CNRS Nantes University US2B US2B
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***  First_try_HSA  ***

elNémo ID: 2407261243581313866

Job options:

ID        	=	 2407261243581313866
JOBID     	=	 First_try_HSA
USERID    	=	 Zitzero
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 First_try_HSA

HEADER    TRANSPORT PROTEIN                       20-NOV-20   7DJN              
TITLE     HUMAN SERUM ALBUMIN                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERUM ALBUMIN;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: ALB, GIG20, GIG42, PRO0903, PRO1708, PRO2044, PRO2619,         
SOURCE   6 PRO2675, UNQ696/PRO1341;                                             
SOURCE   7 EXPRESSION_SYSTEM: KOMAGATAELLA PASTORIS;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 4922                                        
KEYWDS    HUMAN SERUM ALBUMIN, TRANSPORT PROTEIN                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.XIANG,Z.YUE,J.SU                                                    
REVDAT   2   29-NOV-23 7DJN    1       REMARK                                   
REVDAT   1   24-NOV-21 7DJN    0                                                
JRNL        AUTH   W.XIANG,Z.YUE,J.SU                                           
JRNL        TITL   HUMAN SERUM ALBUMIN                                          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.17.1_3660                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.34                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.960                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 64903                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1971                            
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 19.3400 -  4.9000    0.93     4420   152  0.1956 0.2192        
REMARK   3     2  4.9000 -  3.9000    0.93     4471   130  0.1939 0.2173        
REMARK   3     3  3.9000 -  3.4100    0.94     4495   142  0.2208 0.2394        
REMARK   3     4  3.4100 -  3.1000    0.94     4480   142  0.2549 0.3133        
REMARK   3     5  3.1000 -  2.8800    0.95     4554   134  0.2693 0.3438        
REMARK   3     6  2.8800 -  2.7100    0.95     4554   139  0.2696 0.2831        
REMARK   3     7  2.7100 -  2.5700    0.95     4513   146  0.2669 0.2875        
REMARK   3     8  2.5700 -  2.4600    0.95     4547   142  0.2723 0.3119        
REMARK   3     9  2.4600 -  2.3700    0.95     4483   134  0.2816 0.3616        
REMARK   3    10  2.3700 -  2.2800    0.95     4587   144  0.2934 0.3885        
REMARK   3    11  2.2800 -  2.2100    0.94     4497   139  0.3162 0.3766        
REMARK   3    12  2.2100 -  2.1500    0.94     4481   140  0.3320 0.3576        
REMARK   3    13  2.1500 -  2.0900    0.95     4452   148  0.3538 0.3804        
REMARK   3    14  2.0900 -  2.0400    0.92     4398   139  0.3801 0.4200        
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)     : 0.360            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 35.020           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 64.53                          
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      :   NULL           NULL                                  
REMARK   3   ANGLE     :   NULL           NULL                                  
REMARK   3   CHIRALITY :   NULL           NULL                                  
REMARK   3   PLANARITY :   NULL           NULL                                  
REMARK   3   DIHEDRAL  :   NULL           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4760  12.4882 -17.3132              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3410 T22:   0.2063                                     
REMARK   3      T33:   0.3171 T12:  -0.1052                                     
REMARK   3      T13:   0.0349 T23:   0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0567 L22:   0.4953                                     
REMARK   3      L33:   0.6966 L12:  -0.4030                                     
REMARK   3      L13:   0.2806 L23:  -0.0504                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0159 S12:  -0.0274 S13:   0.0147                       
REMARK   3      S21:  -0.0342 S22:  -0.0322 S23:   0.0294                       
REMARK   3      S31:   0.0364 S32:  -0.0011 S33:   0.0004                       
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 7DJN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 30-NOV-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300019527.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-20                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL18U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64942                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.520                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.07600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.97300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 6M4R                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.11                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PHOSPHATE, VAPOR DIFFUSION, HANGING      
REMARK 280  DROP, TEMPERATURE 298K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     HIS A     3                                                      
REMARK 465     ALA A    78                                                      
REMARK 465     THR A    79                                                      
REMARK 465     LEU A    80                                                      
REMARK 465     ARG A    81                                                      
REMARK 465     GLU A    82                                                      
REMARK 465     THR A    83                                                      
REMARK 465     TYR A    84                                                      
REMARK 465     GLY A    85                                                      
REMARK 465     GLU A    86                                                      
REMARK 465     ALA A    92                                                      
REMARK 465     VAL A   116                                                      
REMARK 465     ARG A   117                                                      
REMARK 465     PRO A   118                                                      
REMARK 465     GLU A   119                                                      
REMARK 465     ALA A   171                                                      
REMARK 465     PRO A   299                                                      
REMARK 465     ALA A   300                                                      
REMARK 465     ALA A   569                                                      
REMARK 465     LEU A   583                                                      
REMARK 465     GLY A   584                                                      
REMARK 465     LEU A   585                                                      
REMARK 465     ASP B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     HIS B     3                                                      
REMARK 465     ALA B    59                                                      
REMARK 465     GLU B    60                                                      
REMARK 465     VAL B    77                                                      
REMARK 465     ALA B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     LEU B    80                                                      
REMARK 465     ARG B    81                                                      
REMARK 465     GLU B    82                                                      
REMARK 465     THR B    83                                                      
REMARK 465     TYR B    84                                                      
REMARK 465     GLY B    85                                                      
REMARK 465     CYS B    91                                                      
REMARK 465     ALA B   443                                                      
REMARK 465     ALA B   504                                                      
REMARK 465     LEU B   583                                                      
REMARK 465     GLY B   584                                                      
REMARK 465     LEU B   585                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PHE B  49    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A   5       95.30     59.86                                   
REMARK 500    ALA A  59     -146.39    -82.01                                   
REMARK 500    ARG A 114       45.92   -179.33                                   
REMARK 500    ASN A 130       87.28   -159.73                                   
REMARK 500    TYR A 150       98.51    -63.35                                   
REMARK 500    THR A 166       46.35    -89.89                                   
REMARK 500    GLU A 167      -40.76   -165.07                                   
REMARK 500    ALA A 175       54.91    -68.25                                   
REMARK 500    ALA A 176      -30.91   -155.29                                   
REMARK 500    CYS A 265      -46.84     74.21                                   
REMARK 500    LYS A 274        4.58   -165.25                                   
REMARK 500    ASP A 296     -177.86    -65.74                                   
REMARK 500    VAL A 310      -53.90   -124.63                                   
REMARK 500    ALA A 364      -75.77    -63.26                                   
REMARK 500    GLU A 492      -77.37   -124.00                                   
REMARK 500    PHE A 509      -64.24   -127.60                                   
REMARK 500    HIS A 510      178.39     63.18                                   
REMARK 500    LYS A 536       89.01   -160.84                                   
REMARK 500    THR A 540     -111.56     25.33                                   
REMARK 500    LYS A 541     -135.07     42.48                                   
REMARK 500    ASP A 562       51.04   -117.75                                   
REMARK 500    GLU A 565       19.77     37.85                                   
REMARK 500    LYS A 574      -70.82    -72.75                                   
REMARK 500    SER B   5      -12.86   -163.87                                   
REMARK 500    GLU B   6      -58.35     75.05                                   
REMARK 500    ALA B  55      -70.82    -70.50                                   
REMARK 500    GLN B  94     -119.80   -147.41                                   
REMARK 500    GLU B  95     -171.28     66.54                                   
REMARK 500    GLN B 104       12.95    -68.57                                   
REMARK 500    ASN B 111       84.07    -69.28                                   
REMARK 500    PRO B 118     -166.48    -78.56                                   
REMARK 500    TYR B 150      105.88    -56.19                                   
REMARK 500    ALA B 175      -73.32    -60.73                                   
REMARK 500    ALA B 176       -7.57    -55.70                                   
REMARK 500    PHE B 223       72.48   -119.36                                   
REMARK 500    ILE B 271      -64.38   -124.01                                   
REMARK 500    SER B 272     -168.21   -171.22                                   
REMARK 500    LEU B 275      -32.48   -148.67                                   
REMARK 500    GLU B 280       -1.75   -165.37                                   
REMARK 500    PRO B 282     -179.11    -61.79                                   
REMARK 500    GLU B 292       34.90    -82.86                                   
REMARK 500    MET B 298      129.33     76.81                                   
REMARK 500    ASP B 301       94.38     -6.86                                   
REMARK 500    SER B 304     -159.97    -73.50                                   
REMARK 500    VAL B 310      -59.41   -131.37                                   
REMARK 500    ALA B 322       87.26   -152.77                                   
REMARK 500    ASP B 365       78.13     49.68                                   
REMARK 500    CYS B 438        1.77    -62.96                                   
REMARK 500    ARG B 445      -70.77    -86.43                                   
REMARK 500    VAL B 469      -26.64   -140.27                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7DJN A    1   585  UNP    P02768   ALBU_HUMAN      25    609             
DBREF  7DJN B    1   585  UNP    P02768   ALBU_HUMAN      25    609             
SEQRES   1 A  585  ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP          
SEQRES   2 A  585  LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA          
SEQRES   3 A  585  PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS          
SEQRES   4 A  585  VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR          
SEQRES   5 A  585  CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER          
SEQRES   6 A  585  LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA          
SEQRES   7 A  585  THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS          
SEQRES   8 A  585  ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN          
SEQRES   9 A  585  HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG          
SEQRES  10 A  585  PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN          
SEQRES  11 A  585  GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA          
SEQRES  12 A  585  ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE          
SEQRES  13 A  585  PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS          
SEQRES  14 A  585  GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU          
SEQRES  15 A  585  ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS          
SEQRES  16 A  585  GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU          
SEQRES  17 A  585  ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN          
SEQRES  18 A  585  ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU          
SEQRES  19 A  585  VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS          
SEQRES  20 A  585  GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU          
SEQRES  21 A  585  ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER          
SEQRES  22 A  585  LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS          
SEQRES  23 A  585  SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO          
SEQRES  24 A  585  ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER          
SEQRES  25 A  585  LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL          
SEQRES  26 A  585  PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS          
SEQRES  27 A  585  PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS          
SEQRES  28 A  585  THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA          
SEQRES  29 A  585  ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE          
SEQRES  30 A  585  LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN          
SEQRES  31 A  585  ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE          
SEQRES  32 A  585  GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO          
SEQRES  33 A  585  GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN          
SEQRES  34 A  585  LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU          
SEQRES  35 A  585  ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL          
SEQRES  36 A  585  VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO          
SEQRES  37 A  585  VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU          
SEQRES  38 A  585  VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP          
SEQRES  39 A  585  GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE          
SEQRES  40 A  585  THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU          
SEQRES  41 A  585  ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL          
SEQRES  42 A  585  LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA          
SEQRES  43 A  585  VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS          
SEQRES  44 A  585  LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY          
SEQRES  45 A  585  LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU          
SEQRES   1 B  585  ASP ALA HIS LYS SER GLU VAL ALA HIS ARG PHE LYS ASP          
SEQRES   2 B  585  LEU GLY GLU GLU ASN PHE LYS ALA LEU VAL LEU ILE ALA          
SEQRES   3 B  585  PHE ALA GLN TYR LEU GLN GLN CYS PRO PHE GLU ASP HIS          
SEQRES   4 B  585  VAL LYS LEU VAL ASN GLU VAL THR GLU PHE ALA LYS THR          
SEQRES   5 B  585  CYS VAL ALA ASP GLU SER ALA GLU ASN CYS ASP LYS SER          
SEQRES   6 B  585  LEU HIS THR LEU PHE GLY ASP LYS LEU CYS THR VAL ALA          
SEQRES   7 B  585  THR LEU ARG GLU THR TYR GLY GLU MET ALA ASP CYS CYS          
SEQRES   8 B  585  ALA LYS GLN GLU PRO GLU ARG ASN GLU CYS PHE LEU GLN          
SEQRES   9 B  585  HIS LYS ASP ASP ASN PRO ASN LEU PRO ARG LEU VAL ARG          
SEQRES  10 B  585  PRO GLU VAL ASP VAL MET CYS THR ALA PHE HIS ASP ASN          
SEQRES  11 B  585  GLU GLU THR PHE LEU LYS LYS TYR LEU TYR GLU ILE ALA          
SEQRES  12 B  585  ARG ARG HIS PRO TYR PHE TYR ALA PRO GLU LEU LEU PHE          
SEQRES  13 B  585  PHE ALA LYS ARG TYR LYS ALA ALA PHE THR GLU CYS CYS          
SEQRES  14 B  585  GLN ALA ALA ASP LYS ALA ALA CYS LEU LEU PRO LYS LEU          
SEQRES  15 B  585  ASP GLU LEU ARG ASP GLU GLY LYS ALA SER SER ALA LYS          
SEQRES  16 B  585  GLN ARG LEU LYS CYS ALA SER LEU GLN LYS PHE GLY GLU          
SEQRES  17 B  585  ARG ALA PHE LYS ALA TRP ALA VAL ALA ARG LEU SER GLN          
SEQRES  18 B  585  ARG PHE PRO LYS ALA GLU PHE ALA GLU VAL SER LYS LEU          
SEQRES  19 B  585  VAL THR ASP LEU THR LYS VAL HIS THR GLU CYS CYS HIS          
SEQRES  20 B  585  GLY ASP LEU LEU GLU CYS ALA ASP ASP ARG ALA ASP LEU          
SEQRES  21 B  585  ALA LYS TYR ILE CYS GLU ASN GLN ASP SER ILE SER SER          
SEQRES  22 B  585  LYS LEU LYS GLU CYS CYS GLU LYS PRO LEU LEU GLU LYS          
SEQRES  23 B  585  SER HIS CYS ILE ALA GLU VAL GLU ASN ASP GLU MET PRO          
SEQRES  24 B  585  ALA ASP LEU PRO SER LEU ALA ALA ASP PHE VAL GLU SER          
SEQRES  25 B  585  LYS ASP VAL CYS LYS ASN TYR ALA GLU ALA LYS ASP VAL          
SEQRES  26 B  585  PHE LEU GLY MET PHE LEU TYR GLU TYR ALA ARG ARG HIS          
SEQRES  27 B  585  PRO ASP TYR SER VAL VAL LEU LEU LEU ARG LEU ALA LYS          
SEQRES  28 B  585  THR TYR GLU THR THR LEU GLU LYS CYS CYS ALA ALA ALA          
SEQRES  29 B  585  ASP PRO HIS GLU CYS TYR ALA LYS VAL PHE ASP GLU PHE          
SEQRES  30 B  585  LYS PRO LEU VAL GLU GLU PRO GLN ASN LEU ILE LYS GLN          
SEQRES  31 B  585  ASN CYS GLU LEU PHE GLU GLN LEU GLY GLU TYR LYS PHE          
SEQRES  32 B  585  GLN ASN ALA LEU LEU VAL ARG TYR THR LYS LYS VAL PRO          
SEQRES  33 B  585  GLN VAL SER THR PRO THR LEU VAL GLU VAL SER ARG ASN          
SEQRES  34 B  585  LEU GLY LYS VAL GLY SER LYS CYS CYS LYS HIS PRO GLU          
SEQRES  35 B  585  ALA LYS ARG MET PRO CYS ALA GLU ASP TYR LEU SER VAL          
SEQRES  36 B  585  VAL LEU ASN GLN LEU CYS VAL LEU HIS GLU LYS THR PRO          
SEQRES  37 B  585  VAL SER ASP ARG VAL THR LYS CYS CYS THR GLU SER LEU          
SEQRES  38 B  585  VAL ASN ARG ARG PRO CYS PHE SER ALA LEU GLU VAL ASP          
SEQRES  39 B  585  GLU THR TYR VAL PRO LYS GLU PHE ASN ALA GLU THR PHE          
SEQRES  40 B  585  THR PHE HIS ALA ASP ILE CYS THR LEU SER GLU LYS GLU          
SEQRES  41 B  585  ARG GLN ILE LYS LYS GLN THR ALA LEU VAL GLU LEU VAL          
SEQRES  42 B  585  LYS HIS LYS PRO LYS ALA THR LYS GLU GLN LEU LYS ALA          
SEQRES  43 B  585  VAL MET ASP ASP PHE ALA ALA PHE VAL GLU LYS CYS CYS          
SEQRES  44 B  585  LYS ALA ASP ASP LYS GLU THR CYS PHE ALA GLU GLU GLY          
SEQRES  45 B  585  LYS LYS LEU VAL ALA ALA SER GLN ALA ALA LEU GLY LEU          
FORMUL   3  HOH   *187(H2 O)                                                    
HELIX    1 AA1 SER A    5  GLY A   15  1                                  11    
HELIX    2 AA2 GLY A   15  LEU A   31  1                                  17    
HELIX    3 AA3 PRO A   35  ASP A   56  1                                  22    
HELIX    4 AA4 SER A   65  CYS A   75  1                                  11    
HELIX    5 AA5 GLN A   94  GLN A  104  1                                  11    
HELIX    6 AA6 MET A  123  ASN A  130  1                                   8    
HELIX    7 AA7 ASN A  130  HIS A  146  1                                  17    
HELIX    8 AA8 TYR A  150  CYS A  169  1                                  20    
HELIX    9 AA9 GLU A  184  LYS A  205  1                                  22    
HELIX   10 AB1 GLY A  207  PHE A  223  1                                  17    
HELIX   11 AB2 GLU A  227  HIS A  247  1                                  21    
HELIX   12 AB3 ASP A  249  ILE A  264  1                                  16    
HELIX   13 AB4 LEU A  275  GLU A  280  1                                   6    
HELIX   14 AB5 PRO A  282  GLU A  292  1                                  11    
HELIX   15 AB6 SER A  304  VAL A  310  1                                   7    
HELIX   16 AB7 ASP A  314  ALA A  322  1                                   9    
HELIX   17 AB8 ALA A  322  HIS A  338  1                                  17    
HELIX   18 AB9 SER A  342  CYS A  361  1                                  20    
HELIX   19 AC1 ASP A  365  ALA A  371  1                                   7    
HELIX   20 AC2 LYS A  372  VAL A  415  1                                  44    
HELIX   21 AC3 SER A  419  CYS A  438  1                                  20    
HELIX   22 AC4 PRO A  441  THR A  467  1                                  27    
HELIX   23 AC5 SER A  470  GLU A  479  1                                  10    
HELIX   24 AC6 ASN A  483  LEU A  491  1                                   9    
HELIX   25 AC7 HIS A  510  CYS A  514  5                                   5    
HELIX   26 AC8 SER A  517  LYS A  536  1                                  20    
HELIX   27 AC9 GLU A  542  LYS A  560  1                                  19    
HELIX   28 AD1 GLU A  571  ALA A  581  1                                  11    
HELIX   29 AD2 GLU B    6  GLY B   15  1                                  10    
HELIX   30 AD3 GLY B   15  LEU B   31  1                                  17    
HELIX   31 AD4 PRO B   35  ASP B   56  1                                  22    
HELIX   32 AD5 SER B   65  THR B   76  1                                  12    
HELIX   33 AD6 GLU B   97  GLN B  104  1                                   8    
HELIX   34 AD7 GLU B  119  ASN B  130  1                                  12    
HELIX   35 AD8 ASN B  130  ARG B  144  1                                  15    
HELIX   36 AD9 TYR B  150  CYS B  169  1                                  20    
HELIX   37 AE1 LYS B  174  LYS B  205  1                                  32    
HELIX   38 AE2 GLY B  207  PHE B  223  1                                  17    
HELIX   39 AE3 GLU B  227  HIS B  247  1                                  21    
HELIX   40 AE4 ASP B  249  CYS B  265  1                                  17    
HELIX   41 AE5 PRO B  282  GLU B  292  1                                  11    
HELIX   42 AE6 LEU B  305  VAL B  310  1                                   6    
HELIX   43 AE7 ASP B  314  ALA B  322  1                                   9    
HELIX   44 AE8 ALA B  322  ARG B  337  1                                  16    
HELIX   45 AE9 SER B  342  CYS B  361  1                                  20    
HELIX   46 AF1 ASP B  365  ALA B  371  1                                   7    
HELIX   47 AF2 LYS B  372  VAL B  415  1                                  44    
HELIX   48 AF3 SER B  419  CYS B  438  1                                  20    
HELIX   49 AF4 PRO B  441  GLU B  442  5                                   2    
HELIX   50 AF5 LYS B  444  LYS B  444  5                                   1    
HELIX   51 AF6 ARG B  445  THR B  467  1                                  23    
HELIX   52 AF7 SER B  470  SER B  480  1                                  11    
HELIX   53 AF8 ASN B  483  LEU B  491  1                                   9    
HELIX   54 AF9 HIS B  510  THR B  515  5                                   6    
HELIX   55 AG1 SER B  517  LYS B  536  1                                  20    
HELIX   56 AG2 GLN B  543  CYS B  559  1                                  17    
HELIX   57 AG3 GLU B  565  ALA B  581  1                                  17    
SSBOND   1 CYS A   53    CYS A   62                          1555   1555  2.03  
SSBOND   2 CYS A   75    CYS A   91                          1555   1555  2.02  
SSBOND   3 CYS A   90    CYS A  101                          1555   1555  2.03  
SSBOND   4 CYS A  124    CYS A  169                          1555   1555  2.00  
SSBOND   5 CYS A  168    CYS A  177                          1555   1555  2.03  
SSBOND   6 CYS A  200    CYS A  246                          1555   1555  2.03  
SSBOND   7 CYS A  245    CYS A  253                          1555   1555  1.92  
SSBOND   8 CYS A  265    CYS A  279                          1555   1555  2.03  
SSBOND   9 CYS A  278    CYS A  289                          1555   1555  2.03  
SSBOND  10 CYS A  316    CYS A  361                          1555   1555  2.03  
SSBOND  11 CYS A  360    CYS A  369                          1555   1555  2.03  
SSBOND  12 CYS A  392    CYS A  438                          1555   1555  2.03  
SSBOND  13 CYS A  437    CYS A  448                          1555   1555  2.03  
SSBOND  14 CYS A  461    CYS A  477                          1555   1555  2.03  
SSBOND  15 CYS A  476    CYS A  487                          1555   1555  2.04  
SSBOND  16 CYS A  514    CYS A  559                          1555   1555  2.03  
SSBOND  17 CYS A  558    CYS A  567                          1555   1555  2.03  
SSBOND  18 CYS B   53    CYS B   62                          1555   1555  2.02  
SSBOND  19 CYS B   90    CYS B  101                          1555   1555  2.05  
SSBOND  20 CYS B  124    CYS B  169                          1555   1555  2.03  
SSBOND  21 CYS B  168    CYS B  177                          1555   1555  2.03  
SSBOND  22 CYS B  200    CYS B  246                          1555   1555  2.03  
SSBOND  23 CYS B  245    CYS B  253                          1555   1555  1.92  
SSBOND  24 CYS B  265    CYS B  279                          1555   1555  2.04  
SSBOND  25 CYS B  278    CYS B  289                          1555   1555  2.03  
SSBOND  26 CYS B  316    CYS B  361                          1555   1555  2.02  
SSBOND  27 CYS B  360    CYS B  369                          1555   1555  2.03  
SSBOND  28 CYS B  392    CYS B  438                          1555   1555  2.02  
SSBOND  29 CYS B  437    CYS B  448                          1555   1555  2.00  
SSBOND  30 CYS B  461    CYS B  477                          1555   1555  2.02  
SSBOND  31 CYS B  476    CYS B  487                          1555   1555  2.03  
SSBOND  32 CYS B  514    CYS B  559                          1555   1555  2.03  
SSBOND  33 CYS B  558    CYS B  567                          1555   1555  2.03  
CRYST1   52.092   53.030  117.424  99.17  93.45 117.64 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019197  0.010055  0.003364        0.00000                         
SCALE2      0.000000  0.021287  0.004614        0.00000                         
SCALE3      0.000000  0.000000  0.008730        0.00000                         
ATOM      1  N   LYS A   4      34.289   7.803  38.365  1.00 77.42           N  
ANISOU    1  N   LYS A   4     9751  13807   5859   2248   -905   -511       N  
ATOM      2  CA  LYS A   4      33.870   6.441  38.058  1.00 79.00           C  
ANISOU    2  CA  LYS A   4     9989  13965   6061   2210   -780   -260       C  
ATOM      3  C   LYS A   4      32.352   6.319  38.082  1.00 78.84           C  
ANISOU    3  C   LYS A   4     9995  13970   5992   2197   -657   -153       C  
ATOM      4  O   LYS A   4      31.668   7.151  38.678  1.00 79.97           O  
ANISOU    4  O   LYS A   4    10124  14225   6035   2263   -668   -257       O  
ATOM      5  CB  LYS A   4      34.492   5.452  39.045  1.00 89.58           C  
ANISOU    5  CB  LYS A   4    11335  15462   7238   2338   -790   -144       C  
ATOM      6  CG  LYS A   4      35.994   5.603  39.206  1.00 93.78           C  
ANISOU    6  CG  LYS A   4    11836  16007   7791   2375   -920   -260       C  
ATOM      7  CD  LYS A   4      36.515   4.741  40.343  1.00 96.23           C  
ANISOU    7  CD  LYS A   4    12149  16503   7910   2525   -937   -160       C  
ATOM      8  CE  LYS A   4      37.179   3.479  39.817  1.00 95.68           C  
ANISOU    8  CE  LYS A   4    12101  16333   7919   2480   -900     15       C  
ATOM      9  NZ  LYS A   4      36.906   2.304  40.692  1.00 98.12           N  
ANISOU    9  NZ  LYS A   4    12441  16772   8070   2584   -827    224       N  
ATOM     10  N   SER A   5      31.844   5.273  37.427  1.00 83.18           N  
ANISOU   10  N   SER A   5    10577  14414   6612   2112   -543     53       N  
ATOM     11  CA  SER A   5      30.415   4.993  37.340  1.00 79.00           C  
ANISOU   11  CA  SER A   5    10068  13891   6058   2082   -418    183       C  
ATOM     12  C   SER A   5      29.655   6.134  36.677  1.00 70.77           C  
ANISOU   12  C   SER A   5     9014  12757   5118   2001   -416     44       C  
ATOM     13  O   SER A   5      29.267   7.102  37.340  1.00 70.82           O  
ANISOU   13  O   SER A   5     8999  12884   5024   2081   -456    -97       O  
ATOM     14  CB  SER A   5      29.829   4.708  38.724  1.00 76.61           C  
ANISOU   14  CB  SER A   5     9762  13833   5515   2235   -377    262       C  
ATOM     15  OG  SER A   5      28.461   5.066  38.770  1.00 72.23           O  
ANISOU   15  OG  SER A   5     9205  13317   4923   2225   -293    285       O  
ATOM     16  N   GLU A   6      29.425   6.021  35.367  1.00 65.13           N  
ANISOU   16  N   GLU A   6     8314  11830   4600   1848   -372     82       N  
ATOM     17  CA  GLU A   6      28.693   7.055  34.649  1.00 63.04           C  
ANISOU   17  CA  GLU A   6     8042  11466   4444   1765   -367    -36       C  
ATOM     18  C   GLU A   6      27.202   7.036  34.962  1.00 63.64           C  
ANISOU   18  C   GLU A   6     8122  11622   4435   1785   -264     47       C  
ATOM     19  O   GLU A   6      26.540   8.069  34.816  1.00 64.20           O  
ANISOU   19  O   GLU A   6     8179  11685   4527   1774   -274    -80       O  
ATOM     20  CB  GLU A   6      28.908   6.904  33.141  1.00 59.36           C  
ANISOU   20  CB  GLU A   6     7591  10757   4206   1601   -350    -13       C  
ATOM     21  CG  GLU A   6      30.225   7.474  32.641  1.00 60.82           C  
ANISOU   21  CG  GLU A   6     7756  10846   4507   1562   -464   -162       C  
ATOM     22  CD  GLU A   6      30.345   8.970  32.869  1.00 70.71           C  
ANISOU   22  CD  GLU A   6     8977  12127   5764   1589   -562   -394       C  
ATOM     23  OE1 GLU A   6      29.304   9.661  32.881  1.00 72.09           O  
ANISOU   23  OE1 GLU A   6     9152  12315   5925   1586   -532   -446       O  
ATOM     24  OE2 GLU A   6      31.483   9.455  33.038  1.00 75.26           O  
ANISOU   24  OE2 GLU A   6     9526  12708   6361   1614   -674   -526       O  
ATOM     25  N   VAL A   7      26.660   5.893  35.388  1.00 63.68           N  
ANISOU   25  N   VAL A   7     8143  11704   4348   1816   -165    258       N  
ATOM     26  CA  VAL A   7      25.232   5.820  35.680  1.00 58.57           C  
ANISOU   26  CA  VAL A   7     7492  11138   3624   1831    -60    352       C  
ATOM     27  C   VAL A   7      24.897   6.634  36.926  1.00 64.65           C  
ANISOU   27  C   VAL A   7     8234  12136   4195   1983    -93    237       C  
ATOM     28  O   VAL A   7      23.845   7.280  36.996  1.00 56.99           O  
ANISOU   28  O   VAL A   7     7248  11211   3194   1992    -53    190       O  
ATOM     29  CB  VAL A   7      24.781   4.351  35.806  1.00 55.66           C  
ANISOU   29  CB  VAL A   7     7143  10785   3219   1817     53    619       C  
ATOM     30  CG1 VAL A   7      25.489   3.649  36.961  1.00 58.11           C  
ANISOU   30  CG1 VAL A   7     7457  11266   3358   1949     30    700       C  
ATOM     31  CG2 VAL A   7      23.268   4.267  35.956  1.00 55.95           C  
ANISOU   31  CG2 VAL A   7     7168  10885   3204   1809    167    724       C  
ATOM     32  N   ALA A   8      25.790   6.634  37.921  1.00 58.13           N  
ANISOU   32  N   ALA A   8     7401  11459   3228   2111   -171    182       N  
ATOM     33  CA  ALA A   8      25.573   7.477  39.091  1.00 63.11           C  
ANISOU   33  CA  ALA A   8     8004  12305   3668   2264   -219     46       C  
ATOM     34  C   ALA A   8      25.794   8.947  38.763  1.00 64.91           C  
ANISOU   34  C   ALA A   8     8217  12468   3979   2249   -327   -219       C  
ATOM     35  O   ALA A   8      25.216   9.821  39.419  1.00 70.99           O  
ANISOU   35  O   ALA A   8     8963  13351   4658   2335   -346   -342       O  
ATOM     36  CB  ALA A   8      26.486   7.045  40.238  1.00 61.17           C  
ANISOU   36  CB  ALA A   8     7743  12174   3325   2379   -272     59       C  
ATOM     37  N   HIS A   9      26.624   9.237  37.759  1.00 64.20           N  
ANISOU   37  N   HIS A   9     8132  12176   4083   2134   -395   -305       N  
ATOM     38  CA  HIS A   9      26.812  10.616  37.324  1.00 64.04           C  
ANISOU   38  CA  HIS A   9     8097  12067   4169   2099   -493   -540       C  
ATOM     39  C   HIS A   9      25.520  11.185  36.752  1.00 63.37           C  
ANISOU   39  C   HIS A   9     8013  11915   4150   2035   -423   -555       C  
ATOM     40  O   HIS A   9      25.111  12.301  37.094  1.00 57.89           O  
ANISOU   40  O   HIS A   9     7302  11278   3414   2094   -473   -725       O  
ATOM     41  CB  HIS A   9      27.941  10.687  36.294  1.00 62.05           C  
ANISOU   41  CB  HIS A   9     7847  11609   4118   1978   -564   -595       C  
ATOM     42  CG  HIS A   9      28.087  12.027  35.641  1.00 65.07           C  
ANISOU   42  CG  HIS A   9     8215  11862   4645   1912   -650   -806       C  
ATOM     43  ND1 HIS A   9      28.532  12.177  34.345  1.00 61.92           N  
ANISOU   43  ND1 HIS A   9     7820  11241   4465   1761   -665   -822       N  
ATOM     44  CD2 HIS A   9      27.856  13.278  36.106  1.00 67.04           C  
ANISOU   44  CD2 HIS A   9     8446  12173   4854   1978   -729  -1007       C  
ATOM     45  CE1 HIS A   9      28.564  13.461  34.038  1.00 63.91           C  
ANISOU   45  CE1 HIS A   9     8056  11420   4808   1733   -746  -1015       C  
ATOM     46  NE2 HIS A   9      28.156  14.151  35.089  1.00 68.18           N  
ANISOU   46  NE2 HIS A   9     8585  12124   5198   1862   -789  -1133       N  
ATOM     47  N   ARG A  10      24.856  10.423  35.882  1.00 55.58           N  
ANISOU   47  N   ARG A  10     7045  10807   3266   1919   -311   -380       N  
ATOM     48  CA  ARG A  10      23.625  10.897  35.261  1.00 58.05           C  
ANISOU   48  CA  ARG A  10     7356  11049   3650   1851   -242   -382       C  
ATOM     49  C   ARG A  10      22.429  10.796  36.198  1.00 60.59           C  
ANISOU   49  C   ARG A  10     7662  11571   3787   1958   -159   -313       C  
ATOM     50  O   ARG A  10      21.501  11.607  36.096  1.00 61.57           O  
ANISOU   50  O   ARG A  10     7773  11704   3916   1962   -141   -396       O  
ATOM     51  CB  ARG A  10      23.359  10.120  33.972  1.00 53.24           C  
ANISOU   51  CB  ARG A  10     6770  10239   3221   1688   -159   -228       C  
ATOM     52  CG  ARG A  10      24.532  10.125  33.004  1.00 52.07           C  
ANISOU   52  CG  ARG A  10     6634   9900   3250   1584   -230   -278       C  
ATOM     53  CD  ARG A  10      25.024  11.541  32.733  1.00 51.85           C  
ANISOU   53  CD  ARG A  10     6590   9804   3306   1572   -347   -517       C  
ATOM     54  NE  ARG A  10      26.267  11.542  31.965  1.00 51.92           N  
ANISOU   54  NE  ARG A  10     6601   9662   3464   1489   -419   -564       N  
ATOM     55  CZ  ARG A  10      26.799  12.625  31.409  1.00 56.90           C  
ANISOU   55  CZ  ARG A  10     7219  10180   4222   1436   -512   -738       C  
ATOM     56  NH1 ARG A  10      26.202  13.801  31.535  1.00 64.80           N  
ANISOU   56  NH1 ARG A  10     8207  11192   5221   1461   -549   -888       N  
ATOM     57  NH2 ARG A  10      27.934  12.532  30.727  1.00 57.14           N  
ANISOU   57  NH2 ARG A  10     7244  10085   4380   1361   -569   -760       N  
ATOM     58  N   PHE A  11      22.428   9.820  37.110  1.00 57.20           N  
ANISOU   58  N   PHE A  11     7233  11306   3195   2047   -105   -158       N  
ATOM     59  CA  PHE A  11      21.348   9.722  38.088  1.00 63.72           C  
ANISOU   59  CA  PHE A  11     8037  12345   3829   2160    -25    -86       C  
ATOM     60  C   PHE A  11      21.304  10.955  38.982  1.00 67.50           C  
ANISOU   60  C   PHE A  11     8485  12941   4222   2285   -110   -305       C  
ATOM     61  O   PHE A  11      20.228  11.508  39.239  1.00 60.27           O  
ANISOU   61  O   PHE A  11     7543  12079   3280   2318    -66   -339       O  
ATOM     62  CB  PHE A  11      21.516   8.454  38.928  1.00 59.66           C  
ANISOU   62  CB  PHE A  11     7519  11933   3216   2216     38    120       C  
ATOM     63  CG  PHE A  11      20.263   8.020  39.640  1.00 67.89           C  
ANISOU   63  CG  PHE A  11     8526  13080   4191   2255    156    267       C  
ATOM     64  CD1 PHE A  11      19.913   8.577  40.861  1.00 66.78           C  
ANISOU   64  CD1 PHE A  11     8341  13096   3937   2387    139    186       C  
ATOM     65  CD2 PHE A  11      19.443   7.047  39.094  1.00 63.14           C  
ANISOU   65  CD2 PHE A  11     7930  12417   3643   2159    280    487       C  
ATOM     66  CE1 PHE A  11      18.765   8.176  41.520  1.00 63.60           C  
ANISOU   66  CE1 PHE A  11     7898  12796   3470   2424    247    323       C  
ATOM     67  CE2 PHE A  11      18.293   6.641  39.749  1.00 62.68           C  
ANISOU   67  CE2 PHE A  11     7831  12451   3532   2188    385    623       C  
ATOM     68  CZ  PHE A  11      17.954   7.207  40.963  1.00 63.00           C  
ANISOU   68  CZ  PHE A  11     7827  12658   3454   2322    369    542       C  
ATOM     69  N   LYS A  12      22.467  11.406  39.458  1.00 66.75           N  
ANISOU   69  N   LYS A  12     8387  12867   4107   2350   -236   -455       N  
ATOM     70  CA  LYS A  12      22.510  12.578  40.327  1.00 61.67           C  
ANISOU   70  CA  LYS A  12     7711  12306   3413   2463   -327   -668       C  
ATOM     71  C   LYS A  12      22.222  13.857  39.551  1.00 68.73           C  
ANISOU   71  C   LYS A  12     8612  13096   4407   2413   -390   -868       C  
ATOM     72  O   LYS A  12      21.608  14.789  40.085  1.00 62.24           O  
ANISOU   72  O   LYS A  12     7764  12331   3555   2488   -413   -998       O  
ATOM     73  CB  LYS A  12      23.873  12.672  41.011  1.00 65.44           C  
ANISOU   73  CB  LYS A  12     8181  12824   3858   2537   -447   -770       C  
ATOM     74  CG  LYS A  12      24.198  11.511  41.933  1.00 73.84           C  
ANISOU   74  CG  LYS A  12     9236  14005   4814   2609   -397   -593       C  
ATOM     75  CD  LYS A  12      25.610  11.639  42.476  1.00 75.90           C  
ANISOU   75  CD  LYS A  12     9490  14293   5057   2672   -522   -705       C  
ATOM     76  CE  LYS A  12      26.148  10.307  42.968  1.00 74.05           C  
ANISOU   76  CE  LYS A  12     9262  14120   4754   2702   -476   -508       C  
ATOM     77  NZ  LYS A  12      27.543  10.433  43.475  1.00 67.74           N  
ANISOU   77  NZ  LYS A  12     8451  13347   3938   2765   -600   -620       N  
ATOM     78  N   ASP A  13      22.660  13.923  38.292  1.00 59.08           N  
ANISOU   78  N   ASP A  13     7421  11701   3327   2282   -418   -893       N  
ATOM     79  CA  ASP A  13      22.493  15.146  37.514  1.00 66.76           C  
ANISOU   79  CA  ASP A  13     8392  12517   4457   2211   -482  -1076       C  
ATOM     80  C   ASP A  13      21.049  15.332  37.066  1.00 66.67           C  
ANISOU   80  C   ASP A  13     8377  12481   4473   2170   -378  -1020       C  
ATOM     81  O   ASP A  13      20.541  16.459  37.045  1.00 67.31           O  
ANISOU   81  O   ASP A  13     8449  12553   4572   2200   -423  -1186       O  
ATOM     82  CB  ASP A  13      23.429  15.130  36.304  1.00 56.68           C  
ANISOU   82  CB  ASP A  13     7131  10995   3412   2052   -532  -1090       C  
ATOM     83  CG  ASP A  13      24.851  15.523  36.659  1.00 66.79           C  
ANISOU   83  CG  ASP A  13     8402  12275   4699   2092   -675  -1238       C  
ATOM     84  OD1 ASP A  13      25.106  15.837  37.841  1.00 67.98           O  
ANISOU   84  OD1 ASP A  13     8539  12614   4678   2244   -743  -1340       O  
ATOM     85  OD2 ASP A  13      25.715  15.518  35.757  1.00 64.58           O  
ANISOU   85  OD2 ASP A  13     8127  11814   4596   1973   -721  -1253       O  
ATOM     86  N   LEU A  14      20.370  14.242  36.710  1.00 61.99           N  
ANISOU   86  N   LEU A  14     7790  11875   3889   2103   -243   -790       N  
ATOM     87  CA  LEU A  14      19.028  14.320  36.146  1.00 56.57           C  
ANISOU   87  CA  LEU A  14     7097  11145   3253   2043   -142   -721       C  
ATOM     88  C   LEU A  14      17.919  14.076  37.159  1.00 64.64           C  
ANISOU   88  C   LEU A  14     8091  12402   4068   2168    -49   -637       C  
ATOM     89  O   LEU A  14      16.798  14.551  36.954  1.00 65.85           O  
ANISOU   89  O   LEU A  14     8227  12564   4228   2164      4   -655       O  
ATOM     90  CB  LEU A  14      18.878  13.314  34.999  1.00 55.51           C  
ANISOU   90  CB  LEU A  14     6981  10832   3279   1877    -51   -525       C  
ATOM     91  CG  LEU A  14      19.929  13.390  33.890  1.00 57.41           C  
ANISOU   91  CG  LEU A  14     7247  10841   3726   1745   -121   -573       C  
ATOM     92  CD1 LEU A  14      19.731  12.271  32.878  1.00 62.34           C  
ANISOU   92  CD1 LEU A  14     7890  11317   4480   1602    -26   -369       C  
ATOM     93  CD2 LEU A  14      19.886  14.748  33.212  1.00 62.89           C  
ANISOU   93  CD2 LEU A  14     7939  11401   4553   1698   -201   -776       C  
ATOM     94  N   GLY A  15      18.195  13.355  38.239  1.00 59.30           N  
ANISOU   94  N   GLY A  15     7401  11882   3250   2265    -29   -538       N  
ATOM     95  CA  GLY A  15      17.155  12.942  39.156  1.00 63.12           C  
ANISOU   95  CA  GLY A  15     7841  12508   3635   2339     72   -409       C  
ATOM     96  C   GLY A  15      16.498  11.641  38.725  1.00 63.19           C  
ANISOU   96  C   GLY A  15     7851  12493   3664   2247    213   -140       C  
ATOM     97  O   GLY A  15      16.587  11.212  37.577  1.00 60.97           O  
ANISOU   97  O   GLY A  15     7605  12078   3483   2121    244    -65       O  
ATOM     98  N   GLU A  16      15.809  11.009  39.679  1.00 61.51           N  
ANISOU   98  N   GLU A  16     7597  12413   3360   2312    298      8       N  
ATOM     99  CA  GLU A  16      15.282   9.668  39.439  1.00 61.28           C  
ANISOU   99  CA  GLU A  16     7566  12362   3357   2230    424    275       C  
ATOM    100  C   GLU A  16      14.135   9.679  38.436  1.00 64.28           C  
ANISOU  100  C   GLU A  16     7939  12655   3829   2119    513    343       C  
ATOM    101  O   GLU A  16      14.082   8.826  37.541  1.00 66.19           O  
ANISOU  101  O   GLU A  16     8207  12780   4163   1995    574    496       O  
ATOM    102  CB  GLU A  16      14.829   9.033  40.754  1.00 66.85           C  
ANISOU  102  CB  GLU A  16     8223  13232   3944   2329    487    410       C  
ATOM    103  CG  GLU A  16      14.172   7.672  40.577  1.00 63.24           C  
ANISOU  103  CG  GLU A  16     7756  12747   3524   2243    615    686       C  
ATOM    104  CD  GLU A  16      13.648   7.098  41.877  1.00 81.11           C  
ANISOU  104  CD  GLU A  16     9967  15177   5675   2341    678    817       C  
ATOM    105  OE1 GLU A  16      13.164   5.947  41.866  1.00 82.13           O  
ANISOU  105  OE1 GLU A  16    10084  15287   5834   2278    776   1044       O  
ATOM    106  OE2 GLU A  16      13.718   7.798  42.909  1.00 80.49           O  
ANISOU  106  OE2 GLU A  16     9856  15245   5482   2480    628    691       O  
ATOM    107  N   GLU A  17      13.205  10.628  38.571  1.00 66.39           N  
ANISOU  107  N   GLU A  17     8172  12977   4077   2163    520    231       N  
ATOM    108  CA  GLU A  17      12.018  10.634  37.718  1.00 64.28           C  
ANISOU  108  CA  GLU A  17     7889  12646   3890   2068    609    300       C  
ATOM    109  C   GLU A  17      12.393  10.769  36.247  1.00 57.95           C  
ANISOU  109  C   GLU A  17     7138  11663   3219   1937    587    258       C  
ATOM    110  O   GLU A  17      11.894  10.024  35.396  1.00 56.64           O  
ANISOU  110  O   GLU A  17     6976  11388   3158   1810    670    417       O  
ATOM    111  CB  GLU A  17      11.073  11.760  38.140  1.00 70.25           C  
ANISOU  111  CB  GLU A  17     8599  13494   4598   2154    602    157       C  
ATOM    112  CG  GLU A  17       9.785  11.818  37.333  1.00 80.17           C  
ANISOU  112  CG  GLU A  17     9830  14699   5931   2068    693    222       C  
ATOM    113  CD  GLU A  17       8.656  11.037  37.979  1.00101.72           C  
ANISOU  113  CD  GLU A  17    12497  17538   8615   2081    812    421       C  
ATOM    114  OE1 GLU A  17       8.529   9.828  37.693  1.00107.33           O  
ANISOU  114  OE1 GLU A  17    13208  18196   9375   1987    892    638       O  
ATOM    115  OE2 GLU A  17       7.896  11.632  38.772  1.00108.77           O  
ANISOU  115  OE2 GLU A  17    13338  18565   9427   2186    821    361       O  
ATOM    116  N   ASN A  18      13.276  11.718  35.928  1.00 58.84           N  
ANISOU  116  N   ASN A  18     7282  11692   3381   1946    464     44       N  
ATOM    117  CA  ASN A  18      13.726  11.865  34.549  1.00 60.26           C  
ANISOU  117  CA  ASN A  18     7497  11602   3797   1787    419     -1       C  
ATOM    118  C   ASN A  18      14.645  10.723  34.134  1.00 59.46           C  
ANISOU  118  C   ASN A  18     7429  11385   3778   1697    424    142       C  
ATOM    119  O   ASN A  18      14.736  10.407  32.942  1.00 52.92           O  
ANISOU  119  O   ASN A  18     6623  10346   3137   1551    435    190       O  
ATOM    120  CB  ASN A  18      14.431  13.210  34.365  1.00 59.00           C  
ANISOU  120  CB  ASN A  18     7354  11367   3696   1813    282   -264       C  
ATOM    121  CG  ASN A  18      13.462  14.375  34.313  1.00 63.11           C  
ANISOU  121  CG  ASN A  18     7851  11915   4213   1854    275   -408       C  
ATOM    122  OD1 ASN A  18      12.256  14.189  34.149  1.00 67.72           O  
ANISOU  122  OD1 ASN A  18     8406  12535   4788   1834    374   -312       O  
ATOM    123  ND2 ASN A  18      13.987  15.587  34.451  1.00 60.87           N  
ANISOU  123  ND2 ASN A  18     7576  11611   3939   1913    154   -642       N  
ATOM    124  N   PHE A  19      15.324  10.094  35.095  1.00 55.50           N  
ANISOU  124  N   PHE A  19     6932  11020   3135   1789    414    208       N  
ATOM    125  CA  PHE A  19      16.229   8.991  34.784  1.00 58.99           C  
ANISOU  125  CA  PHE A  19     7406  11364   3643   1720    415    343       C  
ATOM    126  C   PHE A  19      15.471   7.811  34.187  1.00 54.43           C  
