  23.037  1.00  9.53           C  
ANISOU  965  CA  ASN B  75     1291   1175   1157   -249     -9     50       C  
ATOM    966  C   ASN B  75      55.392  42.339  23.277  1.00  8.61           C  
ANISOU  966  C   ASN B  75     1218   1033   1019   -183    -32     15       C  
ATOM    967  O   ASN B  75      54.593  43.219  22.963  1.00  8.41           O  
ANISOU  967  O   ASN B  75     1263    956    976   -164    -41      8       O  
ATOM    968  CB  ASN B  75      57.301  42.025  21.649  1.00  8.43           C  
ANISOU  968  CB  ASN B  75     1136   1063   1005   -227     46     81       C  
ATOM    969  CG  ASN B  75      58.597  42.674  21.177  1.00 12.07           C  
ANISOU  969  CG  ASN B  75     1567   1535   1483   -298     89    127       C  
ATOM    970  OD1 ASN B  75      58.824  43.860  21.424  1.00 15.54           O  
ANISOU  970  OD1 ASN B  75     2042   1926   1934   -367     76    141       O  
ATOM    971  ND2 ASN B  75      59.459  41.904  20.525  1.00 12.05           N  
ANISOU  971  ND2 ASN B  75     1497   1594   1488   -284    144    152       N  
ATOM    972  N  ALEU B  76      55.004  41.207  23.853  0.61  8.04           N  
ANISOU  972  N  ALEU B  76     1103    998    956   -147    -41     -1       N  
ATOM    973  N  BLEU B  76      55.036  41.201  23.860  0.39  7.78           N  
ANISOU  973  N  BLEU B  76     1068    965    922   -148    -41     -1       N  
ATOM    974  CA ALEU B  76      53.593  40.991  24.172  0.61  7.22           C  
ANISOU  974  CA ALEU B  76     1019    880    845    -97    -56    -29       C  
ATOM    975  CA BLEU B  76      53.652  40.912  24.206  0.39  7.40           C  
ANISOU  975  CA BLEU B  76     1036    906    869    -98    -55    -28       C  
ATOM    976  C  ALEU B  76      53.122  41.957  25.247  0.61 11.36           C  
ANISOU  976  C  ALEU B  76     1583   1375   1357   -102    -74    -51       C  
ATOM    977  C  BLEU B  76      53.134  41.900  25.246  0.39 10.28           C  
ANISOU  977  C  BLEU B  76     1445   1241   1222   -102    -73    -51       C  
ATOM    978  O  ALEU B  76      52.029  42.518  25.161  0.61  7.88           O  
ANISOU  978  O  ALEU B  76     1182    905    909    -60    -77    -69       O  
ATOM    979  O  BLEU B  76      52.031  42.431  25.125  0.39  8.37           O  
ANISOU  979  O  BLEU B  76     1238    969    971    -59    -76    -68       O  
ATOM    980  CB ALEU B  76      53.348  39.559  24.636  0.61  6.59           C  
ANISOU  980  CB ALEU B  76      886    837    782    -74    -55    -32       C  
ATOM    981  CB BLEU B  76      53.535  39.485  24.732  0.39  7.74           C  
ANISOU  981  CB BLEU B  76     1025    987    929    -79    -54    -30       C  
ATOM    982  CG ALEU B  76      53.309  38.498  23.541  0.61  8.63           C  
ANISOU  982  CG ALEU B  76     1125   1105   1048    -45    -44    -29       C  
ATOM    983  CG BLEU B  76      52.155  38.845  24.780  0.39  8.01           C  
ANISOU  983  CG BLEU B  76     1052   1018    973    -38    -58    -46       C  
ATOM    984  CD1ALEU B  76      53.423  37.108  24.158  0.61  7.33           C  
ANISOU  984  CD1ALEU B  76      917    960    906    -36    -44    -25       C  
ATOM    985  CD1BLEU B  76      51.467  38.945  23.420  0.39 12.10           C  
ANISOU  985  CD1BLEU B  76     1592   1518   1489     -8    -67    -55       C  
ATOM    986  CD2ALEU B  76      52.039  38.632  22.708  0.61 10.48           C  
ANISOU  986  CD2ALEU B  76     1390   1317   1277     -9    -60    -47       C  
ATOM    987  CD2BLEU B  76      52.284  37.388  25.230  0.39  5.08           C  
ANISOU  987  CD2BLEU B  76      638    669    623    -35    -54    -36       C  
ATOM    988  N   ILE B  77      53.938  42.130  26.280  1.00  8.49           N  
ANISOU  988  N   ILE B  77     1214   1022    990   -146    -89    -55       N  
ATOM    989  CA  ILE B  77      53.589  43.089  27.328  1.00  8.51           C  
ANISOU  989  CA  ILE B  77     1276    990    967   -149   -109    -87       C  
ATOM    990  C   ILE B  77      53.493  44.503  26.734  1.00  9.70           C  
ANISOU  990  C   ILE B  77     1504   1067   1113   -161   -115    -93       C  
ATOM    991  O   ILE B  77      52.524  45.214  26.979  1.00  9.42           O  
ANISOU  991  O   ILE B  77     1528    989   1061   -112   -115   -121       O  
ATOM    992  CB  ILE B  77      54.592  43.043  28.485  1.00  9.09           C  
ANISOU  992  CB  ILE B  77     1339   1087   1026   -200   -142    -93       C  
ATOM    993  CG1 ILE B  77      54.460  41.703  29.227  1.00  6.53           C  
ANISOU  993  CG1 ILE B  77      964    824    695   -170   -137    -82       C  
ATOM    994  CG2 ILE B  77      54.349  44.181  29.461  1.00  9.35           C  
ANISOU  994  CG2 ILE B  77     1459   1072   1021   -208   -169   -136       C  
ATOM    995  CD1 ILE B  77      55.563  41.461  30.286  1.00  9.85           C  
ANISOU  995  CD1 ILE B  77     1365   1279   1097   -210   -183    -78       C  
ATOM    996  N   SER B  78      54.471  44.899  25.931  1.00  9.64           N  
ANISOU  996  N   SER B  78     1496   1043   1124   -219   -113    -62       N  
ATOM    997  CA  SER B  78      54.423  46.211  25.271  1.00 12.44           C  
ANISOU  997  CA  SER B  78     1936   1316   1475   -237   -114    -53       C  
ATOM    998  C   SER B  78      53.189  46.388  24.378  1.00  7.64           C  
ANISOU  998  C   SER B  78     1370    680    853   -153   -101    -50       C  
ATOM    999  O   SER B  78      52.567  47.464  24.366  1.00 10.39           O  
ANISOU  999  O   SER B  78     1805    953   1189   -121   -114    -64       O  
ATOM   1000  CB  SER B  78      55.682  46.431  24.439  1.00 12.42           C  
ANISOU 1000  CB  SER B  78     1911   1313   1496   -319    -96     -5       C  
ATOM   1001  OG  SER B  78      56.808  46.629  25.274  1.00 12.76           O  
ANISOU 1001  OG  SER B  78     1919   1367   1563   -407   -124     -9       O  
ATOM   1002  N   LEU B  79      52.862  45.351  23.608  1.00  8.10           N  
ANISOU 1002  N   LEU B  79     1372    793    912   -113    -84    -34       N  
ATOM   1003  CA  LEU B  79      51.647  45.363  22.785  1.00  8.17           C  
ANISOU 1003  CA  LEU B  79     1404    790    909    -33    -91    -36       C  
ATOM   1004  C   LEU B  79      50.419  45.642  23.643  1.00 10.58           C  
ANISOU 1004  C   LEU B  79     1717   1084   1218     33   -106    -76       C  
ATOM   1005  O   LEU B  79      49.580  46.476  23.291  1.00  9.44           O  
ANISOU 1005  O   LEU B  79     1629    892   1068     94   -121    -81       O  
ATOM   1006  CB  LEU B  79      51.472  44.025  22.049  1.00  6.62           C  
ANISOU 1006  CB  LEU B  79     1142    658    716     -8    -84    -29       C  
ATOM   1007  CG  LEU B  79      50.179  43.845  21.234  1.00  9.26           C  
ANISOU 1007  CG  LEU B  79     1483    993   1042     68   -112    -38       C  
ATOM   1008  CD1 LEU B  79      50.083  44.910  20.128  1.00 11.64           C  
ANISOU 1008  CD1 LEU B  79     1876   1238   1307     93   -124    -10       C  
ATOM   1009  CD2 LEU B  79      50.136  42.443  20.623  1.00 10.35           C  
ANISOU 1009  CD2 LEU B  79     1565   1183   1183     75   -115    -42       C  
ATOM   1010  N   LEU B  80      50.300  44.943  24.774  1.00 10.15           N  
ANISOU 1010  N   LEU B  80     1607   1076   1173     29    -97   -101       N  
ATOM   1011  CA  LEU B  80      49.133  45.152  25.618  1.00  8.28           C  
ANISOU 1011  CA  LEU B  80     1369    840    935     95    -90   -134       C  
ATOM   1012  C   LEU B  80      49.135  46.550  26.220  1.00  9.73           C  
ANISOU 1012  C   LEU B  80     1651    950   1096    109    -97   -162       C  
ATOM   1013  O   LEU B  80      48.081  47.151  26.347  1.00 13.35           O  
ANISOU 1013  O   LEU B  80     2137   1383   1554    191    -93   -184       O  
ATOM   1014  CB  LEU B  80      49.043  44.095  26.718  1.00  7.60           C  
ANISOU 1014  CB  LEU B  80     1216    819    852     85    -68   -144       C  
ATOM   1015  CG  LEU B  80      48.866  42.669  26.204  1.00  6.98           C  
ANISOU 1015  CG  LEU B  80     1052    796    804     77    -63   -122       C  
ATOM   1016  CD1 LEU B  80      48.925  41.694  27.382  1.00 11.54           C  
ANISOU 1016  CD1 LEU B  80     1585   1421   1380     59    -39   -119       C  
ATOM   1017  CD2 LEU B  80      47.549  42.547  25.460  1.00 10.35           C  
ANISOU 1017  CD2 LEU B  80     1442   1231   1258    137    -72   -126       C  
ATOM   1018  N   GLU B  81      50.312  47.080  26.564  1.00  9.62           N  
ANISOU 1018  N   GLU B  81     1690    898   1069     31   -111   -162       N  
ATOM   1019  CA  GLU B  81      50.389  48.425  27.124  1.00 10.50           C  
ANISOU 1019  CA  GLU B  81     1912    919   1159     31   -128   -195       C  
ATOM   1020  C   GLU B  81      49.947  49.481  26.110  1.00 10.95           C  
ANISOU 1020  C   GLU B  81     2051    889   1223     74   -138   -179       C  
ATOM   1021  O   GLU B  81      49.224  50.419  26.452  1.00 11.27           O  
ANISOU 1021  O   GLU B  81     2172    860   1250    145   -143   -212       O  
ATOM   1022  CB  GLU B  81      51.806  48.719  27.614  1.00 10.35           C  
ANISOU 1022  CB  GLU B  81     1920    877   1136    -81   -156   -197       C  
ATOM   1023  CG  GLU B  81      52.164  47.962  28.891  1.00 10.32           C  
ANISOU 1023  CG  GLU B  81     1872    942   1109   -104   -163   -223       C  
ATOM   1024  CD  GLU B  81      53.526  48.352  29.435  1.00 19.67           C  
ANISOU 1024  CD  GLU B  81     3079   2104   2291   -213   -212   -231       C  
ATOM   1025  OE1 GLU B  81      54.415  48.650  28.615  1.00 21.72           O  
ANISOU 1025  OE1 GLU B  81     3324   2339   2588   -290   -222   -193       O  
ATOM   1026  OE2 GLU B  81      53.706  48.362  30.677  1.00 18.83           O  
ANISOU 1026  OE2 GLU B  81     3002   2009   2142   -221   -240   -274       O  
ATOM   1027  N   VAL B  82      50.368  49.320  24.861  1.00 10.42           N  
ANISOU 1027  N   VAL B  82     1969    822   1168     41   -140   -125       N  
ATOM   1028  CA  VAL B  82      49.930  50.226  23.798  1.00 12.72           C  
ANISOU 1028  CA  VAL B  82     2344   1035   1453     88   -151    -96       C  
ATOM   1029  C   VAL B  82      48.418  50.150  23.578  1.00 12.29           C  
ANISOU 1029  C   VAL B  82     2268   1000   1401    220   -160   -112       C  
ATOM   1030  O   VAL B  82      47.742  51.176  23.510  1.00 13.94           O  
ANISOU 1030  O   VAL B  82     2563   1131   1605    298   -176   -122       O  
ATOM   1031  CB  VAL B  82      50.652  49.926  22.467  1.00 13.41           C  
ANISOU 1031  CB  VAL B  82     2421   1138   1536     34   -141    -31       C  
ATOM   1032  CG1 VAL B  82      49.990  50.680  21.309  1.00 12.23           C  
ANISOU 1032  CG1 VAL B  82     2358    923   1365    105   -158      6       C  
ATOM   1033  CG2 VAL B  82      52.135  50.291  22.567  1.00 12.21           C  
ANISOU 1033  CG2 VAL B  82     2289    955   1395    -96   -128     -5       C  
ATOM   1034  N   LEU B  83      47.886  48.936  23.476  1.00 12.34           N  
ANISOU 1034  N   LEU B  83     2159   1108   1421    246   -153   -115       N  
ATOM   1035  CA  LEU B  83      46.462  48.763  23.178  1.00 12.50           C  
ANISOU 1035  CA  LEU B  83     2130   1162   1458    357   -169   -126       C  
ATOM   1036  C   LEU B  83      45.557  49.304  24.286  1.00 14.57           C  
ANISOU 1036  C   LEU B  83     2396   1411   1728    440   -150   -173       C  
ATOM   1037  O   LEU B  83      44.481  49.839  24.017  1.00 12.05           O  
ANISOU 1037  O   LEU B  83     2081   1075   1422    550   -166   -180       O  
ATOM   1038  CB  LEU B  83      46.152  47.287  22.941  1.00 11.14           C  
ANISOU 1038  CB  LEU B  83     1831   1094   1309    344   -167   -122       C  
ATOM   1039  CG  LEU B  83      46.695  46.713  21.630  1.00  9.64           C  
ANISOU 1039  CG  LEU B  83     1640    920   1102    303   -189    -84       C  
ATOM   1040  CD1 LEU B  83      46.605  45.195  21.640  1.00 13.19           C  
ANISOU 1040  CD1 LEU B  83     1982   1454   1575    273   -185    -93       C  
ATOM   1041  CD2 LEU B  83      45.933  47.288  20.434  1.00 14.82           C  
ANISOU 1041  CD2 LEU B  83     2344   1545   1741    383   -240    -64       C  
ATOM   1042  N   SER B  84      46.010  49.180  25.529  1.00 12.12           N  
ANISOU 1042  N   SER B  84     2088   1112   1405    397   -116   -206       N  
ATOM   1043  CA  SER B  84      45.169  49.481  26.688  1.00 13.09           C  
ANISOU 1043  CA  SER B  84     2208   1244   1521    478    -80   -255       C  
ATOM   1044  C   SER B  84      45.453  50.828  27.346  1.00 18.46           C  
ANISOU 1044  C   SER B  84     3035   1814   2166    500    -83   -295       C  
ATOM   1045  O   SER B  84      44.590  51.395  28.019  1.00 17.36           O  
ANISOU 1045  O   SER B  84     2915   1664   2017    597    -55   -334       O  
ATOM   1046  CB  SER B  84      45.339  48.393  27.745  1.00 10.26           C  
ANISOU 1046  CB  SER B  84     1770    975   1155    430    -39   -267       C  
ATOM   1047  OG  SER B  84      46.636  48.483  28.314  1.00 12.07           O  
ANISOU 1047  OG  SER B  84     2063   1175   1349    332    -50   -274       O  
ATOM   1048  N   GLY B  85      46.672  51.327  27.182  1.00 13.49           N  
ANISOU 1048  N   GLY B  85     2496   1110   1521    399   -113   -285       N  
ATOM   1049  CA  GLY B  85      47.090  52.512  27.897  1.00 14.85           C  
ANISOU 1049  CA  GLY B  85     2783   1193   1665    378   -123   -317       C  
ATOM   1050  C   GLY B  85      47.427  52.201  29.343  1.00 14.50           C  
ANISOU 1050  C   GLY B  85     2738   1189   1583    345   -105   -367       C  
ATOM   1051  O   GLY B  85      47.635  53.110  30.137  1.00 16.67           O  
ANISOU 1051  O   GLY B  85     3091   1413   1830    337   -114   -401       O  
ATOM   1052  N   ASP B  86      47.490  50.915  29.686  1.00 14.14           N  
ANISOU 1052  N   ASP B  86     2602   1240   1530    326    -82   -367       N  
ATOM   1053  CA  ASP B  86      47.814  50.519  31.053  1.00 14.95           C  
ANISOU 1053  CA  ASP B  86     2711   1388   1580    300    -67   -406       C  
ATOM   1054  C   ASP B  86      49.304  50.275  31.225  1.00 14.45           C  
ANISOU 1054  C   ASP B  86     2656   1325   1511    160   -118   -394       C  
ATOM   1055  O   ASP B  86      50.029  50.079  30.254  1.00 15.21           O  
ANISOU 1055  O   ASP B  86     2711   1418   1652     84   -143   -344       O  
ATOM   1056  CB  ASP B  86      47.046  49.255  31.459  1.00 15.40           C  
ANISOU 1056  CB  ASP B  86     2641   1571   1639    343     -8   -388       C  
ATOM   1057  CG  ASP B  86      45.577  49.514  31.691  1.00 17.01           C  
ANISOU 1057  CG  ASP B  86     2824   1794   1844    480     52   -412       C  
ATOM   1058  OD1 ASP B  86      45.202  50.684  31.928  1.00 15.53           O  
ANISOU 1058  OD1 ASP B  86     2718   1538   1643    540     52   -444       O  
ATOM   1059  OD2 ASP B  86      44.799  48.543  31.632  1.00 14.51           O  
ANISOU 1059  OD2 ASP B  86     2381   1572   1559    510     98   -382       O  
ATOM   1060  N   SER B  87      49.739  50.279  32.480  1.00 14.84           N  
ANISOU 1060  N   SER B  87     2743   1391   1505    133   -130   -432       N  
ATOM   1061  CA  SER B  87      51.087  49.876  32.843  1.00 12.98           C  
ANISOU 1061  CA  SER B  87     2492   1178   1260     14   -186   -424       C  
ATOM   1062  C   SER B  87      51.049  48.435  33.353  1.00 16.10           C  
ANISOU 1062  C   SER B  87     2788   1694   1636     18   -158   -397       C  
ATOM   1063  O   SER B  87      50.259  48.114  34.236  1.00 14.92           O  
ANISOU 1063  O   SER B  87     2648   1589   1432     93   -111   -419       O  
ATOM   1064  CB  SER B  87      51.647  50.829  33.900  1.00 19.45           C  
ANISOU 1064  CB  SER B  87     3390   1955   2044    -20   -229   -466       C  
ATOM   1065  OG  SER B  87      53.006  50.558  34.173  1.00 35.44           O  
ANISOU 1065  OG  SER B  87     5386   4004   4077   -136   -295   -455       O  
ATOM   1066  N   LEU B  88      51.865  47.560  32.774  1.00 12.37           N  
ANISOU 1066  N   LEU B  88     2216   1274   1209    -54   -178   -342       N  
ATOM   1067  CA  LEU B  88      51.910  46.164  33.215  1.00  9.34           C  
ANISOU 1067  CA  LEU B  88     1742    991    815    -51   -156   -307       C  
ATOM   1068  C   LEU B  88      53.211  45.891  33.947  1.00 11.40           C  
ANISOU 1068  C   LEU B  88     2002   1280   1050   -130   -224   -307       C  
ATOM   1069  O   LEU B  88      54.216  46.546  33.680  1.00 11.78           O  
ANISOU 1069  O   LEU B  88     2067   1285   1123   -210   -285   -314       O  
ATOM   1070  CB  LEU B  88      51.776  45.202  32.023  1.00 11.28           C  
ANISOU 1070  CB  LEU B  88     1874   1279   1132    -52   -128   -247       C  
ATOM   1071  CG  LEU B  88      50.372  44.789  31.569  1.00  9.67           C  
ANISOU 1071  CG  LEU B  88     1625   1097    952     29    -66   -235       C  
ATOM   1072  CD1 LEU B  88      49.581  46.017  31.112  1.00 13.36           C  
ANISOU 1072  CD1 LEU B  88     2157   1494   1425     87    -57   -266       C  
ATOM   1073  CD2 LEU B  88      50.453  43.769  30.437  1.00 11.87           C  
ANISOU 1073  CD2 LEU B  88     1808   1412   1292     11    -60   -186       C  
ATOM   1074  N   PRO B  89      53.207  44.912  34.863  1.00 13.15           N  
ANISOU 1074  N   PRO B  89     2200   1574   1224   -110   -217   -292       N  
ATOM   1075  CA  PRO B  89      54.479  44.481  35.443  1.00 14.87           C  
ANISOU 1075  CA  PRO B  89     2395   1830   1424   -176   -292   -280       C  
ATOM   1076  C   PRO B  89      55.368  43.886  34.360  1.00 13.13           C  
ANISOU 1076  C   PRO B  89     2060   1635   1295   -230   -308   -225       C  
ATOM   1077  O   PRO B  89      54.885  43.537  33.272  1.00 11.77           O  
ANISOU 1077  O   PRO B  89     1833   1461   1180   -207   -253   -194       O  
ATOM   1078  CB  PRO B  89      54.078  43.392  36.454  1.00 16.47           C  
ANISOU 1078  CB  PRO B  89     2595   2103   1560   -123   -263   -256       C  
ATOM   1079  CG  PRO B  89      52.603  43.407  36.519  1.00 17.08           C  
ANISOU 1079  CG  PRO B  89     2696   2177   1618    -42   -166   -264       C  
ATOM   1080  CD  PRO B  89      52.076  44.073  35.300  1.00 14.73           C  
ANISOU 1080  CD  PRO B  89     2375   1825   1395    -32   -138   -273       C  
ATOM   1081  N   ARG B  90      56.650  43.739  34.662  1.00 13.55           N  
ANISOU 1081  N   ARG B  90     2075   1717   1357   -295   -384   -215       N  
ATOM   1082  CA  ARG B  90      57.579  43.205  33.677  1.00 14.11           C  
ANISOU 1082  CA  ARG B  90     2030   1820   1512   -338   -390   -164       C  
ATOM   1083  C   ARG B  90      58.794  42.640  34.402  1.00 19.89           C  
ANISOU 1083  C   ARG B  90     2703   2614   2239   -373   -470   -147       C  
ATOM   1084  O   ARG B  90      59.403  43.338  35.206  1.00 20.66           O  
ANISOU 1084  O   ARG B  90     2843   2703   2303   -426   -555   -184       O  
ATOM   1085  CB  ARG B  90      57.976  44.314  32.684  1.00 18.01           C  
ANISOU 1085  CB  ARG B  90     2527   2253   2064   -405   -392   -171       C  
ATOM   1086  CG  ARG B  90      58.859  43.883  31.541  1.00 20.22           C  
ANISOU 1086  CG  ARG B  90     2693   2566   2425   -444   -372   -117       C  
ATOM   1087  CD  ARG B  90      59.321  45.097  30.726  1.00 17.95           C  
ANISOU 1087  CD  ARG B  90     2423   2213   2182   -525   -373   -116       C  
ATOM   1088  NE  ARG B  90      58.217  45.811  30.085  1.00 17.08           N  
ANISOU 1088  NE  ARG B  90     2405   2026   2058   -486   -322   -130       N  
ATOM   1089  CZ  ARG B  90      57.825  45.613  28.826  1.00 20.43           C  
ANISOU 1089  CZ  ARG B  90     2808   2445   2508   -453   -256    -94       C  
ATOM   1090  NH1 ARG B  90      58.430  44.704  28.069  1.00 12.77           N  
ANISOU 1090  NH1 ARG B  90     1737   1539   1575   -453   -223    -47       N  
ATOM   1091  NH2 ARG B  90      56.822  46.316  28.317  1.00 16.72           N  
ANISOU 1091  NH2 ARG B  90     2424   1905   2022   -411   -227   -106       N  
ATOM   1092  N   GLU B  91      59.115  41.373  34.143  1.00 12.86           N  
ANISOU 1092  N   GLU B  91     1721   1784   1380   -338   -452    -94       N  
ATOM   1093  CA  GLU B  91      60.322  40.730  34.687  1.00 14.18           C  
ANISOU 1093  CA  GLU B  91     1813   2018   1556   -353   -529    -66       C  
ATOM   1094  C   GLU B  91      61.572  41.119  33.916  1.00 17.49           C  
ANISOU 1094  C   GLU B  91     2125   2457   2065   -428   -561    -51       C  
ATOM   1095  O   GLU B  91      61.604  41.006  32.695  1.00 18.05           O  
ANISOU 1095  O   GLU B  91     2138   2521   2201   -428   -490    -24       O  
ATOM   1096  CB  GLU B  91      60.189  39.209  34.642  1.00 21.56           C  
ANISOU 1096  CB  GLU B  91     2699   2996   2498   -276   -492    -12       C  
ATOM   1097  CG  GLU B  91      59.006  38.661  35.395  1.00 31.19           C  
ANISOU 1097  CG  GLU B  91     4007   4204   3642   -212   -450     -9       C  
ATOM   1098  CD  GLU B  91      59.277  38.529  36.874  1.00 41.16           C  
ANISOU 1098  CD  GLU B  91     5331   5498   4810   -199   -524    -12       C  
ATOM   1099  OE1 GLU B  91      60.398  38.878  37.307  1.00 32.97           O  
ANISOU 1099  OE1 GLU B  91     4264   4492   3771   -241   -626    -22       O  
ATOM   1100  OE2 GLU B  91      58.369  38.066  37.599  1.00 45.09           O  
ANISOU 1100  OE2 GLU B  91     5905   5993   5234   -148   -481      0       O  
ATOM   1101  N   LYS B  92      62.616  41.526  34.626  1.00 18.57           N  
ANISOU 1101  N   LYS B  92     2229   2621   2204   -487   -662    -64       N  
ATOM   1102  CA  LYS B  92      63.846  41.952  33.966  1.00 20.44           C  
ANISOU 1102  CA  LYS B  92     2350   2876   2540   -552   -668    -49       C  
ATOM   1103  C   LYS B  92      64.895  40.835  33.845  1.00 21.12           C  
ANISOU 1103  C   LYS B  92     2293   3050   2683   -510   -681      2       C  
ATOM   1104  O   LYS B  92      65.896  40.998  33.146  1.00 18.17           O  
ANISOU 1104  O   LYS B  92     1804   2704   2395   -548   -663     23       O  
ATOM   1105  CB  LYS B  92      64.445  43.142  34.712  1.00 25.35           C  
ANISOU 1105  CB  LYS B  92     3011   3463   3158   -621   -739   -100       C  
ATOM   1106  CG  LYS B  92      63.484  44.294  34.934  1.00 37.08           C  
ANISOU 1106  CG  LYS B  92     4648   4853   4589   -644   -728   -155       C  
ATOM   1107  CD  LYS B  92      63.042  44.894  33.621  1.00 52.88           C  
ANISOU 1107  CD  LYS B  92     6660   6792   6639   -680   -648   -139       C  
ATOM   1108  CE  LYS B  92      62.122  46.085  33.845  1.00 64.42           C  
ANISOU 1108  CE  LYS B  92     8275   8150   8052   -687   -639   -194       C  
ATOM   1109  NZ  LYS B  92      61.789  46.783  32.571  1.00 68.98           N  
ANISOU 1109  NZ  LYS B  92     8873   8658   8677   -722   -571   -174       N  
ATOM   1110  N   GLY B  93      64.676  39.714  34.533  1.00 19.90           N  
ANISOU 1110  N   GLY B  93     2148   2935   2477   -427   -707     22       N  
ATOM   1111  CA  GLY B  93      65.579  38.569  34.448  1.00 18.43           C  
ANISOU 1111  CA  GLY B  93     1844   2820   2341   -363   -718     70       C  
ATOM   1112  C   GLY B  93      65.712  37.999  33.041  1.00 18.10           C  
ANISOU 1112  C   GLY B  93     1705   2797   2376   -337   -623    113       C  
ATOM   1113  O   GLY B  93      64.817  38.152  32.212  1.00 16.59           O  
ANISOU 1113  O   GLY B  93     1563   2561   2178   -340   -542    111       O  
ATOM   1114  N   ARG B  94      66.827  37.332  32.763  1.00 17.44           N  
ANISOU 1114  N   ARG B  94     1497   2770   2360   -294   -621    142       N  
ATOM   1115  CA  ARG B  94      67.132  36.943  31.383  1.00 18.60           C  
ANISOU 1115  CA  ARG B  94     1553   2937   2577   -267   -519    173       C  
ATOM   1116  C   ARG B  94      67.060  35.440  31.123  1.00 21.24           C  
ANISOU 1116  C   ARG B  94     1861   3293   2917   -141   -483    210       C  
ATOM   1117  O   ARG B  94      67.319  34.986  30.013  1.00 21.98           O  
ANISOU 1117  O   ARG B  94     1892   3401   3058    -97   -394    229       O  
ATOM   1118  CB  ARG B  94      68.526  37.447  31.011  1.00 17.62           C  
ANISOU 1118  CB  ARG B  94     1302   2857   2537   -315   -515    175       C  
ATOM   1119  CG  ARG B  94      68.713  38.939  31.183  1.00 17.47           C  
ANISOU 1119  CG  ARG B  94     1306   2804   2527   -443   -547    141       C  
ATOM   1120  CD  ARG B  94      70.179  39.321  31.032  1.00 21.63           C  
ANISOU 1120  CD  ARG B  94     1694   3383   3142   -491   -560    145       C  
ATOM   1121  NE  ARG B  94      70.993  38.803  32.131  1.00 20.56           N  
ANISOU 1121  NE  ARG B  94     1498   3303   3011   -450   -667    134       N  
ATOM   1122  CZ  ARG B  94      72.316  38.910  32.201  1.00 21.21           C  
ANISOU 1122  CZ  ARG B  94     1441   3447   3171   -473   -701    133       C  
ATOM   1123  NH1 ARG B  94      72.994  39.523  31.234  1.00 20.00           N  
ANISOU 1123  NH1 ARG B  94     1193   3308   3099   -542   -625    147       N  
ATOM   1124  NH2 ARG B  94      72.968  38.415  33.248  1.00 22.00           N  
ANISOU 1124  NH2 ARG B  94     1496   3598   3266   -427   -810    120       N  
ATOM   1125  N   MET B  95      66.734  34.663  32.148  1.00 15.86           N  
ANISOU 1125  N   MET B  95     1238   2605   2182    -78   -546    221       N  
ATOM   1126  CA  MET B  95      66.695  33.207  32.014  1.00 18.36           C  
ANISOU 1126  CA  MET B  95     1549   2922   2506     44   -521    259       C  
ATOM   1127  C   MET B  95      65.344  32.685  31.509  1.00 15.13           C  
ANISOU 1127  C   MET B  95     1259   2430   2057     80   -436    251       C  
ATOM   1128  O   MET B  95      64.372  33.434  31.428  1.00 15.89           O  
ANISOU 1128  O   MET B  95     1445   2480   2115     17   -408    218       O  
ATOM   1129  CB  MET B  95      67.032  32.572  33.360  1.00 20.31           C  
ANISOU 1129  CB  MET B  95     1827   3178   2711     98   -619    275       C  
ATOM   1130  CG  MET B  95      68.269  33.173  34.005  1.00 26.70           C  
ANISOU 1130  CG  MET B  95     2557   4041   3547     58   -706    252       C  
ATOM   1131  SD  MET B  95      69.752  32.865  33.033  1.00 46.01           S  
ANISOU 1131  SD  MET B  95     4825   6545   6113     97   -663    260       S  
ATOM   1132  CE  MET B  95      70.146  34.497  32.415  1.00 55.17           C  
ANISOU 1132  CE  MET B  95     5920   7722   7320    -51   -634    225       C  
ATOM   1133  N   ARG B  96      65.274  31.397  31.163  1.00 14.56           N  
ANISOU 1133  N   ARG B  96     1198   2331   2001    182   -397    275       N  
ATOM   1134  CA  ARG B  96      64.004  30.851  30.696  1.00 18.56           C  
ANISOU 1134  CA  ARG B  96     1820   2750   2480    203   -327    260       C  
ATOM   1135  C   ARG B  96      62.921  31.001  31.769  1.00 16.55           C  
ANISOU 1135  C   ARG B  96     1681   2454   2153    166   -358    260       C  
ATOM   1136  O   ARG B  96      61.763  31.259  31.453  1.00 16.83           O  
ANISOU 1136  O   ARG B  96     1792   2437   2166    131   -307    234       O  
ATOM   1137  CB  ARG B  96      64.133  29.375  30.291  1.00 16.53           C  
ANISOU 1137  CB  ARG B  96     1573   2455   2252    315   -295    283       C  
ATOM   1138  CG  ARG B  96      62.793  28.795  29.847  1.00 23.17           C  
ANISOU 1138  CG  ARG B  96     2532   3199   3073    318   -238    265       C  
ATOM   1139  CD  ARG B  96      62.914  27.440  29.167  1.00 23.73           C  
ANISOU 1139  CD  ARG B  96     2624   3213   3178    418   -201    271       C  
ATOM   1140  NE  ARG B  96      61.597  26.868  28.896  1.00 24.30           N  
ANISOU 1140  NE  ARG B  96     2810   3187   3236    402   -168    254       N  
ATOM   1141  CZ  ARG B  96      60.903  27.056  27.775  1.00 25.69           C  
ANISOU 1141  CZ  ARG B  96     3018   3328   3415    375   -115    206       C  
ATOM   1142  NH1 ARG B  96      61.391  27.813  26.799  1.00 26.87           N  
ANISOU 1142  NH1 ARG B  96     3110   3528   3571    366    -77    176       N  
ATOM   1143  NH2 ARG B  96      59.707  26.489  27.632  1.00 23.44           N  
ANISOU 1143  NH2 ARG B  96     2823   2958   3127    354   -102    193       N  
ATOM   1144  N   PHE B  97      63.308  30.845  33.033  1.00 15.67           N  
ANISOU 1144  N   PHE B  97     1579   2372   2002    180   -441    289       N  
ATOM   1145  CA  PHE B  97      62.379  31.054  34.148  1.00 19.06           C  
ANISOU 1145  CA  PHE B  97     2120   2776   2345    150   -463    292       C  
ATOM   1146  C   PHE B  97      61.687  32.420  34.049  1.00 17.97           C  
ANISOU 1146  C   PHE B  97     2018   2631   2179     60   -441    238       C  
ATOM   1147  O   PHE B  97      60.470  32.535  34.219  1.00 16.02           O  
ANISOU 1147  O   PHE B  97     1858   2339   1890     44   -392    225       O  
ATOM   1148  CB  PHE B  97      63.122  30.929  35.484  1.00 24.67           C  
ANISOU 1148  CB  PHE B  97     2834   3537   3004    173   -571    325       C  
ATOM   1149  CG  PHE B  97      62.265  31.215  36.688  1.00 21.40           C  
ANISOU 1149  CG  PHE B  97     2543   3107   2481    148   -590    326       C  
ATOM   1150  CD1 PHE B  97      62.111  32.509  37.161  1.00 25.60           C  
ANISOU 1150  CD1 PHE B  97     3106   3661   2960     74   -622    276       C  
ATOM   1151  CD2 PHE B  97      61.621  30.183  37.355  1.00 32.14           C  
ANISOU 1151  CD2 PHE B  97     3996   4425   3789    200   -568    380       C  
ATOM   1152  CE1 PHE B  97      61.320  32.769  38.265  1.00 32.12           C  
ANISOU 1152  CE1 PHE B  97     4053   4476   3675     65   -627    272       C  
ATOM   1153  CE2 PHE B  97      60.832  30.438  38.466  1.00 31.32           C  
ANISOU 1153  CE2 PHE B  97     4007   4316   3577    181   -566    388       C  
ATOM   1154  CZ  PHE B  97      60.681  31.731  38.918  1.00 33.08           C  
ANISOU 1154  CZ  PHE B  97     4259   4570   3740    120   -593    330       C  
ATOM   1155  N   HIS B  98      62.463  33.457  33.760  1.00 13.93           N  
ANISOU 1155  N   HIS B  98     1436   2161   1695      4   -474    209       N  
ATOM   1156  CA  HIS B  98      61.910  34.802  33.660  1.00 18.30           C  
ANISOU 1156  CA  HIS B  98     2034   2694   2225    -76   -461    160       C  
ATOM   1157  C   HIS B  98      61.069  34.999  32.404  1.00 18.46           C  
ANISOU 1157  C   HIS B  98     2070   2666   2279    -85   -365    139       C  
ATOM   1158  O   HIS B  98      60.061  35.702  32.444  1.00 15.22           O  
ANISOU 1158  O   HIS B  98     1733   2216   1834   -114   -336    108       O  
ATOM   1159  CB  HIS B  98      63.034  35.835  33.706  1.00 19.25           C  
ANISOU 1159  CB  HIS B  98     2079   2861   2375   -148   -530    141       C  
ATOM   1160  CG  HIS B  98      63.938  35.673  34.885  1.00 18.61           C  
ANISOU 1160  CG  HIS B  98     1970   2836   2266   -142   -647    156       C  
ATOM   1161  ND1 HIS B  98      65.151  35.024  34.807  1.00 18.40           N  
ANISOU 1161  ND1 HIS B  98     1820   2872   2298   -104   -693    193       N  
ATOM   1162  CD2 HIS B  98      63.793  36.047  36.180  1.00 18.41           C  
ANISOU 1162  CD2 HIS B  98     2028   2816   2150   -159   -729    137       C  
ATOM   1163  CE1 HIS B  98      65.718  35.014  36.003  1.00 20.79           C  
ANISOU 1163  CE1 HIS B  98     2143   3198   2557    -92   -785    184       C  
ATOM   1164  NE2 HIS B  98      64.921  35.642  36.848  1.00 17.67           N  
ANISOU 1164  NE2 HIS B  98     1874   2773   2067   -127   -812    152       N  
ATOM   1165  N   LYS B  99      61.473  34.402  31.284  1.00 13.48           N  
ANISOU 1165  N   LYS B  99     1374   2038   1710    -51   -317    154       N  
ATOM   1166  CA  LYS B  99      60.663  34.489  30.078  1.00 12.54           C  
ANISOU 1166  CA  LYS B  99     1282   1874   1608    -50   -238    134       C  
ATOM   1167  C   LYS B  99      59.276  33.867  30.283  1.00 11.44           C  
ANISOU 1167  C   LYS B  99     1227   1682   1439    -23   -207    131       C  
ATOM   1168  O   LYS B  99      58.272  34.423  29.841  1.00  9.62           O  
ANISOU 1168  O   LYS B  99     1041   1416   1197    -45   -171    103       O  
ATOM   1169  CB  LYS B  99      61.370  33.807  28.910  1.00 15.13           C  
ANISOU 1169  CB  LYS B  99     1541   2217   1990     -4   -193    148       C  
ATOM   1170  CG  LYS B  99      62.749  34.368  28.640  1.00 15.24           C  
ANISOU 1170  CG  LYS B  99     1448   2297   2047    -33   -206    160       C  
ATOM   1171  CD  LYS B  99      63.403  33.642  27.473  1.00 21.89           C  
ANISOU 1171  CD  LYS B  99     2225   3160   2934     30   -140    174       C  
ATOM   1172  CE  LYS B  99      64.791  34.211  27.190  1.00 28.32           C  
ANISOU 1172  CE  LYS B  99     2908   4052   3800     -3   -137    195       C  
ATOM   1173  NZ  LYS B  99      65.436  33.463  26.081  1.00 29.74           N  
ANISOU 1173  NZ  LYS B  99     3024   4261   4015     75    -57    208       N  
ATOM   1174  N   LEU B 100      59.226  32.725  30.967  1.00 11.54           N  
ANISOU 1174  N   LEU B 100     1257   1686   1441     25   -221    164       N  
ATOM   1175  CA  LEU B 100      57.949  32.066  31.246  1.00 12.07           C  
ANISOU 1175  CA  LEU B 100     1394   1704   1490     37   -188    172       C  
ATOM   1176  C   LEU B 100      57.069  32.952  32.145  1.00 14.47           C  
ANISOU 1176  C   LEU B 100     1753   2009   1735     -2   -187    156       C  
ATOM   1177  O   LEU B 100      55.871  33.111  31.900  1.00 10.45           O  
ANISOU 1177  O   LEU B 100     1275   1470   1225    -15   -141    139       O  
ATOM   1178  CB  LEU B 100      58.177  30.694  31.884  1.00  7.86           C  
ANISOU 1178  CB  LEU B 100      878   1152    956     91   -203    222       C  
ATOM   1179  CG  LEU B 100      58.725  29.621  30.929  1.00  9.60           C  
ANISOU 1179  CG  LEU B 100     1067   1345   1235    149   -188    231       C  
ATOM   1180  CD1 LEU B 100      59.257  28.436  31.727  1.00 13.45           C  
ANISOU 1180  CD1 LEU B 100     1573   1818   1721    212   -223    286       C  
ATOM   1181  CD2 LEU B 100      57.659  29.173  29.900  1.00  9.22           C  
ANISOU 1181  CD2 LEU B 100     1056   1231   1218    141   -135    203       C  
ATOM   1182  N   GLN B 101      57.684  33.546  33.165  1.00 12.78           N  
ANISOU 1182  N   GLN B 101     1550   1834   1471    -17   -241    157       N  
ATOM   1183  CA  GLN B 101      56.978  34.467  34.058  1.00  9.42           C  
ANISOU 1183  CA  GLN B 101     1191   1410    976    -43   -241    131       C  
ATOM   1184  C   GLN B 101      56.480  35.677  33.289  1.00 10.66           C  
ANISOU 1184  C   GLN B 101     1352   1547   1151    -79   -214     80       C  
ATOM   1185  O   GLN B 101      55.359  36.141  33.473  1.00 10.71           O  
ANISOU 1185  O   GLN B 101     1406   1533   1131    -77   -173     59       O  
ATOM   1186  CB  GLN B 101      57.887  34.928  35.199  1.00 13.98           C  
ANISOU 1186  CB  GLN B 101     1789   2031   1493    -55   -324    129       C  
ATOM   1187  CG  GLN B 101      57.951  33.993  36.381  1.00 26.70           C  
ANISOU 1187  CG  GLN B 101     3446   3659   3040    -14   -349    179       C  
ATOM   1188  CD  GLN B 101      58.668  34.647  37.553  1.00 41.22           C  
ANISOU 1188  CD  GLN B 101     5325   5540   4795    -27   -442    163       C  
ATOM   1189  OE1 GLN B 101      59.559  35.479  37.360  1.00 37.73           O  
ANISOU 1189  OE1 GLN B 101     4838   5120   4377    -70   -509    128       O  
ATOM   1190  NE2 GLN B 101      58.265  34.300  38.768  1.00 41.91           N  
ANISOU 1190  NE2 GLN B 101     5503   5637   4782      3   -447    190       N  
ATOM   1191  N   ASN B 102      57.335  36.188  32.417  1.00 12.03           N  
ANISOU 1191  N   ASN B 102     1474   1727   1371   -105   -234     67       N  
ATOM   1192  CA  ASN B 102      57.020  37.371  31.632  1.00 10.13           C  
ANISOU 1192  CA  ASN B 102     1245   1458   1145   -140   -214     29       C  
ATOM   1193  C   ASN B 102      55.843  37.157  30.694  1.00 13.03           C  
ANISOU 1193  C   ASN B 102     1624   1791   1537   -114   -152     23       C  
ATOM   1194  O   ASN B 102      54.920  37.970  30.606  1.00 10.17           O  
ANISOU 1194  O   ASN B 102     1305   1401   1160   -115   -131     -6       O  
ATOM   1195  CB  ASN B 102      58.243  37.776  30.834  1.00 13.01           C  
ANISOU 1195  CB  ASN B 102     1545   1839   1558   -177   -234     34       C  
ATOM   1196  CG  ASN B 102      58.422  39.246  30.784  1.00 17.95           C  
ANISOU 1196  CG  ASN B 102     2202   2441   2178   -239   -256      2       C  
ATOM   1197  OD1 ASN B 102      58.179  39.939  31.767  1.00 13.71           O  
ANISOU 1197  OD1 ASN B 102     1729   1889   1591   -257   -293    -27       O  
ATOM   1198  ND2 ASN B 102      58.824  39.753  29.620  1.00 21.60           N  
ANISOU 1198  ND2 ASN B 102     2633   2891   2684   -270   -228      8       N  
ATOM   1199  N   VAL B 103      55.884  36.050  29.971  1.00  8.29           N  
ANISOU 1199  N   VAL B 103      985   1189    975    -86   -130     45       N  
ATOM   1200  CA  VAL B 103      54.764  35.692  29.147  1.00  6.42           C  
ANISOU 1200  CA  VAL B 103      757    921    761    -66    -90     36       C  
ATOM   1201  C   VAL B 103      53.502  35.572  30.017  1.00 10.22           C  
ANISOU 1201  C   VAL B 103     1271   1394   1219    -58    -68     36       C  
ATOM   1202  O   VAL B 103      52.435  36.039  29.625  1.00  7.18           O  
ANISOU 1202  O   VAL B 103      894    992    841    -53    -45     14       O  
ATOM   1203  CB  VAL B 103      55.015  34.367  28.392  1.00  8.23           C  
ANISOU 1203  CB  VAL B 103      958   1140   1030    -37    -78     54       C  
ATOM   1204  CG1 VAL B 103      53.723  33.880  27.763  1.00 11.25           C  
ANISOU 1204  CG1 VAL B 103     1355   1486   1433    -27    -55     40       C  
ATOM   1205  CG2 VAL B 103      56.115  34.559  27.330  1.00 11.46           C  
ANISOU 1205  CG2 VAL B 103     1333   1564   1458    -33    -76     51       C  
ATOM   1206  N   GLN B 104      53.622  34.966  31.201  1.00 10.04           N  
ANISOU 1206  N   GLN B 104     1263   1387   1165    -51    -73     64       N  
ATOM   1207  CA  GLN B 104      52.432  34.749  32.031  1.00  8.55           C  
ANISOU 1207  CA  GLN B 104     1100   1197    951    -43    -32     75       C  
ATOM   1208  C   GLN B 104      51.808  36.067  32.494  1.00  7.17           C  
ANISOU 1208  C   GLN B 104      961   1031    733    -41    -16     37       C  
ATOM   1209  O   GLN B 104      50.586  36.152  32.693  1.00  8.11           O  
ANISOU 1209  O   GLN B 104     1079   1149    852    -26     34     33       O  
ATOM   1210  CB  GLN B 104      52.759  33.882  33.246  1.00  7.29           C  
ANISOU 1210  CB  GLN B 104      967   1053    749    -34    -36    123       C  
ATOM   1211  CG  GLN B 104      51.513  33.417  34.016  1.00  7.70           C  
ANISOU 1211  CG  GLN B 104     1040   1104    781    -31     28    151       C  
ATOM   1212  CD  GLN B 104      50.673  32.447  33.206  1.00 13.33           C  
ANISOU 1212  CD  GLN B 104     1710   1780   1574    -45     62    169       C  
ATOM   1213  OE1 GLN B 104      51.195  31.502  32.618  1.00 11.13           O  
ANISOU 1213  OE1 GLN B 104     1419   1469   1340    -45     37    187       O  
ATOM   1214  NE2 GLN B 104      49.368  32.687  33.157  1.00  9.47           N  
ANISOU 1214  NE2 GLN B 104     1196   1296   1107    -55    114    160       N  
ATOM   1215  N   ILE B 105      52.641  37.093  32.658  1.00  9.03           N  
ANISOU 1215  N   ILE B 105     1225   1269    937    -55    -59      8       N  
ATOM   1216  CA  ILE B 105      52.146  38.428  33.002  1.00  9.77           C  
ANISOU 1216  CA  ILE B 105     1372   1350    991    -48    -52    -37       C  
ATOM   1217  C   ILE B 105      51.131  38.887  31.948  1.00 12.09           C  
ANISOU 1217  C   ILE B 105     1646   1618   1332    -29    -19    -57       C  
ATOM   1218  O   ILE B 105      50.043  39.373  32.284  1.00  8.59           O  
ANISOU 1218  O   ILE B 105     1220   1172    873      7     21    -77       O  
ATOM   1219  CB  ILE B 105      53.294  39.441  33.107  1.00 10.47           C  
ANISOU 1219  CB  ILE B 105     1494   1428   1058    -85   -115    -66       C  
ATOM   1220  CG1 ILE B 105      54.057  39.243  34.430  1.00 10.32           C  
ANISOU 1220  CG1 ILE B 105     1510   1439    971    -95   -162    -60       C  
ATOM   1221  CG2 ILE B 105      52.762  40.878  33.016  1.00 11.88           C  
ANISOU 1221  CG2 ILE B 105     1733   1562   1218    -79   -110   -117       C  
ATOM   1222  CD1 ILE B 105      55.362  40.023  34.509  1.00 13.09           C  
ANISOU 1222  CD1 ILE B 105     1867   1787   1319   -150   -244    -82       C  
ATOM   1223  N   ALA B 106      51.480  38.709  30.676  1.00  9.31           N  
ANISOU 1223  N   ALA B 106     1255   1250   1034    -43    -36    -51       N  
ATOM   1224  CA  ALA B 106      50.587  39.094  29.588  1.00 10.93           C  
ANISOU 1224  CA  ALA B 106     1446   1431   1275    -21    -22    -66       C  
ATOM   1225  C   ALA B 106      49.300  38.258  29.596  1.00 10.98           C  
ANISOU 1225  C   ALA B 106     1406   1453   1313      3     14    -55       C  
ATOM   1226  O   ALA B 106      48.189  38.796  29.449  1.00  7.65           O  
ANISOU 1226  O   ALA B 106      974   1030    904     37     34    -73       O  
ATOM   1227  CB  ALA B 106      51.309  38.968  28.234  1.00  7.85           C  
ANISOU 1227  CB  ALA B 106     1037   1026    917    -39    -45    -58       C  
ATOM   1228  N   LEU B 107      49.442  36.946  29.773  1.00  7.08           N  
ANISOU 1228  N   LEU B 107      879    971    839    -14     21    -22       N  
ATOM   1229  CA  LEU B 107      48.280  36.067  29.788  1.00  6.99           C  
ANISOU 1229  CA  LEU B 107      820    967    870    -13     53     -5       C  
ATOM   1230  C   LEU B 107      47.362  36.431  30.954  1.00 10.66           C  
ANISOU 1230  C   LEU B 107     1284   1460   1306      8    110     -1       C  
ATOM   1231  O   LEU B 107      46.137  36.470  30.808  1.00  9.33           O  
ANISOU 1231  O   LEU B 107     1064   1305   1176     23    141     -5       O  
ATOM   1232  CB  LEU B 107      48.711  34.589  29.885  1.00  7.30           C  
ANISOU 1232  CB  LEU B 107      845    994    933    -40     51     33       C  
ATOM   1233  CG  LEU B 107      49.604  34.071  28.738  1.00  8.56           C  
ANISOU 1233  CG  LEU B 107     1006   1127   1118    -45      8     26       C  
ATOM   1234  CD1 LEU B 107      50.021  32.629  28.983  1.00  9.99           C  
ANISOU 1234  CD1 LEU B 107     1189   1286   1320    -55      8     62       C  
ATOM   1235  CD2 LEU B 107      48.873  34.165  27.394  1.00 11.43           C  
ANISOU 1235  CD2 LEU B 107     1348   1473   1523    -40    -12     -5       C  
ATOM   1236  N   ASP B 108      47.949  36.707  32.119  1.00  9.74           N  
ANISOU 1236  N   ASP B 108     1225   1359   1119     12    121      5       N  
ATOM   1237  CA  ASP B 108      47.137  37.008  33.291  1.00 12.41           C  
ANISOU 1237  CA  ASP B 108     1579   1727   1408     41    187      8       C  
ATOM   1238  C   ASP B 108      46.389  38.325  33.092  1.00 11.11           C  
ANISOU 1238  C   ASP B 108     1421   1560   1239     91    203    -42       C  
ATOM   1239  O   ASP B 108      45.238  38.458  33.509  1.00 12.36           O  
ANISOU 1239  O   ASP B 108     1545   1748   1403    128    269    -41       O  
ATOM   1240  CB  ASP B 108      47.998  37.075  34.554  1.00 12.67           C  
ANISOU 1240  CB  ASP B 108     1692   1774   1346     41    181     17       C  
ATOM   1241  CG  ASP B 108      48.440  35.700  35.031  1.00 13.59           C  
ANISOU 1241  CG  ASP B 108     1807   1898   1459     12    183     80       C  
ATOM   1242  OD1 ASP B 108      47.814  34.691  34.645  1.00 12.35           O  
ANISOU 1242  OD1 ASP B 108     1592   1733   1368     -9    213    118       O  
ATOM   1243  OD2 ASP B 108      49.427  35.628  35.788  1.00 11.07           O  
ANISOU 1243  OD2 ASP B 108     1545   1587   1072     10    145     91       O  
ATOM   1244  N   TYR B 109      47.037  39.287  32.441  1.00 11.41           N  
ANISOU 1244  N   TYR B 109     1502   1562   1272     95    146    -79       N  
ATOM   1245  CA  TYR B 109      46.380  40.565  32.162  1.00 10.57           C  
ANISOU 1245  CA  TYR B 109     1418   1435   1164    150    152   -123       C  
ATOM   1246  C   TYR B 109      45.108  40.320  31.357  1.00 11.79           C  
ANISOU 1246  C   TYR B 109     1480   1606   1395    180    172   -116       C  
ATOM   1247  O   TYR B 109      44.045  40.846  31.675  1.00 13.05           O  
ANISOU 1247  O   TYR B 109     1614   1785   1558    242    220   -132       O  
ATOM   1248  CB  TYR B 109      47.318  41.520  31.418  1.00 12.80           C  
ANISOU 1248  CB  TYR B 109     1761   1662   1441    133     86   -150       C  
ATOM   1249  CG  TYR B 109      46.652  42.835  31.068  1.00 12.11           C  
ANISOU 1249  CG  TYR B 109     1714   1534   1354    194     86   -189       C  
ATOM   1250  CD1 TYR B 109      46.619  43.884  31.982  1.00 11.45           C  
ANISOU 1250  CD1 TYR B 109     1721   1422   1209    233    100   -232       C  
ATOM   1251  CD2 TYR B 109      46.048  43.017  29.828  1.00 14.73           C  
ANISOU 1251  CD2 TYR B 109     2004   1850   1743    221     66   -185       C  
ATOM   1252  CE1 TYR B 109      45.995  45.077  31.671  1.00 11.71           C  
ANISOU 1252  CE1 TYR B 109     1800   1404   1244    303    101   -267       C  
ATOM   1253  CE2 TYR B 109      45.423  44.217  29.502  1.00 18.83           C  
ANISOU 1253  CE2 TYR B 109     2566   2327   2262    291     60   -213       C  
ATOM   1254  CZ  TYR B 109      45.409  45.240  30.424  1.00 12.26           C  
ANISOU 1254  CZ  TYR B 109     1822   1459   1376    333     81   -254       C  
ATOM   1255  OH  TYR B 109      44.782  46.421  30.096  1.00 13.68           O  
ANISOU 1255  OH  TYR B 109     2054   1584   1560    414     75   -282       O  
ATOM   1256  N   LEU B 110      45.220  39.481  30.331  1.00 11.27           N  
ANISOU 1256  N   LEU B 110     1358   1535   1388    140    134    -95       N  
ATOM   1257  CA  LEU B 110      44.092  39.151  29.480  1.00 11.92           C  
ANISOU 1257  CA  LEU B 110     1351   1633   1545    155    128    -91       C  
ATOM   1258  C   LEU B 110      43.036  38.338  30.219  1.00  9.28           C  
ANISOU 1258  C   LEU B 110      929   1348   1247    148    195    -63       C  
ATOM   1259  O   LEU B 110      41.841  38.611  30.092  1.00 13.22           O  
ANISOU 1259  O   LEU B 110     1351   1879   1794    190    219    -70       O  
ATOM   1260  CB  LEU B 110      44.594  38.388  28.253  1.00  9.74           C  
ANISOU 1260  CB  LEU B 110     1061   1333   1307    109     64    -83       C  
ATOM   1261  CG  LEU B 110      45.436  39.251  27.312  1.00  8.13           C  
ANISOU 1261  CG  LEU B 110      928   1089   1074    120     11   -103       C  
ATOM   1262  CD1 LEU B 110      46.214  38.379  26.308  1.00 11.08           C  
ANISOU 1262  CD1 LEU B 110     1305   1445   1460     77    -30    -92       C  
ATOM   1263  CD2 LEU B 110      44.531  40.241  26.568  1.00 10.04           C  
ANISOU 1263  CD2 LEU B 110     1163   1320   1332    182    -14   -125       C  
ATOM   1264  N   ARG B 111      43.473  37.362  31.013  1.00 10.52           N  
ANISOU 1264  N   ARG B 111     1097   1514   1385     98    228    -26       N  
ATOM   1265  CA  ARG B 111      42.531  36.500  31.716  1.00 10.36           C  
ANISOU 1265  CA  ARG B 111     1001   1535   1401     76    302     16       C  
ATOM   1266  C   ARG B 111      41.703  37.316  32.699  1.00 11.72           C  
ANISOU 1266  C   ARG B 111     1162   1755   1535    142    390      8       C  
ATOM   1267  O   ARG B 111      40.516  37.056  32.876  1.00 14.19           O  
ANISOU 1267  O   ARG B 111     1372   2116   1906    149    453     29       O  
ATOM   1268  CB  ARG B 111      43.265  35.364  32.432  1.00 14.68           C  
ANISOU 1268  CB  ARG B 111     1590   2070   1919     18    320     66       C  
ATOM   1269  CG  ARG B 111      43.804  34.297  31.465  1.00 13.58           C  
ANISOU 1269  CG  ARG B 111     1440   1882   1836    -40    251     78       C  
ATOM   1270  CD  ARG B 111      44.603  33.237  32.202  1.00 13.23           C  
ANISOU 1270  CD  ARG B 111     1450   1818   1761    -78    264    129       C  
ATOM   1271  NE  ARG B 111      43.760  32.475  33.122  1.00 11.88           N  
ANISOU 1271  NE  ARG B 111     1243   1667   1606   -109    347    189       N  
ATOM   1272  CZ  ARG B 111      44.193  31.453  33.860  1.00 14.88           C  
ANISOU 1272  CZ  ARG B 111     1669   2024   1962   -143    371    250       C  
ATOM   1273  NH1 ARG B 111      45.470  31.072  33.795  1.00 12.51           N  
ANISOU 1273  NH1 ARG B 111     1442   1686   1625   -138    311    254       N  
ATOM   1274  NH2 ARG B 111      43.358  30.819  34.666  1.00 17.32           N  
ANISOU 1274  NH2 ARG B 111     1948   2350   2284   -177    457    312       N  
ATOM   1275  N   HIS B 112      42.321  38.322  33.316  1.00 13.33           N  
ANISOU 1275  N   HIS B 112     1472   1948   1646    191    395    -26       N  
ATOM   1276  CA  HIS B 112      41.587  39.188  34.243  1.00 15.20           C  
ANISOU 1276  CA  HIS B 112     1722   2221   1831    272    479    -48       C  
ATOM   1277  C   HIS B 112      40.477  39.924  33.519  1.00 18.29           C  
ANISOU 1277  C   HIS B 112     2029   2627   2293    341    482    -77       C  
ATOM   1278  O   HIS B 112      39.432  40.206  34.107  1.00 21.02           O  
ANISOU 1278  O   HIS B 112     2315   3027   2645    405    572    -77       O  
ATOM   1279  CB  HIS B 112      42.517  40.202  34.918  1.00 13.30           C  
ANISOU 1279  CB  HIS B 112     1629   1946   1477    308    460    -94       C  
ATOM   1280  CG  HIS B 112      41.831  41.061  35.939  1.00 17.16           C  
ANISOU 1280  CG  HIS B 112     2161   2464   1896    400    548   -126       C  
ATOM   1281  ND1 HIS B 112      41.446  42.360  35.682  1.00 25.49           N  
ANISOU 1281  ND1 HIS B 112     3251   3489   2946    488    541   -187       N  
ATOM   1282  CD2 HIS B 112      41.452  40.801  37.212  1.00 25.10           C  
ANISOU 1282  CD2 HIS B 112     3189   3522   2824    426    652   -106       C  
ATOM   1283  CE1 HIS B 112      40.859  42.864  36.755  1.00 27.58           C  
ANISOU 1283  CE1 HIS B 112     3556   3787   3137    571    637   -211       C  
ATOM   1284  NE2 HIS B 112      40.855  41.939  37.699  1.00 31.91           N  
ANISOU 1284  NE2 HIS B 112     4099   4391   3635    534    710   -162       N  
ATOM   1285  N   ARG B 113      40.710  40.240  32.248  1.00 20.59           N  
ANISOU 1285  N   ARG B 113     2315   2876   2634    337    385   -100       N  
ATOM   1286  CA  ARG B 113      39.721  40.947  31.438  1.00 16.80           C  
ANISOU 1286  CA  ARG B 113     1762   2403   2217    410    362   -124       C  
ATOM   1287  C   ARG B 113      38.746  39.965  30.760  1.00 24.12           C  
ANISOU 1287  C   ARG B 113     2530   3377   3258    368    350    -92       C  
ATOM   1288  O   ARG B 113      38.024  40.330  29.829  1.00 18.20           O  
ANISOU 1288  O   ARG B 113     1708   2635   2573    411    295   -107       O  
ATOM   1289  CB  ARG B 113      40.424  41.842  30.406  1.00 17.45           C  
ANISOU 1289  CB  ARG B 113     1934   2413   2284    429    264   -158       C  
ATOM   1290  CG  ARG B 113      41.237  43.014  31.025  1.00 22.00           C  
ANISOU 1290  CG  ARG B 113     2662   2932   2766    469    268   -197       C  
ATOM   1291  CD  ARG B 113      41.981  43.880  29.968  1.00 27.66           C  
ANISOU 1291  CD  ARG B 113     3468   3568   3474    469    177   -217       C  
ATOM   1292  NE  ARG B 113      41.089  44.416  28.929  1.00 31.29           N  
ANISOU 1292  NE  ARG B 113     3880   4019   3989    541    137   -222       N  
ATOM   1293  CZ  ARG B 113      41.203  45.617  28.353  1.00 28.51           C  
ANISOU 1293  CZ  ARG B 113     3616   3596   3620    600     92   -244       C  
ATOM   1294  NH1 ARG B 113      42.173  46.472  28.699  1.00 17.63           N  
ANISOU 1294  NH1 ARG B 113     2380   2141   2179    586     83   -266       N  
ATOM   1295  NH2 ARG B 113      40.322  45.974  27.429  1.00 28.12           N  
ANISOU 1295  NH2 ARG B 113     3517   3549   3621    674     49   -240       N  
ATOM   1296  N   GLN B 114      38.720  38.728  31.254  1.00 18.10           N  
ANISOU 1296  N   GLN B 114     1718   2641   2518    284    394    -45       N  
ATOM   1297  CA  GLN B 114      37.789  37.686  30.797  1.00 19.92           C  
ANISOU 1297  CA  GLN B 114     1799   2908   2861    222    388    -11       C  
ATOM   1298  C   GLN B 114      38.048  37.270  29.351  1.00 22.34           C  
ANISOU 1298  C   GLN B 114     2096   3169   3221    175    259    -28       C  
ATOM   1299  O   GLN B 114      37.156  36.785  28.663  1.00 22.79           O  
ANISOU 1299  O   GLN B 114     2034   3252   3375    146    216    -25       O  
ATOM   1300  CB  GLN B 114      36.329  38.138  30.943  1.00 22.67           C  
ANISOU 1300  CB  GLN B 114     2001   3333   3280    290    446    -12       C  
ATOM   1301  CG  GLN B 114      35.995  38.758  32.295  1.00 34.87           C  
ANISOU 1301  CG  GLN B 114     3564   4926   4758    369    583     -8       C  
ATOM   1302  CD  GLN B 114      36.279  37.820  33.441  1.00 46.28           C  
ANISOU 1302  CD  GLN B 114     5037   6389   6158    295    682     48       C  
ATOM   1303  OE1 GLN B 114      35.912  36.646  33.401  1.00 56.75           O  
ANISOU 1303  OE1 GLN B 114     6284   7726   7553    192    687     95       O  
ATOM   1304  NE2 GLN B 114      36.947  38.327  34.469  1.00 49.22           N  
ANISOU 1304  NE2 GLN B 114     5547   6751   6403    340    742     36       N  
ATOM   1305  N   VAL B 115      39.272  37.467  28.890  1.00 15.83           N  
ANISOU 1305  N   VAL B 115     1400   2284   2332    166    197    -48       N  
ATOM   1306  CA  VAL B 115      39.644  37.042  27.556  1.00 17.02           C  
ANISOU 1306  CA  VAL B 115     1565   2392   2509    128     90    -64       C  
ATOM   1307  C   VAL B 115      39.889  35.534  27.570  1.00 21.08           C  
ANISOU 1307  C   VAL B 115     2061   2886   3063     27     85    -34       C  
ATOM   1308  O   VAL B 115      40.667  35.046  28.385  1.00 15.84           O  
ANISOU 1308  O   VAL B 115     1459   2205   2353     -6    133     -7       O  
ATOM   1309  CB  VAL B 115      40.885  37.785  27.073  1.00 11.85           C  
ANISOU 1309  CB  VAL B 115     1045   1684   1773    155     44    -88       C  
ATOM   1310  CG1 VAL B 115      41.403  37.182  25.794  1.00 18.74           C  
ANISOU 1310  CG1 VAL B 115     1945   2518   2655    114    -44    -99       C  
ATOM   1311  CG2 VAL B 115      40.562  39.272  26.882  1.00 16.31           C  
ANISOU 1311  CG2 VAL B 115     1638   2247   2310    250     34   -117       C  
ATOM   1312  N   LYS B 116      39.213  34.799  26.688  1.00 19.55           N  
ANISOU 1312  N   LYS B 116     1788   2688   2950    -19     18    -41       N  
ATOM   1313  CA  LYS B 116      39.396  33.346  26.632  1.00 23.95           C  
ANISOU 1313  CA  LYS B 116     2341   3206   3552   -116      5    -19       C  
ATOM   1314  C   LYS B 116      40.659  32.970  25.853  1.00 16.24           C  
ANISOU 1314  C   LYS B 116     1486   2163   2522   -126    -59    -42       C  
ATOM   1315  O   LYS B 116      40.893  33.448  24.751  1.00 20.34           O  
ANISOU 1315  O   LYS B 116     2044   2668   3016    -89   -135    -82       O  
ATOM   1316  CB  LYS B 116      38.164  32.666  26.024  1.00 37.41           C  
ANISOU 1316  CB  LYS B 116     3917   4925   5371   -174    -48    -24       C  
ATOM   1317  CG  LYS B 116      36.930  32.736  26.918  1.00 48.13           C  
ANISOU 1317  CG  LYS B 116     5129   6356   6802   -184     38     14       C  
ATOM   1318  CD  LYS B 116      35.784  31.858  26.409  1.00 60.60           C  
ANISOU 1318  CD  LYS B 116     6609   7948   8468   -264    -15     17       C  
ATOM   1319  CE  LYS B 116      36.280  30.725  25.512  1.00 64.40           C  
ANISOU 1319  CE  LYS B 116     7163   8342   8966   -345   -113     -6       C  
ATOM   1320  NZ  LYS B 116      35.716  29.397  25.893  1.00 65.54           N  
ANISOU 1320  NZ  LYS B 116     7276   8460   9167   -458    -87     30       N  
ATOM   1321  N   LEU B 117      41.468  32.117  26.465  1.00 13.70           N  
ANISOU 1321  N   LEU B 117     1224   1804   2180   -168    -21    -10       N  
ATOM   1322  CA  LEU B 117      42.785  31.764  25.959  1.00  9.75           C  
ANISOU 1322  CA  LEU B 117      829   1250   1626   -163    -58    -24       C  
ATOM   1323  C   LEU B 117      42.941  30.251  26.018  1.00 12.16           C  
ANISOU 1323  C   LEU B 117     1150   1494   1976   -231    -65     -3       C  
ATOM   1324  O   LEU B 117      43.914  29.749  26.569  1.00 17.20           O  
ANISOU 1324  O   LEU B 117     1856   2103   2578   -231    -36     25       O  
ATOM   1325  CB  LEU B 117      43.894  32.433  26.776  1.00 12.63           C  
ANISOU 1325  CB  LEU B 117     1266   1628   1905   -121     -8     -7       C  
ATOM   1326  CG  LEU B 117      43.918  33.957  26.839  1.00 13.02           C  
ANISOU 1326  CG  LEU B 117     1328   1714   1903    -58      1    -29       C  
ATOM   1327  CD1 LEU B 117      44.870  34.437  27.913  1.00 17.97           C  
ANISOU 1327  CD1 LEU B 117     2018   2351   2458    -41     48    -11       C  
ATOM   1328  CD2 LEU B 117      44.324  34.522  25.504  1.00 19.31           C  
ANISOU 1328  CD2 LEU B 117     2166   2492   2679    -28    -67    -68       C  
ATOM   1329  N   VAL B 118      41.966  29.534  25.471  1.00 21.18           N  
ANISOU 1329  N   VAL B 118     2231   2615   3203   -289   -110    -15       N  
ATOM   1330  CA  VAL B 118      41.936  28.080  25.582  1.00 20.41           C  
ANISOU 1330  CA  VAL B 118     2150   2442   3162   -366   -117      7       C  
ATOM   1331  C   VAL B 118      43.230  27.449  25.074  1.00 15.00           C  
ANISOU 1331  C   VAL B 118     1586   1686   2429   -341   -151    -14       C  
ATOM   1332  O   VAL B 118      43.637  27.706  23.943  1.00 16.10           O  
ANISOU 1332  O   VAL B 118     1770   1814   2532   -300   -214    -71       O  
ATOM   1333  CB  VAL B 118      40.756  27.480  24.794  1.00 29.02           C  
ANISOU 1333  CB  VAL B 118     3163   3510   4354   -440   -192    -23       C  
ATOM   1334  CG1 VAL B 118      40.686  25.980  25.016  1.00 29.98           C  
ANISOU 1334  CG1 VAL B 118     3311   3537   4543   -533   -195      4       C  
ATOM   1335  CG2 VAL B 118      39.446  28.149  25.200  1.00 35.16           C  
ANISOU 1335  CG2 VAL B 118     3794   4373   5191   -453   -161     -4       C  
ATOM   1336  N   ASN B 119      43.857  26.635  25.925  1.00 14.10           N  
ANISOU 1336  N   ASN B 119     1522   1526   2308   -356   -103     38       N  
ATOM   1337  CA  ASN B 119      45.087  25.897  25.614  1.00 12.75           C  
ANISOU 1337  CA  ASN B 119     1456   1286   2102   -322   -123     28       C  
ATOM   1338  C   ASN B 119      46.316  26.754  25.334  1.00 13.59           C  
ANISOU 1338  C   ASN B 119     1608   1436   2121   -234   -121      6       C  
ATOM   1339  O   ASN B 119      47.375  26.229  24.992  1.00 13.28           O  
ANISOU 1339  O   ASN B 119     1638   1354   2054   -192   -133     -4       O  
ATOM   1340  CB  ASN B 119      44.847  24.961  24.428  1.00 13.32           C  
ANISOU 1340  CB  ASN B 119     1568   1272   2222   -353   -203    -29       C  
ATOM   1341  CG  ASN B 119      43.774  23.948  24.715  1.00 21.81           C  
ANISOU 1341  CG  ASN B 119     2606   2283   3398   -458   -213     -4       C  
ATOM   1342  OD1 ASN B 119      43.600  23.526  25.855  1.00 25.70           O  
ANISOU 1342  OD1 ASN B 119     3083   2765   3917   -500   -146     72       O  
ATOM   1343  ND2 ASN B 119      43.045  23.552  23.687  1.00 28.48           N  
ANISOU 1343  ND2 ASN B 119     3438   3085   4297   -507   -299    -64       N  
ATOM   1344  N   ILE B 120      46.204  28.065  25.490  1.00  9.79           N  
ANISOU 1344  N   ILE B 120     1086   1034   1599   -204   -102      1       N  
ATOM   1345  CA  ILE B 120      47.379  28.898  25.294  1.00  8.76           C  
ANISOU 1345  CA  ILE B 120      995    940   1395   -140    -96    -12       C  
ATOM   1346  C   ILE B 120      48.138  29.058  26.622  1.00  9.71           C  
ANISOU 1346  C   ILE B 120     1127   1087   1476   -125    -46     41       C  
ATOM   1347  O   ILE B 120      47.701  29.785  27.517  1.00 11.52           O  
ANISOU 1347  O   ILE B 120     1327   1364   1686   -131     -9     63       O  
ATOM   1348  CB  ILE B 120      47.008  30.278  24.732  1.00  7.20           C  
ANISOU 1348  CB  ILE B 120      771    797   1169   -114   -110    -45       C  
ATOM   1349  CG1 ILE B 120      46.275  30.135  23.390  1.00  7.16           C  
ANISOU 1349  CG1 ILE B 120      762    770   1189   -120   -176    -96       C  
ATOM   1350  CG2 ILE B 120      48.257  31.126  24.520  1.00  9.58           C  
ANISOU 1350  CG2 ILE B 120     1113   1124   1403    -66   -101    -50       C  
ATOM   1351  CD1 ILE B 120      45.647  31.473  22.900  1.00 13.29           C  
ANISOU 1351  CD1 ILE B 120     1509   1597   1945    -91   -197   -118       C  
ATOM   1352  N   ARG B 121      49.292  28.411  26.714  1.00 10.43           N  
ANISOU 1352  N   ARG B 121     1264   1150   1548    -96    -49     57       N  
ATOM   1353  CA  ARG B 121      50.084  28.408  27.947  1.00  9.48           C  
ANISOU 1353  CA  ARG B 121     1159   1053   1390    -79    -22    108       C  
ATOM   1354  C   ARG B 121      51.336  29.248  27.775  1.00  9.52           C  
ANISOU 1354  C   ARG B 121     1167   1106   1346    -34    -33     93       C  
ATOM   1355  O   ARG B 121      51.791  29.464  26.643  1.00  8.41           O  
ANISOU 1355  O   ARG B 121     1027    962   1204    -11    -50     54       O  
ATOM   1356  CB  ARG B 121      50.483  26.980  28.339  1.00  8.63           C  
ANISOU 1356  CB  ARG B 121     1094    878   1306    -74    -24    150       C  
ATOM   1357  CG  ARG B 121      49.345  25.985  28.413  1.00  8.76           C  
ANISOU 1357  CG  ARG B 121     1115    828   1386   -134    -15    170       C  
ATOM   1358  CD  ARG B 121      49.879  24.548  28.622  1.00  9.46           C  
ANISOU 1358  CD  ARG B 121     1270    825   1500   -122    -24    208       C  
ATOM   1359  NE  ARG B 121      50.855  24.208  27.590  1.00  9.84           N  
ANISOU 1359  NE  ARG B 121     1353    840   1547    -58    -61    160       N  
ATOM   1360  CZ  ARG B 121      51.911  23.424  27.749  1.00  9.64           C  
ANISOU 1360  CZ  ARG B 121     1376    772   1514      6    -70    183       C  
ATOM   1361  NH1 ARG B 121      52.153  22.834  28.913  1.00 10.90           N  
ANISOU 1361  NH1 ARG B 121     1568    909   1667     12    -57    259       N  
ATOM   1362  NH2 ARG B 121      52.735  23.227  26.721  1.00  9.66           N  
ANISOU 1362  NH2 ARG B 121     1399    758   1514     72    -89    132       N  
ATOM   1363  N   ASN B 122      51.922  29.695  28.889  1.00  7.40           N  
ANISOU 1363  N   ASN B 122      900    879   1033    -25    -25    125       N  
ATOM   1364  CA  ASN B 122      53.169  30.432  28.777  1.00 10.66           C  
ANISOU 1364  CA  ASN B 122     1302   1334   1414      1    -44    114       C  
ATOM   1365  C   ASN B 122      54.251  29.579  28.111  1.00  9.53           C  
ANISOU 1365  C   ASN B 122     1158   1171   1293     46    -59    116       C  
ATOM   1366  O   ASN B 122      55.066  30.111  27.362  1.00  6.96           O  
ANISOU 1366  O   ASN B 122      809    874    963     64    -62     94       O  
ATOM   1367  CB  ASN B 122      53.626  30.984  30.144  1.00 10.33           C  
ANISOU 1367  CB  ASN B 122     1269   1338   1320     -2    -52    143       C  
ATOM   1368  CG  ASN B 122      53.958  29.894  31.190  1.00 10.96           C  
ANISOU 1368  CG  ASN B 122     1375   1403   1385     18    -59    201       C  
ATOM   1369  OD1 ASN B 122      53.555  28.730  31.084  1.00 10.07           O  
ANISOU 1369  OD1 ASN B 122     1284   1236   1308     21    -46    227       O  
ATOM   1370  ND2 ASN B 122      54.683  30.305  32.234  1.00  9.11           N  
ANISOU 1370  ND2 ASN B 122     1152   1214   1096     28    -87    222       N  
ATOM   1371  N   ASP B 123      54.238  28.259  28.333  1.00  6.91           N  
ANISOU 1371  N   ASP B 123      854    784    987     65    -61    144       N  
ATOM   1372  CA  ASP B 123      55.190  27.375  27.656  1.00  7.29           C  
ANISOU 1372  CA  ASP B 123      909    802   1057    126    -70    140       C  
ATOM   1373  C   ASP B 123      55.083  27.430  26.137  1.00 11.43           C  
ANISOU 1373  C   ASP B 123     1440   1308   1595    139    -61     81       C  
ATOM   1374  O   ASP B 123      56.093  27.385  25.440  1.00 12.16           O  
ANISOU 1374  O   ASP B 123     1517   1419   1683    192    -51     66       O  
ATOM   1375  CB  ASP B 123      54.995  25.920  28.091  1.00 10.85           C  
ANISOU 1375  CB  ASP B 123     1412   1171   1538    144    -75    176       C  
ATOM   1376  CG  ASP B 123      55.016  25.766  29.584  1.00  9.99           C  
ANISOU 1376  CG  ASP B 123     1318   1075   1402    135    -80    243       C  
ATOM   1377  OD1 ASP B 123      54.011  26.151  30.205  1.00 11.39           O  
ANISOU 1377  OD1 ASP B 123     1501   1263   1564     76    -60    258       O  
ATOM   1378  OD2 ASP B 123      56.025  25.261  30.128  1.00 12.95           O  
ANISOU 1378  OD2 ASP B 123     1699   1455   1767    194   -104    283       O  
ATOM   1379  N   ASP B 124      53.860  27.488  25.625  1.00  8.05           N  
ANISOU 1379  N   ASP B 124     1031    846   1179     94    -64     51       N  
ATOM   1380  CA  ASP B 124      53.669  27.432  24.177  1.00  7.02           C  
ANISOU 1380  CA  ASP B 124      926    692   1049    110    -69     -7       C  
ATOM   1381  C   ASP B 124      54.180  28.689  23.495  1.00 13.78           C  
ANISOU 1381  C   ASP B 124     1756   1616   1863    120    -54    -26       C  
ATOM   1382  O   ASP B 124      54.775  28.620  22.416  1.00 10.96           O  
ANISOU 1382  O   ASP B 124     1417   1261   1485    164    -39    -55       O  
ATOM   1383  CB  ASP B 124      52.199  27.188  23.867  1.00 10.08           C  
ANISOU 1383  CB  ASP B 124     1331   1033   1465     54    -95    -32       C  
ATOM   1384  CG  ASP B 124      51.698  25.920  24.528  1.00 11.77           C  
ANISOU 1384  CG  ASP B 124     1572   1170   1729     27   -103     -4       C  
ATOM   1385  OD1 ASP B 124      52.298  24.859  24.273  1.00 11.86           O  
ANISOU 1385  OD1 ASP B 124     1635   1117   1755     70   -110     -9       O  
ATOM   1386  OD2 ASP B 124      50.757  25.991  25.337  1.00  7.74           O  
ANISOU 1386  OD2 ASP B 124     1035    662   1244    -33    -96     27       O  
ATOM   1387  N   ILE B 125      53.982  29.831  24.142  1.00  9.77           N  
ANISOU 1387  N   ILE B 125     1213   1159   1340     82    -51     -8       N  
ATOM   1388  CA  ILE B 125      54.463  31.103  23.598  1.00  9.96           C  
ANISOU 1388  CA  ILE B 125     1221   1233   1330     79    -37    -17       C  
ATOM   1389  C   ILE B 125      55.987  31.147  23.708  1.00  7.55           C  
ANISOU 1389  C   ILE B 125      878    970   1020    109    -15      6       C  
ATOM   1390  O   ILE B 125      56.686  31.552  22.774  1.00  8.54           O  
ANISOU 1390  O   ILE B 125      995   1121   1128    128     13     -2       O  
ATOM   1391  CB  ILE B 125      53.840  32.300  24.336  1.00  8.63           C  
ANISOU 1391  CB  ILE B 125     1039   1091   1150     35    -44     -9       C  
ATOM   1392  CG1 ILE B 125      52.305  32.278  24.200  1.00 10.19           C  
ANISOU 1392  CG1 ILE B 125     1250   1261   1363     15    -60    -29       C  
ATOM   1393  CG2 ILE B 125      54.472  33.620  23.864  1.00 10.47           C  
ANISOU 1393  CG2 ILE B 125     1267   1359   1354     25    -31    -11       C  
ATOM   1394  CD1 ILE B 125      51.795  32.176  22.750  1.00  8.21           C  
ANISOU 1394  CD1 ILE B 125     1028    986   1106     30    -79    -69       C  
ATOM   1395  N   ALA B 126      56.508  30.714  24.851  1.00  6.33           N  
ANISOU 1395  N   ALA B 126      697    828    882    115    -29     41       N  
ATOM   1396  CA  ALA B 126      57.960  30.704  25.043  1.00  9.08           C  
ANISOU 1396  CA  ALA B 126      988   1225   1237    146    -22     65       C  
ATOM   1397  C   ALA B 126      58.645  29.720  24.096  1.00  8.69           C  
ANISOU 1397  C   ALA B 126      939   1162   1203    221      8     54       C  
ATOM   1398  O   ALA B 126      59.816  29.889  23.778  1.00 10.42           O  
ANISOU 1398  O   ALA B 126     1097   1432   1428    253     34     66       O  
ATOM   1399  CB  ALA B 126      58.307  30.375  26.502  1.00  8.91           C  
ANISOU 1399  CB  ALA B 126      947   1219   1221    146    -60    106       C  
ATOM   1400  N   ASP B 127      57.920  28.686  23.652  1.00  7.42           N  
ANISOU 1400  N   ASP B 127      844    928   1048    250      5     29       N  
ATOM   1401  CA  ASP B 127      58.475  27.712  22.714  1.00 13.28           C  
ANISOU 1401  CA  ASP B 127     1612   1639   1793    331     33      4       C  
ATOM   1402  C   ASP B 127      58.246  28.091  21.253  1.00 16.52           C  
ANISOU 1402  C   ASP B 127     2063   2051   2164    340     66    -44       C  
ATOM   1403  O   ASP B 127      58.669  27.362  20.353  1.00 13.57           O  
ANISOU 1403  O   ASP B 127     1726   1654   1776    414     97    -75       O  
ATOM   1404  CB  ASP B 127      57.879  26.315  22.941  1.00 13.57           C  
ANISOU 1404  CB  ASP B 127     1720   1579   1858    357      5     -5       C  
ATOM   1405  CG  ASP B 127      58.285  25.697  24.271  1.00 19.17           C  
ANISOU 1405  CG  ASP B 127     2410   2278   2596    375    -20     52       C  
ATOM   1406  OD1 ASP B 127      59.290  26.134  24.853  1.00 18.42           O  
ANISOU 1406  OD1 ASP B 127     2240   2256   2501    395    -21     88       O  
ATOM   1407  OD2 ASP B 127      57.578  24.773  24.732  1.00 26.89           O  
ANISOU 1407  OD2 ASP B 127     3449   3173   3596    364    -44     63       O  
ATOM   1408  N   GLY B 128      57.542  29.195  21.014  1.00  9.68           N  
ANISOU 1408  N   GLY B 128     1202   1205   1272    275     58    -51       N  
ATOM   1409  CA  GLY B 128      57.282  29.639  19.652  1.00 11.18           C  
ANISOU 1409  CA  GLY B 128     1442   1396   1410    285     81    -87       C  
ATOM   1410  C   GLY B 128      56.306  28.764  18.869  1.00 13.32           C  
ANISOU 1410  C   GLY B 128     1804   1592   1665    304     46   -144       C  
ATOM   1411  O   GLY B 128      56.429  28.630  17.643  1.00 14.68           O  
ANISOU 1411  O   GLY B 128     2037   1758   1784    350     67   -183       O  
ATOM   1412  N   ASN B 129      55.347  28.154  19.563  1.00 11.78           N  
ANISOU 1412  N   ASN B 129     1622   1339   1513    266     -8   -148       N  
ATOM   1413  CA  ASN B 129      54.378  27.283  18.906  1.00 10.83           C  
ANISOU 1413  CA  ASN B 129     1579   1140   1395    264    -56   -203       C  
ATOM   1414  C   ASN B 129      53.553  28.078  17.899  1.00  9.44           C  
ANISOU 1414  C   ASN B 129     1438    980   1171    241    -86   -238       C  
ATOM   1415  O   ASN B 129      52.917  29.054  18.269  1.00  8.58           O  
ANISOU 1415  O   ASN B 129     1286    905   1067    191   -102   -216       O  
ATOM   1416  CB  ASN B 129      53.453  26.610  19.929  1.00  9.05           C  
ANISOU 1416  CB  ASN B 129     1343    858   1238    205   -101   -186       C  
ATOM   1417  CG  ASN B 129      52.469  25.647  19.272  1.00 13.17           C  
ANISOU 1417  CG  ASN B 129     1935   1290   1779    184   -159   -242       C  
ATOM   1418  OD1 ASN B 129      51.318  25.993  19.015  1.00 12.84           O  
ANISOU 1418  OD1 ASN B 129     1885   1246   1747    127   -208   -263       O  
ATOM   1419  ND2 ASN B 129      52.931  24.437  18.984  1.00 16.71           N  
ANISOU 1419  ND2 ASN B 129     2452   1661   2237    234   -160   -269       N  
ATOM   1420  N   PRO B 130      53.572  27.674  16.616  1.00 12.05           N  
ANISOU 1420  N   PRO B 130     1852   1283   1443    289    -94   -295       N  
ATOM   1421  CA  PRO B 130      52.873  28.507  15.621  1.00 12.56           C  
ANISOU 1421  CA  PRO B 130     1958   1370   1445    279   -129   -322       C  
ATOM   1422  C   PRO B 130      51.369  28.655  15.884  1.00 12.71           C  
ANISOU 1422  C   PRO B 130     1955   1365   1508    209   -217   -335       C  
ATOM   1423  O   PRO B 130      50.877  29.775  15.959  1.00 11.68           O  
ANISOU 1423  O   PRO B 130     1788   1280   1369    184   -228   -310       O  
ATOM   1424  CB  PRO B 130      53.114  27.761  14.311  1.00 16.92           C  
ANISOU 1424  CB  PRO B 130     2622   1885   1923    348   -133   -389       C  
ATOM   1425  CG  PRO B 130      54.418  27.059  14.524  1.00 18.47           C  