ANISOU  126  C   PHE A  19     6828  10706   3147   1607    535    580       C  
ATOM    127  O   PHE A  19      15.718   7.407  33.045  1.00 61.66           O  
ANISOU  127  O   PHE A  19     7770  11410   4246   1469    536    625       O  
ATOM    128  CB  PHE A  19      16.983   8.568  36.047  1.00 63.08           C  
ANISOU  128  CB  PHE A  19     7923  12071   3972   1859    385    373       C  
ATOM    129  CG  PHE A  19      17.969   7.452  35.832  1.00 56.10           C  
ANISOU  129  CG  PHE A  19     7072  11100   3142   1807    378    505       C  
ATOM    130  CD1 PHE A  19      19.287   7.729  35.511  1.00 55.48           C  
ANISOU  130  CD1 PHE A  19     7020  10917   3144   1789    266    380       C  
ATOM    131  CD2 PHE A  19      17.583   6.128  35.973  1.00 56.46           C  
ANISOU  131  CD2 PHE A  19     7120  11171   3161   1779    482    753       C  
ATOM    132  CE1 PHE A  19      20.199   6.707  35.321  1.00 61.67           C  
ANISOU  132  CE1 PHE A  19     7831  11627   3974   1749    259    497       C  
ATOM    133  CE2 PHE A  19      18.490   5.103  35.782  1.00 58.21           C  
ANISOU  133  CE2 PHE A  19     7374  11309   3435   1738    471    871       C  
ATOM    134  CZ  PHE A  19      19.799   5.392  35.456  1.00 55.55           C  
ANISOU  134  CZ  PHE A  19     7063  10872   3170   1727    360    740       C  
ATOM    135  N   LYS A  20      14.538   7.242  34.954  1.00 66.30           N  
ANISOU  135  N   LYS A  20     8298  12378   4514   1667    637    736       N  
ATOM    136  CA  LYS A  20      13.845   6.038  34.511  1.00 68.14           C  
ANISOU  136  CA  LYS A  20     8526  12546   4818   1565    750    976       C  
ATOM    137  C   LYS A  20      12.871   6.309  33.373  1.00 61.49           C  
ANISOU  137  C   LYS A  20     7672  11551   4139   1436    794    972       C  
ATOM    138  O   LYS A  20      12.464   5.365  32.687  1.00 53.56           O  
ANISOU  138  O   LYS A  20     6673  10428   3249   1320    863   1140       O  
ATOM    139  CB  LYS A  20      13.116   5.387  35.688  1.00 72.53           C  
ANISOU  139  CB  LYS A  20     9038  13290   5230   1649    837   1137       C  
ATOM    140  CG  LYS A  20      12.152   6.296  36.426  1.00 75.38           C  
ANISOU  140  CG  LYS A  20     9343  13794   5506   1741    851   1038       C  
ATOM    141  CD  LYS A  20      11.548   5.570  37.618  1.00 77.74           C  
ANISOU  141  CD  LYS A  20     9590  14226   5723   1808    921   1193       C  
ATOM    142  CE  LYS A  20      10.391   6.346  38.220  1.00 84.08           C  
ANISOU  142  CE  LYS A  20    10329  15162   6457   1883    955   1128       C  
ATOM    143  NZ  LYS A  20       9.731   5.581  39.315  1.00 87.22           N  
ANISOU  143  NZ  LYS A  20    10671  15690   6780   1938   1031   1296       N  
ATOM    144  N   ALA A  21      12.485   7.568  33.156  1.00 55.58           N  
ANISOU  144  N   ALA A  21     6909  10803   3407   1457    753    783       N  
ATOM    145  CA  ALA A  21      11.702   7.894  31.970  1.00 59.83           C  
ANISOU  145  CA  ALA A  21     7442  11176   4115   1333    779    760       C  
ATOM    146  C   ALA A  21      12.569   7.849  30.717  1.00 56.92           C  
ANISOU  146  C   ALA A  21     7122  10556   3948   1205    713    707       C  
ATOM    147  O   ALA A  21      12.140   7.338  29.676  1.00 50.47           O  
ANISOU  147  O   ALA A  21     6314   9579   3283   1074    758    799       O  
ATOM    148  CB  ALA A  21      11.050   9.267  32.127  1.00 56.58           C  
ANISOU  148  CB  ALA A  21     7002  10838   3659   1401    750    574       C  
ATOM    149  N   LEU A  22      13.795   8.372  30.803  1.00 62.53           N  
ANISOU  149  N   LEU A  22     7864  11234   4662   1242    605    560       N  
ATOM    150  CA  LEU A  22      14.715   8.301  29.672  1.00 49.14           C  
ANISOU  150  CA  LEU A  22     6209   9316   3146   1129    544    516       C  
ATOM    151  C   LEU A  22      15.182   6.874  29.418  1.00 48.90           C  
ANISOU  151  C   LEU A  22     6204   9210   3164   1064    584    707       C  
ATOM    152  O   LEU A  22      15.411   6.494  28.264  1.00 47.61           O  
ANISOU  152  O   LEU A  22     6068   8852   3170    941    582    740       O  
ATOM    153  CB  LEU A  22      15.916   9.214  29.913  1.00 49.16           C  
ANISOU  153  CB  LEU A  22     6227   9317   3134   1190    419    317       C  
ATOM    154  CG  LEU A  22      15.656  10.720  29.875  1.00 55.40           C  
ANISOU  154  CG  LEU A  22     7003  10114   3931   1229    354    100       C  
ATOM    155  CD1 LEU A  22      16.734  11.461  30.650  1.00 52.87           C  
ANISOU  155  CD1 LEU A  22     6686   9874   3527   1335    240    -70       C  
ATOM    156  CD2 LEU A  22      15.578  11.224  28.439  1.00 47.53           C  
ANISOU  156  CD2 LEU A  22     6023   8894   3141   1095    332     34       C  
ATOM    157  N   VAL A  23      15.341   6.078  30.478  1.00 56.30           N  
ANISOU  157  N   VAL A  23     7135  10300   3955   1150    618    831       N  
ATOM    158  CA  VAL A  23      15.708   4.677  30.305  1.00 53.08           C  
ANISOU  158  CA  VAL A  23     6752   9825   3591   1095    659   1025       C  
ATOM    159  C   VAL A  23      14.566   3.906  29.656  1.00 57.66           C  
ANISOU  159  C   VAL A  23     7322  10323   4265    987    762   1194       C  
ATOM    160  O   VAL A  23      14.798   2.988  28.859  1.00 48.99           O  
ANISOU  160  O   VAL A  23     6252   9065   3296    885    778   1303       O  
ATOM    161  CB  VAL A  23      16.121   4.069  31.659  1.00 58.91           C  
ANISOU  161  CB  VAL A  23     7485  10757   4142   1222    670   1119       C  
ATOM    162  CG1 VAL A  23      16.282   2.558  31.554  1.00 52.50           C  
ANISOU  162  CG1 VAL A  23     6696   9883   3368   1169    727   1345       C  
ATOM    163  CG2 VAL A  23      17.410   4.712  32.154  1.00 54.07           C  
ANISOU  163  CG2 VAL A  23     6887  10195   3463   1313    556    952       C  
ATOM    164  N   LEU A  24      13.319   4.274  29.963  1.00 57.44           N  
ANISOU  164  N   LEU A  24     7249  10400   4175   1009    828   1213       N  
ATOM    165  CA  LEU A  24      12.179   3.643  29.307  1.00 49.97           C  
ANISOU  165  CA  LEU A  24     6284   9376   3328    902    920   1359       C  
ATOM    166  C   LEU A  24      12.078   4.064  27.847  1.00 58.21           C  
ANISOU  166  C   LEU A  24     7347  10201   4570    774    890   1267       C  
ATOM    167  O   LEU A  24      11.583   3.303  27.008  1.00 66.59           O  
ANISOU  167  O   LEU A  24     8413  11128   5760    659    938   1386       O  
ATOM    168  CB  LEU A  24      10.888   3.980  30.049  1.00 61.70           C  
ANISOU  168  CB  LEU A  24     7707  11046   4689    966    999   1397       C  
ATOM    169  CG  LEU A  24       9.583   3.637  29.324  1.00 57.20           C  
ANISOU  169  CG  LEU A  24     7104  10403   4226    857   1085   1506       C  
ATOM    170  CD1 LEU A  24       9.460   2.133  29.086  1.00 50.89           C  
ANISOU  170  CD1 LEU A  24     6315   9521   3501    768   1149   1740       C  
ATOM    171  CD2 LEU A  24       8.378   4.172  30.080  1.00 52.46           C  
ANISOU  171  CD2 LEU A  24     6437  10001   3495    935   1152   1511       C  
ATOM    172  N   ILE A  25      12.529   5.270  27.515  1.00 47.56           N  
ANISOU  172  N   ILE A  25     6009   8812   3251    792    807   1058       N  
ATOM    173  CA  ILE A  25      12.488   5.663  26.113  1.00 46.00           C  
ANISOU  173  CA  ILE A  25     5831   8408   3238    673    778    978       C  
ATOM    174  C   ILE A  25      13.554   4.909  25.328  1.00 54.98           C  
ANISOU  174  C   ILE A  25     7017   9374   4497    594    739   1018       C  
ATOM    175  O   ILE A  25      13.340   4.529  24.171  1.00 58.27           O  
ANISOU  175  O   ILE A  25     7451   9620   5068    478    755   1059       O  
ATOM    176  CB  ILE A  25      12.624   7.189  25.975  1.00 46.24           C  
ANISOU  176  CB  ILE A  25     5857   8440   3272    712    703    752       C  
ATOM    177  CG1 ILE A  25      11.345   7.859  26.483  1.00 49.16           C  
ANISOU  177  CG1 ILE A  25     6177   8948   3554    770    753    724       C  
ATOM    178  CG2 ILE A  25      12.876   7.580  24.520  1.00 44.00           C  
ANISOU  178  CG2 ILE A  25     5601   7937   3179    594    660    669       C  
ATOM    179  CD1 ILE A  25      11.539   9.261  26.988  1.00 46.74           C  
ANISOU  179  CD1 ILE A  25     5861   8727   3171    870    679    515       C  
ATOM    180  N   ALA A  26      14.690   4.620  25.966  1.00 45.56           N  
ANISOU  180  N   ALA A  26     5845   8232   3233    661    691   1013       N  
ATOM    181  CA  ALA A  26      15.803   3.995  25.258  1.00 49.97           C  
ANISOU  181  CA  ALA A  26     6448   8638   3899    600    646   1032       C  
ATOM    182  C   ALA A  26      15.503   2.540  24.909  1.00 50.92           C  
ANISOU  182  C   ALA A  26     6584   8677   4085    527    714   1239       C  
ATOM    183  O   ALA A  26      15.735   2.106  23.773  1.00 50.40           O  
ANISOU  183  O   ALA A  26     6548   8431   4172    426    705   1259       O  
ATOM    184  CB  ALA A  26      17.079   4.103  26.090  1.00 45.62           C  
ANISOU  184  CB  ALA A  26     5910   8176   3249    700    574    968       C  
ATOM    185  N   PHE A  27      14.990   1.766  25.870  1.00 49.50           N  
ANISOU  185  N   PHE A  27     6386   8628   3792    579    781   1396       N  
ATOM    186  CA  PHE A  27      14.728   0.353  25.610  1.00 54.68           C  
ANISOU  186  CA  PHE A  27     7058   9204   4515    511    841   1600       C  
ATOM    187  C   PHE A  27      13.612   0.184  24.586  1.00 48.46           C  
ANISOU  187  C   PHE A  27     6257   8291   3864    391    894   1649       C  
ATOM    188  O   PHE A  27      13.625  -0.765  23.795  1.00 51.57           O  
ANISOU  188  O   PHE A  27     6678   8531   4385    299    909   1750       O  
ATOM    189  CB  PHE A  27      14.354  -0.368  26.905  1.00 57.94           C  
ANISOU  189  CB  PHE A  27     7446   9794   4774    594    905   1764       C  
ATOM    190  CG  PHE A  27      15.462  -0.448  27.927  1.00 59.46           C  
ANISOU  190  CG  PHE A  27     7655  10108   4830    713    856   1748       C  
ATOM    191  CD1 PHE A  27      16.722   0.083  27.686  1.00 62.21           C  
ANISOU  191  CD1 PHE A  27     8032  10405   5200    738    759   1593       C  
ATOM    192  CD2 PHE A  27      15.230  -1.073  29.143  1.00 59.97           C  
ANISOU  192  CD2 PHE A  27     7700  10344   4741    800    909   1896       C  
ATOM    193  CE1 PHE A  27      17.721  -0.003  28.641  1.00 63.38           C  
ANISOU  193  CE1 PHE A  27     8189  10670   5221    849    711   1577       C  
ATOM    194  CE2 PHE A  27      16.224  -1.161  30.101  1.00 65.18           C  
ANISOU  194  CE2 PHE A  27     8374  11125   5268    916    863   1883       C  
ATOM    195  CZ  PHE A  27      17.472  -0.627  29.849  1.00 54.74           C  
ANISOU  195  CZ  PHE A  27     7079   9748   3970    941    762   1720       C  
ATOM    196  N   ALA A  28      12.635   1.095  24.593  1.00 45.43           N  
ANISOU  196  N   ALA A  28     5832   7972   3455    394    920   1575       N  
ATOM    197  CA  ALA A  28      11.538   1.010  23.635  1.00 44.77           C  
ANISOU  197  CA  ALA A  28     5731   7781   3498    285    966   1613       C  
ATOM    198  C   ALA A  28      11.985   1.393  22.231  1.00 44.75           C  
ANISOU  198  C   ALA A  28     5765   7579   3658    195    907   1494       C  
ATOM    199  O   ALA A  28      11.431   0.889  21.247  1.00 42.52           O  
ANISOU  199  O   ALA A  28     5488   7158   3509     90    933   1554       O  
ATOM    200  CB  ALA A  28      10.376   1.896  24.083  1.00 45.28           C  
ANISOU  200  CB  ALA A  28     5739   7983   3482    326   1010   1566       C  
ATOM    201  N   GLN A  29      12.975   2.278  22.113  1.00 45.76           N  
ANISOU  201  N   GLN A  29     5915   7692   3779    235    827   1327       N  
ATOM    202  CA  GLN A  29      13.485   2.657  20.803  1.00 54.06           C  
ANISOU  202  CA  GLN A  29     6998   8564   4979    154    772   1221       C  
ATOM    203  C   GLN A  29      14.471   1.640  20.250  1.00 66.01           C  
ANISOU  203  C   GLN A  29     8557   9946   6576    109    746   1287       C  
ATOM    204  O   GLN A  29      14.715   1.629  19.039  1.00 65.16           O  
ANISOU  204  O   GLN A  29     8476   9678   6606     27    720   1244       O  
ATOM    205  CB  GLN A  29      14.142   4.038  20.870  1.00 40.76           C  
ANISOU  205  CB  GLN A  29     5313   6910   3265    208    696   1020       C  
ATOM    206  CG  GLN A  29      13.152   5.183  21.025  1.00 47.70           C  
ANISOU  206  CG  GLN A  29     6153   7865   4105    233    708    924       C  
ATOM    207  CD  GLN A  29      13.828   6.535  21.105  1.00 44.28           C  
ANISOU  207  CD  GLN A  29     5722   7449   3653    285    625    725       C  
ATOM    208  OE1 GLN A  29      14.995   6.637  21.479  1.00 45.96           O  
ANISOU  208  OE1 GLN A  29     5953   7680   3830    333    564    667       O  
ATOM    209  NE2 GLN A  29      13.096   7.585  20.751  1.00 49.61           N  
ANISOU  209  NE2 GLN A  29     6378   8116   4356    276    620    621       N  
ATOM    210  N   TYR A  30      15.037   0.788  21.105  1.00 72.38           N  
ANISOU  210  N   TYR A  30     9376  10822   7303    167    752   1390       N  
ATOM    211  CA  TYR A  30      15.936  -0.271  20.659  1.00 74.08           C  
ANISOU  211  CA  TYR A  30     9634  10919   7592    134    730   1464       C  
ATOM    212  C   TYR A  30      15.159  -1.529  20.285  1.00 71.39           C  
ANISOU  212  C   TYR A  30     9302  10493   7331     57    794   1642       C  
ATOM    213  O   TYR A  30      15.269  -2.026  19.160  1.00 82.44           O  
ANISOU  213  O   TYR A  30    10731  11724   8871    -29    782   1654       O  
ATOM    214  CB  TYR A  30      16.969  -0.579  21.747  1.00 84.15           C  
ANISOU  214  CB  TYR A  30    10920  12306   8747    237    700   1487       C  
ATOM    215  CG  TYR A  30      18.163   0.336  21.706  1.00 91.99           C  
ANISOU  215  CG  TYR A  30    11922  13307   9724    284    613   1315       C  
ATOM    216  CD1 TYR A  30      18.497   1.008  20.543  1.00 95.58           C  
ANISOU  216  CD1 TYR A  30    12386  13628  10300    216    568   1187       C  
ATOM    217  CD2 TYR A  30      18.958   0.529  22.828  1.00 94.49           C  
ANISOU  217  CD2 TYR A  30    12231  13764   9905    394    575   1282       C  
ATOM    218  CE1 TYR A  30      19.581   1.849  20.497  1.00 98.63           C  
ANISOU  218  CE1 TYR A  30    12774  14018  10682    251    490   1038       C  
ATOM    219  CE2 TYR A  30      20.053   1.368  22.790  1.00 96.71           C  
ANISOU  219  CE2 TYR A  30    12515  14050  10182    431    491   1123       C  
ATOM    220  CZ  TYR A  30      20.362   2.024  21.619  1.00103.01           C  
ANISOU  220  CZ  TYR A  30    13319  14709  11110    356    450   1004       C  
ATOM    221  OH  TYR A  30      21.451   2.865  21.569  1.00107.69           O  
ANISOU  221  OH  TYR A  30    13908  15302  11708    385    367    852       O  
ATOM    222  N   LEU A  31      14.376  -2.053  21.221  1.00 66.97           N  
ANISOU  222  N   LEU A  31     8713  10048   6684     88    860   1781       N  
ATOM    223  CA  LEU A  31      13.509  -3.202  20.983  1.00 71.04           C  
ANISOU  223  CA  LEU A  31     9225  10494   7273     13    924   1959       C  
ATOM    224  C   LEU A  31      12.080  -2.670  20.907  1.00 63.57           C  
ANISOU  224  C   LEU A  31     8227   9600   6329    -25    981   1962       C  
ATOM    225  O   LEU A  31      11.391  -2.540  21.921  1.00 56.07           O  
ANISOU  225  O   LEU A  31     7232   8814   5259     32   1035   2026       O  
ATOM    226  CB  LEU A  31      13.674  -4.254  22.074  1.00 67.33           C  
ANISOU  226  CB  LEU A  31     8757  10112   6712     70    959   2134       C  
ATOM    227  CG  LEU A  31      14.807  -5.251  21.826  1.00 74.29           C  
ANISOU  227  CG  LEU A  31     9696  10881   7652     68    916   2190       C  
ATOM    228  CD1 LEU A  31      15.108  -6.055  23.081  1.00 82.38           C  
ANISOU  228  CD1 LEU A  31    10722  12024   8555    152    941   2340       C  
ATOM    229  CD2 LEU A  31      14.464  -6.169  20.662  1.00 77.83           C  
ANISOU  229  CD2 LEU A  31    10171  11124   8278    -49    924   2264       C  
ATOM    230  N   GLN A  32      11.644  -2.356  19.689  1.00 49.70           N  
ANISOU  230  N   GLN A  32     6473   7706   4705   -116    970   1891       N  
ATOM    231  CA  GLN A  32      10.340  -1.747  19.466  1.00 47.28           C  
ANISOU  231  CA  GLN A  32     6117   7434   4412   -154   1014   1870       C  
ATOM    232  C   GLN A  32       9.195  -2.751  19.486  1.00 42.88           C  
ANISOU  232  C   GLN A  32     5528   6860   3904   -222   1089   2052       C  
ATOM    233  O   GLN A  32       8.032  -2.334  19.519  1.00 52.90           O  
ANISOU  233  O   GLN A  32     6743   8190   5165   -243   1137   2060       O  
ATOM    234  CB  GLN A  32      10.337  -1.000  18.127  1.00 40.64           C  
ANISOU  234  CB  GLN A  32     5292   6454   3694   -222    969   1723       C  
ATOM    235  CG  GLN A  32      11.410   0.074  18.003  1.00 39.87           C  
ANISOU  235  CG  GLN A  32     5220   6362   3567   -168    895   1542       C  
ATOM    236  CD  GLN A  32      11.767   0.382  16.557  1.00 49.14           C  
ANISOU  236  CD  GLN A  32     6427   7361   4884   -246    845   1439       C  
ATOM    237  OE1 GLN A  32      12.837   0.009  16.076  1.00 42.01           O  
ANISOU  237  OE1 GLN A  32     5568   6362   4034   -256    799   1419       O  
ATOM    238  NE2 GLN A  32      10.868   1.066  15.858  1.00 42.44           N  
ANISOU  238  NE2 GLN A  32     5555   6477   4094   -295    857   1377       N  
ATOM    239  N   GLN A  33       9.485  -4.052  19.473  1.00 60.23           N  
ANISOU  239  N   GLN A  33     7754   8975   6157   -258   1098   2198       N  
ATOM    240  CA  GLN A  33       8.453  -5.077  19.380  1.00 62.02           C  
ANISOU  240  CA  GLN A  33     7952   9155   6458   -338   1160   2374       C  
ATOM    241  C   GLN A  33       8.246  -5.837  20.685  1.00 72.85           C  
ANISOU  241  C   GLN A  33     9297  10663   7721   -284   1221   2557       C  
ATOM    242  O   GLN A  33       7.532  -6.846  20.695  1.00 72.28           O  
ANISOU  242  O   GLN A  33     9204  10544   7714   -351   1270   2727       O  
ATOM    243  CB  GLN A  33       8.786  -6.056  18.251  1.00 67.94           C  
ANISOU  243  CB  GLN A  33     8753   9682   7379   -432   1124   2412       C  
ATOM    244  CG  GLN A  33      10.117  -6.767  18.424  1.00 75.93           C  
ANISOU  244  CG  GLN A  33     9828  10638   8386   -390   1077   2439       C  
ATOM    245  CD  GLN A  33      10.752  -7.148  17.100  1.00 83.15           C  
ANISOU  245  CD  GLN A  33    10800  11343   9450   -456   1015   2371       C  
ATOM    246  OE1 GLN A  33      10.189  -6.903  16.033  1.00 80.12           O  
ANISOU  246  OE1 GLN A  33    10411  10855   9175   -535   1005   2307       O  
ATOM    247  NE2 GLN A  33      11.932  -7.755  17.165  1.00 84.48           N  
ANISOU  247  NE2 GLN A  33    11022  11456   9621   -418    971   2385       N  
ATOM    248  N   CYS A  34       8.845  -5.382  21.784  1.00 75.71           N  
ANISOU  248  N   CYS A  34     9657  11191   7918   -166   1217   2528       N  
ATOM    249  CA  CYS A  34       8.607  -6.090  23.030  1.00 76.00           C  
ANISOU  249  CA  CYS A  34     9666  11371   7841   -110   1279   2710       C  
ATOM    250  C   CYS A  34       7.452  -5.453  23.796  1.00 69.91           C  
ANISOU  250  C   CYS A  34     8815  10792   6956    -71   1352   2734       C  
ATOM    251  O   CYS A  34       7.247  -4.238  23.723  1.00 68.63           O  
ANISOU  251  O   CYS A  34     8631  10702   6743    -33   1336   2572       O  
ATOM    252  CB  CYS A  34       9.865  -6.089  23.903  1.00 84.15           C  
ANISOU  252  CB  CYS A  34    10736  12493   8744      6   1239   2688       C  
ATOM    253  SG  CYS A  34      10.903  -7.556  23.694  1.00 99.68           S  
ANISOU  253  SG  CYS A  34    12774  14301  10799    -19   1203   2816       S  
ATOM    254  N   PRO A  35       6.678  -6.250  24.534  1.00 69.73           N  
ANISOU  254  N   PRO A  35     8751  10820   6924    -78   1410   2886       N  
ATOM    255  CA  PRO A  35       5.507  -5.706  25.233  1.00 66.12           C  
ANISOU  255  CA  PRO A  35     8214  10522   6388    -44   1468   2884       C  
ATOM    256  C   PRO A  35       5.892  -4.678  26.288  1.00 62.64           C  
ANISOU  256  C   PRO A  35     7757  10306   5739    104   1466   2789       C  
ATOM    257  O   PRO A  35       7.041  -4.590  26.727  1.00 63.96           O  
ANISOU  257  O   PRO A  35     7970  10520   5811    187   1423   2753       O  
ATOM    258  CB  PRO A  35       4.859  -6.944  25.868  1.00 70.49           C  
ANISOU  258  CB  PRO A  35     8738  11054   6990    -76   1509   3055       C  
ATOM    259  CG  PRO A  35       5.934  -7.982  25.886  1.00 69.23           C  
ANISOU  259  CG  PRO A  35     8648  10781   6874    -80   1468   3131       C  
ATOM    260  CD  PRO A  35       6.787  -7.710  24.690  1.00 65.06           C  
ANISOU  260  CD  PRO A  35     8184  10109   6426   -125   1409   3036       C  
ATOM    261  N   PHE A  36       4.891  -3.892  26.696  1.00 63.07           N  
ANISOU  261  N   PHE A  36     7742  10500   5720    140   1508   2742       N  
ATOM    262  CA  PHE A  36       5.137  -2.758  27.583  1.00 52.60           C  
ANISOU  262  CA  PHE A  36     6398   9383   4203    281   1500   2620       C  
ATOM    263  C   PHE A  36       5.614  -3.210  28.956  1.00 61.46           C  
ANISOU  263  C   PHE A  36     7520  10637   5195    390   1501   2687       C  
ATOM    264  O   PHE A  36       6.570  -2.648  29.503  1.00 61.91           O  
ANISOU  264  O   PHE A  36     7608  10794   5121    499   1455   2591       O  
ATOM    265  CB  PHE A  36       3.868  -1.912  27.711  1.00 53.65           C  
ANISOU  265  CB  PHE A  36     6455   9628   4300    295   1547   2564       C  
ATOM    266  CG  PHE A  36       3.842  -1.036  28.931  1.00 56.69           C  
ANISOU  266  CG  PHE A  36     6806  10244   4490    449   1549   2477       C  
ATOM    267  CD1 PHE A  36       4.606   0.118  28.988  1.00 55.88           C  
ANISOU  267  CD1 PHE A  36     6733  10223   4275    541   1495   2298       C  
ATOM    268  CD2 PHE A  36       3.048  -1.363  30.021  1.00 59.71           C  
ANISOU  268  CD2 PHE A  36     7125  10760   4802    502   1603   2571       C  
ATOM    269  CE1 PHE A  36       4.583   0.928  30.109  1.00 62.33           C  
ANISOU  269  CE1 PHE A  36     7521  11243   4919    686   1487   2203       C  
ATOM    270  CE2 PHE A  36       3.020  -0.557  31.145  1.00 58.89           C  
ANISOU  270  CE2 PHE A  36     6989  10868   4520    648   1601   2486       C  
ATOM    271  CZ  PHE A  36       3.790   0.590  31.189  1.00 59.67           C  
ANISOU  271  CZ  PHE A  36     7121  11038   4513    742   1540   2297       C  
ATOM    272  N   GLU A  37       4.960  -4.220  29.532  1.00 56.70           N  
ANISOU  272  N   GLU A  37     6882  10037   4626    364   1550   2848       N  
ATOM    273  CA  GLU A  37       5.271  -4.618  30.900  1.00 62.66           C  
ANISOU  273  CA  GLU A  37     7625  10934   5250    472   1560   2920       C  
ATOM    274  C   GLU A  37       6.617  -5.320  31.017  1.00 67.24           C  
ANISOU  274  C   GLU A  37     8278  11443   5826    495   1508   2959       C  
ATOM    275  O   GLU A  37       7.117  -5.483  32.134  1.00 62.27           O  
ANISOU  275  O   GLU A  37     7649  10942   5070    602   1502   2987       O  
ATOM    276  CB  GLU A  37       4.164  -5.507  31.461  1.00 68.11           C  
ANISOU  276  CB  GLU A  37     8252  11647   5980    434   1630   3089       C  
ATOM    277  CG  GLU A  37       2.806  -4.822  31.515  1.00 83.03           C  
ANISOU  277  CG  GLU A  37    10059  13635   7855    429   1684   3058       C  
ATOM    278  CD  GLU A  37       1.682  -5.705  31.023  1.00 97.38           C  
ANISOU  278  CD  GLU A  37    11833  15336   9831    297   1735   3196       C  
ATOM    279  OE1 GLU A  37       0.664  -5.158  30.552  1.00101.29           O  
ANISOU  279  OE1 GLU A  37    12276  15842  10368    253   1764   3153       O  
ATOM    280  OE2 GLU A  37       1.812  -6.944  31.110  1.00104.22           O  
ANISOU  280  OE2 GLU A  37    12718  16102  10780    240   1742   3343       O  
ATOM    281  N   ASP A  38       7.218  -5.738  29.902  1.00 62.80           N  
ANISOU  281  N   ASP A  38     7777  10686   5399    402   1470   2959       N  
ATOM    282  CA  ASP A  38       8.570  -6.279  29.961  1.00 61.05           C  
ANISOU  282  CA  ASP A  38     7626  10404   5167    434   1415   2977       C  
ATOM    283  C   ASP A  38       9.616  -5.176  30.054  1.00 69.56           C  
ANISOU  283  C   ASP A  38     8736  11577   6117    535   1353   2805       C  
ATOM    284  O   ASP A  38      10.696  -5.397  30.614  1.00 75.86           O  
ANISOU  284  O   ASP A  38     9572  12416   6835    615   1309   2802       O  
ATOM    285  CB  ASP A  38       8.844  -7.162  28.742  1.00 74.63           C  
ANISOU  285  CB  ASP A  38     9398  11879   7078    304   1393   3039       C  
ATOM    286  CG  ASP A  38       8.219  -8.538  28.865  1.00 79.71           C  
ANISOU  286  CG  ASP A  38    10030  12420   7838    226   1431   3220       C  
ATOM    287  OD1 ASP A  38       7.813  -8.911  29.985  1.00 83.77           O  
ANISOU  287  OD1 ASP A  38    10502  13055   8270    282   1471   3314       O  
ATOM    288  OD2 ASP A  38       8.139  -9.251  27.843  1.00 81.52           O  
ANISOU  288  OD2 ASP A  38    10290  12446   8239    110   1419   3267       O  
ATOM    289  N   HIS A  39       9.315  -3.990  29.521  1.00 69.23           N  
ANISOU  289  N   HIS A  39     8677  11571   6055    534   1345   2658       N  
ATOM    290  CA  HIS A  39      10.264  -2.883  29.573  1.00 70.92           C  
ANISOU  290  CA  HIS A  39     8920  11873   6154    626   1281   2481       C  
ATOM    291  C   HIS A  39      10.288  -2.227  30.949  1.00 66.01           C  
ANISOU  291  C   HIS A  39     8263  11477   5340    776   1275   2410       C  
ATOM    292  O   HIS A  39      11.360  -1.866  31.447  1.00 57.56           O  
ANISOU  292  O   HIS A  39     7224  10484   4162    875   1212   2320       O  
ATOM    293  CB  HIS A  39       9.922  -1.848  28.499  1.00 70.11           C  
ANISOU  293  CB  HIS A  39     8814  11671   6153    560   1249   2303       C  
ATOM    294  CG  HIS A  39      10.307  -2.262  27.113  1.00 72.24           C  
ANISOU  294  CG  HIS A  39     9132  11683   6632    430   1206   2280       C  
ATOM    295  ND1 HIS A  39       9.477  -2.082  26.026  1.00 74.38           N  
ANISOU  295  ND1 HIS A  39     9389  11823   7049    318   1223   2253       N  
ATOM    296  CD2 HIS A  39      11.433  -2.840  26.634  1.00 74.84           C  
ANISOU  296  CD2 HIS A  39     9523  11869   7043    403   1146   2278       C  
ATOM    297  CE1 HIS A  39      10.076  -2.534  24.938  1.00 71.37           C  
ANISOU  297  CE1 HIS A  39     9060  11231   6827    227   1175   2234       C  
ATOM    298  NE2 HIS A  39      11.264  -2.999  25.279  1.00 74.81           N  
ANISOU  298  NE2 HIS A  39     9542  11655   7227    277   1129   2248       N  
ATOM    299  N   VAL A  40       9.120  -2.065  31.577  1.00 74.45           N  
ANISOU  299  N   VAL A  40     9265  12655   6368    798   1335   2444       N  
ATOM    300  CA  VAL A  40       9.068  -1.406  32.879  1.00 78.09           C  
ANISOU  300  CA  VAL A  40     9688  13333   6650    945   1329   2371       C  
ATOM    301  C   VAL A  40       9.797  -2.232  33.934  1.00 77.43           C  
ANISOU  301  C   VAL A  40     9619  13314   6488   1023   1316   2469       C  
ATOM    302  O   VAL A  40      10.387  -1.674  34.869  1.00 76.41           O  
ANISOU  302  O   VAL A  40     9488  13336   6208   1156   1273   2373       O  
ATOM    303  CB  VAL A  40       7.605  -1.123  33.276  1.00 84.33           C  
ANISOU  303  CB  VAL A  40    10398  14222   7420    948   1402   2401       C  
ATOM    304  CG1 VAL A  40       6.778  -2.391  33.212  1.00 88.20           C  
ANISOU  304  CG1 VAL A  40    10859  14626   8025    848   1474   2614       C  
ATOM    305  CG2 VAL A  40       7.525  -0.494  34.664  1.00 67.84           C  
ANISOU  305  CG2 VAL A  40     8267  12361   5147   1107   1396   2333       C  
ATOM    306  N   LYS A  41       9.791  -3.562  33.804  1.00 58.48           N  
ANISOU  306  N   LYS A  41     7234  10795   4189    945   1347   2653       N  
ATOM    307  CA  LYS A  41      10.558  -4.384  34.735  1.00 63.74           C  
ANISOU  307  CA  LYS A  41     7921  11510   4789   1016   1332   2749       C  
ATOM    308  C   LYS A  41      12.055  -4.224  34.500  1.00 63.82           C  
ANISOU  308  C   LYS A  41     7999  11480   4769   1060   1244   2655       C  
ATOM    309  O   LYS A  41      12.841  -4.226  35.455  1.00 59.79           O  
ANISOU  309  O   LYS A  41     7497  11085   4135   1175   1206   2633       O  
ATOM    310  CB  LYS A  41      10.153  -5.854  34.616  1.00 73.64           C  
ANISOU  310  CB  LYS A  41     9176  12636   6169    919   1383   2965       C  
ATOM    311  CG  LYS A  41       8.657  -6.117  34.673  1.00 86.32           C  
ANISOU  311  CG  LYS A  41    10713  14253   7833    853   1466   3067       C  
ATOM    312  CD  LYS A  41       7.975  -5.373  35.811  1.00 94.35           C  
ANISOU  312  CD  LYS A  41    11658  15499   8691    968   1500   3023       C  
ATOM    313  CE  LYS A  41       6.490  -5.189  35.527  1.00 93.02           C  
ANISOU  313  CE  LYS A  41    11420  15337   8585    898   1570   3058       C  
ATOM    314  NZ  LYS A  41       5.993  -6.136  34.489  1.00 85.73           N  
ANISOU  314  NZ  LYS A  41    10509  14202   7862    734   1598   3180       N  
ATOM    315  N   LEU A  42      12.468  -4.094  33.237  1.00 69.49           N  
ANISOU  315  N   LEU A  42     8763  12038   5601    970   1211   2600       N  
ATOM    316  CA  LEU A  42      13.871  -3.814  32.947  1.00 64.10           C  
ANISOU  316  CA  LEU A  42     8139  11327   4888   1012   1126   2496       C  
ATOM    317  C   LEU A  42      14.276  -2.449  33.489  1.00 66.41           C  
ANISOU  317  C   LEU A  42     8419  11787   5028   1134   1068   2290       C  
ATOM    318  O   LEU A  42      15.392  -2.277  33.992  1.00 66.92           O  
ANISOU  318  O   LEU A  42     8509  11916   5000   1227    998   2216       O  
ATOM    319  CB  LEU A  42      14.124  -3.888  31.441  1.00 64.59           C  
ANISOU  319  CB  LEU A  42     8246  11191   5104    890   1108   2479       C  
ATOM    320  CG  LEU A  42      14.135  -5.277  30.800  1.00 64.86           C  
ANISOU  320  CG  LEU A  42     8313  11030   5302    780   1132   2654       C  
ATOM    321  CD1 LEU A  42      14.720  -5.212  29.396  1.00 56.62           C  
ANISOU  321  CD1 LEU A  42     7317   9770   4427    681   1074   2562       C  
ATOM    322  CD2 LEU A  42      14.906  -6.266  31.661  1.00 65.95           C  
ANISOU  322  CD2 LEU A  42     8474  11189   5392    846   1113   2763       C  
ATOM    323  N   VAL A  43      13.375  -1.469  33.397  1.00 61.78           N  
ANISOU  323  N   VAL A  43     7791  11269   4416   1136   1093   2190       N  
ATOM    324  CA  VAL A  43      13.651  -0.142  33.939  1.00 62.16           C  
ANISOU  324  CA  VAL A  43     7823  11469   4325   1252   1035   1983       C  
ATOM    325  C   VAL A  43      13.779  -0.202  35.457  1.00 61.22           C  
ANISOU  325  C   VAL A  43     7673  11533   4055   1391   1028   1994       C  
ATOM    326  O   VAL A  43      14.630   0.473  36.049  1.00 59.65           O  
ANISOU  326  O   VAL A  43     7484  11436   3743   1502    950   1849       O  
ATOM    327  CB  VAL A  43      12.554   0.844  33.493  1.00 64.22           C  
ANISOU  327  CB  VAL A  43     8046  11753   4603   1222   1067   1886       C  
ATOM    328  CG1 VAL A  43      12.609   2.122  34.310  1.00 70.34           C  
ANISOU  328  CG1 VAL A  43     8794  12701   5229   1358   1016   1689       C  
ATOM    329  CG2 VAL A  43      12.687   1.147  32.006  1.00 59.05           C  
ANISOU  329  CG2 VAL A  43     7423  10876   4137   1091   1032   1797       C  
ATOM    330  N   ASN A  44      12.948  -1.020  36.108  1.00 61.46           N  
ANISOU  330  N   ASN A  44     7663  11606   4083   1386   1107   2164       N  
ATOM    331  CA  ASN A  44      13.008  -1.145  37.562  1.00 69.10           C  
ANISOU  331  CA  ASN A  44     8597  12753   4907   1517   1110   2192       C  
ATOM    332  C   ASN A  44      14.352  -1.704  38.012  1.00 68.40           C  
ANISOU  332  C   ASN A  44     8552  12665   4771   1578   1048   2213       C  
ATOM    333  O   ASN A  44      14.980  -1.178  38.938  1.00 62.58           O  
ANISOU  333  O   ASN A  44     7808  12071   3898   1709    990   2105       O  
ATOM    334  CB  ASN A  44      11.869  -2.033  38.061  1.00 74.65           C  
ANISOU  334  CB  ASN A  44     9248  13483   5633   1484   1210   2392       C  
ATOM    335  CG  ASN A  44      10.511  -1.387  37.897  1.00 79.90           C  
ANISOU  335  CG  ASN A  44     9853  14194   6310   1456   1269   2361       C  
ATOM    336  OD1 ASN A  44      10.398  -0.164  37.808  1.00 71.92           O  
ANISOU  336  OD1 ASN A  44     8831  13252   5243   1507   1233   2178       O  
ATOM    337  ND2 ASN A  44       9.468  -2.208  37.855  1.00 82.24           N  
ANISOU  337  ND2 ASN A  44    10111  14452   6685   1376   1355   2536       N  
ATOM    338  N   GLU A  45      14.805  -2.782  37.370  1.00 67.07           N  
ANISOU  338  N   GLU A  45     8430  12337   4718   1487   1055   2348       N  
ATOM    339  CA  GLU A  45      16.073  -3.392  37.754  1.00 71.50           C  
ANISOU  339  CA  GLU A  45     9033  12890   5243   1542    997   2378       C  
ATOM    340  C   GLU A  45      17.257  -2.493  37.417  1.00 71.10           C  
ANISOU  340  C   GLU A  45     9019  12844   5151   1592    891   2177       C  
ATOM    341  O   GLU A  45      18.277  -2.525  38.115  1.00 75.21           O  
ANISOU  341  O   GLU A  45     9554  13442   5581   1691    826   2133       O  
ATOM    342  CB  GLU A  45      16.225  -4.751  37.073  1.00 68.09           C  
ANISOU  342  CB  GLU A  45     8641  12272   4957   1430   1028   2565       C  
ATOM    343  CG  GLU A  45      15.056  -5.703  37.278  1.00 76.53           C  
ANISOU  343  CG  GLU A  45     9675  13309   6094   1362   1125   2764       C  
ATOM    344  CD  GLU A  45      15.086  -6.868  36.305  1.00 76.50           C  
ANISOU  344  CD  GLU A  45     9714  13083   6269   1227   1146   2912       C  
ATOM    345  OE1 GLU A  45      14.643  -7.975  36.679  1.00 77.44           O  
ANISOU  345  OE1 GLU A  45     9823  13166   6436   1194   1199   3093       O  
ATOM    346  OE2 GLU A  45      15.552  -6.674  35.162  1.00 73.02           O  
ANISOU  346  OE2 GLU A  45     9318  12503   5925   1155   1108   2844       O  
ATOM    347  N   VAL A  46      17.145  -1.690  36.356  1.00 58.77           N  
ANISOU  347  N   VAL A  46     7471  11201   3656   1524    870   2054       N  
ATOM    348  CA  VAL A  46      18.219  -0.764  36.011  1.00 60.10           C  
ANISOU  348  CA  VAL A  46     7670  11375   3789   1566    766   1854       C  
ATOM    349  C   VAL A  46      18.243   0.409  36.984  1.00 60.94           C  
ANISOU  349  C   VAL A  46     7740  11666   3750   1698    715   1670       C  
ATOM    350  O   VAL A  46      19.313   0.844  37.428  1.00 60.51           O  
ANISOU  350  O   VAL A  46     7698  11676   3617   1788    621   1541       O  
ATOM    351  CB  VAL A  46      18.071  -0.294  34.552  1.00 58.87           C  
ANISOU  351  CB  VAL A  46     7536  11048   3785   1440    756   1773       C  
ATOM    352  CG1 VAL A  46      18.901   0.959  34.300  1.00 64.59           C  
ANISOU  352  CG1 VAL A  46     8266  11745   4530   1468    640   1508       C  
ATOM    353  CG2 VAL A  46      18.478  -1.404  33.595  1.00 58.51           C  
ANISOU  353  CG2 VAL A  46     7533  10782   3915   1320    764   1899       C  
ATOM    354  N   THR A  47      17.067   0.935  37.337  1.00 62.20           N  
ANISOU  354  N   THR A  47     7850  11910   3873   1714    770   1650       N  
ATOM    355  CA  THR A  47      17.002   2.022  38.308  1.00 63.09           C  
ANISOU  355  CA  THR A  47     7926  12196   3850   1846    723   1479       C  
ATOM    356  C   THR A  47      17.428   1.559  39.696  1.00 68.34           C  
ANISOU  356  C   THR A  47     8571  13005   4391   1970    712   1533       C  
ATOM    357  O   THR A  47      17.990   2.347  40.466  1.00 68.82           O  
ANISOU  357  O   THR A  47     8619  13187   4344   2090    633   1371       O  
ATOM    358  CB  THR A  47      15.589   2.604  38.352  1.00 60.59           C  
ANISOU  358  CB  THR A  47     7558  11934   3528   1836    792   1462       C  
ATOM    359  OG1 THR A  47      15.134   2.857  37.017  1.00 63.15           O  
ANISOU  359  OG1 THR A  47     7900  12114   3978   1709    815   1444       O  
ATOM    360  CG2 THR A  47      15.567   3.906  39.140  1.00 61.43           C  
ANISOU  360  CG2 THR A  47     7634  12194   3514   1966    728   1248       C  
ATOM    361  N   GLU A  48      17.178   0.291  40.032  1.00 68.28           N  
ANISOU  361  N   GLU A  48     8559  12982   4403   1944    785   1756       N  
ATOM    362  CA  GLU A  48      17.595  -0.222  41.333  1.00 67.78           C  
ANISOU  362  CA  GLU A  48     8477  13053   4222   2061    778   1822       C  
ATOM    363  C   GLU A  48      19.113  -0.330  41.422  1.00 64.74           C  
ANISOU  363  C   GLU A  48     8136  12652   3811   2112    679   1752       C  
ATOM    364  O   GLU A  48      19.702  -0.021  42.465  1.00 66.02           O  
ANISOU  364  O   GLU A  48     8280  12954   3849   2242    622   1670       O  
ATOM    365  CB  GLU A  48      16.942  -1.579  41.597  1.00 65.87           C  
ANISOU  365  CB  GLU A  48     8223  12784   4023   2010    880   2081       C  
ATOM    366  CG  GLU A  48      15.528  -1.489  42.149  1.00 70.17           C  
ANISOU  366  CG  GLU A  48     8700  13430   4529   2023    971   2151       C  
ATOM    367  CD  GLU A  48      14.959  -2.846  42.516  1.00 79.03           C  
ANISOU  367  CD  GLU A  48     9806  14534   5690   1979   1062   2405       C  
ATOM    368  OE1 GLU A  48      15.496  -3.865  42.034  1.00 81.37           O  
ANISOU  368  OE1 GLU A  48    10148  14690   6080   1904   1064   2530       O  
ATOM    369  OE2 GLU A  48      13.976  -2.893  43.286  1.00 79.95           O  
ANISOU  369  OE2 GLU A  48     9861  14772   5743   2021   1130   2477       O  
ATOM    370  N   PHE A  49      19.763  -0.766  40.340  1.00 63.23           N  
ANISOU  370  N   PHE A  49     7997  12291   3735   2013    654   1782       N  
ATOM    371  CA  PHE A  49      21.219  -0.853  40.341  1.00 62.99           C  
ANISOU  371  CA  PHE A  49     8004  12241   3688   2058    556   1712       C  
ATOM    372  C   PHE A  49      21.863   0.526  40.377  1.00 69.30           C  
ANISOU  372  C   PHE A  49     8799  13104   4428   2126    446   1448       C  
ATOM    373  O   PHE A  49      22.928   0.696  40.982  1.00 68.86           O  
ANISOU  373  O   PHE A  49     8746  13119   4300   2219    358   1357       O  
ATOM    374  CB  PHE A  49      21.701  -1.631  39.116  1.00 64.77           C  
ANISOU  374  CB  PHE A  49     8285  12269   4057   1936    558   1807       C  
ATOM    375  CG  PHE A  49      23.186  -1.555  38.896  1.00 64.27           C  
ANISOU  375  CG  PHE A  49     8257  12174   3990   1970    450   1710       C  
ATOM    376  CD1 PHE A  49      24.053  -2.294  39.683  1.00 73.89           C  
ANISOU  376  CD1 PHE A  49     9484  13444   5149   2051    418   1779       C  
ATOM    377  CD2 PHE A  49      23.714  -0.741  37.908  1.00 59.37           C  
ANISOU  377  CD2 PHE A  49     7657  11475   3425   1924    379   1548       C  
ATOM    378  CE1 PHE A  49      25.420  -2.225  39.487  1.00 72.35           C  
ANISOU  378  CE1 PHE A  49     9314  13223   4952   2085    316   1688       C  
ATOM    379  CE2 PHE A  49      25.080  -0.667  37.708  1.00 67.07           C  
ANISOU  379  CE2 PHE A  49     8657  12426   4400   1955    276   1458       C  
ATOM    380  CZ  PHE A  49      25.933  -1.411  38.498  1.00 61.78           C  
ANISOU  380  CZ  PHE A  49     7993  11808   3673   2036    245   1527       C  
ATOM    381  N   ALA A  50      21.235   1.520  39.744  1.00 71.19           N  
ANISOU  381  N   ALA A  50     9028  13316   4704   2080    445   1320       N  
ATOM    382  CA  ALA A  50      21.815   2.858  39.702  1.00 69.57           C  
ANISOU  382  CA  ALA A  50     8819  13150   4463   2134    335   1062       C  
ATOM    383  C   ALA A  50      21.893   3.476  41.093  1.00 69.08           C  
ANISOU  383  C   ALA A  50     8715  13275   4258   2286    290    949       C  
ATOM    384  O   ALA A  50      22.844   4.203  41.405  1.00 63.21           O  
ANISOU  384  O   ALA A  50     7971  12574   3471   2359    176    766       O  
ATOM    385  CB  ALA A  50      21.004   3.753  38.766  1.00 64.03           C  
ANISOU  385  CB  ALA A  50     8115  12379   3832   2054    352    961       C  
ATOM    386  N   LYS A  51      20.904   3.196  41.944  1.00 64.37           N  
ANISOU  386  N   LYS A  51     8078  12789   3591   2336    374   1055       N  
ATOM    387  CA  LYS A  51      20.901   3.781  43.281  1.00 66.19           C  
ANISOU  387  CA  LYS A  51     8264  13204   3681   2488    338    954       C  
ATOM    388  C   LYS A  51      22.012   3.209  44.152  1.00 67.38           C  
ANISOU  388  C   LYS A  51     8420  13428   3753   2581    284    984       C  
ATOM    389  O   LYS A  51      22.483   3.885  45.073  1.00 68.57           O  
ANISOU  389  O   LYS A  51     8545  13706   3803   2706    207    836       O  
ATOM    390  CB  LYS A  51      19.537   3.575  43.940  1.00 67.42           C  
ANISOU  390  CB  LYS A  51     8371  13465   3780   2517    447   1073       C  
ATOM    391  CG  LYS A  51      18.449   4.474  43.373  1.00 66.66           C  
ANISOU  391  CG  LYS A  51     8255  13346   3727   2470    479    984       C  
ATOM    392  CD  LYS A  51      17.123   4.266  44.081  1.00 81.53           C  
ANISOU  392  CD  LYS A  51    10081  15345   5550   2507    583   1101       C  
ATOM    393  CE  LYS A  51      16.247   3.280  43.327  1.00 84.91           C  
ANISOU  393  CE  LYS A  51    10514  15663   6086   2369    700   1322       C  
ATOM    394  NZ  LYS A  51      14.799   3.527  43.572  1.00 87.12           N  
ANISOU  394  NZ  LYS A  51    10737  16020   6347   2373    787   1367       N  
ATOM    395  N   THR A  52      22.443   1.974  43.882  1.00 67.14           N  
ANISOU  395  N   THR A  52     8421  13316   3771   2525    320   1170       N  
ATOM    396  CA  THR A  52      23.592   1.429  44.598  1.00 73.60           C  
ANISOU  396  CA  THR A  52     9249  14190   4526   2609    262   1192       C  
ATOM    397  C   THR A  52      24.871   2.160  44.213  1.00 72.91           C  
ANISOU  397  C   THR A  52     9183  14060   4461   2624    126    986       C  
ATOM    398  O   THR A  52      25.760   2.355  45.051  1.00 71.35           O  
ANISOU  398  O   THR A  52     8972  13960   4179   2733     44    895       O  
ATOM    399  CB  THR A  52      23.729  -0.069  44.324  1.00 72.01           C  
ANISOU  399  CB  THR A  52     9079  13895   4386   2541    330   1438       C  
ATOM    400  OG1 THR A  52      24.346  -0.269  43.046  1.00 73.96           O  
ANISOU  400  OG1 THR A  52     9377  13965   4762   2429    296   1433       O  
ATOM    401  CG2 THR A  52      22.363  -0.741  44.334  1.00 68.42           C  
ANISOU  401  CG2 THR A  52     8606  13431   3961   2480    464   1636       C  
ATOM    402  N   CYS A  53      24.978   2.575  42.948  1.00 65.88           N  
ANISOU  402  N   CYS A  53     8322  13024   3686   2513     99    911       N  
ATOM    403  CA  CYS A  53      26.136   3.347  42.510  1.00 70.65           C  
ANISOU  403  CA  CYS A  53     8939  13581   4322   2516    -32    708       C  
ATOM    404  C   CYS A  53      26.070   4.786  43.007  1.00 74.75           C  
ANISOU  404  C   CYS A  53     9423  14191   4786   2595   -114    461       C  
ATOM    405  O   CYS A  53      27.113   5.406  43.243  1.00 65.39           O  
ANISOU  405  O   CYS A  53     8231  13028   3585   2650   -235    287       O  
ATOM    406  CB  CYS A  53      26.246   3.314  40.987  1.00 68.24           C  
ANISOU  406  CB  CYS A  53     8675  13095   4159   2374    -32    713       C  
ATOM    407  SG  CYS A  53      26.463   1.655  40.291  1.00 71.24           S  
ANISOU  407  SG  CYS A  53     9101  13342   4625   2280     45    984       S  
ATOM    408  N   VAL A  54      24.863   5.336  43.160  1.00 72.34           N  
ANISOU  408  N   VAL A  54     9095  13934   4459   2600    -54    440       N  
ATOM    409  CA  VAL A  54      24.722   6.630  43.816  1.00 73.46           C  
ANISOU  409  CA  VAL A  54     9200  14175   4537   2695   -126    219       C  
ATOM    410  C   VAL A  54      25.072   6.512  45.294  1.00 77.41           C  
ANISOU  410  C   VAL A  54     9666  14849   4899   2848   -153    211       C  
ATOM    411  O   VAL A  54      25.619   7.449  45.889  1.00 84.49           O  
ANISOU  411  O   VAL A  54    10539  15814   5748   2940   -259      8       O  
ATOM    412  CB  VAL A  54      23.298   7.176  43.603  1.00 66.04           C  
ANISOU  412  CB  VAL A  54     8242  13243   3608   2666    -48    213       C  
ATOM    413  CG1 VAL A  54      23.103   8.489  44.349  1.00 67.12           C  
ANISOU  413  CG1 VAL A  54     8341  13485   3678   2776   -121    -10       C  
ATOM    414  CG2 VAL A  54      23.022   7.361  42.121  1.00 64.59           C  
ANISOU  414  CG2 VAL A  54     8093  12889   3561   2518    -30    204       C  
ATOM    415  N   ALA A  55      24.775   5.363  45.910  1.00 70.30           N  
ANISOU  415  N   ALA A  55     8758  14016   3935   2878    -60    430       N  
ATOM    416  CA  ALA A  55      25.167   5.147  47.299  1.00 76.58           C  
ANISOU  416  CA  ALA A  55     9522  14979   4596   3025    -83    438       C  
ATOM    417  C   ALA A  55      26.682   5.049  47.434  1.00 83.34           C  
ANISOU  417  C   ALA A  55    10394  15822   5451   3062   -196    357       C  
ATOM    418  O   ALA A  55      27.257   5.539  48.413  1.00 85.45           O  
ANISOU  418  O   ALA A  55    10631  16209   5626   3187   -276    228       O  
ATOM    419  CB  ALA A  55      24.492   3.889  47.844  1.00 73.33           C  
ANISOU  419  CB  ALA A  55     9102  14630   4132   3036     45    703       C  
ATOM    420  N   ASP A  56      27.345   4.423  46.462  1.00 82.32           N  
ANISOU  420  N   ASP A  56    10307  15548   5423   2959   -206    429       N  
ATOM    421  CA  ASP A  56      28.802   4.389  46.416  1.00 83.20           C  
ANISOU  421  CA  ASP A  56    10430  15630   5552   2980   -319    341       C  
ATOM    422  C   ASP A  56      29.232   4.088  44.989  1.00 78.89           C  
ANISOU  422  C   ASP A  56     9929  14899   5148   2838   -330    373       C  
ATOM    423  O   ASP A  56      28.799   3.089  44.407  1.00 74.22           O  
ANISOU  423  O   ASP A  56     9368  14224   4610   2755   -233    577       O  
ATOM    424  CB  ASP A  56      29.372   3.348  47.384  1.00 94.19           C  
ANISOU  424  CB  ASP A  56    11818  17118   6853   3071   -304    482       C  
ATOM    425  CG  ASP A  56      30.701   3.776  47.976  1.00 98.05           C  
ANISOU  425  CG  ASP A  56    12289  17670   7297   3166   -438    317       C  
ATOM    426  OD1 ASP A  56      31.709   3.771  47.239  1.00 95.03           O  
ANISOU  426  OD1 ASP A  56    11926  17182   7000   3108   -517    257       O  
ATOM    427  OD2 ASP A  56      30.736   4.124  49.176  1.00 99.23           O  
ANISOU  427  OD2 ASP A  56    12401  17976   7327   3298   -466    247       O  
ATOM    428  N   GLU A  57      30.091   4.946  44.438  1.00 86.46           N  
ANISOU  428  N   GLU A  57    10887  15791   6172   2813   -449    173       N  
ATOM    429  CA  GLU A  57      30.427   4.892  43.020  1.00 95.46           C  
ANISOU  429  CA  GLU A  57    12062  16761   7447   2679   -467    170       C  
ATOM    430  C   GLU A  57      31.340   3.728  42.654  1.00 96.55           C  
ANISOU  430  C   GLU A  57    12228  16832   7623   2648   -468    316       C  
ATOM    431  O   GLU A  57      31.563   3.499  41.460  1.00 90.00           O  
ANISOU  431  O   GLU A  57    11429  15863   6904   2539   -467    349       O  
ATOM    432  CB  GLU A  57      31.081   6.207  42.592  1.00103.08           C  
ANISOU  432  CB  GLU A  57    13010  17680   8475   2662   -601    -95       C  
ATOM    433  CG  GLU A  57      30.094   7.289  42.184  1.00106.16           C  
ANISOU  433  CG  GLU A  57    13394  18039   8902   2619   -588   -218       C  
ATOM    434  CD  GLU A  57      30.769   8.469  41.515  1.00108.17           C  
ANISOU  434  CD  GLU A  57    13639  18205   9255   2572   -717   -458       C  
ATOM    435  OE1 GLU A  57      30.139   9.098  40.639  1.00104.60           O  
ANISOU  435  OE1 GLU A  57    13199  17661   8883   2486   -703   -521       O  
ATOM    436  OE2 GLU A  57      31.930   8.769  41.866  1.00110.77           O  
ANISOU  436  OE2 GLU A  57    13946  18553   9587   2619   -834   -583       O  
ATOM    437  N   SER A  58      31.870   2.991  43.629  1.00103.25           N  
ANISOU  437  N   SER A  58    13068  17777   8386   2745   -470    403       N  
ATOM    438  CA  SER A  58      32.811   1.921  43.317  1.00105.49           C  
ANISOU  438  CA  SER A  58    13378  17996   8708   2726   -482    529       C  
ATOM    439  C   SER A  58      32.318   0.565  43.806  1.00101.56           C  
ANISOU  439  C   SER A  58    12899  17523   8165   2746   -367    789       C  
ATOM    440  O   SER A  58      33.054  -0.158  44.485  1.00105.69           O  
ANISOU  440  O   SER A  58    13422  18102   8634   2822   -387    862       O  
ATOM    441  CB  SER A  58      34.186   2.227  43.919  1.00111.12           C  
ANISOU  441  CB  SER A  58    14063  18778   9381   2817   -613    385       C  
ATOM    442  OG  SER A  58      34.064   2.905  45.156  1.00113.25           O  
ANISOU  442  OG  SER A  58    14291  19203   9535   2937   -647    268       O  
ATOM    443  N   ALA A  59      31.084   0.201  43.457  1.00 93.39           N  
ANISOU  443  N   ALA A  59    11881  16442   7161   2675   -248    931       N  
ATOM    444  CA  ALA A  59      30.570  -1.117  43.807  1.00 84.90           C  
ANISOU  444  CA  ALA A  59    10823  15364   6070   2672   -138   1185       C  
ATOM    445  C   ALA A  59      31.055  -2.154  42.802  1.00100.88           C  
ANISOU  445  C   ALA A  59    12896  17224   8211   2579   -121   1330       C  
ATOM    446  O   ALA A  59      32.167  -2.039  42.276  1.00111.75           O  
ANISOU  446  O   ALA A  59    14283  18543   9634   2571   -212   1241       O  
ATOM    447  CB  ALA A  59      29.043  -1.104  43.883  1.00 67.21           C  
ANISOU  447  CB  ALA A  59     8572  13141   3824   2632    -20   1280       C  
ATOM    448  N   GLU A  60      30.237  -3.169  42.516  1.00104.62           N  
ANISOU  448  N   GLU A  60    13394  17618   8739   2509     -8   1549       N  
ATOM    449  CA  GLU A  60      30.718  -4.282  41.702  1.00108.50           C  
ANISOU  449  CA  GLU A  60    13933  17955   9338   2436      8   1700       C  
ATOM    450  C   GLU A  60      30.835  -3.895  40.229  1.00 98.95           C  
ANISOU  450  C   GLU A  60    12749  16592   8256   2320    -16   1631       C  
ATOM    451  O   GLU A  60      31.914  -3.993  39.634  1.00101.46           O  
ANISOU  451  O   GLU A  60    13085  16840   8626   2311    -93   1581       O  
ATOM    452  CB  GLU A  60      29.816  -5.509  41.888  1.00117.95           C  
ANISOU  452  CB  GLU A  60    15146  19103  10565   2395    130   1953       C  
ATOM    453  CG  GLU A  60      28.316  -5.265  41.736  1.00124.89           C  
ANISOU  453  CG  GLU A  60    16009  19976  11467   2325    231   2005       C  
ATOM    454  CD  GLU A  60      27.498  -6.543  41.857  1.00128.09           C  
ANISOU  454  CD  GLU A  60    16428  20316  11923   2272    342   2257       C  
ATOM    455  OE1 GLU A  60      26.528  -6.701  41.088  1.00125.84           O  
ANISOU  455  OE1 GLU A  60    16152  19923  11739   2158    417   2334       O  
ATOM    456  OE2 GLU A  60      27.819  -7.387  42.723  1.00129.12           O  
ANISOU  456  OE2 GLU A  60    16559  20503  11998   2343    353   2376       O  
ATOM    457  N   ASN A  61      29.737  -3.445  39.622  1.00 88.83           N  
ANISOU  457  N   ASN A  61    11467  15260   7026   2233     49   1626       N  
ATOM    458  CA  ASN A  61      29.704  -3.186  38.187  1.00 82.78           C  
ANISOU  458  CA  ASN A  61    10727  14342   6384   2115     43   1589       C  
ATOM    459  C   ASN A  61      29.411  -1.726  37.873  1.00 77.76           C  
ANISOU  459  C   ASN A  61    10059  13708   5780   2082      1   1358       C  
ATOM    460  O   ASN A  61      28.992  -1.409  36.755  1.00 70.98           O  
ANISOU  460  O   ASN A  61     9204  12674   5091   1949     24   1311       O  
ATOM    461  CB  ASN A  61      28.669  -4.078  37.501  1.00 81.40           C  
ANISOU  461  CB  ASN A  61    10579  14028   6320   2000    162   1789       C  
ATOM    462  CG  ASN A  61      29.016  -5.553  37.575  1.00 87.69           C  
ANISOU  462  CG  ASN A  61    11411  14748   7161   1997    195   1999       C  
ATOM    463  OD1 ASN A  61      30.180  -5.929  37.730  1.00 86.16           O  
ANISOU  463  OD1 ASN A  61    11229  14555   6951   2055    124   1989       O  
ATOM    464  ND2 ASN A  61      28.001  -6.399  37.454  1.00 95.63           N  
ANISOU  464  ND2 ASN A  61    12428  15675   8232   1925    300   2185       N  
ATOM    465  N   CYS A  62      29.613  -0.831  38.840  1.00 79.59           N  
ANISOU  465  N   CYS A  62    10258  14127   5855   2202    -64   1212       N  
ATOM    466  CA  CYS A  62      29.290   0.573  38.618  1.00 78.07           C  
ANISOU  466  CA  CYS A  62    10036  13941   5685   2181   -108    993       C  
ATOM    467  C   CYS A  62      30.166   1.174  37.527  1.00 77.36           C  
ANISOU  467  C   CYS A  62     9942  13664   5786   2080   -194    825       C  
ATOM    468  O   CYS A  62      29.692   1.969  36.708  1.00 82.98           O  
ANISOU  468  O   CYS A  62    10646  14261   6622   1982   -191    717       O  
ATOM    469  CB  CYS A  62      29.440   1.358  39.920  1.00 71.81           C  
ANISOU  469  CB  CYS A  62     9204  13346   4735   2323   -169    853       C  
ATOM    470  SG  CYS A  62      28.176   1.004  41.157  1.00 73.74           S  
ANISOU  470  SG  CYS A  62     9421  13726   4871   2394    -56    986       S  
ATOM    471  N   ASP A  63      31.443   0.789  37.487  1.00 83.60           N  
ANISOU  471  N   ASP A  63    10736  14423   6606   2102   -270    808       N  
ATOM    472  CA  ASP A  63      32.392   1.345  36.530  1.00 79.02           C  
ANISOU  472  CA  ASP A  63    10143  13686   6196   2017   -356    653       C  
ATOM    473  C   ASP A  63      32.112   0.930  35.091  1.00 70.36           C  
ANISOU  473  C   ASP A  63     9071  12351   5312   1854   -295    724       C  
ATOM    474  O   ASP A  63      32.793   1.424  34.186  1.00 68.44           O  
ANISOU  474  O   ASP A  63     8815  11971   5219   1772   -354    603       O  
ATOM    475  CB  ASP A  63      33.810   0.926  36.914  1.00 86.61           C  
ANISOU  475  CB  ASP A  63    11096  14691   7121   2092   -445    636       C  
ATOM    476  CG  ASP A  63      33.925  -0.563  37.179  1.00 92.27           C  
ANISOU  476  CG  ASP A  63    11849  15419   7792   2128   -384    869       C  
ATOM    477  OD1 ASP A  63      32.919  -1.173  37.597  1.00 91.76           O  
ANISOU  477  OD1 ASP A  63    11807  15413   7644   2149   -286   1036       O  
ATOM    478  OD2 ASP A  63      35.020  -1.125  36.966  1.00 93.75           O  
ANISOU  478  OD2 ASP A  63    12039  15552   8028   2136   -435    888       O  
ATOM    479  N   LYS A  64      31.149   0.042  34.859  1.00 65.55           N  
ANISOU  479  N   LYS A  64     8493  11692   4720   1807   -182    917       N  
ATOM    480  CA  LYS A  64      30.858  -0.416  33.510  1.00 63.56           C  
ANISOU  480  CA  LYS A  64     8266  11218   4664   1659   -128    987       C  
ATOM    481  C   LYS A  64      30.312   0.724  32.657  1.00 62.99           C  
ANISOU  481  C   LYS A  64     8178  11048   4709   1559   -132    837       C  
ATOM    482  O   LYS A  64      29.794   1.725  33.160  1.00 62.44           O  
ANISOU  482  O   LYS A  64     8083  11082   4560   1600   -148    721       O  
ATOM    483  CB  LYS A  64      29.849  -1.563  33.537  1.00 63.78           C  
ANISOU  483  CB  LYS A  64     8328  11225   4680   1632    -10   1221       C  
ATOM    484  CG  LYS A  64      30.455  -2.932  33.773  1.00 68.75           C  
ANISOU  484  CG  LYS A  64     8989  11842   5292   1671      2   1397       C  
ATOM    485  CD  LYS A  64      29.371  -3.996  33.830  1.00 72.23           C  
ANISOU  485  CD  LYS A  64     9458  12258   5728   1639    117   1628       C  
ATOM    486  CE  LYS A  64      29.950  -5.359  34.162  1.00 74.57           C  
ANISOU  486  CE  LYS A  64     9788  12544   5999   1688    127   1810       C  
ATOM    487  NZ  LYS A  64      28.884  -6.341  34.501  1.00 75.43           N  
ANISOU  487  NZ  LYS A  64     9918  12668   6072   1678    235   2043       N  
ATOM    488  N   SER A  65      30.439   0.562  31.344  1.00 59.57           N  
ANISOU  488  N   SER A  65     7759  10411   4463   1431   -120    839       N  
ATOM    489  CA  SER A  65      29.852   1.530  30.436  1.00 58.23           C  
ANISOU  489  CA  SER A  65     7578  10133   4414   1329   -113    723       C  
ATOM    490  C   SER A  65      28.330   1.452  30.501  1.00 58.53           C  
ANISOU  490  C   SER A  65     7626  10192   4422   1301    -13    817       C  
ATOM    491  O   SER A  65      27.747   0.445  30.916  1.00 60.48           O  
ANISOU  491  O   SER A  65     7892  10482   4606   1324     64   1000       O  
ATOM    492  CB  SER A  65      30.325   1.282  29.004  1.00 53.49           C  
ANISOU  492  CB  SER A  65     6992   9319   4012   1205   -118    720       C  
ATOM    493  OG  SER A  65      29.988  -0.023  28.571  1.00 67.41           O  
ANISOU  493  OG  SER A  65     8795  10992   5828   1160    -41    910       O  
ATOM    494  N   LEU A  66      27.683   2.549  30.108  1.00 57.11           N  
ANISOU  494  N   LEU A  66     7427   9983   4289   1253    -15    691       N  
ATOM    495  CA  LEU A  66      26.232   2.527  29.975  1.00 59.87           C  
ANISOU  495  CA  LEU A  66     7781  10331   4637   1211     79    770       C  
ATOM    496  C   LEU A  66      25.801   1.675  28.791  1.00 62.26           C  
ANISOU  496  C   LEU A  66     8113  10446   5097   1083    149    899       C  
ATOM    497  O   LEU A  66      24.694   1.125  28.793  1.00 59.74           O  
ANISOU  497  O   LEU A  66     7801  10128   4769   1054    239   1035       O  
ATOM    498  CB  LEU A  66      25.697   3.953  29.846  1.00 59.73           C  
ANISOU  498  CB  LEU A  66     7736  10328   4631   1200     51    592       C  
ATOM    499  CG  LEU A  66      26.073   4.879  31.003  1.00 57.36           C  
ANISOU  499  CG  LEU A  66     7407  10208   4180   1328    -27    443       C  
ATOM    500  CD1 LEU A  66      25.857   6.335  30.625  1.00 51.43           C  
ANISOU  500  CD1 LEU A  66     6634   9418   3491   1299    -81    241       C  
ATOM    501  CD2 LEU A  66      25.273   4.514  32.244  1.00 51.35           C  
ANISOU  501  CD2 LEU A  66     6638   9649   3224   1440     34    545       C  
ATOM    502  N   HIS A  67      26.664   1.544  27.779  1.00 63.62           N  
ANISOU  502  N   HIS A  67     8298  10460   5413   1009    107    859       N  
ATOM    503  CA  HIS A  67      26.389   0.614  26.690  1.00 65.99           C  
ANISOU  503  CA  HIS A  67     8631  10588   5855    902    164    983       C  
ATOM    504  C   HIS A  67      26.402  -0.827  27.186  1.00 70.42           C  
ANISOU  504  C   HIS A  67     9220  11175   6363    939    212   1184       C  
ATOM    505  O   HIS A  67      25.554  -1.634  26.788  1.00 74.25           O  
ANISOU  505  O   HIS A  67     9726  11584   6904    877    289   1328       O  
ATOM    506  CB  HIS A  67      27.404   0.809  25.563  1.00 69.01           C  
ANISOU  506  CB  HIS A  67     9018  10815   6387    831    104    889       C  
ATOM    507  CG  HIS A  67      27.187   2.057  24.764  1.00 74.14           C  
ANISOU  507  CG  HIS A  67     9648  11391   7131    760     77    731       C  
ATOM    508  ND1 HIS A  67      28.194   2.669  24.049  1.00 73.05           N  
ANISOU  508  ND1 HIS A  67     9496  11168   7091    722      5    602       N  
ATOM    509  CD2 HIS A  67      26.077   2.808  24.568  1.00 75.01           C  
ANISOU  509  CD2 HIS A  67     9748  11499   7255    721    112    686       C  
ATOM    510  CE1 HIS A  67      27.714   3.742  23.446  1.00 73.16           C  
ANISOU  510  CE1 HIS A  67     9495  11127   7176    661     -3    489       C  
ATOM    511  NE2 HIS A  67      26.432   3.849  23.745  1.00 74.43           N  
ANISOU  511  NE2 HIS A  67     9659  11335   7287    662     60    534       N  
ATOM    512  N   THR A  68      27.350  -1.167  28.064  1.00 66.64           N  
ANISOU  512  N   THR A  68     8739  10801   5779   1042    165   1197       N  
ATOM    513  CA  THR A  68      27.384  -2.512  28.629  1.00 64.88           C  
ANISOU  513  CA  THR A  68     8544  10612   5496   1089    207   1393       C  
ATOM    514  C   THR A  68      26.179  -2.757  29.527  1.00 67.20           C  
ANISOU  514  C   THR A  68     8829  11036   5666   1130    289   1519       C  
ATOM    515  O   THR A  68      25.513  -3.791  29.417  1.00 69.32           O  
ANISOU  515  O   THR A  68     9120  11252   5966   1091    364   1701       O  
ATOM    516  CB  THR A  68      28.680  -2.736  29.410  1.00 64.14           C  
ANISOU  516  CB  THR A  68     8447  10615   5307   1199    133   1371       C  
ATOM    517  OG1 THR A  68      29.804  -2.376  28.597  1.00 68.66           O  
ANISOU  517  OG1 THR A  68     9015  11082   5992   1161     55   1240       O  
ATOM    518  CG2 THR A  68      28.804  -4.198  29.826  1.00 65.22           C  
ANISOU  518  CG2 THR A  68     8618  10754   5407   1238    172   1580       C  
ATOM    519  N   LEU A  69      25.882  -1.811  30.422  1.00 65.08           N  
ANISOU  519  N   LEU A  69     8528  10940   5260   1212    274   1423       N  
ATOM    520  CA  LEU A  69      24.758  -1.981  31.338  1.00 69.24           C  
ANISOU  520  CA  LEU A  69     9040  11616   5653   1264    353   1537       C  
ATOM    521  C   LEU A  69      23.441  -2.092  30.579  1.00 65.28           C  
ANISOU  521  C   LEU A  69     8536  11012   5254   1151    440   1611       C  
ATOM    522  O   LEU A  69      22.645  -3.006  30.822  1.00 69.19           O  
ANISOU  522  O   LEU A  69     9038  11521   5731   1136    525   1801       O  
ATOM    523  CB  LEU A  69      24.713  -0.821  32.333  1.00 66.57           C  
ANISOU  523  CB  LEU A  69     8664  11475   5154   1374    312   1390       C  
ATOM    524  CG  LEU A  69      25.853  -0.747  33.350  1.00 60.51           C  
ANISOU  524  CG  LEU A  69     7890  10854   4246   1509    231   1332       C  
ATOM    525  CD1 LEU A  69      25.893   0.623  34.008  1.00 60.51           C  
ANISOU  525  CD1 LEU A  69     7854  11001   4136   1593    166   1129       C  
ATOM    526  CD2 LEU A  69      25.713  -1.844  34.393  1.00 59.79           C  
ANISOU  526  CD2 LEU A  69     7809  10898   4010   1600    285   1536       C  
ATOM    527  N   PHE A  70      23.195  -1.168  29.648  1.00 62.22           N  
ANISOU  527  N   PHE A  70     8140  10521   4981   1069    420   1464       N  
ATOM    528  CA  PHE A  70      21.958  -1.217  28.875  1.00 76.17           C  
ANISOU  528  CA  PHE A  70     9903  12190   6849    962    496   1521       C  
ATOM    529  C   PHE A  70      21.944  -2.412  27.932  1.00 74.85           C  
ANISOU  529  C   PHE A  70     9772  11835   6832    859    531   1664       C  
ATOM    530  O   PHE A  70      20.929  -3.109  27.819  1.00 66.16           O  
ANISOU  530  O   PHE A  70     8672  10704   5762    806    613   1816       O  
ATOM    531  CB  PHE A  70      21.774   0.081  28.089  1.00 77.91           C  
ANISOU  531  CB  PHE A  70    10106  12341   7153    905    457   1326       C  
ATOM    532  CG  PHE A  70      21.498   1.278  28.950  1.00 75.74           C  
ANISOU  532  CG  PHE A  70     9796  12238   6745    996    431   1189       C  
ATOM    533  CD1 PHE A  70      21.114   1.125  30.273  1.00 66.10           C  
ANISOU  533  CD1 PHE A  70     8554  11223   5338   1111    465   1260       C  
ATOM    534  CD2 PHE A  70      21.622   2.558  28.437  1.00 79.14           C  
ANISOU  534  CD2 PHE A  70    10213  12623   7235    971    372    990       C  
ATOM    535  CE1 PHE A  70      20.861   2.225  31.066  1.00 63.15           C  
ANISOU  535  CE1 PHE A  70     8148  11010   4836   1204    437   1124       C  
ATOM    536  CE2 PHE A  70      21.369   3.662  29.225  1.00 77.04           C  
ANISOU  536  CE2 PHE A  70     9916  12505   6851   1059    341    855       C  
ATOM    537  CZ  PHE A  70      20.988   3.495  30.541  1.00 69.91           C  
ANISOU  537  CZ  PHE A  70     8993  11810   5759   1179    372    918       C  
ATOM    538  N   GLY A  71      23.062  -2.666  27.249  1.00 78.49           N  
ANISOU  538  N   GLY A  71    10261  12170   7390    831    469   1616       N  
ATOM    539  CA  GLY A  71      23.111  -3.769  26.308  1.00 86.66           C  
ANISOU  539  CA  GLY A  71    11334  13023   8570    741    494   1732       C  
ATOM    540  C   GLY A  71      22.998  -5.131  26.962  1.00 92.13           C  
ANISOU  540  C   GLY A  71    12048  13744   9213    776    541   1947       C  
ATOM    541  O   GLY A  71      22.412  -6.049  26.384  1.00 98.30           O  
ANISOU  541  O   GLY A  71    12851  14401  10099    695    593   2082       O  
ATOM    542  N   ASP A  72      23.547  -5.284  28.170  1.00 86.17           N  
ANISOU  542  N   ASP A  72    11287  13151   8302    897    522   1983       N  
ATOM    543  CA  ASP A  72      23.550  -6.593  28.818  1.00 91.36           C  
ANISOU  543  CA  ASP A  72    11967  13836   8910    938    562   2194       C  
ATOM    544  C   ASP A  72      22.132  -7.060  29.121  1.00 93.86           C  
ANISOU  544  C   ASP A  72    12268  14187   9207    901    664   2361       C  
ATOM    545  O   ASP A  72      21.753  -8.188  28.789  1.00100.15           O  
ANISOU  545  O   ASP A  72    13090  14871  10093    839    710   2531       O  
ATOM    546  CB  ASP A  72      24.382  -6.549  30.101  1.00 90.68           C  
ANISOU  546  CB  ASP A  72    11874  13937   8645   1084    520   2191       C  
ATOM    547  CG  ASP A  72      25.849  -6.834  29.854  1.00 87.91           C  
ANISOU  547  CG  ASP A  72    11549  13520   8332   1118    435   2132       C  
ATOM    548  OD1 ASP A  72      26.222  -7.063  28.683  1.00 85.24           O  
ANISOU  548  OD1 ASP A  72    11234  12995   8157   1030    412   2094       O  
ATOM    549  OD2 ASP A  72      26.629  -6.829  30.828  1.00 85.95           O  
ANISOU  549  OD2 ASP A  72    11294  13414   7947   1236    391   2122       O  
ATOM    550  N   LYS A  73      21.333  -6.203  29.751  1.00 86.50           N  
ANISOU  550  N   LYS A  73    11292  13410   8162    938    698   2314       N  
ATOM    551  CA  LYS A  73      19.978  -6.575  30.127  1.00 82.75           C  
ANISOU  551  CA  LYS A  73    10790  12996   7653    912    797   2471       C  
ATOM    552  C   LYS A  73      18.965  -6.336  29.020  1.00 82.44           C  
ANISOU  552  C   LYS A  73    10740  12817   7767    779    837   2447       C  
ATOM    553  O   LYS A  73      17.824  -6.800  29.133  1.00 81.39           O  
ANISOU  553  O   LYS A  73    10585  12697   7644    733    921   2592       O  
ATOM    554  CB  LYS A  73      19.569  -5.837  31.396  1.00 83.71           C  
ANISOU  554  CB  LYS A  73    10866  13370   7568   1029    820   2444       C  
ATOM    555  CG  LYS A  73      20.393  -6.292  32.580  1.00 89.63           C  
ANISOU  555  CG  LYS A  73    11626  14271   8157   1164    796   2515       C  
ATOM    556  CD  LYS A  73      20.103  -5.494  33.818  1.00 89.07           C  
ANISOU  556  CD  LYS A  73    11510  14442   7890   1287    802   2450       C  
ATOM    557  CE  LYS A  73      18.671  -5.689  34.254  1.00 80.40           C  
ANISOU  557  CE  LYS A  73    10364  13385   6800   1252    896   2550       C  
ATOM    558  NZ  LYS A  73      18.662  -6.087  35.680  1.00 87.44           N  
ANISOU  558  NZ  LYS A  73    11228  14427   7570   1359    911   2621       N  
ATOM    559  N   LEU A  74      19.354  -5.632  27.955  1.00 85.12           N  
ANISOU  559  N   LEU A  74    11092  13026   8224    716    780   2272       N  
ATOM    560  CA  LEU A  74      18.585  -5.682  26.718  1.00 90.16           C  
ANISOU  560  CA  LEU A  74    11733  13490   9034    581    808   2268       C  
ATOM    561  C   LEU A  74      18.488  -7.107  26.196  1.00 92.83           C  
ANISOU  561  C   LEU A  74    12107  13670   9495    505    838   2446       C  
ATOM    562  O   LEU A  74      17.529  -7.453  25.497  1.00 95.45           O  
ANISOU  562  O   LEU A  74    12432  13893   9940    403    886   2514       O  
ATOM    563  CB  LEU A  74      19.237  -4.785  25.666  1.00 91.98           C  
ANISOU  563  CB  LEU A  74    11977  13606   9367    537    734   2061       C  
ATOM    564  CG  LEU A  74      18.356  -3.967  24.721  1.00 97.70           C  
ANISOU  564  CG  LEU A  74    12680  14252  10189    445    750   1961       C  
ATOM    565  CD1 LEU A  74      17.096  -3.486  25.421  1.00 97.33           C  
ANISOU  565  CD1 LEU A  74    12584  14352  10044    468    818   1994       C  
ATOM    566  CD2 LEU A  74      19.147  -2.797  24.151  1.00 97.96           C  
ANISOU  566  CD2 LEU A  74    12715  14248  10256    448    670   1742       C  
ATOM    567  N   CYS A  75      19.465  -7.945  26.539  1.00 95.92           N  
ANISOU  567  N   CYS A  75    12535  14045   9867    558    805   2522       N  
ATOM    568  CA  CYS A  75      19.606  -9.282  25.983  1.00 98.32           C  
ANISOU  568  CA  CYS A  75    12882  14178  10298    496    813   2666       C  
ATOM    569  C   CYS A  75      19.198 -10.389  26.944  1.00 99.85           C  
ANISOU  569  C   CYS A  75    13076  14440  10424    531    873   2901       C  
ATOM    570  O   CYS A  75      19.233 -11.559  26.554  1.00 96.77           O  
ANISOU  570  O   CYS A  75    12721  13904  10142    480    881   3037       O  
ATOM    571  CB  CYS A  75      21.053  -9.510  25.538  1.00 96.14           C  
ANISOU  571  CB  CYS A  75    12650  13808  10070    525    729   2585       C  
ATOM    572  SG  CYS A  75      21.669  -8.234  24.426  1.00 98.99           S  
ANISOU  572  SG  CYS A  75    13007  14092  10511    485    657   2323       S  
ATOM    573  N   THR A  76      18.839 -10.064  28.190  1.00108.65           N  
ANISOU  573  N   THR A  76    14151  15770  11360    622    913   2952       N  
ATOM    574  CA  THR A  76      18.405 -11.113  29.109  1.00119.19           C  
ANISOU  574  CA  THR A  76    15480  17159  12646    649    970   3165       C  
ATOM    575  C   THR A  76      17.098 -11.747  28.649  1.00122.10           C  
ANISOU  575  C   THR A  76    15828  17402  13161    522   1034   3269       C  
ATOM    576  O   THR A  76      16.914 -12.961  28.785  1.00127.91           O  
ANISOU  576  O   THR A  76    16581  18035  13985    484   1049   3410       O  
ATOM    577  CB  THR A  76      18.253 -10.573  30.532  1.00126.51           C  
ANISOU  577  CB  THR A  76    16361  18322  13385    765    987   3141       C  
ATOM    578  OG1 THR A  76      17.154  -9.655  30.587  1.00130.11           O  
ANISOU  578  OG1 THR A  76    16761  18870  13805    742   1035   3075       O  
ATOM    579  CG2 THR A  76      19.534  -9.904  31.017  1.00126.19           C  
ANISOU  579  CG2 THR A  76    16337  18411  13198    893    914   3020       C  
ATOM    580  N   VAL A  77      16.279 -10.947  27.976  1.00118.74           N  
ANISOU  580  N   VAL A  77    15365  16986  12766    458   1068   3198       N  
ATOM    581  CA  VAL A  77      14.986 -11.466  27.455  1.00118.71           C  
ANISOU  581  CA  VAL A  77    15339  16852  12913    331   1119   3281       C  
ATOM    582  C   VAL A  77      15.003 -11.440  25.924  1.00118.26           C  
ANISOU  582  C   VAL A  77    15294  16658  12981    232   1106   3192       C  
ATOM    583  O   VAL A  77      14.325 -12.291  25.329  1.00118.29           O  
ANISOU  583  O   VAL A  77    15265  16600  13080    137   1147   3204       O  
ATOM    584  CB  VAL A  77      13.794 -10.681  28.035  1.00118.45           C  
ANISOU  584  CB  VAL A  77    15234  16964  12807    342   1189   3318       C  
ATOM    585  CG1 VAL A  77      13.268 -11.314  29.312  1.00119.10           C  
ANISOU  585  CG1 VAL A  77    15303  17189  12761    447   1202   3408       C  
ATOM    586  CG2 VAL A  77      14.149  -9.221  28.272  1.00116.60           C  
ANISOU  586  CG2 VAL A  77    14958  16872  12472    376   1199   3168       C  
ATOM    587  N   MET A  87      16.878 -10.518  16.596  1.00127.80           N  
ANISOU  587  N   MET A  87    16757  16534  15267   -290    739   2401       N  
ATOM    588  CA  MET A  87      17.751  -9.543  17.291  1.00110.55           C  
ANISOU  588  CA  MET A  87    14543  14527  12933   -205    735   2314       C  
ATOM    589  C   MET A  87      18.820 -10.256  18.098  1.00100.16           C  
ANISOU  589  C   MET A  87    13247  13295  11517   -103    715   2373       C  
ATOM    590  O   MET A  87      19.844  -9.610  18.371  1.00 99.05           O  
ANISOU  590  O   MET A  87    13100  13251  11286    -30    677   2262       O  
ATOM    591  CB  MET A  87      16.934  -8.656  18.225  1.00107.29           C  
ANISOU  591  CB  MET A  87    14073  14256  12436   -209    798   2346       C  
ATOM    592  CG  MET A  87      17.564  -7.309  18.505  1.00106.56           C  
ANISOU  592  CG  MET A  87    13948  14321  12218   -140    784   2204       C  
ATOM    593  SD  MET A  87      17.431  -6.181  17.108  1.00105.60           S  
ANISOU  593  SD  MET A  87    13837  14113  12174   -174    723   1982       S  
ATOM    594  CE  MET A  87      17.292  -4.617  17.969  1.00 99.99           C  
ANISOU  594  CE  MET A  87    13083  13601  11308    -86    711   1850       C  
ATOM    595  N   ALA A  88      18.618 -11.529  18.455  1.00 96.72           N  
ANISOU  595  N   ALA A  88    12834  12819  11097    -98    735   2547       N  
ATOM    596  CA  ALA A  88      19.650 -12.089  19.320  1.00 98.75           C  
ANISOU  596  CA  ALA A  88    13115  13135  11269     -1    710   2612       C  
ATOM    597  C   ALA A  88      21.000 -12.184  18.624  1.00103.26           C  
ANISOU  597  C   ALA A  88    13727  13615  11892     30    635   2504       C  
ATOM    598  O   ALA A  88      22.004 -12.461  19.290  1.00106.08           O  
ANISOU  598  O   ALA A  88    14101  14032  12173    120    604   2524       O  
ATOM    599  CB  ALA A  88      19.225 -13.471  19.822  1.00 95.93           C  
ANISOU  599  CB  ALA A  88    12777  12729  10943    -11    745   2829       C  
ATOM    600  N   ASP A  89      21.040 -11.969  17.306  1.00102.34           N  
ANISOU  600  N   ASP A  89    13625  13361  11898    -40    607   2395       N  
ATOM    601  CA  ASP A  89      22.301 -11.930  16.575  1.00106.25           C  
ANISOU  601  CA  ASP A  89    14151  13783  12438    -12    541   2281       C  
ATOM    602  C   ASP A  89      23.250 -10.887  17.152  1.00109.32           C  
ANISOU  602  C   ASP A  89    14513  14320  12706     72    507   2159       C  
ATOM    603  O   ASP A  89      24.470 -11.084  17.165  1.00111.11           O  
ANISOU  603  O   ASP A  89    14757  14542  12918    134    456   2119       O  
ATOM    604  CB  ASP A  89      22.024 -11.633  15.099  1.00102.29           C  
ANISOU  604  CB  ASP A  89    13656  13142  12067   -100    526   2174       C  
ATOM    605  CG  ASP A  89      23.009 -12.307  14.171  1.00102.31           C  
ANISOU  605  CG  ASP A  89    13704  13005  12164    -92    472   2135       C  
ATOM    606  OD1 ASP A  89      23.524 -13.387  14.528  1.00104.06           O  
ANISOU  606  OD1 ASP A  89    13961  13184  12394    -48    456   2237       O  
ATOM    607  OD2 ASP A  89      23.266 -11.757  13.079  1.00103.59           O  
ANISOU  607  OD2 ASP A  89    13867  13103  12391   -127    446   2005       O  
ATOM    608  N   CYS A  90      22.705  -9.771  17.643  1.00110.11           N  
ANISOU  608  N   CYS A  90    14567  14550  12720     76    531   2095       N  
ATOM    609  CA  CYS A  90      23.545  -8.665  18.093  1.00109.40           C  
ANISOU  609  CA  CYS A  90    14449  14587  12531    145    491   1958       C  
ATOM    610  C   CYS A  90      24.224  -8.975  19.420  1.00109.89           C  
ANISOU  610  C   CYS A  90    14510  14786  12459    255    478   2024       C  
ATOM    611  O   CYS A  90      25.385  -8.604  19.632  1.00112.25           O  
ANISOU  611  O   CYS A  90    14803  15138  12709    321    422   1934       O  
ATOM    612  CB  CYS A  90      22.709  -7.393  18.210  1.00106.59           C  
ANISOU  612  CB  CYS A  90    14048  14320  12129    119    516   1867       C  
ATOM    613  SG  CYS A  90      21.877  -6.941  16.677  1.00 99.61           S  
ANISOU  613  SG  CYS A  90    13164  13289  11395     -4    530   1787       S  
ATOM    614  N   CYS A  91      23.430  -9.567  20.314  1.00110.72           N  
ANISOU  614  N   CYS A  91    14615  14953  12501    276    529   2183       N  
ATOM    615  CA  CYS A  91      23.890  -9.856  21.694  1.00107.23           C  
ANISOU  615  CA  CYS A  91    14168  14661  11914    386    523   2255       C  
ATOM    616  C   CYS A  91      24.857 -11.027  21.657  1.00110.67           C  
ANISOU  616  C   CYS A  91    14646  15032  12373    437    482   2325       C  
ATOM    617  O   CYS A  91      25.232 -11.521  22.729  1.00111.92           O  
ANISOU  617  O   CYS A  91    14801  15312  12411    539    462   2363       O  
ATOM    618  CB  CYS A  91      22.697 -10.286  22.535  1.00 99.15           C  
ANISOU  618  CB  CYS A  91    13128  13731  10816    391    597   2414       C  
ATOM    619  SG  CYS A  91      21.358  -9.078  22.618  1.00 90.07           S  
ANISOU  619  SG  CYS A  91    11924  12664   9635    338    650   2343       S  
ATOM    620  N   LYS A  93      27.546 -10.514  20.127  1.00 91.17           N  
ANISOU  620  N   LYS A  93    12196  12434  10011    474    339   2063       N  
ATOM    621  CA  LYS A  93      28.821  -9.783  19.909  1.00 84.49           C  
ANISOU  621  CA  LYS A  93    11326  11621   9154    508    275   1898       C  
ATOM    622  C   LYS A  93      29.200  -8.979  21.141  1.00 81.64           C  
ANISOU  622  C   LYS A  93    10924  11458   8637    594    253   1841       C  
ATOM    623  O   LYS A  93      28.397  -8.932  22.076  1.00 83.05           O  
ANISOU  623  O   LYS A  93    11086  11744   8725    607    295   1888       O  
ATOM    624  CB  LYS A  93      28.736  -8.855  18.694  1.00 82.25           C  
ANISOU  624  CB  LYS A  93    11027  11251   8975    415    272   1761       C  
ATOM    625  CG  LYS A  93      29.767  -9.116  17.605  1.00 78.50           C  
ANISOU  625  CG  LYS A  93    10527  10779   8521    431    209   1602       C  
ATOM    626  CD  LYS A  93      30.351 -10.512  17.665  1.00 77.77           C  
ANISOU  626  CD  LYS A  93    10456  10648   8446    493    163   1631       C  
ATOM    627  CE  LYS A  93      29.787 -11.445  16.614  1.00 76.01           C  
ANISOU  627  CE  LYS A  93    10189  10519   8171    553     98   1499       C  
ATOM    628  NZ  LYS A  93      30.605 -11.432  15.380  1.00 73.46           N  
ANISOU  628  NZ  LYS A  93     9876  10244   7792    653     57   1554       N  
ATOM    629  N   GLN A  94      30.380  -8.369  21.101  1.00 76.44           N  
ANISOU  629  N   GLN A  94    10247  10851   7948    656    186   1737       N  
ATOM    630  CA  GLN A  94      30.875  -7.571  22.246  1.00 81.45           C  
ANISOU  630  CA  GLN A  94    10842  11667   8439    744    149   1664       C  
ATOM    631  C   GLN A  94      30.520  -6.095  22.066  1.00 82.55           C  
ANISOU  631  C   GLN A  94    10939  11847   8581    700    137   1500       C  
ATOM    632  O   GLN A  94      30.127  -5.739  20.971  1.00 76.95           O  
ANISOU  632  O   GLN A  94    10231  11040   7964    605    171   1470       O  
ATOM    633  CB  GLN A  94      32.355  -7.861  22.507  1.00 77.62           C  
ANISOU  633  CB  GLN A  94    10351  11217   7924    828     78   1629       C  
ATOM    634  CG  GLN A  94      32.668  -9.342  22.672  1.00 78.96           C  
ANISOU  634  CG  GLN A  94    10565  11347   8088    881     86   1793       C  
ATOM    635  CD  GLN A  94      34.145  -9.595  22.852  1.00 81.43           C  
ANISOU  635  CD  GLN A  94    10872  11665   8400    954     15   1750       C  
ATOM    636  OE1 GLN A  94      34.974  -8.710  22.657  1.00 86.38           O  
ANISOU  636  OE1 GLN A  94    11464  12295   9063    945    -37   1600       O  
ATOM    637  NE2 GLN A  94      34.489 -10.814  23.229  1.00 76.80           N  
ANISOU  637  NE2 GLN A  94    10320  11083   7777   1028     11   1885       N  
ATOM    638  N   GLU A  95      30.814  -5.259  23.051  1.00 90.11           N  
ANISOU  638  N   GLU A  95    11856  12942   9439    770     83   1388       N  
ATOM    639  CA  GLU A  95      30.328  -3.853  23.074  1.00 97.23           C  
ANISOU  639  CA  GLU A  95    12720  13902  10322    742     75   1250       C  
ATOM    640  C   GLU A  95      30.760  -2.909  21.954  1.00103.83           C  
ANISOU  640  C   GLU A  95    13523  14688  11239    707      9   1079       C  
ATOM    641  O   GLU A  95      29.886  -2.176  21.479  1.00103.91           O  
ANISOU  641  O   GLU A  95    13535  14646  11302    718    -32   1066       O  
ATOM    642  CB  GLU A  95      30.503  -3.212  24.446  1.00 99.23           C  
ANISOU  642  CB  GLU A  95    12949  14351  10402    842     65   1243       C  
ATOM    643  CG  GLU A  95      29.193  -3.075  25.193  1.00 98.28           C  
ANISOU  643  CG  GLU A  95    12841  14289  10213    841    147   1363       C  
ATOM    644  CD  GLU A  95      28.063  -2.464  24.385  1.00 95.00           C  
ANISOU  644  CD  GLU A  95    12418  13805   9873    743    194   1318       C  
ATOM    645  OE1 GLU A  95      26.944  -2.948  24.501  1.00 95.52           O  
ANISOU  645  OE1 GLU A  95    12476  13956   9862    756    249   1376       O  
ATOM    646  OE2 GLU A  95      28.301  -1.484  23.669  1.00 89.93           O  
ANISOU  646  OE2 GLU A  95    11775  13032   9362    658    178   1229       O  
ATOM    647  N   PRO A  96      32.015  -2.817  21.487  1.00 30.00           N  
ATOM    648  CA  PRO A  96      32.311  -1.860  20.435  1.00 30.00           C  
ATOM    649  C   PRO A  96      31.524  -2.193  19.164  1.00 30.00           C  
ATOM    650  O   PRO A  96      31.649  -1.431  18.236  1.00 30.00           O  
ATOM    651  CB  PRO A  96      33.811  -2.019  20.189  1.00 30.00           C  
ATOM    652  CG  PRO A  96      34.330  -2.640  21.464  1.00 30.00           C  
ATOM    653  CD  PRO A  96      33.207  -3.533  21.946  1.00 30.00           C  
ATOM    654  N   GLU A  97      30.792  -3.314  19.137  1.00 92.14           N  
ANISOU  654  N   GLU A  97    12073  12897  10040    481     83   1057       N  
ATOM    655  CA  GLU A  97      30.041  -3.735  17.933  1.00 86.46           C  
ANISOU  655  CA  GLU A  97    11386  12013   9449    391    125   1113       C  
ATOM    656  C   GLU A  97      28.574  -4.049  18.265  1.00 77.61           C  
ANISOU  656  C   GLU A  97    10291  10875   8323    354    199   1228       C  
ATOM    657  O   GLU A  97      27.717  -3.731  17.435  1.00 68.27           O  
ANISOU  657  O   GLU A  97     9113   9602   7224    269    233   1211       O  
ATOM    658  CB  GLU A  97      30.735  -4.941  17.304  1.00 90.60           C  
ANISOU  658  CB  GLU A  97    11942  12452  10031    408    111   1184       C  
ATOM    659  CG  GLU A  97      32.252  -4.928  17.386  1.00 96.30           C  
ANISOU  659  CG  GLU A  97    12636  13210  10744    463     40   1099       C  
ATOM    660  CD  GLU A  97      32.876  -5.761  18.495  1.00105.08           C  
ANISOU  660  CD  GLU A  97    13749  14436  11742    571     14   1164       C  
ATOM    661  OE1 GLU A  97      33.880  -5.306  19.071  1.00108.99           O  
ANISOU  661  OE1 GLU A  97    14256  15013  12142    608     47   1248       O  
ATOM    662  OE2 GLU A  97      32.369  -6.861  18.774  1.00107.77           O  
ANISOU  662  OE2 GLU A  97    14076  14790  12083    622    -39   1133       O  
ATOM    663  N   ARG A  98      28.288  -4.628  19.430  1.00 77.18           N  
ANISOU  663  N   ARG A  98    10249  10905   8170    416    225   1350       N  
ATOM    664  CA  ARG A  98      26.911  -5.082  19.769  1.00 79.08           C  
ANISOU  664  CA  ARG A  98    10505  11140   8403    380    298   1469       C  
ATOM    665  C   ARG A  98      25.973  -3.879  19.915  1.00 84.00           C  
ANISOU  665  C   ARG A  98    11094  11841   8983    359    321   1390       C  
ATOM    666  O   ARG A  98      24.778  -4.018  19.693  1.00 86.55           O  
ANISOU  666  O   ARG A  98    11419  12133   9332    303    381   1457       O  
ATOM    667  CB  ARG A  98      26.924  -6.028  20.976  1.00 77.73           C  
ANISOU  667  CB  ARG A  98    10349  11057   8129    456    324   1624       C  
ATOM    668  CG  ARG A  98      26.843  -5.332  22.322  1.00 73.00           C  
ANISOU  668  CG  ARG A  98     9716  10657   7364    550    314   1595       C  
ATOM    669  CD  ARG A  98      26.231  -6.183  23.411  1.00 76.32           C  
ANISOU  669  CD  ARG A  98    10144  11171   7682    598    372   1767       C  
ATOM    670  NE  ARG A  98      26.125  -5.450  24.660  1.00 79.06           N  
ANISOU  670  NE  ARG A  98    10458  11721   7861    698    358   1724       N  
ATOM    671  CZ  ARG A  98      25.950  -6.008  25.841  1.00 81.10           C  
ANISOU  671  CZ  ARG A  98    10717  12110   7986    785    382   1847       C  
ATOM    672  NH1 ARG A  98      25.847  -7.313  25.958  1.00 84.52           N  
ANISOU  672  NH1 ARG A  98    11183  12489   8443    779    424   2033       N  
ATOM    673  NH2 ARG A  98      25.855  -5.259  26.913  1.00 84.68           N  
ANISOU  673  NH2 ARG A  98    11139  12752   8285    880    362   1784       N  
ATOM    674  N   ASN A  99      26.505  -2.727  20.281  1.00 82.97           N  
ANISOU  674  N   ASN A  99    10928  11808   8789    403    271   1249       N  
ATOM    675  CA  ASN A  99      25.682  -1.527  20.376  1.00 77.18           C  
ANISOU  675  CA  ASN A  99    10164  11131   8030    383    282   1154       C  
ATOM    676  C   ASN A  99      25.314  -1.008  18.992  1.00 71.57           C  
ANISOU  676  C   ASN A  99     9456  10278   7461    277    288   1080       C  
ATOM    677  O   ASN A  99      24.177  -0.576  18.767  1.00 66.78           O  
ANISOU  677  O   ASN A  99     8840   9661   6871    229    331   1076       O  
ATOM    678  CB  ASN A  99      26.411  -0.454  21.184  1.00 74.05           C  
ANISOU  678  CB  ASN A  99     9732  10866   7537    461    217   1016       C  
ATOM    679  CG  ASN A  99      25.669   0.865  21.202  1.00 68.72           C  
ANISOU  679  CG  ASN A  99     9028  10235   6849    443    216    897       C  
ATOM    680  OD1 ASN A  99      24.738   1.054  21.983  1.00 61.59           O  
ANISOU  680  OD1 ASN A  99     8112   9436   5852    479    256    929       O  
ATOM    681  ND2 ASN A  99      26.079   1.788  20.339  1.00 76.67           N  
ANISOU  681  ND2 ASN A  99    10020  11160   7949    390    172    761       N  
ATOM    682  N   GLU A 100      26.263  -1.046  18.050  1.00 76.43           N  
ANISOU  682  N   GLU A 100    10080  10788   8173    243    247   1023       N  
ATOM    683  CA  GLU A 100      25.967  -0.636  16.680  1.00 65.06           C  
ANISOU  683  CA  GLU A 100     8643   9213   6863    147    254    964       C  
ATOM    684  C   GLU A 100      24.922  -1.537  16.042  1.00 61.68           C  
ANISOU  684  C   GLU A 100     8247   8683   6507     80    317   1081       C  
ATOM    685  O   GLU A 100      24.100  -1.068  15.247  1.00 66.34           O  
ANISOU  685  O   GLU A 100     8834   9206   7168      7    342   1048       O  
ATOM    686  CB  GLU A 100      27.241  -0.639  15.834  1.00 66.41           C  
ANISOU  686  CB  GLU A 100     8815   9302   7115    133    202    897       C  
ATOM    687  CG  GLU A 100      28.293   0.377  16.247  1.00 74.25           C  
ANISOU  687  CG  GLU A 100     9769  10376   8069    179    133    766       C  
ATOM    688  CD  GLU A 100      27.739   1.779  16.389  1.00 72.28           C  
ANISOU  688  CD  GLU A 100     9488  10172   7803    162    121    651       C  
ATOM    689  OE1 GLU A 100      26.886   2.175  15.566  1.00 72.04           O  
ANISOU  689  OE1 GLU A 100     9463  10064   7846     88    153    634       O  
ATOM    690  OE2 GLU A 100      28.166   2.489  17.322  1.00 72.44           O  
ANISOU  690  OE2 GLU A 100     9479  10307   7739    226     75    573       O  
ATOM    691  N   CYS A 101      24.943  -2.831  16.371  1.00 67.49           N  
ANISOU  691  N   CYS A 101     9012   9402   7230    102    341   1219       N  
ATOM    692  CA  CYS A 101      23.965  -3.763  15.821  1.00 78.07           C  
ANISOU  692  CA  CYS A 101    10380  10640   8645     37    395   1336       C  
ATOM    693  C   CYS A 101      22.547  -3.380  16.226  1.00 82.14           C  
ANISOU  693  C   CYS A 101    10875  11214   9122     11    451   1371       C  
ATOM    694  O   CYS A 101      21.617  -3.463  15.415  1.00 75.99           O  
ANISOU  694  O   CYS A 101    10100  10344   8429    -69    485   1391       O  
ATOM    695  CB  CYS A 101      24.289  -5.181  16.281  1.00 82.53           C  
ANISOU  695  CB  CYS A 101    10978  11186   9195     76    404   1481       C  
ATOM    696  SG  CYS A 101      23.392  -6.472  15.408  1.00 89.02           S  
ANISOU  696  SG  CYS A 101    11839  11842  10141     -9    449   1615       S  
ATOM    697  N   PHE A 102      22.362  -2.953  17.478  1.00 80.48           N  
ANISOU  697  N   PHE A 102    10637  11161   8780     82    459   1376       N  
ATOM    698  CA  PHE A 102      21.054  -2.474  17.914  1.00 73.34           C  
ANISOU  698  CA  PHE A 102     9705  10332   7828     69    511   1396       C  
ATOM    699  C   PHE A 102      20.643  -1.215  17.165  1.00 70.25           C  
ANISOU  699  C   PHE A 102     9293   9910   7489     18    499   1255       C  
ATOM    700  O   PHE A 102      19.446  -0.960  16.983  1.00 70.89           O  
ANISOU  700  O   PHE A 102     9357   9989   7587    -26    545   1273       O  
ATOM    701  CB  PHE A 102      21.069  -2.202  19.419  1.00 80.36           C  
ANISOU  701  CB  PHE A 102    10569  11411   8553    170    516   1414       C  
ATOM    702  CG  PHE A 102      21.155  -3.440  20.266  1.00 78.04           C  
ANISOU  702  CG  PHE A 102    10292  11165   8195    219    545   1581       C  
ATOM    703  CD1 PHE A 102      20.508  -4.603  19.889  1.00 82.84           C  
ANISOU  703  CD1 PHE A 102    10922  11673   8879    159    595   1733       C  
ATOM    704  CD2 PHE A 102      21.875  -3.432  21.451  1.00 84.55           C  
ANISOU  704  CD2 PHE A 102    11109  12133   8884    327    519   1587       C  
ATOM    705  CE1 PHE A 102      20.581  -5.739  20.673  1.00 83.92           C  
ANISOU  705  CE1 PHE A 102    11075  11847   8964    202    620   1896       C  
ATOM    706  CE2 PHE A 102      21.952  -4.565  22.239  1.00 82.37           C  
ANISOU  706  CE2 PHE A 102    10849  11902   8545    376    546   1749       C  
ATOM    707  CZ  PHE A 102      21.304  -5.719  21.850  1.00 84.34           C  
ANISOU  707  CZ  PHE A 102    11123  12046   8878    312    598   1907       C  
ATOM    708  N   LEU A 103      21.618  -0.419  16.721  1.00 69.68           N  
ANISOU  708  N   LEU A 103     9217   9813   7445     25    438   1118       N  
ATOM    709  CA  LEU A 103      21.308   0.868  16.107  1.00 76.02           C  
ANISOU  709  CA  LEU A 103    10000  10594   8292    -15    420    982       C  
ATOM    710  C   LEU A 103      20.770   0.697  14.694  1.00 69.54           C  
ANISOU  710  C   LEU A 103     9195   9618   7608   -115    441    989       C  
ATOM    711  O   LEU A 103      19.720   1.250  14.346  1.00 70.33           O  
ANISOU  711  O   LEU A 103     9281   9707   7735   -159    470    965       O  
ATOM    712  CB  LEU A 103      22.546   1.755  16.082  1.00 83.27           C  
ANISOU  712  CB  LEU A 103    10905  11529   9206     19    346    843       C  
ATOM    713  CG  LEU A 103      23.209   2.114  17.403  1.00 91.92           C  
ANISOU  713  CG  LEU A 103    11979  12775  10170    120    307    801       C  
ATOM    714  CD1 LEU A 103      23.913   3.432  17.235  1.00 93.83           C  
ANISOU  714  CD1 LEU A 103    12195  13025  10429    127    239    634       C  
ATOM    715  CD2 LEU A 103      22.183   2.185  18.506  1.00 93.97           C  
ANISOU  715  CD2 LEU A 103    12223  13168  10313    172    351    852       C  
ATOM    716  N   GLN A 104      21.482  -0.057  13.856  1.00 66.67           N  
ANISOU  716  N   GLN A 104     8861   9141   7330   -147    424   1016       N  
ATOM    717  CA  GLN A 104      21.049  -0.230  12.475  1.00 62.97           C  
ANISOU  717  CA  GLN A 104     8410   8529   6986   -234    438   1013       C  
ATOM    718  C   GLN A 104      19.791  -1.078  12.357  1.00 63.15           C  
ANISOU  718  C   GLN A 104     8444   8510   7040   -282    497   1134       C  
ATOM    719  O   GLN A 104      19.283  -1.249  11.245  1.00 70.06           O  
ANISOU  719  O   GLN A 104     9331   9271   8016   -354    508   1134       O  
ATOM    720  CB  GLN A 104      22.184  -0.840  11.648  1.00 68.79           C  
ANISOU  720  CB  GLN A 104     9175   9166   7797   -244    402   1007       C  
ATOM    721  CG  GLN A 104      22.122  -0.488  10.165  1.00 70.18           C  
ANISOU  721  CG  GLN A 104     9359   9219   8086   -317    394    941       C  
ATOM    722  CD  GLN A 104      22.627   0.910   9.878  1.00 70.44           C  
ANISOU  722  CD  GLN A 104     9364   9276   8125   -318    357    803       C  
ATOM    723  OE1 GLN A 104      23.797   1.220  10.103  1.00 73.34           O  
ANISOU  723  OE1 GLN A 104     9719   9678   8470   -278    312    746       O  
ATOM    724  NE2 GLN A 104      21.742   1.766   9.384  1.00 75.78           N  
ANISOU  724  NE2 GLN A 104    10027   9933   8834   -366    372    751       N  
ATOM    725  N   HIS A 105      19.270  -1.603  13.464  1.00 60.25           N  