ANISOU 1425  CG  PRO B 130     2813   2079   2126    415    -53   -378       C  
ATOM   1426  CD  PRO B 130      54.435  26.658  15.988  1.00  9.63           C  
ANISOU 1426  CD  PRO B 130     1611    941   1109    373    -60   -332       C  
ATOM   1427  N   LYS B 131      50.655  27.543  16.048  1.00 10.02           N  
ANISOU 1427  N   LYS B 131     1631    953   1223    178   -276   -370       N  
ATOM   1428  CA  LYS B 131      49.203  27.611  16.178  1.00 14.33           C  
ANISOU 1428  CA  LYS B 131     2141   1484   1821    108   -359   -384       C  
ATOM   1429  C   LYS B 131      48.758  28.426  17.390  1.00  8.48           C  
ANISOU 1429  C   LYS B 131     1291    792   1136     59   -334   -321       C  
ATOM   1430  O   LYS B 131      47.817  29.234  17.301  1.00  9.29           O  
ANISOU 1430  O   LYS B 131     1352    930   1246     36   -374   -320       O  
ATOM   1431  CB  LYS B 131      48.608  26.210  16.263  1.00 15.26           C  
ANISOU 1431  CB  LYS B 131     2286   1507   2004     65   -418   -423       C  
ATOM   1432  CG  LYS B 131      47.099  26.199  16.475  1.00 21.58           C  
ANISOU 1432  CG  LYS B 131     3021   2299   2880    -22   -500   -430       C  
ATOM   1433  CD  LYS B 131      46.570  24.780  16.605  1.00 33.51           C  
ANISOU 1433  CD  LYS B 131     4558   3706   4469    -84   -554   -461       C  
ATOM   1434  CE  LYS B 131      45.174  24.764  17.208  1.00 48.24           C  
ANISOU 1434  CE  LYS B 131     6312   5583   6433   -185   -594   -434       C  
ATOM   1435  NZ  LYS B 131      44.183  25.459  16.347  1.00 57.84           N  
ANISOU 1435  NZ  LYS B 131     7489   6863   7626   -188   -664   -459       N  
ATOM   1436  N   LEU B 132      49.437  28.235  18.522  1.00  8.02           N  
ANISOU 1436  N   LEU B 132     1195    739   1113     54   -271   -270       N  
ATOM   1437  CA  LEU B 132      48.995  28.904  19.738  1.00  7.47           C  
ANISOU 1437  CA  LEU B 132     1042    712   1086     12   -247   -218       C  
ATOM   1438  C   LEU B 132      49.512  30.350  19.805  1.00  9.13           C  
ANISOU 1438  C   LEU B 132     1234    991   1244     38   -208   -192       C  
ATOM   1439  O   LEU B 132      48.905  31.194  20.459  1.00  7.40           O  
ANISOU 1439  O   LEU B 132      964    806   1041     16   -204   -169       O  
ATOM   1440  CB  LEU B 132      49.426  28.097  20.968  1.00  9.60           C  
ANISOU 1440  CB  LEU B 132     1293    955   1401     -6   -207   -173       C  
ATOM   1441  CG  LEU B 132      48.712  26.738  21.014  1.00  9.67           C  
ANISOU 1441  CG  LEU B 132     1321    880   1474    -51   -246   -188       C  
ATOM   1442  CD1 LEU B 132      49.352  25.795  22.036  1.00 11.39           C  
ANISOU 1442  CD1 LEU B 132     1553   1053   1722    -49   -207   -140       C  
ATOM   1443  CD2 LEU B 132      47.222  26.920  21.300  1.00 12.96           C  
ANISOU 1443  CD2 LEU B 132     1669   1306   1951   -124   -279   -184       C  
ATOM   1444  N   THR B 133      50.616  30.640  19.121  1.00  8.98           N  
ANISOU 1444  N   THR B 133     1258    989   1165     85   -176   -196       N  
ATOM   1445  CA  THR B 133      51.080  32.027  19.027  1.00  7.10           C  
ANISOU 1445  CA  THR B 133     1012    802    883     96   -144   -170       C  
ATOM   1446  C   THR B 133      50.146  32.834  18.134  1.00 10.60           C  
ANISOU 1446  C   THR B 133     1483   1252   1293    102   -191   -192       C  
ATOM   1447  O   THR B 133      49.750  33.949  18.493  1.00  6.65           O  
ANISOU 1447  O   THR B 133      960    774    794     92   -191   -170       O  
ATOM   1448  CB  THR B 133      52.523  32.107  18.490  1.00  7.59           C  
ANISOU 1448  CB  THR B 133     1100    886    898    135    -86   -159       C  
ATOM   1449  OG1 THR B 133      53.398  31.430  19.406  1.00 10.92           O  
ANISOU 1449  OG1 THR B 133     1481   1310   1356    139    -53   -134       O  
ATOM   1450  CG2 THR B 133      52.977  33.563  18.335  1.00  7.90           C  
ANISOU 1450  CG2 THR B 133     1136    967    899    127    -54   -127       C  
ATOM   1451  N   LEU B 134      49.786  32.269  16.974  1.00  9.06           N  
ANISOU 1451  N   LEU B 134     1347   1032   1065    126   -237   -237       N  
ATOM   1452  CA  LEU B 134      48.764  32.879  16.120  1.00 10.77           C  
ANISOU 1452  CA  LEU B 134     1589   1252   1250    137   -306   -260       C  
ATOM   1453  C   LEU B 134      47.463  33.060  16.894  1.00  8.38           C  
ANISOU 1453  C   LEU B 134     1203    954   1024     99   -353   -256       C  
ATOM   1454  O   LEU B 134      46.851  34.125  16.853  1.00  8.29           O  
ANISOU 1454  O   LEU B 134     1175    969   1007    113   -374   -243       O  
ATOM   1455  CB  LEU B 134      48.502  32.037  14.885  1.00 10.61           C  
ANISOU 1455  CB  LEU B 134     1647   1200   1184    162   -368   -319       C  
ATOM   1456  CG  LEU B 134      49.680  31.899  13.922  1.00  8.76           C  
ANISOU 1456  CG  LEU B 134     1507    968    855    218   -314   -329       C  
ATOM   1457  CD1 LEU B 134      49.340  30.860  12.866  1.00 10.84           C  
ANISOU 1457  CD1 LEU B 134     1859   1188   1073    243   -381   -403       C  
ATOM   1458  CD2 LEU B 134      49.996  33.277  13.301  1.00 13.49           C  
ANISOU 1458  CD2 LEU B 134     2145   1608   1373    247   -283   -290       C  
ATOM   1459  N   GLY B 135      47.061  32.012  17.613  1.00  7.61           N  
ANISOU 1459  N   GLY B 135     1057    832   1002     55   -362   -264       N  
ATOM   1460  CA  GLY B 135      45.830  32.042  18.383  1.00  7.95           C  
ANISOU 1460  CA  GLY B 135     1008    887   1125     13   -389   -254       C  
ATOM   1461  C   GLY B 135      45.816  33.145  19.425  1.00  7.84           C  
ANISOU 1461  C   GLY B 135      943    915   1120     20   -331   -210       C  
ATOM   1462  O   GLY B 135      44.781  33.783  19.649  1.00  9.70           O  
ANISOU 1462  O   GLY B 135     1120   1179   1388     24   -353   -206       O  
ATOM   1463  N   LEU B 136      46.950  33.358  20.078  1.00  7.91           N  
ANISOU 1463  N   LEU B 136      973    929   1102     25   -262   -179       N  
ATOM   1464  CA  LEU B 136      47.058  34.440  21.065  1.00  7.96           C  
ANISOU 1464  CA  LEU B 136      954    965   1103     30   -214   -147       C  
ATOM   1465  C   LEU B 136      46.849  35.812  20.422  1.00 10.29           C  
ANISOU 1465  C   LEU B 136     1281   1273   1356     70   -233   -150       C  
ATOM   1466  O   LEU B 136      46.105  36.631  20.949  1.00  6.77           O  
ANISOU 1466  O   LEU B 136      801    842    928     86   -231   -144       O  
ATOM   1467  CB  LEU B 136      48.413  34.405  21.767  1.00  6.36           C  
ANISOU 1467  CB  LEU B 136      773    766    877     22   -158   -119       C  
ATOM   1468  CG  LEU B 136      48.670  35.538  22.767  1.00  7.76           C  
ANISOU 1468  CG  LEU B 136      943    967   1038     22   -122    -96       C  
ATOM   1469  CD1 LEU B 136      47.566  35.604  23.812  1.00 10.41           C  
ANISOU 1469  CD1 LEU B 136     1227   1317   1410     14   -109    -90       C  
ATOM   1470  CD2 LEU B 136      50.019  35.364  23.437  1.00 10.71           C  
ANISOU 1470  CD2 LEU B 136     1326   1348   1394      7    -88    -72       C  
ATOM   1471  N   ILE B 137      47.509  36.072  19.294  1.00  8.11           N  
ANISOU 1471  N   ILE B 137     1075    987   1021     94   -245   -156       N  
ATOM   1472  CA  ILE B 137      47.300  37.362  18.638  1.00  8.60           C  
ANISOU 1472  CA  ILE B 137     1183   1048   1037    132   -264   -148       C  
ATOM   1473  C   ILE B 137      45.844  37.529  18.182  1.00  7.28           C  
ANISOU 1473  C   ILE B 137      986    887    893    163   -340   -170       C  
ATOM   1474  O   ILE B 137      45.273  38.609  18.328  1.00  8.55           O  
ANISOU 1474  O   ILE B 137     1143   1051   1055    200   -350   -159       O  
ATOM   1475  CB  ILE B 137      48.251  37.565  17.445  1.00  9.75           C  
ANISOU 1475  CB  ILE B 137     1416   1183   1104    151   -252   -141       C  
ATOM   1476  CG1 ILE B 137      49.707  37.471  17.917  1.00  8.70           C  
ANISOU 1476  CG1 ILE B 137     1285   1056    963    121   -176   -115       C  
ATOM   1477  CG2 ILE B 137      47.988  38.924  16.782  1.00  7.10           C  
ANISOU 1477  CG2 ILE B 137     1143    836    720    189   -272   -120       C  
ATOM   1478  CD1 ILE B 137      50.057  38.373  19.118  1.00  8.67           C  
ANISOU 1478  CD1 ILE B 137     1254   1054    985     93   -139    -87       C  
ATOM   1479  N   TRP B 138      45.237  36.467  17.650  1.00  7.56           N  
ANISOU 1479  N   TRP B 138      997    923    954    151   -398   -203       N  
ATOM   1480  CA  TRP B 138      43.832  36.515  17.248  1.00  8.46           C  
ANISOU 1480  CA  TRP B 138     1057   1052   1104    170   -485   -226       C  
ATOM   1481  C   TRP B 138      42.924  36.906  18.419  1.00 10.07           C  
ANISOU 1481  C   TRP B 138     1153   1285   1388    168   -459   -210       C  
ATOM   1482  O   TRP B 138      42.021  37.721  18.262  1.00  9.84           O  
ANISOU 1482  O   TRP B 138     1090   1277   1373    219   -499   -210       O  
ATOM   1483  CB  TRP B 138      43.363  35.175  16.680  1.00  8.84           C  
ANISOU 1483  CB  TRP B 138     1087   1088   1183    133   -555   -269       C  
ATOM   1484  CG  TRP B 138      41.864  35.129  16.479  1.00  9.74           C  
ANISOU 1484  CG  TRP B 138     1109   1228   1364    133   -648   -290       C  
ATOM   1485  CD1 TRP B 138      40.970  34.341  17.147  1.00 12.72           C  
ANISOU 1485  CD1 TRP B 138     1368   1618   1848     73   -662   -297       C  
ATOM   1486  CD2 TRP B 138      41.097  35.933  15.577  1.00 10.68           C  
ANISOU 1486  CD2 TRP B 138     1236   1370   1454    195   -740   -301       C  
ATOM   1487  NE1 TRP B 138      39.687  34.588  16.693  1.00 13.18           N  
ANISOU 1487  NE1 TRP B 138     1348   1710   1949     89   -747   -310       N  
ATOM   1488  CE2 TRP B 138      39.741  35.564  15.732  1.00 17.04           C  
ANISOU 1488  CE2 TRP B 138     1917   2204   2352    168   -791   -311       C  
ATOM   1489  CE3 TRP B 138      41.425  36.925  14.646  1.00 10.64           C  
ANISOU 1489  CE3 TRP B 138     1336   1359   1347    269   -768   -290       C  
ATOM   1490  CZ2 TRP B 138      38.714  36.162  15.000  1.00 19.62           C  
ANISOU 1490  CZ2 TRP B 138     2220   2558   2677    215   -860   -310       C  
ATOM   1491  CZ3 TRP B 138      40.401  37.511  13.905  1.00 13.86           C  
ANISOU 1491  CZ3 TRP B 138     1732   1785   1751    316   -838   -288       C  
ATOM   1492  CH2 TRP B 138      39.064  37.126  14.082  1.00 12.50           C  
ANISOU 1492  CH2 TRP B 138     1431   1645   1674    292   -887   -301       C  
ATOM   1493  N  ATHR B 139      43.139  36.323  19.603  0.81  9.41           N  
ANISOU 1493  N  ATHR B 139     1019   1205   1351    120   -390   -196       N  
ATOM   1494  N  BTHR B 139      43.190  36.313  19.575  0.19  9.17           N  
ANISOU 1494  N  BTHR B 139      993   1173   1317    119   -390   -196       N  
ATOM   1495  CA ATHR B 139      42.253  36.671  20.733  0.81  9.60           C  
ANISOU 1495  CA ATHR B 139      947   1264   1437    124   -351   -180       C  
ATOM   1496  CA BTHR B 139      42.414  36.585  20.771  0.19 10.87           C  
ANISOU 1496  CA BTHR B 139     1117   1421   1594    118   -345   -179       C  
ATOM   1497  C  ATHR B 139      42.455  38.121  21.139  0.81  9.65           C  
ANISOU 1497  C  ATHR B 139      993   1271   1401    185   -311   -165       C  
ATOM   1498  C  BTHR B 139      42.490  38.056  21.155  0.19  9.79           C  
ANISOU 1498  C  BTHR B 139     1011   1288   1419    181   -310   -165       C  
ATOM   1499  O  ATHR B 139      41.496  38.794  21.548  0.81 11.82           O  
ANISOU 1499  O  ATHR B 139     1208   1573   1710    232   -307   -165       O  
ATOM   1500  O  BTHR B 139      41.505  38.664  21.583  0.19 11.50           O  
ANISOU 1500  O  BTHR B 139     1163   1534   1674    224   -305   -165       O  
ATOM   1501  CB ATHR B 139      42.452  35.771  21.982  0.81 11.63           C  
ANISOU 1501  CB ATHR B 139     1159   1524   1735     63   -277   -158       C  
ATOM   1502  CB BTHR B 139      42.907  35.741  21.938  0.19 12.88           C  
ANISOU 1502  CB BTHR B 139     1351   1672   1873     60   -270   -156       C  
ATOM   1503  OG1ATHR B 139      43.700  36.065  22.625  0.81 15.96           O  
ANISOU 1503  OG1ATHR B 139     1780   2057   2226     61   -214   -138       O  
ATOM   1504  OG1BTHR B 139      43.318  34.451  21.465  0.19 15.60           O  
ANISOU 1504  OG1BTHR B 139     1718   1983   2228     10   -297   -168       O  
ATOM   1505  CG2ATHR B 139      42.377  34.298  21.605  0.81 15.86           C  
ANISOU 1505  CG2ATHR B 139     1678   2033   2313     -3   -314   -170       C  
ATOM   1506  CG2BTHR B 139      41.808  35.570  22.898  0.19 14.69           C  
ANISOU 1506  CG2BTHR B 139     1471   1937   2172     45   -235   -141       C  
ATOM   1507  N   ILE B 140      43.681  38.612  20.981  1.00  8.32           N  
ANISOU 1507  N   ILE B 140      925   1071   1164    185   -285   -155       N  
ATOM   1508  CA  ILE B 140      43.980  40.010  21.288  1.00  7.31           C  
ANISOU 1508  CA  ILE B 140      856    924    997    229   -257   -143       C  
ATOM   1509  C   ILE B 140      43.291  40.945  20.281  1.00  8.93           C  
ANISOU 1509  C   ILE B 140     1092   1117   1184    301   -320   -147       C  
ATOM   1510  O   ILE B 140      42.667  41.936  20.672  1.00  8.91           O  
ANISOU 1510  O   ILE B 140     1084   1109   1192    362   -315   -146       O  
ATOM   1511  CB  ILE B 140      45.516  40.242  21.315  1.00  9.70           C  
ANISOU 1511  CB  ILE B 140     1245   1196   1243    192   -218   -126       C  
ATOM   1512  CG1 ILE B 140      46.127  39.587  22.571  1.00 11.47           C  
ANISOU 1512  CG1 ILE B 140     1439   1436   1484    141   -161   -119       C  
ATOM   1513  CG2 ILE B 140      45.865  41.741  21.311  1.00 10.36           C  
ANISOU 1513  CG2 ILE B 140     1410   1240   1287    224   -207   -115       C  
ATOM   1514  CD1 ILE B 140      47.662  39.423  22.504  1.00  7.14           C  
ANISOU 1514  CD1 ILE B 140      940    875    899     99   -137   -103       C  
ATOM   1515  N   ILE B 141      43.387  40.620  18.989  1.00  8.14           N  
ANISOU 1515  N   ILE B 141     1033   1010   1051    305   -383   -151       N  
ATOM   1516  CA  ILE B 141      42.677  41.369  17.958  1.00  8.91           C  
ANISOU 1516  CA  ILE B 141     1165   1099   1122    378   -460   -150       C  
ATOM   1517  C   ILE B 141      41.163  41.384  18.209  1.00 11.60           C  
ANISOU 1517  C   ILE B 141     1387   1482   1538    426   -509   -167       C  
ATOM   1518  O   ILE B 141      40.508  42.425  18.115  1.00 10.32           O  
ANISOU 1518  O   ILE B 141     1230   1314   1378    509   -536   -159       O  
ATOM   1519  CB  ILE B 141      42.947  40.783  16.554  1.00 10.98           C  
ANISOU 1519  CB  ILE B 141     1489   1357   1324    372   -525   -159       C  
ATOM   1520  CG1 ILE B 141      44.425  40.939  16.190  1.00  9.44           C  
ANISOU 1520  CG1 ILE B 141     1406   1130   1052    341   -463   -134       C  
ATOM   1521  CG2 ILE B 141      42.070  41.475  15.515  1.00 16.02           C  
ANISOU 1521  CG2 ILE B 141     2161   1996   1932    454   -623   -157       C  
ATOM   1522  CD1 ILE B 141      44.837  40.142  14.950  1.00  9.22           C  
ANISOU 1522  CD1 ILE B 141     1441   1104    957    334   -499   -149       C  
ATOM   1523  N   LEU B 142      40.622  40.218  18.548  1.00  9.96           N  
ANISOU 1523  N   LEU B 142     1070   1315   1400    373   -518   -186       N  
ATOM   1524  CA  LEU B 142      39.197  40.085  18.820  1.00 11.67           C  
ANISOU 1524  CA  LEU B 142     1144   1584   1705    400   -556   -198       C  
ATOM   1525  C   LEU B 142      38.785  40.971  19.989  1.00 12.08           C  
ANISOU 1525  C   LEU B 142     1149   1651   1788    455   -476   -185       C  
ATOM   1526  O   LEU B 142      37.818  41.718  19.909  1.00 14.88           O  
ANISOU 1526  O   LEU B 142     1448   2030   2175    542   -508   -186       O  
ATOM   1527  CB  LEU B 142      38.856  38.629  19.127  1.00 16.61           C  
ANISOU 1527  CB  LEU B 142     1668   2237   2405    308   -558   -212       C  
ATOM   1528  CG  LEU B 142      37.386  38.212  19.156  1.00 28.08           C  
ANISOU 1528  CG  LEU B 142     2960   3749   3962    302   -610   -221       C  
ATOM   1529  CD1 LEU B 142      36.684  38.591  17.851  1.00 30.71           C  
ANISOU 1529  CD1 LEU B 142     3318   4086   4264    345   -713   -229       C  
ATOM   1530  CD2 LEU B 142      37.284  36.704  19.409  1.00 27.86           C  
ANISOU 1530  CD2 LEU B 142     2870   3720   3996    185   -603   -227       C  
ATOM   1531  N   HIS B 143      39.542  40.889  21.074  1.00 11.59           N  
ANISOU 1531  N   HIS B 143     1116   1575   1712    412   -375   -175       N  
ATOM   1532  CA  HIS B 143      39.205  41.632  22.279  1.00 12.09           C  
ANISOU 1532  CA  HIS B 143     1153   1652   1790    461   -292   -171       C  
ATOM   1533  C   HIS B 143      39.328  43.144  22.093  1.00 17.71           C  
ANISOU 1533  C   HIS B 143     1965   2315   2451    556   -299   -172       C  
ATOM   1534  O   HIS B 143      38.424  43.891  22.479  1.00 17.98           O  
ANISOU 1534  O   HIS B 143     1952   2365   2515    649   -285   -179       O  
ATOM   1535  CB  HIS B 143      40.091  41.184  23.446  1.00  9.49           C  
ANISOU 1535  CB  HIS B 143      855   1315   1436    392   -198   -162       C  
ATOM   1536  CG  HIS B 143      39.778  41.887  24.730  1.00 14.38           C  
ANISOU 1536  CG  HIS B 143     1465   1949   2051    442   -111   -165       C  
ATOM   1537  ND1 HIS B 143      38.613  41.659  25.435  1.00 19.61           N  
ANISOU 1537  ND1 HIS B 143     2000   2676   2776    472    -61   -163       N  
ATOM   1538  CD2 HIS B 143      40.471  42.808  25.437  1.00 16.75           C  
ANISOU 1538  CD2 HIS B 143     1871   2205   2287    468    -64   -174       C  
ATOM   1539  CE1 HIS B 143      38.605  42.413  26.519  1.00 19.52           C  
ANISOU 1539  CE1 HIS B 143     2026   2664   2728    527     21   -172       C  
ATOM   1540  NE2 HIS B 143      39.721  43.117  26.548  1.00 18.85           N  
ANISOU 1540  NE2 HIS B 143     2088   2509   2566    523     13   -183       N  
ATOM   1541  N   PHE B 144      40.426  43.605  21.496  1.00  9.97           N  
ANISOU 1541  N   PHE B 144     1122   1269   1397    538   -317   -162       N  
ATOM   1542  CA  PHE B 144      40.690  45.047  21.473  1.00 11.42           C  
ANISOU 1542  CA  PHE B 144     1422   1384   1534    608   -312   -156       C  
ATOM   1543  C   PHE B 144      40.081  45.779  20.290  1.00 16.20           C  
ANISOU 1543  C   PHE B 144     2064   1965   2126    698   -400   -145       C  
ATOM   1544  O   PHE B 144      39.717  46.953  20.401  1.00 20.29           O  
ANISOU 1544  O   PHE B 144     2637   2438   2637    792   -402   -143       O  
ATOM   1545  CB  PHE B 144      42.202  45.317  21.518  1.00 11.53           C  
ANISOU 1545  CB  PHE B 144     1563   1336   1482    535   -278   -142       C  
ATOM   1546  CG  PHE B 144      42.784  45.173  22.892  1.00 13.23           C  
ANISOU 1546  CG  PHE B 144     1777   1555   1696    483   -200   -156       C  
ATOM   1547  CD1 PHE B 144      42.602  46.173  23.839  1.00 16.61           C  
ANISOU 1547  CD1 PHE B 144     2250   1948   2113    536   -159   -175       C  
ATOM   1548  CD2 PHE B 144      43.474  44.027  23.252  1.00 12.63           C  
ANISOU 1548  CD2 PHE B 144     1661   1515   1623    392   -172   -151       C  
ATOM   1549  CE1 PHE B 144      43.115  46.037  25.113  1.00 15.91           C  
ANISOU 1549  CE1 PHE B 144     2172   1866   2006    493    -97   -192       C  
ATOM   1550  CE2 PHE B 144      44.003  43.892  24.522  1.00 13.62           C  
ANISOU 1550  CE2 PHE B 144     1792   1647   1736    353   -112   -159       C  
ATOM   1551  CZ  PHE B 144      43.811  44.893  25.454  1.00 15.18           C  
ANISOU 1551  CZ  PHE B 144     2038   1817   1914    401    -77   -181       C  
ATOM   1552  N   GLN B 145      39.947  45.093  19.164  1.00 22.60           N  
ANISOU 1552  N   GLN B 145     3474   3380   1732    614  -1059   -592       N  
ATOM   1553  CA  GLN B 145      39.528  45.779  17.960  1.00 20.87           C  
ANISOU 1553  CA  GLN B 145     3122   3090   1717    595   -930   -641       C  
ATOM   1554  C   GLN B 145      38.167  45.340  17.456  1.00 25.06           C  
ANISOU 1554  C   GLN B 145     3580   3747   2194    579   -690   -513       C  
ATOM   1555  O   GLN B 145      37.294  46.164  17.202  1.00 26.10           O  
ANISOU 1555  O   GLN B 145     3687   3925   2306    640   -561   -576       O  
ATOM   1556  CB  GLN B 145      40.555  45.567  16.857  1.00 21.58           C  
ANISOU 1556  CB  GLN B 145     3076   2991   2131    495  -1011   -624       C  
ATOM   1557  CG  GLN B 145      40.121  46.146  15.530  1.00 23.93           C  
ANISOU 1557  CG  GLN B 145     3255   3222   2617    467   -872   -640       C  
ATOM   1558  CD  GLN B 145      41.239  46.169  14.524  1.00 23.97           C  
ANISOU 1558  CD  GLN B 145     3152   3033   2923    386   -942   -652       C  
ATOM   1559  OE1 GLN B 145      42.367  46.515  14.858  1.00 17.18           O  
ANISOU 1559  OE1 GLN B 145     2298   2055   2176    386  -1112   -739       O  
ATOM   1560  NE2 GLN B 145      40.941  45.795  13.289  1.00 26.47           N  
ANISOU 1560  NE2 GLN B 145     3369   3318   3372    317   -811   -565       N  
ATOM   1561  N   ILE B 146      37.990  44.041  17.290  1.00 23.53           N  
ANISOU 1561  N   ILE B 146     3341   3596   2004    496   -640   -331       N  
ATOM   1562  CA  ILE B 146      36.793  43.547  16.621  1.00 26.10           C  
ANISOU 1562  CA  ILE B 146     3563   4008   2346    450   -441   -207       C  
ATOM   1563  C   ILE B 146      35.565  43.643  17.525  1.00 31.23           C  
ANISOU 1563  C   ILE B 146     4271   4854   2741    531   -283   -170       C  
ATOM   1564  O   ILE B 146      34.469  43.949  17.063  1.00 47.40           O  
ANISOU 1564  O   ILE B 146     6227   6973   4809    548   -121   -152       O  
ATOM   1565  CB  ILE B 146      36.994  42.104  16.146  1.00 24.23           C  
ANISOU 1565  CB  ILE B 146     3259   3732   2214    328   -442    -35       C  
ATOM   1566  CG1 ILE B 146      38.165  42.062  15.166  1.00 22.49           C  
ANISOU 1566  CG1 ILE B 146     2971   3317   2257    261   -558    -82       C  
ATOM   1567  CG2 ILE B 146      35.738  41.579  15.475  1.00 29.51           C  
ANISOU 1567  CG2 ILE B 146     3819   4483   2910    269   -261     84       C  
ATOM   1568  CD1 ILE B 146      38.619  40.672  14.805  1.00 26.96           C  
ANISOU 1568  CD1 ILE B 146     3493   3810   2939    159   -586     55       C  
ATOM   1569  N   SER B 147      35.760  43.416  18.814  1.00 31.99           N  
ANISOU 1569  N   SER B 147     4519   5037   2598    587   -330   -158       N  
ATOM   1570  CA  SER B 147      34.664  43.409  19.780  1.00 44.62           C  
ANISOU 1570  CA  SER B 147     6194   6831   3927    668   -156   -108       C  
ATOM   1571  C   SER B 147      34.015  44.780  20.006  1.00 51.59           C  
ANISOU 1571  C   SER B 147     7107   7770   4725    803    -57   -284       C  
ATOM   1572  O   SER B 147      32.968  44.877  20.650  1.00 46.83           O  
ANISOU 1572  O   SER B 147     6533   7328   3932    881    135   -252       O  
ATOM   1573  CB  SER B 147      35.164  42.865  21.120  1.00 47.29           C  
ANISOU 1573  CB  SER B 147     6726   7243   4001    702   -248    -56       C  
ATOM   1574  OG  SER B 147      34.098  42.344  21.887  1.00 61.54           O  
ANISOU 1574  OG  SER B 147     8569   9213   5603    717    -41     85       O  
ATOM   1575  N   ASP B 148      34.636  45.834  19.485  1.00 54.70           N  
ANISOU 1575  N   ASP B 148     7489   8021   5273    834   -177   -464       N  
ATOM   1576  CA  ASP B 148      34.165  47.198  19.722  1.00 62.22           C  
ANISOU 1576  CA  ASP B 148     8485   8986   6169    970   -113   -649       C  
ATOM   1577  C   ASP B 148      32.895  47.540  18.960  1.00 56.73           C  
ANISOU 1577  C   ASP B 148     7626   8345   5583    995     98   -608       C  
ATOM   1578  O   ASP B 148      32.092  48.361  19.401  1.00 59.71           O  
ANISOU 1578  O   ASP B 148     8027   8794   5865   1121    231   -698       O  
ATOM   1579  CB  ASP B 148      35.251  48.204  19.343  1.00 67.69           C  
ANISOU 1579  CB  ASP B 148     9203   9483   7034    980   -313   -839       C  
ATOM   1580  CG  ASP B 148      36.300  48.357  20.416  1.00 78.46           C  
ANISOU 1580  CG  ASP B 148    10732  10788   8291    991   -510   -932       C  
ATOM   1581  OD1 ASP B 148      36.011  48.009  21.582  1.00 83.66           O  
ANISOU 1581  OD1 ASP B 148    11511  11561   8717   1018   -463   -883       O  
ATOM   1582  OD2 ASP B 148      37.412  48.830  20.094  1.00 81.06           O  
ANISOU 1582  OD2 ASP B 148    11049  10941   8808    952   -703  -1032       O  
ATOM   1583  N   ILE B 149      32.722  46.896  17.818  1.00 47.37           N  
ANISOU 1583  N   ILE B 149     6274   7115   4608    875    118   -471       N  
ATOM   1584  CA  ILE B 149      31.776  47.356  16.815  1.00 43.34           C  
ANISOU 1584  CA  ILE B 149     5597   6603   4266    884    238   -451       C  
ATOM   1585  C   ILE B 149      30.320  47.401  17.283  1.00 45.75           C  
ANISOU 1585  C   ILE B 149     5837   7088   4458    969    467   -392       C  
ATOM   1586  O   ILE B 149      29.839  46.504  17.979  1.00 43.86           O  
ANISOU 1586  O   ILE B 149     5609   6988   4066    945    576   -261       O  
ATOM   1587  CB  ILE B 149      31.874  46.480  15.556  1.00 40.84           C  
ANISOU 1587  CB  ILE B 149     5141   6219   4158    729    201   -309       C  
ATOM   1588  CG1 ILE B 149      30.881  46.954  14.502  1.00 42.21           C  
ANISOU 1588  CG1 ILE B 149     5154   6397   4488    738    294   -283       C  
ATOM   1589  CG2 ILE B 149      31.638  45.015  15.896  1.00 41.98           C  
ANISOU 1589  CG2 ILE B 149     5269   6459   4224    628    250   -126       C  
ATOM   1590  CD1 ILE B 149      31.058  46.292  13.184  1.00 42.97           C  
ANISOU 1590  CD1 ILE B 149     5148   6409   4771    598    234   -186       C  
ATOM   1591  N   GLN B 150      29.646  48.491  16.924  1.00 40.32           N  
ANISOU 1591  N   GLN B 150     5076   6386   3856   1074    544   -485       N  
ATOM   1592  CA  GLN B 150      28.197  48.566  16.987  1.00 40.38           C  
ANISOU 1592  CA  GLN B 150     4948   6523   3873   1132    752   -408       C  
ATOM   1593  C   GLN B 150      27.690  49.108  15.652  1.00 39.50           C  
ANISOU 1593  C   GLN B 150     4656   6342   4012   1131    744   -397       C  
ATOM   1594  O   GLN B 150      28.351  49.926  15.007  1.00 41.44           O  
ANISOU 1594  O   GLN B 150     4934   6431   4381   1148    614   -506       O  
ATOM   1595  CB  GLN B 150      27.731  49.430  18.158  1.00 50.09           C  
ANISOU 1595  CB  GLN B 150     6287   7765   4980   1252    845   -517       C  
ATOM   1596  CG  GLN B 150      28.685  50.536  18.551  1.00 56.01           C  
ANISOU 1596  CG  GLN B 150     7210   8380   5690   1332    705   -730       C  
ATOM   1597  CD  GLN B 150      28.445  51.014  19.964  1.00 71.40           C  
ANISOU 1597  CD  GLN B 150     9316  10370   7443   1418    782   -823       C  
ATOM   1598  OE1 GLN B 150      28.548  50.243  20.920  1.00 78.32           O  
ANISOU 1598  OE1 GLN B 150    10301  11345   8113   1390    815   -760       O  
ATOM   1599  NE2 GLN B 150      28.104  52.288  20.106  1.00 77.42           N  
ANISOU 1599  NE2 GLN B 150    10097  11050   8269   1520    817   -965       N  
ATOM   1600  N   VAL B 151      26.532  48.618  15.222  1.00 36.71           N  
ANISOU 1600  N   VAL B 151     4121   6065   3762   1077    851   -246       N  
ATOM   1601  CA  VAL B 151      26.021  48.898  13.882  1.00 30.19           C  
ANISOU 1601  CA  VAL B 151     3124   5179   3167   1044    807   -197       C  
ATOM   1602  C   VAL B 151      24.541  49.223  13.939  1.00 33.89           C  
ANISOU 1602  C   VAL B 151     3450   5692   3733   1083    934   -138       C  
ATOM   1603  O   VAL B 151      23.790  48.542  14.638  1.00 36.81           O  
ANISOU 1603  O   VAL B 151     3774   6169   4043   1052   1063    -45       O  
ATOM   1604  CB  VAL B 151      26.219  47.694  12.929  1.00 29.51           C  
ANISOU 1604  CB  VAL B 151     2950   5090   3173    865    724    -51       C  
ATOM   1605  CG1 VAL B 151      25.898  48.086  11.491  1.00 29.39           C  
ANISOU 1605  CG1 VAL B 151     2810   4991   3365    832    635    -24       C  
ATOM   1606  CG2 VAL B 151      27.632  47.164  13.014  1.00 36.49           C  
ANISOU 1606  CG2 VAL B 151     3999   5871   3995    769    583    -82       C  
ATOM   1607  N   SER B 152      24.109  50.248  13.208  1.00 33.99           N  
ANISOU 1607  N   SER B 152     3391   5615   3910   1148    899   -186       N  
ATOM   1608  CA  SER B 152      22.683  50.565  13.172  1.00 44.76           C  
ANISOU 1608  CA  SER B 152     4595   7015   5396   1188   1006   -132       C  
ATOM   1609  C   SER B 152      21.935  49.416  12.505  1.00 46.67           C  
ANISOU 1609  C   SER B 152     4664   7327   5743   1045    997     42       C  
ATOM   1610  O   SER B 152      22.302  48.971  11.412  1.00 48.59           O  
ANISOU 1610  O   SER B 152     4869   7526   6067    942    858    101       O  
ATOM   1611  CB  SER B 152      22.419  51.886  12.447  1.00 49.15           C  
ANISOU 1611  CB  SER B 152     5109   7444   6120   1283    948   -206       C  
ATOM   1612  OG  SER B 152      23.016  51.900  11.164  1.00 57.48           O  
ANISOU 1612  OG  SER B 152     6155   8407   7277   1216    779   -175       O  
ATOM   1613  N   GLY B 153      20.915  48.915  13.194  1.00 46.24           N  
ANISOU 1613  N   GLY B 153     4515   7371   5683   1032   1145    117       N  
ATOM   1614  CA  GLY B 153      20.125  47.802  12.702  1.00 45.47           C  
ANISOU 1614  CA  GLY B 153     4254   7325   5698    889   1139    273       C  
ATOM   1615  C   GLY B 153      20.452  46.476  13.367  1.00 48.66           C  
ANISOU 1615  C   GLY B 153     4716   7799   5974    773   1190    369       C  
ATOM   1616  O   GLY B 153      19.795  45.469  13.102  1.00 51.91           O  
ANISOU 1616  O   GLY B 153     5007   8238   6480    645   1194    495       O  
ATOM   1617  N   GLN B 154      21.461  46.470  14.235  1.00 42.88           N  
ANISOU 1617  N   GLN B 154     4175   7084   5034    816   1215    307       N  
ATOM   1618  CA  GLN B 154      21.923  45.229  14.848  1.00 42.01           C  
ANISOU 1618  CA  GLN B 154     4143   7024   4794    709   1240    405       C  
ATOM   1619  C   GLN B 154      20.869  44.602  15.752  1.00 53.46           C  
ANISOU 1619  C   GLN B 154     5527   8561   6226    682   1420    509       C  
ATOM   1620  O   GLN B 154      20.162  45.298  16.484  1.00 56.52           O  
ANISOU 1620  O   GLN B 154     5901   8996   6578    796   1570    455       O  
ATOM   1621  CB  GLN B 154      23.221  45.462  15.635  1.00 45.11           C  
ANISOU 1621  CB  GLN B 154     4764   7416   4958    777   1210    305       C  
ATOM   1622  CG  GLN B 154      23.114  46.380  16.848  1.00 43.66           C  
ANISOU 1622  CG  GLN B 154     4712   7268   4610    935   1329    182       C  
ATOM   1623  CD  GLN B 154      24.477  46.704  17.451  1.00 42.64           C  
ANISOU 1623  CD  GLN B 154     4818   7107   4275    995   1235     54       C  
ATOM   1624  OE1 GLN B 154      25.458  46.866  16.733  1.00 42.96           O  
ANISOU 1624  OE1 GLN B 154     4898   7071   4352    978   1078     -8       O  
ATOM   1625  NE2 GLN B 154      24.538  46.798  18.773  1.00 42.94           N  
ANISOU 1625  NE2 GLN B 154     5017   7198   4100   1062   1323      8       N  
ATOM   1626  N   SER B 155      20.761  43.279  15.679  1.00 58.80           N  
ANISOU 1626  N   SER B 155     6158   9245   6938    528   1409    654       N  
ATOM   1627  CA  SER B 155      19.852  42.531  16.538  1.00 61.69           C  
ANISOU 1627  CA  SER B 155     6469   9681   7291    483   1579    769       C  
ATOM   1628  C   SER B 155      20.437  42.426  17.942  1.00 64.69           C  
ANISOU 1628  C   SER B 155     7058  10122   7401    544   1686    759       C  
ATOM   1629  O   SER B 155      21.462  43.038  18.247  1.00 67.07           O  
ANISOU 1629  O   SER B 155     7537  10412   7536    633   1621    643       O  
ATOM   1630  CB  SER B 155      19.574  41.141  15.961  1.00 59.11           C  
ANISOU 1630  CB  SER B 155     6037   9311   7110    292   1513    920       C  
ATOM   1631  OG  SER B 155      18.966  41.237  14.684  1.00 54.56           O  
ANISOU 1631  OG  SER B 155     5285   8679   6765    235   1398    917       O  
ATOM   1632  N   GLU B 156      19.795  41.633  18.790  1.00 65.04           N  
ANISOU 1632  N   GLU B 156     7087  10226   7400    492   1840    877       N  
ATOM   1633  CA  GLU B 156      20.069  41.686  20.224  1.00 68.54           C  
ANISOU 1633  CA  GLU B 156     7726  10742   7573    569   1974    864       C  
ATOM   1634  C   GLU B 156      21.352  40.947  20.611  1.00 59.67           C  
ANISOU 1634  C   GLU B 156     6810   9591   6271    514   1857    906       C  
ATOM   1635  O   GLU B 156      22.329  41.565  21.037  1.00 60.15           O  
ANISOU 1635  O   GLU B 156     7064   9649   6141    608   1782    785       O  
ATOM   1636  CB  GLU B 156      18.882  41.119  21.020  1.00 77.54           C  
ANISOU 1636  CB  GLU B 156     8777  11961   8722    533   2201    984       C  
ATOM   1637  CG  GLU B 156      17.462  41.410  20.484  1.00 82.10           C  
ANISOU 1637  CG  GLU B 156     9085  12558   9553    531   2303   1001       C  
ATOM   1638  CD  GLU B 156      17.302  42.740  19.744  1.00 87.47           C  
ANISOU 1638  CD  GLU B 156     9683  13208  10345    651   2238    844       C  
ATOM   1639  OE1 GLU B 156      17.777  43.777  20.253  1.00 88.48           O  
ANISOU 1639  OE1 GLU B 156     9960  13348  10312    797   2261    695       O  
ATOM   1640  OE2 GLU B 156      16.695  42.745  18.648  1.00 88.88           O  
ANISOU 1640  OE2 GLU B 156     9654  13340  10777    596   2153    868       O  
ATOM   1641  N   ASP B 157      21.347  39.626  20.465  1.00 55.03           N  
ANISOU 1641  N   ASP B 157     6181   8969   5758    361   1830   1071       N  
ATOM   1642  CA  ASP B 157      22.504  38.833  20.849  1.00 58.70           C  
ANISOU 1642  CA  ASP B 157     6830   9395   6078    304   1720   1131       C  
ATOM   1643  C   ASP B 157      23.389  38.536  19.653  1.00 51.51           C  
ANISOU 1643  C   ASP B 157     5885   8379   5307    222   1502   1118       C  
ATOM   1644  O   ASP B 157      24.006  37.475  19.579  1.00 51.49           O  
ANISOU 1644  O   ASP B 157     5934   8311   5321    112   1412   1222       O  
ATOM   1645  CB  ASP B 157      22.071  37.532  21.530  1.00 67.96           C  
ANISOU 1645  CB  ASP B 157     8010  10576   7236    191   1824   1322       C  
ATOM   1646  CG  ASP B 157      20.930  37.741  22.521  1.00 78.96           C  
ANISOU 1646  CG  ASP B 157     9376  12077   8547    245   2073   1356       C  
ATOM   1647  OD1 ASP B 157      20.671  38.906  22.897  1.00 79.68           O  
ANISOU 1647  OD1 ASP B 157     9499  12238   8537    386   2160   1218       O  
ATOM   1648  OD2 ASP B 157      20.311  36.735  22.932  1.00 84.31           O  
ANISOU 1648  OD2 ASP B 157    10005  12763   9265    145   2187   1517       O  
ATOM   1649  N   MET B 158      23.452  39.489  18.725  1.00 44.60           N  
ANISOU 1649  N   MET B 158     4928   7483   4535    278   1424    989       N  
ATOM   1650  CA  MET B 158      24.404  39.411  17.621  1.00 35.53           C  
ANISOU 1650  CA  MET B 158     3772   6245   3482    219   1229    949       C  
ATOM   1651  C   MET B 158      25.827  39.409  18.157  1.00 31.09           C  
ANISOU 1651  C   MET B 158     3425   5667   2719    257   1122    904       C  
ATOM   1652  O   MET B 158      26.143  40.159  19.072  1.00 36.20           O  
ANISOU 1652  O   MET B 158     4226   6368   3161    387   1153    805       O  
ATOM   1653  CB  MET B 158      24.219  40.579  16.652  1.00 35.63           C  
ANISOU 1653  CB  MET B 158     3682   6244   3610    292   1179    812       C  
ATOM   1654  CG  MET B 158      23.353  40.276  15.435  1.00 36.94           C  
ANISOU 1654  CG  MET B 158     3638   6358   4038    188   1136    863       C  
ATOM   1655  SD  MET B 158      23.166  41.728  14.371  1.00 42.02           S  
ANISOU 1655  SD  MET B 158     4191   6978   4797    291   1066    713       S  
ATOM   1656  CE  MET B 158      22.970  40.959  12.764  1.00 45.14           C  
ANISOU 1656  CE  MET B 158     4452   7267   5432    116    900    773       C  
ATOM   1657  N   THR B 159      26.683  38.559  17.603  1.00 28.16           N  
ANISOU 1657  N   THR B 159     3074   5210   2414    143    984    970       N  
ATOM   1658  CA  THR B 159      28.102  38.596  17.943  1.00 29.49           C  
ANISOU 1658  CA  THR B 159     3429   5346   2428    176    844    923       C  
ATOM   1659  C   THR B 159      28.755  39.779  17.242  1.00 29.40           C  
ANISOU 1659  C   THR B 159     3435   5277   2459    256    723    721       C  
ATOM   1660  O   THR B 159      28.161  40.372  16.336  1.00 27.03           O  
ANISOU 1660  O   THR B 159     2993   4964   2313    262    747    659       O  
ATOM   1661  CB  THR B 159      28.827  37.296  17.541  1.00 29.27           C  
ANISOU 1661  CB  THR B 159     3411   5208   2501     26    726   1055       C  
ATOM   1662  OG1 THR B 159      28.840  37.178  16.114  1.00 28.47           O  
ANISOU 1662  OG1 THR B 159     3174   4992   2652    -72    639   1014       O  
ATOM   1663  CG2 THR B 159      28.136  36.077  18.153  1.00 33.23           C  
ANISOU 1663  CG2 THR B 159     3895   5696   3034    -63    821   1228       C  
ATOM   1664  N   ALA B 160      29.976  40.116  17.651  1.00 31.44           N  
ANISOU 1664  N   ALA B 160     3866   5459   2620    311    569    610       N  
ATOM   1665  CA  ALA B 160      30.724  41.187  16.995  1.00 29.82           C  
ANISOU 1665  CA  ALA B 160     3683   5136   2510    366    429    411       C  
ATOM   1666  C   ALA B 160      30.951  40.853  15.531  1.00 23.22           C  
ANISOU 1666  C   ALA B 160     2723   4161   1937    247    343    419       C  
ATOM   1667  O   ALA B 160      30.807  41.708  14.656  1.00 21.01           O  
ANISOU 1667  O   ALA B 160     2373   3832   1778    275    326    316       O  
ATOM   1668  CB  ALA B 160      32.050  41.427  17.695  1.00 27.25           C  
ANISOU 1668  CB  ALA B 160     3543   4739   2071    418    258    312       C  
ATOM   1669  N   LYS B 161      31.305  39.602  15.263  1.00 19.70           N  
ANISOU 1669  N   LYS B 161     2263   3647   1574    119    292    544       N  
ATOM   1670  CA  LYS B 161      31.488  39.144  13.896  1.00 23.12           C  
ANISOU 1670  CA  LYS B 161     2601   3952   2233      2    225    550       C  
ATOM   1671  C   LYS B 161      30.218  39.342  13.061  1.00 20.68           C  
ANISOU 1671  C   LYS B 161     2130   3704   2024    -30    321    577       C  
ATOM   1672  O   LYS B 161      30.271  39.807  11.921  1.00 17.81           O  
ANISOU 1672  O   LYS B 161     1712   3264   1791    -47    265    500       O  
ATOM   1673  CB  LYS B 161      31.901  37.677  13.896  1.00 28.87           C  
ANISOU 1673  CB  LYS B 161     3342   4602   3024   -121    180    687       C  
ATOM   1674  CG  LYS B 161      31.996  37.054  12.530  1.00 34.76           C  
ANISOU 1674  CG  LYS B 161     4005   5219   3984   -245    129    692       C  
ATOM   1675  CD  LYS B 161      32.477  35.626  12.665  1.00 38.08           C  
ANISOU 1675  CD  LYS B 161     4455   5543   4470   -349     85    814       C  
ATOM   1676  CE  LYS B 161      32.364  34.880  11.367  1.00 36.62           C  
ANISOU 1676  CE  LYS B 161     4195   5238   4480   -477     58    819       C  
ATOM   1677  NZ  LYS B 161      32.917  33.508  11.515  1.00 33.86           N  
ANISOU 1677  NZ  LYS B 161     3884   4767   4215   -567     13    923       N  
ATOM   1678  N   GLU B 162      29.076  38.993  13.638  1.00 18.99           N  
ANISOU 1678  N   GLU B 162     1835   3629   1750    -35    466    696       N  
ATOM   1679  CA  GLU B 162      27.804  39.166  12.947  1.00 19.32           C  
ANISOU 1679  CA  GLU B 162     1695   3738   1906    -62    549    734       C  
ATOM   1680  C   GLU B 162      27.485  40.638  12.702  1.00 23.20           C  
ANISOU 1680  C   GLU B 162     2157   4267   2392     76    568    597       C  
ATOM   1681  O   GLU B 162      26.899  40.986  11.678  1.00 20.13           O  
ANISOU 1681  O   GLU B 162     1645   3861   2141     56    543    579       O  
ATOM   1682  CB  GLU B 162      26.676  38.510  13.744  1.00 21.41           C  
ANISOU 1682  CB  GLU B 162     1867   4136   2130    -91    716    894       C  
ATOM   1683  CG  GLU B 162      26.720  36.990  13.722  1.00 25.74           C  
ANISOU 1683  CG  GLU B 162     2421   4591   2768   -245    677   1027       C  
ATOM   1684  CD  GLU B 162      25.689  36.364  14.638  1.00 34.26           C  
ANISOU 1684  CD  GLU B 162     3466   5722   3828   -257    811   1140       C  
ATOM   1685  OE1 GLU B 162      25.185  37.063  15.543  1.00 30.15           O  
ANISOU 1685  OE1 GLU B 162     2963   5317   3174   -139    943   1123       O  
ATOM   1686  OE2 GLU B 162      25.381  35.167  14.454  1.00 42.10           O  
ANISOU 1686  OE2 GLU B 162     4420   6631   4944   -383    791   1238       O  
ATOM   1687  N   LYS B 163      27.860  41.499  13.644  1.00 20.09           N  
ANISOU 1687  N   LYS B 163     1882   3914   1838    217    600    499       N  
ATOM   1688  CA  LYS B 163      27.647  42.934  13.475  1.00 19.79           C  
ANISOU 1688  CA  LYS B 163     1832   3881   1804    358    613    356       C  
ATOM   1689  C   LYS B 163      28.535  43.481  12.369  1.00 20.19           C  
ANISOU 1689  C   LYS B 163     1921   3769   1982    338    452    247       C  
ATOM   1690  O   LYS B 163      28.096  44.315  11.577  1.00 18.66           O  
ANISOU 1690  O   LYS B 163     1648   3551   1891    384    443    196       O  
ATOM   1691  CB  LYS B 163      27.910  43.691  14.780  1.00 21.60           C  
ANISOU 1691  CB  LYS B 163     2207   4176   1825    510    674    256       C  
ATOM   1692  CG  LYS B 163      26.844  43.479  15.846  1.00 23.51           C  
ANISOU 1692  CG  LYS B 163     2410   4600   1923    572    886    346       C  
ATOM   1693  CD  LYS B 163      27.260  44.149  17.140  1.00 28.47           C  
ANISOU 1693  CD  LYS B 163     3233   5279   2306    718    924    229       C  
ATOM   1694  CE  LYS B 163      26.332  43.783  18.286  1.00 37.53           C  
ANISOU 1694  CE  LYS B 163     4401   6511   3346    732   1092    316       C  
ATOM   1695  NZ  LYS B 163      26.836  44.331  19.580  1.00 38.79           N  
ANISOU 1695  NZ  LYS B 163     4787   6691   3260    845   1095    199       N  
ATOM   1696  N   LEU B 164      29.784  43.021  12.312  1.00 16.78           N  
ANISOU 1696  N   LEU B 164     1603   3221   1550    274    332    222       N  
ATOM   1697  CA  LEU B 164      30.690  43.466  11.256  1.00 15.15           C  
ANISOU 1697  CA  LEU B 164     1428   2856   1473    248    207    133       C  
ATOM   1698  C   LEU B 164      30.208  42.983   9.891  1.00 15.47           C  
ANISOU 1698  C   LEU B 164     1360   2859   1658    139    187    201       C  
ATOM   1699  O   LEU B 164      30.370  43.674   8.884  1.00 15.04           O  
ANISOU 1699  O   LEU B 164     1296   2724   1695    149    135    142       O  
ATOM   1700  CB  LEU B 164      32.117  42.977  11.503  1.00 14.46           C  
ANISOU 1700  CB  LEU B 164     1458   2654   1383    201     95    103       C  
ATOM   1701  CG  LEU B 164      33.197  43.506  10.554  1.00 15.42           C  
ANISOU 1701  CG  LEU B 164     1612   2606   1643    184     -8      8       C  
ATOM   1702  CD1 LEU B 164      33.365  45.028  10.701  1.00 17.73           C  
ANISOU 1702  CD1 LEU B 164     1941   2863   1933    308    -24   -130       C  
ATOM   1703  CD2 LEU B 164      34.517  42.806  10.822  1.00 17.51           C  
ANISOU 1703  CD2 LEU B 164     1951   2764   1938    130   -106      5       C  
ATOM   1704  N   LEU B 165      29.613  41.797   9.849  1.00 14.70           N  
ANISOU 1704  N   LEU B 165     1191   2816   1579     31    222    328       N  
ATOM   1705  CA  LEU B 165      29.085  41.317   8.581  1.00 14.24           C  
ANISOU 1705  CA  LEU B 165     1039   2724   1647    -77    182    378       C  
ATOM   1706  C   LEU B 165      27.892  42.183   8.155  1.00 16.52           C  
ANISOU 1706  C   LEU B 165     1200   3099   1978    -10    220    378       C  
ATOM   1707  O   LEU B 165      27.779  42.561   6.983  1.00 16.86           O  
ANISOU 1707  O   LEU B 165     1218   3085   2102    -28    147    352       O  
ATOM   1708  CB  LEU B 165      28.695  39.843   8.667  1.00 14.78           C  
ANISOU 1708  CB  LEU B 165     1054   2812   1750   -216    199    506       C  
ATOM   1709  CG  LEU B 165      28.378  39.158   7.329  1.00 20.63           C  
ANISOU 1709  CG  LEU B 165     1736   3485   2618   -349    122    533       C  
ATOM   1710  CD1 LEU B 165      29.640  38.942   6.481  1.00 20.19           C  
ANISOU 1710  CD1 LEU B 165     1806   3265   2601   -395     29    452       C  
ATOM   1711  CD2 LEU B 165      27.647  37.838   7.562  1.00 19.45           C  
ANISOU 1711  CD2 LEU B 165     1516   3355   2520   -469    149    654       C  
ATOM   1712  N   LEU B 166      27.030  42.527   9.107  1.00 17.89           N  
ANISOU 1712  N   LEU B 166     1299   3406   2092     79    338    410       N  
ATOM   1713  CA  LEU B 166      25.908  43.417   8.817  1.00 19.62           C  
ANISOU 1713  CA  LEU B 166     1380   3702   2372    168    384    408       C  
ATOM   1714  C   LEU B 166      26.378  44.786   8.317  1.00 17.42           C  
ANISOU 1714  C   LEU B 166     1170   3338   2113    284    324    284       C  
ATOM   1715  O   LEU B 166      25.820  45.333   7.361  1.00 21.87           O  
ANISOU 1715  O   LEU B 166     1650   3884   2774    303    272    291       O  
ATOM   1716  CB  LEU B 166      25.025  43.594  10.058  1.00 20.85           C  
ANISOU 1716  CB  LEU B 166     1458   4010   2454    265    557    448       C  
ATOM   1717  CG  LEU B 166      23.879  44.592   9.920  1.00 24.20           C  
ANISOU 1717  CG  LEU B 166     1781   4453   2960    374    602    421       C  
ATOM   1718  CD1 LEU B 166      22.925  44.149   8.823  1.00 24.96           C  
ANISOU 1718  CD1 LEU B 166     1747   4514   3223    266    518    498       C  
ATOM   1719  CD2 LEU B 166      23.146  44.764  11.241  1.00 25.62           C  
ANISOU 1719  CD2 LEU B 166     1949   4728   3056    466    777    431       C  
ATOM   1720  N   TRP B 167      27.395  45.340   8.967  1.00 18.81           N  
ANISOU 1720  N   TRP B 167     1495   3451   2202    359    319    179       N  
ATOM   1721  CA  TRP B 167      27.966  46.615   8.536  1.00 18.74           C  
ANISOU 1721  CA  TRP B 167     1558   3331   2233    454    260     63       C  
ATOM   1722  C   TRP B 167      28.460  46.535   7.101  1.00 19.06           C  
ANISOU 1722  C   TRP B 167     1619   3250   2373    362    147     76       C  
ATOM   1723  O   TRP B 167      28.174  47.423   6.289  1.00 17.61           O  
ANISOU 1723  O   TRP B 167     1407   3021   2263    417    111     62       O  
ATOM   1724  CB  TRP B 167      29.113  47.031   9.453  1.00 17.19           C  
ANISOU 1724  CB  TRP B 167     1517   3068   1946    514    243    -53       C  
ATOM   1725  CG  TRP B 167      29.769  48.329   9.071  1.00 16.14           C  
ANISOU 1725  CG  TRP B 167     1454   2797   1880    598    182   -173       C  
ATOM   1726  CD1 TRP B 167      29.343  49.588   9.389  1.00 21.13           C  
ANISOU 1726  CD1 TRP B 167     2081   3424   2525    747    223   -259       C  
ATOM   1727  CD2 TRP B 167      30.989  48.495   8.331  1.00 17.38           C  
ANISOU 1727  CD2 TRP B 167     1694   2790   2120    537     81   -216       C  
ATOM   1728  NE1 TRP B 167      30.220  50.522   8.893  1.00 19.85           N  
ANISOU 1728  NE1 TRP B 167     1996   3095   2452    774    141   -348       N  
ATOM   1729  CE2 TRP B 167      31.233  49.880   8.235  1.00 19.89           C  
ANISOU 1729  CE2 TRP B 167     2049   3006   2503    644     61   -317       C  
ATOM   1730  CE3 TRP B 167      31.896  47.606   7.744  1.00 14.63           C  
ANISOU 1730  CE3 TRP B 167     1384   2362   1810    406     19   -178       C  
ATOM   1731  CZ2 TRP B 167      32.344  50.402   7.565  1.00 16.87           C  
ANISOU 1731  CZ2 TRP B 167     1734   2449   2226    613    -14   -366       C  
ATOM   1732  CZ3 TRP B 167      32.996  48.126   7.079  1.00 12.22           C  
ANISOU 1732  CZ3 TRP B 167     1144   1895   1605    386    -43   -234       C  
ATOM   1733  CH2 TRP B 167      33.208  49.513   6.996  1.00 15.06           C  
ANISOU 1733  CH2 TRP B 167     1532   2160   2031    484    -57   -320       C  
ATOM   1734  N   SER B 168      29.209  45.478   6.795  1.00 13.35           N  
ANISOU 1734  N   SER B 168      955   2471   1647    231     97    106       N  
ATOM   1735  CA  SER B 168      29.723  45.261   5.438  1.00 13.25           C  
ANISOU 1735  CA  SER B 168      982   2347   1705    140     14    114       C  
ATOM   1736  C   SER B 168      28.590  45.175   4.419  1.00 17.02           C  
ANISOU 1736  C   SER B 168     1355   2879   2232    103    -21    189       C  
ATOM   1737  O   SER B 168      28.668  45.751   3.336  1.00 16.73           O  
ANISOU 1737  O   SER B 168     1348   2775   2232    110    -81    182       O  
ATOM   1738  CB  SER B 168      30.557  43.980   5.382  1.00 11.91           C  
ANISOU 1738  CB  SER B 168      876   2119   1531     13    -12    135       C  
ATOM   1739  OG  SER B 168      31.604  44.038   6.328  1.00 15.20           O  
ANISOU 1739  OG  SER B 168     1376   2485   1913     49     -7     75       O  
ATOM   1740  N   GLN B 169      27.534  44.457   4.781  1.00 15.74           N  
ANISOU 1740  N   GLN B 169     1068   2839   2074     61     11    270       N  
ATOM   1741  CA  GLN B 169      26.368  44.313   3.913  1.00 18.22           C  
ANISOU 1741  CA  GLN B 169     1252   3213   2456     19    -45    345       C  
ATOM   1742  C   GLN B 169      25.696  45.654   3.654  1.00 22.43           C  
ANISOU 1742  C   GLN B 169     1716   3772   3035    159    -52    334       C  
ATOM   1743  O   GLN B 169      25.332  45.949   2.517  1.00 19.58           O  
ANISOU 1743  O   GLN B 169     1337   3384   2717    145   -154    363       O  
ATOM   1744  CB  GLN B 169      25.373  43.326   4.518  1.00 18.36           C  
ANISOU 1744  CB  GLN B 169     1128   3345   2502    -52      7    436       C  
ATOM   1745  CG  GLN B 169      25.855  41.888   4.417  1.00 17.99           C  
ANISOU 1745  CG  GLN B 169     1147   3241   2449   -211    -22    465       C  
ATOM   1746  CD  GLN B 169      25.082  40.934   5.295  1.00 20.05           C  
ANISOU 1746  CD  GLN B 169     1341   3553   2725   -264     56    542       C  
ATOM   1747  OE1 GLN B 169      24.339  41.349   6.190  1.00 18.67           O  
ANISOU 1747  OE1 GLN B 169     1079   3474   2540   -178    161    573       O  
ATOM   1748  NE2 GLN B 169      25.254  39.645   5.049  1.00 16.92           N  
ANISOU 1748  NE2 GLN B 169      992   3081   2355   -398     15    571       N  
ATOM   1749  N   ARG B 170      25.533  46.460   4.702  1.00 16.04           N  
ANISOU 1749  N   ARG B 170      880   3007   2209    299     51    292       N  
ATOM   1750  CA  ARG B 170      24.914  47.778   4.557  1.00 16.99           C  
ANISOU 1750  CA  ARG B 170      934   3131   2391    451     57    273       C  
ATOM   1751  C   ARG B 170      25.753  48.710   3.682  1.00 16.16           C  
ANISOU 1751  C   ARG B 170      964   2877   2301    490    -26    219       C  
ATOM   1752  O   ARG B 170      25.209  49.470   2.869  1.00 16.85           O  
ANISOU 1752  O   ARG B 170     1003   2941   2459    550    -91    255       O  
ATOM   1753  CB  ARG B 170      24.684  48.422   5.926  1.00 17.96           C  
ANISOU 1753  CB  ARG B 170     1038   3309   2477    595    198    209       C  
ATOM   1754  CG  ARG B 170      23.645  47.722   6.783  1.00 30.38           C  
ANISOU 1754  CG  ARG B 170     2508   4994   4041    565    306    269       C  
ATOM   1755  CD  ARG B 170      23.582  48.332   8.179  1.00 27.38           C  
ANISOU 1755  CD  ARG B 170     2164   4659   3578    703    456    192       C  
ATOM   1756  NE  ARG B 170      23.378  49.776   8.131  1.00 29.31           N  
ANISOU 1756  NE  ARG B 170     2424   4831   3884    856    462    105       N  
ATOM   1757  CZ  ARG B 170      22.181  50.360   8.095  1.00 37.94           C  
ANISOU 1757  CZ  ARG B 170     3396   5936   5085    925    505    125       C  
ATOM   1758  NH1 ARG B 170      21.080  49.621   8.096  1.00 45.45           N  
ANISOU 1758  NH1 ARG B 170     4198   6973   6097    856    543    223       N  
ATOM   1759  NH2 ARG B 170      22.082  51.681   8.050  1.00 38.63           N  
ANISOU 1759  NH2 ARG B 170     3505   5933   5239   1060    506     45       N  
ATOM   1760  N   MET B 171      27.072  48.645   3.836  1.00 15.57           N  
ANISOU 1760  N   MET B 171     1047   2695   2172    453    -24    146       N  
ATOM   1761  CA  MET B 171      27.955  49.533   3.087  1.00 19.60           C  
ANISOU 1761  CA  MET B 171     1679   3054   2714    482    -75    103       C  
ATOM   1762  C   MET B 171      27.905  49.270   1.577  1.00 19.82           C  
ANISOU 1762  C   MET B 171     1738   3039   2752    393   -171    179       C  
ATOM   1763  O   MET B 171      28.088  50.195   0.790  1.00 16.34           O  
ANISOU 1763  O   MET B 171     1355   2507   2347    445   -211    191       O  
ATOM   1764  CB  MET B 171      29.395  49.408   3.577  1.00 14.87           C  
ANISOU 1764  CB  MET B 171     1215   2350   2085    447    -54     16       C  
ATOM   1765  CG  MET B 171      29.626  49.964   4.976  1.00 18.03           C  
ANISOU 1765  CG  MET B 171     1632   2760   2458    554      7    -83       C  
ATOM   1766  SD  MET B 171      29.531  51.764   5.062  1.00 20.66           S  
ANISOU 1766  SD  MET B 171     1983   2992   2876    727     14   -165       S  
ATOM   1767  CE  MET B 171      31.134  52.212   4.396  1.00 23.59           C  
ANISOU 1767  CE  MET B 171     2492   3150   3321    667    -44   -212       C  
ATOM   1768  N   VAL B 172      27.646  48.029   1.171  1.00 16.03           N  
ANISOU 1768  N   VAL B 172     1235   2621   2235    260   -210    230       N  
ATOM   1769  CA  VAL B 172      27.683  47.703  -0.259  1.00 18.68           C  
ANISOU 1769  CA  VAL B 172     1637   2915   2546    170   -307    280       C  
ATOM   1770  C   VAL B 172      26.305  47.544  -0.901  1.00 20.97           C  
ANISOU 1770  C   VAL B 172     1802   3307   2860    156   -410    367       C  
ATOM   1771  O   VAL B 172      26.202  47.103  -2.049  1.00 19.96           O  
ANISOU 1771  O   VAL B 172     1733   3165   2687     69   -515    403       O  
ATOM   1772  CB  VAL B 172      28.488  46.417  -0.526  1.00 21.09           C  
ANISOU 1772  CB  VAL B 172     2036   3179   2797     22   -305    257       C  
ATOM   1773  CG1 VAL B 172      29.919  46.588  -0.039  1.00 16.30           C  
ANISOU 1773  CG1 VAL B 172     1541   2458   2194     34   -226    180       C  
ATOM   1774  CG2 VAL B 172      27.823  45.196   0.119  1.00 16.91           C  
ANISOU 1774  CG2 VAL B 172     1396   2754   2273    -63   -301    286       C  
ATOM   1775  N   GLU B 173      25.254  47.919  -0.180  1.00 17.79           N  
ANISOU 1775  N   GLU B 173     1225   3003   2529    246   -384    396       N  
ATOM   1776  CA  GLU B 173      23.928  47.998  -0.795  1.00 17.85           C  
ANISOU 1776  CA  GLU B 173     1082   3097   2604    257   -495    485       C  
ATOM   1777  C   GLU B 173      23.943  49.028  -1.914  1.00 18.42           C  
ANISOU 1777  C   GLU B 173     1233   3092   2672    329   -600    522       C  
ATOM   1778  O   GLU B 173      24.609  50.062  -1.805  1.00 18.59           O  
ANISOU 1778  O   GLU B 173     1350   3015   2698    432   -542    486       O  
ATOM   1779  CB  GLU B 173      22.859  48.364   0.231  1.00 24.42           C  
ANISOU 1779  CB  GLU B 173     1752   3997   3528    355   -401    479       C  
ATOM   1780  CG  GLU B 173      22.034  47.175   0.711  1.00 35.36           C  
ANISOU 1780  CG  GLU B 173     3032   5460   4942    246   -369    501       C  
ATOM   1781  CD  GLU B 173      21.396  47.418   2.055  1.00 34.29           C  
ANISOU 1781  CD  GLU B 173     2785   5386   4857    334   -211    484       C  
ATOM   1782  OE1 GLU B 173      21.291  48.591   2.458  1.00 49.35           O  
ANISOU 1782  OE1 GLU B 173     4678   7277   6797    487   -152    447       O  
ATOM   1783  OE2 GLU B 173      21.025  46.433   2.719  1.00 25.55           O  
ANISOU 1783  OE2 GLU B 173     1619   4336   3751    252   -140    508       O  
ATOM   1784  N   GLY B 174      23.205  48.744  -2.984  1.00 19.56           N  
ANISOU 1784  N   GLY B 174     1351   3272   2811    270   -759    593       N  
ATOM   1785  CA  GLY B 174      23.126  49.655  -4.105  1.00 20.45           C  
ANISOU 1785  CA  GLY B 174     1545   3326   2900    336   -880    656       C  
ATOM   1786  C   GLY B 174      24.193  49.428  -5.161  1.00 19.70           C  
ANISOU 1786  C   GLY B 174     1701   3134   2652    247   -914    645       C  
ATOM   1787  O   GLY B 174      24.103  49.988  -6.250  1.00 25.55           O  
ANISOU 1787  O   GLY B 174     2540   3835   3332    275  -1025    714       O  
ATOM   1788  N   TYR B 175      25.204  48.624  -4.845  1.00 18.17           N  
ANISOU 1788  N   TYR B 175     1613   2897   2393    148   -809    562       N  
ATOM   1789  CA  TYR B 175      26.239  48.293  -5.822  1.00 18.68           C  
ANISOU 1789  CA  TYR B 175     1906   2868   2322     63   -806    539       C  
ATOM   1790  C   TYR B 175      25.843  47.045  -6.589  1.00 20.70           C  
ANISOU 1790  C   TYR B 175     2198   3180   2489    -84   -929    537       C  
ATOM   1791  O   TYR B 175      25.677  45.970  -5.998  1.00 28.26           O  
ANISOU 1791  O   TYR B 175     3070   4183   3483   -177   -911    493       O  
ATOM   1792  CB  TYR B 175      27.597  48.079  -5.150  1.00 18.03           C  
ANISOU 1792  CB  TYR B 175     1914   2694   2243     39   -636    449       C  
ATOM   1793  CG  TYR B 175      28.161  49.345  -4.566  1.00 16.87           C  
ANISOU 1793  CG  TYR B 175     1773   2461   2176    167   -537    435       C  
ATOM   1794  CD1 TYR B 175      27.835  49.739  -3.278  1.00 15.28           C  
ANISOU 1794  CD1 TYR B 175     1429   2298   2076    255   -477    399       C  
ATOM   1795  CD2 TYR B 175      29.000  50.165  -5.310  1.00 21.03           C  
ANISOU 1795  CD2 TYR B 175     2454   2862   2676    199   -500    458       C  
ATOM   1796  CE1 TYR B 175      28.325  50.906  -2.747  1.00 17.77           C  
ANISOU 1796  CE1 TYR B 175     1761   2522   2467    371   -404    365       C  
ATOM   1797  CE2 TYR B 175      29.503  51.344  -4.777  1.00 17.85           C  
ANISOU 1797  CE2 TYR B 175     2049   2358   2375    307   -422    442       C  
ATOM   1798  CZ  TYR B 175      29.163  51.707  -3.494  1.00 18.17           C  
ANISOU 1798  CZ  TYR B 175     1952   2432   2518    392   -385    385       C  
ATOM   1799  OH  TYR B 175      29.639  52.882  -2.954  1.00 17.73           O  
ANISOU 1799  OH  TYR B 175     1906   2265   2566    498   -324    348       O  
ATOM   1800  N   GLN B 176      25.721  47.207  -7.896  1.00 25.05           N  
ANISOU 1800  N   GLN B 176     2887   3714   2916   -104  -1053    583       N  
ATOM   1801  CA  GLN B 176      25.329  46.143  -8.816  1.00 35.81           C  
ANISOU 1801  CA  GLN B 176     4323   5117   4167   -237  -1204    568       C  
ATOM   1802  C   GLN B 176      26.202  44.906  -8.689  1.00 31.02           C  
ANISOU 1802  C   GLN B 176     3819   4458   3511   -364  -1104    460       C  
ATOM   1803  O   GLN B 176      27.426  44.986  -8.773  1.00 34.74           O  
ANISOU 1803  O   GLN B 176     4445   4829   3926   -358   -952    412       O  
ATOM   1804  CB  GLN B 176      25.389  46.646 -10.262  1.00 41.66           C  
ANISOU 1804  CB  GLN B 176     5273   5827   4727   -221  -1319    624       C  
ATOM   1805  CG  GLN B 176      24.506  47.844 -10.572  1.00 46.41           C  
ANISOU 1805  CG  GLN B 176     5796   6464   5375    -91  -1440    742       C  
ATOM   1806  CD  GLN B 176      23.049  47.469 -10.737  1.00 52.91           C  
ANISOU 1806  CD  GLN B 176     6447   7374   6282    -99  -1579    733       C  
ATOM   1807  OE1 GLN B 176      22.715  46.317 -11.023  1.00 53.25           O  
ANISOU 1807  OE1 GLN B 176     6493   7445   6294   -219  -1642    662       O  
ATOM   1808  NE2 GLN B 176      22.169  48.443 -10.558  1.00 57.57           N  
ANISOU 1808  NE2 GLN B 176     6889   7993   6993     30  -1625    804       N  
ATOM   1809  N   GLY B 177      25.562  43.764  -8.482  1.00 30.01           N  
ANISOU 1809  N   GLY B 177     3588   4385   3428   -477  -1190    428       N  
ATOM   1810  CA  GLY B 177      26.252  42.492  -8.536  1.00 36.57           C  
ANISOU 1810  CA  GLY B 177     4525   5154   4217   -604  -1133    330       C  
ATOM   1811  C   GLY B 177      27.192  42.167  -7.396  1.00 33.09           C  
ANISOU 1811  C   GLY B 177     4051   4655   3869   -599   -931    281       C  
ATOM   1812  O   GLY B 177      27.930  41.186  -7.477  1.00 36.64           O  
ANISOU 1812  O   GLY B 177     4602   5027   4292   -686   -869    204       O  
ATOM   1813  N   LEU B 178      27.176  42.977  -6.339  1.00 20.22           N  
ANISOU 1813  N   LEU B 178     2286   3054   2344   -491   -838    321       N  
ATOM   1814  CA  LEU B 178      28.009  42.710  -5.176  1.00 15.89           C  
ANISOU 1814  CA  LEU B 178     1704   2463   1872   -480   -677    279       C  
ATOM   1815  C   LEU B 178      27.188  42.025  -4.093  1.00 22.62           C  
ANISOU 1815  C   LEU B 178     2359   3403   2833   -520   -682    308       C  
ATOM   1816  O   LEU B 178      26.044  42.404  -3.848  1.00 26.96           O  
ANISOU 1816  O   LEU B 178     2744   4055   3444   -481   -747    373       O  
ATOM   1817  CB  LEU B 178      28.628  44.010  -4.639  1.00 17.89           C  
ANISOU 1817  CB  LEU B 178     1962   2679   2156   -340   -568    286       C  
ATOM   1818  CG  LEU B 178      29.980  44.410  -5.232  1.00 28.39           C  
ANISOU 1818  CG  LEU B 178     3478   3879   3431   -322   -474    245       C  
ATOM   1819  CD1 LEU B 178      30.041  44.234  -6.735  1.00 20.77           C  
ANISOU 1819  CD1 LEU B 178     2684   2880   2329   -376   -537    250       C  
ATOM   1820  CD2 LEU B 178      30.303  45.836  -4.881  1.00 17.46           C  
ANISOU 1820  CD2 LEU B 178     2080   2455   2098   -192   -413    268       C  
ATOM   1821  N   ARG B 179      27.767  40.999  -3.476  1.00 19.53           N  
ANISOU 1821  N   ARG B 179     1981   2966   2474   -595   -608    270       N  
ATOM   1822  CA  ARG B 179      27.138  40.291  -2.366  1.00 21.84           C  
ANISOU 1822  CA  ARG B 179     2108   3329   2862   -638   -581    314       C  
ATOM   1823  C   ARG B 179      28.126  40.135  -1.242  1.00 18.09           C  
ANISOU 1823  C   ARG B 179     1660   2808   2405   -602   -443    290       C  
ATOM   1824  O   ARG B 179      29.278  39.818  -1.484  1.00 18.50           O  
ANISOU 1824  O   ARG B 179     1850   2747   2432   -623   -399    230       O  
ATOM   1825  CB  ARG B 179      26.662  38.890  -2.775  1.00 19.99           C  
ANISOU 1825  CB  ARG B 179     1892   3049   2655   -758   -635    297       C  
ATOM   1826  CG  ARG B 179      25.576  38.835  -3.790  1.00 25.52           C  
ANISOU 1826  CG  ARG B 179     2567   3780   3348   -791   -777    307       C  
ATOM   1827  CD  ARG B 179      25.125  37.392  -3.944  1.00 24.95           C  
ANISOU 1827  CD  ARG B 179     2495   3651   3332   -897   -810    281       C  
ATOM   1828  NE  ARG B 179      24.695  36.850  -2.657  1.00 21.85           N  
ANISOU 1828  NE  ARG B 179     1971   3284   3047   -894   -708    334       N  
ATOM   1829  CZ  ARG B 179      23.428  36.817  -2.260  1.00 24.68           C  
ANISOU 1829  CZ  ARG B 179     2163   3716   3496   -890   -723    394       C  
ATOM   1830  NH1 ARG B 179      22.475  37.290  -3.054  1.00 28.61           N  
ANISOU 1830  NH1 ARG B 179     2595   4265   4009   -883   -847    404       N  
ATOM   1831  NH2 ARG B 179      23.115  36.316  -1.074  1.00 27.75           N  
ANISOU 1831  NH2 ARG B 179     2457   4127   3961   -892   -616    449       N  
ATOM   1832  N   CYS B 180      27.682  40.335  -0.007  1.00 14.37           N  
ANISOU 1832  N   CYS B 180     1059   2424   1978   -545   -374    339       N  
ATOM   1833  CA  CYS B 180      28.533  40.026   1.136  1.00 12.66           C  
ANISOU 1833  CA  CYS B 180      874   2175   1761   -523   -271    326       C  
ATOM   1834  C   CYS B 180      27.859  38.945   1.982  1.00 19.50           C  
ANISOU 1834  C   CYS B 180     1667   3077   2667   -577   -233    388       C  
ATOM   1835  O   CYS B 180      27.006  39.235   2.822  1.00 20.06           O  
ANISOU 1835  O   CYS B 180     1622   3251   2747   -523   -179    444       O  
ATOM   1836  CB  CYS B 180      28.814  41.277   1.962  1.00 16.76           C  
ANISOU 1836  CB  CYS B 180     1387   2727   2252   -371   -199    303       C  
ATOM   1837  SG  CYS B 180      29.925  40.980   3.350  1.00 21.54           S  
ANISOU 1837  SG  CYS B 180     2055   3295   2836   -338   -115    277       S  
ATOM   1838  N   ASP B 181      28.240  37.697   1.733  1.00 16.76           N  
ANISOU 1838  N   ASP B 181     1401   2624   2343   -668   -248    372       N  
ATOM   1839  CA  ASP B 181      27.618  36.538   2.379  1.00 17.27           C  
ANISOU 1839  CA  ASP B 181     1417   2687   2456   -723   -221    430       C  
ATOM   1840  C   ASP B 181      28.433  35.972   3.533  1.00 19.49           C  
ANISOU 1840  C   ASP B 181     1741   2936   2729   -716   -148    461       C  
ATOM   1841  O   ASP B 181      27.924  35.189   4.338  1.00 18.99           O  
ANISOU 1841  O   ASP B 181     1628   2894   2692   -747   -107    537       O  
ATOM   1842  CB  ASP B 181      27.399  35.432   1.352  1.00 15.15           C  
ANISOU 1842  CB  ASP B 181     1201   2322   2234   -822   -295    393       C  
ATOM   1843  CG  ASP B 181      26.411  35.825   0.274  1.00 22.17           C  
ANISOU 1843  CG  ASP B 181     2037   3256   3130   -847   -395    382       C  
ATOM   1844  OD1 ASP B 181      25.290  36.242   0.631  1.00 23.20           O  
ANISOU 1844  OD1 ASP B 181     2030   3488   3297   -821   -394    443       O  
ATOM   1845  OD2 ASP B 181      26.758  35.720  -0.925  1.00 20.87           O  
ANISOU 1845  OD2 ASP B 181     1972   3025   2932   -888   -474    313       O  
ATOM   1846  N   ASN B 182      29.707  36.335   3.578  1.00 13.84           N  
ANISOU 1846  N   ASN B 182     1113   2159   1985   -682   -139    408       N  
ATOM   1847  CA  ASN B 182      30.641  35.739   4.531  1.00 17.10           C  
ANISOU 1847  CA  ASN B 182     1576   2519   2401   -682   -104    435       C  
ATOM   1848  C   ASN B 182      31.903  36.594   4.634  1.00 14.80           C  
ANISOU 1848  C   ASN B 182     1338   2192   2092   -628   -105    377       C  
ATOM   1849  O   ASN B 182      32.000  37.642   3.989  1.00 13.52           O  
ANISOU 1849  O   ASN B 182     1190   2038   1909   -574   -116    310       O  
ATOM   1850  CB  ASN B 182      30.995  34.309   4.099  1.00 13.83           C  
ANISOU 1850  CB  ASN B 182     1237   1963   2055   -748   -124    413       C  
ATOM   1851  CG  ASN B 182      31.574  34.258   2.695  1.00 13.98           C  
ANISOU 1851  CG  ASN B 182     1345   1871   2095   -760   -157    300       C  
ATOM   1852  OD1 ASN B 182      32.485  35.014   2.365  1.00 12.39           O  
ANISOU 1852  OD1 ASN B 182     1196   1632   1879   -716   -149    240       O  
ATOM   1853  ND2 ASN B 182      31.033  33.383   1.860  1.00 18.83           N  
ANISOU 1853  ND2 ASN B 182     1973   2436   2747   -825   -189    273       N  
ATOM   1854  N   PHE B 183      32.876  36.133   5.415  1.00 11.37           N  
ANISOU 1854  N   PHE B 183      952   1694   1672   -621   -100    394       N  
ATOM   1855  CA  PHE B 183      34.162  36.799   5.467  1.00 10.54           C  
ANISOU 1855  CA  PHE B 183      923   1505   1577   -540   -112    307       C  
ATOM   1856  C   PHE B 183      35.243  35.953   4.799  1.00 11.08           C  
ANISOU 1856  C   PHE B 183     1054   1400   1755   -596   -130    267       C  
ATOM   1857  O   PHE B 183      36.407  35.983   5.206  1.00 12.40           O  
ANISOU 1857  O   PHE B 183     1257   1480   1975   -552   -145    238       O  
ATOM   1858  CB  PHE B 183      34.555  37.118   6.919  1.00 12.67           C  
ANISOU 1858  CB  PHE B 183     1206   1828   1778   -453   -113    332       C  
ATOM   1859  CG  PHE B 183      33.841  38.306   7.492  1.00 15.72           C  
ANISOU 1859  CG  PHE B 183     1562   2354   2055   -354    -81    315       C  
ATOM   1860  CD1 PHE B 183      34.005  39.562   6.927  1.00 16.00           C  
ANISOU 1860  CD1 PHE B 183     1607   2374   2096   -282    -86    218       C  
ATOM   1861  CD2 PHE B 183      33.011  38.171   8.599  1.00 17.25           C  
ANISOU 1861  CD2 PHE B 183     1722   2687   2146   -327    -31    398       C  
ATOM   1862  CE1 PHE B 183      33.359  40.666   7.453  1.00 16.53           C  
ANISOU 1862  CE1 PHE B 183     1649   2550   2083   -180    -55    192       C  
ATOM   1863  CE2 PHE B 183      32.358  39.271   9.129  1.00 16.57           C  
ANISOU 1863  CE2 PHE B 183     1611   2722   1963   -222     19    367       C  
ATOM   1864  CZ  PHE B 183      32.533  40.518   8.561  1.00 14.74           C  
ANISOU 1864  CZ  PHE B 183     1387   2462   1752   -145      0    257       C  
ATOM   1865  N   THR B 184      34.863  35.205   3.765  1.00 12.36           N  
ANISOU 1865  N   THR B 184     1256   1510   1930   -631   -112    225       N  
ATOM   1866  CA  THR B 184      35.848  34.456   2.992  1.00 10.41           C  
ANISOU 1866  CA  THR B 184     1090   1123   1743   -630    -81    142       C  
ATOM   1867  C   THR B 184      35.646  34.712   1.487  1.00 10.34           C  
ANISOU 1867  C   THR B 184     1125   1085   1720   -648    -61     61       C  
ATOM   1868  O   THR B 184      36.132  35.698   0.968  1.00 10.21           O  
ANISOU 1868  O   THR B 184     1133   1053   1694   -617    -43     17       O  
ATOM   1869  CB  THR B 184      35.802  32.942   3.295  1.00 13.92           C  
ANISOU 1869  CB  THR B 184     1548   1511   2230   -672    -79    177       C  
ATOM   1870  OG1 THR B 184      34.499  32.421   3.026  1.00 13.04           O  
ANISOU 1870  OG1 THR B 184     1400   1450   2104   -733    -95    212       O  
ATOM   1871  CG2 THR B 184      36.152  32.673   4.778  1.00 17.01           C  
ANISOU 1871  CG2 THR B 184     1908   1912   2642   -658   -113    283       C  
ATOM   1872  N   THR B 185      34.905  33.841   0.813  1.00 13.92           N  
ANISOU 1872  N   THR B 185     1837   1697   1753   -467   -275    292       N  
ATOM   1873  CA  THR B 185      34.777  33.911  -0.646  1.00 12.23           C  
ANISOU 1873  CA  THR B 185     1640   1447   1559   -459   -312    247       C  
ATOM   1874  C   THR B 185      34.192  35.226  -1.174  1.00 10.13           C  
ANISOU 1874  C   THR B 185     1293   1256   1299   -440   -285    222       C  
ATOM   1875  O   THR B 185      34.514  35.639  -2.290  1.00  9.24           O  
ANISOU 1875  O   THR B 185     1201   1126   1185   -400   -299    178       O  
ATOM   1876  CB  THR B 185      33.924  32.740  -1.171  1.00 13.33           C  
ANISOU 1876  CB  THR B 185     1822   1520   1724   -545   -382    275       C  
ATOM   1877  OG1 THR B 185      32.614  32.799  -0.600  1.00 17.64           O  
ANISOU 1877  OG1 THR B 185     2282   2129   2292   -633   -370    337       O  
ATOM   1878  CG2 THR B 185      34.557  31.407  -0.786  1.00 17.42           C  
ANISOU 1878  CG2 THR B 185     2444   1937   2238   -555   -426    295       C  
ATOM   1879  N   SER B 186      33.330  35.879  -0.397  1.00 11.99           N  
ANISOU 1879  N   SER B 186     1444   1575   1538   -460   -245    251       N  
ATOM   1880  CA  SER B 186      32.698  37.111  -0.868  1.00 10.31           C  
ANISOU 1880  CA  SER B 186     1159   1424   1334   -432   -228    228       C  
ATOM   1881  C   SER B 186      33.722  38.199  -1.156  1.00 10.73           C  
ANISOU 1881  C   SER B 186     1230   1473   1373   -350   -209    177       C  
ATOM   1882  O   SER B 186      33.450  39.114  -1.941  1.00  7.84           O  
ANISOU 1882  O   SER B 186      840   1123   1017   -323   -215    154       O  
ATOM   1883  CB  SER B 186      31.674  37.631   0.152  1.00  9.81           C  
ANISOU 1883  CB  SER B 186     1002   1458   1268   -443   -179    262       C  
ATOM   1884  OG  SER B 186      30.580  36.747   0.285  1.00  9.60           O  
ANISOU 1884  OG  SER B 186      930   1451   1265   -533   -194    323       O  
ATOM   1885  N   TRP B 187      34.889  38.107  -0.514  1.00 14.74           N  
ANISOU 1885  N   TRP B 187     1778   1960   1864   -316   -192    169       N  