ANISOU  725  N   HIS A 105     8067   8234   6589   -243    533   1237       N  
ATOM    726  CA  HIS A 105      18.022  -2.349  13.455  1.00 66.02           C  
ANISOU  726  CA  HIS A 105     8798   8938   7350   -291    592   1358       C  
ATOM    727  C   HIS A 105      16.839  -1.513  13.927  1.00 57.58           C  
ANISOU  727  C   HIS A 105     7686   7966   6226   -293    631   1339       C  
ATOM    728  O   HIS A 105      15.734  -2.047  14.071  1.00 60.77           O  
ANISOU  728  O   HIS A 105     8077   8373   6641   -328    684   1443       O  
ATOM    729  CB  HIS A 105      18.159  -3.610  14.307  1.00 81.68           C  
ANISOU  729  CB  HIS A 105    10796  10949   9287   -254    614   1509       C  
ATOM    730  CG  HIS A 105      19.050  -4.646  13.697  1.00 97.35           C  
ANISOU  730  CG  HIS A 105    12827  12813  11350   -263    583   1549       C  
ATOM    731  ND1 HIS A 105      19.910  -5.425  14.441  1.00101.16           N  
ANISOU  731  ND1 HIS A 105    13329  13330  11778   -197    567   1621       N  
ATOM    732  CD2 HIS A 105      19.222  -5.022  12.407  1.00100.07           C  
ANISOU  732  CD2 HIS A 105    13200  13005  11818   -324    563   1523       C  
ATOM    733  CE1 HIS A 105      20.567  -6.241  13.637  1.00102.63           C  
ANISOU  733  CE1 HIS A 105    13554  13386  12055   -217    539   1637       C  
ATOM    734  NE2 HIS A 105      20.169  -6.016  12.398  1.00100.22           N  
ANISOU  734  NE2 HIS A 105    13254  12968  11856   -293    536   1576       N  
ATOM    735  N   LYS A 106      17.046  -0.220  14.172  1.00 54.25           N  
ANISOU  735  N   LYS A 106     7241   7622   5750   -256    604   1209       N  
ATOM    736  CA  LYS A 106      15.932   0.674  14.459  1.00 51.40           C  
ANISOU  736  CA  LYS A 106     6842   7339   5348   -257    635   1171       C  
ATOM    737  C   LYS A 106      14.997   0.736  13.259  1.00 46.00           C  
ANISOU  737  C   LYS A 106     6157   6540   4780   -350    656   1165       C  
ATOM    738  O   LYS A 106      15.432   0.973  12.128  1.00 40.44           O  
ANISOU  738  O   LYS A 106     5474   5721   4170   -396    622   1093       O  
ATOM    739  CB  LYS A 106      16.447   2.071  14.805  1.00 47.45           C  
ANISOU  739  CB  LYS A 106     6323   6918   4788   -202    588   1016       C  
ATOM    740  CG  LYS A 106      16.725   2.292  16.284  1.00 47.22           C  
ANISOU  740  CG  LYS A 106     6274   7058   4610   -100    584   1016       C  
ATOM    741  CD  LYS A 106      17.337   3.665  16.525  1.00 47.81           C  
ANISOU  741  CD  LYS A 106     6334   7189   4644    -50    523    849       C  
ATOM    742  CE  LYS A 106      17.254   4.063  17.991  1.00 46.70           C  
ANISOU  742  CE  LYS A 106     6166   7231   4347     54    523    833       C  
ATOM    743  NZ  LYS A 106      17.752   5.449  18.216  1.00 52.55           N  
ANISOU  743  NZ  LYS A 106     6891   8018   5058    100    457    661       N  
ATOM    744  N   ASP A 107      13.708   0.522  13.508  1.00 50.61           N  
ANISOU  744  N   ASP A 107     6713   7162   5354   -374    713   1243       N  
ATOM    745  CA  ASP A 107      12.708   0.414  12.452  1.00 42.16           C  
ANISOU  745  CA  ASP A 107     5637   5990   4391   -462    736   1258       C  
ATOM    746  C   ASP A 107      11.940   1.728  12.357  1.00 43.85           C  
ANISOU  746  C   ASP A 107     5816   6259   4586   -459    740   1153       C  
ATOM    747  O   ASP A 107      11.159   2.066  13.253  1.00 37.29           O  
ANISOU  747  O   ASP A 107     4945   5555   3670   -419    778   1175       O  
ATOM    748  CB  ASP A 107      11.767  -0.757  12.727  1.00 51.83           C  
ANISOU  748  CB  ASP A 107     6849   7211   5634   -500    794   1420       C  
ATOM    749  CG  ASP A 107      10.990  -1.180  11.500  1.00 55.19           C  
ANISOU  749  CG  ASP A 107     7280   7499   6193   -598    803   1444       C  
ATOM    750  OD1 ASP A 107      10.933  -0.394  10.532  1.00 48.45           O  
ANISOU  750  OD1 ASP A 107     6429   6581   5397   -629    775   1333       O  
ATOM    751  OD2 ASP A 107      10.439  -2.302  11.503  1.00 54.97           O  
ANISOU  751  OD2 ASP A 107     7250   7424   6212   -642    835   1575       O  
ATOM    752  N   ASP A 108      12.155   2.461  11.261  1.00 39.53           N  
ANISOU  752  N   ASP A 108     5283   5619   4119   -497    702   1043       N  
ATOM    753  CA  ASP A 108      11.451   3.720  11.049  1.00 33.44           C  
ANISOU  753  CA  ASP A 108     4483   4879   3344   -496    700    941       C  
ATOM    754  C   ASP A 108       9.992   3.514  10.668  1.00 41.38           C  
ANISOU  754  C   ASP A 108     5458   5869   4394   -552    749   1000       C  
ATOM    755  O   ASP A 108       9.198   4.455  10.775  1.00 44.55           O  
ANISOU  755  O   ASP A 108     5827   6330   4771   -537    760    939       O  
ATOM    756  CB  ASP A 108      12.154   4.542   9.968  1.00 37.31           C  
ANISOU  756  CB  ASP A 108     4997   5270   3910   -522    644    817       C  
ATOM    757  CG  ASP A 108      13.302   5.362  10.516  1.00 39.54           C  
ANISOU  757  CG  ASP A 108     5285   5606   4133   -457    593    717       C  
ATOM    758  OD1 ASP A 108      13.061   6.191  11.418  1.00 44.66           O  
ANISOU  758  OD1 ASP A 108     5906   6367   4696   -396    591    661       O  
ATOM    759  OD2 ASP A 108      14.444   5.175  10.047  1.00 37.18           O  
ANISOU  759  OD2 ASP A 108     5014   5238   3875   -464    554    691       O  
ATOM    760  N   ASN A 109       9.622   2.314  10.227  1.00 47.21           N  
ANISOU  760  N   ASN A 109     6207   6529   5202   -613    775   1114       N  
ATOM    761  CA  ASN A 109       8.253   1.997   9.818  1.00 37.59           C  
ANISOU  761  CA  ASN A 109     4956   5287   4039   -675    818   1177       C  
ATOM    762  C   ASN A 109       7.840   0.674  10.452  1.00 42.91           C  
ANISOU  762  C   ASN A 109     5617   5982   4705   -692    865   1341       C  
ATOM    763  O   ASN A 109       7.676  -0.338   9.760  1.00 34.72           O  
ANISOU  763  O   ASN A 109     4598   4829   3764   -761    866   1415       O  
ATOM    764  CB  ASN A 109       8.145   1.938   8.294  1.00 45.83           C  
ANISOU  764  CB  ASN A 109     6024   6178   5212   -752    790   1134       C  
ATOM    765  CG  ASN A 109       6.735   2.178   7.798  1.00 48.43           C  
ANISOU  765  CG  ASN A 109     6312   6499   5589   -803    819   1142       C  
ATOM    766  OD1 ASN A 109       5.887   2.695   8.524  1.00 40.39           O  
ANISOU  766  OD1 ASN A 109     5245   5595   4505   -773    855   1148       O  
ATOM    767  ND2 ASN A 109       6.476   1.804   6.550  1.00 48.66           N  
ANISOU  767  ND2 ASN A 109     6359   6399   5730   -874    801   1137       N  
ATOM    768  N   PRO A 110       7.654   0.649  11.771  1.00 39.06           N  
ANISOU  768  N   PRO A 110     5098   5640   4102   -630    903   1402       N  
ATOM    769  CA  PRO A 110       7.375  -0.621  12.447  1.00 44.33           C  
ANISOU  769  CA  PRO A 110     5755   6331   4756   -642    949   1570       C  
ATOM    770  C   PRO A 110       5.955  -1.103  12.197  1.00 50.59           C  
ANISOU  770  C   PRO A 110     6500   7110   5612   -714   1000   1666       C  
ATOM    771  O   PRO A 110       5.012  -0.316  12.078  1.00 50.96           O  
ANISOU  771  O   PRO A 110     6501   7210   5650   -720   1021   1617       O  
ATOM    772  CB  PRO A 110       7.594  -0.290  13.927  1.00 44.17           C  
ANISOU  772  CB  PRO A 110     5711   6493   4580   -542    973   1589       C  
ATOM    773  CG  PRO A 110       7.285   1.164  14.027  1.00 42.38           C  
ANISOU  773  CG  PRO A 110     5456   6350   4294   -496    963   1449       C  
ATOM    774  CD  PRO A 110       7.673   1.786  12.710  1.00 45.16           C  
ANISOU  774  CD  PRO A 110     5843   6566   4751   -542    906   1319       C  
ATOM    775  N   ASN A 111       5.813  -2.426  12.124  1.00 55.23           N  
ANISOU  775  N   ASN A 111     7097   7622   6267   -769   1018   1805       N  
ATOM    776  CA  ASN A 111       4.518  -3.058  11.900  1.00 57.26           C  
ANISOU  776  CA  ASN A 111     7305   7852   6598   -848   1063   1914       C  
ATOM    777  C   ASN A 111       3.639  -2.956  13.142  1.00 57.47           C  
ANISOU  777  C   ASN A 111     7262   8057   6518   -809   1137   2010       C  
ATOM    778  O   ASN A 111       3.350  -3.970  13.787  1.00 74.29           O  
ANISOU  778  O   ASN A 111     9371  10211   8643   -826   1180   2171       O  
ATOM    779  CB  ASN A 111       4.714  -4.522  11.499  1.00 68.67           C  
ANISOU  779  CB  ASN A 111     8784   9155   8152   -916   1053   2034       C  
ATOM    780  CG  ASN A 111       3.561  -5.063  10.679  1.00 84.04           C  
ANISOU  780  CG  ASN A 111    10699  11004  10230  -1020   1065   2088       C  
ATOM    781  OD1 ASN A 111       2.401  -4.961  11.074  1.00 93.00           O  
ANISOU  781  OD1 ASN A 111    11762  12223  11349  -1042   1119   2153       O  
ATOM    782  ND2 ASN A 111       3.878  -5.646   9.527  1.00 90.03           N  
ANISOU  782  ND2 ASN A 111    11505  11587  11114  -1081   1013   2060       N  
ATOM    783  N   LEU A 112       3.202  -1.741  13.480  1.00 42.58           N  
ANISOU  783  N   LEU A 112     5336   6296   4546   -755   1151   1914       N  
ATOM    784  CA  LEU A 112       2.433  -1.486  14.691  1.00 56.51           C  
ANISOU  784  CA  LEU A 112     7032   8252   6189   -698   1219   1983       C  
ATOM    785  C   LEU A 112       1.160  -0.724  14.331  1.00 67.39           C  
ANISOU  785  C   LEU A 112     8345   9674   7587   -723   1246   1934       C  
ATOM    786  O   LEU A 112       1.223   0.260  13.574  1.00 54.79           O  
ANISOU  786  O   LEU A 112     6765   8032   6020   -720   1202   1782       O  
ATOM    787  CB  LEU A 112       3.265  -0.692  15.709  1.00 54.28           C  
ANISOU  787  CB  LEU A 112     6763   8110   5749   -575   1206   1904       C  
ATOM    788  CG  LEU A 112       4.547  -1.354  16.219  1.00 52.47           C  
ANISOU  788  CG  LEU A 112     6591   7866   5478   -533   1180   1948       C  
ATOM    789  CD1 LEU A 112       5.142  -0.559  17.371  1.00 41.49           C  
ANISOU  789  CD1 LEU A 112     5198   6647   3921   -408   1174   1880       C  
ATOM    790  CD2 LEU A 112       4.289  -2.792  16.641  1.00 60.65           C  
ANISOU  790  CD2 LEU A 112     7617   8886   6541   -575   1227   2153       C  
ATOM    791  N   PRO A 113      -0.007  -1.158  14.820  1.00 80.64           N  
ANISOU  791  N   PRO A 113     9947  11437   9255   -750   1317   2063       N  
ATOM    792  CA  PRO A 113      -1.256  -0.495  14.429  1.00 93.88           C  
ANISOU  792  CA  PRO A 113    11557  13154  10960   -776   1343   2021       C  
ATOM    793  C   PRO A 113      -2.225  -0.213  15.571  1.00113.56           C  
ANISOU  793  C   PRO A 113    13960  15856  13331   -718   1423   2093       C  
ATOM    794  O   PRO A 113      -3.026  -1.090  15.911  1.00121.74           O  
ANISOU  794  O   PRO A 113    14937  16927  14392   -769   1484   2258       O  
ATOM    795  CB  PRO A 113      -1.861  -1.516  13.462  1.00 95.80           C  
ANISOU  795  CB  PRO A 113    11790  13241  11368   -905   1342   2113       C  
ATOM    796  CG  PRO A 113      -1.307  -2.901  13.997  1.00 91.50           C  
ANISOU  796  CG  PRO A 113    11272  12656  10838   -929   1358   2278       C  
ATOM    797  CD  PRO A 113      -0.253  -2.585  15.057  1.00 85.02           C  
ANISOU  797  CD  PRO A 113    10488  11949   9866   -815   1356   2256       C  
ATOM    798  N   ARG A 114      -2.191   0.997  16.145  1.00120.10           N  
ANISOU  798  N   ARG A 114    14774  16824  14034   -613   1422   1973       N  
ATOM    799  CA  ARG A 114      -3.174   1.430  17.141  1.00120.50           C  
ANISOU  799  CA  ARG A 114    14736  17083  13964   -546   1494   2015       C  
ATOM    800  C   ARG A 114      -2.912   2.855  17.618  1.00117.74           C  
ANISOU  800  C   ARG A 114    14393  16854  13489   -423   1468   1843       C  
ATOM    801  O   ARG A 114      -2.967   3.119  18.823  1.00117.61           O  
ANISOU  801  O   ARG A 114    14342  17025  13318   -321   1508   1864       O  
ATOM    802  CB  ARG A 114      -3.180   0.496  18.358  1.00116.43           C  
ANISOU  802  CB  ARG A 114    14189  16694  13356   -516   1563   2199       C  
ATOM    803  CG  ARG A 114      -4.524  -0.167  18.631  1.00111.31           C  
ANISOU  803  CG  ARG A 114    13441  16121  12731   -574   1650   2369       C  
ATOM    804  CD  ARG A 114      -4.359  -1.461  19.417  1.00109.41           C  
ANISOU  804  CD  ARG A 114    13204  15878  12490   -586   1678   2538       C  
ATOM    805  NE  ARG A 114      -4.025  -1.212  20.817  1.00107.16           N  
ANISOU  805  NE  ARG A 114    12909  15782  12023   -456   1707   2552       N  
ATOM    806  CZ  ARG A 114      -3.267  -2.012  21.559  1.00104.32           C  
ANISOU  806  CZ  ARG A 114    12592  15423  11623   -424   1700   2636       C  
ATOM    807  NH1 ARG A 114      -2.756  -3.119  21.038  1.00101.28           N  
ANISOU  807  NH1 ARG A 114    12262  14854  11366   -511   1667   2712       N  
ATOM    808  NH2 ARG A 114      -3.017  -1.704  22.825  1.00104.44           N  
ANISOU  808  NH2 ARG A 114    12594  15621  11469   -300   1723   2638       N  
ATOM    809  N   LEU A 115      -2.650   3.786  16.701  1.00112.77           N  
ANISOU  809  N   LEU A 115    13804  16122  12921   -429   1400   1673       N  
ATOM    810  CA  LEU A 115      -2.140   5.102  17.099  1.00111.73           C  
ANISOU  810  CA  LEU A 115    13696  16069  12687   -317   1356   1500       C  
ATOM    811  C   LEU A 115      -3.224   6.166  17.263  1.00117.78           C  
ANISOU  811  C   LEU A 115    14396  16954  13402   -260   1380   1418       C  
ATOM    812  O   LEU A 115      -3.025   7.309  16.838  1.00118.94           O  
ANISOU  812  O   LEU A 115    14569  17065  13556   -222   1323   1251       O  
ATOM    813  CB  LEU A 115      -1.075   5.565  16.109  1.00102.33           C  
ANISOU  813  CB  LEU A 115    12593  14705  11585   -344   1265   1362       C  
ATOM    814  CG  LEU A 115      -0.058   6.553  16.697  1.00 98.98           C  
ANISOU  814  CG  LEU A 115    12211  14339  11058   -235   1209   1217       C  
ATOM    815  CD1 LEU A 115       0.214   6.256  18.172  1.00 97.41           C  
ANISOU  815  CD1 LEU A 115    11992  14320  10699   -139   1248   1286       C  
ATOM    816  CD2 LEU A 115       1.235   6.577  15.898  1.00 98.37           C  
ANISOU  816  CD2 LEU A 115    12218  14093  11063   -273   1130   1138       C  
ATOM    817  N   VAL A 120     -14.159   8.703  23.502  1.00105.91           N  
ANISOU  817  N   VAL A 120    11978  17395  10869    532   2014   1660       N  
ATOM    818  CA  VAL A 120     -12.805   8.243  23.919  1.00103.33           C  
ANISOU  818  CA  VAL A 120    11665  17228  10368    684   2006   1618       C  
ATOM    819  C   VAL A 120     -12.485   9.128  25.109  1.00103.80           C  
ANISOU  819  C   VAL A 120    11657  17399  10385    695   2065   1791       C  
ATOM    820  O   VAL A 120     -11.376   9.084  25.619  1.00103.52           O  
ANISOU  820  O   VAL A 120    11648  17445  10240    773   2060   1821       O  
ATOM    821  CB  VAL A 120     -11.739   8.331  22.811  1.00 97.63           C  
ANISOU  821  CB  VAL A 120    10930  16639   9527    843   1976   1412       C  
ATOM    822  CG1 VAL A 120     -11.797   7.119  21.896  1.00 90.36           C  
ANISOU  822  CG1 VAL A 120    10075  15600   8657    828   1918   1244       C  
ATOM    823  CG2 VAL A 120     -11.842   9.624  22.019  1.00100.91           C  
ANISOU  823  CG2 VAL A 120    11234  17168   9941    872   2026   1434       C  
ATOM    824  N   ASP A 121     -13.461   9.927  25.508  1.00110.57           N  
ANISOU  824  N   ASP A 121    12423  18264  11325    620   2120   1907       N  
ATOM    825  CA  ASP A 121     -13.280  10.698  26.752  1.00116.56           C  
ANISOU  825  CA  ASP A 121    13107  19152  12028    647   2178   2060       C  
ATOM    826  C   ASP A 121     -13.602   9.729  27.889  1.00118.49           C  
ANISOU  826  C   ASP A 121    13392  19313  12314    567   2188   2227       C  
ATOM    827  O   ASP A 121     -13.733  10.202  29.015  1.00119.12           O  
ANISOU  827  O   ASP A 121    13429  19511  12322    612   2228   2344       O  
ATOM    828  CB  ASP A 121     -14.154  11.944  26.770  1.00120.64           C  
ANISOU  828  CB  ASP A 121    13513  19696  12629    583   2232   2141       C  
ATOM    829  CG  ASP A 121     -13.494  13.152  26.133  1.00123.67           C  
ANISOU  829  CG  ASP A 121    13894  19882  13213    389   2242   2269       C  
ATOM    830  OD1 ASP A 121     -12.687  12.952  25.209  1.00125.35           O  
ANISOU  830  OD1 ASP A 121    14108  20043  13477    312   2265   2435       O  
ATOM    831  OD2 ASP A 121     -13.803  14.280  26.560  1.00124.01           O  
ANISOU  831  OD2 ASP A 121    13934  19821  13364    317   2223   2201       O  
ATOM    832  N   VAL A 122     -13.786   8.439  27.586  1.00 30.00           N  
ATOM    833  CA  VAL A 122     -13.970   7.416  28.649  1.00 30.00           C  
ATOM    834  C   VAL A 122     -12.672   6.615  28.709  1.00 30.00           C  
ATOM    835  O   VAL A 122     -12.708   5.490  29.220  1.00 30.00           O  
ATOM    836  CB  VAL A 122     -15.217   6.538  28.460  1.00 30.00           C  
ATOM    837  CG1 VAL A 122     -16.493   7.362  28.477  1.00 30.00           C  
ATOM    838  CG2 VAL A 122     -15.149   5.692  27.201  1.00 30.00           C  
ATOM    839  N   MET A 123     -11.598   7.128  28.108  1.00116.94           N  
ANISOU  839  N   MET A 123    13483  18804  12144    519   2040   2089       N  
ATOM    840  CA  MET A 123     -10.265   6.508  28.300  1.00112.67           C  
ANISOU  840  CA  MET A 123    13044  18222  11543    567   1979   1989       C  
ATOM    841  C   MET A 123      -9.732   7.367  29.427  1.00108.95           C  
ANISOU  841  C   MET A 123    12579  17942  10877    752   1956   1872       C  
ATOM    842  O   MET A 123      -8.750   6.976  30.037  1.00104.71           O  
ANISOU  842  O   MET A 123    12084  17443  10259    805   1938   1906       O  
ATOM    843  CB  MET A 123      -9.324   6.788  27.128  1.00111.60           C  
ANISOU  843  CB  MET A 123    12963  17951  11488    513   1931   1852       C  
ATOM    844  CG  MET A 123      -9.749   6.271  25.776  1.00110.96           C  
ANISOU  844  CG  MET A 123    12969  17883  11306    609   1863   1690       C  
ATOM    845  SD  MET A 123      -8.839   7.194  24.501  1.00109.83           S  
ANISOU  845  SD  MET A 123    12894  17566  11269    546   1795   1522       S  
ATOM    846  CE  MET A 123      -7.292   6.292  24.466  1.00103.90           C  
ANISOU  846  CE  MET A 123    12132  16603  10742    335   1823   1688       C  
ATOM    847  N   CYS A 124     -10.265   8.580  29.540  1.00104.63           N  
ANISOU  847  N   CYS A 124    11991  17511  10253    855   1950   1727       N  
ATOM    848  CA  CYS A 124      -9.928   9.562  30.605  1.00 93.28           C  
ANISOU  848  CA  CYS A 124    10566  16238   8639   1034   1912   1585       C  
ATOM    849  C   CYS A 124     -10.152   8.868  31.942  1.00 96.31           C  
ANISOU  849  C   CYS A 124    10900  16782   8912   1115   1951   1704       C  
ATOM    850  O   CYS A 124      -9.609   9.331  32.960  1.00102.44           O  
ANISOU  850  O   CYS A 124    11701  17677   9545   1253   1914   1619       O  
ATOM    851  CB  CYS A 124     -10.771  10.810  30.449  1.00 89.42           C  
ANISOU  851  CB  CYS A 124    10039  15828   8108   1124   1896   1409       C  
ATOM    852  SG  CYS A 124     -10.766  11.839  31.918  1.00 98.08           S  
ANISOU  852  SG  CYS A 124    11100  17168   8999   1348   1873   1278       S  
ATOM    853  N   THR A 125     -10.887   7.765  31.917  1.00 75.80           N  
ANISOU  853  N   THR A 125     8233  14189   6380   1031   2023   1899       N  
ATOM    854  CA  THR A 125     -10.984   6.979  33.152  1.00 84.33           C  
ANISOU  854  CA  THR A 125     9276  15396   7371   1086   2061   2040       C  
ATOM    855  C   THR A 125      -9.595   6.405  33.408  1.00 85.18           C  
ANISOU  855  C   THR A 125     9467  15442   7454   1082   2025   2081       C  
ATOM    856  O   THR A 125      -9.131   6.554  34.535  1.00 83.43           O  
ANISOU  856  O   THR A 125     9249  15356   7093   1204   2014   2077       O  
ATOM    857  CB  THR A 125     -11.972   5.826  32.989  1.00 90.95           C  
ANISOU  857  CB  THR A 125    10031  16215   8310    973   2139   2248       C  
ATOM    858  OG1 THR A 125     -11.771   5.270  31.690  1.00 98.82           O  
ANISOU  858  OG1 THR A 125    11078  17012   9457    815   2138   2372       O  
ATOM    859  CG2 THR A 125     -13.406   6.264  33.186  1.00 94.48           C  
ANISOU  859  CG2 THR A 125    10405  16671   8822    939   2167   2206       C  
ATOM    860  N   ALA A 126      -8.934   5.838  32.390  1.00 81.25           N  
ANISOU  860  N   ALA A 126     9038  14741   7092    949   2003   2117       N  
ATOM    861  CA  ALA A 126      -7.657   5.166  32.615  1.00 80.00           C  
ANISOU  861  CA  ALA A 126     8961  14513   6924    937   1968   2163       C  
ATOM    862  C   ALA A 126      -6.611   6.116  33.181  1.00 74.80           C  
ANISOU  862  C   ALA A 126     8362  13939   6120   1082   1897   1983       C  
ATOM    863  O   ALA A 126      -5.711   5.681  33.910  1.00 73.13           O  
ANISOU  863  O   ALA A 126     8191  13760   5836   1134   1874   2019       O  
ATOM    864  CB  ALA A 126      -7.152   4.533  31.318  1.00 75.74           C  
ANISOU  864  CB  ALA A 126     8485  13737   6557    775   1949   2208       C  
ATOM    865  N   PHE A 127      -6.705   7.407  32.856  1.00 62.49           N  
ANISOU  865  N   PHE A 127     6809  12414   4522   1150   1857   1786       N  
ATOM    866  CA  PHE A 127      -5.812   8.384  33.468  1.00 67.47           C  
ANISOU  866  CA  PHE A 127     7488  13132   5014   1297   1783   1599       C  
ATOM    867  C   PHE A 127      -6.002   8.419  34.979  1.00 73.46           C  
ANISOU  867  C   PHE A 127     8198  14100   5612   1445   1796   1621       C  
ATOM    868  O   PHE A 127      -5.029   8.400  35.739  1.00 75.39           O  
ANISOU  868  O   PHE A 127     8487  14399   5759   1530   1750   1585       O  
ATOM    869  CB  PHE A 127      -6.048   9.769  32.864  1.00 72.11           C  
ANISOU  869  CB  PHE A 127     8083  13717   5599   1344   1739   1385       C  
ATOM    870  CG  PHE A 127      -5.286  10.868  33.553  1.00 73.71           C  
ANISOU  870  CG  PHE A 127     8327  14016   5665   1504   1655   1176       C  
ATOM    871  CD1 PHE A 127      -3.912  10.973  33.410  1.00 74.69           C  
ANISOU  871  CD1 PHE A 127     8540  14060   5777   1511   1580   1090       C  
ATOM    872  CD2 PHE A 127      -5.944  11.795  34.346  1.00 72.69           C  
ANISOU  872  CD2 PHE A 127     8145  14052   5424   1648   1646   1063       C  
ATOM    873  CE1 PHE A 127      -3.208  11.982  34.043  1.00 81.06           C  
ANISOU  873  CE1 PHE A 127     9384  14947   6470   1654   1494    891       C  
ATOM    874  CE2 PHE A 127      -5.246  12.806  34.983  1.00 74.39           C  
ANISOU  874  CE2 PHE A 127     8398  14342   5524   1794   1558    864       C  
ATOM    875  CZ  PHE A 127      -3.877  12.899  34.832  1.00 80.88           C  
ANISOU  875  CZ  PHE A 127     9308  15078   6342   1795   1481    776       C  
ATOM    876  N   HIS A 128      -7.255   8.446  35.435  1.00 71.47           N  
ANISOU  876  N   HIS A 128     7852  13971   5331   1477   1858   1685       N  
ATOM    877  CA  HIS A 128      -7.523   8.575  36.861  1.00 76.48           C  
ANISOU  877  CA  HIS A 128     8434  14820   5807   1627   1872   1698       C  
ATOM    878  C   HIS A 128      -7.412   7.256  37.615  1.00 72.83           C  
ANISOU  878  C   HIS A 128     7950  14394   5329   1599   1923   1917       C  
ATOM    879  O   HIS A 128      -7.312   7.274  38.846  1.00 71.69           O  
ANISOU  879  O   HIS A 128     7778  14419   5043   1729   1924   1930       O  
ATOM    880  CB  HIS A 128      -8.905   9.193  37.079  1.00 78.91           C  
ANISOU  880  CB  HIS A 128     8646  15257   6080   1684   1915   1672       C  
ATOM    881  CG  HIS A 128      -8.944  10.670  36.837  1.00 90.88           C  
ANISOU  881  CG  HIS A 128    10178  16803   7550   1781   1851   1429       C  
ATOM    882  ND1 HIS A 128      -7.960  11.522  37.292  1.00 94.45           N  
ANISOU  882  ND1 HIS A 128    10692  17293   7902   1905   1762   1241       N  
ATOM    883  CD2 HIS A 128      -9.838  11.444  36.179  1.00 95.81           C  
ANISOU  883  CD2 HIS A 128    10765  17417   8223   1773   1858   1339       C  
ATOM    884  CE1 HIS A 128      -8.250  12.759  36.929  1.00 95.18           C  
ANISOU  884  CE1 HIS A 128    10786  17390   7986   1968   1715   1045       C  
ATOM    885  NE2 HIS A 128      -9.384  12.739  36.252  1.00 96.48           N  
ANISOU  885  NE2 HIS A 128    10893  17529   8238   1892   1774   1101       N  
ATOM    886  N   ASP A 129      -7.425   6.116  36.917  1.00 77.64           N  
ANISOU  886  N   ASP A 129     8571  14847   6081   1438   1963   2087       N  
ATOM    887  CA  ASP A 129      -7.175   4.848  37.596  1.00 84.41           C  
ANISOU  887  CA  ASP A 129     9422  15717   6932   1411   2001   2286       C  
ATOM    888  C   ASP A 129      -5.700   4.658  37.919  1.00 86.18           C  
ANISOU  888  C   ASP A 129     9735  15905   7102   1453   1938   2248       C  
ATOM    889  O   ASP A 129      -5.368   4.064  38.950  1.00 73.82           O  
ANISOU  889  O   ASP A 129     8160  14438   5449   1519   1951   2344       O  
ATOM    890  CB  ASP A 129      -7.669   3.668  36.755  1.00 88.99           C  
ANISOU  890  CB  ASP A 129     9988  16130   7692   1225   2055   2474       C  
ATOM    891  CG  ASP A 129      -8.974   3.957  36.048  1.00101.47           C  
ANISOU  891  CG  ASP A 129    11498  17692   9363   1154   2099   2478       C  
ATOM    892  OD1 ASP A 129      -9.855   4.595  36.660  1.00106.68           O  
ANISOU  892  OD1 ASP A 129    12081  18523   9929   1252   2127   2438       O  
ATOM    893  OD2 ASP A 129      -9.126   3.534  34.883  1.00102.04           O  
ANISOU  893  OD2 ASP A 129    11590  17580   9601   1003   2104   2520       O  
ATOM    894  N   ASN A 130      -4.809   5.149  37.055  1.00 66.90           N  
ANISOU  894  N   ASN A 130     7377  13329   4712   1418   1870   2110       N  
ATOM    895  CA  ASN A 130      -3.368   4.999  37.270  1.00 66.38           C  
ANISOU  895  CA  ASN A 130     7397  13221   4603   1453   1804   2064       C  
ATOM    896  C   ASN A 130      -2.677   6.074  36.421  1.00 64.52           C  
ANISOU  896  C   ASN A 130     7230  12896   4388   1459   1725   1847       C  
ATOM    897  O   ASN A 130      -2.298   5.821  35.277  1.00 62.80           O  
ANISOU  897  O   ASN A 130     7065  12497   4300   1334   1710   1854       O  
ATOM    898  CB  ASN A 130      -2.891   3.604  36.912  1.00 66.01           C  
ANISOU  898  CB  ASN A 130     7387  13025   4668   1325   1826   2252       C  
ATOM    899  CG  ASN A 130      -1.494   3.311  37.426  1.00 68.33           C  
ANISOU  899  CG  ASN A 130     7753  13316   4893   1384   1769   2236       C  
ATOM    900  OD1 ASN A 130      -0.731   4.222  37.746  1.00 68.50           O  
ANISOU  900  OD1 ASN A 130     7811  13403   4811   1494   1698   2060       O  
ATOM    901  ND2 ASN A 130      -1.151   2.030  37.506  1.00 73.02           N  
ANISOU  901  ND2 ASN A 130     8366  13830   5547   1310   1794   2418       N  
ATOM    902  N   GLU A 131      -2.524   7.267  37.005  1.00 67.29           N  
ANISOU  902  N   GLU A 131     7579  13378   4612   1606   1671   1656       N  
ATOM    903  CA  GLU A 131      -1.910   8.387  36.295  1.00 70.61           C  
ANISOU  903  CA  GLU A 131     8059  13726   5044   1624   1589   1435       C  
ATOM    904  C   GLU A 131      -0.492   8.068  35.851  1.00 73.55           C  
ANISOU  904  C   GLU A 131     8525  13967   5455   1577   1527   1410       C  
ATOM    905  O   GLU A 131      -0.036   8.569  34.816  1.00 60.45           O  
ANISOU  905  O   GLU A 131     6919  12177   3872   1517   1481   1298       O  
ATOM    906  CB  GLU A 131      -1.901   9.633  37.184  1.00 82.44           C  
ANISOU  906  CB  GLU A 131     9541  15388   6395   1803   1531   1236       C  
ATOM    907  CG  GLU A 131      -3.265  10.245  37.443  1.00 93.31           C  
ANISOU  907  CG  GLU A 131    10832  16884   7737   1860   1576   1208       C  
ATOM    908  CD  GLU A 131      -3.981   9.610  38.622  1.00102.03           C  
ANISOU  908  CD  GLU A 131    11857  18160   8751   1926   1645   1364       C  
ATOM    909  OE1 GLU A 131      -3.889   8.375  38.787  1.00101.85           O  
ANISOU  909  OE1 GLU A 131    11828  18108   8764   1851   1698   1567       O  
ATOM    910  OE2 GLU A 131      -4.638  10.349  39.383  1.00107.81           O  
ANISOU  910  OE2 GLU A 131    12530  19055   9376   2054   1644   1284       O  
ATOM    911  N   GLU A 132       0.220   7.246  36.617  1.00 62.99           N  
ANISOU  911  N   GLU A 132     7206  12666   4063   1606   1523   1514       N  
ATOM    912  CA  GLU A 132       1.622   6.989  36.319  1.00 61.95           C  
ANISOU  912  CA  GLU A 132     7159  12429   3951   1582   1457   1481       C  
ATOM    913  C   GLU A 132       1.767   6.015  35.155  1.00 64.92           C  
ANISOU  913  C   GLU A 132     7572  12605   4491   1406   1489   1621       C  
ATOM    914  O   GLU A 132       2.408   6.335  34.149  1.00 66.59           O  
ANISOU  914  O   GLU A 132     7843  12682   4777   1342   1442   1531       O  
ATOM    915  CB  GLU A 132       2.327   6.473  37.577  1.00 68.81           C  
ANISOU  915  CB  GLU A 132     8031  13413   4700   1684   1440   1539       C  
ATOM    916  CG  GLU A 132       2.481   7.535  38.674  1.00 64.73           C  
ANISOU  916  CG  GLU A 132     7494  13079   4021   1866   1381   1363       C  
ATOM    917  CD  GLU A 132       1.161   7.912  39.338  1.00 83.02           C  
ANISOU  917  CD  GLU A 132     9721  15552   6270   1940   1439   1377       C  
ATOM    918  OE1 GLU A 132       1.114   8.945  40.041  1.00 89.99           O  
ANISOU  918  OE1 GLU A 132    10584  16567   7040   2081   1389   1211       O  
ATOM    919  OE2 GLU A 132       0.168   7.178  39.154  1.00 85.23           O  
ANISOU  919  OE2 GLU A 132     9949  15820   6615   1857   1530   1552       O  
ATOM    920  N   THR A 133       1.153   4.831  35.261  1.00 70.79           N  
ANISOU  920  N   THR A 133     8278  13323   5298   1327   1567   1839       N  
ATOM    921  CA  THR A 133       1.214   3.865  34.166  1.00 60.00           C  
ANISOU  921  CA  THR A 133     6942  11757   4100   1159   1594   1973       C  
ATOM    922  C   THR A 133       0.618   4.432  32.881  1.00 67.38           C  
ANISOU  922  C   THR A 133     7873  12578   5151   1062   1601   1900       C  
ATOM    923  O   THR A 133       1.068   4.082  31.784  1.00 58.14           O  
ANISOU  923  O   THR A 133     6754  11232   4106    946   1585   1920       O  
ATOM    924  CB  THR A 133       0.498   2.571  34.563  1.00 61.28           C  
ANISOU  924  CB  THR A 133     7055  11915   4313   1096   1673   2206       C  
ATOM    925  OG1 THR A 133       1.041   2.080  35.796  1.00 67.66           O  
ANISOU  925  OG1 THR A 133     7863  12839   5005   1195   1668   2273       O  
ATOM    926  CG2 THR A 133       0.674   1.505  33.492  1.00 64.22           C  
ANISOU  926  CG2 THR A 133     7467  12069   4866    929   1687   2338       C  
ATOM    927  N   PHE A 134      -0.379   5.313  32.994  1.00 65.85           N  
ANISOU  927  N   PHE A 134     7619  12483   4916   1113   1623   1814       N  
ATOM    928  CA  PHE A 134      -0.945   5.953  31.811  1.00 61.01           C  
ANISOU  928  CA  PHE A 134     7001  11776   4404   1035   1626   1730       C  
ATOM    929  C   PHE A 134       0.101   6.794  31.089  1.00 59.67           C  
ANISOU  929  C   PHE A 134     6908  11526   4237   1043   1544   1548       C  
ATOM    930  O   PHE A 134       0.237   6.720  29.862  1.00 64.14           O  
ANISOU  930  O   PHE A 134     7507  11935   4929    927   1538   1545       O  
ATOM    931  CB  PHE A 134      -2.147   6.812  32.210  1.00 67.40           C  
ANISOU  931  CB  PHE A 134     7732  12728   5149   1112   1657   1658       C  
ATOM    932  CG  PHE A 134      -2.968   7.297  31.047  1.00 66.12           C  
ANISOU  932  CG  PHE A 134     7546  12477   5099   1025   1677   1610       C  
ATOM    933  CD1 PHE A 134      -4.016   6.536  30.555  1.00 63.75           C  
ANISOU  933  CD1 PHE A 134     7190  12114   4919    906   1748   1767       C  
ATOM    934  CD2 PHE A 134      -2.700   8.521  30.453  1.00 69.21           C  
ANISOU  934  CD2 PHE A 134     7970  12848   5479   1063   1620   1404       C  
ATOM    935  CE1 PHE A 134      -4.776   6.981  29.489  1.00 69.04           C  
ANISOU  935  CE1 PHE A 134     7834  12706   5692    829   1764   1721       C  
ATOM    936  CE2 PHE A 134      -3.457   8.972  29.387  1.00 67.48           C  
ANISOU  936  CE2 PHE A 134     7727  12552   5361    987   1639   1361       C  
ATOM    937  CZ  PHE A 134      -4.496   8.201  28.905  1.00 62.32           C  
ANISOU  937  CZ  PHE A 134     7014  11841   4822    871   1711   1521       C  
ATOM    938  N   LEU A 135       0.857   7.598  31.839  1.00 56.33           N  
ANISOU  938  N   LEU A 135     6513  11210   3680   1181   1476   1392       N  
ATOM    939  CA  LEU A 135       1.837   8.484  31.217  1.00 72.79           C  
ANISOU  939  CA  LEU A 135     8666  13226   5763   1197   1391   1202       C  
ATOM    940  C   LEU A 135       3.034   7.706  30.681  1.00 68.35           C  
ANISOU  940  C   LEU A 135     8177  12496   5295   1109   1346   1258       C  
ATOM    941  O   LEU A 135       3.587   8.055  29.633  1.00 54.65           O  
ANISOU  941  O   LEU A 135     6496  10552   3717   1023   1270   1147       O  
ATOM    942  CB  LEU A 135       2.292   9.548  32.215  1.00 80.83           C  
ANISOU  942  CB  LEU A 135     9691  14389   6630   1367   1316   1009       C  
ATOM    943  CG  LEU A 135       3.307  10.565  31.687  1.00 85.34           C  
ANISOU  943  CG  LEU A 135    10331  14855   7240   1383   1198    782       C  
ATOM    944  CD1 LEU A 135       2.802  11.204  30.401  1.00 78.10           C  
ANISOU  944  CD1 LEU A 135     9420  13747   6506   1277   1172    688       C  
ATOM    945  CD2 LEU A 135       3.613  11.624  32.735  1.00 84.43           C  
ANISOU  945  CD2 LEU A 135    10213  14918   6948   1563   1134    595       C  
ATOM    946  N   LYS A 136       3.452   6.651  31.386  1.00 74.66           N  
ANISOU  946  N   LYS A 136     8982  13346   6039   1122   1376   1416       N  
ATOM    947  CA  LYS A 136       4.604   5.880  30.926  1.00 74.41           C  
ANISOU  947  CA  LYS A 136     9019  13172   6081   1051   1337   1475       C  
ATOM    948  C   LYS A 136       4.248   4.975  29.751  1.00 65.80           C  
ANISOU  948  C   LYS A 136     7936  11871   5192    875   1374   1611       C  
ATOM    949  O   LYS A 136       5.110   4.685  28.912  1.00 56.51           O  
ANISOU  949  O   LYS A 136     6823  10496   4153    789   1313   1584       O  
ATOM    950  CB  LYS A 136       5.199   5.064  32.074  1.00 76.82           C  
ANISOU  950  CB  LYS A 136     9329  13571   6287   1123   1339   1584       C  
ATOM    951  CG  LYS A 136       5.882   5.914  33.152  1.00 85.36           C  
ANISOU  951  CG  LYS A 136    10420  14809   7205   1288   1267   1422       C  
ATOM    952  CD  LYS A 136       5.359   5.625  34.551  1.00 90.46           C  
ANISOU  952  CD  LYS A 136    11008  15628   7736   1392   1306   1500       C  
ATOM    953  CE  LYS A 136       5.751   6.727  35.519  1.00 94.10           C  
ANISOU  953  CE  LYS A 136    11463  16246   8044   1558   1234   1306       C  
ATOM    954  NZ  LYS A 136       5.069   8.004  35.177  1.00 92.82           N  
ANISOU  954  NZ  LYS A 136    11277  16113   7876   1590   1216   1130       N  
ATOM    955  N   LYS A 137       2.995   4.517  29.667  1.00 61.69           N  
ANISOU  955  N   LYS A 137     7353  11390   4699    821   1470   1754       N  
ATOM    956  CA  LYS A 137       2.568   3.799  28.470  1.00 61.23           C  
ANISOU  956  CA  LYS A 137     7298  11128   4838    655   1496   1855       C  
ATOM    957  C   LYS A 137       2.489   4.730  27.269  1.00 56.35           C  
ANISOU  957  C   LYS A 137     6703  10343   4363    590   1431   1673       C  
ATOM    958  O   LYS A 137       2.627   4.280  26.127  1.00 49.54           O  
ANISOU  958  O   LYS A 137     5876   9271   3678    460   1410   1697       O  
ATOM    959  CB  LYS A 137       1.222   3.116  28.707  1.00 68.97           C  
ANISOU  959  CB  LYS A 137     8200  12148   5856    606   1587   2020       C  
ATOM    960  CG  LYS A 137       0.924   1.989  27.726  1.00 73.86           C  
ANISOU  960  CG  LYS A 137     8827  12571   6665    441   1616   2173       C  
ATOM    961  CD  LYS A 137      -0.307   1.197  28.135  1.00 64.00           C  
ANISOU  961  CD  LYS A 137     7504  11348   5465    397   1687   2330       C  
ATOM    962  CE  LYS A 137      -0.106   0.510  29.475  1.00 58.32           C  
ANISOU  962  CE  LYS A 137     6771  10743   4644    478   1706   2438       C  
ATOM    963  NZ  LYS A 137      -1.335  -0.210  29.913  1.00 58.90           N  
ANISOU  963  NZ  LYS A 137     6767  10857   4757    439   1777   2589       N  
ATOM    964  N   TYR A 138       2.266   6.025  27.506  1.00 56.56           N  
ANISOU  964  N   TYR A 138     6713  10461   4315    681   1397   1491       N  
ATOM    965  CA  TYR A 138       2.335   7.000  26.423  1.00 59.33           C  
ANISOU  965  CA  TYR A 138     7094  10653   4795    632   1324   1308       C  
ATOM    966  C   TYR A 138       3.757   7.108  25.886  1.00 58.78           C  
ANISOU  966  C   TYR A 138     7109  10420   4804    602   1223   1205       C  
ATOM    967  O   TYR A 138       3.973   7.118  24.668  1.00 61.02           O  
ANISOU  967  O   TYR A 138     7429  10500   5255    493   1184   1165       O  
ATOM    968  CB  TYR A 138       1.831   8.359  26.911  1.00 61.54           C  
ANISOU  968  CB  TYR A 138     7339  11073   4969    749   1305   1137       C  
ATOM    969  CG  TYR A 138       2.184   9.518  26.004  1.00 72.20           C  
ANISOU  969  CG  TYR A 138     8732  12274   6426    728   1210    924       C  
ATOM    970  CD1 TYR A 138       1.401   9.824  24.899  1.00 76.89           C  
ANISOU  970  CD1 TYR A 138     9313  12741   7162    635   1217    898       C  
ATOM    971  CD2 TYR A 138       3.296  10.312  26.258  1.00 72.29           C  
ANISOU  971  CD2 TYR A 138     8795  12272   6398    801   1111    753       C  
ATOM    972  CE1 TYR A 138       1.718  10.883  24.068  1.00 75.52           C  
ANISOU  972  CE1 TYR A 138     9178  12432   7085    617   1133    714       C  
ATOM    973  CE2 TYR A 138       3.622  11.371  25.434  1.00 71.33           C  
ANISOU  973  CE2 TYR A 138     8710  12010   6381    777   1025    569       C  
ATOM    974  CZ  TYR A 138       2.829  11.653  24.341  1.00 73.37           C  
ANISOU  974  CZ  TYR A 138     8957  12144   6777    686   1038    554       C  
ATOM    975  OH  TYR A 138       3.150  12.708  23.518  1.00 69.13           O  
ANISOU  975  OH  TYR A 138     8455  11467   6343    663    955    382       O  
ATOM    976  N   LEU A 139       4.741   7.190  26.786  1.00 52.61           N  
ANISOU  976  N   LEU A 139     6355   9733   3901    703   1181   1162       N  
ATOM    977  CA  LEU A 139       6.137   7.217  26.361  1.00 56.06           C  
ANISOU  977  CA  LEU A 139     6864  10030   4405    679   1088   1077       C  
ATOM    978  C   LEU A 139       6.501   5.952  25.596  1.00 57.81           C  
ANISOU  978  C   LEU A 139     7119  10085   4761    554   1107   1229       C  
ATOM    979  O   LEU A 139       7.232   6.006  24.600  1.00 57.36           O  
ANISOU  979  O   LEU A 139     7113   9841   4839    476   1044   1161       O  
ATOM    980  CB  LEU A 139       7.052   7.382  27.575  1.00 56.13           C  
ANISOU  980  CB  LEU A 139     6887  10192   4248    813   1047   1028       C  
ATOM    981  CG  LEU A 139       6.917   8.658  28.407  1.00 53.99           C  
ANISOU  981  CG  LEU A 139     6592  10086   3837    954   1008    852       C  
ATOM    982  CD1 LEU A 139       7.695   8.526  29.705  1.00 59.00           C  
ANISOU  982  CD1 LEU A 139     7232  10893   4291   1087    984    850       C  
ATOM    983  CD2 LEU A 139       7.391   9.866  27.617  1.00 54.05           C  
ANISOU  983  CD2 LEU A 139     6633   9953   3949    933    907    633       C  
ATOM    984  N   TYR A 140       5.992   4.803  26.046  1.00 51.53           N  
ANISOU  984  N   TYR A 140     6296   9354   3930    535   1191   1436       N  
ATOM    985  CA  TYR A 140       6.317   3.536  25.400  1.00 53.32           C  
ANISOU  985  CA  TYR A 140     6555   9424   4280    423   1207   1586       C  
ATOM    986  C   TYR A 140       5.758   3.470  23.984  1.00 52.40           C  
ANISOU  986  C   TYR A 140     6444   9112   4355    285   1208   1580       C  
ATOM    987  O   TYR A 140       6.456   3.043  23.056  1.00 45.15           O  
ANISOU  987  O   TYR A 140     5578   8009   3569    201   1163   1574       O  
ATOM    988  CB  TYR A 140       5.788   2.378  26.247  1.00 53.57           C  
ANISOU  988  CB  TYR A 140     6549   9573   4233    435   1299   1814       C  
ATOM    989  CG  TYR A 140       5.682   1.055  25.520  1.00 59.74           C  
ANISOU  989  CG  TYR A 140     7347  10190   5160    305   1331   1988       C  
ATOM    990  CD1 TYR A 140       6.806   0.271  25.298  1.00 62.50           C  
ANISOU  990  CD1 TYR A 140     7761  10422   5566    278   1287   2031       C  
ATOM    991  CD2 TYR A 140       4.454   0.583  25.073  1.00 53.47           C  
ANISOU  991  CD2 TYR A 140     6503   9360   4451    213   1403   2106       C  
ATOM    992  CE1 TYR A 140       6.712  -0.943  24.643  1.00 54.59           C  
ANISOU  992  CE1 TYR A 140     6777   9265   4699    166   1310   2182       C  
ATOM    993  CE2 TYR A 140       4.351  -0.629  24.415  1.00 48.59           C  
ANISOU  993  CE2 TYR A 140     5902   8587   3975     95   1425   2259       C  
ATOM    994  CZ  TYR A 140       5.482  -1.387  24.205  1.00 48.22           C  
ANISOU  994  CZ  TYR A 140     5922   8419   3979     74   1377   2294       C  
ATOM    995  OH  TYR A 140       5.384  -2.594  23.553  1.00 58.55           O  
ANISOU  995  OH  TYR A 140     7250   9567   5429    -37   1393   2438       O  
ATOM    996  N   GLU A 141       4.507   3.894  23.794  1.00 46.39           N  
ANISOU  996  N   GLU A 141     5626   8394   3606    265   1257   1577       N  
ATOM    997  CA  GLU A 141       3.881   3.762  22.482  1.00 49.76           C  
ANISOU  997  CA  GLU A 141     6051   8648   4208    136   1262   1584       C  
ATOM    998  C   GLU A 141       4.466   4.738  21.468  1.00 46.41           C  
ANISOU  998  C   GLU A 141     5674   8078   3880    110   1174   1390       C  
ATOM    999  O   GLU A 141       4.538   4.417  20.276  1.00 50.50           O  
ANISOU  999  O   GLU A 141     6222   8412   4553      2   1153   1393       O  
ATOM   1000  CB  GLU A 141       2.368   3.958  22.596  1.00 55.13           C  
ANISOU 1000  CB  GLU A 141     6651   9425   4871    128   1339   1637       C  
ATOM   1001  CG  GLU A 141       1.652   2.902  23.433  1.00 47.48           C  
ANISOU 1001  CG  GLU A 141     5625   8581   3834    129   1436   1854       C  
ATOM   1002  CD  GLU A 141       1.658   1.524  22.792  1.00 55.31           C  
ANISOU 1002  CD  GLU A 141     6635   9416   4965      2   1458   2024       C  
ATOM   1003  OE1 GLU A 141       1.953   1.421  21.583  1.00 56.22           O  
ANISOU 1003  OE1 GLU A 141     6795   9329   5236    -94   1407   1970       O  
ATOM   1004  OE2 GLU A 141       1.364   0.539  23.501  1.00 59.60           O  
ANISOU 1004  OE2 GLU A 141     7147  10038   5462      0   1525   2212       O  
ATOM   1005  N   ILE A 142       4.892   5.920  21.912  1.00 43.86           N  
ANISOU 1005  N   ILE A 142     5358   7835   3471    207   1121   1222       N  
ATOM   1006  CA  ILE A 142       5.428   6.914  20.986  1.00 47.97           C  
ANISOU 1006  CA  ILE A 142     5919   8221   4085    182   1038   1043       C  
ATOM   1007  C   ILE A 142       6.869   6.587  20.614  1.00 47.92           C  
ANISOU 1007  C   ILE A 142     5980   8093   4135    157    970   1013       C  
ATOM   1008  O   ILE A 142       7.251   6.643  19.439  1.00 41.65           O  
ANISOU 1008  O   ILE A 142     5223   7123   3480     71    929    966       O  
ATOM   1009  CB  ILE A 142       5.306   8.326  21.591  1.00 49.92           C  
ANISOU 1009  CB  ILE A 142     6147   8590   4231    293   1002    871       C  
ATOM   1010  CG1 ILE A 142       3.844   8.777  21.606  1.00 55.34           C  
ANISOU 1010  CG1 ILE A 142     6770   9357   4900    302   1060    876       C  
ATOM   1011  CG2 ILE A 142       6.159   9.319  20.815  1.00 52.25           C  
ANISOU 1011  CG2 ILE A 142     6491   8750   4612    278    905    691       C  
ATOM   1012  CD1 ILE A 142       3.270   9.035  20.226  1.00 54.47           C  
ANISOU 1012  CD1 ILE A 142     6664   9081   4952    195   1052    842       C  
ATOM   1013  N   ALA A 143       7.689   6.236  21.608  1.00 42.59           N  
ANISOU 1013  N   ALA A 143     5318   7516   3348    234    958   1044       N  
ATOM   1014  CA  ALA A 143       9.100   5.970  21.348  1.00 47.29           C  
ANISOU 1014  CA  ALA A 143     5971   8013   3986    223    891   1009       C  
ATOM   1015  C   ALA A 143       9.298   4.741  20.468  1.00 50.06           C  
ANISOU 1015  C   ALA A 143     6352   8204   4465    112    910   1139       C  
ATOM   1016  O   ALA A 143      10.223   4.714  19.648  1.00 54.86           O  
ANISOU 1016  O   ALA A 143     7005   8668   5170     64    852   1083       O  
ATOM   1017  CB  ALA A 143       9.854   5.803  22.667  1.00 49.29           C  
ANISOU 1017  CB  ALA A 143     6226   8419   4083    337    877   1023       C  
ATOM   1018  N   ARG A 144       8.450   3.720  20.618  1.00 48.04           N  
ANISOU 1018  N   ARG A 144     6070   7969   4215     72    987   1313       N  
ATOM   1019  CA  ARG A 144       8.600   2.511  19.817  1.00 43.98           C  
ANISOU 1019  CA  ARG A 144     5585   7299   3826    -30   1000   1436       C  
ATOM   1020  C   ARG A 144       8.166   2.714  18.371  1.00 41.35           C  
ANISOU 1020  C   ARG A 144     5262   6795   3653   -138    986   1384       C  
ATOM   1021  O   ARG A 144       8.632   1.986  17.489  1.00 48.65           O  
ANISOU 1021  O   ARG A 144     6227   7564   4695   -214    965   1422       O  
ATOM   1022  CB  ARG A 144       7.812   1.358  20.444  1.00 51.14           C  
ANISOU 1022  CB  ARG A 144     6458   8276   4697    -44   1084   1641       C  
ATOM   1023  CG  ARG A 144       6.305   1.453  20.268  1.00 54.59           C  
ANISOU 1023  CG  ARG A 144     6834   8747   5160    -90   1152   1695       C  
ATOM   1024  CD  ARG A 144       5.584   0.517  21.226  1.00 62.10           C  
ANISOU 1024  CD  ARG A 144     7738   9822   6035    -75   1237   1892       C  
ATOM   1025  NE  ARG A 144       5.926  -0.880  20.978  1.00 63.04           N  
ANISOU 1025  NE  ARG A 144     7889   9826   6238   -144   1248   2048       N  
ATOM   1026  CZ  ARG A 144       5.048  -1.813  20.626  1.00 63.11           C  
ANISOU 1026  CZ  ARG A 144     7870   9769   6340   -237   1302   2200       C  
ATOM   1027  NH1 ARG A 144       3.768  -1.501  20.483  1.00 62.85           N  
ANISOU 1027  NH1 ARG A 144     7772   9783   6325   -272   1353   2218       N  
ATOM   1028  NH2 ARG A 144       5.451  -3.060  20.420  1.00 59.23           N  
ANISOU 1028  NH2 ARG A 144     7414   9164   5928   -293   1301   2331       N  
ATOM   1029  N   ARG A 145       7.286   3.679  18.109  1.00 41.51           N  
ANISOU 1029  N   ARG A 145     5247   6845   3680   -139    995   1297       N  
ATOM   1030  CA  ARG A 145       6.903   4.026  16.748  1.00 43.13           C  
ANISOU 1030  CA  ARG A 145     5462   6898   4026   -229    974   1232       C  
ATOM   1031  C   ARG A 145       7.753   5.147  16.168  1.00 44.52           C  
ANISOU 1031  C   ARG A 145     5673   7005   4236   -214    895   1052       C  
ATOM   1032  O   ARG A 145       7.730   5.356  14.950  1.00 47.90           O  
ANISOU 1032  O   ARG A 145     6122   7291   4786   -288    868   1000       O  
ATOM   1033  CB  ARG A 145       5.425   4.426  16.700  1.00 41.30           C  
ANISOU 1033  CB  ARG A 145     5170   6728   3795   -245   1027   1245       C  
ATOM   1034  CG  ARG A 145       4.467   3.279  16.960  1.00 41.24           C  
ANISOU 1034  CG  ARG A 145     5121   6752   3797   -293   1106   1431       C  
ATOM   1035  CD  ARG A 145       3.046   3.785  17.129  1.00 53.68           C  
ANISOU 1035  CD  ARG A 145     6624   8426   5346   -287   1161   1438       C  
ATOM   1036  NE  ARG A 145       2.079   2.696  17.229  1.00 48.88           N  
ANISOU 1036  NE  ARG A 145     5969   7831   4772   -351   1235   1618       N  
ATOM   1037  CZ  ARG A 145       1.829   2.019  18.344  1.00 50.47           C  
ANISOU 1037  CZ  ARG A 145     6134   8168   4875   -311   1296   1759       C  
ATOM   1038  NH1 ARG A 145       2.474   2.318  19.464  1.00 49.74           N  
ANISOU 1038  NH1 ARG A 145     6048   8215   4634   -200   1292   1736       N  
ATOM   1039  NH2 ARG A 145       0.932   1.043  18.341  1.00 51.55           N  
ANISOU 1039  NH2 ARG A 145     6224   8300   5062   -381   1361   1926       N  
ATOM   1040  N   HIS A 146       8.495   5.865  17.008  1.00 44.58           N  
ANISOU 1040  N   HIS A 146     5687   7112   4140   -119    855    958       N  
ATOM   1041  CA  HIS A 146       9.394   6.936  16.582  1.00 37.47           C  
ANISOU 1041  CA  HIS A 146     4816   6152   3270   -101    776    791       C  
ATOM   1042  C   HIS A 146      10.738   6.699  17.256  1.00 37.77           C  
ANISOU 1042  C   HIS A 146     4883   6226   3243    -43    732    777       C  
ATOM   1043  O   HIS A 146      11.071   7.349  18.256  1.00 39.75           O  
ANISOU 1043  O   HIS A 146     5121   6603   3379     53    705    703       O  
ATOM   1044  CB  HIS A 146       8.820   8.310  16.928  1.00 37.71           C  
ANISOU 1044  CB  HIS A 146     4816   6269   3244    -39    760    659       C  
ATOM   1045  CG  HIS A 146       7.480   8.573  16.315  1.00 52.08           C  
ANISOU 1045  CG  HIS A 146     6602   8065   5120    -87    802    670       C  
ATOM   1046  ND1 HIS A 146       7.330   9.185  15.089  1.00 53.36           N  
ANISOU 1046  ND1 HIS A 146     6780   8091   5403   -153    771    591       N  
ATOM   1047  CD2 HIS A 146       6.228   8.299  16.753  1.00 54.13           C  
ANISOU 1047  CD2 HIS A 146     6811   8424   5332    -78    874    756       C  
ATOM   1048  CE1 HIS A 146       6.044   9.281  14.801  1.00 46.38           C  
ANISOU 1048  CE1 HIS A 146     5858   7223   4543   -180    817    621       C  
ATOM   1049  NE2 HIS A 146       5.354   8.751  15.795  1.00 52.87           N  
ANISOU 1049  NE2 HIS A 146     6637   8186   5266   -137    881    721       N  
ATOM   1050  N   PRO A 147      11.544   5.774  16.724  1.00 39.77           N  
ANISOU 1050  N   PRO A 147     5173   6370   3567    -95    718    843       N  
ATOM   1051  CA  PRO A 147      12.773   5.366  17.426  1.00 37.73           C  
ANISOU 1051  CA  PRO A 147     4938   6155   3242    -37    684    854       C  
ATOM   1052  C   PRO A 147      13.841   6.444  17.494  1.00 38.51           C  
ANISOU 1052  C   PRO A 147     5049   6256   3328      9    601    690       C  
ATOM   1053  O   PRO A 147      14.844   6.245  18.190  1.00 45.20           O  
ANISOU 1053  O   PRO A 147     5906   7160   4107     69    566    683       O  
ATOM   1054  CB  PRO A 147      13.257   4.163  16.608  1.00 37.19           C  
ANISOU 1054  CB  PRO A 147     4907   5946   3278   -114    689    955       C  
ATOM   1055  CG  PRO A 147      12.716   4.411  15.232  1.00 36.13           C  
ANISOU 1055  CG  PRO A 147     4779   5670   3280   -209    689    921       C  
ATOM   1056  CD  PRO A 147      11.386   5.088  15.429  1.00 43.52           C  
ANISOU 1056  CD  PRO A 147     5672   6679   4185   -203    729    901       C  
ATOM   1057  N   TYR A 148      13.669   7.567  16.799  1.00 39.95           N  
ANISOU 1057  N   TYR A 148     5227   6377   3575    -17    566    562       N  
ATOM   1058  CA  TYR A 148      14.612   8.675  16.861  1.00 45.83           C  
ANISOU 1058  CA  TYR A 148     5977   7118   4318     21    486    405       C  
ATOM   1059  C   TYR A 148      14.016   9.907  17.527  1.00 37.12           C  
ANISOU 1059  C   TYR A 148     4844   6119   3140     92    469    289       C  
ATOM   1060  O   TYR A 148      14.585  10.997  17.408  1.00 38.11           O  
ANISOU 1060  O   TYR A 148     4972   6218   3290    110    399    146       O  
ATOM   1061  CB  TYR A 148      15.109   9.032  15.457  1.00 35.34           C  
ANISOU 1061  CB  TYR A 148     4673   5618   3138    -66    447    344       C  
ATOM   1062  CG  TYR A 148      15.940   7.951  14.807  1.00 34.83           C  
ANISOU 1062  CG  TYR A 148     4639   5453   3143   -120    447    427       C  
ATOM   1063  CD1 TYR A 148      15.344   6.955  14.045  1.00 34.42           C  
ANISOU 1063  CD1 TYR A 148     4601   5317   3161   -192    500    543       C  
ATOM   1064  CD2 TYR A 148      17.321   7.925  14.954  1.00 34.83           C  
ANISOU 1064  CD2 TYR A 148     4652   5443   3139    -95    390    385       C  
ATOM   1065  CE1 TYR A 148      16.097   5.965  13.446  1.00 34.37           C  
ANISOU 1065  CE1 TYR A 148     4625   5217   3219   -234    495    611       C  
ATOM   1066  CE2 TYR A 148      18.084   6.937  14.359  1.00 35.78           C  
ANISOU 1066  CE2 TYR A 148     4799   5476   3320   -136    389    457       C  
ATOM   1067  CZ  TYR A 148      17.465   5.960  13.605  1.00 35.13           C  
ANISOU 1067  CZ  TYR A 148     4734   5308   3305   -203    442    568       C  
ATOM   1068  OH  TYR A 148      18.215   4.972  13.009  1.00 47.47           O  
ANISOU 1068  OH  TYR A 148     6326   6782   4929   -237    437    633       O  
ATOM   1069  N   PHE A 149      12.885   9.762  18.216  1.00 37.88           N  
ANISOU 1069  N   PHE A 149     4910   6332   3149    133    530    349       N  
ATOM   1070  CA  PHE A 149      12.262  10.899  18.881  1.00 47.10           C  
ANISOU 1070  CA  PHE A 149     6049   7610   4238    211    516    238       C  
ATOM   1071  C   PHE A 149      13.238  11.559  19.849  1.00 39.22           C  
ANISOU 1071  C   PHE A 149     5052   6705   3146    310    443    121       C  
ATOM   1072  O   PHE A 149      13.987  10.884  20.561  1.00 39.77           O  
ANISOU 1072  O   PHE A 149     5129   6841   3140    353    437    174       O  
ATOM   1073  CB  PHE A 149      11.003  10.455  19.628  1.00 39.43           C  
ANISOU 1073  CB  PHE A 149     5039   6777   3167    252    601    341       C  
ATOM   1074  CG  PHE A 149       9.991  11.551  19.810  1.00 42.17           C  
ANISOU 1074  CG  PHE A 149     5352   7190   3479    298    605    244       C  
ATOM   1075  CD1 PHE A 149      10.163  12.518  20.788  1.00 43.82           C  
ANISOU 1075  CD1 PHE A 149     5548   7525   3578    412    559    115       C  
ATOM   1076  CD2 PHE A 149       8.871  11.617  19.000  1.00 39.28           C  
ANISOU 1076  CD2 PHE A 149     4968   6762   3193    231    651    277       C  
ATOM   1077  CE1 PHE A 149       9.237  13.529  20.954  1.00 41.01           C  
ANISOU 1077  CE1 PHE A 149     5163   7228   3192    461    559     20       C  
ATOM   1078  CE2 PHE A 149       7.941  12.626  19.160  1.00 46.22           C  
ANISOU 1078  CE2 PHE A 149     5816   7703   4042    279    654    187       C  
ATOM   1079  CZ  PHE A 149       8.124  13.583  20.139  1.00 43.37           C  
ANISOU 1079  CZ  PHE A 149     5443   7464   3570    395    609     58       C  
ATOM   1080  N   TYR A 150      13.237  12.891  19.851  1.00 42.84           N  
ANISOU 1080  N   TYR A 150     5503   7159   3614    344    382    -42       N  
ATOM   1081  CA  TYR A 150      14.067  13.666  20.763  1.00 49.18           C  
ANISOU 1081  CA  TYR A 150     6304   8047   4335    440    302   -175       C  
ATOM   1082  C   TYR A 150      13.641  13.390  22.199  1.00 41.42           C  
ANISOU 1082  C   TYR A 150     5294   7274   3168    559    337   -139       C  
ATOM   1083  O   TYR A 150      12.666  13.974  22.683  1.00 42.07           O  
ANISOU 1083  O   TYR A 150     5349   7455   3179    621    359   -182       O  
ATOM   1084  CB  TYR A 150      13.963  15.158  20.435  1.00 44.69           C  
ANISOU 1084  CB  TYR A 150     5732   7423   3825    450    233   -352       C  
ATOM   1085  CG  TYR A 150      15.096  15.997  20.980  1.00 41.86           C  
ANISOU 1085  CG  TYR A 150     5378   7082   3444    511    128   -504       C  
ATOM   1086  CD1 TYR A 150      16.317  15.424  21.310  1.00 40.48           C  
ANISOU 1086  CD1 TYR A 150     5215   6920   3248    519     92   -481       C  
ATOM   1087  CD2 TYR A 150      14.947  17.367  21.154  1.00 42.41           C  
ANISOU 1087  CD2 TYR A 150     5439   7152   3521    559     59   -673       C  
ATOM   1088  CE1 TYR A 150      17.355  16.191  21.804  1.00 45.41           C  
ANISOU 1088  CE1 TYR A 150     5837   7561   3857    572     -9   -623       C  
ATOM   1089  CE2 TYR A 150      15.980  18.142  21.647  1.00 43.08           C  
ANISOU 1089  CE2 TYR A 150     5525   7246   3596    610    -45   -817       C  
ATOM   1090  CZ  TYR A 150      17.181  17.549  21.969  1.00 45.83           C  
ANISOU 1090  CZ  TYR A 150     5880   7610   3923    614    -79   -791       C  
ATOM   1091  OH  TYR A 150      18.213  18.317  22.459  1.00 48.82           O  
ANISOU 1091  OH  TYR A 150     6254   7998   4296    662   -186   -936       O  
ATOM   1092  N   ALA A 151      14.367  12.501  22.880  1.00 41.93           N  
ANISOU 1092  N   ALA A 151     5367   7412   3155    595    341    -57       N  
ATOM   1093  CA  ALA A 151      13.936  12.021  24.193  1.00 52.51           C  
ANISOU 1093  CA  ALA A 151     6682   8954   4317    702    389     16       C  
ATOM   1094  C   ALA A 151      13.783  13.129  25.229  1.00 51.84           C  
ANISOU 1094  C   ALA A 151     6574   9019   4104    832    340   -137       C  
ATOM   1095  O   ALA A 151      12.776  13.118  25.958  1.00 60.54           O  
ANISOU 1095  O   ALA A 151     7643  10270   5088    904    400    -98       O  
ATOM   1096  CB  ALA A 151      14.897  10.932  24.681  1.00 45.30           C  
ANISOU 1096  CB  ALA A 151     5785   8077   3350    719    390    121       C  
ATOM   1097  N   PRO A 152      14.711  14.084  25.374  1.00 49.57           N  
ANISOU 1097  N   PRO A 152     6297   8708   3831    871    233   -310       N  
ATOM   1098  CA  PRO A 152      14.453  15.187  26.314  1.00 59.86           C  
ANISOU 1098  CA  PRO A 152     7579  10145   5019    996    182   -467       C  
ATOM   1099  C   PRO A 152      13.212  15.987  25.966  1.00 58.35           C  
ANISOU 1099  C   PRO A 152     7370   9943   4859    994    210   -524       C  
ATOM   1100  O   PRO A 152      12.532  16.489  26.870  1.00 53.79           O  
ANISOU 1100  O   PRO A 152     6764   9523   4149   1108    218   -584       O  
ATOM   1101  CB  PRO A 152      15.724  16.041  26.212  1.00 58.28           C  
ANISOU 1101  CB  PRO A 152     7397   9865   4884   1001     55   -638       C  
ATOM   1102  CG  PRO A 152      16.767  15.113  25.711  1.00 50.90           C  
ANISOU 1102  CG  PRO A 152     6484   8832   4022    920     51   -541       C  
ATOM   1103  CD  PRO A 152      16.059  14.185  24.783  1.00 49.21           C  
ANISOU 1103  CD  PRO A 152     6278   8524   3894    811    152   -370       C  
ATOM   1104  N   GLU A 153      12.890  16.117  24.678  1.00 53.57           N  
ANISOU 1104  N   GLU A 153     6777   9160   4418    873    226   -507       N  
ATOM   1105  CA  GLU A 153      11.653  16.779  24.287  1.00 54.05           C  
ANISOU 1105  CA  GLU A 153     6818   9207   4510    867    259   -543       C  
ATOM   1106  C   GLU A 153      10.441  15.884  24.506  1.00 52.48           C  
ANISOU 1106  C   GLU A 153     6589   9111   4241    867    381   -375       C  
ATOM   1107  O   GLU A 153       9.342  16.387  24.765  1.00 51.52           O  
ANISOU 1107  O   GLU A 153     6435   9074   4066    919    416   -405       O  
ATOM   1108  CB  GLU A 153      11.732  17.221  22.824  1.00 50.97           C  
ANISOU 1108  CB  GLU A 153     6452   8596   4317    740    232   -579       C  
ATOM   1109  CG  GLU A 153      10.622  18.169  22.394  1.00 59.63           C  
ANISOU 1109  CG  GLU A 153     7535   9664   5460    743    239   -656       C  
ATOM   1110  CD  GLU A 153      10.657  19.496  23.132  1.00 70.06           C  
ANISOU 1110  CD  GLU A 153     8847  11054   6717    858    156   -852       C  
ATOM   1111  OE1 GLU A 153      11.742  19.891  23.610  1.00 70.25           O  
ANISOU 1111  OE1 GLU A 153     8887  11085   6722    902     67   -956       O  
ATOM   1112  OE2 GLU A 153       9.595  20.146  23.232  1.00 73.37           O  
ANISOU 1112  OE2 GLU A 153     9244  11523   7110    907    174   -905       O  
ATOM   1113  N   LEU A 154      10.617  14.563  24.411  1.00 44.21           N  
ANISOU 1113  N   LEU A 154     5547   8057   3195    809    444   -197       N  
ATOM   1114  CA  LEU A 154       9.513  13.653  24.694  1.00 44.69           C  
ANISOU 1114  CA  LEU A 154     5573   8217   3190    807    558    -26       C  
ATOM   1115  C   LEU A 154       9.085  13.735  26.154  1.00 51.82           C  
ANISOU 1115  C   LEU A 154     6438   9362   3888    954    587    -26       C  
ATOM   1116  O   LEU A 154       7.900  13.557  26.461  1.00 46.98           O  
ANISOU 1116  O   LEU A 154     5781   8859   3210    980    670     52       O  
ATOM   1117  CB  LEU A 154       9.904  12.221  24.331  1.00 44.19           C  
ANISOU 1117  CB  LEU A 154     5529   8086   3177    718    608    159       C  
ATOM   1118  CG  LEU A 154       8.801  11.166  24.442  1.00 45.82           C  
ANISOU 1118  CG  LEU A 154     5700   8357   3352    686    724    355       C  
ATOM   1119  CD1 LEU A 154       7.548  11.612  23.703  1.00 45.68           C  
ANISOU 1119  CD1 LEU A 154     5653   8290   3412    633    766    345       C  
ATOM   1120  CD2 LEU A 154       9.288   9.826  23.917  1.00 50.70           C  
ANISOU 1120  CD2 LEU A 154     6346   8867   4052    588    755    518       C  
ATOM   1121  N   LEU A 155      10.028  14.001  27.062  1.00 47.13           N  
ANISOU 1121  N   LEU A 155     5857   8862   3190   1053    519   -113       N  
ATOM   1122  CA  LEU A 155       9.662  14.265  28.449  1.00 58.66           C  
ANISOU 1122  CA  LEU A 155     7283  10559   4447   1209    532   -145       C  
ATOM   1123  C   LEU A 155       8.779  15.498  28.559  1.00 60.90           C  
ANISOU 1123  C   LEU A 155     7539  10895   4704   1277    515   -295       C  
ATOM   1124  O   LEU A 155       7.911  15.567  29.437  1.00 50.47           O  
ANISOU 1124  O   LEU A 155     6174   9766   3234   1382    570   -274       O  
ATOM   1125  CB  LEU A 155      10.921  14.443  29.299  1.00 51.68           C  
ANISOU 1125  CB  LEU A 155     6420   9747   3470   1301    444   -239       C  
ATOM   1126  CG  LEU A 155      11.948  13.312  29.339  1.00 55.07           C  
ANISOU 1126  CG  LEU A 155     6877  10141   3907   1258    445   -114       C  
ATOM   1127  CD1 LEU A 155      12.971  13.576  30.431  1.00 61.39           C  
ANISOU 1127  CD1 LEU A 155     7685  11069   4573   1383    363   -212       C  
ATOM   1128  CD2 LEU A 155      11.277  11.968  29.548  1.00 53.73           C  
ANISOU 1128  CD2 LEU A 155     6687  10043   3686   1230    567    126       C  
ATOM   1129  N   PHE A 156       8.987  16.480  27.678  1.00 48.27           N  
ANISOU 1129  N   PHE A 156     5964   9130   3247   1224    438   -443       N  
ATOM   1130  CA  PHE A 156       8.185  17.697  27.724  1.00 48.68           C  
ANISOU 1130  CA  PHE A 156     5995   9212   3288   1289    412   -593       C  
ATOM   1131  C   PHE A 156       6.758  17.437  27.257  1.00 59.56           C  
ANISOU 1131  C   PHE A 156     7335  10602   4693   1243    516   -485       C  
ATOM   1132  O   PHE A 156       5.799  17.913  27.877  1.00 58.63           O  
ANISOU 1132  O   PHE A 156     7174  10634   4467   1343    549   -525       O  
ATOM   1133  CB  PHE A 156       8.842  18.785  26.876  1.00 59.94           C  
ANISOU 1133  CB  PHE A 156     7460  10445   4870   1236    300   -768       C  
ATOM   1134  CG  PHE A 156       8.087  20.076  26.861  1.00 68.20           C  
ANISOU 1134  CG  PHE A 156     8492  11499   5921   1301    262   -929       C  
ATOM   1135  CD1 PHE A 156       8.075  20.896  27.972  1.00 68.03           C  
ANISOU 1135  CD1 PHE A 156     8457  11632   5760   1457    205  -1081       C  
ATOM   1136  CD2 PHE A 156       7.384  20.468  25.734  1.00 76.37           C  
ANISOU 1136  CD2 PHE A 156     9529  12388   7101   1210    279   -932       C  
ATOM   1137  CE1 PHE A 156       7.379  22.081  27.962  1.00 73.09           C  
ANISOU 1137  CE1 PHE A 156     9087  12276   6409   1523    166  -1234       C  
ATOM   1138  CE2 PHE A 156       6.685  21.657  25.720  1.00 81.92           C  
ANISOU 1138  CE2 PHE A 156    10219  13094   7811   1274    241  -1079       C  
ATOM   1139  CZ  PHE A 156       6.685  22.466  26.836  1.00 75.85           C  
ANISOU 1139  CZ  PHE A 156     9438  12474   6906   1431    184  -1231       C  
ATOM   1140  N   PHE A 157       6.599  16.686  26.163  1.00 59.09           N  
ANISOU 1140  N   PHE A 157     7286  10390   4776   1097    566   -352       N  
ATOM   1141  CA  PHE A 157       5.265  16.278  25.735  1.00 57.41           C  
ANISOU 1141  CA  PHE A 157     7031  10191   4590   1046    667   -231       C  
ATOM   1142  C   PHE A 157       4.581  15.427  26.794  1.00 55.93           C  
ANISOU 1142  C   PHE A 157     6792  10222   4238   1117    768    -80       C  
ATOM   1143  O   PHE A 157       3.355  15.488  26.944  1.00 48.98           O  
ANISOU 1143  O   PHE A 157     5858   9441   3313   1144    841    -35       O  
ATOM   1144  CB  PHE A 157       5.345  15.512  24.414  1.00 54.42           C  
ANISOU 1144  CB  PHE A 157     6677   9611   4390    877    695   -113       C  
ATOM   1145  CG  PHE A 157       5.599  16.384  23.219  1.00 51.78           C  
ANISOU 1145  CG  PHE A 157     6379   9074   4223    801    621   -238       C  
ATOM   1146  CD1 PHE A 157       4.587  17.166  22.688  1.00 56.99           C  
ANISOU 1146  CD1 PHE A 157     7016   9702   4937    795    630   -302       C  
ATOM   1147  CD2 PHE A 157       6.848  16.416  22.619  1.00 49.51           C  
ANISOU 1147  CD2 PHE A 157     6144   8631   4038    735    547   -285       C  
ATOM   1148  CE1 PHE A 157       4.815  17.967  21.585  1.00 55.45           C  
ANISOU 1148  CE1 PHE A 157     6855   9321   4894    726    564   -407       C  
ATOM   1149  CE2 PHE A 157       7.084  17.216  21.516  1.00 43.79           C  
ANISOU 1149  CE2 PHE A 157     5448   7724   3464    664    484   -388       C  
ATOM   1150  CZ  PHE A 157       6.065  17.993  20.999  1.00 43.67           C  
ANISOU 1150  CZ  PHE A 157     5415   7677   3502    660    492   -447       C  
ATOM   1151  N   ALA A 158       5.354  14.628  27.533  1.00 48.95           N  
ANISOU 1151  N   ALA A 158     5920   9417   3262   1150    774      3       N  
ATOM   1152  CA  ALA A 158       4.787  13.824  28.610  1.00 58.53           C  
ANISOU 1152  CA  ALA A 158     7084  10845   4308   1225    869    154       C  
ATOM   1153  C   ALA A 158       4.194  14.709  29.699  1.00 56.17           C  
ANISOU 1153  C   ALA A 158     6743  10766   3835   1392    867     41       C  
ATOM   1154  O   ALA A 158       3.066  14.485  30.153  1.00 52.80           O  
ANISOU 1154  O   ALA A 158     6254  10491   3317   1436    961    133       O  
ATOM   1155  CB  ALA A 158       5.856  12.897  29.187  1.00 58.91           C  
ANISOU 1155  CB  ALA A 158     7162  10928   4293   1237    860    248       C  
ATOM   1156  N   LYS A 159       4.944  15.727  30.130  1.00 58.89           N  
ANISOU 1156  N   LYS A 159     7116  11128   4130   1489    760   -163       N  
ATOM   1157  CA  LYS A 159       4.420  16.661  31.122  1.00 53.64           C  
ANISOU 1157  CA  LYS A 159     6416  10660   3304   1656    744   -298       C  
ATOM   1158  C   LYS A 159       3.216  17.420  30.578  1.00 60.62           C  
ANISOU 1158  C   LYS A 159     7266  11521   4247   1648    770   -360       C  
ATOM   1159  O   LYS A 159       2.223  17.615  31.289  1.00 63.49           O  
ANISOU 1159  O   LYS A 159     7570  12076   4476   1753    832   -350       O  
ATOM   1160  CB  LYS A 159       5.515  17.634  31.561  1.00 56.15           C  
ANISOU 1160  CB  LYS A 159     6777  10969   3588   1747    608   -518       C  
ATOM   1161  CG  LYS A 159       5.113  18.535  32.719  1.00 67.99           C  
ANISOU 1161  CG  LYS A 159     8246  12686   4903   1937    580   -666       C  
ATOM   1162  CD  LYS A 159       6.282  19.380  33.200  1.00 78.15           C  
ANISOU 1162  CD  LYS A 159     9576  13962   6158   2023    438   -876       C  
ATOM   1163  CE  LYS A 159       6.546  20.548  32.263  1.00 75.10           C  
ANISOU 1163  CE  LYS A 159     9225  13359   5949   1965    332  -1066       C  
ATOM   1164  NZ  LYS A 159       7.548  21.497  32.824  1.00 71.53           N  
ANISOU 1164  NZ  LYS A 159     8805  12911   5462   2061    189  -1287       N  
ATOM   1165  N   ARG A 160       3.284  17.855  29.317  1.00 56.22           N  
ANISOU 1165  N   ARG A 160     6742  10734   3887   1529    724   -421       N  
ATOM   1166  CA  ARG A 160       2.141  18.522  28.703  1.00 53.95           C  
ANISOU 1166  CA  ARG A 160     6423  10409   3669   1513    749   -468       C  
ATOM   1167  C   ARG A 160       0.968  17.566  28.524  1.00 54.78           C  
ANISOU 1167  C   ARG A 160     6466  10579   3768   1452    884   -260       C  
ATOM   1168  O   ARG A 160      -0.191  17.996  28.553  1.00 64.73           O  
ANISOU 1168  O   ARG A 160     7673  11922   5000   1495    931   -275       O  
ATOM   1169  CB  ARG A 160       2.543  19.128  27.359  1.00 53.05           C  
ANISOU 1169  CB  ARG A 160     6359  10030   3766   1394    671   -564       C  
ATOM   1170  CG  ARG A 160       3.262  20.460  27.467  1.00 70.71           C  
ANISOU 1170  CG  ARG A 160     8637  12207   6022   1467    538   -803       C  
ATOM   1171  CD  ARG A 160       3.104  21.275  26.193  1.00 89.09           C  
ANISOU 1171  CD  ARG A 160    10992  14317   8541   1375    486   -895       C  
ATOM   1172  NE  ARG A 160       3.596  22.640  26.351  1.00105.89           N  
ANISOU 1172  NE  ARG A 160    13152  16397  10687   1454    362  -1125       N  
ATOM   1173  CZ  ARG A 160       3.371  23.622  25.485  1.00111.91           C  
ANISOU 1173  CZ  ARG A 160    13932  17002  11585   1417    305  -1239       C  
ATOM   1174  NH1 ARG A 160       2.656  23.395  24.391  1.00110.62           N  
ANISOU 1174  NH1 ARG A 160    13761  16724  11546   1306    360  -1148       N  
ATOM   1175  NH2 ARG A 160       3.861  24.834  25.712  1.00113.04           N  
ANISOU 1175  NH2 ARG A 160    14104  17102  11744   1491    189  -1445       N  
ATOM   1176  N   TYR A 161       1.248  16.276  28.332  1.00 54.04           N  
ANISOU 1176  N   TYR A 161     6378  10446   3709   1352    944    -65       N  
ATOM   1177  CA  TYR A 161       0.181  15.282  28.287  1.00 51.73           C  
ANISOU 1177  CA  TYR A 161     6022  10225   3406   1296   1070    145       C  
ATOM   1178  C   TYR A 161      -0.515  15.176  29.637  1.00 71.77           C  
ANISOU 1178  C   TYR A 161     8492  13049   5728   1441   1146    199       C  
ATOM   1179  O   TYR A 161      -1.747  15.238  29.719  1.00 70.13           O  
ANISOU 1179  O   TYR A 161     8214  12947   5486   1462   1224    251       O  
ATOM   1180  CB  TYR A 161       0.745  13.926  27.865  1.00 76.03           C  
ANISOU 1180  CB  TYR A 161     9128  13195   6566   1166   1106    333       C  
ATOM   1181  CG  TYR A 161      -0.219  13.068  27.080  1.00 82.94           C  
ANISOU 1181  CG  TYR A 161     9963  14000   7552   1036   1198    510       C  
ATOM   1182  CD1 TYR A 161      -0.660  13.458  25.823  1.00 86.83           C  
ANISOU 1182  CD1 TYR A 161    10464  14315   8214    933   1178    460       C  
ATOM   1183  CD2 TYR A 161      -0.681  11.862  27.593  1.00 89.00           C  
ANISOU 1183  CD2 TYR A 161    10684  14878   8257   1014   1301    728       C  
ATOM   1184  CE1 TYR A 161      -1.539  12.675  25.100  1.00 91.80           C  
ANISOU 1184  CE1 TYR A 161    11055  14880   8946    814   1254    613       C  
ATOM   1185  CE2 TYR A 161      -1.560  11.072  26.877  1.00 93.00           C  
ANISOU 1185  CE2 TYR A 161    11150  15313   8873    890   1378    887       C  
ATOM   1186  CZ  TYR A 161      -1.985  11.483  25.631  1.00 97.83           C  
ANISOU 1186  CZ  TYR A 161    11770  15750   9652    791   1352    824       C  
ATOM   1187  OH  TYR A 161      -2.860  10.701  24.913  1.00102.64           O  
ANISOU 1187  OH  TYR A 161    12338  16289  10372    669   1422    974       O  
ATOM   1188  N   LYS A 162       0.264  15.014  30.709  1.00 54.61           N  
ANISOU 1188  N   LYS A 162     6334  11010   3404   1546   1123    188       N  
ATOM   1189  CA  LYS A 162      -0.317  15.002  32.047  1.00 56.54           C  
ANISOU 1189  CA  LYS A 162     6516  11527   3437   1698   1182    223       C  
ATOM   1190  C   LYS A 162      -1.027  16.319  32.339  1.00 61.23           C  
ANISOU 1190  C   LYS A 162     7079  12198   3987   1816   1142     34       C  
ATOM   1191  O   LYS A 162      -2.187  16.328  32.765  1.00 67.15           O  
ANISOU 1191  O   LYS A 162     7754  13055   4704   1856   1205     94       O  
ATOM   1192  CB  LYS A 162       0.770  14.725  33.088  1.00 65.52           C  
ANISOU 1192  CB  LYS A 162     7687  12734   4475   1780   1127    215       C  
ATOM   1193  CG  LYS A 162       0.293  14.821  34.528  1.00 66.50           C  
ANISOU 1193  CG  LYS A 162     7752  13051   4465   1922   1138    225       C  
ATOM   1194  CD  LYS A 162       1.437  14.588  35.506  1.00 79.28           C  
ANISOU 1194  CD  LYS A 162     9404  14732   5987   2005   1076    205       C  
ATOM   1195  CE  LYS A 162       1.788  13.110  35.623  1.00 80.74           C  
ANISOU 1195  CE  LYS A 162     9593  14898   6187   1921   1142    442       C  
ATOM   1196  NZ  LYS A 162       2.527  12.815  36.884  1.00 74.09           N  
ANISOU 1196  NZ  LYS A 162     8754  14175   5224   2030   1106    455       N  
ATOM   1197  N   ALA A 163      -0.350  17.443  32.079  1.00 68.66           N  
ANISOU 1197  N   ALA A 163     8077  13069   4944   1866   1031   -197       N  
ATOM   1198  CA  ALA A 163      -0.906  18.762  32.375  1.00 68.76           C  
ANISOU 1198  CA  ALA A 163     8069  13141   4917   1988    976   -397       C  
ATOM   1199  C   ALA A 163      -2.303  18.935  31.788  1.00 71.36           C  
ANISOU 1199  C   ALA A 163     8336  13475   5300   1952   1053   -353       C  
ATOM   1200  O   ALA A 163      -3.208  19.454  32.453  1.00 75.69           O  
ANISOU 1200  O   ALA A 163     8826  14146   5786   2055   1065   -394       O  
ATOM   1201  CB  ALA A 163       0.028  19.852  31.847  1.00 78.41           C  
ANISOU 1201  CB  ALA A 163     9367  14193   6232   1989    834   -629       C  
ATOM   1202  N   ALA A 164      -2.493  18.510  30.535  1.00 68.44           N  
ANISOU 1202  N   ALA A 164     7979  12912   5112   1784   1080   -263       N  
ATOM   1203  CA  ALA A 164      -3.798  18.647  29.895  1.00 70.61           C  
ANISOU 1203  CA  ALA A 164     8195  13174   5458   1737   1146   -220       C  
ATOM   1204  C   ALA A 164      -4.841  17.781  30.583  1.00 65.83           C  
ANISOU 1204  C   ALA A 164     7496  12780   4737   1764   1282    -22       C  
ATOM   1205  O   ALA A 164      -5.975  18.219  30.808  1.00 60.26           O  
ANISOU 1205  O   ALA A 164     6722  12163   4010   1821   1315    -38       O  
ATOM   1206  CB  ALA A 164      -3.697  18.294  28.412  1.00 64.32           C  
ANISOU 1206  CB  ALA A 164     7436  12110   4895   1544   1134   -159       C  
ATOM   1207  N   PHE A 165      -4.475  16.550  30.931  1.00 59.94           N  
ANISOU 1207  N   PHE A 165     6747  12048   3978   1701   1333    172       N  
ATOM   1208  CA  PHE A 165      -5.386  15.690  31.673  1.00 78.28           C  
ANISOU 1208  CA  PHE A 165     8988  14495   6260   1702   1426    367       C  
ATOM   1209  C   PHE A 165      -5.632  16.191  33.091  1.00 82.01           C  
ANISOU 1209  C   PHE A 165     9421  15157   6583   1874   1403    300       C  
ATOM   1210  O   PHE A 165      -6.627  15.795  33.708  1.00 77.29           O  
ANISOU 1210  O   PHE A 165     8742  14685   5942   1901   1475    422       O  
ATOM   1211  CB  PHE A 165      -4.838  14.261  31.701  1.00 80.84           C  
ANISOU 1211  CB  PHE A 165     9328  14769   6617   1594   1474    581       C  
ATOM   1212  CG  PHE A 165      -5.090  13.492  30.434  1.00 74.11           C  
ANISOU 1212  CG  PHE A 165     8478  13761   5920   1415   1530    717       C  
ATOM   1213  CD1 PHE A 165      -6.324  12.918  30.184  1.00 76.56           C  
ANISOU 1213  CD1 PHE A 165     8708  14084   6296   1339   1618    869       C  
ATOM   1214  CD2 PHE A 165      -4.091  13.353  29.488  1.00 73.48           C  
ANISOU 1214  CD2 PHE A 165     8478  13504   5937   1318   1482    685       C  
ATOM   1215  CE1 PHE A 165      -6.555  12.215  29.013  1.00 73.74           C  
ANISOU 1215  CE1 PHE A 165     8351  13575   6091   1173   1661    988       C  
ATOM   1216  CE2 PHE A 165      -4.314  12.653  28.319  1.00 70.43           C  
ANISOU 1216  CE2 PHE A 165     8100  12920   5741   1143   1504    797       C  
ATOM   1217  CZ  PHE A 165      -5.545  12.084  28.081  1.00 67.37           C  
ANISOU 1217  CZ  PHE A 165     7629  12579   5390   1078   1604    951       C  
ATOM   1218  N   THR A 166      -4.759  17.044  33.621  1.00 89.74           N  
ANISOU 1218  N   THR A 166    10453  16159   7485   1991   1301    109       N  
ATOM   1219  CA  THR A 166      -4.961  17.640  34.947  1.00 92.83           C  
ANISOU 1219  CA  THR A 166    10808  16726   7737   2164   1265     21       C  
ATOM   1220  C   THR A 166      -5.739  18.949  34.856  1.00 96.89           C  
ANISOU 1220  C   THR A 166    11297  17274   8245   2259   1225   -165       C  
ATOM   1221  O   THR A 166      -5.393  19.948  35.480  1.00102.14           O  
ANISOU 1221  O   THR A 166    11982  17989   8840   2394   1132   -356       O  
ATOM   1222  CB  THR A 166      -3.627  17.870  35.646  1.00 95.84           C  
ANISOU 1222  CB  THR A 166    11254  17119   8043   2247   1168    -89       C  
ATOM   1223  OG1 THR A 166      -2.841  18.780  34.877  1.00113.19           O  
ANISOU 1223  OG1 THR A 166    13528  19171  10307   2235   1068   -292       O  
ATOM   1224  CG2 THR A 166      -2.855  16.565  35.800  1.00 89.54           C  
ANISOU 1224  CG2 THR A 166    10480  16295   7245   2165   1206     96       C  
ATOM   1225  N   GLU A 167      -6.824  18.955  34.091  1.00 96.10           N  
ANISOU 1225  N   GLU A 167    11148  17144   8223   2190   1291   -110       N  
ATOM   1226  CA  GLU A 167      -7.570  20.188  33.878  1.00 96.40           C  
ANISOU 1226  CA  GLU A 167    11164  17195   8269   2271   1252   -285       C  
ATOM   1227  C   GLU A 167      -8.946  19.916  33.292  1.00 98.57           C  
ANISOU 1227  C   GLU A 167    11359  17487   8607   2202   1349   -167       C  
ATOM   1228  O   GLU A 167      -9.932  20.535  33.702  1.00107.10           O  
ANISOU 1228  O   GLU A 167    12376  18679   9640   2299   1358   -220       O  
ATOM   1229  CB  GLU A 167      -6.789  21.121  32.952  1.00 90.92           C  
ANISOU 1229  CB  GLU A 167    10558  16329   7661   2252   1151   -491       C  
ATOM   1230  CG  GLU A 167      -7.576  22.343  32.494  1.00 90.41           C  
ANISOU 1230  CG  GLU A 167    10476  16237   7636   2312   1113   -661       C  
ATOM   1231  CD  GLU A 167      -6.754  23.610  32.506  1.00 91.99           C  
ANISOU 1231  CD  GLU A 167    10753  16354   7846   2401    971   -923       C  
ATOM   1232  OE1 GLU A 167      -7.359  24.702  32.548  1.00 87.22           O  
ANISOU 1232  OE1 GLU A 167    10133  15762   7244   2496    922  -1078       O  
ATOM   1233  OE2 GLU A 167      -5.510  23.512  32.463  1.00 93.75           O  
ANISOU 1233  OE2 GLU A 167    11049  16492   8080   2373    906   -973       O  
ATOM   1234  N   CYS A 168      -9.028  18.981  32.349  1.00 96.13           N  
ANISOU 1234  N   CYS A 168    11049  17069   8407   2036   1420     -6       N  
ATOM   1235  CA  CYS A 168     -10.231  18.785  31.561  1.00 99.89           C  
ANISOU 1235  CA  CYS A 168    11457  17523   8973   1951   1498     86       C  
ATOM   1236  C   CYS A 168     -10.888  17.428  31.760  1.00 99.04           C  
ANISOU 1236  C   CYS A 168    11278  17469   8885   1853   1609    351       C  
ATOM   1237  O   CYS A 168     -11.868  17.134  31.067  1.00110.61           O  
ANISOU 1237  O   CYS A 168    12683  18905  10438   1764   1674    445       O  
ATOM   1238  CB  CYS A 168      -9.907  18.976  30.074  1.00 91.55           C  
ANISOU 1238  CB  CYS A 168    10456  16272   8059   1829   1478     30       C  
ATOM   1239  SG  CYS A 168      -8.709  20.291  29.759  1.00 92.85           S  
ANISOU 1239  SG  CYS A 168    10730  16325   8224   1906   1337   -256       S  
ATOM   1240  N   CYS A 169     -10.282  16.585  32.595  1.00 85.09           N  
ANISOU 1240  N   CYS A 169     9513  15773   7044   1867   1628    473       N  
ATOM   1241  CA  CYS A 169     -10.822  15.219  32.812  1.00 84.90           C  
ANISOU 1241  CA  CYS A 169     9435  15763   7060   1758   1723    729       C  
ATOM   1242  C   CYS A 169     -11.724  15.263  34.043  1.00 93.67           C  
ANISOU 1242  C   CYS A 169    10449  17071   8069   1844   1782    830       C  
ATOM   1243  O   CYS A 169     -12.011  14.191  34.611  1.00 97.87           O  
ANISOU 1243  O   CYS A 169    10931  17621   8633   1760   1860   1044       O  
ATOM   1244  CB  CYS A 169      -9.687  14.214  32.945  1.00 90.77           C  
ANISOU 1244  CB  CYS A 169    10246  16429   7813   1690   1713    828       C  
ATOM   1245  SG  CYS A 169      -9.452  13.261  31.425  1.00 95.73           S  
ANISOU 1245  SG  CYS A 169    10928  16817   8629   1479   1729    918       S  
ATOM   1246  N   GLN A 170     -12.114  16.413  34.562  1.00 85.84           N  
ANISOU 1246  N   GLN A 170     9431  16227   6959   2011   1744    683       N  
ATOM   1247  CA  GLN A 170     -13.045  16.352  35.721  1.00 93.53           C  
ANISOU 1247  CA  GLN A 170    10298  17385   7854   2088   1806    765       C  
ATOM   1248  C   GLN A 170     -13.961  17.562  35.662  1.00100.82           C  
ANISOU 1248  C   GLN A 170    11188  18373   8746   2199   1770    582       C  
ATOM   1249  O   GLN A 170     -14.660  17.832  36.650  1.00 97.84           O  
ANISOU 1249  O   GLN A 170    10747  18176   8252   2336   1777    555       O  
ATOM   1250  CB  GLN A 170     -12.319  16.294  37.065  1.00 89.33           C  
ANISOU 1250  CB  GLN A 170     9748  17021   7171   2204   1808    822       C  
ATOM   1251  CG  GLN A 170     -10.878  16.778  37.034  1.00 88.31           C  
ANISOU 1251  CG  GLN A 170     9710  16876   6968   2290   1715    683       C  
ATOM   1252  CD  GLN A 170     -10.052  16.006  38.031  1.00 91.67           C  
ANISOU 1252  CD  GLN A 170    10119  17437   7275   2357   1734    801       C  
ATOM   1253  OE1 GLN A 170      -8.855  16.234  38.186  1.00 93.12           O  
ANISOU 1253  OE1 GLN A 170    10260  17802   7321   2514   1720    746       O  
ATOM   1254  NE2 GLN A 170     -10.695  15.076  38.718  1.00 89.70           N  
ANISOU 1254  NE2 GLN A 170     9903  17100   7080   2242   1766    963       N  
ATOM   1255  N   ALA A 172     -17.023  19.969  33.578  1.00120.37           N  
ANISOU 1255  N   ALA A 172    13557  20820  11357   2292   1736    214       N  
ATOM   1256  CA  ALA A 172     -18.367  19.654  33.048  1.00121.88           C  
ANISOU 1256  CA  ALA A 172    13650  21058  11602   2252   1806    294       C  
ATOM   1257  C   ALA A 172     -18.253  18.854  31.755  1.00120.41           C  
ANISOU 1257  C   ALA A 172    13464  20708  11580   2050   1860    432       C  
ATOM   1258  O   ALA A 172     -18.455  17.623  31.795  1.00120.54           O  
ANISOU 1258  O   ALA A 172    13422  20746  11634   1944   1942    647       O  
ATOM   1259  CB  ALA A 172     -19.050  20.963  32.754  1.00122.36           C  
ANISOU 1259  CB  ALA A 172    13703  21135  11655   2368   1747     83       C  
ATOM   1260  N   ASP A 173     -18.016  19.546  30.643  1.00118.65           N  
ANISOU 1260  N   ASP A 173    13307  20317  11458   1995   1809    309       N  
ATOM   1261  CA  ASP A 173     -17.857  18.931  29.300  1.00115.12           C  
ANISOU 1261  CA  ASP A 173    12875  19699  11166   1807   1845    418       C  
ATOM   1262  C   ASP A 173     -16.378  18.574  29.127  1.00108.91           C  
ANISOU 1262  C   ASP A 173    12198  18786  10398   1750   1800    404       C  
ATOM   1263  O   ASP A 173     -15.584  19.491  28.840  1.00108.14           O  
ANISOU 1263  O   ASP A 173    12184  18630  10275   1823   1714    214       O  
ATOM   1264  CB  ASP A 173     -18.375  19.846  28.188  1.00114.08           C  
ANISOU 1264  CB  ASP A 173    12736  19470  11138   1780   1824    301       C  
ATOM   1265  CG  ASP A 173     -18.697  19.108  26.899  1.00111.22           C  
ANISOU 1265  CG  ASP A 173    12339  18987  10932   1590   1885    457       C  
ATOM   1266  OD1 ASP A 173     -18.484  17.879  26.853  1.00108.67           O  
ANISOU 1266  OD1 ASP A 173    12088  18507  10695   1478   1868    476       O  
ATOM   1267  OD2 ASP A 173     -19.158  19.769  25.948  1.00112.68           O  
ANISOU 1267  OD2 ASP A 173    12424  19233  11156   1553   1946    558       O  
ATOM   1268  N   LYS A 174     -16.031  17.299  29.321  1.00 98.82           N  
ANISOU 1268  N   LYS A 174    10920  17460   9168   1620   1854    605       N  
ATOM   1269  CA  LYS A 174     -14.634  16.864  29.195  1.00 88.01           C  
ANISOU 1269  CA  LYS A 174     9649  15982   7809   1569   1815    611       C  
ATOM   1270  C   LYS A 174     -14.216  17.038  27.735  1.00 92.58           C  
ANISOU 1270  C   LYS A 174    10287  16360   8528   1440   1792    574       C  
ATOM   1271  O   LYS A 174     -13.331  17.897  27.464  1.00 91.67           O  
ANISOU 1271  O   LYS A 174    10265  16158   8408   1460   1721    440       O  
ATOM   1272  CB  LYS A 174     -14.544  15.442  29.750  1.00 78.30           C  
ANISOU 1272  CB  LYS A 174     8399  14782   6570   1495   1876    838       C  
ATOM   1273  CG  LYS A 174     -14.676  15.366  31.267  1.00 72.94           C  
ANISOU 1273  CG  LYS A 174     7672  14304   5737   1631   1892    872       C  
ATOM   1274  CD  LYS A 174     -15.391  14.161  31.842  1.00 72.24           C  
ANISOU 1274  CD  LYS A 174     7491  14284   5672   1557   1987   1108       C  
ATOM   1275  CE  LYS A 174     -15.960  14.448  33.224  1.00 77.82           C  
ANISOU 1275  CE  LYS A 174     8144  15206   6219   1700   2006   1142       C  
ATOM   1276  NZ  LYS A 174     -17.243  13.744  33.479  1.00 71.91           N  
ANISOU 1276  NZ  LYS A 174     7386  14581   5356   1879   1953    934       N  
ATOM   1277  N   ALA A 175     -14.919  16.337  26.843  1.00 96.02           N  
ANISOU 1277  N   ALA A 175    10668  16723   9092   1307   1849    689       N  
ATOM   1278  CA  ALA A 175     -14.562  16.329  25.425  1.00 96.00           C  
ANISOU 1278  CA  ALA A 175    10710  16538   9228   1182   1831    663       C  
ATOM   1279  C   ALA A 175     -14.815  17.706  24.806  1.00 99.88           C  
ANISOU 1279  C   ALA A 175    11227  16950   9771   1245   1748    443       C  
ATOM   1280  O   ALA A 175     -15.529  17.861  23.817  1.00108.07           O  
ANISOU 1280  O   ALA A 175    12237  17882  10941   1165   1743    439       O  
ATOM   1281  CB  ALA A 175     -15.333  15.241  24.691  1.00 95.92           C  
ANISOU 1281  CB  ALA A 175    10635  16455   9358   1012   1902    863       C  
ATOM   1282  N   ALA A 176     -14.209  18.720  25.424  1.00 94.20           N  
ANISOU 1282  N   ALA A 176    10564  16282   8947   1392   1675    256       N  
ATOM   1283  CA  ALA A 176     -14.330  20.104  24.983  1.00 92.83           C  
ANISOU 1283  CA  ALA A 176    10425  16033   8813   1471   1584     34       C  
ATOM   1284  C   ALA A 176     -13.116  20.890  25.453  1.00 87.93           C  
ANISOU 1284  C   ALA A 176     9907  15371   8132   1569   1478   -147       C  
ATOM   1285  O   ALA A 176     -12.693  21.848  24.799  1.00 81.09           O  
ANISOU 1285  O   ALA A 176     9115  14336   7361   1574   1372   -318       O  
ATOM   1286  CB  ALA A 176     -15.622  20.732  25.510  1.00 93.41           C  
ANISOU 1286  CB  ALA A 176    10392  16322   8779   1606   1640     -9       C  
ATOM   1287  N   CYS A 177     -12.557  20.493  26.596  1.00 88.08           N  
ANISOU 1287  N   CYS A 177     9928  15546   7994   1649   1504   -107       N  
ATOM   1288  CA  CYS A 177     -11.298  21.044  27.078  1.00 90.13           C  
ANISOU 1288  CA  CYS A 177    10282  15765   8199   1727   1404   -257       C  
ATOM   1289  C   CYS A 177     -10.110  20.170  26.708  1.00 88.33           C  
ANISOU 1289  C   CYS A 177    10133  15373   8057   1592   1377   -166       C  
ATOM   1290  O   CYS A 177      -9.010  20.689  26.485  1.00 89.17           O  
ANISOU 1290  O   CYS A 177    10333  15334   8214   1591   1270   -299       O  
ATOM   1291  CB  CYS A 177     -11.351  21.218  28.601  1.00 92.70           C  
ANISOU 1291  CB  CYS A 177    10572  16334   8318   1901   1419   -285       C  
ATOM   1292  SG  CYS A 177      -9.859  21.916  29.352  1.00 95.25           S  
ANISOU 1292  SG  CYS A 177    10998  16637   8555   2015   1292   -477       S  
ATOM   1293  N   LEU A 178     -10.321  18.856  26.623  1.00 83.38           N  
ANISOU 1293  N   LEU A 178     9466  14764   7453   1479   1470     60       N  
ATOM   1294  CA  LEU A 178      -9.233  17.917  26.380  1.00 77.99           C  
ANISOU 1294  CA  LEU A 178     8850  13947   6835   1363   1454    161       C  
ATOM   1295  C   LEU A 178      -8.782  17.936  24.924  1.00 78.19           C  
ANISOU 1295  C   LEU A 178     8947  13682   7081   1207   1385    132       C  
ATOM   1296  O   LEU A 178      -7.584  18.034  24.638  1.00 78.75           O  
ANISOU 1296  O   LEU A 178     9109  13603   7209   1171   1302     63       O  
ATOM   1297  CB  LEU A 178      -9.677  16.507  26.781  1.00 73.20           C  
ANISOU 1297  CB  LEU A 178     8175  13454   6185   1298   1576    415       C  
ATOM   1298  CG  LEU A 178      -8.611  15.411  26.821  1.00 70.61           C  
ANISOU 1298  CG  LEU A 178     7905  13040   5885   1207   1575    543       C  
ATOM   1299  CD1 LEU A 178      -7.719  15.554  28.046  1.00 69.86           C  
ANISOU 1299  CD1 LEU A 178     7843  13089   5614   1343   1547    488       C  
ATOM   1300  CD2 LEU A 178      -9.266  14.038  26.778  1.00 71.31           C  
ANISOU 1300  CD2 LEU A 178     7923  13167   6003   1097   1689    799       C  
ATOM   1301  N   LEU A 179      -9.729  17.842  23.994  1.00 79.33           N  
ANISOU 1301  N   LEU A 179     9047  13748   7345   1116   1419    185       N  
ATOM   1302  CA  LEU A 179      -9.422  17.591  22.592  1.00 78.36           C  
ANISOU 1302  CA  LEU A 179     8980  13368   7425    954   1375    203       C  
ATOM   1303  C   LEU A 179      -8.748  18.767  21.883  1.00 70.58           C  
ANISOU 1303  C   LEU A 179     8080  12205   6530    967   1254     -2       C  
ATOM   1304  O   LEU A 179      -7.825  18.536  21.090  1.00 59.66           O  
ANISOU 1304  O   LEU A 179     6775  10625   5269    863   1197     -6       O  
ATOM   1305  CB  LEU A 179     -10.697  17.176  21.852  1.00 82.28           C  
ANISOU 1305  CB  LEU A 179     9398  13852   8014    864   1445    313       C  
ATOM   1306  CG  LEU A 179     -10.993  15.673  21.914  1.00 83.79           C  
ANISOU 1306  CG  LEU A 179     9538  14074   8224    754   1540    551       C  
ATOM   1307  CD1 LEU A 179     -11.913  15.252  20.783  1.00 83.91           C  
ANISOU 1307  CD1 LEU A 179     9508  13981   8395    621   1571    636       C  
ATOM   1308  CD2 LEU A 179      -9.707  14.854  21.891  1.00 84.38           C  
ANISOU 1308  CD2 LEU A 179     9695  14036   8330    681   1511    616       C  
ATOM   1309  N   PRO A 180      -9.163  20.024  22.102  1.00 76.20           N  
ANISOU 1309  N   PRO A 180     8781  12974   7195   1088   1210   -172       N  
ATOM   1310  CA  PRO A 180      -8.393  21.135  21.515  1.00 75.87           C  
ANISOU 1310  CA  PRO A 180     8827  12758   7241   1101   1089   -362       C  
ATOM   1311  C   PRO A 180      -6.944  21.170  21.968  1.00 79.60           C  
ANISOU 1311  C   PRO A 180     9379  13184   7680   1122   1018   -426       C  
ATOM   1312  O   PRO A 180      -6.089  21.698  21.246  1.00 84.86           O  
ANISOU 1312  O   PRO A 180    10124  13659   8460   1072    925   -526       O  
ATOM   1313  CB  PRO A 180      -9.159  22.387  21.973  1.00 77.34           C  
ANISOU 1313  CB  PRO A 180     8978  13059   7350   1254   1065   -522       C  
ATOM   1314  CG  PRO A 180     -10.065  21.927  23.058  1.00 87.76           C  
ANISOU 1314  CG  PRO A 180    10199  14644   8504   1346   1169   -428       C  
ATOM   1315  CD  PRO A 180     -10.408  20.516  22.718  1.00 85.28           C  
ANISOU 1315  CD  PRO A 180     9840  14325   8238   1207   1266   -198       C  
ATOM   1316  N   LYS A 181      -6.639  20.625  23.146  1.00 78.63           N  
ANISOU 1316  N   LYS A 181     9236  13234   7404   1195   1059   -367       N  
ATOM   1317  CA  LYS A 181      -5.255  20.470  23.573  1.00 67.37           C  
ANISOU 1317  CA  LYS A 181     7881  11770   5947   1203    998   -402       C  
ATOM   1318  C   LYS A 181      -4.669  19.131  23.155  1.00 59.10           C  
ANISOU 1318  C   LYS A 181     6856  10630   4969   1062   1038   -223       C  
ATOM   1319  O   LYS A 181      -3.454  19.032  22.947  1.00 53.57           O  
ANISOU 1319  O   LYS A 181     6227   9807   4319   1018    972   -256       O  
ATOM   1320  CB  LYS A 181      -5.147  20.629  25.091  1.00 72.75           C  
ANISOU 1320  CB  LYS A 181     8534  12689   6417   1369   1011   -445       C  
ATOM   1321  CG  LYS A 181      -5.538  22.007  25.589  1.00 68.83           C  
ANISOU 1321  CG  LYS A 181     8027  12280   5845   1526    954   -649       C  
ATOM   1322  CD  LYS A 181      -4.904  22.307  26.933  1.00 68.85           C  
ANISOU 1322  CD  LYS A 181     8040  12453   5668   1681    917   -742       C  
ATOM   1323  CE  LYS A 181      -5.836  21.925  28.070  1.00 70.58           C  
ANISOU 1323  CE  LYS A 181     8169  12958   5690   1801   1022   -656       C  
ATOM   1324  NZ  LYS A 181      -7.250  22.280  27.766  1.00 67.48           N  
ANISOU 1324  NZ  LYS A 181     7703  12627   5311   1822   1082   -648       N  