ATOM   1886  CA  TRP B 187      35.891  39.172  -0.570  1.00 11.35           C  
ANISOU 1886  CA  TRP B 187     1349   1532   1431   -255   -176    134       C  
ATOM   1887  C   TRP B 187      37.023  38.937  -1.568  1.00 10.43           C  
ANISOU 1887  C   TRP B 187     1279   1366   1319   -227   -188    114       C  
ATOM   1888  O   TRP B 187      37.869  39.811  -1.769  1.00  8.64           O  
ANISOU 1888  O   TRP B 187     1042   1143   1099   -190   -175     98       O  
ATOM   1889  CB  TRP B 187      36.493  39.384   0.830  1.00  8.66           C  
ANISOU 1889  CB  TRP B 187     1009   1211   1070   -231   -156    137       C  
ATOM   1890  CG  TRP B 187      35.447  39.768   1.824  1.00 10.42           C  
ANISOU 1890  CG  TRP B 187     1189   1499   1270   -237   -128    152       C  
ATOM   1891  CD1 TRP B 187      34.614  38.922   2.499  1.00 11.72           C  
ANISOU 1891  CD1 TRP B 187     1342   1696   1418   -283   -111    199       C  
ATOM   1892  CD2 TRP B 187      35.086  41.094   2.223  1.00 10.54           C  
ANISOU 1892  CD2 TRP B 187     1169   1559   1276   -191   -110    124       C  
ATOM   1893  NE1 TRP B 187      33.765  39.638   3.304  1.00 12.19           N  
ANISOU 1893  NE1 TRP B 187     1348   1834   1449   -262    -69    202       N  
ATOM   1894  CE2 TRP B 187      34.033  40.975   3.155  1.00 10.72           C  
ANISOU 1894  CE2 TRP B 187     1154   1653   1266   -197    -71    149       C  
ATOM   1895  CE3 TRP B 187      35.559  42.376   1.892  1.00  8.97           C  
ANISOU 1895  CE3 TRP B 187      973   1343   1093   -145   -124     82       C  
ATOM   1896  CZ2 TRP B 187      33.437  42.087   3.760  1.00 11.59           C  
ANISOU 1896  CZ2 TRP B 187     1230   1822   1351   -138    -43    121       C  
ATOM   1897  CZ3 TRP B 187      34.966  43.481   2.491  1.00 10.54           C  
ANISOU 1897  CZ3 TRP B 187     1151   1580   1275    -96   -112     55       C  
ATOM   1898  CH2 TRP B 187      33.922  43.330   3.420  1.00 14.71           C  
ANISOU 1898  CH2 TRP B 187     1644   2184   1763    -83    -70     68       C  
ATOM   1899  N   ARG B 188      37.061  37.764  -2.186  1.00 11.23           N  
ANISOU 1899  N   ARG B 188     1431   1420   1415   -242   -214    116       N  
ATOM   1900  CA  ARG B 188      38.242  37.395  -2.961  1.00 11.49           C  
ANISOU 1900  CA  ARG B 188     1510   1416   1439   -194   -214     94       C  
ATOM   1901  C   ARG B 188      38.508  38.275  -4.185  1.00 14.81           C  
ANISOU 1901  C   ARG B 188     1924   1853   1852   -164   -198     76       C  
ATOM   1902  O   ARG B 188      39.660  38.420  -4.589  1.00 18.18           O  
ANISOU 1902  O   ARG B 188     2354   2281   2272   -118   -171     69       O  
ATOM   1903  CB  ARG B 188      38.161  35.938  -3.425  1.00 18.47           C  
ANISOU 1903  CB  ARG B 188     2471   2235   2311   -203   -254     88       C  
ATOM   1904  CG  ARG B 188      37.563  35.782  -4.796  1.00 32.15           C  
ANISOU 1904  CG  ARG B 188     4244   3946   4027   -209   -284     66       C  
ATOM   1905  CD  ARG B 188      37.848  34.440  -5.385  1.00 29.23           C  
ANISOU 1905  CD  ARG B 188     3973   3498   3636   -190   -328     42       C  
ATOM   1906  NE  ARG B 188      39.164  34.292  -6.005  1.00 15.99           N  
ANISOU 1906  NE  ARG B 188     2335   1813   1929    -96   -297      8       N  
ATOM   1907  CZ  ARG B 188      39.524  33.152  -6.592  1.00 11.36           C  
ANISOU 1907  CZ  ARG B 188     1846   1157   1313    -49   -332    -27       C  
ATOM   1908  NH1 ARG B 188      38.654  32.148  -6.620  1.00 11.63           N  
ANISOU 1908  NH1 ARG B 188     1953   1112   1353   -104   -411    -30       N  
ATOM   1909  NH2 ARG B 188      40.721  33.001  -7.155  1.00 11.76           N  
ANISOU 1909  NH2 ARG B 188     1922   1215   1331     53   -293    -58       N  
ATOM   1910  N   ASP B 189      37.476  38.843  -4.803  1.00  8.29           N  
ANISOU 1910  N   ASP B 189     1085   1042   1024   -188   -212     76       N  
ATOM   1911  CA  ASP B 189      37.719  39.479  -6.097  1.00  9.25           C  
ANISOU 1911  CA  ASP B 189     1224   1169   1123   -160   -204     67       C  
ATOM   1912  C   ASP B 189      37.987  40.966  -5.931  1.00 13.01           C  
ANISOU 1912  C   ASP B 189     1649   1676   1618   -150   -178     81       C  
ATOM   1913  O   ASP B 189      38.167  41.684  -6.914  1.00 10.51           O  
ANISOU 1913  O   ASP B 189     1343   1364   1285   -135   -170     89       O  
ATOM   1914  CB  ASP B 189      36.561  39.197  -7.083  1.00 11.62           C  
ANISOU 1914  CB  ASP B 189     1557   1456   1404   -184   -254     59       C  
ATOM   1915  CG  ASP B 189      35.283  39.997  -6.807  1.00 10.43           C  
ANISOU 1915  CG  ASP B 189     1344   1338   1281   -217   -276     74       C  
ATOM   1916  OD1 ASP B 189      35.166  40.785  -5.839  1.00  9.41           O  
ANISOU 1916  OD1 ASP B 189     1155   1240   1179   -215   -251     84       O  
ATOM   1917  OD2 ASP B 189      34.343  39.804  -7.607  1.00 10.56           O  
ANISOU 1917  OD2 ASP B 189     1375   1349   1288   -238   -327     70       O  
ATOM   1918  N   GLY B 190      38.037  41.412  -4.672  1.00 10.59           N  
ANISOU 1918  N   GLY B 190     1299   1384   1341   -158   -171     85       N  
ATOM   1919  CA  GLY B 190      38.368  42.791  -4.362  1.00 11.36           C  
ANISOU 1919  CA  GLY B 190     1365   1491   1461   -148   -163     90       C  
ATOM   1920  C   GLY B 190      37.291  43.842  -4.559  1.00 12.23           C  
ANISOU 1920  C   GLY B 190     1459   1609   1579   -148   -184     89       C  
ATOM   1921  O   GLY B 190      37.479  45.007  -4.191  1.00  9.27           O  
ANISOU 1921  O   GLY B 190     1071   1227   1225   -136   -190     88       O  
ATOM   1922  N  BARG B 191      36.155  43.455  -5.127  0.41  9.36           N  
ANISOU 1922  N  BARG B 191     1098   1255   1203   -158   -206     88       N  
ATOM   1923  N  CARG B 191      36.166  43.458  -5.154  0.59  9.10           N  
ANISOU 1923  N  CARG B 191     1066   1222   1170   -158   -206     88       N  
ATOM   1924  CA BARG B 191      35.130  44.445  -5.433  0.41  9.57           C  
ANISOU 1924  CA BARG B 191     1104   1294   1241   -144   -231     88       C  
ATOM   1925  CA CARG B 191      35.114  44.436  -5.410  0.59  9.57           C  
ANISOU 1925  CA CARG B 191     1102   1293   1240   -144   -231     88       C  
ATOM   1926  C  BARG B 191      34.411  44.950  -4.169  0.41  9.25           C  
ANISOU 1926  C  BARG B 191     1012   1283   1218   -126   -227     74       C  
ATOM   1927  C  CARG B 191      34.520  44.979  -4.116  0.59  8.63           C  
ANISOU 1927  C  CARG B 191      937   1203   1140   -125   -225     74       C  
ATOM   1928  O  BARG B 191      34.016  46.116  -4.104  0.41 11.21           O  
ANISOU 1928  O  BARG B 191     1250   1530   1480    -89   -242     65       O  
ATOM   1929  O  CARG B 191      34.299  46.186  -3.986  0.59  8.83           O  
ANISOU 1929  O  CARG B 191      955   1222   1179    -89   -238     64       O  
ATOM   1930  CB BARG B 191      34.141  43.873  -6.457  0.41 10.41           C  
ANISOU 1930  CB BARG B 191     1219   1406   1331   -160   -269     92       C  
ATOM   1931  CB CARG B 191      34.012  43.837  -6.282  0.59 12.15           C  
ANISOU 1931  CB CARG B 191     1429   1630   1555   -161   -269     91       C  
ATOM   1932  CG BARG B 191      34.839  43.425  -7.743  0.41  8.14           C  
ANISOU 1932  CG BARG B 191     1000   1091   1003   -159   -272     96       C  
ATOM   1933  CG CARG B 191      34.442  43.646  -7.706  0.59 12.06           C  
ANISOU 1933  CG CARG B 191     1482   1593   1507   -159   -283     97       C  
ATOM   1934  CD BARG B 191      33.853  43.063  -8.848  0.41 13.77           C  
ANISOU 1934  CD BARG B 191     1739   1802   1692   -169   -329     93       C  
ATOM   1935  CD CARG B 191      33.269  43.282  -8.593  0.59 14.94           C  
ANISOU 1935  CD CARG B 191     1855   1963   1859   -173   -344     95       C  
ATOM   1936  NE BARG B 191      32.894  42.066  -8.391  0.41 13.53           N  
ANISOU 1936  NE BARG B 191     1676   1781   1683   -211   -364     87       N  
ATOM   1937  NE CARG B 191      33.687  43.135  -9.979  0.59 15.82           N  
ANISOU 1937  NE CARG B 191     2046   2051   1914   -159   -360     95       N  
ATOM   1938  CZ BARG B 191      31.774  41.759  -9.032  0.41  9.49           C  
ANISOU 1938  CZ BARG B 191     1157   1274   1173   -235   -431     87       C  
ATOM   1939  CZ CARG B 191      32.891  42.692 -10.946  0.59 19.76           C  
ANISOU 1939  CZ CARG B 191     2581   2544   2385   -169   -426     87       C  
ATOM   1940  NH1BARG B 191      30.953  40.851  -8.524  0.41  7.85           N  
ANISOU 1940  NH1BARG B 191      908   1076    997   -290   -461     93       N  
ATOM   1941  NH1CARG B 191      33.343  42.584 -12.194  0.59  8.01           N  
ANISOU 1941  NH1CARG B 191     1180   1039    826   -144   -435     85       N  
ATOM   1942  NH2BARG B 191      31.468  42.364 -10.169  0.41  7.85           N  
ANISOU 1942  NH2BARG B 191      982   1062    937   -211   -474     87       N  
ATOM   1943  NH2CARG B 191      31.642  42.350 -10.651  0.59 19.68           N  
ANISOU 1943  NH2CARG B 191     2515   2549   2412   -203   -482     85       N  
ATOM   1944  N   LEU B 192      34.260  44.096  -3.159  1.00  7.47           N  
ANISOU 1944  N   LEU B 192      766   1085    987   -144   -206     74       N  
ATOM   1945  CA  LEU B 192      33.705  44.544  -1.878  1.00 11.46           C  
ANISOU 1945  CA  LEU B 192     1232   1633   1490   -116   -187     62       C  
ATOM   1946  C   LEU B 192      34.600  45.593  -1.200  1.00 12.76           C  
ANISOU 1946  C   LEU B 192     1424   1769   1654    -77   -187     36       C  
ATOM   1947  O   LEU B 192      34.103  46.624  -0.730  1.00  9.51           O  
ANISOU 1947  O   LEU B 192     1002   1367   1243    -27   -194     11       O  
ATOM   1948  CB  LEU B 192      33.485  43.373  -0.924  1.00  8.81           C  
ANISOU 1948  CB  LEU B 192      879   1331   1136   -151   -160     80       C  
ATOM   1949  CG  LEU B 192      32.344  42.396  -1.215  1.00 12.21           C  
ANISOU 1949  CG  LEU B 192     1267   1796   1576   -202   -165    112       C  
ATOM   1950  CD1 LEU B 192      32.158  41.437  -0.025  1.00 12.67           C  
ANISOU 1950  CD1 LEU B 192     1310   1888   1614   -238   -132    144       C  
ATOM   1951  CD2 LEU B 192      31.051  43.139  -1.560  1.00 16.50           C  
ANISOU 1951  CD2 LEU B 192     1740   2390   2140   -177   -176    111       C  
ATOM   1952  N   PHE B 193      35.911  45.356  -1.154  1.00  9.56           N  
ANISOU 1952  N   PHE B 193     1053   1327   1252    -96   -188     40       N  
ATOM   1953  CA  PHE B 193      36.809  46.321  -0.504  1.00  8.62           C  
ANISOU 1953  CA  PHE B 193      956   1176   1143    -75   -206     20       C  
ATOM   1954  C   PHE B 193      36.707  47.683  -1.187  1.00 10.64           C  
ANISOU 1954  C   PHE B 193     1226   1390   1425    -55   -238     14       C  
ATOM   1955  O   PHE B 193      36.648  48.717  -0.519  1.00  8.70           O  
ANISOU 1955  O   PHE B 193      999   1120   1184    -19   -266    -17       O  
ATOM   1956  CB  PHE B 193      38.275  45.858  -0.535  1.00  8.92           C  
ANISOU 1956  CB  PHE B 193     1006   1187   1194   -104   -208     35       C  
ATOM   1957  CG  PHE B 193      38.580  44.665   0.335  1.00  8.23           C  
ANISOU 1957  CG  PHE B 193      922   1123   1084   -112   -194     39       C  
ATOM   1958  CD1 PHE B 193      38.341  44.694   1.709  1.00  9.96           C  
ANISOU 1958  CD1 PHE B 193     1149   1365   1271    -91   -196     20       C  
ATOM   1959  CD2 PHE B 193      39.152  43.520  -0.225  1.00  7.83           C  
ANISOU 1959  CD2 PHE B 193      875   1067   1034   -131   -180     61       C  
ATOM   1960  CE1 PHE B 193      38.652  43.581   2.512  1.00 10.25           C  
ANISOU 1960  CE1 PHE B 193     1197   1417   1279   -101   -188     35       C  
ATOM   1961  CE2 PHE B 193      39.460  42.418   0.558  1.00 11.03           C  
ANISOU 1961  CE2 PHE B 193     1294   1478   1421   -135   -178     69       C  
ATOM   1962  CZ  PHE B 193      39.222  42.457   1.936  1.00 13.02           C  
ANISOU 1962  CZ  PHE B 193     1553   1750   1643   -124   -183     61       C  
ATOM   1963  N   ASN B 194      36.682  47.689  -2.521  1.00  8.40           N  
ANISOU 1963  N   ASN B 194      947   1092   1152    -75   -240     43       N  
ATOM   1964  CA  ASN B 194      36.569  48.947  -3.251  1.00 10.74           C  
ANISOU 1964  CA  ASN B 194     1267   1344   1471    -61   -274     52       C  
ATOM   1965  C   ASN B 194      35.225  49.648  -3.026  1.00  8.30           C  
ANISOU 1965  C   ASN B 194      950   1045   1161     -2   -298     24       C  
ATOM   1966  O   ASN B 194      35.169  50.878  -2.852  1.00  9.67           O  
ANISOU 1966  O   ASN B 194     1154   1168   1352     35   -338      7       O  
ATOM   1967  CB  ASN B 194      36.787  48.711  -4.747  1.00  9.59           C  
ANISOU 1967  CB  ASN B 194     1137   1191   1317    -89   -267     95       C  
ATOM   1968  CG  ASN B 194      38.252  48.594  -5.100  1.00  9.56           C  
ANISOU 1968  CG  ASN B 194     1139   1171   1322   -128   -244    129       C  
ATOM   1969  OD1 ASN B 194      38.969  49.593  -5.195  1.00 10.18           O  
ANISOU 1969  OD1 ASN B 194     1231   1207   1432   -147   -263    153       O  
ATOM   1970  ND2 ASN B 194      38.713  47.365  -5.279  1.00  8.40           N  
ANISOU 1970  ND2 ASN B 194      981   1057   1153   -141   -206    133       N  
ATOM   1971  N   ALA B 195      34.147  48.872  -3.022  1.00 11.84           N  
ANISOU 1971  N   ALA B 195     1352   1555   1591      8   -278     21       N  
ATOM   1972  CA  ALA B 195      32.817  49.446  -2.837  1.00 14.80           C  
ANISOU 1972  CA  ALA B 195     1693   1962   1969     70   -292     -1       C  
ATOM   1973  C   ALA B 195      32.691  50.101  -1.465  1.00 11.69           C  
ANISOU 1973  C   ALA B 195     1301   1577   1563    134   -285    -48       C  
ATOM   1974  O   ALA B 195      32.075  51.145  -1.323  1.00  9.78           O  
ANISOU 1974  O   ALA B 195     1067   1321   1329    209   -312    -78       O  
ATOM   1975  CB  ALA B 195      31.750  48.390  -3.016  1.00  9.63           C  
ANISOU 1975  CB  ALA B 195      970   1383   1307     51   -272     15       C  
ATOM   1976  N   ILE B 196      33.284  49.484  -0.451  1.00 10.08           N  
ANISOU 1976  N   ILE B 196     1102   1394   1335    113   -252    -57       N  
ATOM   1977  CA  ILE B 196      33.187  50.033   0.888  1.00  9.36           C  
ANISOU 1977  CA  ILE B 196     1027   1316   1212    179   -246   -106       C  
ATOM   1978  C   ILE B 196      33.926  51.367   0.962  1.00 12.25           C  
ANISOU 1978  C   ILE B 196     1472   1585   1600    209   -311   -140       C  
ATOM   1979  O   ILE B 196      33.417  52.327   1.527  1.00 11.62           O  
ANISOU 1979  O   ILE B 196     1419   1489   1506    295   -334   -191       O  
ATOM   1980  CB  ILE B 196      33.742  49.052   1.933  1.00 10.52           C  
ANISOU 1980  CB  ILE B 196     1176   1502   1319    146   -209   -103       C  
ATOM   1981  CG1 ILE B 196      32.776  47.874   2.055  1.00 13.39           C  
ANISOU 1981  CG1 ILE B 196     1467   1959   1662    123   -150    -67       C  
ATOM   1982  CG2 ILE B 196      33.951  49.751   3.307  1.00 12.59           C  
ANISOU 1982  CG2 ILE B 196     1488   1761   1536    215   -219   -160       C  
ATOM   1983  CD1 ILE B 196      33.259  46.796   2.991  1.00 16.71           C  
ANISOU 1983  CD1 ILE B 196     1896   2410   2042     83   -116    -47       C  
ATOM   1984  N   ILE B 197      35.109  51.433   0.366  1.00  9.19           N  
ANISOU 1984  N   ILE B 197     1116   1128   1246    138   -341   -110       N  
ATOM   1985  CA  ILE B 197      35.857  52.684   0.340  1.00  9.89           C  
ANISOU 1985  CA  ILE B 197     1273   1115   1370    139   -412   -125       C  
ATOM   1986  C   ILE B 197      35.101  53.753  -0.464  1.00  9.55           C  
ANISOU 1986  C   ILE B 197     1256   1022   1353    187   -454   -125       C  
ATOM   1987  O   ILE B 197      35.029  54.918  -0.062  1.00 12.70           O  
ANISOU 1987  O   ILE B 197     1717   1346   1762    244   -515   -167       O  
ATOM   1988  CB  ILE B 197      37.267  52.481  -0.252  1.00  9.95           C  
ANISOU 1988  CB  ILE B 197     1285   1079   1417     43   -424    -72       C  
ATOM   1989  CG1 ILE B 197      38.084  51.522   0.628  1.00 10.91           C  
ANISOU 1989  CG1 ILE B 197     1386   1240   1519     11   -401    -77       C  
ATOM   1990  CG2 ILE B 197      37.989  53.830  -0.374  1.00  9.59           C  
ANISOU 1990  CG2 ILE B 197     1301    922   1421     23   -505    -69       C  
ATOM   1991  CD1 ILE B 197      39.381  51.028  -0.042  1.00 12.57           C  
ANISOU 1991  CD1 ILE B 197     1570   1441   1767    -71   -392    -20       C  
ATOM   1992  N   HIS B 198      34.540  53.356  -1.599  1.00 10.94           N  
ANISOU 1992  N   HIS B 198     1393   1230   1535    170   -431    -80       N  
ATOM   1993  CA  HIS B 198      33.776  54.276  -2.436  1.00 12.94           C  
ANISOU 1993  CA  HIS B 198     1668   1441   1808    218   -477    -72       C  
ATOM   1994  C   HIS B 198      32.548  54.823  -1.703  1.00 14.39           C  
ANISOU 1994  C   HIS B 198     1839   1653   1975    340   -486   -135       C  
ATOM   1995  O   HIS B 198      32.220  56.002  -1.815  1.00 12.74           O  
ANISOU 1995  O   HIS B 198     1685   1370   1786    410   -548   -159       O  
ATOM   1996  CB  HIS B 198      33.344  53.582  -3.733  1.00 11.91           C  
ANISOU 1996  CB  HIS B 198     1498   1354   1673    180   -456    -17       C  
ATOM   1997  CG  HIS B 198      32.552  54.458  -4.649  1.00 12.52           C  
ANISOU 1997  CG  HIS B 198     1600   1393   1766    230   -511     -1       C  
ATOM   1998  ND1 HIS B 198      31.178  54.535  -4.601  1.00 13.80           N  
ANISOU 1998  ND1 HIS B 198     1710   1609   1925    314   -520    -28       N  
ATOM   1999  CD2 HIS B 198      32.937  55.312  -5.633  1.00 12.74           C  
ANISOU 1999  CD2 HIS B 198     1695   1333   1812    209   -563     46       C  
ATOM   2000  CE1 HIS B 198      30.746  55.391  -5.511  1.00 15.47           C  
ANISOU 2000  CE1 HIS B 198     1961   1765   2153    352   -584     -6       C  
ATOM   2001  NE2 HIS B 198      31.800  55.870  -6.157  1.00 13.24           N  
ANISOU 2001  NE2 HIS B 198     1758   1392   1880    286   -610     42       N  
ATOM   2002  N   ARG B 199      31.861  53.967  -0.954  1.00 12.81           N  
ANISOU 2002  N   ARG B 199     1565   1563   1739    369   -422   -158       N  
ATOM   2003  CA  ARG B 199      30.708  54.426  -0.186  1.00 14.01           C  
ANISOU 2003  CA  ARG B 199     1687   1769   1868    493   -410   -214       C  
ATOM   2004  C   ARG B 199      31.133  55.533   0.789  1.00 18.09           C  
ANISOU 2004  C   ARG B 199     2300   2205   2369    570   -456   -285       C  
ATOM   2005  O   ARG B 199      30.411  56.516   0.989  1.00 17.80           O  
ANISOU 2005  O   ARG B 199     2291   2143   2330    691   -491   -336       O  
ATOM   2006  CB  ARG B 199      30.061  53.261   0.567  1.00 15.99           C  
ANISOU 2006  CB  ARG B 199     1840   2157   2076    491   -321   -210       C  
ATOM   2007  CG  ARG B 199      28.983  53.679   1.578  1.00 28.92           C  
ANISOU 2007  CG  ARG B 199     3437   3878   3675    625   -283   -266       C  
ATOM   2008  CD  ARG B 199      27.716  54.167   0.893  1.00 38.47           C  
ANISOU 2008  CD  ARG B 199     4576   5126   4917    708   -300   -263       C  
ATOM   2009  NE  ARG B 199      26.972  53.070   0.284  1.00 48.63           N  
ANISOU 2009  NE  ARG B 199     5740   6513   6225    638   -262   -199       N  
ATOM   2010  CZ  ARG B 199      25.777  52.649   0.688  1.00 49.80           C  
ANISOU 2010  CZ  ARG B 199     5760   6798   6365    685   -202   -189       C  
ATOM   2011  NH1 ARG B 199      25.163  53.241   1.704  1.00 54.60           N  
ANISOU 2011  NH1 ARG B 199     6342   7473   6932    819   -157   -242       N  
ATOM   2012  NH2 ARG B 199      25.190  51.637   0.067  1.00 47.84           N  
ANISOU 2012  NH2 ARG B 199     5409   6622   6148    597   -189   -126       N  
ATOM   2013  N   HIS B 200      32.319  55.381   1.365  1.00 13.09           N  
ANISOU 2013  N   HIS B 200     1721   1525   1726    505   -467   -291       N  
ATOM   2014  CA  HIS B 200      32.828  56.324   2.365  1.00 13.90           C  
ANISOU 2014  CA  HIS B 200     1926   1546   1810    563   -527   -363       C  
ATOM   2015  C   HIS B 200      33.290  57.635   1.725  1.00 20.40           C  
ANISOU 2015  C   HIS B 200     2847   2212   2694    559   -636   -364       C  
ATOM   2016  O   HIS B 200      32.923  58.729   2.176  1.00 17.30           O  
ANISOU 2016  O   HIS B 200     2535   1746   2294    667   -699   -432       O  
ATOM   2017  CB  HIS B 200      33.974  55.674   3.156  1.00 11.90           C  
ANISOU 2017  CB  HIS B 200     1692   1297   1534    484   -519   -362       C  
ATOM   2018  CG  HIS B 200      34.599  56.575   4.173  1.00 18.80           C  
ANISOU 2018  CG  HIS B 200     2677   2080   2388    527   -599   -436       C  
ATOM   2019  ND1 HIS B 200      33.895  57.107   5.231  1.00 21.41           N  
ANISOU 2019  ND1 HIS B 200     3057   2429   2647    667   -601   -526       N  
ATOM   2020  CD2 HIS B 200      35.866  57.037   4.295  1.00 21.88           C  
ANISOU 2020  CD2 HIS B 200     3138   2359   2818    450   -687   -435       C  
ATOM   2021  CE1 HIS B 200      34.699  57.863   5.958  1.00 21.75           C  
ANISOU 2021  CE1 HIS B 200     3215   2366   2682    677   -696   -586       C  
ATOM   2022  NE2 HIS B 200      35.900  57.840   5.408  1.00 17.77           N  
ANISOU 2022  NE2 HIS B 200     2719   1779   2252    538   -755   -528       N  
ATOM   2023  N   LYS B 201      34.089  57.518   0.666  1.00 15.24           N  
ANISOU 2023  N   LYS B 201     2191   1506   2095    438   -656   -284       N  
ATOM   2024  CA  LYS B 201      34.621  58.681  -0.046  1.00 13.43           C  
ANISOU 2024  CA  LYS B 201     2048   1129   1927    405   -753   -255       C  
ATOM   2025  C   LYS B 201      34.708  58.383  -1.546  1.00 11.59           C  
ANISOU 2025  C   LYS B 201     1775    904   1726    321   -732   -156       C  
ATOM   2026  O   LYS B 201      35.727  57.888  -2.041  1.00 14.28           O  
ANISOU 2026  O   LYS B 201     2093   1247   2086    203   -710    -90       O  
ATOM   2027  CB  LYS B 201      35.990  59.086   0.510  1.00 23.07           C  
ANISOU 2027  CB  LYS B 201     3336   2253   3178    322   -820   -259       C  
ATOM   2028  CG  LYS B 201      35.912  59.932   1.779  1.00 27.00           C  
ANISOU 2028  CG  LYS B 201     3932   2677   3650    418   -896   -364       C  
ATOM   2029  CD  LYS B 201      37.242  60.615   2.063  1.00 30.51           C  
ANISOU 2029  CD  LYS B 201     4443   3011   4140    316   -992   -348       C  
ATOM   2030  CE  LYS B 201      37.178  61.423   3.345  1.00 35.59           C  
ANISOU 2030  CE  LYS B 201     5168   3625   4730    401  -1055   -436       C  
ATOM   2031  NZ  LYS B 201      38.524  61.937   3.724  1.00 35.67           N  
ANISOU 2031  NZ  LYS B 201     5210   3566   4779    296  -1137   -402       N  
ATOM   2032  N   PRO B 202      33.621  58.671  -2.268  1.00 17.27           N  
ANISOU 2032  N   PRO B 202     2483   1636   2445    392   -739   -148       N  
ATOM   2033  CA  PRO B 202      33.501  58.259  -3.675  1.00 14.24           C  
ANISOU 2033  CA  PRO B 202     2063   1279   2067    331   -717    -63       C  
ATOM   2034  C   PRO B 202      34.603  58.833  -4.561  1.00 15.94           C  
ANISOU 2034  C   PRO B 202     2344   1392   2321    225   -760     20       C  
ATOM   2035  O   PRO B 202      34.937  58.191  -5.545  1.00 15.10           O  
ANISOU 2035  O   PRO B 202     2203   1331   2203    149   -715     92       O  
ATOM   2036  CB  PRO B 202      32.119  58.784  -4.094  1.00 18.77           C  
ANISOU 2036  CB  PRO B 202     2633   1860   2640    448   -750    -82       C  
ATOM   2037  CG  PRO B 202      31.651  59.670  -2.986  1.00 20.08           C  
ANISOU 2037  CG  PRO B 202     2846   1979   2805    574   -795   -174       C  
ATOM   2038  CD  PRO B 202      32.374  59.244  -1.743  1.00 14.39           C  
ANISOU 2038  CD  PRO B 202     2125   1283   2060    547   -759   -223       C  
ATOM   2039  N   MET B 203      35.172  59.990  -4.228  1.00 14.48           N  
ANISOU 2039  N   MET B 203     2251   1072   2179    216   -846     13       N  
ATOM   2040  CA  MET B 203      36.265  60.529  -5.056  1.00 14.95           C  
ANISOU 2040  CA  MET B 203     2358   1041   2281     94   -881    111       C  
ATOM   2041  C   MET B 203      37.516  59.633  -5.053  1.00 15.16           C  
ANISOU 2041  C   MET B 203     2316   1131   2312    -28   -812    160       C  
ATOM   2042  O   MET B 203      38.381  59.779  -5.912  1.00 16.75           O  
ANISOU 2042  O   MET B 203     2520   1307   2536   -131   -803    258       O  
ATOM   2043  CB  MET B 203      36.651  61.949  -4.606  1.00 17.49           C  
ANISOU 2043  CB  MET B 203     2760   1257   2629     83   -966     85       C  
ATOM   2044  CG  MET B 203      35.578  62.996  -4.840  1.00 23.27           C  
ANISOU 2044  CG  MET B 203     3556   1939   3349    185  -1023     48       C  
ATOM   2045  SD  MET B 203      34.979  63.012  -6.539  1.00 31.72           S  
ANISOU 2045  SD  MET B 203     4620   3029   4402    174  -1001    142       S  
ATOM   2046  CE  MET B 203      36.446  63.490  -7.443  1.00 28.87           C  
ANISOU 2046  CE  MET B 203     4284   2617   4069      5  -1002    267       C  
ATOM   2047  N   LEU B 204      37.611  58.694  -4.113  1.00 12.02           N  
ANISOU 2047  N   LEU B 204     1856    823   1888    -12   -758     99       N  
ATOM   2048  CA  LEU B 204      38.814  57.878  -3.991  1.00 14.43           C  
ANISOU 2048  CA  LEU B 204     2097   1182   2202   -110   -705    137       C  
ATOM   2049  C   LEU B 204      38.834  56.675  -4.925  1.00 15.46           C  
ANISOU 2049  C   LEU B 204     2156   1427   2292   -140   -606    188       C  
ATOM   2050  O   LEU B 204      39.894  56.099  -5.166  1.00 13.24           O  
ANISOU 2050  O   LEU B 204     1826   1185   2020   -216   -559    238       O  
ATOM   2051  CB  LEU B 204      38.978  57.366  -2.553  1.00 13.13           C  
ANISOU 2051  CB  LEU B 204     1910   1056   2021    -79   -701     53       C  
ATOM   2052  CG  LEU B 204      39.186  58.366  -1.420  1.00 11.45           C  
ANISOU 2052  CG  LEU B 204     1776    739   1834    -50   -802    -15       C  
ATOM   2053  CD1 LEU B 204      39.409  57.587  -0.108  1.00 12.16           C  
ANISOU 2053  CD1 LEU B 204     1838    898   1885    -24   -779    -84       C  
ATOM   2054  CD2 LEU B 204      40.354  59.288  -1.721  1.00 16.64           C  
ANISOU 2054  CD2 LEU B 204     2468   1289   2564   -158   -878     50       C  
ATOM   2055  N   ILE B 205      37.659  56.279  -5.415  1.00 11.06           N  
ANISOU 2055  N   ILE B 205     1589    923   1690    -72   -579    171       N  
ATOM   2056  CA  ILE B 205      37.495  55.010  -6.130  1.00  9.55           C  
ANISOU 2056  CA  ILE B 205     1342    835   1452    -85   -500    195       C  
ATOM   2057  C   ILE B 205      36.738  55.203  -7.439  1.00 11.31           C  
ANISOU 2057  C   ILE B 205     1593   1059   1646    -65   -510    239       C  
ATOM   2058  O   ILE B 205      35.659  55.803  -7.464  1.00 11.76           O  
ANISOU 2058  O   ILE B 205     1675   1089   1705      6   -560    211       O  
ATOM   2059  CB  ILE B 205      36.720  53.969  -5.284  1.00  8.38           C  
ANISOU 2059  CB  ILE B 205     1139    772   1272    -32   -462    125       C  
ATOM   2060  CG1 ILE B 205      37.443  53.669  -3.975  1.00 10.36           C  
ANISOU 2060  CG1 ILE B 205     1371   1031   1534    -45   -454     84       C  
ATOM   2061  CG2 ILE B 205      36.485  52.666  -6.091  1.00  8.67           C  
ANISOU 2061  CG2 ILE B 205     1135    893   1265    -50   -402    148       C  
ATOM   2062  CD1 ILE B 205      38.790  53.023  -4.159  1.00 14.58           C  
ANISOU 2062  CD1 ILE B 205     1875   1585   2079   -124   -416    129       C  
ATOM   2063  N   ASP B 206      37.305  54.700  -8.527  1.00 12.19           N  
ANISOU 2063  N   ASP B 206     1701   1205   1726   -118   -463    305       N  
ATOM   2064  CA  ASP B 206      36.604  54.705  -9.812  1.00 12.15           C  
ANISOU 2064  CA  ASP B 206     1731   1213   1673    -97   -472    344       C  
ATOM   2065  C   ASP B 206      35.936  53.354  -9.992  1.00 14.17           C  
ANISOU 2065  C   ASP B 206     1943   1561   1880    -71   -435    304       C  
ATOM   2066  O   ASP B 206      36.614  52.380 -10.330  1.00 11.79           O  
ANISOU 2066  O   ASP B 206     1624   1312   1545   -106   -373    318       O  
ATOM   2067  CB  ASP B 206      37.585  54.995 -10.956  1.00 14.69           C  
ANISOU 2067  CB  ASP B 206     2090   1521   1970   -164   -442    443       C  
ATOM   2068  CG  ASP B 206      36.913  55.053 -12.332  1.00 20.06           C  
ANISOU 2068  CG  ASP B 206     2827   2212   2582   -139   -458    488       C  
ATOM   2069  OD1 ASP B 206      35.771  54.585 -12.502  1.00 17.91           O  
ANISOU 2069  OD1 ASP B 206     2549   1973   2281    -80   -488    441       O  
ATOM   2070  OD2 ASP B 206      37.553  55.571 -13.263  1.00 23.42           O  
ANISOU 2070  OD2 ASP B 206     3301   2617   2982   -184   -444    579       O  
ATOM   2071  N   MET B 207      34.623  53.274  -9.768  1.00 11.29           N  
ANISOU 2071  N   MET B 207     1558   1215   1516     -9   -474    256       N  
ATOM   2072  CA  MET B 207      33.978  51.966  -9.788  1.00 11.92           C  
ANISOU 2072  CA  MET B 207     1589   1375   1566     -3   -450    221       C  
ATOM   2073  C   MET B 207      33.905  51.399 -11.201  1.00 12.39           C  
ANISOU 2073  C   MET B 207     1687   1457   1562    -20   -451    258       C  
ATOM   2074  O   MET B 207      33.794  50.191 -11.361  1.00 10.92           O  
ANISOU 2074  O   MET B 207     1484   1321   1345    -35   -428    237       O  
ATOM   2075  CB  MET B 207      32.573  52.017  -9.172  1.00 10.14           C  
ANISOU 2075  CB  MET B 207     1309   1180   1365     59   -488    172       C  
ATOM   2076  CG  MET B 207      32.589  52.152  -7.639  1.00 13.61           C  
ANISOU 2076  CG  MET B 207     1704   1626   1839     84   -465    121       C  
ATOM   2077  SD  MET B 207      33.389  50.775  -6.770  1.00 12.63           S  
ANISOU 2077  SD  MET B 207     1541   1554   1703     27   -391    103       S  
ATOM   2078  CE  MET B 207      32.297  49.407  -7.201  1.00 12.23           C  
ANISOU 2078  CE  MET B 207     1437   1580   1630     13   -387     99       C  
ATOM   2079  N   ASN B 208      33.957  52.255 -12.222  1.00  9.99           N  
ANISOU 2079  N   ASN B 208     1450   1112   1232    -15   -485    313       N  
ATOM   2080  CA  ASN B 208      34.023  51.721 -13.583  1.00 13.08           C  
ANISOU 2080  CA  ASN B 208     1897   1531   1543    -25   -480    349       C  
ATOM   2081  C   ASN B 208      35.265  50.852 -13.737  1.00 14.23           C  
ANISOU 2081  C   ASN B 208     2045   1712   1649    -67   -392    361       C  
ATOM   2082  O   ASN B 208      35.189  49.730 -14.246  1.00 12.29           O  
ANISOU 2082  O   ASN B 208     1814   1510   1347    -63   -377    337       O  
ATOM   2083  CB  ASN B 208      34.030  52.827 -14.634  1.00 11.93           C  
ANISOU 2083  CB  ASN B 208     1833   1336   1364    -17   -521    421       C  
ATOM   2084  CG  ASN B 208      34.190  52.270 -16.042  1.00 18.31           C  
ANISOU 2084  CG  ASN B 208     2712   2180   2064    -22   -509    459       C  
ATOM   2085  OD1 ASN B 208      33.402  51.432 -16.481  1.00 17.41           O  
ANISOU 2085  OD1 ASN B 208     2604   2104   1909      2   -547    419       O  
ATOM   2086  ND2 ASN B 208      35.234  52.703 -16.737  1.00 22.06           N  
ANISOU 2086  ND2 ASN B 208     3242   2648   2492    -54   -455    537       N  
ATOM   2087  N   LYS B 209      36.401  51.358 -13.263  1.00 13.18           N  
ANISOU 2087  N   LYS B 209     1898   1559   1553   -102   -343    394       N  
ATOM   2088  CA  LYS B 209      37.643  50.582 -13.278  1.00 11.88           C  
ANISOU 2088  CA  LYS B 209     1712   1437   1366   -131   -257    406       C  
ATOM   2089  C   LYS B 209      37.506  49.299 -12.474  1.00 12.24           C  
ANISOU 2089  C   LYS B 209     1709   1518   1422   -120   -240    333       C  
ATOM   2090  O   LYS B 209      37.935  48.230 -12.919  1.00 13.20           O  
ANISOU 2090  O   LYS B 209     1843   1680   1491   -112   -196    321       O  
ATOM   2091  CB  LYS B 209      38.802  51.407 -12.724  1.00 18.24           C  
ANISOU 2091  CB  LYS B 209     2486   2213   2232   -179   -227    454       C  
ATOM   2092  CG  LYS B 209      39.148  52.635 -13.544  1.00 28.94           C  
ANISOU 2092  CG  LYS B 209     3891   3524   3580   -212   -238    547       C  
ATOM   2093  CD  LYS B 209      40.260  52.345 -14.525  1.00 41.07           C  
ANISOU 2093  CD  LYS B 209     5432   5119   5052   -240   -147    622       C  
ATOM   2094  CE  LYS B 209      41.317  53.432 -14.464  1.00 51.51           C  
ANISOU 2094  CE  LYS B 209     6733   6407   6433   -316   -129    718       C  
ATOM   2095  NZ  LYS B 209      41.867  53.577 -13.089  1.00 55.38           N  
ANISOU 2095  NZ  LYS B 209     7148   6866   7027   -351   -148    682       N  
ATOM   2096  N   VAL B 210      36.902  49.406 -11.296  1.00  7.87           N  
ANISOU 2096  N   VAL B 210     1109    949    932   -114   -274    286       N  
ATOM   2097  CA  VAL B 210      36.722  48.245 -10.424  1.00  9.76           C  
ANISOU 2097  CA  VAL B 210     1304   1219   1184   -112   -260    231       C  
ATOM   2098  C   VAL B 210      35.983  47.133 -11.181  1.00 12.09           C  
ANISOU 2098  C   VAL B 210     1628   1541   1425   -100   -279    207       C  
ATOM   2099  O   VAL B 210      36.435  45.984 -11.195  1.00 11.83           O  
ANISOU 2099  O   VAL B 210     1603   1527   1367   -104   -248    187       O  
ATOM   2100  CB  VAL B 210      35.966  48.618  -9.134  1.00 10.26           C  
ANISOU 2100  CB  VAL B 210     1320   1274   1305    -98   -292    192       C  
ATOM   2101  CG1 VAL B 210      35.570  47.363  -8.339  1.00 14.55           C  
ANISOU 2101  CG1 VAL B 210     1823   1854   1849   -103   -278    150       C  
ATOM   2102  CG2 VAL B 210      36.831  49.545  -8.260  1.00  7.40           C  
ANISOU 2102  CG2 VAL B 210      946    875    991   -110   -284    200       C  
ATOM   2103  N   TYR B 211      34.874  47.473 -11.832  1.00 10.00           N  
ANISOU 2103  N   TYR B 211     1384   1272   1145    -84   -340    209       N  
ATOM   2104  CA  TYR B 211      34.111  46.457 -12.563  1.00 10.50           C  
ANISOU 2104  CA  TYR B 211     1476   1352   1162    -82   -382    184       C  
ATOM   2105  C   TYR B 211      34.881  45.827 -13.724  1.00 11.23           C  
ANISOU 2105  C   TYR B 211     1652   1450   1166    -73   -354    194       C  
ATOM   2106  O   TYR B 211      34.603  44.692 -14.100  1.00 13.20           O  
ANISOU 2106  O   TYR B 211     1936   1702   1376    -73   -379    158       O  
ATOM   2107  CB  TYR B 211      32.798  47.047 -13.084  1.00 13.64           C  
ANISOU 2107  CB  TYR B 211     1873   1748   1564    -64   -467    189       C  
ATOM   2108  CG  TYR B 211      31.787  47.206 -11.974  1.00 13.61           C  
ANISOU 2108  CG  TYR B 211     1775   1762   1636    -60   -494    165       C  
ATOM   2109  CD1 TYR B 211      31.315  46.098 -11.281  1.00 14.94           C  
ANISOU 2109  CD1 TYR B 211     1889   1959   1830    -91   -493    135       C  
ATOM   2110  CD2 TYR B 211      31.313  48.459 -11.612  1.00 15.81           C  
ANISOU 2110  CD2 TYR B 211     2023   2028   1957    -21   -517    174       C  
ATOM   2111  CE1 TYR B 211      30.402  46.242 -10.253  1.00 19.56           C  
ANISOU 2111  CE1 TYR B 211     2379   2579   2474    -85   -500    123       C  
ATOM   2112  CE2 TYR B 211      30.396  48.611 -10.589  1.00 12.55           C  
ANISOU 2112  CE2 TYR B 211     1521   1646   1601      1   -528    148       C  
ATOM   2113  CZ  TYR B 211      29.943  47.505  -9.916  1.00 17.97           C  
ANISOU 2113  CZ  TYR B 211     2142   2380   2306    -32   -512    126       C  
ATOM   2114  OH  TYR B 211      29.036  47.665  -8.888  1.00 23.25           O  
ANISOU 2114  OH  TYR B 211     2714   3097   3022     -8   -507    111       O  
ATOM   2115  N   ARG B 212      35.840  46.553 -14.287  1.00 11.55           N  
ANISOU 2115  N   ARG B 212     1725   1492   1172    -65   -302    243       N  