ATOM   1325  N   LEU A 182      -5.500  18.099  23.028  1.00 61.33           N  
ANISOU 1325  N   LEU A 182     7077  10967   5259    990   1141    -36       N  
ATOM   1326  CA  LEU A 182      -5.056  16.825  22.482  1.00 57.69           C  
ANISOU 1326  CA  LEU A 182     6637  10393   4888    846   1175    133       C  
ATOM   1327  C   LEU A 182      -5.104  16.794  20.964  1.00 84.86           C  
ANISOU 1327  C   LEU A 182    10113  13602   8529    702   1143    135       C  
ATOM   1328  O   LEU A 182      -4.958  15.718  20.374  1.00 98.34           O  
ANISOU 1328  O   LEU A 182    11829  15210  10325    577   1176    278       O  
ATOM   1329  CB  LEU A 182      -5.886  15.679  23.058  1.00 69.18           C  
ANISOU 1329  CB  LEU A 182     8011  12004   6268    829   1295    340       C  
ATOM   1330  CG  LEU A 182      -5.065  14.781  23.983  1.00 73.13           C  
ANISOU 1330  CG  LEU A 182     8528  12592   6664    852   1320    446       C  
ATOM   1331  CD1 LEU A 182      -4.595  15.565  25.199  1.00 50.33           C  
ANISOU 1331  CD1 LEU A 182     5650   9871   3601   1024   1282    314       C  
ATOM   1332  CD2 LEU A 182      -5.864  13.565  24.398  1.00 77.06           C  
ANISOU 1332  CD2 LEU A 182     8950  13212   7118    811   1440    672       C  
ATOM   1333  N   ASP A 183      -5.294  17.948  20.323  1.00 85.85           N  
ANISOU 1333  N   ASP A 183    10258  13636   8725    722   1078    -20       N  
ATOM   1334  CA  ASP A 183      -5.092  18.091  18.890  1.00 74.28           C  
ANISOU 1334  CA  ASP A 183     8841  11942   7441    601   1029    -45       C  
ATOM   1335  C   ASP A 183      -3.909  18.982  18.544  1.00 64.49           C  
ANISOU 1335  C   ASP A 183     7686  10559   6258    612    917   -205       C  
ATOM   1336  O   ASP A 183      -3.390  18.887  17.427  1.00 65.82           O  
ANISOU 1336  O   ASP A 183     7907  10535   6568    504    876   -203       O  
ATOM   1337  CB  ASP A 183      -6.358  18.647  18.221  1.00 72.09           C  
ANISOU 1337  CB  ASP A 183     8513  11652   7224    593   1047    -74       C  
ATOM   1338  CG  ASP A 183      -7.387  17.568  17.942  1.00 69.31           C  
ANISOU 1338  CG  ASP A 183     8089  11343   6903    508   1145    107       C  
ATOM   1339  OD1 ASP A 183      -6.994  16.386  17.852  1.00 66.13           O  
ANISOU 1339  OD1 ASP A 183     7696  10901   6529    417   1180    249       O  
ATOM   1340  OD2 ASP A 183      -8.584  17.900  17.810  1.00 71.37           O  
ANISOU 1340  OD2 ASP A 183     8283  11673   7163    532   1182    105       O  
ATOM   1341  N   GLU A 184      -3.467  19.830  19.474  1.00 54.04           N  
ANISOU 1341  N   GLU A 184     6377   9327   4828    741    865   -340       N  
ATOM   1342  CA  GLU A 184      -2.283  20.657  19.281  1.00 56.72           C  
ANISOU 1342  CA  GLU A 184     6792   9542   5218    754    756   -490       C  
ATOM   1343  C   GLU A 184      -1.006  19.947  19.712  1.00 60.96           C  
ANISOU 1343  C   GLU A 184     7371  10069   5722    732    737   -443       C  
ATOM   1344  O   GLU A 184       0.049  20.156  19.100  1.00 51.92           O  
ANISOU 1344  O   GLU A 184     6288   8764   4675    672    665   -498       O  
ATOM   1345  CB  GLU A 184      -2.436  21.973  20.055  1.00 60.78           C  
ANISOU 1345  CB  GLU A 184     7300  10151   5644    906    697   -674       C  
ATOM   1346  CG  GLU A 184      -1.228  22.898  20.004  1.00 67.97           C  
ANISOU 1346  CG  GLU A 184     8281  10945   6601    930    578   -838       C  
ATOM   1347  CD  GLU A 184      -1.350  24.068  20.966  1.00 78.61           C  
ANISOU 1347  CD  GLU A 184     9621  12406   7842   1092    519  -1016       C  
ATOM   1348  OE1 GLU A 184      -1.813  23.858  22.107  1.00 83.73           O  
ANISOU 1348  OE1 GLU A 184    10221  13267   8327   1203    568   -999       O  
ATOM   1349  OE2 GLU A 184      -0.986  25.200  20.580  1.00 81.40           O  
ANISOU 1349  OE2 GLU A 184    10015  12636   8277   1110    422  -1172       O  
ATOM   1350  N   LEU A 185      -1.083  19.102  20.743  1.00 63.18           N  
ANISOU 1350  N   LEU A 185     7616  10520   5868    780    803   -338       N  
ATOM   1351  CA  LEU A 185       0.098  18.391  21.227  1.00 60.00           C  
ANISOU 1351  CA  LEU A 185     7251  10122   5424    770    788   -288       C  
ATOM   1352  C   LEU A 185       0.555  17.336  20.226  1.00 56.89           C  
ANISOU 1352  C   LEU A 185     6889   9566   5161    616    807   -154       C  
ATOM   1353  O   LEU A 185       1.736  17.278  19.863  1.00 49.95           O  
ANISOU 1353  O   LEU A 185     6068   8564   4346    569    745   -186       O  
ATOM   1354  CB  LEU A 185      -0.208  17.750  22.581  1.00 65.10           C  
ANISOU 1354  CB  LEU A 185     7847  11001   5888    865    859   -196       C  
ATOM   1355  CG  LEU A 185       0.956  17.505  23.539  1.00 69.58           C  
ANISOU 1355  CG  LEU A 185     8447  11642   6350    931    822   -214       C  
ATOM   1356  CD1 LEU A 185       1.652  18.815  23.856  1.00 67.82           C  
ANISOU 1356  CD1 LEU A 185     8260  11403   6104   1026    709   -434       C  
ATOM   1357  CD2 LEU A 185       0.460  16.834  24.813  1.00 72.82           C  
ANISOU 1357  CD2 LEU A 185     8800  12293   6577   1024    907   -102       C  
ATOM   1358  N   ARG A 186      -0.367  16.482  19.779  1.00 56.80           N  
ANISOU 1358  N   ARG A 186     6836   9554   5191    538    892     -4       N  
ATOM   1359  CA  ARG A 186      -0.032  15.464  18.792  1.00 63.81           C  
ANISOU 1359  CA  ARG A 186     7753  10286   6206    396    909    119       C  
ATOM   1360  C   ARG A 186       0.365  16.073  17.453  1.00 64.40           C  
ANISOU 1360  C   ARG A 186     7879  10150   6441    314    838     28       C  
ATOM   1361  O   ARG A 186       1.151  15.466  16.718  1.00 58.48           O  
ANISOU 1361  O   ARG A 186     7175   9260   5786    220    818     77       O  
ATOM   1362  CB  ARG A 186      -1.213  14.508  18.618  1.00 70.90           C  
ANISOU 1362  CB  ARG A 186     8589  11231   7118    335   1008    286       C  
ATOM   1363  CG  ARG A 186      -1.026  13.494  17.515  1.00 82.78           C  
ANISOU 1363  CG  ARG A 186    10120  12568   8765    188   1021    402       C  
ATOM   1364  CD  ARG A 186      -1.776  12.216  17.823  1.00 93.34           C  
ANISOU 1364  CD  ARG A 186    11402  13982  10080    142   1116    597       C  
ATOM   1365  NE  ARG A 186      -1.697  11.851  19.236  1.00 97.56           N  
ANISOU 1365  NE  ARG A 186    11906  14709  10452    236   1162    661       N  
ATOM   1366  CZ  ARG A 186      -2.559  11.034  19.832  1.00 99.97           C  
ANISOU 1366  CZ  ARG A 186    12144  15144  10697    235   1254    816       C  
ATOM   1367  NH1 ARG A 186      -2.436  10.739  21.120  1.00 99.68           N  
ANISOU 1367  NH1 ARG A 186    12081  15287  10505    328   1294    875       N  
ATOM   1368  NH2 ARG A 186      -3.552  10.514  19.132  1.00 98.63           N  
ANISOU 1368  NH2 ARG A 186    11929  14925  10622    142   1304    915       N  
ATOM   1369  N   ASP A 187      -0.158  17.255  17.119  1.00 66.27           N  
ANISOU 1369  N   ASP A 187     8109  10363   6708    352    801   -102       N  
ATOM   1370  CA  ASP A 187       0.310  17.952  15.926  1.00 62.90           C  
ANISOU 1370  CA  ASP A 187     7734   9743   6424    287    728   -195       C  
ATOM   1371  C   ASP A 187       1.756  18.402  16.091  1.00 61.15           C  
ANISOU 1371  C   ASP A 187     7571   9455   6209    307    642   -294       C  
ATOM   1372  O   ASP A 187       2.558  18.289  15.156  1.00 52.28           O  
ANISOU 1372  O   ASP A 187     6494   8170   5199    219    602   -294       O  
ATOM   1373  CB  ASP A 187      -0.593  19.147  15.624  1.00 72.71           C  
ANISOU 1373  CB  ASP A 187     8955  10983   7690    335    705   -308       C  
ATOM   1374  CG  ASP A 187      -1.777  18.776  14.754  1.00 72.13           C  
ANISOU 1374  CG  ASP A 187     8842  10873   7691    261    763   -221       C  
ATOM   1375  OD1 ASP A 187      -1.949  17.572  14.470  1.00 71.08           O  
ANISOU 1375  OD1 ASP A 187     8693  10727   7585    177    822    -72       O  
ATOM   1376  OD2 ASP A 187      -2.535  19.685  14.357  1.00 74.13           O  
ANISOU 1376  OD2 ASP A 187     9078  11109   7979    290    745   -303       O  
ATOM   1377  N   GLU A 188       2.106  18.917  17.272  1.00 59.71           N  
ANISOU 1377  N   GLU A 188     7383   9399   5904    423    612   -382       N  
ATOM   1378  CA  GLU A 188       3.499  19.247  17.551  1.00 62.87           C  
ANISOU 1378  CA  GLU A 188     7831   9752   6303    444    531   -469       C  
ATOM   1379  C   GLU A 188       4.356  17.993  17.664  1.00 59.94           C  
ANISOU 1379  C   GLU A 188     7479   9372   5922    388    557   -344       C  
ATOM   1380  O   GLU A 188       5.564  18.044  17.405  1.00 54.19           O  
ANISOU 1380  O   GLU A 188     6795   8548   5247    356    495   -384       O  
ATOM   1381  CB  GLU A 188       3.603  20.068  18.837  1.00 71.08           C  
ANISOU 1381  CB  GLU A 188     8858  10942   7207    590    490   -597       C  
ATOM   1382  CG  GLU A 188       3.029  21.472  18.740  1.00 76.89           C  
ANISOU 1382  CG  GLU A 188     9588  11663   7964    656    437   -756       C  
ATOM   1383  CD  GLU A 188       3.387  22.328  19.940  1.00 90.36           C  
ANISOU 1383  CD  GLU A 188    11292  13489   9551    798    373   -906       C  
ATOM   1384  OE1 GLU A 188       4.508  22.173  20.469  1.00 94.28           O  
ANISOU 1384  OE1 GLU A 188    11815  13998  10011    818    326   -934       O  
ATOM   1385  OE2 GLU A 188       2.547  23.153  20.356  1.00 93.83           O  
ANISOU 1385  OE2 GLU A 188    11703  14012   9934    895    367  -1000       O  
ATOM   1386  N   GLY A 189       3.753  16.866  18.048  1.00 48.40           N  
ANISOU 1386  N   GLY A 189     5983   8009   4397    376    646   -189       N  
ATOM   1387  CA  GLY A 189       4.519  15.637  18.180  1.00 48.12           C  
ANISOU 1387  CA  GLY A 189     5967   7963   4354    328    671    -63       C  
ATOM   1388  C   GLY A 189       5.011  15.113  16.844  1.00 44.97           C  
ANISOU 1388  C   GLY A 189     5608   7368   4110    196    659     -9       C  
ATOM   1389  O   GLY A 189       6.174  14.722  16.708  1.00 44.87           O  
ANISOU 1389  O   GLY A 189     5635   7286   4127    165    622      0       O  
ATOM   1390  N   LYS A 190       4.130  15.093  15.840  1.00 51.29           N  
ANISOU 1390  N   LYS A 190     6396   8083   5008    121    689     26       N  
ATOM   1391  CA  LYS A 190       4.541  14.666  14.506  1.00 51.14           C  
ANISOU 1391  CA  LYS A 190     6415   7882   5135      3    674     65       C  
ATOM   1392  C   LYS A 190       5.597  15.601  13.933  1.00 41.92           C  
ANISOU 1392  C   LYS A 190     5294   6592   4041     -7    584    -67       C  
ATOM   1393  O   LYS A 190       6.527  15.158  13.249  1.00 52.37           O  
ANISOU 1393  O   LYS A 190     6656   7799   5442    -75    559    -41       O  
ATOM   1394  CB  LYS A 190       3.328  14.594  13.578  1.00 55.12           C  
ANISOU 1394  CB  LYS A 190     6893   8330   5720    -63    716    111       C  
ATOM   1395  CG  LYS A 190       2.232  13.655  14.053  1.00 51.72           C  
ANISOU 1395  CG  LYS A 190     6408   8009   5234    -68    806    250       C  
ATOM   1396  CD  LYS A 190       2.754  12.239  14.233  1.00 56.70           C  
ANISOU 1396  CD  LYS A 190     7052   8632   5861   -117    841    395       C  
ATOM   1397  CE  LYS A 190       1.693  11.335  14.842  1.00 63.67           C  
ANISOU 1397  CE  LYS A 190     7875   9632   6684   -118    930    540       C  
ATOM   1398  NZ  LYS A 190       2.207   9.960  15.096  1.00 62.60           N  
ANISOU 1398  NZ  LYS A 190     7754   9488   6545   -160    962    684       N  
ATOM   1399  N   ALA A 191       5.470  16.902  14.205  1.00 39.25           N  
ANISOU 1399  N   ALA A 191     4952   6280   3684     63    534   -209       N  
ATOM   1400  CA  ALA A 191       6.481  17.854  13.761  1.00 40.78           C  
ANISOU 1400  CA  ALA A 191     5184   6361   3948     56    445   -335       C  
ATOM   1401  C   ALA A 191       7.804  17.630  14.483  1.00 47.75           C  
ANISOU 1401  C   ALA A 191     6088   7275   4779     89    402   -357       C  
ATOM   1402  O   ALA A 191       8.874  17.702  13.867  1.00 48.86           O  
ANISOU 1402  O   ALA A 191     6262   7299   5002     35    353   -383       O  
ATOM   1403  CB  ALA A 191       5.986  19.284  13.979  1.00 46.32           C  
ANISOU 1403  CB  ALA A 191     5874   7084   4641    129    398   -481       C  
ATOM   1404  N   SER A 192       7.751  17.352  15.788  1.00 44.44           N  
ANISOU 1404  N   SER A 192     5646   7020   4220    179    422   -345       N  
ATOM   1405  CA  SER A 192       8.978  17.182  16.561  1.00 47.18           C  
ANISOU 1405  CA  SER A 192     6010   7411   4505    223    377   -373       C  
ATOM   1406  C   SER A 192       9.762  15.958  16.103  1.00 36.75           C  
ANISOU 1406  C   SER A 192     4712   6020   3230    143    399   -250       C  
ATOM   1407  O   SER A 192      10.988  16.018  15.951  1.00 36.43           O  
ANISOU 1407  O   SER A 192     4699   5915   3229    126    341   -291       O  
ATOM   1408  CB  SER A 192       8.643  17.081  18.051  1.00 38.75           C  
ANISOU 1408  CB  SER A 192     4910   6547   3266    343    400   -374       C  
ATOM   1409  OG  SER A 192       9.809  16.842  18.819  1.00 45.31           O  
ANISOU 1409  OG  SER A 192     5756   7429   4030    389    357   -394       O  
ATOM   1410  N   SER A 193       9.070  14.839  15.880  1.00 36.59           N  
ANISOU 1410  N   SER A 193     4681   6012   3210     95    481   -100       N  
ATOM   1411  CA  SER A 193       9.748  13.606  15.489  1.00 40.72           C  
ANISOU 1411  CA  SER A 193     5227   6470   3774     26    503     19       C  
ATOM   1412  C   SER A 193      10.330  13.715  14.084  1.00 39.67           C  
ANISOU 1412  C   SER A 193     5129   6153   3792    -72    467     -2       C  
ATOM   1413  O   SER A 193      11.397  13.158  13.800  1.00 34.47           O  
ANISOU 1413  O   SER A 193     4497   5430   3170   -106    444     28       O  
ATOM   1414  CB  SER A 193       8.781  12.430  15.561  1.00 36.32           C  
ANISOU 1414  CB  SER A 193     4648   5959   3193     -5    594    181       C  
ATOM   1415  OG  SER A 193       9.181  11.380  14.697  1.00 41.06           O  
ANISOU 1415  OG  SER A 193     5276   6440   3886    -98    610    283       O  
ATOM   1416  N   ALA A 194       9.639  14.425  13.192  1.00 34.34           N  
ANISOU 1416  N   ALA A 194     4451   5396   3199   -112    463    -50       N  
ATOM   1417  CA  ALA A 194      10.124  14.575  11.825  1.00 40.77           C  
ANISOU 1417  CA  ALA A 194     5296   6045   4150   -201    433    -67       C  
ATOM   1418  C   ALA A 194      11.336  15.497  11.767  1.00 36.45           C  
ANISOU 1418  C   ALA A 194     4768   5445   3637   -186    349   -187       C  
ATOM   1419  O   ALA A 194      12.301  15.214  11.050  1.00 32.48           O  
ANISOU 1419  O   ALA A 194     4289   4842   3208   -242    325   -174       O  
ATOM   1420  CB  ALA A 194       8.999  15.094  10.933  1.00 40.99           C  
ANISOU 1420  CB  ALA A 194     5313   6012   4249   -241    452    -82       C  
ATOM   1421  N   LYS A 195      11.310  16.598  12.523  1.00 33.79           N  
ANISOU 1421  N   LYS A 195     4418   5173   3248   -109    303   -307       N  
ATOM   1422  CA  LYS A 195      12.455  17.503  12.541  1.00 33.81           C  
ANISOU 1422  CA  LYS A 195     4433   5125   3288    -97    217   -425       C  
ATOM   1423  C   LYS A 195      13.676  16.836  13.165  1.00 34.06           C  
ANISOU 1423  C   LYS A 195     4473   5199   3271    -77    196   -400       C  
ATOM   1424  O   LYS A 195      14.804  17.034  12.699  1.00 33.88           O  
ANISOU 1424  O   LYS A 195     4463   5092   3319   -114    144   -437       O  
ATOM   1425  CB  LYS A 195      12.100  18.787  13.287  1.00 34.62           C  
ANISOU 1425  CB  LYS A 195     4520   5291   3344    -12    168   -563       C  
ATOM   1426  CG  LYS A 195      11.110  19.674  12.551  1.00 45.20           C  
ANISOU 1426  CG  LYS A 195     5857   6563   4754    -31    168   -611       C  
ATOM   1427  CD  LYS A 195      10.455  20.673  13.491  1.00 52.51           C  
ANISOU 1427  CD  LYS A 195     6763   7588   5603     72    140   -725       C  
ATOM   1428  CE  LYS A 195      11.438  21.743  13.937  1.00 56.80           C  
ANISOU 1428  CE  LYS A 195     7314   8108   6159    117     39   -872       C  
ATOM   1429  NZ  LYS A 195      10.791  22.742  14.832  1.00 62.17           N  
ANISOU 1429  NZ  LYS A 195     7978   8879   6766    225      4   -995       N  
ATOM   1430  N   GLN A 196      13.470  16.039  14.215  1.00 39.04           N  
ANISOU 1430  N   GLN A 196     5090   5963   3780    -17    236   -334       N  
ATOM   1431  CA  GLN A 196      14.586  15.330  14.832  1.00 39.90           C  
ANISOU 1431  CA  GLN A 196     5205   6118   3836      7    218   -301       C  
ATOM   1432  C   GLN A 196      15.095  14.204  13.943  1.00 34.24           C  
ANISOU 1432  C   GLN A 196     4511   5304   3194    -78    249   -185       C  
ATOM   1433  O   GLN A 196      16.300  13.925  13.928  1.00 37.70           O  
ANISOU 1433  O   GLN A 196     4961   5715   3649    -86    211   -189       O  
ATOM   1434  CB  GLN A 196      14.171  14.781  16.198  1.00 40.45           C  
ANISOU 1434  CB  GLN A 196     5256   6362   3750     99    256   -251       C  
ATOM   1435  CG  GLN A 196      15.273  14.033  16.935  1.00 36.57           C  
ANISOU 1435  CG  GLN A 196     4772   5933   3191    136    237   -212       C  
ATOM   1436  CD  GLN A 196      16.398  14.940  17.388  1.00 36.96           C  
ANISOU 1436  CD  GLN A 196     4820   5993   3231    184    140   -355       C  
ATOM   1437  OE1 GLN A 196      16.216  16.147  17.541  1.00 42.34           O  
ANISOU 1437  OE1 GLN A 196     5491   6677   3920    218     88   -487       O  
ATOM   1438  NE2 GLN A 196      17.572  14.361  17.610  1.00 38.63           N  
ANISOU 1438  NE2 GLN A 196     5039   6207   3431    188    111   -330       N  
ATOM   1439  N   ARG A 197      14.198  13.541  13.206  1.00 35.61           N  
ANISOU 1439  N   ARG A 197     4689   5428   3413   -139    315    -85       N  
ATOM   1440  CA  ARG A 197      14.629  12.497  12.283  1.00 41.61           C  
ANISOU 1440  CA  ARG A 197     5473   6087   4251   -217    340     14       C  
ATOM   1441  C   ARG A 197      15.572  13.050  11.222  1.00 32.18           C  
ANISOU 1441  C   ARG A 197     4296   4762   3169   -274    286    -52       C  
ATOM   1442  O   ARG A 197      16.504  12.358  10.797  1.00 31.82           O  
ANISOU 1442  O   ARG A 197     4267   4661   3162   -307    278     -8       O  
ATOM   1443  CB  ARG A 197      13.413  11.840  11.626  1.00 32.60           C  
ANISOU 1443  CB  ARG A 197     4331   4908   3148   -273    409    114       C  
ATOM   1444  CG  ARG A 197      13.728  10.544  10.898  1.00 35.98           C  
ANISOU 1444  CG  ARG A 197     4784   5254   3635   -339    440    229       C  
ATOM   1445  CD  ARG A 197      14.360   9.536  11.842  1.00 49.69           C  
ANISOU 1445  CD  ARG A 197     6525   7067   5290   -295    451    307       C  
ATOM   1446  NE  ARG A 197      14.729   8.291  11.174  1.00 32.30           N  
ANISOU 1446  NE  ARG A 197     4348   4778   3146   -351    472    411       N  
ATOM   1447  CZ  ARG A 197      15.904   8.073  10.593  1.00 39.54           C  
ANISOU 1447  CZ  ARG A 197     5288   5616   4118   -374    434    394       C  
ATOM   1448  NH1 ARG A 197      16.830   9.023  10.584  1.00 31.69           N  
ANISOU 1448  NH1 ARG A 197     4290   4616   3134   -354    374    284       N  
ATOM   1449  NH2 ARG A 197      16.153   6.905  10.018  1.00 38.90           N  
ANISOU 1449  NH2 ARG A 197     5231   5461   4086   -416    455    488       N  
ATOM   1450  N   LEU A 198      15.350  14.292  10.790  1.00 31.99           N  
ANISOU 1450  N   LEU A 198     4265   4689   3199   -283    249   -155       N  
ATOM   1451  CA  LEU A 198      16.273  14.927   9.856  1.00 33.51           C  
ANISOU 1451  CA  LEU A 198     4469   4767   3497   -334    196   -217       C  
ATOM   1452  C   LEU A 198      17.625  15.188  10.510  1.00 40.31           C  
ANISOU 1452  C   LEU A 198     5323   5661   4333   -296    132   -281       C  
ATOM   1453  O   LEU A 198      18.670  15.039   9.867  1.00 31.42           O  
ANISOU 1453  O   LEU A 198     4202   4460   3274   -339    107   -277       O  
ATOM   1454  CB  LEU A 198      15.667  16.227   9.327  1.00 36.40           C  
ANISOU 1454  CB  LEU A 198     4830   5077   3925   -347    170   -308       C  
ATOM   1455  CG  LEU A 198      16.563  17.122   8.469  1.00 31.37           C  
ANISOU 1455  CG  LEU A 198     4197   4327   3396   -394    111   -380       C  
ATOM   1456  CD1 LEU A 198      16.976  16.409   7.191  1.00 29.96           C  
ANISOU 1456  CD1 LEU A 198     4035   4046   3301   -474    138   -299       C  
ATOM   1457  CD2 LEU A 198      15.855  18.430   8.156  1.00 33.43           C  
ANISOU 1457  CD2 LEU A 198     4453   4544   3706   -393     83   -468       C  
ATOM   1458  N   LYS A 199      17.624  15.573  11.790  1.00 38.44           N  
ANISOU 1458  N   LYS A 199     5069   5539   3996   -212    105   -342       N  
ATOM   1459  CA  LYS A 199      18.882  15.802  12.493  1.00 33.28           C  
ANISOU 1459  CA  LYS A 199     4405   4927   3313   -170     39   -408       C  
ATOM   1460  C   LYS A 199      19.697  14.520  12.593  1.00 38.79           C  
ANISOU 1460  C   LYS A 199     5112   5643   3984   -176     60   -309       C  
ATOM   1461  O   LYS A 199      20.914  14.528  12.370  1.00 39.68           O  
ANISOU 1461  O   LYS A 199     5221   5716   4140   -193     15   -334       O  
ATOM   1462  CB  LYS A 199      18.611  16.371  13.887  1.00 39.76           C  
ANISOU 1462  CB  LYS A 199     5208   5882   4017    -68      8   -490       C  
ATOM   1463  CG  LYS A 199      18.069  17.790  13.895  1.00 38.65           C  
ANISOU 1463  CG  LYS A 199     5058   5721   3906    -49    -37   -617       C  
ATOM   1464  CD  LYS A 199      18.139  18.391  15.292  1.00 44.85           C  
ANISOU 1464  CD  LYS A 199     5826   6636   4578     60    -89   -721       C  
ATOM   1465  CE  LYS A 199      17.579  19.804  15.321  1.00 44.96           C  
ANISOU 1465  CE  LYS A 199     5833   6625   4625     87   -139   -855       C  
ATOM   1466  NZ  LYS A 199      16.132  19.833  14.971  1.00 42.97           N  
ANISOU 1466  NZ  LYS A 199     5584   6374   4368     81    -72   -813       N  
ATOM   1467  N   CYS A 200      19.042  13.406  12.928  1.00 33.30           N  
ANISOU 1467  N   CYS A 200     4427   5007   3221   -161    128   -195       N  
ATOM   1468  CA  CYS A 200      19.743  12.131  13.020  1.00 37.02           C  
ANISOU 1468  CA  CYS A 200     4910   5487   3669   -163    149    -93       C  
ATOM   1469  C   CYS A 200      20.262  11.688  11.657  1.00 32.99           C  
ANISOU 1469  C   CYS A 200     4417   4840   3277   -249    157    -49       C  
ATOM   1470  O   CYS A 200      21.386  11.183  11.550  1.00 32.28           O  
ANISOU 1470  O   CYS A 200     4330   4732   3203   -252    134    -30       O  
ATOM   1471  CB  CYS A 200      18.820  11.068  13.617  1.00 33.68           C  
ANISOU 1471  CB  CYS A 200     4492   5143   3161   -136    222     27       C  
ATOM   1472  SG  CYS A 200      18.329  11.385  15.338  1.00 46.19           S  
ANISOU 1472  SG  CYS A 200     6054   6917   4581    -19    221     -4       S  
ATOM   1473  N   ALA A 201      19.454  11.857  10.607  1.00 31.64           N  
ANISOU 1473  N   ALA A 201     4256   4579   3185   -313    190    -32       N  
ATOM   1474  CA  ALA A 201      19.891  11.475   9.269  1.00 35.96           C  
ANISOU 1474  CA  ALA A 201     4820   5004   3838   -389    197      6       C  
ATOM   1475  C   ALA A 201      21.099  12.291   8.829  1.00 38.20           C  
ANISOU 1475  C   ALA A 201     5091   5236   4188   -407    134    -81       C  
ATOM   1476  O   ALA A 201      22.046  11.745   8.253  1.00 32.58           O  
ANISOU 1476  O   ALA A 201     4383   4475   3520   -434    127    -49       O  
ATOM   1477  CB  ALA A 201      18.741  11.638   8.276  1.00 30.17           C  
ANISOU 1477  CB  ALA A 201     4098   4197   3170   -446    237     28       C  
ATOM   1478  N   SER A 202      21.086  13.599   9.092  1.00 30.88           N  
ANISOU 1478  N   SER A 202     4144   4317   3271   -392     86   -190       N  
ATOM   1479  CA  SER A 202      22.210  14.439   8.690  1.00 37.15           C  
ANISOU 1479  CA  SER A 202     4920   5057   4139   -417     23   -270       C  
ATOM   1480  C   SER A 202      23.484  14.070   9.441  1.00 47.36           C  
ANISOU 1480  C   SER A 202     6197   6411   5388   -375    -19   -282       C  
ATOM   1481  O   SER A 202      24.582  14.165   8.880  1.00 42.87           O  
ANISOU 1481  O   SER A 202     5613   5791   4886   -408    -50   -296       O  
ATOM   1482  CB  SER A 202      21.870  15.912   8.912  1.00 34.04           C  
ANISOU 1482  CB  SER A 202     4510   4656   3769   -406    -26   -386       C  
ATOM   1483  OG  SER A 202      22.025  16.271  10.274  1.00 44.08           O  
ANISOU 1483  OG  SER A 202     5765   6034   4949   -327    -69   -456       O  
ATOM   1484  N   LEU A 203      23.357  13.641  10.698  1.00 47.04           N  
ANISOU 1484  N   LEU A 203     6154   6485   5234   -301    -18   -273       N  
ATOM   1485  CA  LEU A 203      24.526  13.262  11.484  1.00 40.30           C  
ANISOU 1485  CA  LEU A 203     5285   5700   4327   -252    -60   -283       C  
ATOM   1486  C   LEU A 203      25.049  11.886  11.091  1.00 40.82           C  
ANISOU 1486  C   LEU A 203     5368   5747   4396   -266    -21   -170       C  
ATOM   1487  O   LEU A 203      26.266  11.671  11.051  1.00 45.22           O  
ANISOU 1487  O   LEU A 203     5909   6302   4971   -263    -57   -179       O  
ATOM   1488  CB  LEU A 203      24.185  13.288  12.975  1.00 33.60           C  
ANISOU 1488  CB  LEU A 203     4431   4990   3347   -159    -73   -311       C  
ATOM   1489  CG  LEU A 203      24.383  14.613  13.713  1.00 39.86           C  
ANISOU 1489  CG  LEU A 203     5196   5828   4120   -114   -150   -455       C  
ATOM   1490  CD1 LEU A 203      23.687  14.586  15.070  1.00 43.78           C  
ANISOU 1490  CD1 LEU A 203     5691   6466   4475    -18   -143   -470       C  
ATOM   1491  CD2 LEU A 203      25.863  14.912  13.871  1.00 41.52           C  
ANISOU 1491  CD2 LEU A 203     5377   6036   4361   -109   -227   -521       C  
ATOM   1492  N   GLN A 204      24.152  10.946  10.798  1.00 37.36           N  
ANISOU 1492  N   GLN A 204     4960   5293   3943   -282     49    -66       N  
ATOM   1493  CA  GLN A 204      24.552   9.568  10.544  1.00 39.02           C  
ANISOU 1493  CA  GLN A 204     5191   5486   4151   -286     83     42       C  
ATOM   1494  C   GLN A 204      24.793   9.273   9.069  1.00 36.67           C  
ANISOU 1494  C   GLN A 204     4905   5064   3962   -361    102     75       C  
ATOM   1495  O   GLN A 204      25.667   8.460   8.746  1.00 41.52           O  
ANISOU 1495  O   GLN A 204     5526   5655   4594   -361    100    120       O  
ATOM   1496  CB  GLN A 204      23.495   8.607  11.096  1.00 38.94           C  
ANISOU 1496  CB  GLN A 204     5204   5525   4067   -261    145    144       C  
ATOM   1497  CG  GLN A 204      23.454   8.558  12.615  1.00 48.48           C  
ANISOU 1497  CG  GLN A 204     6400   6872   5147   -173    133    140       C  
ATOM   1498  CD  GLN A 204      22.148   8.008  13.150  1.00 55.01           C  
ANISOU 1498  CD  GLN A 204     7240   7756   5907   -155    197    225       C  
ATOM   1499  OE1 GLN A 204      21.336   7.462  12.403  1.00 63.77           O  
ANISOU 1499  OE1 GLN A 204     8368   8794   7069   -210    250    300       O  
ATOM   1500  NE2 GLN A 204      21.937   8.152  14.453  1.00 60.15           N  
ANISOU 1500  NE2 GLN A 204     7876   8538   6439    -76    192    215       N  
ATOM   1501  N   LYS A 205      24.049   9.909   8.165  1.00 33.81           N  
ANISOU 1501  N   LYS A 205     4549   4629   3670   -418    119     51       N  
ATOM   1502  CA  LYS A 205      24.225   9.649   6.741  1.00 42.50           C  
ANISOU 1502  CA  LYS A 205     5661   5621   4865   -483    138     82       C  
ATOM   1503  C   LYS A 205      25.184  10.631   6.076  1.00 45.73           C  
ANISOU 1503  C   LYS A 205     6042   5983   5351   -515     92      5       C  
ATOM   1504  O   LYS A 205      25.936  10.243   5.175  1.00 43.71           O  
ANISOU 1504  O   LYS A 205     5786   5672   5151   -544     95     31       O  
ATOM   1505  CB  LYS A 205      22.872   9.690   6.024  1.00 43.01           C  
ANISOU 1505  CB  LYS A 205     5747   5629   4964   -527    185    112       C  
ATOM   1506  CG  LYS A 205      21.978   8.496   6.304  1.00 62.79           C  
ANISOU 1506  CG  LYS A 205     8280   8152   7426   -517    238    211       C  
ATOM   1507  CD  LYS A 205      22.253   7.361   5.332  1.00 71.80           C  
ANISOU 1507  CD  LYS A 205     9447   9214   8619   -550    263    286       C  
ATOM   1508  CE  LYS A 205      21.312   7.414   4.139  1.00 74.52           C  
ANISOU 1508  CE  LYS A 205     9808   9472   9034   -611    293    301       C  
ATOM   1509  NZ  LYS A 205      21.790   6.555   3.020  1.00 75.97           N  
ANISOU 1509  NZ  LYS A 205    10014   9573   9277   -640    302    344       N  
ATOM   1510  N   PHE A 206      25.182  11.897   6.500  1.00 34.24           N  
ANISOU 1510  N   PHE A 206     4561   4548   3900   -509     49    -88       N  
ATOM   1511  CA  PHE A 206      25.931  12.932   5.803  1.00 39.77           C  
ANISOU 1511  CA  PHE A 206     5232   5190   4688   -552      7   -155       C  
ATOM   1512  C   PHE A 206      27.116  13.484   6.582  1.00 41.61           C  
ANISOU 1512  C   PHE A 206     5426   5475   4911   -521    -62   -229       C  
ATOM   1513  O   PHE A 206      27.967  14.147   5.983  1.00 45.63           O  
ANISOU 1513  O   PHE A 206     5903   5936   5499   -560    -96   -268       O  
ATOM   1514  CB  PHE A 206      24.997  14.086   5.414  1.00 36.26           C  
ANISOU 1514  CB  PHE A 206     4789   4697   4290   -584      4   -209       C  
ATOM   1515  CG  PHE A 206      23.957  13.698   4.401  1.00 42.02           C  
ANISOU 1515  CG  PHE A 206     5551   5363   5052   -626     63   -145       C  
ATOM   1516  CD1 PHE A 206      24.224  13.786   3.045  1.00 30.63           C  
ANISOU 1516  CD1 PHE A 206     4111   3834   3695   -684     76   -122       C  
ATOM   1517  CD2 PHE A 206      22.719  13.222   4.806  1.00 43.69           C  
ANISOU 1517  CD2 PHE A 206     5787   5607   5206   -605    105   -106       C  
ATOM   1518  CE1 PHE A 206      23.272  13.421   2.110  1.00 32.41           C  
ANISOU 1518  CE1 PHE A 206     4364   4003   3946   -718    125    -70       C  
ATOM   1519  CE2 PHE A 206      21.762  12.857   3.875  1.00 36.08           C  
ANISOU 1519  CE2 PHE A 206     4848   4585   4277   -645    154    -52       C  
ATOM   1520  CZ  PHE A 206      22.040  12.956   2.526  1.00 36.20           C  
ANISOU 1520  CZ  PHE A 206     4867   4511   4374   -700    161    -37       C  
ATOM   1521  N   GLY A 207      27.197  13.238   7.880  1.00 32.95           N  
ANISOU 1521  N   GLY A 207     4325   4476   3719   -452    -83   -247       N  
ATOM   1522  CA  GLY A 207      28.402  13.545   8.618  1.00 34.48           C  
ANISOU 1522  CA  GLY A 207     4480   4725   3896   -418   -150   -309       C  
ATOM   1523  C   GLY A 207      28.207  14.693   9.597  1.00 41.60           C  
ANISOU 1523  C   GLY A 207     5362   5678   4768   -381   -210   -420       C  
ATOM   1524  O   GLY A 207      27.246  15.464   9.528  1.00 37.27           O  
ANISOU 1524  O   GLY A 207     4824   5103   4232   -392   -206   -461       O  
ATOM   1525  N   GLU A 208      29.161  14.794  10.528  1.00 40.98           N  
ANISOU 1525  N   GLU A 208     5252   5674   4645   -331   -272   -475       N  
ATOM   1526  CA  GLU A 208      29.144  15.864  11.519  1.00 47.81           C  
ANISOU 1526  CA  GLU A 208     6095   6592   5478   -287   -343   -595       C  
ATOM   1527  C   GLU A 208      29.267  17.232  10.860  1.00 40.86           C  
ANISOU 1527  C   GLU A 208     5190   5616   4718   -349   -391   -681       C  
ATOM   1528  O   GLU A 208      28.651  18.206  11.312  1.00 37.07           O  
ANISOU 1528  O   GLU A 208     4712   5141   4234   -330   -426   -769       O  
ATOM   1529  CB  GLU A 208      30.279  15.650  12.521  1.00 56.01           C  
ANISOU 1529  CB  GLU A 208     7100   7723   6456   -226   -406   -635       C  
ATOM   1530  CG  GLU A 208      30.074  16.310  13.871  1.00 63.66           C  
ANISOU 1530  CG  GLU A 208     8060   8792   7337   -145   -467   -739       C  
ATOM   1531  CD  GLU A 208      31.222  16.039  14.825  1.00 73.01           C  
ANISOU 1531  CD  GLU A 208     9211  10072   8458    -82   -531   -776       C  
ATOM   1532  OE1 GLU A 208      32.336  16.546  14.577  1.00 76.05           O  
ANISOU 1532  OE1 GLU A 208     9550  10421   8924   -116   -596   -835       O  
ATOM   1533  OE2 GLU A 208      31.011  15.315  15.821  1.00 76.41           O  
ANISOU 1533  OE2 GLU A 208     9658  10617   8758      2   -516   -743       O  
ATOM   1534  N   ARG A 209      30.062  17.323   9.792  1.00 39.67           N  
ANISOU 1534  N   ARG A 209     5016   5381   4676   -422   -392   -656       N  
ATOM   1535  CA  ARG A 209      30.260  18.597   9.106  1.00 44.41           C  
ANISOU 1535  CA  ARG A 209     5591   5885   5400   -488   -435   -723       C  
ATOM   1536  C   ARG A 209      28.945  19.151   8.570  1.00 38.77           C  
ANISOU 1536  C   ARG A 209     4911   5105   4714   -515   -398   -722       C  
ATOM   1537  O   ARG A 209      28.718  20.366   8.595  1.00 38.07           O  
ANISOU 1537  O   ARG A 209     4812   4969   4684   -531   -449   -809       O  
ATOM   1538  CB  ARG A 209      31.274  18.415   7.976  1.00 41.35           C  
ANISOU 1538  CB  ARG A 209     5172   5429   5111   -560   -424   -669       C  
ATOM   1539  CG  ARG A 209      31.677  19.684   7.249  1.00 51.25           C  
ANISOU 1539  CG  ARG A 209     6389   6586   6500   -634   -470   -723       C  
ATOM   1540  CD  ARG A 209      32.756  19.373   6.221  1.00 51.56           C  
ANISOU 1540  CD  ARG A 209     6390   6583   6619   -694   -452   -658       C  
ATOM   1541  NE  ARG A 209      33.176  20.552   5.470  1.00 55.09           N  
ANISOU 1541  NE  ARG A 209     6796   6937   7200   -770   -489   -691       N  
ATOM   1542  CZ  ARG A 209      32.644  20.929   4.312  1.00 56.14           C  
ANISOU 1542  CZ  ARG A 209     6946   6980   7406   -831   -446   -645       C  
ATOM   1543  NH1 ARG A 209      31.663  20.221   3.770  1.00 55.23           N  
ANISOU 1543  NH1 ARG A 209     6886   6856   7244   -824   -368   -572       N  
ATOM   1544  NH2 ARG A 209      33.091  22.016   3.698  1.00 51.16           N  
ANISOU 1544  NH2 ARG A 209     6274   6267   6898   -899   -482   -669       N  
ATOM   1545  N   ALA A 210      28.061  18.273   8.091  1.00 32.21           N  
ANISOU 1545  N   ALA A 210     4122   4270   3845   -518   -315   -627       N  
ATOM   1546  CA  ALA A 210      26.778  18.727   7.562  1.00 34.58           C  
ANISOU 1546  CA  ALA A 210     4454   4515   4170   -541   -278   -621       C  
ATOM   1547  C   ALA A 210      25.874  19.254   8.670  1.00 39.84           C  
ANISOU 1547  C   ALA A 210     5132   5248   4758   -474   -301   -696       C  
ATOM   1548  O   ALA A 210      25.229  20.297   8.508  1.00 39.76           O  
ANISOU 1548  O   ALA A 210     5125   5188   4793   -485   -323   -759       O  
ATOM   1549  CB  ALA A 210      26.091  17.592   6.804  1.00 30.92           C  
ANISOU 1549  CB  ALA A 210     4027   4034   3685   -561   -188   -503       C  
ATOM   1550  N   PHE A 211      25.809  18.546   9.801  1.00 39.39           N  
ANISOU 1550  N   PHE A 211     5081   5307   4581   -398   -296   -688       N  
ATOM   1551  CA  PHE A 211      24.970  18.997  10.907  1.00 39.32           C  
ANISOU 1551  CA  PHE A 211     5079   5379   4482   -323   -314   -757       C  
ATOM   1552  C   PHE A 211      25.474  20.313  11.483  1.00 38.80           C  
ANISOU 1552  C   PHE A 211     4983   5309   4449   -301   -413   -901       C  
ATOM   1553  O   PHE A 211      24.676  21.201  11.808  1.00 40.08           O  
ANISOU 1553  O   PHE A 211     5152   5471   4606   -272   -437   -980       O  
ATOM   1554  CB  PHE A 211      24.909  17.926  11.996  1.00 33.88           C  
ANISOU 1554  CB  PHE A 211     4398   4823   3653   -245   -286   -708       C  
ATOM   1555  CG  PHE A 211      24.073  18.315  13.186  1.00 42.75           C  
ANISOU 1555  CG  PHE A 211     5524   6051   4667   -158   -299   -772       C  
ATOM   1556  CD1 PHE A 211      22.715  18.049  13.209  1.00 42.09           C  
ANISOU 1556  CD1 PHE A 211     5464   5996   4534   -142   -231   -721       C  
ATOM   1557  CD2 PHE A 211      24.647  18.940  14.284  1.00 46.45           C  
ANISOU 1557  CD2 PHE A 211     5970   6597   5083    -88   -380   -885       C  
ATOM   1558  CE1 PHE A 211      21.942  18.402  14.300  1.00 47.13           C  
ANISOU 1558  CE1 PHE A 211     6100   6742   5065    -56   -238   -777       C  
ATOM   1559  CE2 PHE A 211      23.879  19.297  15.377  1.00 42.53           C  
ANISOU 1559  CE2 PHE A 211     5476   6208   4478      2   -392   -948       C  
ATOM   1560  CZ  PHE A 211      22.525  19.026  15.386  1.00 39.70           C  
ANISOU 1560  CZ  PHE A 211     5138   5881   4064     20   -318   -891       C  
ATOM   1561  N   LYS A 212      26.794  20.455  11.628  1.00 36.40           N  
ANISOU 1561  N   LYS A 212     4645   5002   4183   -312   -476   -940       N  
ATOM   1562  CA  LYS A 212      27.344  21.692  12.172  1.00 39.58           C  
ANISOU 1562  CA  LYS A 212     5016   5393   4630   -297   -580  -1080       C  
ATOM   1563  C   LYS A 212      27.068  22.868  11.245  1.00 37.44           C  
ANISOU 1563  C   LYS A 212     4742   4986   4495   -367   -604  -1125       C  
ATOM   1564  O   LYS A 212      26.777  23.977  11.709  1.00 37.69           O  
ANISOU 1564  O   LYS A 212     4770   5002   4549   -340   -671  -1240       O  
ATOM   1565  CB  LYS A 212      28.845  21.538  12.418  1.00 36.16           C  
ANISOU 1565  CB  LYS A 212     4539   4979   4220   -304   -640  -1103       C  
ATOM   1566  CG  LYS A 212      29.185  20.598  13.563  1.00 46.10           C  
ANISOU 1566  CG  LYS A 212     5797   6381   5338   -216   -640  -1087       C  
ATOM   1567  CD  LYS A 212      30.686  20.500  13.778  1.00 58.71           C  
ANISOU 1567  CD  LYS A 212     7346   7996   6964   -223   -705  -1115       C  
ATOM   1568  CE  LYS A 212      31.042  20.646  15.249  1.00 72.74           C  
ANISOU 1568  CE  LYS A 212     9106   9900   8633   -123   -781  -1213       C  
ATOM   1569  NZ  LYS A 212      32.295  19.918  15.595  1.00 78.15           N  
ANISOU 1569  NZ  LYS A 212     9757  10647   9288   -103   -808  -1188       N  
ATOM   1570  N   ALA A 213      27.145  22.642   9.931  1.00 34.53           N  
ANISOU 1570  N   ALA A 213     4379   4521   4219   -454   -552  -1034       N  
ATOM   1571  CA  ALA A 213      26.824  23.702   8.981  1.00 34.32           C  
ANISOU 1571  CA  ALA A 213     4353   4367   4319   -520   -566  -1058       C  
ATOM   1572  C   ALA A 213      25.370  24.136   9.115  1.00 34.25           C  
ANISOU 1572  C   ALA A 213     4382   4357   4276   -484   -542  -1085       C  
ATOM   1573  O   ALA A 213      25.067  25.334   9.078  1.00 35.58           O  
ANISOU 1573  O   ALA A 213     4548   4458   4512   -490   -597  -1173       O  
ATOM   1574  CB  ALA A 213      27.121  23.238   7.555  1.00 35.48           C  
ANISOU 1574  CB  ALA A 213     4501   4431   4550   -608   -504   -943       C  
ATOM   1575  N   TRP A 214      24.455  23.176   9.275  1.00 39.89           N  
ANISOU 1575  N   TRP A 214     5127   5142   4887   -447   -462  -1010       N  
ATOM   1576  CA  TRP A 214      23.057  23.528   9.499  1.00 34.12           C  
ANISOU 1576  CA  TRP A 214     4423   4429   4111   -405   -437  -1035       C  
ATOM   1577  C   TRP A 214      22.888  24.288  10.808  1.00 34.91           C  
ANISOU 1577  C   TRP A 214     4514   4604   4145   -316   -509  -1167       C  
ATOM   1578  O   TRP A 214      22.093  25.231  10.890  1.00 35.24           O  
ANISOU 1578  O   TRP A 214     4566   4616   4207   -293   -535  -1243       O  
ATOM   1579  CB  TRP A 214      22.184  22.272   9.496  1.00 33.76           C  
ANISOU 1579  CB  TRP A 214     4404   4454   3968   -385   -340   -923       C  
ATOM   1580  CG  TRP A 214      20.735  22.561   9.766  1.00 37.97           C  
ANISOU 1580  CG  TRP A 214     4957   5021   4450   -340   -309   -941       C  
ATOM   1581  CD1 TRP A 214      19.756  22.775   8.841  1.00 38.91           C  
ANISOU 1581  CD1 TRP A 214     5093   5068   4622   -380   -264   -903       C  
ATOM   1582  CD2 TRP A 214      20.106  22.679  11.050  1.00 42.95           C  
ANISOU 1582  CD2 TRP A 214     5586   5772   4962   -242   -320  -1003       C  
ATOM   1583  NE1 TRP A 214      18.557  23.018   9.467  1.00 37.81           N  
ANISOU 1583  NE1 TRP A 214     4962   4996   4409   -315   -247   -937       N  
ATOM   1584  CE2 TRP A 214      18.745  22.965  10.823  1.00 35.33           C  
ANISOU 1584  CE2 TRP A 214     4635   4802   3986   -229   -278   -998       C  
ATOM   1585  CE3 TRP A 214      20.562  22.571  12.368  1.00 47.78           C  
ANISOU 1585  CE3 TRP A 214     6183   6503   5469   -159   -361  -1063       C  
ATOM   1586  CZ2 TRP A 214      17.836  23.141  11.864  1.00 50.66           C  
ANISOU 1586  CZ2 TRP A 214     6574   6856   5818   -136   -273  -1048       C  
ATOM   1587  CZ3 TRP A 214      19.658  22.749  13.400  1.00 50.82           C  
ANISOU 1587  CZ3 TRP A 214     6569   7001   5741    -65   -357  -1113       C  
ATOM   1588  CH2 TRP A 214      18.311  23.030  13.142  1.00 44.99           C  
ANISOU 1588  CH2 TRP A 214     5843   6257   4995    -54   -311  -1104       C  
ATOM   1589  N   ALA A 215      23.626  23.887  11.846  1.00 35.54           N  
ANISOU 1589  N   ALA A 215     4577   4786   4142   -260   -545  -1200       N  
ATOM   1590  CA  ALA A 215      23.515  24.563  13.134  1.00 40.43           C  
ANISOU 1590  CA  ALA A 215     5187   5489   4685   -165   -617  -1331       C  
ATOM   1591  C   ALA A 215      24.045  25.989  13.058  1.00 46.99           C  
ANISOU 1591  C   ALA A 215     5998   6223   5634   -187   -725  -1464       C  
ATOM   1592  O   ALA A 215      23.436  26.911  13.613  1.00 42.64           O  
ANISOU 1592  O   ALA A 215     5452   5679   5069   -129   -775  -1577       O  
ATOM   1593  CB  ALA A 215      24.254  23.769  14.210  1.00 37.25           C  
ANISOU 1593  CB  ALA A 215     4768   5219   4166    -99   -633  -1330       C  
ATOM   1594  N   VAL A 216      25.172  26.190  12.369  1.00 42.62           N  
ANISOU 1594  N   VAL A 216     5418   5575   5200   -270   -761  -1452       N  
ATOM   1595  CA  VAL A 216      25.755  27.526  12.251  1.00 47.29           C  
ANISOU 1595  CA  VAL A 216     5986   6063   5921   -304   -865  -1568       C  
ATOM   1596  C   VAL A 216      24.760  28.485  11.608  1.00 45.53           C  
ANISOU 1596  C   VAL A 216     5787   5734   5779   -326   -864  -1595       C  
ATOM   1597  O   VAL A 216      24.552  29.606  12.086  1.00 47.13           O  
ANISOU 1597  O   VAL A 216     5989   5902   6016   -289   -947  -1726       O  
ATOM   1598  CB  VAL A 216      27.075  27.468  11.461  1.00 46.94           C  
ANISOU 1598  CB  VAL A 216     5903   5936   5997   -401   -885  -1520       C  
ATOM   1599  CG1 VAL A 216      27.491  28.861  11.015  1.00 47.91           C  
ANISOU 1599  CG1 VAL A 216     6002   5919   6281   -462   -974  -1605       C  
ATOM   1600  CG2 VAL A 216      28.171  26.826  12.299  1.00 46.70           C  
ANISOU 1600  CG2 VAL A 216     5839   6008   5897   -364   -921  -1536       C  
ATOM   1601  N   ALA A 217      24.122  28.052  10.519  1.00 36.83           N  
ANISOU 1601  N   ALA A 217     4709   4578   4708   -383   -773  -1477       N  
ATOM   1602  CA  ALA A 217      23.153  28.908   9.841  1.00 40.72           C  
ANISOU 1602  CA  ALA A 217     5225   4972   5274   -404   -767  -1492       C  
ATOM   1603  C   ALA A 217      21.928  29.152  10.714  1.00 40.76           C  
ANISOU 1603  C   ALA A 217     5254   5059   5173   -301   -765  -1565       C  
ATOM   1604  O   ALA A 217      21.441  30.285  10.816  1.00 44.92           O  
ANISOU 1604  O   ALA A 217     5789   5526   5752   -277   -823  -1665       O  
ATOM   1605  CB  ALA A 217      22.748  28.286   8.504  1.00 39.31           C  
ANISOU 1605  CB  ALA A 217     5065   4733   5137   -480   -669  -1347       C  
ATOM   1606  N   ARG A 218      21.416  28.096  11.352  1.00 38.80           N  
ANISOU 1606  N   ARG A 218     5016   4950   4776   -239   -697  -1512       N  
ATOM   1607  CA  ARG A 218      20.232  28.226  12.197  1.00 40.76           C  
ANISOU 1607  CA  ARG A 218     5281   5297   4911   -138   -683  -1567       C  
ATOM   1608  C   ARG A 218      20.470  29.194  13.349  1.00 38.64           C  
ANISOU 1608  C   ARG A 218     4999   5068   4614    -52   -791  -1737       C  
ATOM   1609  O   ARG A 218      19.614  30.034  13.652  1.00 42.37           O  
ANISOU 1609  O   ARG A 218     5484   5537   5078      8   -821  -1828       O  
ATOM   1610  CB  ARG A 218      19.825  26.853  12.734  1.00 44.98           C  
ANISOU 1610  CB  ARG A 218     5819   5977   5293    -92   -593  -1469       C  
ATOM   1611  CG  ARG A 218      18.456  26.800  13.393  1.00 51.63           C  
ANISOU 1611  CG  ARG A 218     6673   6926   6019     -3   -549  -1484       C  
ATOM   1612  CD  ARG A 218      17.390  27.526  12.583  1.00 62.79           C  
ANISOU 1612  CD  ARG A 218     8103   8247   7508    -27   -531  -1491       C  
ATOM   1613  NE  ARG A 218      16.124  27.643  13.307  1.00 75.02           N  
ANISOU 1613  NE  ARG A 218     9654   9903   8947     70   -502  -1527       N  
ATOM   1614  CZ  ARG A 218      15.355  26.618  13.671  1.00 84.94           C  
ANISOU 1614  CZ  ARG A 218    10908  11282  10083    105   -411  -1434       C  
ATOM   1615  NH1 ARG A 218      15.697  25.371  13.373  1.00 88.41           N  
ANISOU 1615  NH1 ARG A 218    11348  11745  10499     53   -343  -1300       N  
ATOM   1616  NH2 ARG A 218      14.226  26.841  14.328  1.00 88.14           N  
ANISOU 1616  NH2 ARG A 218    11308  11786  10394    194   -389  -1473       N  
ATOM   1617  N   LEU A 219      21.629  29.091  14.004  1.00 41.68           N  
ANISOU 1617  N   LEU A 219     5359   5494   4982    -38   -855  -1786       N  
ATOM   1618  CA  LEU A 219      21.906  29.952  15.149  1.00 46.83           C  
ANISOU 1618  CA  LEU A 219     5999   6193   5600     50   -965  -1956       C  
ATOM   1619  C   LEU A 219      22.200  31.382  14.712  1.00 45.46           C  
ANISOU 1619  C   LEU A 219     5820   5860   5591      6  -1067  -2067       C  
ATOM   1620  O   LEU A 219      21.793  32.336  15.384  1.00 48.51           O  
ANISOU 1620  O   LEU A 219     6213   6251   5968     84  -1144  -2211       O  
ATOM   1621  CB  LEU A 219      23.071  29.390  15.962  1.00 41.11           C  
ANISOU 1621  CB  LEU A 219     5247   5562   4810     76  -1006  -1974       C  
ATOM   1622  CG  LEU A 219      22.916  27.967  16.505  1.00 51.83           C  
ANISOU 1622  CG  LEU A 219     6609   7078   6006    125   -916  -1864       C  