ATOM   2116  CA  ARG B 212      36.558  46.054 -15.470  1.00 13.88           C  
ANISOU 2116  CA  ARG B 212     2099   1810   1366    -41   -260    258       C  
ATOM   2117  C   ARG B 212      37.892  45.361 -15.132  1.00 11.90           C  
ANISOU 2117  C   ARG B 212     1826   1586   1110    -33   -168    252       C  
ATOM   2118  O   ARG B 212      38.493  44.727 -15.995  1.00 14.25           O  
ANISOU 2118  O   ARG B 212     2182   1912   1320      5   -123    249       O  
ATOM   2119  CB  ARG B 212      36.802  47.205 -16.466  1.00 16.91           C  
ANISOU 2119  CB  ARG B 212     2533   2194   1697    -35   -250    331       C  
ATOM   2120  CG  ARG B 212      35.519  47.766 -17.072  1.00 20.60           C  
ANISOU 2120  CG  ARG B 212     3043   2636   2146    -23   -351    337       C  
ATOM   2121  CD  ARG B 212      35.778  48.770 -18.173  1.00 44.91           C  
ANISOU 2121  CD  ARG B 212     6196   5711   5155    -14   -345    417       C  
ATOM   2122  NE  ARG B 212      37.016  49.518 -17.968  1.00 60.52           N  
ANISOU 2122  NE  ARG B 212     8147   7691   7156    -46   -256    488       N  
ATOM   2123  CZ  ARG B 212      37.327  50.639 -18.612  1.00 65.00           C  
ANISOU 2123  CZ  ARG B 212     8758   8241   7697    -62   -248    579       C  
ATOM   2124  NH1 ARG B 212      36.481  51.156 -19.495  1.00 57.95           N  
ANISOU 2124  NH1 ARG B 212     7947   7326   6748    -38   -325    607       N  
ATOM   2125  NH2 ARG B 212      38.479  51.250 -18.363  1.00 65.26           N  
ANISOU 2125  NH2 ARG B 212     8753   8276   7767   -108   -171    649       N  
ATOM   2126  N   GLN B 213      38.337  45.480 -13.887  1.00  8.50           N  
ANISOU 2126  N   GLN B 213     1314   1148    767    -59   -143    248       N  
ATOM   2127  CA  GLN B 213      39.666  45.025 -13.494  1.00  8.46           C  
ANISOU 2127  CA  GLN B 213     1270   1171    772    -51    -64    254       C  
ATOM   2128  C   GLN B 213      39.713  43.582 -12.995  1.00  8.18           C  
ANISOU 2128  C   GLN B 213     1240   1133    737    -27    -67    191       C  
ATOM   2129  O   GLN B 213      38.690  43.011 -12.640  1.00 10.44           O  
ANISOU 2129  O   GLN B 213     1539   1390   1038    -40   -131    148       O  
ATOM   2130  CB  GLN B 213      40.236  45.960 -12.409  1.00  8.89           C  
ANISOU 2130  CB  GLN B 213     1243   1214    921    -92    -50    285       C  
ATOM   2131  CG  GLN B 213      40.816  47.228 -13.052  1.00 11.34           C  
ANISOU 2131  CG  GLN B 213     1553   1528   1228   -118    -22    367       C  
ATOM   2132  CD  GLN B 213      41.209  48.334 -12.080  1.00 13.22           C  
ANISOU 2132  CD  GLN B 213     1733   1729   1562   -169    -41    397       C  
ATOM   2133  OE1 GLN B 213      41.901  49.270 -12.476  1.00 15.44           O  
ANISOU 2133  OE1 GLN B 213     2005   2006   1857   -206    -18    471       O  
ATOM   2134  NE2 GLN B 213      40.768  48.247 -10.827  1.00 15.32           N  
ANISOU 2134  NE2 GLN B 213     1966   1966   1889   -172    -86    343       N  
ATOM   2135  N   THR B 214      40.919  43.013 -12.983  1.00  8.65           N  
ANISOU 2135  N   THR B 214     1282   1222    781      6      3    192       N  
ATOM   2136  CA  THR B 214      41.161  41.680 -12.429  1.00  9.56           C  
ANISOU 2136  CA  THR B 214     1405   1324    902     36     -1    138       C  
ATOM   2137  C   THR B 214      41.064  41.719 -10.910  1.00  9.02           C  
ANISOU 2137  C   THR B 214     1266   1233    928     -6    -27    131       C  
ATOM   2138  O   THR B 214      41.092  42.806 -10.292  1.00  9.93           O  
ANISOU 2138  O   THR B 214     1322   1351   1100    -46    -30    163       O  
ATOM   2139  CB  THR B 214      42.556  41.133 -12.796  1.00 10.62           C  
ANISOU 2139  CB  THR B 214     1530   1505   1000    102     83    143       C  
ATOM   2140  OG1 THR B 214      43.556  41.904 -12.111  1.00 10.10           O  
ANISOU 2140  OG1 THR B 214     1359   1473   1005     76    132    194       O  
ATOM   2141  CG2 THR B 214      42.808  41.186 -14.310  1.00 12.26           C  
ANISOU 2141  CG2 THR B 214     1807   1755   1096    157    133    157       C  
ATOM   2142  N   ASN B 215      40.970  40.539 -10.308  1.00  7.41           N  
ANISOU 2142  N   ASN B 215     1080   1002    733      7    -52     89       N  
ATOM   2143  CA  ASN B 215      40.908  40.432  -8.852  1.00 10.47           C  
ANISOU 2143  CA  ASN B 215     1415   1374   1190    -26    -73     86       C  
ATOM   2144  C   ASN B 215      42.127  41.051  -8.185  1.00  8.95           C  
ANISOU 2144  C   ASN B 215     1145   1210   1044    -23    -30    116       C  
ATOM   2145  O   ASN B 215      42.000  41.828  -7.236  1.00 10.05           O  
ANISOU 2145  O   ASN B 215     1237   1346   1235    -62    -49    129       O  
ATOM   2146  CB  ASN B 215      40.770  38.961  -8.428  1.00  7.90           C  
ANISOU 2146  CB  ASN B 215     1135   1008    859    -11   -104     49       C  
ATOM   2147  CG  ASN B 215      39.456  38.357  -8.877  1.00  9.30           C  
ANISOU 2147  CG  ASN B 215     1376   1146   1012    -40   -169     26       C  
ATOM   2148  OD1 ASN B 215      38.623  39.039  -9.487  1.00  9.47           O  
ANISOU 2148  OD1 ASN B 215     1399   1178   1020    -65   -192     33       O  
ATOM   2149  ND2 ASN B 215      39.256  37.072  -8.574  1.00  9.10           N  
ANISOU 2149  ND2 ASN B 215     1403   1070    986    -42   -210      1       N  
ATOM   2150  N   LEU B 216      43.312  40.698  -8.668  1.00 10.58           N  
ANISOU 2150  N   LEU B 216     1340   1449   1232     27     24    125       N  
ATOM   2151  CA  LEU B 216      44.539  41.213  -8.059  1.00 13.32           C  
ANISOU 2151  CA  LEU B 216     1597   1831   1634     24     56    159       C  
ATOM   2152  C   LEU B 216      44.659  42.741  -8.212  1.00 12.95           C  
ANISOU 2152  C   LEU B 216     1502   1799   1620    -32     65    211       C  
ATOM   2153  O   LEU B 216      45.097  43.416  -7.289  1.00 11.22           O  
ANISOU 2153  O   LEU B 216     1222   1574   1466    -71     43    229       O  
ATOM   2154  CB  LEU B 216      45.771  40.527  -8.656  1.00 12.31           C  
ANISOU 2154  CB  LEU B 216     1447   1750   1480     99    120    163       C  
ATOM   2155  CG  LEU B 216      46.022  39.067  -8.244  1.00 12.58           C  
ANISOU 2155  CG  LEU B 216     1518   1759   1503    167    103    115       C  
ATOM   2156  CD1 LEU B 216      47.184  38.503  -9.034  1.00 15.22           C  
ANISOU 2156  CD1 LEU B 216     1833   2149   1801    264    175    114       C  
ATOM   2157  CD2 LEU B 216      46.291  38.967  -6.728  1.00 10.75           C  
ANISOU 2157  CD2 LEU B 216     1237   1505   1343    140     55    116       C  
ATOM   2158  N   GLU B 217      44.275  43.282  -9.367  1.00 10.63           N  
ANISOU 2158  N   GLU B 217     1245   1515   1278    -37     86    236       N  
ATOM   2159  CA  GLU B 217      44.276  44.738  -9.551  1.00 10.12           C  
ANISOU 2159  CA  GLU B 217     1154   1445   1245    -94     81    291       C  
ATOM   2160  C   GLU B 217      43.333  45.414  -8.543  1.00  9.41           C  
ANISOU 2160  C   GLU B 217     1071   1300   1206   -135      6    268       C  
ATOM   2161  O   GLU B 217      43.675  46.426  -7.915  1.00  7.74           O  
ANISOU 2161  O   GLU B 217      820   1066   1054   -178    -20    292       O  
ATOM   2162  CB  GLU B 217      43.875  45.105 -10.988  1.00 16.34           C  
ANISOU 2162  CB  GLU B 217     2003   2247   1958    -84    108    323       C  
ATOM   2163  CG  GLU B 217      44.950  44.799 -12.028  1.00 12.74           C  
ANISOU 2163  CG  GLU B 217     1533   1863   1444    -43    201    364       C  
ATOM   2164  CD  GLU B 217      44.423  44.873 -13.444  1.00 19.48           C  
ANISOU 2164  CD  GLU B 217     2476   2733   2194    -15    221    379       C  
ATOM   2165  OE1 GLU B 217      43.197  44.843 -13.617  1.00 13.58           O  
ANISOU 2165  OE1 GLU B 217     1803   1939   1420    -18    153    342       O  
ATOM   2166  OE2 GLU B 217      45.231  44.960 -14.380  1.00 21.05           O  
ANISOU 2166  OE2 GLU B 217     2667   2998   2333     11    306    432       O  
ATOM   2167  N   ASN B 218      42.142  44.855  -8.386  1.00  8.79           N  
ANISOU 2167  N   ASN B 218     1040   1198   1100   -120    -32    220       N  
ATOM   2168  CA  ASN B 218      41.173  45.431  -7.459  1.00 10.06           C  
ANISOU 2168  CA  ASN B 218     1199   1325   1297   -142    -89    196       C  
ATOM   2169  C   ASN B 218      41.651  45.388  -6.011  1.00  9.93           C  
ANISOU 2169  C   ASN B 218     1141   1303   1330   -152   -106    178       C  
ATOM   2170  O   ASN B 218      41.491  46.355  -5.263  1.00  8.36           O  
ANISOU 2170  O   ASN B 218      930   1078   1167   -169   -141    174       O  
ATOM   2171  CB  ASN B 218      39.831  44.716  -7.591  1.00  6.13           C  
ANISOU 2171  CB  ASN B 218      740    823    767   -129   -119    160       C  
ATOM   2172  CG  ASN B 218      39.023  45.245  -8.751  1.00 10.90           C  
ANISOU 2172  CG  ASN B 218     1383   1421   1335   -126   -139    174       C  
ATOM   2173  OD1 ASN B 218      39.240  46.380  -9.181  1.00 10.96           O  
ANISOU 2173  OD1 ASN B 218     1395   1418   1353   -135   -140    212       O  
ATOM   2174  ND2 ASN B 218      38.097  44.434  -9.272  1.00 10.97           N  
ANISOU 2174  ND2 ASN B 218     1429   1433   1308   -117   -166    150       N  
ATOM   2175  N   LEU B 219      42.232  44.259  -5.620  1.00  7.97           N  
ANISOU 2175  N   LEU B 219      882   1072   1075   -132    -87    163       N  
ATOM   2176  CA  LEU B 219      42.732  44.096  -4.260  1.00  9.66           C  
ANISOU 2176  CA  LEU B 219     1066   1282   1324   -136   -110    148       C  
ATOM   2177  C   LEU B 219      43.881  45.055  -3.986  1.00 10.60           C  
ANISOU 2177  C   LEU B 219     1131   1400   1495   -161   -118    178       C  
ATOM   2178  O   LEU B 219      43.900  45.739  -2.961  1.00  8.89           O  
ANISOU 2178  O   LEU B 219      907   1159   1310   -180   -165    164       O  
ATOM   2179  CB  LEU B 219      43.189  42.658  -4.035  1.00  7.57           C  
ANISOU 2179  CB  LEU B 219      807   1027   1041   -103    -96    133       C  
ATOM   2180  CG  LEU B 219      42.057  41.630  -4.022  1.00  5.75           C  
ANISOU 2180  CG  LEU B 219      632    781    773    -97   -109    108       C  
ATOM   2181  CD1 LEU B 219      42.601  40.219  -4.297  1.00  6.93           C  
ANISOU 2181  CD1 LEU B 219      812    922    900    -57    -97     97       C  
ATOM   2182  CD2 LEU B 219      41.331  41.714  -2.673  1.00  8.05           C  
ANISOU 2182  CD2 LEU B 219      921   1066   1072   -118   -140     95       C  
ATOM   2183  N   ASP B 220      44.841  45.083  -4.902  1.00  8.69           N  
ANISOU 2183  N   ASP B 220      855   1188   1261   -161    -73    219       N  
ATOM   2184  CA  ASP B 220      46.007  45.953  -4.772  1.00  9.50           C  
ANISOU 2184  CA  ASP B 220      888   1298   1425   -202    -79    265       C  
ATOM   2185  C   ASP B 220      45.543  47.397  -4.631  1.00  8.26           C  
ANISOU 2185  C   ASP B 220      753   1087   1298   -253   -130    278       C  
ATOM   2186  O   ASP B 220      45.976  48.110  -3.725  1.00 11.99           O  
ANISOU 2186  O   ASP B 220     1204   1526   1825   -289   -189    276       O  
ATOM   2187  CB  ASP B 220      46.924  45.797  -5.978  1.00 12.39           C  
ANISOU 2187  CB  ASP B 220     1206   1720   1780   -193     -3    321       C  
ATOM   2188  CG  ASP B 220      48.225  46.576  -5.843  1.00 23.38           C  
ANISOU 2188  CG  ASP B 220     2500   3135   3248   -246     -4    384       C  
ATOM   2189  OD1 ASP B 220      48.815  46.602  -4.739  1.00 22.50           O  
ANISOU 2189  OD1 ASP B 220     2341   3013   3194   -263    -59    371       O  
ATOM   2190  OD2 ASP B 220      48.657  47.161  -6.858  1.00 27.76           O  
ANISOU 2190  OD2 ASP B 220     3024   3720   3802   -276     48    453       O  
ATOM   2191  N   GLN B 221      44.638  47.814  -5.513  1.00  8.30           N  
ANISOU 2191  N   GLN B 221      810   1076   1267   -251   -118    287       N  
ATOM   2192  CA  GLN B 221      44.170  49.199  -5.494  1.00 10.82           C  
ANISOU 2192  CA  GLN B 221     1162   1334   1615   -287   -171    301       C  
ATOM   2193  C   GLN B 221      43.411  49.542  -4.217  1.00  8.92           C  
ANISOU 2193  C   GLN B 221      955   1048   1387   -270   -239    236       C  
ATOM   2194  O   GLN B 221      43.633  50.610  -3.639  1.00 11.12           O  
ANISOU 2194  O   GLN B 221     1245   1270   1712   -299   -302    235       O  
ATOM   2195  CB  GLN B 221      43.299  49.495  -6.708  1.00 10.46           C  
ANISOU 2195  CB  GLN B 221     1169   1282   1522   -275   -152    323       C  
ATOM   2196  CG  GLN B 221      44.131  49.657  -7.978  1.00 18.71           C  
ANISOU 2196  CG  GLN B 221     2194   2362   2551   -302    -91    404       C  
ATOM   2197  CD  GLN B 221      43.276  49.831  -9.208  1.00 21.24           C  
ANISOU 2197  CD  GLN B 221     2582   2682   2806   -282    -77    425       C  
ATOM   2198  OE1 GLN B 221      42.098  50.216  -9.118  1.00 17.28           O  
ANISOU 2198  OE1 GLN B 221     2133   2137   2296   -262   -131    391       O  
ATOM   2199  NE2 GLN B 221      43.862  49.562 -10.374  1.00 23.97           N  
ANISOU 2199  NE2 GLN B 221     2925   3082   3100   -279     -6    481       N  
ATOM   2200  N   ALA B 222      42.519  48.661  -3.770  1.00  8.60           N  
ANISOU 2200  N   ALA B 222      934   1033   1302   -223   -229    185       N  
ATOM   2201  CA  ALA B 222      41.768  48.955  -2.541  1.00  8.92           C  
ANISOU 2201  CA  ALA B 222     1000   1050   1338   -196   -275    128       C  
ATOM   2202  C   ALA B 222      42.722  49.097  -1.367  1.00 12.47           C  
ANISOU 2202  C   ALA B 222     1434   1486   1819   -212   -317    112       C  
ATOM   2203  O   ALA B 222      42.582  50.003  -0.559  1.00 10.44           O  
ANISOU 2203  O   ALA B 222     1209   1182   1576   -206   -378     79       O  
ATOM   2204  CB  ALA B 222      40.746  47.878  -2.244  1.00  9.86           C  
ANISOU 2204  CB  ALA B 222     1127   1213   1407   -158   -247     95       C  
ATOM   2205  N   PHE B 223      43.694  48.196  -1.277  1.00  8.76           N  
ANISOU 2205  N   PHE B 223      919   1052   1357   -222   -293    131       N  
ATOM   2206  CA  PHE B 223      44.611  48.220  -0.139  1.00  8.30           C  
ANISOU 2206  CA  PHE B 223      840    986   1328   -233   -344    116       C  
ATOM   2207  C   PHE B 223      45.459  49.481  -0.201  1.00 12.41           C  
ANISOU 2207  C   PHE B 223     1342   1456   1918   -292   -404    145       C  
ATOM   2208  O   PHE B 223      45.717  50.104   0.826  1.00 11.82           O  
ANISOU 2208  O   PHE B 223     1290   1337   1863   -302   -484    113       O  
ATOM   2209  CB  PHE B 223      45.505  46.974  -0.104  1.00 11.51           C  
ANISOU 2209  CB  PHE B 223     1196   1442   1735   -222   -312    134       C  
ATOM   2210  CG  PHE B 223      44.744  45.675   0.029  1.00  9.68           C  
ANISOU 2210  CG  PHE B 223      995   1240   1441   -176   -271    111       C  
ATOM   2211  CD1 PHE B 223      43.432  45.658   0.492  1.00  8.86           C  
ANISOU 2211  CD1 PHE B 223      944   1132   1291   -156   -272     77       C  
ATOM   2212  CD2 PHE B 223      45.342  44.468  -0.321  1.00  9.32           C  
ANISOU 2212  CD2 PHE B 223      924   1227   1390   -152   -234    128       C  
ATOM   2213  CE1 PHE B 223      42.744  44.464   0.622  1.00 12.44           C  
ANISOU 2213  CE1 PHE B 223     1419   1609   1698   -134   -240     70       C  
ATOM   2214  CE2 PHE B 223      44.645  43.259  -0.203  1.00  9.98           C  
ANISOU 2214  CE2 PHE B 223     1049   1318   1423   -121   -212    111       C  
ATOM   2215  CZ  PHE B 223      43.344  43.264   0.278  1.00 11.10           C  
ANISOU 2215  CZ  PHE B 223     1239   1453   1526   -123   -217     88       C  
ATOM   2216  N  ASER B 224      45.873  49.864  -1.407  0.66  9.15           N  
ANISOU 2216  N  ASER B 224      894   1045   1537   -333   -368    209       N  
ATOM   2217  N  BSER B 224      45.878  49.855  -1.408  0.34 10.09           N  
ANISOU 2217  N  BSER B 224     1013   1165   1656   -333   -368    209       N  
ATOM   2218  CA ASER B 224      46.712  51.041  -1.580  0.66 12.21           C  
ANISOU 2218  CA ASER B 224     1260   1385   1993   -402   -416    256       C  
ATOM   2219  CA BSER B 224      46.704  51.042  -1.605  0.34 12.03           C  
ANISOU 2219  CA BSER B 224     1237   1362   1970   -402   -415    257       C  
ATOM   2220  C  ASER B 224      45.966  52.328  -1.208  0.66 12.47           C  
ANISOU 2220  C  ASER B 224     1380   1324   2034   -405   -494    222       C  
ATOM   2221  C  BSER B 224      45.966  52.324  -1.213  0.34 12.29           C  
ANISOU 2221  C  BSER B 224     1357   1301   2011   -405   -494    223       C  
ATOM   2222  O  ASER B 224      46.513  53.181  -0.514  0.66 12.11           O  
ANISOU 2222  O  ASER B 224     1358   1224   2019   -424   -564    211       O  
ATOM   2223  O  BSER B 224      46.515  53.169  -0.508  0.34 12.20           O  
ANISOU 2223  O  BSER B 224     1370   1237   2031   -423   -564    211       O  
ATOM   2224  CB ASER B 224      47.225  51.131  -3.019  0.66 13.52           C  
ANISOU 2224  CB ASER B 224     1376   1587   2173   -439   -343    342       C  
ATOM   2225  CB BSER B 224      47.172  51.139  -3.063  0.34 12.74           C  
ANISOU 2225  CB BSER B 224     1279   1487   2072   -439   -342    343       C  
ATOM   2226  OG ASER B 224      48.039  52.279  -3.183  0.66 10.85           O  
ANISOU 2226  OG ASER B 224     1029   1210   1883   -495   -376    390       O  
ATOM   2227  OG BSER B 224      48.018  50.055  -3.409  0.34 11.06           O  
ANISOU 2227  OG BSER B 224      984   1363   1856   -424   -270    371       O  
ATOM   2228  N   VAL B 225      44.726  52.460  -1.675  1.00 12.26           N  
ANISOU 2228  N   VAL B 225     1410   1283   1966   -366   -476    202       N  
ATOM   2229  CA  VAL B 225      43.917  53.647  -1.384  1.00 10.72           C  
ANISOU 2229  CA  VAL B 225     1300    999   1775   -345   -548    164       C  
ATOM   2230  C   VAL B 225      43.603  53.737   0.104  1.00 12.14           C  
ANISOU 2230  C   VAL B 225     1527   1155   1931   -293   -611     74       C  
ATOM   2231  O   VAL B 225      43.700  54.806   0.698  1.00 12.99           O  
ANISOU 2231  O   VAL B 225     1696   1174   2067   -299   -705     42       O  
ATOM   2232  CB  VAL B 225      42.600  53.645  -2.179  1.00  9.85           C  
ANISOU 2232  CB  VAL B 225     1228    900   1615   -289   -505    158       C  
ATOM   2233  CG1 VAL B 225      41.671  54.770  -1.715  1.00 12.12           C  
ANISOU 2233  CG1 VAL B 225     1599   1105   1901   -236   -580    103       C  
ATOM   2234  CG2 VAL B 225      42.896  53.781  -3.675  1.00 14.72           C  
ANISOU 2234  CG2 VAL B 225     1825   1526   2242   -337   -459    248       C  
ATOM   2235  N   ALA B 226      43.230  52.615   0.709  1.00 11.46           N  
ANISOU 2235  N   ALA B 226     1422   1145   1785   -241   -562     35       N  
ATOM   2236  CA  ALA B 226      42.926  52.630   2.130  1.00 11.00           C  
ANISOU 2236  CA  ALA B 226     1414   1082   1684   -186   -608    -43       C  
ATOM   2237  C   ALA B 226      44.151  53.056   2.944  1.00 13.42           C  
ANISOU 2237  C   ALA B 226     1724   1340   2035   -233   -700    -50       C  
ATOM   2238  O   ALA B 226      44.018  53.796   3.917  1.00 14.54           O  
ANISOU 2238  O   ALA B 226     1942   1429   2155   -195   -768   -109       O  
ATOM   2239  CB  ALA B 226      42.413  51.265   2.595  1.00 14.03           C  
ANISOU 2239  CB  ALA B 226     1774   1560   1998   -139   -534    -60       C  
ATOM   2240  N   GLU B 227      45.345  52.630   2.542  1.00  9.78           N  
ANISOU 2240  N   GLU B 227     1186    912   1619   -291   -670     16       N  
ATOM   2241  CA  GLU B 227      46.524  53.027   3.312  1.00 10.48           C  
ANISOU 2241  CA  GLU B 227     1269    974   1740   -318   -730     21       C  
ATOM   2242  C   GLU B 227      46.859  54.501   3.109  1.00 16.11           C  
ANISOU 2242  C   GLU B 227     2020   1594   2506   -359   -800     41       C  
ATOM   2243  O   GLU B 227      47.045  55.252   4.079  1.00 17.18           O  
ANISOU 2243  O   GLU B 227     2220   1666   2639   -346   -887     -3       O  
ATOM   2244  CB  GLU B 227      47.721  52.153   2.956  1.00 11.49           C  
ANISOU 2244  CB  GLU B 227     1293   1169   1902   -357   -683     81       C  
ATOM   2245  CG  GLU B 227      48.969  52.452   3.793  1.00 11.46           C  
ANISOU 2245  CG  GLU B 227     1270   1147   1936   -385   -752     85       C  
ATOM   2246  CD  GLU B 227      50.039  51.389   3.588  1.00 23.52           C  
ANISOU 2246  CD  GLU B 227     2693   2755   3487   -398   -706    129       C  
ATOM   2247  OE1 GLU B 227      49.822  50.230   3.991  1.00 27.59           O  
ANISOU 2247  OE1 GLU B 227     3203   3323   3958   -349   -678    104       O  
ATOM   2248  OE2 GLU B 227      51.088  51.705   3.009  1.00 21.60           O  
ANISOU 2248  OE2 GLU B 227     2374   2523   3308   -452   -700    191       O  
ATOM   2249  N   ARG B 228      46.940  54.905   1.847  1.00 12.35           N  
ANISOU 2249  N   ARG B 228     1511   1109   2071   -408   -764    111       N  
ATOM   2250  CA  ARG B 228      47.359  56.245   1.481  1.00 18.50           C  
ANISOU 2250  CA  ARG B 228     2317   1808   2903   -460   -826    152       C  
ATOM   2251  C   ARG B 228      46.358  57.290   1.970  1.00 20.15           C  
ANISOU 2251  C   ARG B 228     2646   1919   3089   -407   -906     86       C  
ATOM   2252  O   ARG B 228      46.745  58.316   2.527  1.00 21.98           O  
ANISOU 2252  O   ARG B 228     2933   2071   3347   -420  -1000     73       O  
ATOM   2253  CB  ARG B 228      47.529  56.345  -0.042  1.00 20.54           C  
ANISOU 2253  CB  ARG B 228     2522   2092   3191   -515   -757    245       C  
ATOM   2254  CG  ARG B 228      47.904  57.738  -0.560  1.00 26.11           C  
ANISOU 2254  CG  ARG B 228     3257   2718   3947   -577   -816    302       C  
ATOM   2255  CD  ARG B 228      47.547  57.915  -2.044  1.00 37.10           C  
ANISOU 2255  CD  ARG B 228     4637   4123   5334   -604   -749    377       C  
ATOM   2256  NE  ARG B 228      47.496  56.654  -2.779  1.00 48.60           N  
ANISOU 2256  NE  ARG B 228     6021   5686   6757   -591   -633    404       N  
ATOM   2257  CZ  ARG B 228      46.447  56.235  -3.487  1.00 50.89           C  
ANISOU 2257  CZ  ARG B 228     6340   5994   7003   -552   -582    400       C  
ATOM   2258  NH1 ARG B 228      45.348  56.982  -3.570  1.00 45.15           N  
ANISOU 2258  NH1 ARG B 228     5705   5187   6262   -519   -633    370       N  
ATOM   2259  NH2 ARG B 228      46.499  55.066  -4.118  1.00 42.83           N  
ANISOU 2259  NH2 ARG B 228     5257   5068   5950   -541   -484    424       N  
ATOM   2260  N   ASP B 229      45.072  57.007   1.784  1.00 15.76           N  
ANISOU 2260  N   ASP B 229     2132   1372   2486   -341   -873     40       N  
ATOM   2261  CA  ASP B 229      44.033  58.016   1.968  1.00 16.34           C  
ANISOU 2261  CA  ASP B 229     2311   1359   2538   -276   -934    -18       C  
ATOM   2262  C   ASP B 229      43.209  57.880   3.259  1.00 17.36           C  
ANISOU 2262  C   ASP B 229     2512   1489   2594   -167   -963   -133       C  
ATOM   2263  O   ASP B 229      42.677  58.873   3.756  1.00 18.53           O  
ANISOU 2263  O   ASP B 229     2754   1563   2722   -101  -1032   -191       O  
ATOM   2264  CB  ASP B 229      43.096  58.003   0.756  1.00 20.76           C  
ANISOU 2264  CB  ASP B 229     2872   1920   3097   -265   -885     12       C  
ATOM   2265  CG  ASP B 229      43.764  58.525  -0.496  1.00 27.50           C  
ANISOU 2265  CG  ASP B 229     3690   2755   4002   -355   -870    122       C  
ATOM   2266  OD1 ASP B 229      44.143  59.717  -0.519  1.00 28.11           O  
ANISOU 2266  OD1 ASP B 229     3813   2752   4114   -384   -945    144       O  
ATOM   2267  OD2 ASP B 229      43.904  57.751  -1.461  1.00 37.53           O  
ANISOU 2267  OD2 ASP B 229     4890   4096   5273   -393   -784    186       O  
ATOM   2268  N   LEU B 230      43.107  56.670   3.800  1.00 16.38           N  
ANISOU 2268  N   LEU B 230     2347   1455   2421   -143   -907   -164       N  
ATOM   2269  CA  LEU B 230      42.318  56.442   5.014  1.00 16.64           C  
ANISOU 2269  CA  LEU B 230     2443   1514   2365    -38   -916   -265       C  
ATOM   2270  C   LEU B 230      43.175  56.045   6.219  1.00 20.39           C  
ANISOU 2270  C   LEU B 230     2921   2015   2812    -42   -943   -284       C  
ATOM   2271  O   LEU B 230      42.651  55.827   7.309  1.00 21.00           O  
ANISOU 2271  O   LEU B 230     3054   2124   2802     43   -945   -358       O  
ATOM   2272  CB  LEU B 230      41.259  55.361   4.759  1.00 16.19           C  
ANISOU 2272  CB  LEU B 230     2341   1564   2246     15   -812   -276       C  
ATOM   2273  CG  LEU B 230      40.307  55.639   3.581  1.00 20.83           C  
ANISOU 2273  CG  LEU B 230     2911   2153   2850     37   -759   -244       C  
ATOM   2274  CD1 LEU B 230      39.263  54.528   3.471  1.00 19.21           C  
ANISOU 2274  CD1 LEU B 230     2645   2074   2580     91   -642   -239       C  
ATOM   2275  CD2 LEU B 230      39.636  56.987   3.728  1.00 24.33           C  
ANISOU 2275  CD2 LEU B 230     3453   2498   3295    113   -834   -303       C  
ATOM   2276  N   GLY B 231      44.485  55.950   6.015  1.00 17.10           N  
ANISOU 2276  N   GLY B 231     2442   1592   2462   -134   -960   -215       N  
ATOM   2277  CA  GLY B 231      45.411  55.589   7.078  1.00 19.44           C  
ANISOU 2277  CA  GLY B 231     2734   1906   2745   -144   -997   -226       C  
ATOM   2278  C   GLY B 231      45.313  54.153   7.574  1.00 21.82           C  
ANISOU 2278  C   GLY B 231     2997   2310   2983   -117   -934   -237       C  
ATOM   2279  O   GLY B 231      45.742  53.845   8.687  1.00 23.71           O  
ANISOU 2279  O   GLY B 231     3264   2565   3180    -93   -969   -267       O  
ATOM   2280  N   VAL B 232      44.770  53.270   6.743  1.00 15.26           N  
ANISOU 2280  N   VAL B 232     2105   1546   2145   -122   -849   -208       N  
ATOM   2281  CA  VAL B 232      44.593  51.875   7.112  1.00 15.76           C  
ANISOU 2281  CA  VAL B 232     2136   1704   2149    -98   -793   -208       C  
ATOM   2282  C   VAL B 232      45.783  51.052   6.639  1.00 15.28           C  
ANISOU 2282  C   VAL B 232     1977   1679   2148   -162   -766   -135       C  
ATOM   2283  O   VAL B 232      45.973  50.873   5.450  1.00 13.35           O  
ANISOU 2283  O   VAL B 232     1665   1450   1959   -206   -716    -78       O  
ATOM   2284  CB  VAL B 232      43.301  51.304   6.507  1.00 19.05           C  
ANISOU 2284  CB  VAL B 232     2540   2179   2519    -58   -705   -208       C  
ATOM   2285  CG1 VAL B 232      43.158  49.821   6.826  1.00 19.57           C  
ANISOU 2285  CG1 VAL B 232     2571   2336   2528    -41   -628   -183       C  
ATOM   2286  CG2 VAL B 232      42.105  52.086   7.005  1.00 18.42           C  
ANISOU 2286  CG2 VAL B 232     2541   2083   2373     28   -707   -278       C  
ATOM   2287  N  ATHR B 233      46.565  50.553   7.594  0.51 17.61           N  
ANISOU 2287  N  ATHR B 233     2272   1994   2424   -156   -800   -141       N  
ATOM   2288  N  BTHR B 233      46.622  50.591   7.557  0.49 17.46           N  
ANISOU 2288  N  BTHR B 233     2251   1973   2411   -159   -801   -138       N  
ATOM   2289  CA ATHR B 233      47.685  49.642   7.342  0.51 17.87           C  
ANISOU 2289  CA ATHR B 233     2216   2071   2503   -190   -780    -85       C  
ATOM   2290  CA BTHR B 233      47.815  49.898   7.099  0.49 15.88           C  
ANISOU 2290  CA BTHR B 233     1954   1807   2274   -206   -782    -76       C  
ATOM   2291  C  ATHR B 233      47.359  48.525   6.348  0.51 12.03           C  
ANISOU 2291  C  ATHR B 233     1412   1392   1765   -190   -692    -43       C  
ATOM   2292  C  BTHR B 233      47.455  48.599   6.392  0.49 12.05           C  
ANISOU 2292  C  BTHR B 233     1414   1391   1772   -193   -698    -43       C  
ATOM   2293  O  ATHR B 233      46.341  47.843   6.504  0.51 13.49           O  
ANISOU 2293  O  ATHR B 233     1631   1611   1882   -150   -659    -62       O  
ATOM   2294  O  BTHR B 233      46.522  47.891   6.773  0.49 14.02           O  
ANISOU 2294  O  BTHR B 233     1706   1675   1948   -148   -674    -68       O  
ATOM   2295  CB ATHR B 233      48.146  48.975   8.666  0.51 17.63           C  
ANISOU 2295  CB ATHR B 233     2216   2063   2418   -156   -826   -109       C  
ATOM   2296  CB BTHR B 233      48.795  49.594   8.231  0.49 21.87           C  
ANISOU 2296  CB BTHR B 233     2716   2570   3023   -199   -846    -86       C  
ATOM   2297  OG1ATHR B 233      48.465  49.984   9.627  0.51 25.35           O  
ANISOU 2297  OG1ATHR B 233     3262   2982   3388   -151   -914   -152       O  
ATOM   2298  OG1BTHR B 233      48.507  50.429   9.359  0.49 31.28           O  
ANISOU 2298  OG1BTHR B 233     4009   3710   4166   -168   -921   -148       O  
ATOM   2299  CG2ATHR B 233      49.359  48.090   8.436  0.51 17.62           C  
ANISOU 2299  CG2ATHR B 233     2122   2102   2469   -179   -819    -57       C  
ATOM   2300  CG2BTHR B 233      50.210  49.848   7.741  0.49 17.26           C  
ANISOU 2300  CG2BTHR B 233     2040   1980   2538   -261   -868    -31       C  
ATOM   2301  N   ARG B 234      48.203  48.325   5.331  1.00 13.95           N  
ANISOU 2301  N   ARG B 234     1566   1654   2079   -231   -655     16       N  
ATOM   2302  CA  ARG B 234      47.998  47.165   4.463  1.00 13.87           C  
ANISOU 2302  CA  ARG B 234     1504   1701   2066   -217   -578     51       C  
ATOM   2303  C   ARG B 234      48.361  45.905   5.233  1.00 17.31           C  
ANISOU 2303  C   ARG B 234     1936   2174   2468   -175   -591     47       C  
ATOM   2304  O   ARG B 234      49.538  45.627   5.427  1.00 24.47           O  
ANISOU 2304  O   ARG B 234     2788   3096   3415   -178   -613     68       O  
ATOM   2305  CB  ARG B 234      48.847  47.261   3.188  1.00 17.96           C  
ANISOU 2305  CB  ARG B 234     1930   2239   2653   -255   -528    112       C  
ATOM   2306  CG  ARG B 234      48.767  46.013   2.292  1.00 18.65           C  
ANISOU 2306  CG  ARG B 234     1968   2384   2735   -226   -453    144       C  
ATOM   2307  CD  ARG B 234      49.756  46.095   1.136  1.00 31.28           C  
ANISOU 2307  CD  ARG B 234     3473   4021   4390   -249   -397    204       C  
ATOM   2308  NE  ARG B 234      49.306  47.056   0.140  1.00 29.49           N  
ANISOU 2308  NE  ARG B 234     3257   3773   4174   -292   -363    231       N  
ATOM   2309  CZ  ARG B 234      49.005  46.766  -1.125  1.00 27.84           C  
ANISOU 2309  CZ  ARG B 234     3035   3597   3947   -283   -280    264       C  
ATOM   2310  NH1 ARG B 234      49.134  45.531  -1.584  1.00 30.14           N  
ANISOU 2310  NH1 ARG B 234     3313   3939   4200   -221   -214    262       N  
ATOM   2311  NH2 ARG B 234      48.589  47.727  -1.938  1.00 17.72           N  
ANISOU 2311  NH2 ARG B 234     1774   2289   2670   -325   -264    293       N  
ATOM   2312  N   LEU B 235      47.357  45.155   5.675  1.00  8.95           N  
ANISOU 2312  N   LEU B 235      940   1130   1332   -135   -566     26       N  
ATOM   2313  CA  LEU B 235      47.601  43.921   6.440  1.00  9.88           C  
ANISOU 2313  CA  LEU B 235     1077   1272   1406    -94   -576     32       C  
ATOM   2314  C   LEU B 235      47.670  42.715   5.526  1.00 13.85           C  
ANISOU 2314  C   LEU B 235     1547   1798   1919    -74   -502     68       C  
ATOM   2315  O   LEU B 235      48.268  41.696   5.878  1.00 12.68           O  
ANISOU 2315  O   LEU B 235     1393   1659   1766    -40   -519     84       O  
ATOM   2316  CB  LEU B 235      46.488  43.681   7.458  1.00 10.92           C  
ANISOU 2316  CB  LEU B 235     1305   1409   1435    -64   -568      3       C  
ATOM   2317  CG  LEU B 235      46.240  44.780   8.484  1.00 12.85           C  
ANISOU 2317  CG  LEU B 235     1612   1634   1637    -56   -636    -48       C  
ATOM   2318  CD1 LEU B 235      45.098  44.366   9.409  1.00 15.20           C  
ANISOU 2318  CD1 LEU B 235     1992   1963   1819    -13   -598    -64       C  
ATOM   2319  CD2 LEU B 235      47.514  45.020   9.277  1.00 13.51           C  
ANISOU 2319  CD2 LEU B 235     1686   1697   1748    -61   -726    -56       C  
ATOM   2320  N   LEU B 236      47.039  42.838   4.363  1.00 10.86           N  
ANISOU 2320  N   LEU B 236     1157   1422   1548    -87   -429     77       N  
ATOM   2321  CA  LEU B 236      46.855  41.699   3.462  1.00 11.90           C  
ANISOU 2321  CA  LEU B 236     1288   1565   1670    -62   -363     96       C  
ATOM   2322  C   LEU B 236      47.581  41.849   2.139  1.00 15.29           C  
ANISOU 2322  C   LEU B 236     1645   2013   2152    -64   -320    121       C  
ATOM   2323  O   LEU B 236      47.636  42.933   1.570  1.00 11.23           O  
ANISOU 2323  O   LEU B 236     1098   1499   1671   -103   -311    131       O  
ATOM   2324  CB  LEU B 236      45.366  41.487   3.167  1.00  8.77           C  
ANISOU 2324  CB  LEU B 236      950   1162   1220    -71   -315     87       C  
ATOM   2325  CG  LEU B 236      44.396  41.514   4.349  1.00 10.35           C  
ANISOU 2325  CG  LEU B 236     1210   1364   1358    -72   -331     71       C  
ATOM   2326  CD1 LEU B 236      42.961  41.337   3.835  1.00 13.75           C  
ANISOU 2326  CD1 LEU B 236     1664   1802   1756    -87   -278     72       C  
ATOM   2327  CD2 LEU B 236      44.771  40.433   5.393  1.00 11.37           C  
ANISOU 2327  CD2 LEU B 236     1376   1491   1451    -48   -363     85       C  
ATOM   2328  N  AASP B 237      48.180  40.767   1.645  0.59 14.47           N  
ANISOU 2328  N  AASP B 237     1521   1924   2053    -16   -291    134       N  
ATOM   2329  N  BASP B 237      48.083  40.715   1.666  0.41 13.54           N  
ANISOU 2329  N  BASP B 237     1411   1804   1930    -15   -290    132       N  
ATOM   2330  CA AASP B 237      48.764  40.773   0.299  0.59 10.07           C  
ANISOU 2330  CA AASP B 237      905   1399   1523      1   -228    156       C  
ATOM   2331  CA BASP B 237      48.656  40.560   0.344  0.41 12.83           C  
ANISOU 2331  CA BASP B 237     1269   1745   1863      8   -228    152       C  
ATOM   2332  C  AASP B 237      47.745  40.215  -0.690  0.59  9.67           C  
ANISOU 2332  C  AASP B 237      924   1334   1417     16   -172    143       C  
ATOM   2333  C  BASP B 237      47.522  40.244  -0.637  0.41  9.67           C  
ANISOU 2333  C  BASP B 237      935   1327   1410      9   -175    139       C  
ATOM   2334  O  AASP B 237      47.253  39.110  -0.484  0.59  9.13           O  
ANISOU 2334  O  AASP B 237      922   1236   1310     46   -179    125       O  
ATOM   2335  O  BASP B 237      46.694  39.382  -0.353  0.41 13.68           O  
ANISOU 2335  O  BASP B 237     1519   1804   1876     21   -184    121       O  
ATOM   2336  CB AASP B 237      50.037  39.925   0.224  0.59 15.54           C  
ANISOU 2336  CB AASP B 237     1534   2125   2246     67   -225    170       C  
ATOM   2337  CB BASP B 237      49.688  39.427   0.377  0.41 13.18           C  
ANISOU 2337  CB BASP B 237     1279   1807   1920     84   -229    157       C  
ATOM   2338  CG AASP B 237      51.231  40.569   0.907  0.59 20.02           C  
ANISOU 2338  CG AASP B 237     1998   2722   2885     47   -281    194       C  
ATOM   2339  CG BASP B 237      50.696  39.515  -0.732  0.41 17.36           C  
ANISOU 2339  CG BASP B 237     1716   2395   2485    118   -167    184       C  
ATOM   2340  OD1AASP B 237      51.254  41.805   1.090  0.59 23.01           O  
ANISOU 2340  OD1AASP B 237     2347   3097   3300    -27   -311    207       O  
ATOM   2341  OD1BASP B 237      50.338  40.005  -1.816  0.41 21.90           O  
ANISOU 2341  OD1BASP B 237     2291   2986   3042     97   -105    194       O  
ATOM   2342  OD2AASP B 237      52.163  39.818   1.253  0.59 16.69           O  
ANISOU 2342  OD2AASP B 237     1530   2323   2489    107   -305    200       O  
ATOM   2343  OD2BASP B 237      51.854  39.090  -0.511  0.41 15.35           O  
ANISOU 2343  OD2BASP B 237     1383   2177   2272    171   -179    197       O  
ATOM   2344  N   PRO B 238      47.454  40.956  -1.775  1.00 11.56           N  
ANISOU 2344  N   PRO B 238     1151   1587   1654    -10   -127    155       N  
ATOM   2345  CA  PRO B 238      46.469  40.542  -2.788  1.00  9.16           C  
ANISOU 2345  CA  PRO B 238      915   1270   1296      1    -88    141       C  
ATOM   2346  C   PRO B 238      46.596  39.069  -3.210  1.00 10.89           C  
ANISOU 2346  C   PRO B 238     1182   1477   1478     70    -72    120       C  
ATOM   2347  O   PRO B 238      45.575  38.412  -3.358  1.00 10.15           O  
ANISOU 2347  O   PRO B 238     1168   1343   1345     65    -86     98       O  
ATOM   2348  CB  PRO B 238      46.767  41.471  -3.962  1.00 13.64           C  
ANISOU 2348  CB  PRO B 238     1443   1870   1869    -16    -39    173       C  
ATOM   2349  CG  PRO B 238      47.240  42.754  -3.282  1.00 14.28           C  
ANISOU 2349  CG  PRO B 238     1461   1953   2013    -76    -75    200       C  
ATOM   2350  CD  PRO B 238      48.067  42.260  -2.101  1.00 11.85           C  
ANISOU 2350  CD  PRO B 238     1115   1649   1740    -57   -120    191       C  
ATOM   2351  N   GLU B 239      47.815  38.556  -3.360  1.00 11.81           N  
ANISOU 2351  N   GLU B 239     1251   1624   1612    133    -51    127       N  
ATOM   2352  CA  GLU B 239      47.984  37.170  -3.799  1.00 13.32           C  
ANISOU 2352  CA  GLU B 239     1502   1793   1767    218    -42     98       C  
ATOM   2353  C   GLU B 239      47.451  36.147  -2.794  1.00 14.62           C  
ANISOU 2353  C   GLU B 239     1745   1888   1922    219   -108     79       C  
ATOM   2354  O   GLU B 239      47.147  35.012  -3.179  1.00 12.84           O  
ANISOU 2354  O   GLU B 239     1606   1611   1661    264   -120     52       O  
ATOM   2355  CB  GLU B 239      49.453  36.869  -4.095  1.00 14.86           C  
ANISOU 2355  CB  GLU B 239     1615   2045   1986    305     -2    109       C  
ATOM   2356  CG  GLU B 239      49.970  37.667  -5.283  1.00 29.31           C  
ANISOU 2356  CG  GLU B 239     3375   3953   3809    310     82    139       C  
ATOM   2357  CD  GLU B 239      51.113  36.995  -6.002  1.00 52.72           C  
ANISOU 2357  CD  GLU B 239     6290   6980   6760    427    147    137       C  
ATOM   2358  OE1 GLU B 239      52.103  36.626  -5.335  1.00 56.26           O  
ANISOU 2358  OE1 GLU B 239     6662   7455   7260    478    130    145       O  
ATOM   2359  OE2 GLU B 239      51.017  36.842  -7.240  1.00 60.25           O  
ANISOU 2359  OE2 GLU B 239     7284   7962   7645    478    216    127       O  
ATOM   2360  N   ASP B 240      47.333  36.542  -1.525  1.00 12.00           N  
ANISOU 2360  N   ASP B 240     1392   1550   1617    169   -154     95       N  
ATOM   2361  CA  ASP B 240      46.800  35.638  -0.496  1.00 13.29           C  
ANISOU 2361  CA  ASP B 240     1630   1656   1762    160   -210     94       C  
ATOM   2362  C   ASP B 240      45.278  35.709  -0.395  1.00 15.43           C  
ANISOU 2362  C   ASP B 240     1963   1898   2001     85   -217     94       C  
ATOM   2363  O   ASP B 240      44.636  34.815   0.185  1.00 11.71           O  
ANISOU 2363  O   ASP B 240     1561   1378   1509     66   -251    103       O  
ATOM   2364  CB  ASP B 240      47.424  35.946   0.875  1.00 11.83           C  
ANISOU 2364  CB  ASP B 240     1404   1486   1604    153   -258    112       C  
ATOM   2365  CG  ASP B 240      48.906  35.650   0.921  1.00 16.88           C  
ANISOU 2365  CG  ASP B 240     1976   2153   2284    230   -270    117       C  
ATOM   2366  OD1 ASP B 240      49.380  34.791   0.143  1.00 15.16           O  
ANISOU 2366  OD1 ASP B 240     1771   1926   2062    309   -246    103       O  
ATOM   2367  OD2 ASP B 240      49.602  36.276   1.748  1.00 16.77           O  
ANISOU 2367  OD2 ASP B 240     1896   2170   2306    217   -308    131       O  
ATOM   2368  N   VAL B 241      44.701  36.765  -0.964  1.00 10.11           N  
ANISOU 2368  N   VAL B 241     1258   1256   1328     42   -186     92       N  
ATOM   2369  CA  VAL B 241      43.256  36.966  -0.904  1.00  9.03           C  
ANISOU 2369  CA  VAL B 241     1154   1109   1169    -21   -191     94       C  
ATOM   2370  C   VAL B 241      42.558  36.480  -2.183  1.00  9.27           C  
ANISOU 2370  C   VAL B 241     1233   1113   1176    -23   -182     78       C  
ATOM   2371  O   VAL B 241      41.424  36.001  -2.133  1.00 11.36           O  
ANISOU 2371  O   VAL B 241     1540   1350   1426    -69   -205     83       O  
ATOM   2372  CB  VAL B 241      42.916  38.453  -0.643  1.00  7.50           C  
ANISOU 2372  CB  VAL B 241      906    956    989    -59   -179     97       C  
ATOM   2373  CG1 VAL B 241      41.394  38.675  -0.632  1.00  7.12           C  
ANISOU 2373  CG1 VAL B 241      876    910    921   -107   -179     98       C  
ATOM   2374  CG2 VAL B 241      43.551  38.900   0.695  1.00  9.18           C  
ANISOU 2374  CG2 VAL B 241     1090   1183   1215    -57   -207    102       C  
ATOM   2375  N   ASP B 242      43.240  36.594  -3.323  1.00 11.18           N  
ANISOU 2375  N   ASP B 242     1469   1369   1410     25   -150     64       N  
ATOM   2376  CA  ASP B 242      42.665  36.158  -4.596  1.00  9.68           C  
ANISOU 2376  CA  ASP B 242     1341   1155   1182     35   -149     41       C  
ATOM   2377  C   ASP B 242      42.844  34.648  -4.727  1.00 12.20           C  
ANISOU 2377  C   ASP B 242     1747   1408   1481     81   -183     17       C  
ATOM   2378  O   ASP B 242      43.595  34.175  -5.574  1.00 11.82           O  
ANISOU 2378  O   ASP B 242     1730   1355   1404    162   -163    -11       O  
ATOM   2379  CB  ASP B 242      43.327  36.890  -5.767  1.00  7.34           C  
ANISOU 2379  CB  ASP B 242     1015    908    867     76    -94     40       C  
ATOM   2380  CG  ASP B 242      42.760  36.479  -7.108  1.00 12.10           C  
ANISOU 2380  CG  ASP B 242     1696   1489   1411     97    -98     12       C  
ATOM   2381  OD1 ASP B 242      41.602  35.994  -7.150  1.00 10.27           O  
ANISOU 2381  OD1 ASP B 242     1523   1211   1170     51   -153     -1       O  
ATOM   2382  OD2 ASP B 242      43.475  36.639  -8.121  1.00 12.52           O  
ANISOU 2382  OD2 ASP B 242     1752   1580   1427    157    -47      7       O  
ATOM   2383  N   VAL B 243      42.170  33.905  -3.854  1.00 10.42           N  
ANISOU 2383  N   VAL B 243     1563   1130   1267     33   -234     31       N  
ATOM   2384  CA  VAL B 243      42.277  32.445  -3.791  1.00 10.19           C  
ANISOU 2384  CA  VAL B 243     1630   1015   1228     63   -286     17       C  
ATOM   2385  C   VAL B 243      40.877  31.875  -3.571  1.00 11.84           C  
ANISOU 2385  C   VAL B 243     1892   1166   1440    -34   -343     37       C  
ATOM   2386  O   VAL B 243      39.974  32.609  -3.163  1.00 11.15           O  
ANISOU 2386  O   VAL B 243     1745   1125   1366   -112   -332     67       O  
ATOM   2387  CB  VAL B 243      43.200  31.986  -2.637  1.00 13.76           C  
ANISOU 2387  CB  VAL B 243     2071   1454   1702    103   -298     37       C  
ATOM   2388  CG1 VAL B 243      44.604  32.559  -2.794  1.00 14.39           C  
ANISOU 2388  CG1 VAL B 243     2073   1600   1795    190   -248     25       C  
ATOM   2389  CG2 VAL B 243      42.603  32.423  -1.324  1.00 10.65           C  
ANISOU 2389  CG2 VAL B 243     1636   1085   1325     21   -306     84       C  
ATOM   2390  N   PRO B 244      40.684  30.569  -3.818  1.00 14.68           N  
ANISOU 2390  N   PRO B 244     2361   1426   1792    -30   -409     23       N  
ATOM   2391  CA  PRO B 244      39.327  30.029  -3.653  1.00 16.77           C  
ANISOU 2391  CA  PRO B 244     2664   1637   2072   -143   -470     54       C  
ATOM   2392  C   PRO B 244      38.758  30.195  -2.247  1.00 17.61           C  
ANISOU 2392  C   PRO B 244     2711   1777   2204   -230   -460    126       C  
ATOM   2393  O   PRO B 244      37.561  30.440  -2.108  1.00 16.06           O  
ANISOU 2393  O   PRO B 244     2472   1608   2022   -326   -467    162       O  
ATOM   2394  CB  PRO B 244      39.504  28.544  -3.994  1.00 17.92           C  
ANISOU 2394  CB  PRO B 244     2950   1649   2210   -116   -553     29       C  
ATOM   2395  CG  PRO B 244      40.626  28.536  -4.981  1.00 19.45           C  
ANISOU 2395  CG  PRO B 244     3181   1845   2364     25   -525    -42       C  
ATOM   2396  CD  PRO B 244      41.582  29.593  -4.466  1.00 17.36           C  
ANISOU 2396  CD  PRO B 244     2795   1694   2107     77   -433    -27       C  
ATOM   2397  N   GLN B 245      39.605  30.090  -1.225  1.00 14.49           N  
ANISOU 2397  N   GLN B 245     2307   1389   1808   -189   -443    148       N  
ATOM   2398  CA  GLN B 245      39.143  30.216   0.150  1.00 15.28           C  
ANISOU 2398  CA  GLN B 245     2368   1526   1913   -257   -430    216       C  
ATOM   2399  C   GLN B 245      40.032  31.161   0.962  1.00 13.25           C  
ANISOU 2399  C   GLN B 245     2040   1349   1645   -200   -379    213       C  
ATOM   2400  O   GLN B 245      40.979  30.723   1.608  1.00 15.43           O  
ANISOU 2400  O   GLN B 245     2346   1600   1916   -145   -398    221       O  
ATOM   2401  CB  GLN B 245      39.086  28.834   0.818  1.00 16.37           C  
ANISOU 2401  CB  GLN B 245     2604   1563   2053   -291   -494    265       C  
ATOM   2402  CG  GLN B 245      38.042  27.892   0.225  1.00 22.65           C  
ANISOU 2402  CG  GLN B 245     3469   2267   2868   -382   -562    284       C  
ATOM   2403  CD  GLN B 245      36.619  28.294   0.577  1.00 36.06           C  
ANISOU 2403  CD  GLN B 245     5088   4033   4581   -509   -540    346       C  
ATOM   2404  OE1 GLN B 245      36.384  29.035   1.538  1.00 37.53           O  
ANISOU 2404  OE1 GLN B 245     5189   4319   4751   -529   -475    387       O  
ATOM   2405  NE2 GLN B 245      35.657  27.800  -0.196  1.00 42.25           N  
ANISOU 2405  NE2 GLN B 245     5879   4790   5385   -570   -586    339       N  
ATOM   2406  N   PRO B 246      39.744  32.470   0.901  1.00 13.78           N  
ANISOU 2406  N   PRO B 246     2018   1507   1712   -209   -328    200       N  
ATOM   2407  CA  PRO B 246      40.502  33.458   1.677  1.00 12.59           C  
ANISOU 2407  CA  PRO B 246     1807   1422   1555   -167   -296    195       C  
ATOM   2408  C   PRO B 246      40.435  33.150   3.168  1.00 13.85           C  
ANISOU 2408  C   PRO B 246     1985   1590   1687   -189   -307    243       C  
ATOM   2409  O   PRO B 246      39.467  32.558   3.643  1.00 10.99           O  
ANISOU 2409  O   PRO B 246     1650   1217   1309   -258   -311    293       O  
ATOM   2410  CB  PRO B 246      39.802  34.785   1.346  1.00 14.54           C  
ANISOU 2410  CB  PRO B 246     1979   1739   1805   -192   -255    179       C  
ATOM   2411  CG  PRO B 246      39.195  34.549   0.000  1.00 10.01           C  
ANISOU 2411  CG  PRO B 246     1423   1138   1242   -211   -263    160       C  
ATOM   2412  CD  PRO B 246      38.735  33.105   0.037  1.00 11.99           C  
ANISOU 2412  CD  PRO B 246     1751   1313   1493   -252   -311    186       C  
ATOM   2413  N   ASP B 247      41.474  33.525   3.892  1.00 10.53           N  
ANISOU 2413  N   ASP B 247     1549   1191   1260   -135   -314    234       N  
ATOM   2414  CA  ASP B 247      41.525  33.279   5.329  1.00 12.30           C  
ANISOU 2414  CA  ASP B 247     1803   1427   1442   -143   -331    277       C  
ATOM   2415  C   ASP B 247      40.565  34.187   6.085  1.00 12.56           C  
ANISOU 2415  C   ASP B 247     1798   1539   1434   -185   -287    291       C  
ATOM   2416  O   ASP B 247      40.700  35.408   6.044  1.00 10.89           O  
ANISOU 2416  O   ASP B 247     1533   1379   1227   -161   -267    250       O  
ATOM   2417  CB  ASP B 247      42.940  33.493   5.862  1.00 10.83           C  
ANISOU 2417  CB  ASP B 247     1609   1244   1261    -70   -367    258       C  
ATOM   2418  CG  ASP B 247      43.027  33.230   7.337  1.00 13.22           C  
ANISOU 2418  CG  ASP B 247     1958   1557   1508    -71   -397    300       C  
ATOM   2419  OD1 ASP B 247      42.858  32.053   7.724  1.00 12.87           O  
ANISOU 2419  OD1 ASP B 247     1991   1457   1443    -86   -425    352       O  
ATOM   2420  OD2 ASP B 247      43.234  34.197   8.106  1.00 12.75           O  
ANISOU 2420  OD2 ASP B 247     1870   1555   1420    -58   -397    284       O  
ATOM   2421  N   GLU B 248      39.629  33.585   6.816  1.00 11.09           N  
ANISOU 2421  N   GLU B 248     1643   1363   1207   -242   -273    353       N  
ATOM   2422  CA  GLU B 248      38.562  34.352   7.451  1.00 14.14           C  
ANISOU 2422  CA  GLU B 248     1985   1839   1549   -272   -215    369       C  
ATOM   2423  C   GLU B 248      39.070  35.325   8.514  1.00 12.24           C  
ANISOU 2423  C   GLU B 248     1742   1656   1253   -214   -211    340       C  
ATOM   2424  O   GLU B 248      38.669  36.481   8.534  1.00 10.81           O  
ANISOU 2424  O   GLU B 248     1513   1533   1061   -194   -178    299       O  
ATOM   2425  CB  GLU B 248      37.528  33.411   8.075  1.00 12.93           C  
ANISOU 2425  CB  GLU B 248     1857   1696   1359   -350   -193    458       C  
ATOM   2426  CG  GLU B 248      36.358  34.165   8.675  1.00 18.14           C  
ANISOU 2426  CG  GLU B 248     2452   2469   1972   -370   -117    479       C  
ATOM   2427  CD  GLU B 248      35.307  33.247   9.248  1.00 27.76           C  
ANISOU 2427  CD  GLU B 248     3673   3714   3159   -460    -83    583       C  
ATOM   2428  OE1 GLU B 248      35.668  32.170   9.758  1.00 30.91           O  
ANISOU 2428  OE1 GLU B 248     4152   4053   3538   -491   -119    647       O  
ATOM   2429  OE2 GLU B 248      34.119  33.611   9.197  1.00 24.12           O  
ANISOU 2429  OE2 GLU B 248     3129   3337   2698   -499    -22    608       O  
ATOM   2430  N   LYS B 249      39.935  34.853   9.407  1.00  9.36           N  
ANISOU 2430  N   LYS B 249     1439   1268    850   -184   -256    359       N  
ATOM   2431  CA  LYS B 249      40.482  35.725  10.444  1.00 10.59           C  
ANISOU 2431  CA  LYS B 249     1608   1469    948   -130   -273    327       C  
ATOM   2432  C   LYS B 249      41.186  36.939   9.848  1.00 10.65           C  
ANISOU 2432  C   LYS B 249     1562   1475   1011    -89   -297    246       C  
ATOM   2433  O   LYS B 249      41.063  38.055  10.357  1.00  9.96           O  
ANISOU 2433  O   LYS B 249     1466   1431    888    -61   -293    204       O  
ATOM   2434  CB  LYS B 249      41.446  34.949  11.340  1.00 10.18           C  
ANISOU 2434  CB  LYS B 249     1631   1379    858   -101   -340    359       C  
ATOM   2435  CG  LYS B 249      40.739  33.974  12.287  1.00 11.13           C  
ANISOU 2435  CG  LYS B 249     1821   1511    895   -141   -318    450       C  
ATOM   2436  CD  LYS B 249      41.737  33.208  13.156  1.00 11.84           C  
ANISOU 2436  CD  LYS B 249     1998   1556    946   -105   -397    485       C  
ATOM   2437  CE  LYS B 249      41.032  32.231  14.100  1.00 12.94           C  
ANISOU 2437  CE  LYS B 249     2217   1703    996   -153   -374    591       C  
ATOM   2438  NZ  LYS B 249      42.016  31.342  14.838  1.00 13.73           N  
ANISOU 2438  NZ  LYS B 249     2384   1742   1089   -106   -443    611       N  
ATOM   2439  N   SER B 250      41.936  36.705   8.776  1.00  9.47           N  
ANISOU 2439  N   SER B 250     1382   1272    943    -83   -323    229       N  
ATOM   2440  CA  SER B 250      42.660  37.778   8.096  1.00 10.01           C  
ANISOU 2440  CA  SER B 250     1392   1339   1071    -59   -340    172       C  
ATOM   2441  C   SER B 250      41.705  38.810   7.503  1.00 12.99           C  
ANISOU 2441  C   SER B 250     1729   1749   1460    -78   -291    143       C  
ATOM   2442  O   SER B 250      41.887  40.018   7.677  1.00 10.64           O  
ANISOU 2442  O   SER B 250     1412   1465   1166    -59   -306    101       O  
ATOM   2443  CB  SER B 250      43.556  37.201   6.990  1.00 11.89           C  
ANISOU 2443  CB  SER B 250     1603   1532   1384    -45   -356    170       C  
ATOM   2444  OG  SER B 250      44.613  36.446   7.561  1.00 14.62           O  
ANISOU 2444  OG  SER B 250     1974   1850   1730     -6   -413    187       O  
ATOM   2445  N   ILE B 251      40.700  38.327   6.781  1.00 10.52           N  
ANISOU 2445  N   ILE B 251     1404   1437   1155   -114   -244    166       N  
ATOM   2446  CA  ILE B 251      39.672  39.203   6.233  1.00  9.78           C  
ANISOU 2446  CA  ILE B 251     1268   1378   1070   -127   -202    146       C  
ATOM   2447  C   ILE B 251      38.988  40.026   7.338  1.00 11.31           C  
ANISOU 2447  C   ILE B 251     1467   1631   1198   -102   -180    131       C  
ATOM   2448  O   ILE B 251      38.900  41.252   7.242  1.00 11.53           O  
ANISOU 2448  O   ILE B 251     1477   1670   1234    -72   -184     83       O  
ATOM   2449  CB  ILE B 251      38.616  38.397   5.463  1.00 11.21           C  
ANISOU 2449  CB  ILE B 251     1437   1557   1266   -176   -170    181       C  
ATOM   2450  CG1 ILE B 251      39.267  37.680   4.273  1.00 12.45           C  
ANISOU 2450  CG1 ILE B 251     1606   1651   1475   -182   -195    179       C  
ATOM   2451  CG2 ILE B 251      37.446  39.298   5.049  1.00 12.51           C  
ANISOU 2451  CG2 ILE B 251     1549   1770   1436   -181   -133    165       C  
ATOM   2452  CD1 ILE B 251      39.922  38.596   3.281  1.00 12.96           C  
ANISOU 2452  CD1 ILE B 251     1636   1706   1582   -154   -199    137       C  
ATOM   2453  N   ILE B 252      38.523  39.357   8.387  1.00  9.14           N  
ANISOU 2453  N   ILE B 252     1225   1394    853   -110   -158    172       N  
ATOM   2454  CA  ILE B 252      37.828  40.051   9.472  1.00  9.00           C  
ANISOU 2454  CA  ILE B 252     1218   1449    753    -72   -123    159       C  
ATOM   2455  C   ILE B 252      38.695  41.139  10.107  1.00 13.93           C  
ANISOU 2455  C   ILE B 252     1881   2059   1352    -10   -178     91       C  
ATOM   2456  O   ILE B 252      38.223  42.246  10.374  1.00 13.62           O  
ANISOU 2456  O   ILE B 252     1840   2050   1284     37   -166     40       O  
ATOM   2457  CB  ILE B 252      37.371  39.065  10.573  1.00  9.52           C  
ANISOU 2457  CB  ILE B 252     1323   1562    733    -92    -87    228       C  
ATOM   2458  CG1 ILE B 252      36.223  38.189  10.061  1.00 13.10           C  
ANISOU 2458  CG1 ILE B 252     1728   2039   1210   -164    -31    299       C  
ATOM   2459  CG2 ILE B 252      36.910  39.808  11.822  1.00 16.50           C  
ANISOU 2459  CG2 ILE B 252     2235   2528   1507    -30    -51    207       C  
ATOM   2460  CD1 ILE B 252      35.858  37.024  11.005  1.00 17.46           C  
ANISOU 2460  CD1 ILE B 252     2320   2619   1694   -211     -3    393       C  
ATOM   2461  N   THR B 253      39.964  40.828  10.332  1.00  9.81           N  
ANISOU 2461  N   THR B 253     1393   1486    847     -8   -248     89       N  
ATOM   2462  CA  THR B 253      40.895  41.797  10.903  1.00  9.45           C  
ANISOU 2462  CA  THR B 253     1380   1418    794     33   -323     30       C  
ATOM   2463  C   THR B 253      40.983  43.050  10.030  1.00 10.26           C  
ANISOU 2463  C   THR B 253     1442   1488    970     37   -342    -23       C  
ATOM   2464  O   THR B 253      40.913  44.175  10.519  1.00 11.47           O  
ANISOU 2464  O   THR B 253     1626   1637   1095     76   -373    -81       O  
ATOM   2465  CB  THR B 253      42.300  41.188  11.080  1.00  9.19           C  
ANISOU 2465  CB  THR B 253     1362   1338    793     27   -403     45       C  
ATOM   2466  OG1 THR B 253      42.210  40.041  11.934  1.00 12.35           O  
ANISOU 2466  OG1 THR B 253     1815   1756   1120     28   -396    100       O  
ATOM   2467  CG2 THR B 253      43.253  42.224  11.715  1.00  9.53           C  
ANISOU 2467  CG2 THR B 253     1429   1355    835     57   -499    -13       C  
ATOM   2468  N   TYR B 254      41.121  42.855   8.729  1.00  8.73           N  
ANISOU 2468  N   TYR B 254     1189   1264    863     -2   -325     -4       N  
ATOM   2469  CA  TYR B 254      41.267  43.994   7.838  1.00 13.01           C  
ANISOU 2469  CA  TYR B 254     1697   1771   1473     -7   -343    -38       C  
ATOM   2470  C   TYR B 254      39.950  44.765   7.669  1.00  8.59           C  
ANISOU 2470  C   TYR B 254     1133   1240    889     19   -296    -63       C  
ATOM   2471  O   TYR B 254      39.949  45.995   7.642  1.00 10.70           O  
ANISOU 2471  O   TYR B 254     1416   1478   1171     45   -331   -110       O  
ATOM   2472  CB  TYR B 254      41.802  43.540   6.479  1.00  9.00           C  
ANISOU 2472  CB  TYR B 254     1135   1236   1048    -47   -331     -5       C  
ATOM   2473  CG  TYR B 254      42.129  44.710   5.594  1.00  8.88           C  
ANISOU 2473  CG  TYR B 254     1090   1184   1099    -61   -352    -24       C  
ATOM   2474  CD1 TYR B 254      43.237  45.506   5.852  1.00 11.36           C  
ANISOU 2474  CD1 TYR B 254     1401   1462   1455    -70   -424    -40       C  
ATOM   2475  CD2 TYR B 254      41.315  45.042   4.522  1.00 12.20           C  
ANISOU 2475  CD2 TYR B 254     1489   1606   1541    -70   -310    -18       C  
ATOM   2476  CE1 TYR B 254      43.538  46.596   5.037  1.00  9.37           C  
ANISOU 2476  CE1 TYR B 254     1125   1169   1268    -97   -446    -42       C  
ATOM   2477  CE2 TYR B 254      41.597  46.136   3.712  1.00 11.93           C  
ANISOU 2477  CE2 TYR B 254     1439   1533   1561    -84   -332    -24       C  
ATOM   2478  CZ  TYR B 254      42.705  46.902   3.976  1.00 12.84           C  
ANISOU 2478  CZ  TYR B 254     1552   1607   1719   -102   -396    -32       C  
ATOM   2479  OH  TYR B 254      42.998  47.976   3.179  1.00 10.07           O  
ANISOU 2479  OH  TYR B 254     1189   1213   1426   -130   -420    -22       O  
ATOM   2480  N   VAL B 255      38.835  44.055   7.571  1.00  9.27           N  
ANISOU 2480  N   VAL B 255     1199   1380    945     13   -225    -30       N  
ATOM   2481  CA  VAL B 255      37.538  44.719   7.405  1.00 11.83           C  
ANISOU 2481  CA  VAL B 255     1498   1746   1252     45   -179    -49       C  
ATOM   2482  C   VAL B 255      37.225  45.553   8.651  1.00 13.39           C  
ANISOU 2482  C   VAL B 255     1744   1975   1366    121   -184   -101       C  
ATOM   2483  O   VAL B 255      36.744  46.689   8.551  1.00 14.41           O  
ANISOU 2483  O   VAL B 255     1880   2098   1498    176   -192   -152       O  
ATOM   2484  CB  VAL B 255      36.414  43.708   7.123  1.00 10.61           C  
ANISOU 2484  CB  VAL B 255     1294   1652   1087     11   -109      7       C  
ATOM   2485  CG1 VAL B 255      35.042  44.390   7.115  1.00 11.71           C  
ANISOU 2485  CG1 VAL B 255     1388   1855   1207     55    -60     -8       C  
ATOM   2486  CG2 VAL B 255      36.659  43.045   5.766  1.00 11.84           C  
ANISOU 2486  CG2 VAL B 255     1419   1761   1317    -50   -119     40       C  
ATOM   2487  N  ASER B 256      37.501  44.985   9.822  0.61 10.13           N  
ANISOU 2487  N  ASER B 256     1380   1596    875    134   -183    -91       N  
ATOM   2488  N  BSER B 256      37.525  45.012   9.829  0.39 10.62           N  
ANISOU 2488  N  BSER B 256     1442   1655    937    135   -185    -92       N  
ATOM   2489  CA ASER B 256      37.367  45.722  11.066  0.61 11.80           C  
ANISOU 2489  CA ASER B 256     1660   1836    989    216   -195   -147       C  
ATOM   2490  CA BSER B 256      37.315  45.763  11.062  0.39 11.72           C  
ANISOU 2490  CA BSER B 256     1648   1827    977    218   -193   -149       C  
ATOM   2491  C  ASER B 256      38.198  47.006  11.040  0.61 12.96           C  
ANISOU 2491  C  ASER B 256     1859   1895   1171    245   -296   -224       C  
ATOM   2492  C  BSER B 256      38.238  46.985  11.141  0.39 13.48           C  
ANISOU 2492  C  BSER B 256     1930   1962   1230    248   -299   -225       C  
ATOM   2493  O  ASER B 256      37.751  48.053  11.504  0.61 13.78           O  
ANISOU 2493  O  ASER B 256     2010   1998   1229    324   -310   -293       O  
ATOM   2494  O  BSER B 256      37.930  47.954  11.834  0.39 15.40           O  
ANISOU 2494  O  BSER B 256     2234   2206   1410    329   -320   -295       O  
ATOM   2495  CB ASER B 256      37.786  44.847  12.250  0.61 11.10           C  
ANISOU 2495  CB ASER B 256     1628   1781    807    215   -198   -116       C  
ATOM   2496  CB BSER B 256      37.522  44.865  12.285  0.39 11.35           C  
ANISOU 2496  CB BSER B 256     1655   1830    828    223   -179   -115       C  
ATOM   2497  OG ASER B 256      37.827  45.607  13.437  0.61 13.17           O  
ANISOU 2497  OG ASER B 256     1977   2062    964    300   -227   -181       O  
ATOM   2498  OG BSER B 256      38.805  44.271  12.274  0.39 14.20           O  
ANISOU 2498  OG BSER B 256     2039   2128   1228    174   -254    -93       O  
ATOM   2499  N  ASER B 257      39.405  46.923  10.490  0.61 14.17           N  
ANISOU 2499  N  ASER B 257     2003   1973   1410    183   -368   -211       N  
ATOM   2500  N  BSER B 257      39.365  46.944  10.436  0.39 13.98           N  
ANISOU 2500  N  BSER B 257     1976   1949   1389    183   -366   -211       N  
ATOM   2501  CA ASER B 257      40.273  48.094  10.401  0.61 12.84           C  
ANISOU 2501  CA ASER B 257     1870   1715   1294    184   -472   -265       C  
ATOM   2502  CA BSER B 257      40.259  48.100  10.409  0.39 12.85           C  
ANISOU 2502  CA BSER B 257     1872   1717   1294    185   -472   -266       C  
ATOM   2503  C  ASER B 257      39.697  49.157   9.469  0.61 12.36           C  
ANISOU 2503  C  ASER B 257     1791   1614   1293    196   -469   -290       C  
ATOM   2504  C  BSER B 257      39.723  49.160   9.451  0.39 12.68           C  
ANISOU 2504  C  BSER B 257     1831   1653   1336    194   -471   -290       C  
ATOM   2505  O  ASER B 257      39.876  50.351   9.698  0.61 15.71           O  
ANISOU 2505  O  ASER B 257     2274   1971   1725    230   -545   -352       O  
ATOM   2506  O  BSER B 257      39.957  50.353   9.642  0.39 15.18           O  
ANISOU 2506  O  BSER B 257     2205   1899   1665    224   -549   -349       O  
ATOM   2507  CB ASER B 257      41.674  47.689   9.932  0.61 11.90           C  
ANISOU 2507  CB ASER B 257     1713   1545   1262    107   -535   -227       C  
ATOM   2508  CB BSER B 257      41.682  47.697  10.009  0.39 12.31           C  
ANISOU 2508  CB BSER B 257     1770   1598   1309    110   -537   -229       C  
ATOM   2509  OG ASER B 257      42.236  46.721  10.800  0.61 14.47           O  
ANISOU 2509  OG ASER B 257     2061   1900   1536    106   -552   -204       O  
ATOM   2510  OG BSER B 257      41.789  47.476   8.615  0.39 11.09           O  
ANISOU 2510  OG BSER B 257     1536   1427   1249     53   -501   -181       O  
ATOM   2511  N   LEU B 258      39.013  48.723   8.416  1.00 12.04           N  
ANISOU 2511  N   LEU B 258     1676   1603   1294    169   -395   -243       N  
ATOM   2512  CA  LEU B 258      38.325  49.664   7.524  1.00 13.96           C  
ANISOU 2512  CA  LEU B 258     1904   1816   1583    190   -390   -260       C  
ATOM   2513  C   LEU B 258      37.221  50.376   8.308  1.00 16.60           C  
ANISOU 2513  C   LEU B 258     2279   2187   1839    298   -369   -323       C  
ATOM   2514  O   LEU B 258      37.110  51.603   8.273  1.00 16.14           O  
ANISOU 2514  O   LEU B 258     2273   2064   1796    350   -426   -380       O  
ATOM   2515  CB  LEU B 258      37.738  48.950   6.309  1.00 14.62           C  
ANISOU 2515  CB  LEU B 258     1907   1935   1713    145   -321   -199       C  
ATOM   2516  CG  LEU B 258      38.722  48.500   5.234  1.00 17.98           C  
ANISOU 2516  CG  LEU B 258     2297   2319   2217     61   -337   -147       C  
ATOM   2517  CD1 LEU B 258      37.974  47.786   4.135  1.00 17.51           C  
ANISOU 2517  CD1 LEU B 258     2180   2295   2176     35   -276   -102       C  
ATOM   2518  CD2 LEU B 258      39.502  49.678   4.666  1.00 15.87           C  
ANISOU 2518  CD2 LEU B 258     2050   1962   2017     39   -409   -158       C  
ATOM   2519  N   TYR B 259      36.413  49.593   9.017  1.00 14.43           N  
ANISOU 2519  N   TYR B 259     1984   2019   1481    334   -285   -308       N  
ATOM   2520  CA  TYR B 259      35.379  50.135   9.892  1.00 18.55           C  
ANISOU 2520  CA  TYR B 259     2533   2605   1909    450   -243   -363       C  
ATOM   2521  C   TYR B 259      35.942  51.178  10.860  1.00 20.78           C  
ANISOU 2521  C   TYR B 259     2937   2822   2135    525   -332   -455       C  
ATOM   2522  O   TYR B 259      35.349  52.244  11.057  1.00 21.89           O  
ANISOU 2522  O   TYR B 259     3124   2945   2249    628   -349   -528       O  
ATOM   2523  CB  TYR B 259      34.712  48.998  10.660  1.00 17.66           C  
ANISOU 2523  CB  TYR B 259     2382   2620   1707    454   -141   -314       C  
ATOM   2524  CG  TYR B 259      33.806  49.433  11.793  1.00 18.80           C  
ANISOU 2524  CG  TYR B 259     2558   2857   1727    580    -82   -364       C  
ATOM   2525  CD1 TYR B 259      32.453  49.690  11.573  1.00 22.18           C  
ANISOU 2525  CD1 TYR B 259     2907   3375   2145    649      2   -363       C  
ATOM   2526  CD2 TYR B 259      34.294  49.550  13.086  1.00 21.27           C  
ANISOU 2526  CD2 TYR B 259     2976   3179   1927    636   -109   -409       C  
ATOM   2527  CE1 TYR B 259      31.619  50.074  12.625  1.00 28.20           C  
ANISOU 2527  CE1 TYR B 259     3689   4241   2786    781     72   -407       C  
ATOM   2528  CE2 TYR B 259      33.478  49.934  14.132  1.00 25.66           C  
ANISOU 2528  CE2 TYR B 259     3571   3830   2350    766    -45   -458       C  
ATOM   2529  CZ  TYR B 259      32.142  50.192  13.899  1.00 30.42           C  
ANISOU 2529  CZ  TYR B 259     4087   4530   2943    841     53   -456       C  
ATOM   2530  OH  TYR B 259      31.343  50.569  14.961  1.00 37.70           O  
ANISOU 2530  OH  TYR B 259     5027   5539   3759    958    121   -485       O  
ATOM   2531  N   ASP B 260      37.095  50.876  11.455  1.00 14.53           N  
ANISOU 2531  N   ASP B 260     2201   1990   1329    479   -400   -456       N  
ATOM   2532  CA  ASP B 260      37.716  51.786  12.425  1.00 14.61           C  
ANISOU 2532  CA  ASP B 260     2335   1931   1285    538   -507   -545       C  
ATOM   2533  C   ASP B 260      38.077  53.140  11.821  1.00 17.95           C  
ANISOU 2533  C   ASP B 260     2805   2219   1796    540   -615   -599       C  
ATOM   2534  O   ASP B 260      38.103  54.160  12.522  1.00 18.52           O  
ANISOU 2534  O   ASP B 260     2967   2229   1842    610   -676   -664       O  
ATOM   2535  CB  ASP B 260      38.985  51.159  13.020  1.00 17.90           C  
ANISOU 2535  CB  ASP B 260     2785   2323   1692    470   -579   -524       C  
ATOM   2536  CG  ASP B 260      38.695  50.176  14.127  1.00 25.57           C  
ANISOU 2536  CG  ASP B 260     3780   3404   2531    507   -511   -502       C  
ATOM   2537  OD1 ASP B 260      37.541  50.115  14.596  1.00 28.16           O  
ANISOU 2537  OD1 ASP B 260     4109   3830   2760    592   -410   -512       O  
ATOM   2538  OD2 ASP B 260      39.637  49.460  14.531  1.00 29.01           O  
ANISOU 2538  OD2 ASP B 260     4223   3829   2971    447   -553   -462       O  
ATOM   2539  N   ALA B 261      38.383  53.149  10.530  1.00 17.23           N  
ANISOU 2539  N   ALA B 261     2638   2076   1831    447   -622   -539       N  
ATOM   2540  CA  ALA B 261      38.791  54.375   9.863  1.00 18.15           C  
ANISOU 2540  CA  ALA B 261     2796   2060   2040    425   -724   -565       C  
ATOM   2541  C   ALA B 261      37.601  55.149   9.299  1.00 23.08           C  
ANISOU 2541  C   ALA B 261     3421   2677   2670    511   -689   -593       C  
ATOM   2542  O   ALA B 261      37.781  56.197   8.687  1.00 27.61           O  
ANISOU 2542  O   ALA B 261     4037   3135   3318    501   -771   -608       O  
ATOM   2543  CB  ALA B 261      39.777  54.066   8.758  1.00 20.76           C  
ANISOU 2543  CB  ALA B 261     3050   2346   2493    287   -746   -479       C  
ATOM   2544  N   MET B 262      36.390  54.645   9.509  1.00 23.22           N  
ANISOU 2544  N   MET B 262     3389   2818   2616    592   -574   -593       N  
ATOM   2545  CA  MET B 262      35.209  55.287   8.942  1.00 29.54           C  
ANISOU 2545  CA  MET B 262     4167   3630   3429    680   -538   -613       C  
ATOM   2546  C   MET B 262      34.193  55.700  10.001  1.00 42.75           C  
ANISOU 2546  C   MET B 262     5886   5373   4983    848   -494   -698       C  
ATOM   2547  O   MET B 262      33.204  55.005  10.222  1.00 46.46           O  
ANISOU 2547  O   MET B 262     6270   5988   5395    896   -373   -672       O  
ATOM   2548  CB  MET B 262      34.550  54.365   7.923  1.00 20.11           C  
ANISOU 2548  CB  MET B 262     2837   2526   2280    622   -437   -522       C  
ATOM   2549  CG  MET B 262      35.460  54.049   6.748  1.00 17.83           C  
ANISOU 2549  CG  MET B 262     2509   2171   2095    481   -472   -446       C  
ATOM   2550  SD  MET B 262      34.757  52.890   5.557  1.00 25.93           S  
ANISOU 2550  SD  MET B 262     3402   3290   3159    414   -373   -352       S  
ATOM   2551  CE  MET B 262      36.121  52.735   4.421  1.00 21.99           C  
ANISOU 2551  CE  MET B 262     2899   2701   2754    278   -425   -286       C  
ATOM   2552  N   PRO B 263      34.428  56.856  10.636  1.00 52.18           N  
ANISOU 2552  N   PRO B 263     7200   6472   6155    923   -589   -775       N  
ATOM   2553  CA  PRO B 263      33.540  57.405  11.667  1.00 58.35           C  
ANISOU 2553  CA  PRO B 263     8017   7316   6837   1068   -550   -826       C  
ATOM   2554  C   PRO B 263      32.160  57.762  11.117  1.00 57.20           C  
ANISOU 2554  C   PRO B 263     7799   7236   6697   1171   -479   -831       C  
ATOM   2555  O   PRO B 263      31.158  57.360  11.709  1.00 59.57           O  
ANISOU 2555  O   PRO B 263     8035   7684   6914   1256   -365   -828       O  
ATOM   2556  CB  PRO B 263      34.281  58.661  12.127  1.00 63.69           C  
ANISOU 2556  CB  PRO B 263     8821   7842   7535   1078   -692   -871       C  
ATOM   2557  CG  PRO B 263      35.077  59.075  10.932  1.00 64.14           C  
ANISOU 2557  CG  PRO B 263     8880   7761   7728    958   -788   -832       C  
ATOM   2558  CD  PRO B 263      35.514  57.790  10.289  1.00 57.60           C  
ANISOU 2558  CD  PRO B 263     7961   6986   6936    842   -732   -772       C  
TER    2559      PRO B 263                                                      
HETATM 2560 CA    CA A 101      32.605  12.711  -3.800  1.00 23.18          CA  
HETATM 2561 CA    CA A 102      32.601   2.574   1.977  1.00 17.19          CA  
HETATM 2562 MG    MG B 301      53.727  26.859  32.114  1.00 11.52          MG  
HETATM 2563 CL    CL B 302      47.723  27.664  31.601  1.00 11.46          CL  
HETATM 2564  C1  EDO B 303      46.211  52.809  20.843  1.00 42.18           C  
HETATM 2565  O1  EDO B 303      44.959  52.737  21.543  1.00 44.15           O  
HETATM 2566  C2  EDO B 303      46.321  51.630  19.881  1.00 32.71           C  
HETATM 2567  O2  EDO B 303      47.457  51.793  19.017  1.00 25.39           O  
HETATM 2568  C1  EDO B 304      23.458  39.933   0.669  1.00 42.23           C  
HETATM 2569  O1  EDO B 304      22.615  39.254   1.607  1.00 48.73           O  
HETATM 2570  C2  EDO B 304      24.281  40.958   1.433  1.00 36.62           C  
HETATM 2571  O2  EDO B 304      25.193  41.629   0.551  1.00 24.68           O  
HETATM 2572  C1  EDO B 305      26.340  52.655   7.490  1.00 48.45           C  
HETATM 2573  O1  EDO B 305      26.155  51.491   8.309  1.00 43.54           O  
HETATM 2574  C2  EDO B 305      25.547  52.496   6.197  1.00 49.08           C  
HETATM 2575  O2  EDO B 305      25.765  53.638   5.361  1.00 47.41           O  
HETATM 2576  C1  GOL B 306      46.575  20.861  25.043  1.00 45.29           C  
HETATM 2577  O1  GOL B 306      45.540  19.892  24.992  1.00 51.78           O  
HETATM 2578  C2  GOL B 306      47.219  20.763  26.414  1.00 37.93           C  
HETATM 2579  O2  GOL B 306      47.757  21.985  26.913  1.00 16.09           O  
HETATM 2580  C3  GOL B 306      46.132  20.198  27.304  1.00 38.46           C  
HETATM 2581  O3  GOL B 306      44.938  20.905  27.039  1.00 39.36           O  
HETATM 2582  O   HOH A 201      44.918   3.238   2.789  1.00 10.37           O  
HETATM 2583  O   HOH A 202      42.505   8.879 -10.966  1.00 10.26           O  
HETATM 2584  O   HOH A 203      37.539   3.275   7.868  1.00 19.03           O  
HETATM 2585  O   HOH A 204      32.039  11.181  -5.411  1.00 25.83           O  
HETATM 2586  O   HOH A 205      48.010   9.608 -10.820  1.00 21.95           O  
HETATM 2587  O   HOH A 206      29.643  10.810   4.094  1.00 22.06           O  
HETATM 2588  O   HOH A 207      44.786  17.506  -9.536  1.00 20.45           O  
HETATM 2589  O   HOH A 208      36.665  -1.930  -1.137  1.00 23.56           O  
HETATM 2590  O   HOH A 209      31.224  20.407  -6.244  1.00 24.09           O  
HETATM 2591  O   HOH A 210      42.916  18.779  -5.464  1.00 24.15           O  
HETATM 2592  O   HOH A 211      36.173   4.726  -6.051  1.00 26.41           O  