ATOM   1623  CD1 LEU A 219      23.999  27.663  17.528  1.00 59.03           C  
ANISOU 1623  CD1 LEU A 219     7493   8093   6842    179   -981  -1920       C  
ATOM   1624  CD2 LEU A 219      21.533  27.750  17.096  1.00 49.47           C  
ANISOU 1624  CD2 LEU A 219     6332   6895   5570    219   -854  -1858       C  
ATOM   1625  N   SER A 220      22.908  31.552  13.592  1.00 51.89           N  
ANISOU 1625  N   SER A 220     6623   6533   6559   -114  -1070  -2003       N  
ATOM   1626  CA  SER A 220      23.222  32.896  13.117  1.00 57.88           C  
ANISOU 1626  CA  SER A 220     7375   7129   7486   -166  -1164  -2092       C  
ATOM   1627  C   SER A 220      21.954  33.663  12.763  1.00 59.00           C  
ANISOU 1627  C   SER A 220     7551   7206   7659   -141  -1153  -2123       C  
ATOM   1628  O   SER A 220      21.875  34.880  12.971  1.00 58.74           O  
ANISOU 1628  O   SER A 220     7522   7089   7708   -118  -1251  -2253       O  
ATOM   1629  CB  SER A 220      24.162  32.823  11.915  1.00 53.59           C  
ANISOU 1629  CB  SER A 220     6809   6460   7091   -301  -1150  -1990       C  
ATOM   1630  OG  SER A 220      25.422  32.289  12.284  1.00 40.82           O  
ANISOU 1630  OG  SER A 220     5154   4894   5461   -321  -1179  -1982       O  
ATOM   1631  N   GLN A 221      20.951  32.968  12.223  1.00 52.58           N  
ANISOU 1631  N   GLN A 221     6763   6429   6786   -144  -1040  -2008       N  
ATOM   1632  CA  GLN A 221      19.656  33.598  11.988  1.00 51.48           C  
ANISOU 1632  CA  GLN A 221     6653   6254   6654   -105  -1024  -2037       C  
ATOM   1633  C   GLN A 221      18.982  33.970  13.300  1.00 50.10           C  
ANISOU 1633  C   GLN A 221     6484   6197   6356     35  -1068  -2174       C  
ATOM   1634  O   GLN A 221      18.332  35.017  13.400  1.00 56.53           O  
ANISOU 1634  O   GLN A 221     7314   6954   7212     82  -1123  -2279       O  
ATOM   1635  CB  GLN A 221      18.752  32.659  11.191  1.00 45.58           C  
ANISOU 1635  CB  GLN A 221     5924   5536   5858   -136   -892  -1883       C  
ATOM   1636  CG  GLN A 221      18.971  32.663   9.695  1.00 52.61           C  
ANISOU 1636  CG  GLN A 221     6820   6286   6885   -258   -853  -1768       C  
ATOM   1637  CD  GLN A 221      17.993  31.751   8.985  1.00 53.77           C  
ANISOU 1637  CD  GLN A 221     6985   6468   6976   -276   -732  -1633       C  
ATOM   1638  OE1 GLN A 221      17.676  30.666   9.474  1.00 50.35           O  
ANISOU 1638  OE1 GLN A 221     6551   6166   6413   -237   -664  -1575       O  
ATOM   1639  NE2 GLN A 221      17.501  32.188   7.831  1.00 52.82           N  
ANISOU 1639  NE2 GLN A 221     6881   6232   6956   -335   -709  -1581       N  
ATOM   1640  N   ARG A 222      19.131  33.121  14.317  1.00 50.28           N  
ANISOU 1640  N   ARG A 222     6495   6387   6223    107  -1044  -2175       N  
ATOM   1641  CA  ARG A 222      18.403  33.292  15.568  1.00 48.90           C  
ANISOU 1641  CA  ARG A 222     6324   6355   5901    249  -1065  -2284       C  
ATOM   1642  C   ARG A 222      19.049  34.342  16.462  1.00 60.04           C  
ANISOU 1642  C   ARG A 222     7724   7751   7338    313  -1208  -2474       C  
ATOM   1643  O   ARG A 222      18.350  35.172  17.053  1.00 58.12           O  
ANISOU 1643  O   ARG A 222     7491   7528   7063    410  -1262  -2605       O  
ATOM   1644  CB  ARG A 222      18.318  31.951  16.295  1.00 45.50           C  
ANISOU 1644  CB  ARG A 222     5884   6112   5292    301   -981  -2198       C  
ATOM   1645  CG  ARG A 222      17.363  31.934  17.468  1.00 57.62           C  
ANISOU 1645  CG  ARG A 222     7421   7817   6656    446   -969  -2269       C  
ATOM   1646  CD  ARG A 222      16.588  30.635  17.494  1.00 71.86           C  
ANISOU 1646  CD  ARG A 222     9223   9749   8330    458   -833  -2114       C  
ATOM   1647  NE  ARG A 222      15.643  30.559  16.386  1.00 86.02           N  
ANISOU 1647  NE  ARG A 222    11032  11460  10193    392   -753  -2015       N  
ATOM   1648  CZ  ARG A 222      14.770  29.573  16.215  1.00 88.89           C  
ANISOU 1648  CZ  ARG A 222    11395  11906  10474    389   -636  -1882       C  
ATOM   1649  NH1 ARG A 222      14.719  28.571  17.082  1.00 92.50           N  
ANISOU 1649  NH1 ARG A 222    11839  12529  10779    448   -582  -1824       N  
ATOM   1650  NH2 ARG A 222      13.946  29.592  15.177  1.00 87.75           N  
ANISOU 1650  NH2 ARG A 222    11261  11677  10402    329   -577  -1806       N  
ATOM   1651  N   PHE A 223      20.377  34.319  16.576  1.00 57.85           N  
ANISOU 1651  N   PHE A 223     7423   7440   7119    263  -1275  -2497       N  
ATOM   1652  CA  PHE A 223      21.125  35.248  17.419  1.00 50.73           C  
ANISOU 1652  CA  PHE A 223     6504   6520   6249    315  -1420  -2678       C  
ATOM   1653  C   PHE A 223      22.112  36.024  16.553  1.00 48.47           C  
ANISOU 1653  C   PHE A 223     6203   6035   6179    190  -1498  -2691       C  
ATOM   1654  O   PHE A 223      23.332  35.841  16.666  1.00 48.77           O  
ANISOU 1654  O   PHE A 223     6208   6063   6260    141  -1547  -2694       O  
ATOM   1655  CB  PHE A 223      21.853  34.507  18.538  1.00 55.71           C  
ANISOU 1655  CB  PHE A 223     7111   7317   6738    383  -1438  -2705       C  
ATOM   1656  CG  PHE A 223      21.011  33.472  19.227  1.00 51.85           C  
ANISOU 1656  CG  PHE A 223     6632   7026   6040    479  -1335  -2636       C  
ATOM   1657  CD1 PHE A 223      19.772  33.803  19.750  1.00 61.02           C  
ANISOU 1657  CD1 PHE A 223     7814   8270   7103    589  -1316  -2698       C  
ATOM   1658  CD2 PHE A 223      21.458  32.168  19.351  1.00 47.50           C  
ANISOU 1658  CD2 PHE A 223     6070   6582   5396    461  -1257  -2505       C  
ATOM   1659  CE1 PHE A 223      18.996  32.855  20.387  1.00 60.27           C  
ANISOU 1659  CE1 PHE A 223     7720   8361   6819    674  -1217  -2624       C  
ATOM   1660  CE2 PHE A 223      20.686  31.214  19.986  1.00 50.67           C  
ANISOU 1660  CE2 PHE A 223     6478   7160   5613    545  -1161  -2431       C  
ATOM   1661  CZ  PHE A 223      19.453  31.558  20.504  1.00 55.45           C  
ANISOU 1661  CZ  PHE A 223     7099   7849   6122    649  -1140  -2488       C  
ATOM   1662  N   PRO A 224      21.618  36.909  15.682  1.00 45.62           N  
ANISOU 1662  N   PRO A 224     5861   5515   5957    138  -1513  -2697       N  
ATOM   1663  CA  PRO A 224      22.527  37.634  14.783  1.00 60.13           C  
ANISOU 1663  CA  PRO A 224     7681   7160   8006     13  -1578  -2688       C  
ATOM   1664  C   PRO A 224      23.356  38.695  15.485  1.00 63.93           C  
ANISOU 1664  C   PRO A 224     8140   7576   8575     34  -1740  -2868       C  
ATOM   1665  O   PRO A 224      24.278  39.241  14.867  1.00 61.38           O  
ANISOU 1665  O   PRO A 224     7791   7105   8425    -73  -1801  -2861       O  
ATOM   1666  CB  PRO A 224      21.576  38.254  13.757  1.00 56.60           C  
ANISOU 1666  CB  PRO A 224     7266   6580   7659    -27  -1542  -2642       C  
ATOM   1667  CG  PRO A 224      20.314  38.476  14.521  1.00 55.52           C  
ANISOU 1667  CG  PRO A 224     7159   6541   7395    109  -1536  -2733       C  
ATOM   1668  CD  PRO A 224      20.228  37.384  15.561  1.00 45.63           C  
ANISOU 1668  CD  PRO A 224     5898   5507   5934    201  -1482  -2723       C  
ATOM   1669  N   LYS A 225      23.055  39.007  16.747  1.00 73.75           N  
ANISOU 1669  N   LYS A 225     9390   8927   9705    170  -1811  -3028       N  
ATOM   1670  CA  LYS A 225      23.898  39.913  17.517  1.00 81.07           C  
ANISOU 1670  CA  LYS A 225    10294   9809  10700    200  -1972  -3209       C  
ATOM   1671  C   LYS A 225      25.089  39.190  18.128  1.00 82.83           C  
ANISOU 1671  C   LYS A 225    10474  10137  10862    192  -1997  -3207       C  
ATOM   1672  O   LYS A 225      26.148  39.798  18.317  1.00 87.97           O  
ANISOU 1672  O   LYS A 225    11089  10707  11628    151  -2117  -3299       O  
ATOM   1673  CB  LYS A 225      23.079  40.590  18.614  1.00 88.85           C  
ANISOU 1673  CB  LYS A 225    11304  10868  11585    359  -2046  -3394       C  
ATOM   1674  CG  LYS A 225      21.848  41.314  18.103  1.00 95.34           C  
ANISOU 1674  CG  LYS A 225    12168  11601  12456    384  -2025  -3409       C  
ATOM   1675  CD  LYS A 225      22.229  42.484  17.214  1.00 99.93           C  
ANISOU 1675  CD  LYS A 225    12746  11945  13277    277  -2087  -3394       C  
ATOM   1676  CE  LYS A 225      21.035  43.386  16.959  1.00102.08           C  
ANISOU 1676  CE  LYS A 225    13058  12140  13589    331  -2083  -3424       C  
ATOM   1677  NZ  LYS A 225      21.458  44.744  16.524  1.00104.08           N  
ANISOU 1677  NZ  LYS A 225    13304  12193  14049    270  -2164  -3433       N  
ATOM   1678  N   ALA A 226      24.931  37.907  18.450  1.00 76.85           N  
ANISOU 1678  N   ALA A 226     9716   9554   9928    233  -1888  -3102       N  
ATOM   1679  CA  ALA A 226      26.060  37.109  18.898  1.00 72.74           C  
ANISOU 1679  CA  ALA A 226     9157   9130   9352    219  -1897  -3072       C  
ATOM   1680  C   ALA A 226      27.085  36.999  17.781  1.00 78.17           C  
ANISOU 1680  C   ALA A 226     9810   9680  10210     58  -1885  -2957       C  
ATOM   1681  O   ALA A 226      26.738  36.845  16.607  1.00 83.99           O  
ANISOU 1681  O   ALA A 226    10561  10322  11029    -35  -1796  -2819       O  
ATOM   1682  CB  ALA A 226      25.598  35.716  19.329  1.00 65.86           C  
ANISOU 1682  CB  ALA A 226     8298   8458   8269    287  -1771  -2958       C  
ATOM   1683  N   GLU A 227      28.350  37.061  18.224  1.00 78.10           N  
ANISOU 1683  N   GLU A 227     9753   9669  10254     28  -1976  -3014       N  
ATOM   1684  CA  GLU A 227      29.590  37.040  17.406  1.00 81.45           C  
ANISOU 1684  CA  GLU A 227    10133   9968  10847   -121  -1978  -2920       C  
ATOM   1685  C   GLU A 227      29.969  35.615  16.984  1.00 75.20           C  
ANISOU 1685  C   GLU A 227     9327   9282   9963   -155  -1859  -2749       C  
ATOM   1686  O   GLU A 227      29.504  34.667  17.574  1.00 75.30           O  
ANISOU 1686  O   GLU A 227     9367   9448   9794    -72  -1773  -2695       O  
ATOM   1687  CB  GLU A 227      30.776  37.639  18.172  1.00 93.26           C  
ANISOU 1687  CB  GLU A 227    11576  11398  12459   -143  -2139  -3067       C  
ATOM   1688  CG  GLU A 227      30.513  38.972  18.860  1.00106.06           C  
ANISOU 1688  CG  GLU A 227    13168  13192  13936    -54  -2186  -3138       C  
ATOM   1689  CD  GLU A 227      31.384  40.151  18.441  1.00123.82           C  
ANISOU 1689  CD  GLU A 227    15346  15389  16313   -135  -2285  -3174       C  
ATOM   1690  OE1 GLU A 227      30.861  41.274  18.405  1.00129.64           O  
ANISOU 1690  OE1 GLU A 227    16054  15945  17258   -252  -2339  -3173       O  
ATOM   1691  OE2 GLU A 227      32.579  39.951  18.183  1.00136.62           O  
ANISOU 1691  OE2 GLU A 227    16935  17149  17825    -85  -2306  -3193       O  
ATOM   1692  N   PHE A 228      30.895  35.503  16.046  1.00 71.42           N  
ANISOU 1692  N   PHE A 228     8802   8722   9612   -277  -1855  -2661       N  
ATOM   1693  CA  PHE A 228      31.280  34.195  15.530  1.00 66.56           C  
ANISOU 1693  CA  PHE A 228     8174   8180   8935   -320  -1738  -2489       C  
ATOM   1694  C   PHE A 228      31.849  33.264  16.596  1.00 73.50           C  
ANISOU 1694  C   PHE A 228     9034   9239   9654   -236  -1747  -2509       C  
ATOM   1695  O   PHE A 228      31.940  32.059  16.345  1.00 77.29           O  
ANISOU 1695  O   PHE A 228     9518   9802  10046   -242  -1642  -2372       O  
ATOM   1696  CB  PHE A 228      32.291  34.366  14.392  1.00 63.70           C  
ANISOU 1696  CB  PHE A 228     7762   7686   8754   -467  -1737  -2398       C  
ATOM   1697  CG  PHE A 228      32.616  33.089  13.669  1.00 62.83           C  
ANISOU 1697  CG  PHE A 228     7645   7631   8598   -516  -1613  -2218       C  
ATOM   1698  CD1 PHE A 228      31.660  32.452  12.895  1.00 49.48           C  
ANISOU 1698  CD1 PHE A 228     6004   5942   6856   -527  -1483  -2086       C  
ATOM   1699  CD2 PHE A 228      33.878  32.527  13.763  1.00 60.19           C  
ANISOU 1699  CD2 PHE A 228     7251   7347   8272   -549  -1631  -2186       C  
ATOM   1700  CE1 PHE A 228      31.957  31.276  12.229  1.00 55.73           C  
ANISOU 1700  CE1 PHE A 228     6791   6778   7607   -567  -1375  -1930       C  
ATOM   1701  CE2 PHE A 228      34.181  31.353  13.099  1.00 60.99           C  
ANISOU 1701  CE2 PHE A 228     7347   7497   8330   -586  -1520  -2027       C  
ATOM   1702  CZ  PHE A 228      33.220  30.727  12.332  1.00 59.24           C  
ANISOU 1702  CZ  PHE A 228     7179   7270   8059   -595  -1394  -1901       C  
ATOM   1703  N   ALA A 229      32.227  33.775  17.769  1.00 74.77           N  
ANISOU 1703  N   ALA A 229     9176   9460   9774   -154  -1870  -2676       N  
ATOM   1704  CA  ALA A 229      32.768  32.908  18.812  1.00 70.29           C  
ANISOU 1704  CA  ALA A 229     8590   9070   9048    -66  -1881  -2695       C  
ATOM   1705  C   ALA A 229      31.664  32.138  19.523  1.00 58.36           C  
ANISOU 1705  C   ALA A 229     7133   7719   7322     59  -1797  -2668       C  
ATOM   1706  O   ALA A 229      31.687  30.903  19.579  1.00 72.31           O  
ANISOU 1706  O   ALA A 229     8908   9598   8970     80  -1701  -2544       O  
ATOM   1707  CB  ALA A 229      33.576  33.726  19.822  1.00 74.99           C  
ANISOU 1707  CB  ALA A 229     9142   9681   9671    -18  -2048  -2888       C  
ATOM   1708  N   GLU A 230      30.687  32.858  20.075  1.00 61.20           N  
ANISOU 1708  N   GLU A 230     7529   8090   7633    145  -1833  -2783       N  
ATOM   1709  CA  GLU A 230      29.639  32.206  20.850  1.00 68.01           C  
ANISOU 1709  CA  GLU A 230     8435   9117   8287    271  -1760  -2766       C  
ATOM   1710  C   GLU A 230      28.747  31.350  19.960  1.00 65.52           C  
ANISOU 1710  C   GLU A 230     8157   8795   7941    226  -1600  -2580       C  
ATOM   1711  O   GLU A 230      28.295  30.278  20.376  1.00 70.72           O  
ANISOU 1711  O   GLU A 230     8835   9597   8437    290  -1508  -2490       O  
ATOM   1712  CB  GLU A 230      28.817  33.251  21.600  1.00 72.70           C  
ANISOU 1712  CB  GLU A 230     9055   9723   8846    374  -1839  -2940       C  
ATOM   1713  CG  GLU A 230      28.029  32.688  22.767  1.00 82.46           C  
ANISOU 1713  CG  GLU A 230    10317  11167   9848    531  -1801  -2966       C  
ATOM   1714  CD  GLU A 230      28.770  32.815  24.083  1.00 94.89           C  
ANISOU 1714  CD  GLU A 230    11863  12870  11321    639  -1917  -3114       C  
ATOM   1715  OE1 GLU A 230      29.801  33.519  24.120  1.00 99.62           O  
ANISOU 1715  OE1 GLU A 230    12423  13382  12046    595  -2043  -3222       O  
ATOM   1716  OE2 GLU A 230      28.320  32.214  25.080  1.00100.05           O  
ANISOU 1716  OE2 GLU A 230    12530  13714  11770    768  -1883  -3119       O  
ATOM   1717  N   VAL A 231      28.482  31.806  18.734  1.00 62.59           N  
ANISOU 1717  N   VAL A 231     7796   8259   7727    117  -1567  -2520       N  
ATOM   1718  CA  VAL A 231      27.742  30.983  17.782  1.00 57.57           C  
ANISOU 1718  CA  VAL A 231     7191   7607   7076     63  -1422  -2343       C  
ATOM   1719  C   VAL A 231      28.499  29.689  17.510  1.00 59.72           C  
ANISOU 1719  C   VAL A 231     7444   7938   7306     21  -1349  -2199       C  
ATOM   1720  O   VAL A 231      27.927  28.593  17.550  1.00 58.22           O  
ANISOU 1720  O   VAL A 231     7281   7846   6996     52  -1241  -2082       O  
ATOM   1721  CB  VAL A 231      27.473  31.768  16.485  1.00 45.98           C  
ANISOU 1721  CB  VAL A 231     5731   5947   5791    -48  -1413  -2309       C  
ATOM   1722  CG1 VAL A 231      26.922  30.844  15.409  1.00 42.38           C  
ANISOU 1722  CG1 VAL A 231     5300   5471   5331   -113  -1270  -2123       C  
ATOM   1723  CG2 VAL A 231      26.509  32.912  16.752  1.00 47.60           C  
ANISOU 1723  CG2 VAL A 231     5965   6103   6018      9  -1467  -2436       C  
ATOM   1724  N   SER A 232      29.804  29.797  17.244  1.00 66.98           N  
ANISOU 1724  N   SER A 232     8317   8801   8331    -51  -1409  -2206       N  
ATOM   1725  CA  SER A 232      30.625  28.602  17.076  1.00 65.56           C  
ANISOU 1725  CA  SER A 232     8116   8686   8110    -79  -1353  -2085       C  
ATOM   1726  C   SER A 232      30.680  27.777  18.354  1.00 60.04           C  
ANISOU 1726  C   SER A 232     7421   8175   7218     42  -1353  -2103       C  
ATOM   1727  O   SER A 232      30.776  26.546  18.294  1.00 54.61           O  
ANISOU 1727  O   SER A 232     6740   7566   6443     49  -1266  -1974       O  
ATOM   1728  CB  SER A 232      32.038  28.991  16.636  1.00 59.78           C  
ANISOU 1728  CB  SER A 232     7322   7865   7526   -170  -1429  -2106       C  
ATOM   1729  OG  SER A 232      32.779  27.857  16.227  1.00 62.33           O  
ANISOU 1729  OG  SER A 232     7626   8229   7829   -209  -1363  -1975       O  
ATOM   1730  N   LYS A 233      30.622  28.433  19.515  1.00 60.21           N  
ANISOU 1730  N   LYS A 233     7437   8271   7169    142  -1450  -2260       N  
ATOM   1731  CA  LYS A 233      30.610  27.703  20.779  1.00 57.91           C  
ANISOU 1731  CA  LYS A 233     7150   8171   6682    269  -1450  -2279       C  
ATOM   1732  C   LYS A 233      29.304  26.938  20.956  1.00 57.24           C  
ANISOU 1732  C   LYS A 233     7116   8182   6452    332  -1330  -2181       C  
ATOM   1733  O   LYS A 233      29.310  25.755  21.317  1.00 60.29           O  
ANISOU 1733  O   LYS A 233     7510   8687   6710    375  -1257  -2074       O  
ATOM   1734  CB  LYS A 233      30.833  28.670  21.945  1.00 62.35           C  
ANISOU 1734  CB  LYS A 233     7694   8789   7206    365  -1590  -2482       C  
ATOM   1735  CG  LYS A 233      31.476  28.035  23.171  1.00 68.53           C  
ANISOU 1735  CG  LYS A 233     8457   9751   7830    472  -1631  -2519       C  
ATOM   1736  CD  LYS A 233      30.439  27.401  24.086  1.00 70.53           C  
ANISOU 1736  CD  LYS A 233     8750  10179   7868    604  -1562  -2491       C  
ATOM   1737  CE  LYS A 233      31.033  27.057  25.443  1.00 74.54           C  
ANISOU 1737  CE  LYS A 233     9238  10869   8216    729  -1629  -2564       C  
ATOM   1738  NZ  LYS A 233      30.455  25.803  26.000  1.00 72.69           N  
ANISOU 1738  NZ  LYS A 233     9031  10802   7785    813  -1517  -2432       N  
ATOM   1739  N   LEU A 234      28.171  27.600  20.707  1.00 53.21           N  
ANISOU 1739  N   LEU A 234     6636   7619   5962    340  -1308  -2215       N  
ATOM   1740  CA  LEU A 234      26.880  26.939  20.863  1.00 55.31           C  
ANISOU 1740  CA  LEU A 234     6942   7975   6098    397  -1196  -2125       C  
ATOM   1741  C   LEU A 234      26.688  25.829  19.838  1.00 54.82           C  
ANISOU 1741  C   LEU A 234     6896   7872   6062    309  -1067  -1927       C  
ATOM   1742  O   LEU A 234      25.984  24.851  20.114  1.00 52.20           O  
ANISOU 1742  O   LEU A 234     6586   7644   5602    355   -971  -1821       O  
ATOM   1743  CB  LEU A 234      25.749  27.963  20.758  1.00 55.44           C  
ANISOU 1743  CB  LEU A 234     6982   7937   6145    421  -1207  -2211       C  
ATOM   1744  CG  LEU A 234      25.736  29.082  21.802  1.00 46.36           C  
ANISOU 1744  CG  LEU A 234     5823   6831   4959    525  -1332  -2416       C  
ATOM   1745  CD1 LEU A 234      24.694  30.133  21.456  1.00 46.46           C  
ANISOU 1745  CD1 LEU A 234     5861   6754   5039    530  -1345  -2493       C  
ATOM   1746  CD2 LEU A 234      25.495  28.525  23.193  1.00 49.33           C  
ANISOU 1746  CD2 LEU A 234     6201   7424   5117    672  -1327  -2447       C  
ATOM   1747  N   VAL A 235      27.300  25.957  18.659  1.00 52.07           N  
ANISOU 1747  N   VAL A 235     6535   7373   5875    185  -1065  -1875       N  
ATOM   1748  CA  VAL A 235      27.188  24.912  17.644  1.00 51.93           C  
ANISOU 1748  CA  VAL A 235     6532   7313   5885    105   -952  -1698       C  
ATOM   1749  C   VAL A 235      27.874  23.636  18.117  1.00 48.57           C  
ANISOU 1749  C   VAL A 235     6098   7000   5358    136   -917  -1609       C  
ATOM   1750  O   VAL A 235      27.323  22.535  18.001  1.00 54.11           O  
ANISOU 1750  O   VAL A 235     6825   7755   5979    145   -816  -1476       O  
ATOM   1751  CB  VAL A 235      27.769  25.401  16.304  1.00 46.41           C  
ANISOU 1751  CB  VAL A 235     5817   6438   5377    -26   -963  -1672       C  
ATOM   1752  CG1 VAL A 235      28.115  24.219  15.407  1.00 45.14           C  
ANISOU 1752  CG1 VAL A 235     5660   6256   5237    -97   -870  -1506       C  
ATOM   1753  CG2 VAL A 235      26.789  26.327  15.608  1.00 49.61           C  
ANISOU 1753  CG2 VAL A 235     6246   6732   5871    -63   -954  -1700       C  
ATOM   1754  N   THR A 236      29.087  23.768  18.662  1.00 54.13           N  
ANISOU 1754  N   THR A 236     6764   7738   6066    154  -1006  -1680       N  
ATOM   1755  CA  THR A 236      29.838  22.596  19.102  1.00 55.86           C  
ANISOU 1755  CA  THR A 236     6972   8059   6195    187   -983  -1599       C  
ATOM   1756  C   THR A 236      29.094  21.837  20.195  1.00 56.12           C  
ANISOU 1756  C   THR A 236     7032   8259   6033    304   -934  -1563       C  
ATOM   1757  O   THR A 236      29.019  20.603  20.163  1.00 53.46           O  
ANISOU 1757  O   THR A 236     6711   7978   5623    311   -850  -1424       O  
ATOM   1758  CB  THR A 236      31.223  23.015  19.593  1.00 62.19           C  
ANISOU 1758  CB  THR A 236     7721   8875   7032    196  -1099  -1703       C  
ATOM   1759  OG1 THR A 236      31.842  23.861  18.616  1.00 68.71           O  
ANISOU 1759  OG1 THR A 236     8516   9544   8045     85  -1148  -1741       O  
ATOM   1760  CG2 THR A 236      32.099  21.793  19.828  1.00 53.27           C  
ANISOU 1760  CG2 THR A 236     6578   7829   5834    215  -1073  -1607       C  
ATOM   1761  N   ASP A 237      28.537  22.558  21.170  1.00 54.72           N  
ANISOU 1761  N   ASP A 237     6858   8163   5770    399   -986  -1685       N  
ATOM   1762  CA  ASP A 237      27.763  21.907  22.222  1.00 45.99           C  
ANISOU 1762  CA  ASP A 237     5774   7228   4474    515   -935  -1649       C  
ATOM   1763  C   ASP A 237      26.501  21.268  21.655  1.00 45.04           C  
ANISOU 1763  C   ASP A 237     5690   7094   4331    487   -806  -1510       C  
ATOM   1764  O   ASP A 237      26.179  20.117  21.973  1.00 42.53           O  
ANISOU 1764  O   ASP A 237     5388   6871   3903    522   -723  -1382       O  
ATOM   1765  CB  ASP A 237      27.414  22.916  23.318  1.00 50.93           C  
ANISOU 1765  CB  ASP A 237     6393   7942   5017    626  -1021  -1820       C  
ATOM   1766  CG  ASP A 237      28.645  23.517  23.972  1.00 63.81           C  
ANISOU 1766  CG  ASP A 237     7985   9596   6662    661  -1157  -1965       C  
ATOM   1767  OD1 ASP A 237      29.673  22.813  24.070  1.00 58.06           O  
ANISOU 1767  OD1 ASP A 237     7236   8900   5924    650  -1170  -1914       O  
ATOM   1768  OD2 ASP A 237      28.585  24.694  24.387  1.00 56.58           O  
ANISOU 1768  OD2 ASP A 237     7060   8666   5773    701  -1256  -2134       O  
ATOM   1769  N   LEU A 238      25.777  22.001  20.804  1.00 42.09           N  
ANISOU 1769  N   LEU A 238     5329   6599   4065    423   -790  -1532       N  
ATOM   1770  CA  LEU A 238      24.566  21.461  20.194  1.00 51.76           C  
ANISOU 1770  CA  LEU A 238     6584   7803   5281    390   -674  -1409       C  
ATOM   1771  C   LEU A 238      24.854  20.207  19.380  1.00 50.31           C  
ANISOU 1771  C   LEU A 238     6411   7573   5133    312   -589  -1238       C  
ATOM   1772  O   LEU A 238      24.015  19.300  19.319  1.00 55.41           O  
ANISOU 1772  O   LEU A 238     7078   8263   5713    317   -492  -1113       O  
ATOM   1773  CB  LEU A 238      23.907  22.522  19.313  1.00 48.12           C  
ANISOU 1773  CB  LEU A 238     6131   7205   4948    328   -684  -1468       C  
ATOM   1774  CG  LEU A 238      22.502  22.218  18.793  1.00 51.68           C  
ANISOU 1774  CG  LEU A 238     6608   7643   5386    310   -580  -1375       C  
ATOM   1775  CD1 LEU A 238      21.527  22.061  19.948  1.00 40.87           C  
ANISOU 1775  CD1 LEU A 238     5242   6441   3846    429   -549  -1388       C  
ATOM   1776  CD2 LEU A 238      22.040  23.308  17.839  1.00 55.01           C  
ANISOU 1776  CD2 LEU A 238     7037   7917   5949    243   -602  -1436       C  
ATOM   1777  N   THR A 239      26.029  20.134  18.751  1.00 45.39           N  
ANISOU 1777  N   THR A 239     5771   6862   4614    240   -627  -1231       N  
ATOM   1778  CA  THR A 239      26.368  18.957  17.958  1.00 45.37           C  
ANISOU 1778  CA  THR A 239     5779   6814   4647    173   -553  -1079       C  
ATOM   1779  C   THR A 239      26.554  17.729  18.841  1.00 43.31           C  
ANISOU 1779  C   THR A 239     5523   6689   4242    247   -516   -989       C  
ATOM   1780  O   THR A 239      26.116  16.629  18.484  1.00 49.75           O  
ANISOU 1780  O   THR A 239     6364   7506   5034    225   -426   -847       O  
ATOM   1781  CB  THR A 239      27.627  19.224  17.133  1.00 47.38           C  
ANISOU 1781  CB  THR A 239     6006   6956   5039     89   -605  -1099       C  
ATOM   1782  OG1 THR A 239      27.454  20.427  16.374  1.00 53.43           O  
ANISOU 1782  OG1 THR A 239     6766   7598   5938     23   -644  -1180       O  
ATOM   1783  CG2 THR A 239      27.894  18.070  16.179  1.00 37.39           C  
ANISOU 1783  CG2 THR A 239     4755   5635   3818     20   -527   -949       C  
ATOM   1784  N   LYS A 240      27.195  17.897  20.000  1.00 43.34           N  
ANISOU 1784  N   LYS A 240     5506   6809   4151    337   -588  -1071       N  
ATOM   1785  CA  LYS A 240      27.373  16.771  20.911  1.00 54.72           C  
ANISOU 1785  CA  LYS A 240     6953   8389   5448    417   -557   -986       C  
ATOM   1786  C   LYS A 240      26.045  16.311  21.499  1.00 55.93           C  
ANISOU 1786  C   LYS A 240     7131   8644   5475    480   -475   -913       C  
ATOM   1787  O   LYS A 240      25.869  15.115  21.763  1.00 47.13           O  
ANISOU 1787  O   LYS A 240     6032   7594   4279    503   -405   -776       O  
ATOM   1788  CB  LYS A 240      28.348  17.148  22.028  1.00 58.28           C  
ANISOU 1788  CB  LYS A 240     7373   8947   5824    505   -660  -1101       C  
ATOM   1789  CG  LYS A 240      28.737  15.990  22.932  1.00 63.02           C  
ANISOU 1789  CG  LYS A 240     7977   9686   6281    588   -638  -1011       C  
ATOM   1790  CD  LYS A 240      29.605  16.458  24.090  1.00 60.25           C  
ANISOU 1790  CD  LYS A 240     7594   9453   5844    686   -747  -1139       C  
ATOM   1791  CE  LYS A 240      29.870  15.327  25.071  1.00 58.87           C  
ANISOU 1791  CE  LYS A 240     7426   9432   5510    782   -722  -1046       C  
ATOM   1792  NZ  LYS A 240      30.363  15.832  26.382  1.00 65.35           N  
ANISOU 1792  NZ  LYS A 240     8222  10402   6208    903   -819  -1175       N  
ATOM   1793  N   VAL A 241      25.105  17.237  21.705  1.00 58.60           N  
ANISOU 1793  N   VAL A 241     7471   8997   5798    507   -483  -1000       N  
ATOM   1794  CA  VAL A 241      23.801  16.875  22.257  1.00 52.22           C  
ANISOU 1794  CA  VAL A 241     6678   8293   4870    568   -403   -934       C  
ATOM   1795  C   VAL A 241      23.090  15.887  21.341  1.00 47.01           C  
ANISOU 1795  C   VAL A 241     6042   7561   4260    486   -291   -765       C  
ATOM   1796  O   VAL A 241      22.664  14.808  21.771  1.00 47.32           O  
ANISOU 1796  O   VAL A 241     6091   7685   4203    518   -217   -634       O  
ATOM   1797  CB  VAL A 241      22.948  18.135  22.491  1.00 54.12           C  
ANISOU 1797  CB  VAL A 241     6913   8545   5106    606   -436  -1068       C  
ATOM   1798  CG1 VAL A 241      21.546  17.750  22.944  1.00 57.33           C  
ANISOU 1798  CG1 VAL A 241     7328   9057   5399    661   -344   -991       C  
ATOM   1799  CG2 VAL A 241      23.608  19.045  23.514  1.00 60.70           C  
ANISOU 1799  CG2 VAL A 241     7723   9461   5877    701   -551  -1240       C  
ATOM   1800  N   HIS A 242      22.957  16.236  20.061  1.00 42.38           N  
ANISOU 1800  N   HIS A 242     5463   6814   3825    379   -280   -764       N  
ATOM   1801  CA  HIS A 242      22.186  15.412  19.140  1.00 40.36           C  
ANISOU 1801  CA  HIS A 242     5229   6483   3621    302   -182   -621       C  
ATOM   1802  C   HIS A 242      22.955  14.195  18.645  1.00 37.94           C  
ANISOU 1802  C   HIS A 242     4935   6129   3350    252   -151   -497       C  
ATOM   1803  O   HIS A 242      22.328  13.215  18.228  1.00 40.51           O  
ANISOU 1803  O   HIS A 242     5280   6433   3678    216    -67   -361       O  
ATOM   1804  CB  HIS A 242      21.713  16.258  17.959  1.00 37.63           C  
ANISOU 1804  CB  HIS A 242     4888   5992   3416    215   -183   -668       C  
ATOM   1805  CG  HIS A 242      20.647  17.242  18.323  1.00 38.08           C  
ANISOU 1805  CG  HIS A 242     4939   6089   3439    261   -190   -757       C  
ATOM   1806  ND1 HIS A 242      19.311  16.907  18.374  1.00 43.88           N  
ANISOU 1806  ND1 HIS A 242     5681   6870   4122    273   -108   -683       N  
ATOM   1807  CD2 HIS A 242      20.721  18.547  18.675  1.00 46.45           C  
ANISOU 1807  CD2 HIS A 242     5986   7151   4511    301   -271   -916       C  
ATOM   1808  CE1 HIS A 242      18.607  17.966  18.732  1.00 43.96           C  
ANISOU 1808  CE1 HIS A 242     5681   6914   4109    323   -135   -793       C  
ATOM   1809  NE2 HIS A 242      19.439  18.974  18.921  1.00 46.89           N  
ANISOU 1809  NE2 HIS A 242     6042   7254   4518    342   -236   -937       N  
ATOM   1810  N   THR A 243      24.289  14.231  18.677  1.00 38.06           N  
ANISOU 1810  N   THR A 243     4938   6127   3395    251   -218   -542       N  
ATOM   1811  CA  THR A 243      25.052  13.020  18.398  1.00 39.23           C  
ANISOU 1811  CA  THR A 243     5096   6256   3555    227   -191   -427       C  
ATOM   1812  C   THR A 243      24.734  11.935  19.419  1.00 45.75           C  
ANISOU 1812  C   THR A 243     5933   7215   4236    306   -142   -320       C  
ATOM   1813  O   THR A 243      24.515  10.775  19.055  1.00 43.70           O  
ANISOU 1813  O   THR A 243     5696   6925   3982    275    -73   -178       O  
ATOM   1814  CB  THR A 243      26.552  13.325  18.387  1.00 50.98           C  
ANISOU 1814  CB  THR A 243     6559   7722   5089    225   -277   -505       C  
ATOM   1815  OG1 THR A 243      26.858  14.201  17.295  1.00 59.08           O  
ANISOU 1815  OG1 THR A 243     7573   8611   6262    137   -311   -576       O  
ATOM   1816  CG2 THR A 243      27.357  12.041  18.238  1.00 37.76           C  
ANISOU 1816  CG2 THR A 243     4893   6045   3408    219   -253   -390       C  
ATOM   1817  N   GLU A 244      24.677  12.302  20.701  1.00 39.58           N  
ANISOU 1817  N   GLU A 244     5136   6579   3323    410   -177   -383       N  
ATOM   1818  CA  GLU A 244      24.400  11.324  21.748  1.00 51.67           C  
ANISOU 1818  CA  GLU A 244     6675   8252   4706    494   -131   -278       C  
ATOM   1819  C   GLU A 244      22.980  10.775  21.638  1.00 41.11           C  
ANISOU 1819  C   GLU A 244     5353   6927   3339    477    -29   -159       C  
ATOM   1820  O   GLU A 244      22.770   9.557  21.692  1.00 40.24           O  
ANISOU 1820  O   GLU A 244     5259   6831   3198    472     37     -6       O  
ATOM   1821  CB  GLU A 244      24.632  11.955  23.121  1.00 50.37           C  
ANISOU 1821  CB  GLU A 244     6488   8249   4402    616   -196   -386       C  
ATOM   1822  CG  GLU A 244      26.078  11.910  23.589  1.00 51.09           C  
ANISOU 1822  CG  GLU A 244     6563   8378   4472    659   -281   -443       C  
ATOM   1823  CD  GLU A 244      26.434  13.071  24.497  1.00 52.64           C  
ANISOU 1823  CD  GLU A 244     6731   8667   4601    744   -380   -621       C  
ATOM   1824  OE1 GLU A 244      25.609  14.000  24.629  1.00 49.76           O  
ANISOU 1824  OE1 GLU A 244     6362   8317   4227    761   -387   -711       O  
ATOM   1825  OE2 GLU A 244      27.538  13.055  25.079  1.00 50.78           O  
ANISOU 1825  OE2 GLU A 244     6477   8491   4325    796   -455   -675       O  
ATOM   1826  N   CYS A 245      21.992  11.660  21.479  1.00 40.11           N  
ANISOU 1826  N   CYS A 245     5219   6792   3228    468    -17   -227       N  
ATOM   1827  CA  CYS A 245      20.597  11.227  21.428  1.00 46.21           C  
ANISOU 1827  CA  CYS A 245     5997   7591   3971    455     77   -123       C  
ATOM   1828  C   CYS A 245      20.336  10.318  20.232  1.00 45.28           C  
ANISOU 1828  C   CYS A 245     5902   7331   3970    345    141      6       C  
ATOM   1829  O   CYS A 245      19.722   9.252  20.367  1.00 42.26           O  
ANISOU 1829  O   CYS A 245     5529   6978   3550    339    217    154       O  
ATOM   1830  CB  CYS A 245      19.674  12.443  21.385  1.00 45.52           C  
ANISOU 1830  CB  CYS A 245     5895   7510   3891    465     67   -236       C  
ATOM   1831  SG  CYS A 245      18.974  12.916  22.989  1.00 53.96           S  
ANISOU 1831  SG  CYS A 245     6937   8801   4763    613     67   -291       S  
ATOM   1832  N   CYS A 246      20.782  10.734  19.043  1.00 43.96           N  
ANISOU 1832  N   CYS A 246     5744   7013   3948    258    110    -47       N  
ATOM   1833  CA  CYS A 246      20.575   9.924  17.846  1.00 43.86           C  
ANISOU 1833  CA  CYS A 246     5754   6865   4046    158    163     60       C  
ATOM   1834  C   CYS A 246      21.335   8.604  17.922  1.00 48.18           C  
ANISOU 1834  C   CYS A 246     6319   7407   4581    159    179    177       C  
ATOM   1835  O   CYS A 246      20.878   7.596  17.372  1.00 60.52           O  
ANISOU 1835  O   CYS A 246     7902   8908   6186    107    240    303       O  
ATOM   1836  CB  CYS A 246      21.000  10.705  16.600  1.00 48.69           C  
ANISOU 1836  CB  CYS A 246     6368   7329   4803     76    122    -28       C  
ATOM   1837  SG  CYS A 246      19.993  12.166  16.200  1.00 45.56           S  
ANISOU 1837  SG  CYS A 246     5959   6897   4455     55    110   -145       S  
ATOM   1838  N   HIS A 247      22.492   8.590  18.586  1.00 38.92           N  
ANISOU 1838  N   HIS A 247     5139   6295   3355    219    120    136       N  
ATOM   1839  CA  HIS A 247      23.262   7.370  18.805  1.00 45.48           C  
ANISOU 1839  CA  HIS A 247     5985   7136   4159    237    128    242       C  
ATOM   1840  C   HIS A 247      22.692   6.505  19.921  1.00 49.87           C  
ANISOU 1840  C   HIS A 247     6545   7822   4581    309    181    360       C  
ATOM   1841  O   HIS A 247      23.195   5.399  20.144  1.00 56.29           O  
ANISOU 1841  O   HIS A 247     7374   8643   5369    327    195    468       O  
ATOM   1842  CB  HIS A 247      24.716   7.723  19.128  1.00 46.57           C  
ANISOU 1842  CB  HIS A 247     6107   7299   4287    278     42    149       C  
ATOM   1843  CG  HIS A 247      25.694   6.629  18.832  1.00 65.73           C  
ANISOU 1843  CG  HIS A 247     8551   9680   6746    268     40    234       C  
ATOM   1844  ND1 HIS A 247      25.748   5.981  17.618  1.00 74.39           N  
ANISOU 1844  ND1 HIS A 247     9669  10636   7959    184     73    303       N  
ATOM   1845  CD2 HIS A 247      26.657   6.066  19.600  1.00 75.75           C  
ANISOU 1845  CD2 HIS A 247     9815  11026   7940    339      6    258       C  
ATOM   1846  CE1 HIS A 247      26.706   5.071  17.647  1.00 75.27           C  
ANISOU 1846  CE1 HIS A 247     9791  10739   8070    204     59    363       C  
ATOM   1847  NE2 HIS A 247      27.269   5.098  18.841  1.00 73.02           N  
ANISOU 1847  NE2 HIS A 247     9490  10584   7670    297     19    341       N  
ATOM   1848  N   GLY A 248      21.671   6.979  20.629  1.00 49.65           N  
ANISOU 1848  N   GLY A 248     6501   7899   4466    354    210    346       N  
ATOM   1849  CA  GLY A 248      21.073   6.223  21.709  1.00 51.70           C  
ANISOU 1849  CA  GLY A 248     6757   8295   4592    425    265    464       C  
ATOM   1850  C   GLY A 248      21.585   6.550  23.094  1.00 42.79           C  
ANISOU 1850  C   GLY A 248     5610   7339   3308    549    220    407       C  
ATOM   1851  O   GLY A 248      21.182   5.884  24.055  1.00 64.40           O  
ANISOU 1851  O   GLY A 248     8344  10205   5922    618    266    513       O  
ATOM   1852  N   ASP A 249      22.460   7.547  23.231  1.00 43.32           N  
ANISOU 1852  N   ASP A 249     5664   7418   3378    581    130    245       N  
ATOM   1853  CA  ASP A 249      22.988   7.950  24.535  1.00 50.68           C  
ANISOU 1853  CA  ASP A 249     6577   8516   4165    704     73    169       C  
ATOM   1854  C   ASP A 249      22.062   9.018  25.111  1.00 51.98           C  
ANISOU 1854  C   ASP A 249     6719   8779   4253    759     71     67       C  
ATOM   1855  O   ASP A 249      22.355  10.215  25.116  1.00 61.12           O  
ANISOU 1855  O   ASP A 249     7860   9929   5432    775     -5   -103       O  
ATOM   1856  CB  ASP A 249      24.422   8.444  24.402  1.00 52.04           C  
ANISOU 1856  CB  ASP A 249     6741   8647   4385    709    -30     45       C  
ATOM   1857  CG  ASP A 249      25.278   7.518  23.560  1.00 56.69           C  
ANISOU 1857  CG  ASP A 249     7349   9112   5078    639    -26    130       C  
ATOM   1858  OD1 ASP A 249      25.179   6.286  23.745  1.00 54.05           O  
ANISOU 1858  OD1 ASP A 249     7035   8795   4705    649     30    287       O  
ATOM   1859  OD2 ASP A 249      26.045   8.021  22.711  1.00 61.14           O  
ANISOU 1859  OD2 ASP A 249     7907   9561   5763    576    -80     43       O  
ATOM   1860  N   LEU A 250      20.919   8.555  25.621  1.00 52.58           N  
ANISOU 1860  N   LEU A 250     6790   8950   4238    791    155    176       N  
ATOM   1861  CA  LEU A 250      19.846   9.465  26.006  1.00 48.50           C  
ANISOU 1861  CA  LEU A 250     6250   8517   3662    834    172     99       C  
ATOM   1862  C   LEU A 250      20.154  10.204  27.303  1.00 46.88           C  
ANISOU 1862  C   LEU A 250     6023   8490   3299    972    108    -24       C  
ATOM   1863  O   LEU A 250      19.771  11.370  27.454  1.00 46.04           O  
ANISOU 1863  O   LEU A 250     5900   8412   3179   1007     68   -172       O  
ATOM   1864  CB  LEU A 250      18.532   8.693  26.140  1.00 53.92           C  
ANISOU 1864  CB  LEU A 250     6930   9256   4301    822    287    264       C  
ATOM   1865  CG  LEU A 250      17.646   8.540  24.900  1.00 58.62           C  
ANISOU 1865  CG  LEU A 250     7531   9698   5041    698    347    324       C  
ATOM   1866  CD1 LEU A 250      18.413   7.979  23.711  1.00 59.29           C  
ANISOU 1866  CD1 LEU A 250     7648   9593   5285    588    331    363       C  
ATOM   1867  CD2 LEU A 250      16.450   7.661  25.221  1.00 62.03           C  
ANISOU 1867  CD2 LEU A 250     7950  10204   5414    696    456    499       C  
ATOM   1868  N   LEU A 251      20.835   9.552  28.247  1.00 46.78           N  
ANISOU 1868  N   LEU A 251     6012   8598   3165   1057     94     31       N  
ATOM   1869  CA  LEU A 251      21.079  10.179  29.542  1.00 52.90           C  
ANISOU 1869  CA  LEU A 251     6766   9560   3773   1201     35    -80       C  
ATOM   1870  C   LEU A 251      22.072  11.329  29.423  1.00 55.08           C  
ANISOU 1870  C   LEU A 251     7036   9785   4109   1210    -93   -294       C  
ATOM   1871  O   LEU A 251      21.831  12.426  29.942  1.00 51.09           O  
ANISOU 1871  O   LEU A 251     6512   9354   3546   1282   -147   -451       O  
ATOM   1872  CB  LEU A 251      21.570   9.135  30.544  1.00 49.28           C  
ANISOU 1872  CB  LEU A 251     6311   9243   3171   1289     53     43       C  
ATOM   1873  CG  LEU A 251      20.616   7.964  30.786  1.00 56.16           C  
ANISOU 1873  CG  LEU A 251     7185  10177   3978   1285    177    267       C  
ATOM   1874  CD1 LEU A 251      21.330   6.838  31.514  1.00 62.60           C  
ANISOU 1874  CD1 LEU A 251     8011  11078   4694   1346    186    401       C  
ATOM   1875  CD2 LEU A 251      19.390   8.419  31.564  1.00 63.27           C  
ANISOU 1875  CD2 LEU A 251     8055  11241   4742   1367    231    260       C  
ATOM   1876  N   GLU A 252      23.199  11.097  28.744  1.00 53.21           N  
ANISOU 1876  N   GLU A 252     6811   9419   3990   1140   -143   -303       N  
ATOM   1877  CA  GLU A 252      24.163  12.172  28.529  1.00 55.70           C  
ANISOU 1877  CA  GLU A 252     7113   9668   4383   1131   -263   -494       C  
ATOM   1878  C   GLU A 252      23.573  13.282  27.673  1.00 63.69           C  
ANISOU 1878  C   GLU A 252     8123  10556   5523   1057   -277   -607       C  
ATOM   1879  O   GLU A 252      23.937  14.453  27.834  1.00 71.98           O  
ANISOU 1879  O   GLU A 252     9157  11598   6595   1084   -373   -788       O  
ATOM   1880  CB  GLU A 252      25.433  11.624  27.877  1.00 54.29           C  
ANISOU 1880  CB  GLU A 252     6942   9374   4312   1061   -301   -462       C  
ATOM   1881  CG  GLU A 252      25.972  10.352  28.512  1.00 60.15           C  
ANISOU 1881  CG  GLU A 252     7694  10208   4954   1118   -274   -320       C  
ATOM   1882  CD  GLU A 252      25.403   9.091  27.888  1.00 56.49           C  
ANISOU 1882  CD  GLU A 252     7257   9671   4534   1044   -162   -112       C  
ATOM   1883  OE1 GLU A 252      24.190   9.063  27.591  1.00 56.81           O  
ANISOU 1883  OE1 GLU A 252     7304   9693   4587   1007    -82    -51       O  
ATOM   1884  OE2 GLU A 252      26.170   8.126  27.695  1.00 54.45           O  
ANISOU 1884  OE2 GLU A 252     7013   9373   4302   1026   -157    -13       O  
ATOM   1885  N   CYS A 253      22.659  12.931  26.764  1.00 63.94           N  
ANISOU 1885  N   CYS A 253     8168  10485   5640    964   -188   -502       N  
ATOM   1886  CA  CYS A 253      22.062  13.915  25.866  1.00 58.64           C  
ANISOU 1886  CA  CYS A 253     7497   9689   5095    890   -196   -593       C  
ATOM   1887  C   CYS A 253      21.136  14.857  26.626  1.00 45.46           C  
ANISOU 1887  C   CYS A 253     5811   8135   3326    982   -206   -700       C  
ATOM   1888  O   CYS A 253      21.174  16.077  26.426  1.00 47.39           O  
ANISOU 1888  O   CYS A 253     6048   8324   3633    980   -279   -864       O  
ATOM   1889  CB  CYS A 253      21.313  13.201  24.739  1.00 60.37           C  
ANISOU 1889  CB  CYS A 253     7735   9783   5420    775    -97   -447       C  
ATOM   1890  SG  CYS A 253      20.121  14.210  23.826  1.00 61.58           S  
ANISOU 1890  SG  CYS A 253     7886   9829   5680    707    -74   -514       S  
ATOM   1891  N   ALA A 254      20.288  14.306  27.500  1.00 58.36           N  
ANISOU 1891  N   ALA A 254     7438   9931   4805   1065   -132   -608       N  
ATOM   1892  CA  ALA A 254      19.436  15.149  28.334  1.00 59.11           C  
ANISOU 1892  CA  ALA A 254     7514  10163   4783   1171   -140   -710       C  
ATOM   1893  C   ALA A 254      20.254  15.973  29.319  1.00 52.62           C  
ANISOU 1893  C   ALA A 254     6679   9444   3870   1286   -257   -888       C  
ATOM   1894  O   ALA A 254      19.886  17.111  29.629  1.00 49.14           O  
ANISOU 1894  O   ALA A 254     6227   9035   3408   1346   -313  -1049       O  
ATOM   1895  CB  ALA A 254      18.416  14.289  29.082  1.00 49.53           C  
ANISOU 1895  CB  ALA A 254     6289   9114   3416   1237    -29   -555       C  
ATOM   1896  N   ASP A 255      21.358  15.416  29.823  1.00 49.57           N  
ANISOU 1896  N   ASP A 255     6295   9110   3432   1322   -300   -867       N  
ATOM   1897  CA  ASP A 255      22.217  16.155  30.742  1.00 50.17           C  
ANISOU 1897  CA  ASP A 255     6356   9281   3427   1428   -421  -1039       C  
ATOM   1898  C   ASP A 255      22.899  17.322  30.038  1.00 58.53           C  
ANISOU 1898  C   ASP A 255     7411  10177   4650   1361   -532  -1219       C  
ATOM   1899  O   ASP A 255      22.889  18.455  30.535  1.00 55.54           O  
ANISOU 1899  O   ASP A 255     7021   9839   4244   1433   -621  -1403       O  
ATOM   1900  CB  ASP A 255      23.254  15.212  31.351  1.00 54.26           C  
ANISOU 1900  CB  ASP A 255     6874   9882   3861   1473   -438   -961       C  
ATOM   1901  CG  ASP A 255      23.758  15.688  32.697  1.00 61.93           C  
ANISOU 1901  CG  ASP A 255     7827  11038   4666   1629   -530  -1094       C  
ATOM   1902  OD1 ASP A 255      23.176  16.643  33.253  1.00 61.70           O  
ANISOU 1902  OD1 ASP A 255     7786  11093   4565   1714   -566  -1233       O  
ATOM   1903  OD2 ASP A 255      24.741  15.104  33.197  1.00 63.54           O  
ANISOU 1903  OD2 ASP A 255     8028  11305   4809   1671   -568  -1064       O  
ATOM   1904  N   ASP A 256      23.499  17.061  28.873  1.00 51.49           N  
ANISOU 1904  N   ASP A 256     6529   9101   3932   1225   -531  -1167       N  
ATOM   1905  CA  ASP A 256      24.170  18.122  28.129  1.00 55.44           C  
ANISOU 1905  CA  ASP A 256     7023   9441   4601   1150   -629  -1317       C  
ATOM   1906  C   ASP A 256      23.185  19.167  27.625  1.00 56.50           C  
ANISOU 1906  C   ASP A 256     7162   9496   4811   1121   -627  -1405       C  
ATOM   1907  O   ASP A 256      23.539  20.346  27.511  1.00 65.75           O  
ANISOU 1907  O   ASP A 256     8323  10595   6064   1117   -728  -1576       O  
ATOM   1908  CB  ASP A 256      24.958  17.526  26.961  1.00 56.38           C  
ANISOU 1908  CB  ASP A 256     7150   9394   4879   1014   -612  -1221       C  
ATOM   1909  CG  ASP A 256      26.166  16.733  27.419  1.00 63.15           C  
ANISOU 1909  CG  ASP A 256     7998  10311   5687   1043   -646  -1176       C  
ATOM   1910  OD1 ASP A 256      26.744  17.086  28.468  1.00 63.93           O  
ANISOU 1910  OD1 ASP A 256     8077  10532   5680   1148   -731  -1285       O  
ATOM   1911  OD2 ASP A 256      26.536  15.757  26.734  1.00 61.44           O  
ANISOU 1911  OD2 ASP A 256     7793  10019   5533    966   -591  -1036       O  
ATOM   1912  N   ARG A 257      21.951  18.759  27.319  1.00 52.14           N  
ANISOU 1912  N   ARG A 257     6621   8952   4237   1102   -515  -1291       N  
ATOM   1913  CA  ARG A 257      20.935  19.724  26.912  1.00 51.90           C  
ANISOU 1913  CA  ARG A 257     6593   8864   4264   1088   -510  -1372       C  
ATOM   1914  C   ARG A 257      20.587  20.668  28.056  1.00 51.51           C  
ANISOU 1914  C   ARG A 257     6529   8956   4086   1232   -576  -1537       C  
ATOM   1915  O   ARG A 257      20.338  21.859  27.833  1.00 48.47           O  
ANISOU 1915  O   ARG A 257     6143   8498   3775   1233   -642  -1687       O  
ATOM   1916  CB  ARG A 257      19.689  18.992  26.416  1.00 52.46           C  
ANISOU 1916  CB  ARG A 257     6673   8932   4328   1043   -375  -1207       C  
ATOM   1917  CG  ARG A 257      18.562  19.901  25.954  1.00 45.87           C  
ANISOU 1917  CG  ARG A 257     5838   8041   3549   1030   -359  -1274       C  
ATOM   1918  CD  ARG A 257      17.381  19.077  25.475  1.00 56.31           C  
ANISOU 1918  CD  ARG A 257     7163   9368   4865    981   -227  -1103       C  
ATOM   1919  NE  ARG A 257      16.337  19.890  24.861  1.00 61.70           N  
ANISOU 1919  NE  ARG A 257     7845   9978   5621    954   -210  -1156       N  
ATOM   1920  CZ  ARG A 257      15.179  20.182  25.443  1.00 62.63           C  
ANISOU 1920  CZ  ARG A 257     7945  10218   5634   1039   -168  -1174       C  