HETATM 2593  O   HOH A 212      36.486   6.976  -9.408  1.00 23.14           O  
HETATM 2594  O   HOH A 213      29.614   3.641   6.885  1.00 31.96           O  
HETATM 2595  O   HOH A 214      48.527   2.004  -2.666  1.00 26.87           O  
HETATM 2596  O   HOH A 215      31.290   1.643   6.763  1.00 24.56           O  
HETATM 2597  O   HOH A 216      32.861   6.718  12.234  1.00 28.02           O  
HETATM 2598  O   HOH A 217      47.095   1.606   2.595  1.00 18.68           O  
HETATM 2599  O   HOH A 218      49.373  -0.371  -3.356  1.00 29.44           O  
HETATM 2600  O   HOH A 219      30.633  -0.647   7.981  1.00 32.74           O  
HETATM 2601  O   HOH A 220      40.563   6.489 -10.511  1.00 28.17           O  
HETATM 2602  O   HOH A 221      30.392   5.697   0.614  1.00 27.47           O  
HETATM 2603  O   HOH A 222      26.682   1.988  -1.437  1.00 36.77           O  
HETATM 2604  O   HOH A 223      33.541   3.280  10.030  1.00 42.61           O  
HETATM 2605  O   HOH A 224      47.462   0.562 -12.206  1.00 33.57           O  
HETATM 2606  O   HOH A 225      29.555   5.200  -3.339  1.00 43.71           O  
HETATM 2607  O   HOH A 226      39.971   2.165   9.042  1.00 31.09           O  
HETATM 2608  O   HOH A 227      29.437  11.035  -7.963  1.00 36.23           O  
HETATM 2609  O   HOH A 228      29.342  13.829   5.262  1.00 47.04           O  
HETATM 2610  O   HOH A 229      27.318   8.886   4.436  1.00 42.80           O  
HETATM 2611  O   HOH A 230      34.718  -4.204   7.390  1.00 38.02           O  
HETATM 2612  O   HOH A 231      38.137  10.290  14.429  1.00 40.64           O  
HETATM 2613  O   HOH A 232      44.726  19.747  -1.237  1.00 37.52           O  
HETATM 2614  O   HOH A 233      32.168  17.066   1.478  1.00 43.46           O  
HETATM 2615  O   HOH A 234      34.193   8.938 -10.147  1.00 40.08           O  
HETATM 2616  O   HOH A 235      42.121   4.507  13.487  1.00 42.90           O  
HETATM 2617  O   HOH A 236      42.700  19.457  -7.990  1.00 20.73           O  
HETATM 2618  O   HOH A 237      51.834   7.922  -5.355  1.00 55.88           O  
HETATM 2619  O   HOH A 238      40.154  19.482  -8.811  1.00 18.53           O  
HETATM 2620  O   HOH A 239      30.639   3.837   2.619  1.00 21.25           O  
HETATM 2621  O   HOH A 240      36.269   1.717  -5.975  1.00 34.23           O  
HETATM 2622  O   HOH A 241      45.922  -2.862   2.611  1.00 36.72           O  
HETATM 2623  O   HOH A 242      43.861   6.232 -12.139  1.00 31.31           O  
HETATM 2624  O   HOH A 243      35.546   1.994   9.382  1.00 45.38           O  
HETATM 2625  O   HOH A 244      45.597  -0.247 -12.843  1.00 37.04           O  
HETATM 2626  O   HOH A 245      44.235  -2.607  -6.386  1.00 44.11           O  
HETATM 2627  O   HOH A 246      50.628   4.096  -2.313  1.00 44.57           O  
HETATM 2628  O   HOH A 247      42.430  19.647  -2.373  1.00 52.03           O  
HETATM 2629  O   HOH A 248      27.492   1.158  -3.693  1.00 38.50           O  
HETATM 2630  O   HOH A 249      44.475  11.761  12.753  1.00 47.24           O  
HETATM 2631  O   HOH A 250      26.170   4.492   2.056  1.00 47.71           O  
HETATM 2632  O   HOH A 251      27.983   6.032   0.910  1.00 43.36           O  
HETATM 2633  O   HOH A 252      43.671   2.922  12.036  1.00 40.70           O  
HETATM 2634  O   HOH A 253      27.241   6.046   3.348  1.00 50.02           O  
HETATM 2635  O   HOH A 254      35.895  23.108   4.045  1.00 54.21           O  
HETATM 2636  O   HOH A 255      33.544  19.191  -0.531  1.00 47.58           O  
HETATM 2637  O   HOH A 256      34.692  11.522  -8.917  1.00 26.34           O  
HETATM 2638  O   HOH A 257      53.204   5.794  -7.907  1.00 48.47           O  
HETATM 2639  O   HOH A 258      34.685  20.079  17.937  1.00 50.51           O  
HETATM 2640  O   HOH B 401      50.407  29.236  31.305  1.00  9.19           O  
HETATM 2641  O   HOH B 402      42.206  29.628  12.261  1.00 14.07           O  
HETATM 2642  O   HOH B 403      43.556  38.171 -10.399  1.00 11.74           O  
HETATM 2643  O   HOH B 404      51.898  29.685  34.643  1.00 10.08           O  
HETATM 2644  O   HOH B 405      33.438  57.795  -7.764  1.00 23.31           O  
HETATM 2645  O   HOH B 406      36.635  42.524  -1.841  1.00  8.53           O  
HETATM 2646  O   HOH B 407      47.476  30.927  31.702  1.00  9.57           O  
HETATM 2647  O   HOH B 408      55.751  32.686  20.472  1.00 12.10           O  
HETATM 2648  O   HOH B 409      43.449  26.836  28.890  1.00 22.50           O  
HETATM 2649  O   HOH B 410      59.147  39.537  23.178  1.00 11.64           O  
HETATM 2650  O   HOH B 411      57.510  34.385  19.213  1.00  8.92           O  
HETATM 2651  O   HOH B 412      45.356  49.091   3.421  1.00 10.26           O  
HETATM 2652  O   HOH B 413      51.605  24.627  15.282  1.00 11.48           O  
HETATM 2653  O   HOH B 414      44.944  31.602  -6.466  1.00 24.22           O  
HETATM 2654  O   HOH B 415      47.983   0.983  -0.178  1.00 14.67           O  
HETATM 2655  O   HOH B 416      34.652  37.707  -4.488  1.00 11.37           O  
HETATM 2656  O   HOH B 417      56.425  37.258  11.340  1.00 11.29           O  
HETATM 2657  O   HOH B 418      40.605  32.013   9.493  1.00 11.32           O  
HETATM 2658  O   HOH B 419      45.602  44.948   3.029  1.00 13.95           O  
HETATM 2659  O   HOH B 420      45.778  29.529  15.584  1.00 12.30           O  
HETATM 2660  O   HOH B 421      37.702  41.566 -10.266  1.00 13.28           O  
HETATM 2661  O   HOH B 422      49.347  40.622  34.674  1.00 16.78           O  
HETATM 2662  O   HOH B 423      42.318  49.238  30.984  1.00 23.92           O  
HETATM 2663  O   HOH B 424      34.789  41.083  -3.222  1.00 10.59           O  
HETATM 2664  O   HOH B 425      44.710  31.998  14.782  1.00 13.42           O  
HETATM 2665  O   HOH B 426      39.049  30.676   6.642  1.00 20.56           O  
HETATM 2666  O   HOH B 427      56.528  38.781  23.829  1.00 10.10           O  
HETATM 2667  O   HOH B 428      50.661  22.935  23.714  1.00 12.73           O  
HETATM 2668  O   HOH B 429      57.935  35.085   8.763  1.00 24.99           O  
HETATM 2669  O   HOH B 430      47.769  46.358  -9.447  1.00 27.81           O  
HETATM 2670  O   HOH B 431      44.647  37.565  36.415  1.00 26.79           O  
HETATM 2671  O   HOH B 432      32.966  55.576  -9.469  1.00 13.03           O  
HETATM 2672  O   HOH B 433      50.677  11.101  -0.229  1.00 21.59           O  
HETATM 2673  O   HOH B 434      45.001   4.543   5.383  1.00 16.07           O  
HETATM 2674  O   HOH B 435      55.083  44.487   9.669  1.00 22.08           O  
HETATM 2675  O   HOH B 436      54.169  33.803   6.737  1.00 17.13           O  
HETATM 2676  O   HOH B 437      32.600  33.882   7.217  1.00 14.47           O  
HETATM 2677  O   HOH B 438      30.786  33.514  -2.252  1.00 23.76           O  
HETATM 2678  O   HOH B 439      46.420  31.424  29.290  1.00 13.94           O  
HETATM 2679  O   HOH B 440      52.327  47.036   9.932  1.00 18.99           O  
HETATM 2680  O   HOH B 441      42.257  28.748  -1.123  1.00 18.96           O  
HETATM 2681  O   HOH B 442      29.217  35.913  -1.875  1.00 15.14           O  
HETATM 2682  O   HOH B 443      46.188  29.295  12.689  1.00 23.15           O  
HETATM 2683  O   HOH B 444      46.328  34.759  -5.844  1.00 16.48           O  
HETATM 2684  O   HOH B 445      48.173  23.639  24.857  1.00 15.18           O  
HETATM 2685  O   HOH B 446      27.654  50.323  -8.857  1.00 23.92           O  
HETATM 2686  O   HOH B 447      43.335  61.478  -2.649  1.00 23.20           O  
HETATM 2687  O   HOH B 448      59.740  43.196   9.459  1.00 19.46           O  
HETATM 2688  O   HOH B 449      42.263  49.877  13.298  1.00 28.15           O  
HETATM 2689  O   HOH B 450      34.809  61.487  -1.785  1.00 21.93           O  
HETATM 2690  O   HOH B 451      63.928  29.587  26.351  1.00 25.25           O  
HETATM 2691  O   HOH B 452      54.005  36.027  36.002  1.00 19.50           O  
HETATM 2692  O   HOH B 453      46.237  20.789   0.653  1.00 23.81           O  
HETATM 2693  O   HOH B 454      45.910  40.897 -12.877  1.00 23.36           O  
HETATM 2694  O   HOH B 455      42.412  57.341  -5.115  1.00 24.64           O  
HETATM 2695  O   HOH B 456      58.364  28.019  16.027  1.00 20.05           O  
HETATM 2696  O   HOH B 457      39.885  53.259  -8.671  1.00 26.23           O  
HETATM 2697  O   HOH B 458      57.272  30.573   9.566  1.00 27.36           O  
HETATM 2698  O   HOH B 459      48.173  53.580  24.339  1.00 26.48           O  
HETATM 2699  O   HOH B 460      49.607  23.826  19.123  1.00 19.74           O  
HETATM 2700  O   HOH B 461      32.264  52.183 -18.940  1.00 20.57           O  
HETATM 2701  O   HOH B 462      30.096  34.697   8.266  1.00 28.36           O  
HETATM 2702  O   HOH B 463      25.105  39.442  10.463  1.00 23.12           O  
HETATM 2703  O   HOH B 464      50.526  22.127  21.017  1.00 19.78           O  
HETATM 2704  O   HOH B 465      56.150  30.712  34.918  1.00 19.41           O  
HETATM 2705  O   HOH B 466      42.414  31.882  19.561  1.00 24.80           O  
HETATM 2706  O   HOH B 467      50.794  52.057  28.535  1.00 23.35           O  
HETATM 2707  O   HOH B 468      58.348  24.527  29.188  1.00 22.21           O  
HETATM 2708  O   HOH B 469      42.114  51.243  11.040  1.00 23.14           O  
HETATM 2709  O   HOH B 470      24.343  44.037   0.869  1.00 23.17           O  
HETATM 2710  O   HOH B 471      45.484  32.062   1.111  1.00 28.52           O  
HETATM 2711  O   HOH B 472      21.886  42.908   5.383  1.00 32.92           O  
HETATM 2712  O   HOH B 473      56.654  48.188  14.500  1.00 18.84           O  
HETATM 2713  O   HOH B 474      51.137  24.403   2.373  1.00 29.74           O  
HETATM 2714  O   HOH B 475      58.210  41.213   9.567  1.00 29.32           O  
HETATM 2715  O   HOH B 476      39.051  37.731  22.540  1.00 21.63           O  
HETATM 2716  O   HOH B 477      65.488  29.079  33.633  1.00 25.79           O  
HETATM 2717  O   HOH B 478      51.876  12.387   4.771  1.00 26.73           O  
HETATM 2718  O   HOH B 479      49.963   7.996   0.453  1.00 26.66           O  
HETATM 2719  O   HOH B 480      61.968  31.183  24.835  1.00 27.88           O  
HETATM 2720  O   HOH B 481      44.639  50.314  10.457  1.00 23.19           O  
HETATM 2721  O   HOH B 482      36.807  54.980 -15.697  1.00 22.19           O  
HETATM 2722  O   HOH B 483      56.086  47.280  31.375  1.00 25.31           O  
HETATM 2723  O   HOH B 484      55.733  23.927  20.607  1.00 30.52           O  
HETATM 2724  O   HOH B 485      42.964  49.544  21.774  1.00 29.06           O  
HETATM 2725  O   HOH B 486      59.919  30.905  12.400  1.00 36.92           O  
HETATM 2726  O   HOH B 487      54.622  24.144  23.017  1.00 24.11           O  
HETATM 2727  O   HOH B 488      29.457  34.823  15.137  1.00 35.08           O  
HETATM 2728  O   HOH B 489      50.547  52.813  13.778  1.00 27.14           O  
HETATM 2729  O   HOH B 490      55.162  33.815   3.950  1.00 25.64           O  
HETATM 2730  O   HOH B 491      66.032  30.936  27.648  1.00 26.53           O  
HETATM 2731  O   HOH B 492      37.188  33.341  17.748  1.00 33.09           O  
HETATM 2732  O   HOH B 493      52.368  25.734  10.285  1.00 33.39           O  
HETATM 2733  O   HOH B 494      43.825  47.990  16.149  1.00 26.58           O  
HETATM 2734  O   HOH B 495      37.266  35.877  24.783  1.00 36.63           O  
HETATM 2735  O   HOH B 496      51.083  10.153  11.913  1.00 26.76           O  
HETATM 2736  O   HOH B 497      28.799  36.002  10.543  1.00 25.30           O  
HETATM 2737  O   HOH B 498      23.528  40.050   8.365  1.00 23.71           O  
HETATM 2738  O   HOH B 499      55.468  37.679  37.593  1.00 25.60           O  
HETATM 2739  O   HOH B 500      53.231  27.502   7.983  1.00 23.42           O  
HETATM 2740  O   HOH B 501      51.147  43.545  -0.315  1.00 30.84           O  
HETATM 2741  O   HOH B 502      52.774  14.742   5.304  1.00 40.12           O  
HETATM 2742  O   HOH B 503      67.864  29.817  30.781  1.00 32.09           O  
HETATM 2743  O   HOH B 504      32.188  60.212   4.324  1.00 31.58           O  
HETATM 2744  O   HOH B 505      19.875  44.486  -0.031  1.00 29.30           O  
HETATM 2745  O   HOH B 506      29.522  57.018  -2.459  1.00 26.27           O  
HETATM 2746  O   HOH B 507      57.761  56.261  17.937  1.00 33.23           O  
HETATM 2747  O   HOH B 508      46.768  23.474  19.993  1.00 31.47           O  
HETATM 2748  O   HOH B 509      28.854  59.093  -0.440  1.00 34.17           O  
HETATM 2749  O   HOH B 510      58.844  30.595  35.511  1.00 21.35           O  
HETATM 2750  O   HOH B 511      22.909  50.970   2.969  1.00 39.73           O  
HETATM 2751  O   HOH B 512      55.078  49.812  26.329  1.00 26.04           O  
HETATM 2752  O   HOH B 513      57.480  49.033  25.882  1.00 21.22           O  
HETATM 2753  O   HOH B 514      41.172  30.603  17.233  1.00 35.21           O  
HETATM 2754  O   HOH B 515      41.929  29.931   6.417  1.00 31.07           O  
HETATM 2755  O   HOH B 516      53.268   3.241   4.037  1.00 24.70           O  
HETATM 2756  O   HOH B 517      40.431  61.653  -5.894  1.00 29.32           O  
HETATM 2757  O   HOH B 518      35.629  30.913  -4.033  1.00 36.54           O  
HETATM 2758  O   HOH B 519      44.682  47.147  11.450  1.00 25.68           O  
HETATM 2759  O   HOH B 520      46.756  22.456  22.434  1.00 45.06           O  
HETATM 2760  O   HOH B 521      55.161  36.176  40.052  1.00 29.58           O  
HETATM 2761  O   HOH B 522      52.413  26.890   2.886  1.00 29.71           O  
HETATM 2762  O   HOH B 523      51.946  35.175  -0.445  1.00 30.74           O  
HETATM 2763  O   HOH B 524      34.312  56.217 -14.157  1.00 28.55           O  
HETATM 2764  O   HOH B 525      44.806   3.096   7.593  1.00 23.20           O  
HETATM 2765  O   HOH B 526      36.061  39.999  27.636  1.00 39.82           O  
HETATM 2766  O   HOH B 527      48.485  38.245   3.046  1.00 24.59           O  
HETATM 2767  O   HOH B 528      40.699  30.977  22.927  1.00 37.98           O  
HETATM 2768  O   HOH B 529      44.148  24.504  20.573  1.00 33.76           O  
HETATM 2769  O   HOH B 530      57.976  23.138  27.073  1.00 32.55           O  
HETATM 2770  O   HOH B 531      34.268  29.636   3.193  1.00 43.44           O  
HETATM 2771  O   HOH B 532      49.037  49.533   0.864  1.00 29.22           O  
HETATM 2772  O   HOH B 533      35.665  31.875  -6.151  1.00 27.22           O  
HETATM 2773  O   HOH B 534      53.857  20.741  24.313  1.00 30.59           O  
HETATM 2774  O   HOH B 535      42.395  49.005  18.585  1.00 43.32           O  
HETATM 2775  O   HOH B 536      29.007  31.587  -1.460  1.00 44.29           O  
HETATM 2776  O   HOH B 537      43.444  35.394   2.534  1.00 28.73           O  
HETATM 2777  O   HOH B 538      50.571  53.399  26.371  1.00 37.03           O  
HETATM 2778  O   HOH B 539      57.631  29.907  37.871  1.00 37.13           O  
HETATM 2779  O   HOH B 540      44.944  37.256   3.941  1.00 28.97           O  
HETATM 2780  O   HOH B 541      56.653  49.672  29.775  1.00 33.92           O  
HETATM 2781  O   HOH B 542      52.861   0.919   0.577  1.00 33.01           O  
HETATM 2782  O   HOH B 543      45.064  47.877   9.159  1.00 34.53           O  
HETATM 2783  O   HOH B 544      36.971  29.867   8.267  1.00 31.30           O  
HETATM 2784  O   HOH B 545      50.671  22.465  16.872  1.00 30.60           O  
HETATM 2785  O   HOH B 546      58.419  45.068   8.007  1.00 31.42           O  
HETATM 2786  O   HOH B 547      27.078  54.852  -2.585  1.00 50.39           O  
HETATM 2787  O   HOH B 548      43.630  28.736  16.722  1.00 40.33           O  
HETATM 2788  O   HOH B 549      23.976  42.869  -2.355  1.00 32.02           O  
HETATM 2789  O   HOH B 550      22.312  51.545  -7.160  1.00 38.92           O  
HETATM 2790  O   HOH B 551      36.452  48.151  15.969  1.00 36.38           O  
HETATM 2791  O   HOH B 552      38.361  30.193   3.908  1.00 30.88           O  
HETATM 2792  O   HOH B 553      27.875  34.200   6.791  1.00 28.07           O  
HETATM 2793  O   HOH B 554      50.183  40.448   4.394  1.00 31.58           O  
HETATM 2794  O   HOH B 555      51.841  44.671   3.443  1.00 33.95           O  
HETATM 2795  O   HOH B 556      42.622   2.996   9.382  1.00 29.95           O  
HETATM 2796  O   HOH B 557      51.699  55.071  14.324  1.00 30.19           O  
HETATM 2797  O   HOH B 558      30.129  58.121  -7.338  1.00 40.38           O  
HETATM 2798  O   HOH B 559      33.185  36.892  -6.939  1.00 25.46           O  
HETATM 2799  O   HOH B 560      34.648  34.093  -4.441  1.00 27.07           O  
HETATM 2800  O   HOH B 561      59.171  50.489  24.582  1.00 32.95           O  
HETATM 2801  O   HOH B 562      27.858  32.683  16.161  1.00 41.83           O  
HETATM 2802  O   HOH B 563      35.814  37.991  25.869  1.00 44.59           O  
HETATM 2803  O   HOH B 564      46.416  48.512 -10.572  1.00 41.05           O  
HETATM 2804  O   HOH B 565      38.872  35.032  23.157  1.00 29.82           O  
HETATM 2805  O   HOH B 566      56.197  36.751   3.720  1.00 42.75           O  
HETATM 2806  O   HOH B 567      40.543  48.948  21.973  1.00 40.26           O  
HETATM 2807  O   HOH B 568      61.708  54.128  23.339  1.00 32.75           O  
HETATM 2808  O   HOH B 569      46.696  40.001  36.516  1.00 40.70           O  
HETATM 2809  O   HOH B 570      47.405  17.583  10.108  1.00 42.00           O  
HETATM 2810  O   HOH B 571      23.830  36.601   2.831  1.00 43.66           O  
HETATM 2811  O   HOH B 572      42.220  54.429  11.548  1.00 45.79           O  
HETATM 2812  O   HOH B 573      40.134  28.055   4.005  1.00 37.23           O  
HETATM 2813  O   HOH B 574      54.336  56.911  20.342  1.00 40.23           O  
HETATM 2814  O   HOH B 575      54.609  50.620  31.849  1.00 36.84           O  
HETATM 2815  O   HOH B 576      62.731  29.369  22.630  1.00 54.92           O  
HETATM 2816  O   HOH B 577      49.239  55.810   5.811  1.00 40.09           O  
HETATM 2817  O   HOH B 578      25.239  34.801   4.858  1.00 42.25           O  
HETATM 2818  O   HOH B 579      50.884  39.685  36.973  1.00 19.39           O  
HETATM 2819  O   HOH B 580      55.400  31.318   7.489  1.00 21.19           O  
HETATM 2820  O   HOH B 581      50.951  20.594  24.976  1.00 14.86           O  
HETATM 2821  O   HOH B 582      48.691  43.249  35.287  1.00 14.81           O  
HETATM 2822  O   HOH B 583      34.875  34.493  -7.218  1.00 24.33           O  
HETATM 2823  O   HOH B 584      63.636  33.450  23.970  1.00 27.96           O  
HETATM 2824  O   HOH B 585      59.721  27.987  35.195  1.00 27.01           O  
HETATM 2825  O   HOH B 586      28.503  57.939  -4.840  1.00 28.25           O  
HETATM 2826  O   HOH B 587      31.592  38.105  -8.933  1.00 28.97           O  
HETATM 2827  O   HOH B 588      31.833  60.555  -7.394  1.00 40.63           O  
HETATM 2828  O   HOH B 589      55.689  39.249   4.655  1.00 38.56           O  
HETATM 2829  O   HOH B 590      30.575  61.733  -9.527  1.00 44.40           O  
HETATM 2830  O   HOH B 591      50.887  52.984   6.926  1.00 48.58           O  
HETATM 2831  O   HOH B 592      60.851  26.499  37.138  1.00 37.13           O  
HETATM 2832  O   HOH B 593      45.615  42.676  35.560  1.00 22.95           O  
HETATM 2833  O   HOH B 594      51.419  37.265  36.434  1.00 17.43           O  
HETATM 2834  O   HOH B 595      53.632  29.926   9.363  1.00 16.82           O  
HETATM 2835  O   HOH B 596      24.638  45.525  -3.132  1.00 27.85           O  
HETATM 2836  O   HOH B 597      35.363  58.446  -9.011  1.00 44.23           O  
HETATM 2837  O   HOH B 598      42.160  50.633  28.782  1.00 29.34           O  
HETATM 2838  O   HOH B 599      47.179  31.229  -0.161  1.00 36.94           O  
HETATM 2839  O   HOH B 600      56.813  32.095  39.144  1.00 62.44           O  
HETATM 2840  O   HOH B 601      51.640  26.966  32.018  1.00 10.31           O  
HETATM 2841  O   HOH B 602      53.730  27.781  33.995  1.00 13.42           O  
HETATM 2842  O   HOH B 603      61.319  36.919  22.204  1.00 12.66           O  
HETATM 2843  O   HOH B 604      55.778  26.844  32.381  1.00  9.40           O  
HETATM 2844  O   HOH B 605      35.122  40.527 -10.705  1.00 14.86           O  
HETATM 2845  O   HOH B 606      43.814  30.570  29.917  1.00 20.95           O  
HETATM 2846  O   HOH B 607      62.139  37.786  29.224  1.00 21.32           O  
HETATM 2847  O   HOH B 608      32.514  48.679 -16.213  1.00 24.05           O  
HETATM 2848  O   HOH B 609      48.306  35.005  -7.715  1.00 32.76           O  
HETATM 2849  O   HOH B 610      29.979  37.464  -4.041  1.00 27.19           O  
HETATM 2850  O   HOH B 611      32.043  40.600  -5.726  1.00 29.23           O  
HETATM 2851  O   HOH B 612      64.511  40.198  30.193  1.00 27.05           O  
HETATM 2852  O   HOH B 613      49.368  43.671  37.906  1.00 28.09           O  
HETATM 2853  O   HOH B 614      32.477  37.564  17.220  1.00 26.75           O  
HETATM 2854  O   HOH B 615      43.482  30.338  -7.994  1.00 33.66           O  
HETATM 2855  O   HOH B 616      56.705  43.666   6.136  1.00 31.16           O  
HETATM 2856  O   HOH B 617      58.684  21.016  27.193  1.00 36.29           O  
HETATM 2857  O   HOH B 618      62.920  41.198  23.629  1.00 31.18           O  
HETATM 2858  O   HOH B 619      62.480  39.639  21.443  1.00 35.99           O  
HETATM 2859  O   HOH B 620      59.007  25.479  38.331  1.00 28.78           O  
HETATM 2860  O   HOH B 621      63.774  38.001  19.148  1.00 31.06           O  
HETATM 2861  O   HOH B 622      52.020  54.097   4.833  1.00 31.32           O  
HETATM 2862  O   HOH B 623      62.390  42.006  37.579  1.00 26.00           O  
HETATM 2863  O   HOH B 624      40.775  60.809   2.509  1.00 34.08           O  
HETATM 2864  O   HOH B 625      35.919  33.655  13.365  1.00 34.78           O  
HETATM 2865  O   HOH B 626      45.511  27.803  28.964  1.00 27.04           O  
HETATM 2866  O   HOH B 627      55.815  42.182   8.436  1.00 30.62           O  
HETATM 2867  O   HOH B 628      46.901  55.677  29.818  1.00 31.61           O  
HETATM 2868  O   HOH B 629      67.111  36.992  27.578  1.00 36.96           O  
HETATM 2869  O   HOH B 630      65.423  37.422  24.691  1.00 45.61           O  
HETATM 2870  O   HOH B 631      61.090  36.593  39.390  1.00 37.58           O  
HETATM 2871  O   HOH B 632      63.857  37.371  14.929  1.00 35.70           O  
HETATM 2872  O   HOH B 633      56.536  19.153  27.174  1.00 24.80           O  
HETATM 2873  O   HOH B 634      54.856   5.259   4.472  1.00 36.15           O  
HETATM 2874  O   HOH B 635      61.942  38.647  31.675  1.00 38.29           O  
HETATM 2875  O   HOH B 636      30.990  38.836  20.071  1.00 33.65           O  
HETATM 2876  O   HOH B 637      46.614  51.801  10.412  1.00 41.40           O  
HETATM 2877  O   HOH B 638      21.053  40.418   9.409  1.00 41.03           O  
HETATM 2878  O   HOH B 639      31.191  39.535  -3.942  1.00 37.42           O  
HETATM 2879  O   HOH B 640      53.997  10.783   4.248  1.00 34.28           O  
HETATM 2880  O   HOH B 641      42.881  61.681   1.268  1.00 33.36           O  
HETATM 2881  O   HOH B 642      60.138  29.312  14.314  1.00 37.19           O  
HETATM 2882  O   HOH B 643      34.875  35.644  15.451  1.00 43.43           O  
HETATM 2883  O   HOH B 644      63.647  35.364  22.880  1.00 34.41           O  
HETATM 2884  O   HOH B 645      24.876  52.605  -3.243  1.00 38.05           O  
HETATM 2885  O   HOH B 646      44.194  27.533  13.150  1.00 48.40           O  
HETATM 2886  O   HOH B 647      39.956  29.722  10.989  1.00 44.96           O  
HETATM 2887  O   HOH B 648      48.193  52.948  12.907  1.00 46.48           O  
HETATM 2888  O   HOH B 649      40.751  32.542  32.744  1.00 32.40           O  
HETATM 2889  O   HOH B 650      42.992  60.144  -5.294  1.00 47.33           O  
HETATM 2890  O   HOH B 651      41.128  31.366  29.241  1.00 28.82           O  
HETATM 2891  O   HOH B 652      38.159  63.178   6.013  1.00 35.75           O  
HETATM 2892  O   HOH B 653      40.936  47.129  32.401  1.00 36.97           O  
HETATM 2893  O   HOH B 654      58.125  17.702  27.870  1.00 34.99           O  
HETATM 2894  O   HOH B 655      53.816  40.178  38.390  1.00 37.51           O  
HETATM 2895  O   HOH B 656      44.900  63.025   0.675  1.00 37.30           O  
HETATM 2896  O   HOH B 657      43.883  55.576  28.917  1.00 40.74           O  
HETATM 2897  O   HOH B 658      55.642  29.506   6.032  1.00 41.20           O  
HETATM 2898  O   HOH B 659      49.491  58.864   2.828  1.00 37.21           O  
HETATM 2899  O   HOH B 660      51.399   9.476  14.805  1.00 41.94           O  
HETATM 2900  O   HOH B 661      38.047  49.902  18.203  1.00 45.04           O  
HETATM 2901  O   HOH B 662      64.415  37.440  12.573  1.00 47.21           O  
HETATM 2902  O   HOH B 663      61.921  49.863  22.896  1.00 41.28           O  
HETATM 2903  O   HOH B 664      28.773  34.040  12.376  1.00 34.71           O  
HETATM 2904  O   HOH B 665      54.120  21.774  21.509  1.00 49.59           O  
HETATM 2905  O   HOH B 666      43.606  30.896   2.817  1.00 43.15           O  
HETATM 2906  O   HOH B 667      62.721  39.204  36.906  1.00 25.45           O  
HETATM 2907  O   HOH B 668      63.178  44.925  30.457  1.00 43.22           O  
HETATM 2908  O   HOH B 669      40.250  50.960  -7.313  1.00 15.35           O  
HETATM 2909  O   HOH B 670      44.997  29.133  -1.058  1.00 37.53           O  
HETATM 2910  O   HOH B 671      44.850  27.220   3.777  1.00 32.54           O  
HETATM 2911  O   HOH B 672      48.666  43.770  -9.089  1.00 46.22           O  
HETATM 2912  O   HOH B 673      47.698  50.174  -6.535  1.00 38.96           O  
HETATM 2913  O   HOH B 674      45.766  52.942  -6.307  1.00 38.69           O  
HETATM 2914  O   HOH B 675      25.921  36.204   9.659  1.00 37.15           O  
HETATM 2915  O   HOH B 676      29.908  44.034  19.887  1.00 42.93           O  
HETATM 2916  O   HOH B 677      36.209  51.273  19.678  1.00 55.04           O  
HETATM 2917  O   HOH B 678      23.082  44.793  -0.799  1.00 47.99           O  
HETATM 2918  O   HOH B 679      52.781  37.290  -1.585  1.00 45.08           O  
HETATM 2919  O   HOH B 680      63.610  34.315  12.975  1.00 39.02           O  
HETATM 2920  O   HOH B 681      50.631  40.215  -3.815  1.00 29.34           O  
HETATM 2921  O   HOH B 682      48.308  40.558  38.462  1.00 36.19           O  
HETATM 2922  O   HOH B 683      28.626  39.708  -9.801  1.00 36.90           O  
HETATM 2923  O   HOH B 684      55.226  56.701  17.329  1.00 39.43           O  
HETATM 2924  O   HOH B 685      62.684  43.619  24.475  1.00 43.55           O  
HETATM 2925  O   HOH B 686      61.972  26.601  23.634  1.00 34.85           O  
HETATM 2926  O   HOH B 687      61.312  25.004  31.144  1.00 39.75           O  
HETATM 2927  O   HOH B 688      36.629  51.373  16.938  1.00 45.52           O  
HETATM 2928  O   HOH B 689      54.493  35.918   1.515  1.00 42.08           O  
HETATM 2929  O   HOH B 690      44.104  28.014  19.180  1.00 67.45           O  
HETATM 2930  O   HOH B 691      39.353  45.253  33.521  1.00 40.90           O  
HETATM 2931  O   HOH B 692      43.101  28.866  21.025  1.00 50.42           O  
HETATM 2932  O   HOH B 693      61.701  37.429  41.770  1.00 44.15           O  
HETATM 2933  O   HOH B 694      46.261  42.163 -15.575  1.00 49.03           O  
HETATM 2934  O   HOH B 695      31.008  59.518   6.865  1.00 51.00           O  
HETATM 2935  O   HOH B 696      61.836  42.203  18.155  1.00 46.42           O  
HETATM 2936  O   HOH B 697      61.382  25.659  20.974  1.00 39.92           O  
HETATM 2937  O   HOH B 698      35.414  46.095  14.566  1.00 52.60           O  
HETATM 2938  O   HOH B 699      57.376  24.985  19.027  1.00 46.34           O  
HETATM 2939  O   HOH B 700      46.054  48.845 -13.285  1.00 44.62           O  
HETATM 2940  O   HOH B 701      46.935  53.230  15.109  1.00 56.71           O  
HETATM 2941  O   HOH B 702      52.547  15.166  11.096  1.00 47.54           O  
HETATM 2942  O   HOH B 703      22.809  38.284  -6.090  1.00 35.65           O  
HETATM 2943  O   HOH B 704      37.275  32.015  12.717  1.00 51.43           O  
HETATM 2944  O   HOH B 705      65.715  45.354  31.750  1.00 46.65           O  
HETATM 2945  O   HOH B 706      51.068  -3.483   7.826  1.00 41.44           O  
HETATM 2946  O   HOH B 707      33.845  51.487 -20.424  1.00 46.87           O  
HETATM 2947  O   HOH B 708      41.680  27.370  15.422  1.00 46.82           O  
HETATM 2948  O   HOH B 709      49.919  51.272  -7.657  1.00 32.10           O  
HETATM 2949  O   HOH B 710      43.010  27.714  31.336  1.00 27.12           O  
HETATM 2950  O   HOH B 711      25.791  51.594  10.984  1.00 56.21           O  
HETATM 2951  O   HOH B 712      22.690  44.595  -2.814  1.00 25.04           O  
HETATM 2952  O   HOH B 713      48.748  39.163   5.355  1.00 33.78           O  
HETATM 2953  O   HOH B 714      41.681  54.061  -7.317  1.00 36.92           O  
HETATM 2954  O   HOH B 715      49.641  24.102  12.878  1.00 39.13           O  
HETATM 2955  O   HOH B 716      55.273  36.205   8.144  1.00 27.65           O  
HETATM 2956  O   HOH B 717      21.173  43.355  -1.945  1.00 39.41           O  
HETATM 2957  O   HOH B 718      54.669  39.871   7.540  1.00 32.20           O  
HETATM 2958  O   HOH B 719      21.594  50.249   4.737  1.00 41.36           O  
HETATM 2959  O   HOH B 720      26.258  38.003 -10.165  1.00 32.73           O  
HETATM 2960  O   HOH B 721      28.565  31.632   2.814  1.00 29.90           O  
HETATM 2961  O   HOH B 722      27.580  51.494  12.361  1.00 59.44           O  
HETATM 2962  O   HOH B 723      64.778  33.447  10.660  1.00 44.81           O  
HETATM 2963  O   HOH B 724      37.962  59.228   6.774  1.00 42.56           O  
HETATM 2964  O   HOH B 725      54.669  25.697  11.045  1.00 47.46           O  
HETATM 2965  O   HOH B 726      59.573  49.058  27.847  1.00 48.51           O  
HETATM 2966  O   HOH B 727      55.213  21.577  26.421  1.00 20.36           O  
HETATM 2967  O   HOH B 728      27.213  46.677  19.620  1.00 54.50           O  
HETATM 2968  O   HOH B 729      51.195  57.361   1.765  1.00 53.70           O  
HETATM 2969  O   HOH B 730      49.318   7.827  15.822  1.00 41.79           O  
HETATM 2970  O   HOH B 731      27.883  43.700  22.621  1.00 47.38           O  
HETATM 2971  O   HOH B 732      53.543  56.182   5.843  1.00 44.39           O  
HETATM 2972  O   HOH B 733      48.063  44.358 -13.929  1.00 53.63           O  
HETATM 2973  O   HOH B 734      48.232  42.077 -11.320  1.00 45.04           O  
HETATM 2974  O   HOH B 735      37.233  31.217  22.572  1.00 54.40           O  
HETATM 2975  O   HOH B 736      65.737  39.329  11.915  1.00 56.56           O  
HETATM 2976  O   HOH B 737      31.006  56.099   6.312  1.00 48.12           O  
HETATM 2977  O   HOH B 738      33.854  39.051  20.402  1.00 54.20           O  
HETATM 2978  O   HOH B 739      30.215  53.825   8.453  1.00 41.06           O  
HETATM 2979  O   HOH B 740      72.249  41.404  28.912  1.00 38.86           O  
HETATM 2980  O   HOH B 741      39.703  49.907 -16.838  1.00 46.07           O  
HETATM 2981  O   HOH B 742      41.452  49.012  26.701  1.00 33.27           O  
HETATM 2982  O   HOH B 743      59.311  46.259  35.545  1.00 36.61           O  
HETATM 2983  O   HOH B 744      36.876  39.802  24.815  1.00 44.86           O  
HETATM 2984  O   HOH B 745      46.056  25.945  11.028  1.00 41.16           O  
HETATM 2985  O   HOH B 746      47.057  25.789  13.003  1.00 48.24           O  
HETATM 2986  O   HOH B 747      59.401  23.342  31.260  1.00 38.63           O  
HETATM 2987  O   HOH B 748      42.430  49.546 -15.007  1.00 33.66           O  
HETATM 2988  O   HOH B 749      36.855  43.104  29.807  1.00 36.68           O  
HETATM 2989  O   HOH B 750      39.871  56.634 -13.070  1.00 38.86           O  
HETATM 2990  O   HOH B 751      64.805  38.358  28.056  1.00 27.70           O  
HETATM 2991  O   HOH B 752      42.616  20.317   6.882  1.00 32.41           O  
HETATM 2992  O   HOH B 753      45.884  59.360   4.926  1.00 49.21           O  
HETATM 2993  O   HOH B 754      23.895  37.387   6.575  1.00 41.90           O  
HETATM 2994  O   HOH B 755      45.396  16.397   9.868  1.00 42.81           O  
HETATM 2995  O   HOH B 756      51.288  19.106   1.334  1.00 39.49           O  
HETATM 2996  O   HOH B 757      30.142  59.669   1.604  1.00 42.76           O  
HETATM 2997  O   HOH B 758      23.547  42.986 -11.400  1.00 50.65           O  
HETATM 2998  O   HOH B 759      47.565  37.527   5.150  1.00 41.20           O  
HETATM 2999  O   HOH B 760      37.021  33.783  31.379  1.00 46.78           O  
HETATM 3000  O   HOH B 761      36.770  38.969  22.797  1.00 35.10           O  
HETATM 3001  O   HOH B 762      38.749  30.925  17.127  1.00 50.01           O  
HETATM 3002  O   HOH B 763      63.566  44.701  27.310  1.00 47.55           O  
HETATM 3003  O   HOH B 764      43.678  43.222  33.327  1.00 15.36           O  
HETATM 3004  O   HOH B 765      42.680  45.221  33.271  1.00 31.16           O  
HETATM 3005  O   HOH B 766      64.107  33.957  19.666  1.00 39.62           O  
HETATM 3006  O   HOH B 767      55.765  38.329   8.347  1.00 36.80           O  
HETATM 3007  O   HOH B 768      48.497  18.334  24.726  1.00 64.69           O  
HETATM 3008  O   HOH B 769      47.497  17.251  26.791  1.00 49.10           O  
CONECT   99 2560                                                                
CONECT  116 2560                                                                
CONECT  128 2560                                                                
CONECT  137 2560                                                                
CONECT  179 2560                                                                
CONECT  180 2560                                                                
CONECT  376 2561                                                                
CONECT  389 2561                                                                
CONECT  401 2561                                                                
CONECT  410 2561                                                                
CONECT  455 2561                                                                
CONECT  456 2561                                                                
CONECT 1369 2562                                                                
CONECT 1377 2562                                                                
CONECT 2560   99  116  128  137                                                 
CONECT 2560  179  180 2585                                                      
CONECT 2561  376  389  401  410                                                 
CONECT 2561  455  456 2620                                                      
CONECT 2562 1369 1377 2840 2841                                                 
CONECT 2562 2843                                                                
CONECT 2564 2565 2566                                                           
CONECT 2565 2564                                                                
CONECT 2566 2564 2567                                                           
CONECT 2567 2566                                                                
CONECT 2568 2569 2570                                                           
CONECT 2569 2568                                                                
CONECT 2570 2568 2571                                                           
CONECT 2571 2570                                                                
CONECT 2572 2573 2574                                                           
CONECT 2573 2572                                                                
CONECT 2574 2572 2575                                                           
CONECT 2575 2574                                                                
CONECT 2576 2577 2578                                                           
CONECT 2577 2576                                                                
CONECT 2578 2576 2579 2580                                                      
CONECT 2579 2578                                                                
CONECT 2580 2578 2581                                                           
CONECT 2581 2580                                                                
CONECT 2585 2560                                                                
CONECT 2620 2561                                                                
CONECT 2840 2562                                                                
CONECT 2841 2562                                                                
CONECT 2843 2562                                                                
MASTER      476    0    8   19    2    0   12    6 2940    2   43   24          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.