ATOM   1921  NH1 ARG A 257      14.913  19.728  26.661  1.00 65.20           N  
ANISOU 1921  NH1 ARG A 257     8252  10749   5774   1157   -135  -1139       N  
ATOM   1922  NH2 ARG A 257      14.286  20.928  24.807  1.00 64.59           N  
ANISOU 1922  NH2 ARG A 257     8192  10389   5961   1010   -158  -1223       N  
ATOM   1923  N   ALA A 258      20.567  20.156  29.289  1.00 59.65           N  
ANISOU 1923  N   ALA A 258     7550  10192   4923   1358   -563  -1512       N  
ATOM   1924  CA  ALA A 258      20.352  21.023  30.441  1.00 53.84           C  
ANISOU 1924  CA  ALA A 258     6799   9607   4050   1509   -635  -1679       C  
ATOM   1925  C   ALA A 258      21.555  21.926  30.679  1.00 59.19           C  
ANISOU 1925  C   ALA A 258     7470  10235   4786   1529   -790  -1873       C  
ATOM   1926  O   ALA A 258      21.399  23.088  31.072  1.00 62.42           O  
ANISOU 1926  O   ALA A 258     7873  10656   5187   1599   -880  -2061       O  
ATOM   1927  CB  ALA A 258      20.052  20.183  31.683  1.00 54.34           C  
ANISOU 1927  CB  ALA A 258     6852   9911   3885   1641   -576  -1590       C  
ATOM   1928  N   ASP A 259      22.764  21.409  30.442  1.00 51.28           N  
ANISOU 1928  N   ASP A 259     6466   9175   3844   1469   -827  -1832       N  
ATOM   1929  CA  ASP A 259      23.963  22.227  30.595  1.00 60.71           C  
ANISOU 1929  CA  ASP A 259     7646  10312   5110   1473   -975  -2006       C  
ATOM   1930  C   ASP A 259      23.992  23.359  29.576  1.00 65.06           C  
ANISOU 1930  C   ASP A 259     8200  10653   5869   1369  -1036  -2119       C  
ATOM   1931  O   ASP A 259      24.378  24.488  29.900  1.00 63.68           O  
ANISOU 1931  O   ASP A 259     8013  10451   5732   1409  -1162  -2314       O  
ATOM   1932  CB  ASP A 259      25.214  21.358  30.461  1.00 68.37           C  
ANISOU 1932  CB  ASP A 259     8608  11261   6108   1422   -989  -1919       C  
ATOM   1933  CG  ASP A 259      25.452  20.483  31.678  1.00 76.11           C  
ANISOU 1933  CG  ASP A 259     9582  12456   6879   1549   -972  -1858       C  
ATOM   1934  OD1 ASP A 259      24.729  20.646  32.683  1.00 72.61           O  
ANISOU 1934  OD1 ASP A 259     9137  12187   6264   1682   -961  -1900       O  
ATOM   1935  OD2 ASP A 259      26.364  19.631  31.627  1.00 79.27           O  
ANISOU 1935  OD2 ASP A 259     9979  12857   7284   1519   -969  -1765       O  
ATOM   1936  N   LEU A 260      23.585  23.076  28.336  1.00 49.63           N  
ANISOU 1936  N   LEU A 260     6260   8545   4052   1236   -953  -1998       N  
ATOM   1937  CA  LEU A 260      23.607  24.105  27.302  1.00 50.96           C  
ANISOU 1937  CA  LEU A 260     6432   8512   4420   1133  -1004  -2085       C  
ATOM   1938  C   LEU A 260      22.501  25.130  27.517  1.00 50.37           C  
ANISOU 1938  C   LEU A 260     6364   8448   4324   1197  -1020  -2203       C  
ATOM   1939  O   LEU A 260      22.712  26.331  27.311  1.00 54.48           O  
ANISOU 1939  O   LEU A 260     6882   8861   4956   1184  -1122  -2364       O  
ATOM   1940  CB  LEU A 260      23.486  23.463  25.920  1.00 47.24           C  
ANISOU 1940  CB  LEU A 260     5975   7887   4088    981   -909  -1919       C  
ATOM   1941  CG  LEU A 260      23.315  24.415  24.736  1.00 48.91           C  
ANISOU 1941  CG  LEU A 260     6193   7894   4497    871   -935  -1973       C  
ATOM   1942  CD1 LEU A 260      24.504  25.356  24.640  1.00 53.78           C  
ANISOU 1942  CD1 LEU A 260     6788   8408   5237    837  -1073  -2122       C  
ATOM   1943  CD2 LEU A 260      23.139  23.636  23.441  1.00 44.82           C  
ANISOU 1943  CD2 LEU A 260     5690   7253   4087    738   -832  -1797       C  
ATOM   1944  N   ALA A 261      21.314  24.675  27.927  1.00 49.69           N  
ANISOU 1944  N   ALA A 261     6287   8492   4102   1268   -919  -2124       N  
ATOM   1945  CA  ALA A 261      20.218  25.603  28.185  1.00 55.40           C  
ANISOU 1945  CA  ALA A 261     7013   9245   4791   1343   -929  -2234       C  
ATOM   1946  C   ALA A 261      20.552  26.558  29.322  1.00 69.67           C  
ANISOU 1946  C   ALA A 261     8809  11152   6511   1482  -1058  -2450       C  
ATOM   1947  O   ALA A 261      20.123  27.717  29.308  1.00 75.69           O  
ANISOU 1947  O   ALA A 261     9575  11858   7325   1516  -1127  -2604       O  
ATOM   1948  CB  ALA A 261      18.937  24.830  28.497  1.00 50.31           C  
ANISOU 1948  CB  ALA A 261     6369   8744   4003   1399   -792  -2096       C  
ATOM   1949  N   LYS A 262      21.317  26.093  30.308  1.00 70.22           N  
ANISOU 1949  N   LYS A 262     8865  11366   6449   1566  -1098  -2466       N  
ATOM   1950  CA  LYS A 262      21.755  26.934  31.412  1.00 84.59           C  
ANISOU 1950  CA  LYS A 262    10673  13287   8182   1700  -1232  -2676       C  
ATOM   1951  C   LYS A 262      23.036  27.697  31.091  1.00 86.49           C  
ANISOU 1951  C   LYS A 262    10903  13373   8585   1632  -1377  -2815       C  
ATOM   1952  O   LYS A 262      23.308  28.723  31.726  1.00 89.40           O  
ANISOU 1952  O   LYS A 262    11265  13758   8946   1716  -1508  -3023       O  
ATOM   1953  CB  LYS A 262      21.933  26.074  32.672  1.00 89.42           C  
ANISOU 1953  CB  LYS A 262    11273  14143   8561   1834  -1207  -2628       C  
ATOM   1954  CG  LYS A 262      22.645  26.743  33.835  1.00 98.99           C  
ANISOU 1954  CG  LYS A 262    12470  15470   9673   1971  -1352  -2832       C  
ATOM   1955  CD  LYS A 262      22.639  25.861  35.070  1.00103.90           C  
ANISOU 1955  CD  LYS A 262    13081  16351  10046   2113  -1310  -2767       C  
ATOM   1956  CE  LYS A 262      23.325  26.552  36.235  1.00106.19           C  
ANISOU 1956  CE  LYS A 262    13340  16700  10308   2226  -1430  -2918       C  
ATOM   1957  NZ  LYS A 262      24.655  27.091  35.837  1.00104.63           N  
ANISOU 1957  NZ  LYS A 262    13133  16347  10274   2144  -1568  -3038       N  
ATOM   1958  N   TYR A 263      23.820  27.233  30.113  1.00 79.86           N  
ANISOU 1958  N   TYR A 263    10061  12385   7898   1482  -1359  -2707       N  
ATOM   1959  CA  TYR A 263      24.934  28.040  29.624  1.00 78.40           C  
ANISOU 1959  CA  TYR A 263     9861  12031   7897   1397  -1487  -2827       C  
ATOM   1960  C   TYR A 263      24.426  29.328  28.991  1.00 85.58           C  
ANISOU 1960  C   TYR A 263    10781  12774   8960   1353  -1542  -2949       C  
ATOM   1961  O   TYR A 263      24.997  30.404  29.205  1.00 91.28           O  
ANISOU 1961  O   TYR A 263    11491  13425   9768   1367  -1684  -3135       O  
ATOM   1962  CB  TYR A 263      25.773  27.239  28.629  1.00 82.88           C  
ANISOU 1962  CB  TYR A 263    10421  12480   8591   1247  -1438  -2670       C  
ATOM   1963  CG  TYR A 263      26.877  28.042  27.979  1.00 86.94           C  
ANISOU 1963  CG  TYR A 263    10912  12812   9310   1141  -1554  -2768       C  
ATOM   1964  CD1 TYR A 263      28.097  28.223  28.617  1.00 90.56           C  
ANISOU 1964  CD1 TYR A 263    11337  13309   9764   1173  -1674  -2875       C  
ATOM   1965  CD2 TYR A 263      26.698  28.623  26.729  1.00 88.48           C  
ANISOU 1965  CD2 TYR A 263    11115  12800   9705   1009  -1543  -2749       C  
ATOM   1966  CE1 TYR A 263      29.109  28.958  28.028  1.00 93.69           C  
ANISOU 1966  CE1 TYR A 263    11705  13540  10355   1071  -1779  -2959       C  
ATOM   1967  CE2 TYR A 263      27.703  29.359  26.134  1.00 92.49           C  
ANISOU 1967  CE2 TYR A 263    11597  13143  10402    909  -1644  -2826       C  
ATOM   1968  CZ  TYR A 263      28.906  29.524  26.787  1.00 97.82           C  
ANISOU 1968  CZ  TYR A 263    12235  13858  11075    937  -1761  -2930       C  
ATOM   1969  OH  TYR A 263      29.910  30.257  26.196  1.00103.62           O  
ANISOU 1969  OH  TYR A 263    12935  14430  12004    832  -1861  -3001       O  
ATOM   1970  N   ILE A 264      23.352  29.237  28.207  1.00 87.56           N  
ANISOU 1970  N   ILE A 264    11055  12961   9254   1299  -1435  -2848       N  
ATOM   1971  CA  ILE A 264      22.586  30.405  27.789  1.00 87.48           C  
ANISOU 1971  CA  ILE A 264    11060  12834   9344   1294  -1473  -2958       C  
ATOM   1972  C   ILE A 264      21.900  30.949  29.039  1.00 92.93           C  
ANISOU 1972  C   ILE A 264    11752  13694   9864   1476  -1520  -3110       C  
ATOM   1973  O   ILE A 264      21.934  30.306  30.093  1.00102.96           O  
ANISOU 1973  O   ILE A 264    13013  15170  10939   1591  -1500  -3097       O  
ATOM   1974  CB  ILE A 264      21.584  30.043  26.674  1.00 81.04           C  
ANISOU 1974  CB  ILE A 264    10265  11929   8598   1200  -1339  -2798       C  
ATOM   1975  CG1 ILE A 264      22.250  29.120  25.649  1.00 72.64           C  
ANISOU 1975  CG1 ILE A 264     9198  10763   7638   1049  -1269  -2618       C  
ATOM   1976  CG2 ILE A 264      21.071  31.287  25.961  1.00 86.46           C  
ANISOU 1976  CG2 ILE A 264    10966  12443   9442   1158  -1391  -2901       C  
ATOM   1977  CD1 ILE A 264      21.273  28.311  24.819  1.00 62.91           C  
ANISOU 1977  CD1 ILE A 264     7984   9511   6407    983  -1117  -2429       C  
ATOM   1978  N   CYS A 265      21.291  32.135  28.934  1.00 94.35           N  
ANISOU 1978  N   CYS A 265    11944  13792  10113   1507  -1584  -3256       N  
ATOM   1979  CA  CYS A 265      20.732  32.895  30.055  1.00 94.36           C  
ANISOU 1979  CA  CYS A 265    11947  13926   9981   1682  -1656  -3441       C  
ATOM   1980  C   CYS A 265      21.839  33.533  30.889  1.00 91.23           C  
ANISOU 1980  C   CYS A 265    11525  13525   9612   1734  -1803  -3591       C  
ATOM   1981  O   CYS A 265      21.758  34.718  31.226  1.00101.20           O  
ANISOU 1981  O   CYS A 265    12781  14710  10963   1781  -1892  -3726       O  
ATOM   1982  CB  CYS A 265      19.832  32.032  30.951  1.00 97.91           C  
ANISOU 1982  CB  CYS A 265    12393  14628  10180   1815  -1543  -3355       C  
ATOM   1983  SG  CYS A 265      18.547  31.098  30.093  1.00104.05           S  
ANISOU 1983  SG  CYS A 265    13181  15411  10944   1741  -1341  -3109       S  
ATOM   1984  N   GLU A 266      22.877  32.764  31.228  1.00 86.02           N  
ANISOU 1984  N   GLU A 266    10847  12939   8897   1721  -1819  -3547       N  
ATOM   1985  CA  GLU A 266      23.995  33.323  31.982  1.00 91.23           C  
ANISOU 1985  CA  GLU A 266    11475  13583   9607   1756  -1947  -3661       C  
ATOM   1986  C   GLU A 266      24.869  34.231  31.127  1.00 95.13           C  
ANISOU 1986  C   GLU A 266    11959  13829  10356   1619  -2056  -3740       C  
ATOM   1987  O   GLU A 266      25.605  35.060  31.673  1.00 91.96           O  
ANISOU 1987  O   GLU A 266    11530  13374  10036   1646  -2173  -3860       O  
ATOM   1988  CB  GLU A 266      24.839  32.201  32.589  1.00 83.47           C  
ANISOU 1988  CB  GLU A 266    10472  12756   8486   1785  -1929  -3583       C  
ATOM   1989  CG  GLU A 266      24.113  31.395  33.654  1.00 80.60           C  
ANISOU 1989  CG  GLU A 266    10109  12644   7871   1935  -1834  -3506       C  
ATOM   1990  CD  GLU A 266      24.927  30.216  34.150  1.00 85.60           C  
ANISOU 1990  CD  GLU A 266    10727  13420   8375   1955  -1808  -3406       C  
ATOM   1991  OE1 GLU A 266      26.136  30.155  33.843  1.00 87.72           O  
ANISOU 1991  OE1 GLU A 266    10979  13604   8745   1873  -1884  -3427       O  
ATOM   1992  OE2 GLU A 266      24.357  29.351  34.847  1.00 91.54           O  
ANISOU 1992  OE2 GLU A 266    11482  14370   8927   2053  -1710  -3300       O  
ATOM   1993  N   ASN A 267      24.806  34.092  29.806  1.00 93.99           N  
ANISOU 1993  N   ASN A 267    11833  13535  10343   1474  -2019  -3669       N  
ATOM   1994  CA  ASN A 267      25.493  34.967  28.863  1.00 90.43           C  
ANISOU 1994  CA  ASN A 267    11373  12839  10148   1333  -2105  -3718       C  
ATOM   1995  C   ASN A 267      24.509  35.458  27.813  1.00 80.69           C  
ANISOU 1995  C   ASN A 267    10173  11462   9024   1265  -2058  -3696       C  
ATOM   1996  O   ASN A 267      24.767  35.434  26.608  1.00 82.64           O  
ANISOU 1996  O   ASN A 267    10420  11538   9440   1113  -2027  -3600       O  
ATOM   1997  CB  ASN A 267      26.678  34.254  28.221  1.00 88.08           C  
ANISOU 1997  CB  ASN A 267    11051  12488   9928   1204  -2111  -3634       C  
ATOM   1998  CG  ASN A 267      27.576  33.589  29.243  1.00 89.88           C  
ANISOU 1998  CG  ASN A 267    11249  12883  10019   1281  -2148  -3645       C  
ATOM   1999  OD1 ASN A 267      28.576  34.164  29.672  1.00 96.90           O  
ANISOU 1999  OD1 ASN A 267    12101  13723  10994   1278  -2256  -3733       O  
ATOM   2000  ND2 ASN A 267      27.224  32.372  29.641  1.00 85.35           N  
ANISOU 2000  ND2 ASN A 267    10685  12492   9252   1342  -2034  -3513       N  
ATOM   2001  N   GLN A 268      23.351  35.922  28.285  1.00 79.53           N  
ANISOU 2001  N   GLN A 268    10046  11377   8797   1377  -2029  -3743       N  
ATOM   2002  CA  GLN A 268      22.248  36.241  27.387  1.00 84.16           C  
ANISOU 2002  CA  GLN A 268    10665  11865   9447   1336  -1968  -3712       C  
ATOM   2003  C   GLN A 268      22.557  37.450  26.515  1.00 88.46           C  
ANISOU 2003  C   GLN A 268    11211  12148  10251   1225  -2052  -3769       C  
ATOM   2004  O   GLN A 268      22.280  37.436  25.310  1.00 80.77           O  
ANISOU 2004  O   GLN A 268    10256  11035   9399   1108  -2006  -3692       O  
ATOM   2005  CB  GLN A 268      20.981  36.485  28.200  1.00 83.04           C  
ANISOU 2005  CB  GLN A 268    10535  11864   9153   1493  -1923  -3753       C  
ATOM   2006  CG  GLN A 268      19.726  36.533  27.373  1.00 87.60           C  
ANISOU 2006  CG  GLN A 268    11144  12394   9747   1469  -1835  -3701       C  
ATOM   2007  CD  GLN A 268      18.504  36.723  28.231  1.00 98.34           C  
ANISOU 2007  CD  GLN A 268    12505  13911  10948   1629  -1788  -3736       C  
ATOM   2008  OE1 GLN A 268      17.459  37.154  27.752  1.00 98.28           O  
ANISOU 2008  OE1 GLN A 268    12516  13852  10973   1637  -1748  -3737       O  
ATOM   2009  NE2 GLN A 268      18.631  36.415  29.517  1.00102.89           N  
ANISOU 2009  NE2 GLN A 268    13058  14683  11352   1760  -1793  -3762       N  
ATOM   2010  N   ASP A 269      23.109  38.511  27.106  1.00 89.90           N  
ANISOU 2010  N   ASP A 269    11372  12263  10524   1262  -2170  -3891       N  
ATOM   2011  CA  ASP A 269      23.364  39.729  26.345  1.00 94.94           C  
ANISOU 2011  CA  ASP A 269    12011  12657  11406   1166  -2249  -3938       C  
ATOM   2012  C   ASP A 269      24.469  39.549  25.313  1.00 94.42           C  
ANISOU 2012  C   ASP A 269    11926  12433  11516    988  -2269  -3863       C  
ATOM   2013  O   ASP A 269      24.557  40.348  24.374  1.00 97.57           O  
ANISOU 2013  O   ASP A 269    12329  12624  12118    880  -2298  -3850       O  
ATOM   2014  CB  ASP A 269      23.706  40.879  27.292  1.00104.53           C  
ANISOU 2014  CB  ASP A 269    13204  13846  12666   1255  -2372  -4087       C  
ATOM   2015  CG  ASP A 269      22.472  41.512  27.904  1.00107.52           C  
ANISOU 2015  CG  ASP A 269    13603  14290  12959   1399  -2367  -4168       C  
ATOM   2016  OD1 ASP A 269      21.804  42.310  27.213  1.00110.15           O  
ANISOU 2016  OD1 ASP A 269    13960  14478  13414   1366  -2370  -4177       O  
ATOM   2017  OD2 ASP A 269      22.167  41.204  29.074  1.00107.79           O  
ANISOU 2017  OD2 ASP A 269    13629  14525  12803   1549  -2358  -4217       O  
ATOM   2018  N   SER A 270      25.309  38.529  25.465  1.00 88.12           N  
ANISOU 2018  N   SER A 270    11105  11733  10644    958  -2251  -3806       N  
ATOM   2019  CA  SER A 270      26.308  38.187  24.464  1.00 77.12           C  
ANISOU 2019  CA  SER A 270     9689  10216   9399    793  -2255  -3719       C  
ATOM   2020  C   SER A 270      25.779  37.214  23.419  1.00 76.37           C  
ANISOU 2020  C   SER A 270     9615  10116   9287    708  -2110  -3537       C  
ATOM   2021  O   SER A 270      26.536  36.804  22.533  1.00 67.97           O  
ANISOU 2021  O   SER A 270     8528   8959   8338    571  -2073  -3409       O  
ATOM   2022  CB  SER A 270      27.552  37.597  25.136  1.00 79.54           C  
ANISOU 2022  CB  SER A 270     9950  10623   9647    802  -2303  -3729       C  
ATOM   2023  OG  SER A 270      28.304  38.606  25.787  1.00 86.26           O  
ANISOU 2023  OG  SER A 270    10770  11415  10591    828  -2424  -3844       O  
ATOM   2024  N   ILE A 271      24.504  36.839  23.503  1.00 75.62           N  
ANISOU 2024  N   ILE A 271     9555  10116   9062    782  -2003  -3478       N  
ATOM   2025  CA  ILE A 271      23.895  35.931  22.540  1.00 75.45           C  
ANISOU 2025  CA  ILE A 271     9550  10085   9032    703  -1840  -3264       C  
ATOM   2026  C   ILE A 271      22.764  36.658  21.821  1.00 80.18           C  
ANISOU 2026  C   ILE A 271    10183  10569   9714    687  -1811  -3266       C  
ATOM   2027  O   ILE A 271      22.838  36.888  20.609  1.00 82.88           O  
ANISOU 2027  O   ILE A 271    10529  10739  10222    558  -1783  -3178       O  
ATOM   2028  CB  ILE A 271      23.406  34.642  23.224  1.00 72.78           C  
ANISOU 2028  CB  ILE A 271     9217   9972   8465    791  -1725  -3160       C  
ATOM   2029  CG1 ILE A 271      24.602  33.846  23.756  1.00 60.73           C  
ANISOU 2029  CG1 ILE A 271     7658   8541   6875    789  -1746  -3131       C  
ATOM   2030  CG2 ILE A 271      22.602  33.797  22.258  1.00 72.63           C  
ANISOU 2030  CG2 ILE A 271     9217   9936   8440    719  -1564  -2957       C  
ATOM   2031  CD1 ILE A 271      24.231  32.742  24.721  1.00 53.26           C  
ANISOU 2031  CD1 ILE A 271     6715   7829   5692    904  -1666  -3067       C  
ATOM   2032  N   SER A 272      21.718  37.034  22.559  1.00 76.02           N  
ANISOU 2032  N   SER A 272     9678  10139   9068    824  -1817  -3366       N  
ATOM   2033  CA  SER A 272      20.626  37.827  22.008  1.00 82.32           C  
ANISOU 2033  CA  SER A 272    10505  10835   9936    831  -1804  -3394       C  
ATOM   2034  C   SER A 272      19.729  38.299  23.142  1.00 98.77           C  
ANISOU 2034  C   SER A 272    12602  13057  11869   1010  -1843  -3548       C  
ATOM   2035  O   SER A 272      19.481  37.553  24.093  1.00106.02           O  
ANISOU 2035  O   SER A 272    13512  14187  12584   1119  -1795  -3539       O  
ATOM   2036  CB  SER A 272      19.802  37.030  20.989  1.00 76.97           C  
ANISOU 2036  CB  SER A 272     9843  10146   9256    755  -1644  -3188       C  
ATOM   2037  OG  SER A 272      18.440  37.418  21.031  1.00 69.93           O  
ANISOU 2037  OG  SER A 272     8975   9283   8311    836  -1605  -3219       O  
ATOM   2038  N   SER A 273      19.232  39.532  23.022  1.00105.16           N  
ANISOU 2038  N   SER A 273    13431  13748  12777   1044  -1928  -3685       N  
ATOM   2039  CA  SER A 273      18.361  40.125  24.038  1.00111.96           C  
ANISOU 2039  CA  SER A 273    14296  14719  13523   1210  -1950  -3797       C  
ATOM   2040  C   SER A 273      16.909  39.819  23.678  1.00107.00           C  
ANISOU 2040  C   SER A 273    13695  14158  12804   1257  -1842  -3747       C  
ATOM   2041  O   SER A 273      16.160  40.668  23.189  1.00107.35           O  
ANISOU 2041  O   SER A 273    13757  14086  12946   1259  -1852  -3775       O  
ATOM   2042  CB  SER A 273      18.608  41.625  24.147  1.00120.27           C  
ANISOU 2042  CB  SER A 273    15345  15607  14746   1218  -2072  -3909       C  
ATOM   2043  OG  SER A 273      19.977  41.934  23.950  1.00122.80           O  
ANISOU 2043  OG  SER A 273    15642  15798  15218   1115  -2159  -3918       O  
ATOM   2044  N   LYS A 274      16.506  38.573  23.935  1.00 98.74           N  
ANISOU 2044  N   LYS A 274    12636  13295  11584   1282  -1707  -3604       N  
ATOM   2045  CA  LYS A 274      15.162  38.126  23.582  1.00 85.46           C  
ANISOU 2045  CA  LYS A 274    10962  11683   9826   1305  -1572  -3488       C  
ATOM   2046  C   LYS A 274      14.799  36.818  24.276  1.00 79.45           C  
ANISOU 2046  C   LYS A 274    10181  11161   8844   1369  -1450  -3367       C  
ATOM   2047  O   LYS A 274      13.726  36.257  24.032  1.00 73.81           O  
ANISOU 2047  O   LYS A 274     9464  10525   8055   1381  -1326  -3249       O  
ATOM   2048  CB  LYS A 274      15.045  37.966  22.063  1.00 83.94           C  
ANISOU 2048  CB  LYS A 274    10782  11309   9804   1138  -1500  -3328       C  
ATOM   2049  CG  LYS A 274      13.639  38.132  21.518  1.00 83.59           C  
ANISOU 2049  CG  LYS A 274    10751  11254   9757   1159  -1417  -3277       C  
ATOM   2050  CD  LYS A 274      13.608  37.918  20.017  1.00 83.97           C  
ANISOU 2050  CD  LYS A 274    10810  11129   9964    995  -1350  -3116       C  
ATOM   2051  CE  LYS A 274      12.302  37.280  19.584  1.00 88.01           C  
ANISOU 2051  CE  LYS A 274    11321  11718  10402   1002  -1210  -2982       C  
ATOM   2052  NZ  LYS A 274      12.263  35.830  19.915  1.00 92.38           N  
ANISOU 2052  NZ  LYS A 274    11853  12444  10804    997  -1091  -2831       N  
ATOM   2053  N   LEU A 275      15.676  36.327  25.149  1.00 82.23           N  
ANISOU 2053  N   LEU A 275    10516  11632   9094   1412  -1485  -3394       N  
ATOM   2054  CA  LEU A 275      15.487  35.033  25.791  1.00 83.93           C  
ANISOU 2054  CA  LEU A 275    10713  12064   9112   1462  -1373  -3265       C  
ATOM   2055  C   LEU A 275      15.180  35.142  27.278  1.00 92.16           C  
ANISOU 2055  C   LEU A 275    11743  13333   9941   1655  -1408  -3393       C  
ATOM   2056  O   LEU A 275      15.127  34.115  27.963  1.00 99.33           O  
ANISOU 2056  O   LEU A 275    12634  14434  10673   1710  -1328  -3297       O  
ATOM   2057  CB  LEU A 275      16.730  34.157  25.583  1.00 82.10           C  
ANISOU 2057  CB  LEU A 275    10471  11811   8913   1357  -1364  -3156       C  
ATOM   2058  CG  LEU A 275      16.954  33.560  24.188  1.00 75.18           C  
ANISOU 2058  CG  LEU A 275     9601  10777   8186   1176  -1281  -2970       C  
ATOM   2059  CD1 LEU A 275      17.503  34.592  23.209  1.00 68.96           C  
ANISOU 2059  CD1 LEU A 275     8825   9743   7632   1065  -1374  -3039       C  
ATOM   2060  CD2 LEU A 275      17.879  32.356  24.265  1.00 79.05           C  
ANISOU 2060  CD2 LEU A 275    10077  11331   8629   1119  -1234  -2838       C  
ATOM   2061  N   LYS A 276      14.961  36.356  27.791  1.00 88.16           N  
ANISOU 2061  N   LYS A 276    11246  12808   9444   1762  -1525  -3607       N  
ATOM   2062  CA  LYS A 276      14.800  36.552  29.229  1.00 94.85           C  
ANISOU 2062  CA  LYS A 276    12065  13838  10134   1930  -1553  -3683       C  
ATOM   2063  C   LYS A 276      13.517  35.916  29.745  1.00 96.27           C  
ANISOU 2063  C   LYS A 276    12230  14236  10111   2041  -1423  -3601       C  
ATOM   2064  O   LYS A 276      13.493  35.355  30.847  1.00 98.99           O  
ANISOU 2064  O   LYS A 276    12548  14790  10276   2149  -1387  -3571       O  
ATOM   2065  CB  LYS A 276      14.824  38.043  29.553  1.00 93.01           C  
ANISOU 2065  CB  LYS A 276    11828  13485  10026   1986  -1681  -3847       C  
ATOM   2066  CG  LYS A 276      15.183  38.375  30.989  1.00 95.49           C  
ANISOU 2066  CG  LYS A 276    12111  13935  10237   2129  -1754  -3946       C  
ATOM   2067  CD  LYS A 276      14.325  39.520  31.502  1.00 93.63           C  
ANISOU 2067  CD  LYS A 276    11866  13699  10010   2253  -1804  -4067       C  
ATOM   2068  CE  LYS A 276      14.563  39.780  32.979  1.00 95.28           C  
ANISOU 2068  CE  LYS A 276    12040  14067  10094   2411  -1867  -4162       C  
ATOM   2069  NZ  LYS A 276      15.174  41.119  33.214  1.00 95.19           N  
ANISOU 2069  NZ  LYS A 276    12027  13903  10240   2429  -2025  -4328       N  
ATOM   2070  N   GLU A 277      12.438  36.005  28.973  1.00101.35           N  
ANISOU 2070  N   GLU A 277    12886  14838  10783   2016  -1349  -3560       N  
ATOM   2071  CA  GLU A 277      11.167  35.412  29.366  1.00109.84           C  
ANISOU 2071  CA  GLU A 277    13940  16113  11680   2108  -1218  -3471       C  
ATOM   2072  C   GLU A 277      11.129  33.902  29.156  1.00112.74           C  
ANISOU 2072  C   GLU A 277    14293  16582  11959   2034  -1072  -3240       C  
ATOM   2073  O   GLU A 277      10.073  33.291  29.350  1.00114.24           O  
ANISOU 2073  O   GLU A 277    14459  16922  12025   2082   -948  -3127       O  
ATOM   2074  CB  GLU A 277      10.018  36.087  28.612  1.00113.41           C  
ANISOU 2074  CB  GLU A 277    14403  16473  12216   2103  -1192  -3495       C  
ATOM   2075  CG  GLU A 277       9.934  37.594  28.838  1.00119.28           C  
ANISOU 2075  CG  GLU A 277    15149  17091  13082   2165  -1319  -3664       C  
ATOM   2076  CD  GLU A 277       8.607  38.022  29.437  1.00125.36           C  
ANISOU 2076  CD  GLU A 277    15891  17992  13750   2308  -1277  -3694       C  
ATOM   2077  OE1 GLU A 277       8.613  38.875  30.351  1.00128.54           O  
ANISOU 2077  OE1 GLU A 277    16276  18428  14137   2426  -1365  -3817       O  
ATOM   2078  OE2 GLU A 277       7.559  37.504  28.996  1.00125.88           O  
ANISOU 2078  OE2 GLU A 277    15949  18130  13752   2305  -1157  -3596       O  
ATOM   2079  N   CYS A 278      12.250  33.289  28.765  1.00110.74           N  
ANISOU 2079  N   CYS A 278    14048  16243  11786   1912  -1081  -3152       N  
ATOM   2080  CA  CYS A 278      12.349  31.840  28.672  1.00102.47           C  
ANISOU 2080  CA  CYS A 278    12986  15284  10665   1845   -954  -2929       C  
ATOM   2081  C   CYS A 278      13.169  31.214  29.789  1.00 95.12           C  
ANISOU 2081  C   CYS A 278    12043  14525   9575   1925   -977  -2934       C  
ATOM   2082  O   CYS A 278      13.058  30.004  30.006  1.00 92.72           O  
ANISOU 2082  O   CYS A 278    11723  14346   9161   1914   -866  -2757       O  
ATOM   2083  CB  CYS A 278      12.961  31.424  27.324  1.00100.24           C  
ANISOU 2083  CB  CYS A 278    12720  14785  10580   1645   -928  -2796       C  
ATOM   2084  SG  CYS A 278      11.862  31.583  25.896  1.00 98.19           S  
ANISOU 2084  SG  CYS A 278    12471  14365  10473   1530   -842  -2693       S  
ATOM   2085  N   CYS A 279      13.973  31.997  30.507  1.00 94.17           N  
ANISOU 2085  N   CYS A 279    11927  14414   9439   2008  -1120  -3130       N  
ATOM   2086  CA  CYS A 279      14.867  31.441  31.514  1.00101.28           C  
ANISOU 2086  CA  CYS A 279    12816  15465  10200   2079  -1156  -3143       C  
ATOM   2087  C   CYS A 279      14.255  31.370  32.907  1.00104.88           C  
ANISOU 2087  C   CYS A 279    13239  16157  10455   2256  -1125  -3155       C  
ATOM   2088  O   CYS A 279      14.764  30.621  33.748  1.00 98.52           O  
ANISOU 2088  O   CYS A 279    12414  15499   9520   2310  -1106  -3089       O  
ATOM   2089  CB  CYS A 279      16.162  32.255  31.573  1.00105.43           C  
ANISOU 2089  CB  CYS A 279    13349  15854  10854   2052  -1321  -3306       C  
ATOM   2090  SG  CYS A 279      16.997  32.404  29.979  1.00110.71           S  
ANISOU 2090  SG  CYS A 279    14039  16219  11809   1825  -1352  -3250       S  
ATOM   2091  N   GLU A 280      13.197  32.133  33.179  1.00110.81           N  
ANISOU 2091  N   GLU A 280    13975  16935  11193   2344  -1118  -3221       N  
ATOM   2092  CA  GLU A 280      12.501  32.043  34.458  1.00112.16           C  
ANISOU 2092  CA  GLU A 280    14103  17326  11186   2505  -1074  -3206       C  
ATOM   2093  C   GLU A 280      11.550  30.862  34.518  1.00104.15           C  
ANISOU 2093  C   GLU A 280    13068  16486  10017   2516   -903  -3005       C  
ATOM   2094  O   GLU A 280      10.845  30.697  35.519  1.00102.70           O  
ANISOU 2094  O   GLU A 280    12843  16492   9685   2643   -849  -2967       O  
ATOM   2095  CB  GLU A 280      11.731  33.333  34.746  1.00116.26           C  
ANISOU 2095  CB  GLU A 280    14609  17813  11751   2601  -1137  -3356       C  
ATOM   2096  CG  GLU A 280      12.613  34.555  34.824  1.00118.71           C  
ANISOU 2096  CG  GLU A 280    14934  17959  12213   2603  -1308  -3551       C  
ATOM   2097  CD  GLU A 280      11.987  35.765  34.178  1.00117.12           C  
ANISOU 2097  CD  GLU A 280    14748  17592  12162   2590  -1363  -3666       C  
ATOM   2098  OE1 GLU A 280      10.788  35.703  33.836  1.00115.27           O  
ANISOU 2098  OE1 GLU A 280    14508  17399  11891   2607  -1271  -3608       O  
ATOM   2099  OE2 GLU A 280      12.692  36.783  34.022  1.00116.07           O  
ANISOU 2099  OE2 GLU A 280    14630  17287  12186   2563  -1499  -3809       O  
ATOM   2100  N   LYS A 281      11.527  30.062  33.489  1.00 94.68           N  
ANISOU 2100  N   LYS A 281    11893  15225   8855   2388   -821  -2876       N  
ATOM   2101  CA  LYS A 281      10.656  28.927  33.267  1.00 85.14           C  
ANISOU 2101  CA  LYS A 281    10669  14139   7539   2363   -656  -2673       C  
ATOM   2102  C   LYS A 281      11.313  27.660  33.799  1.00 84.47           C  
ANISOU 2102  C   LYS A 281    10577  14183   7335   2357   -599  -2520       C  
ATOM   2103  O   LYS A 281      12.542  27.582  33.880  1.00 88.10           O  
ANISOU 2103  O   LYS A 281    11056  14587   7830   2326   -684  -2565       O  
ATOM   2104  CB  LYS A 281      10.374  28.813  31.771  1.00 80.83           C  
ANISOU 2104  CB  LYS A 281    10143  13379   7191   2186   -605  -2575       C  
ATOM   2105  CG  LYS A 281       9.497  27.693  31.370  1.00 82.10           C  
ANISOU 2105  CG  LYS A 281    10280  13594   7320   2118   -441  -2338       C  
ATOM   2106  CD  LYS A 281       8.022  28.046  31.391  1.00 86.69           C  
ANISOU 2106  CD  LYS A 281    10831  14260   7847   2186   -368  -2340       C  
ATOM   2107  CE  LYS A 281       7.615  29.160  30.466  1.00 86.44           C  
ANISOU 2107  CE  LYS A 281    10819  14035   7989   2138   -426  -2458       C  
ATOM   2108  NZ  LYS A 281       6.199  28.862  30.134  1.00 86.90           N  
ANISOU 2108  NZ  LYS A 281    10842  14155   8021   2134   -301  -2341       N  
ATOM   2109  N   PRO A 282      10.536  26.646  34.188  1.00 84.85           N  
ANISOU 2109  N   PRO A 282    10593  14402   7245   2386   -458  -2331       N  
ATOM   2110  CA  PRO A 282      11.150  25.383  34.619  1.00 88.02           C  
ANISOU 2110  CA  PRO A 282    10990  14909   7545   2371   -400  -2166       C  
ATOM   2111  C   PRO A 282      12.020  24.749  33.537  1.00 83.57           C  
ANISOU 2111  C   PRO A 282    10457  14143   7151   2189   -398  -2059       C  
ATOM   2112  O   PRO A 282      11.997  25.121  32.361  1.00 64.64           O  
ANISOU 2112  O   PRO A 282     8079  11526   4954   2057   -412  -2067       O  
ATOM   2113  CB  PRO A 282       9.945  24.498  34.977  1.00 90.21           C  
ANISOU 2113  CB  PRO A 282    11223  15354   7700   2403   -239  -1965       C  
ATOM   2114  CG  PRO A 282       8.733  25.213  34.477  1.00 89.72           C  
ANISOU 2114  CG  PRO A 282    11146  15256   7688   2408   -206  -2016       C  
ATOM   2115  CD  PRO A 282       9.099  26.670  34.517  1.00 87.11           C  
ANISOU 2115  CD  PRO A 282    10834  14812   7451   2458   -358  -2267       C  
ATOM   2116  N   LEU A 283      12.789  23.744  33.977  1.00 83.43           N  
ANISOU 2116  N   LEU A 283    10441  14202   7057   2184   -375  -1942       N  
ATOM   2117  CA  LEU A 283      13.859  23.134  33.184  1.00 85.31           C  
ANISOU 2117  CA  LEU A 283    10705  14267   7442   2036   -393  -1855       C  
ATOM   2118  C   LEU A 283      13.374  22.640  31.824  1.00 84.74           C  
ANISOU 2118  C   LEU A 283    10642  14013   7544   1863   -303  -1700       C  
ATOM   2119  O   LEU A 283      13.906  23.029  30.779  1.00 85.06           O  
ANISOU 2119  O   LEU A 283    10706  13834   7778   1739   -357  -1742       O  
ATOM   2120  CB  LEU A 283      14.484  21.980  33.978  1.00 88.44           C  
ANISOU 2120  CB  LEU A 283    11095  14813   7696   2079   -356  -1723       C  
ATOM   2121  CG  LEU A 283      15.584  21.052  33.424  1.00 89.06           C  
ANISOU 2121  CG  LEU A 283    11194  14773   7872   1956   -355  -1599       C  
ATOM   2122  CD1 LEU A 283      15.012  19.862  32.634  1.00 81.64           C  
ANISOU 2122  CD1 LEU A 283    10255  13770   6994   1831   -214  -1353       C  
ATOM   2123  CD2 LEU A 283      16.650  21.805  32.617  1.00 91.08           C  
ANISOU 2123  CD2 LEU A 283    11473  14808   8324   1859   -478  -1737       C  
ATOM   2124  N   LEU A 284      12.389  21.744  31.817  1.00 85.78           N  
ANISOU 2124  N   LEU A 284    10751  14233   7607   1850   -165  -1513       N  
ATOM   2125  CA  LEU A 284      11.995  21.139  30.550  1.00 89.52           C  
ANISOU 2125  CA  LEU A 284    11234  14540   8241   1685    -81  -1358       C  
ATOM   2126  C   LEU A 284      11.279  22.133  29.650  1.00 90.22           C  
ANISOU 2126  C   LEU A 284    11327  14486   8469   1634   -100  -1453       C  
ATOM   2127  O   LEU A 284      11.345  22.010  28.420  1.00 84.86           O  
ANISOU 2127  O   LEU A 284    10666  13609   7967   1488    -86  -1395       O  
ATOM   2128  CB  LEU A 284      11.129  19.912  30.804  1.00 87.79           C  
ANISOU 2128  CB  LEU A 284    10987  14451   7920   1683     65  -1133       C  
ATOM   2129  CG  LEU A 284      11.986  18.665  31.004  1.00 83.86           C  
ANISOU 2129  CG  LEU A 284    10501  13973   7389   1644     95   -978       C  
ATOM   2130  CD1 LEU A 284      11.108  17.445  31.070  1.00 80.81           C  
ANISOU 2130  CD1 LEU A 284    10090  13674   6941   1615    238   -745       C  
ATOM   2131  CD2 LEU A 284      13.023  18.535  29.889  1.00 74.06           C  
ANISOU 2131  CD2 LEU A 284     9298  12497   6344   1498     40   -976       C  
ATOM   2132  N   GLU A 285      10.611  23.128  30.237  1.00 93.95           N  
ANISOU 2132  N   GLU A 285    11781  15054   8860   1757   -135  -1603       N  
ATOM   2133  CA  GLU A 285       9.951  24.162  29.453  1.00 95.50           C  
ANISOU 2133  CA  GLU A 285    11983  15119   9185   1723   -164  -1708       C  
ATOM   2134  C   GLU A 285      10.890  25.298  29.053  1.00 90.79           C  
ANISOU 2134  C   GLU A 285    11420  14348   8727   1697   -311  -1903       C  
ATOM   2135  O   GLU A 285      10.578  26.019  28.100  1.00 85.62           O  
ANISOU 2135  O   GLU A 285    10779  13524   8227   1624   -337  -1959       O  
ATOM   2136  CB  GLU A 285       8.744  24.712  30.222  1.00101.25           C  
ANISOU 2136  CB  GLU A 285    12676  16025   9770   1869   -132  -1778       C  
ATOM   2137  CG  GLU A 285       7.541  25.105  29.358  1.00103.97           C  
ANISOU 2137  CG  GLU A 285    13007  16286  10211   1818    -77  -1758       C  
ATOM   2138  CD  GLU A 285       6.321  25.472  30.197  1.00109.56           C  
ANISOU 2138  CD  GLU A 285    13670  17201  10757   1969    -29  -1802       C  
ATOM   2139  OE1 GLU A 285       6.367  25.243  31.420  1.00111.60           O  
ANISOU 2139  OE1 GLU A 285    13905  17676  10820   2105    -19  -1814       O  
ATOM   2140  OE2 GLU A 285       5.338  26.025  29.650  1.00112.60           O  
ANISOU 2140  OE2 GLU A 285    14042  17537  11206   1960     -5  -1830       O  
ATOM   2141  N   LYS A 286      12.028  25.479  29.741  1.00 90.17           N  
ANISOU 2141  N   LYS A 286    11353  14305   8603   1753   -410  -2005       N  
ATOM   2142  CA  LYS A 286      12.936  26.560  29.351  1.00 85.55           C  
ANISOU 2142  CA  LYS A 286    10793  13549   8163   1719   -552  -2186       C  
ATOM   2143  C   LYS A 286      13.784  26.173  28.145  1.00 78.74           C  
ANISOU 2143  C   LYS A 286     9954  12471   7494   1540   -557  -2097       C  
ATOM   2144  O   LYS A 286      14.024  27.007  27.265  1.00 71.76           O  
ANISOU 2144  O   LYS A 286     9087  11393   6784   1459   -624  -2181       O  
ATOM   2145  CB  LYS A 286      13.837  26.988  30.521  1.00 87.61           C  
ANISOU 2145  CB  LYS A 286    11052  13922   8312   1845   -668  -2346       C  
ATOM   2146  CG  LYS A 286      14.721  25.901  31.112  1.00 91.15           C  
ANISOU 2146  CG  LYS A 286    11497  14478   8659   1853   -649  -2240       C  
ATOM   2147  CD  LYS A 286      16.062  26.432  31.602  1.00 96.18           C  
ANISOU 2147  CD  LYS A 286    12142  15093   9311   1889   -796  -2400       C  
ATOM   2148  CE  LYS A 286      16.783  25.363  32.419  1.00102.20           C  
ANISOU 2148  CE  LYS A 286    12894  16009   9928   1937   -773  -2302       C  
ATOM   2149  NZ  LYS A 286      17.865  24.671  31.659  1.00100.16           N  
ANISOU 2149  NZ  LYS A 286    12648  15609   9801   1794   -776  -2196       N  
ATOM   2150  N   SER A 287      14.252  24.923  28.078  1.00 81.92           N  
ANISOU 2150  N   SER A 287    10355  12902   7867   1480   -488  -1925       N  
ATOM   2151  CA  SER A 287      14.967  24.492  26.882  1.00 82.41           C  
ANISOU 2151  CA  SER A 287    10438  12769   8107   1315   -481  -1831       C  
ATOM   2152  C   SER A 287      14.024  24.369  25.693  1.00 77.80           C  
ANISOU 2152  C   SER A 287     9859  12060   7640   1207   -395  -1727       C  
ATOM   2153  O   SER A 287      14.434  24.601  24.550  1.00 77.37           O  
ANISOU 2153  O   SER A 287     9823  11810   7763   1082   -419  -1720       O  
ATOM   2154  CB  SER A 287      15.691  23.167  27.132  1.00 83.11           C  
ANISOU 2154  CB  SER A 287    10525  12921   8131   1288   -431  -1677       C  
ATOM   2155  OG  SER A 287      14.957  22.331  28.007  1.00 89.09           O  
ANISOU 2155  OG  SER A 287    11264  13882   8705   1377   -336  -1566       O  
ATOM   2156  N   HIS A 288      12.764  24.006  25.942  1.00 73.47           N  
ANISOU 2156  N   HIS A 288     9291  11629   6994   1254   -295  -1644       N  
ATOM   2157  CA  HIS A 288      11.761  24.046  24.884  1.00 67.11           C  
ANISOU 2157  CA  HIS A 288     8486  10718   6294   1168   -225  -1572       C  
ATOM   2158  C   HIS A 288      11.449  25.478  24.475  1.00 66.18           C  
ANISOU 2158  C   HIS A 288     8378  10490   6277   1181   -306  -1743       C  
ATOM   2159  O   HIS A 288      11.149  25.736  23.304  1.00 64.56           O  
ANISOU 2159  O   HIS A 288     8186  10120   6223   1077   -293  -1716       O  
ATOM   2160  CB  HIS A 288      10.490  23.330  25.340  1.00 62.70           C  
ANISOU 2160  CB  HIS A 288     7896  10325   5603   1221   -102  -1446       C  
ATOM   2161  CG  HIS A 288       9.345  23.460  24.385  1.00 67.30           C  
ANISOU 2161  CG  HIS A 288     8470  10822   6277   1153    -36  -1390       C  
ATOM   2162  ND1 HIS A 288       9.221  22.675  23.259  1.00 69.52           N  
ANISOU 2162  ND1 HIS A 288     8761  10977   6677   1011     31  -1238       N  
ATOM   2163  CD2 HIS A 288       8.270  24.284  24.389  1.00 68.51           C  
ANISOU 2163  CD2 HIS A 288     8606  11003   6420   1212    -32  -1470       C  
ATOM   2164  CE1 HIS A 288       8.120  23.009  22.610  1.00 70.62           C  
ANISOU 2164  CE1 HIS A 288     8888  11070   6873    983     74  -1225       C  
ATOM   2165  NE2 HIS A 288       7.524  23.983  23.276  1.00 70.74           N  
ANISOU 2165  NE2 HIS A 288     8886  11178   6814   1103     39  -1362       N  
ATOM   2166  N   CYS A 289      11.517  26.416  25.422  1.00 61.22           N  
ANISOU 2166  N   CYS A 289     7745   9951   5567   1312   -393  -1921       N  
ATOM   2167  CA  CYS A 289      11.328  27.826  25.098  1.00 75.96           C  
ANISOU 2167  CA  CYS A 289     9624  11702   7535   1332   -486  -2098       C  
ATOM   2168  C   CYS A 289      12.460  28.340  24.218  1.00 73.67           C  
ANISOU 2168  C   CYS A 289     9362  11192   7436   1216   -580  -2154       C  
ATOM   2169  O   CYS A 289      12.218  28.993  23.196  1.00 72.43           O  
ANISOU 2169  O   CYS A 289     9221  10864   7436   1137   -599  -2178       O  
ATOM   2170  CB  CYS A 289      11.234  28.649  26.384  1.00 87.94           C  
ANISOU 2170  CB  CYS A 289    11131  13369   8915   1506   -566  -2282       C  
ATOM   2171  SG  CYS A 289      10.378  30.230  26.215  1.00 97.73           S  
ANISOU 2171  SG  CYS A 289    12376  14535  10221   1576   -640  -2475       S  
ATOM   2172  N   ILE A 290      13.706  28.053  24.604  1.00 73.12           N  
ANISOU 2172  N   ILE A 290     9296  11130   7357   1207   -638  -2172       N  
ATOM   2173  CA  ILE A 290      14.856  28.492  23.820  1.00 67.74           C  
ANISOU 2173  CA  ILE A 290     8632  10254   6853   1098   -725  -2218       C  
ATOM   2174  C   ILE A 290      14.852  27.839  22.444  1.00 66.23           C  
ANISOU 2174  C   ILE A 290     8452   9914   6797    938   -646  -2052       C  
ATOM   2175  O   ILE A 290      15.289  28.444  21.457  1.00 65.25           O  
ANISOU 2175  O   ILE A 290     8343   9603   6848    839   -695  -2082       O  
ATOM   2176  CB  ILE A 290      16.160  28.200  24.592  1.00 69.75           C  
ANISOU 2176  CB  ILE A 290     8880  10572   7051   1128   -796  -2261       C  
ATOM   2177  CG1 ILE A 290      16.178  28.976  25.911  1.00 76.42           C  
ANISOU 2177  CG1 ILE A 290     9714  11553   7769   1291   -890  -2449       C  
ATOM   2178  CG2 ILE A 290      17.381  28.556  23.758  1.00 67.94           C  
ANISOU 2178  CG2 ILE A 290     8658  10149   7006   1007   -876  -2290       C  
ATOM   2179  CD1 ILE A 290      17.454  28.804  26.708  1.00 79.64           C  
ANISOU 2179  CD1 ILE A 290    10113  12026   8121   1331   -975  -2512       C  
ATOM   2180  N   ALA A 291      14.348  26.607  22.347  1.00 65.41           N  
ANISOU 2180  N   ALA A 291     8342   9892   6620    913   -524  -1874       N  
ATOM   2181  CA  ALA A 291      14.249  25.959  21.045  1.00 66.52           C  
ANISOU 2181  CA  ALA A 291     8494   9899   6882    771   -449  -1722       C  
ATOM   2182  C   ALA A 291      13.183  26.609  20.174  1.00 77.95           C  
ANISOU 2182  C   ALA A 291     9948  11247   8422    735   -423  -1731       C  
ATOM   2183  O   ALA A 291      13.299  26.598  18.943  1.00 79.31           O  
ANISOU 2183  O   ALA A 291    10135  11258   8740    616   -408  -1670       O  
ATOM   2184  CB  ALA A 291      13.957  24.469  21.218  1.00 59.84           C  
ANISOU 2184  CB  ALA A 291     7640   9163   5936    758   -332  -1536       C  
ATOM   2185  N   GLU A 292      12.148  27.181  20.786  1.00 78.27           N  
ANISOU 2185  N   GLU A 292     9976  11386   8378    841   -419  -1808       N  
ATOM   2186  CA  GLU A 292      11.054  27.806  20.058  1.00 74.22           C  
ANISOU 2186  CA  GLU A 292     9465  10797   7937    823   -395  -1822       C  
ATOM   2187  C   GLU A 292      11.119  29.328  20.084  1.00 73.27           C  
ANISOU 2187  C   GLU A 292     9358  10587   7895    870   -510  -2014       C  
ATOM   2188  O   GLU A 292      10.134  29.985  19.735  1.00 77.78           O  
ANISOU 2188  O   GLU A 292     9929  11123   8500    892   -502  -2054       O  
ATOM   2189  CB  GLU A 292       9.710  27.331  20.615  1.00 73.44           C  
ANISOU 2189  CB  GLU A 292     9339  10869   7697    904   -296  -1757       C  
ATOM   2190  CG  GLU A 292       9.423  25.858  20.367  1.00 82.46           C  
ANISOU 2190  CG  GLU A 292    10469  12068   8796    838   -175  -1550       C  
ATOM   2191  CD  GLU A 292       9.087  25.564  18.915  1.00 88.67           C  
ANISOU 2191  CD  GLU A 292    11267  12694   9729    701   -124  -1441       C  
ATOM   2192  OE1 GLU A 292      10.026  25.412  18.104  1.00 88.59           O  
ANISOU 2192  OE1 GLU A 292    11282  12540   9838    597   -153  -1411       O  
ATOM   2193  OE2 GLU A 292       7.885  25.484  18.585  1.00 90.76           O  
ANISOU 2193  OE2 GLU A 292    11514  12982   9988    700    -55  -1387       O  
ATOM   2194  N   VAL A 293      12.252  29.902  20.492  1.00 65.99           N  
ANISOU 2194  N   VAL A 293     8445   9624   7006    887   -622  -2136       N  
ATOM   2195  CA  VAL A 293      12.397  31.351  20.461  1.00 70.38           C  
ANISOU 2195  CA  VAL A 293     9014  10070   7657    920   -741  -2318       C  
ATOM   2196  C   VAL A 293      12.485  31.815  19.013  1.00 78.41           C  
ANISOU 2196  C   VAL A 293    10052  10865   8877    787   -752  -2280       C  
ATOM   2197  O   VAL A 293      13.031  31.119  18.146  1.00 74.14           O  
ANISOU 2197  O   VAL A 293     9516  10239   8415    664   -707  -2150       O  
ATOM   2198  CB  VAL A 293      13.627  31.792  21.277  1.00 78.48           C  
ANISOU 2198  CB  VAL A 293    10039  11108   8671    965   -862  -2454       C  
ATOM   2199  CG1 VAL A 293      14.920  31.435  20.559  1.00 71.68           C  
ANISOU 2199  CG1 VAL A 293     9183  10116   7936    832   -887  -2387       C  
ATOM   2200  CG2 VAL A 293      13.572  33.284  21.569  1.00 86.37           C  
ANISOU 2200  CG2 VAL A 293    11048  12036   9731   1038   -989  -2663       C  
ATOM   2201  N   GLU A 294      11.915  32.981  18.736  1.00 81.94           N  
ANISOU 2201  N   GLU A 294    10510  11220   9402    815   -808  -2390       N  
ATOM   2202  CA  GLU A 294      11.998  33.557  17.405  1.00 83.90           C  
ANISOU 2202  CA  GLU A 294    10780  11258   9842    700   -828  -2364       C  
ATOM   2203  C   GLU A 294      13.279  34.376  17.273  1.00 75.47           C  
ANISOU 2203  C   GLU A 294     9721  10044   8909    651   -953  -2468       C  
ATOM   2204  O   GLU A 294      13.956  34.685  18.256  1.00 68.04           O  
ANISOU 2204  O   GLU A 294     8773   9163   7917    721  -1039  -2589       O  
ATOM   2205  CB  GLU A 294      10.763  34.409  17.111  1.00 96.14           C  
ANISOU 2205  CB  GLU A 294    12338  12769  11422    750   -828  -2422       C  
ATOM   2206  CG  GLU A 294       9.449  33.697  17.402  1.00108.22           C  
ANISOU 2206  CG  GLU A 294    13847  14462  12809    815   -712  -2340       C  
ATOM   2207  CD  GLU A 294       8.491  33.724  16.225  1.00116.55           C  
ANISOU 2207  CD  GLU A 294    14908  15425  13951    748   -646  -2247       C  
ATOM   2208  OE1 GLU A 294       8.159  32.639  15.703  1.00118.51           O  
ANISOU 2208  OE1 GLU A 294    15146  15708  14175    678   -539  -2083       O  
ATOM   2209  OE2 GLU A 294       8.068  34.829  15.827  1.00119.71           O  
ANISOU 2209  OE2 GLU A 294    15324  15717  14445    767   -704  -2338       O  
ATOM   2210  N   ASN A 295      13.612  34.722  16.032  1.00 67.23           N  
ANISOU 2210  N   ASN A 295     8692   8812   8039    527   -964  -2415       N  
ATOM   2211  CA  ASN A 295      14.872  35.399  15.759  1.00 66.64           C  
ANISOU 2211  CA  ASN A 295     8620   8591   8110    458  -1071  -2482       C  
ATOM   2212  C   ASN A 295      14.927  36.751  16.456  1.00 69.03           C  
ANISOU 2212  C   ASN A 295     8929   8851   8450    546  -1206  -2688       C  
ATOM   2213  O   ASN A 295      13.917  37.448  16.585  1.00 76.69           O  
ANISOU 2213  O   ASN A 295     9912   9820   9407    624  -1219  -2765       O  
ATOM   2214  CB  ASN A 295      15.060  35.581  14.253  1.00 60.22           C  
ANISOU 2214  CB  ASN A 295     7819   7590   7473    317  -1049  -2379       C  
ATOM   2215  CG  ASN A 295      14.847  34.297  13.482  1.00 56.97           C  
ANISOU 2215  CG  ASN A 295     7405   7214   7026    237   -918  -2185       C  
ATOM   2216  OD1 ASN A 295      15.084  33.205  13.998  1.00 45.64           O  
ANISOU 2216  OD1 ASN A 295     5957   5911   5474    252   -860  -2117       O  
ATOM   2217  ND2 ASN A 295      14.396  34.421  12.239  1.00 62.65           N  
ANISOU 2217  ND2 ASN A 295     8140   7815   7851    155   -873  -2096       N  
ATOM   2218  N   ASP A 296      16.122  37.115  16.915  1.00 68.66           N  
ANISOU 2218  N   ASP A 296     8870   8767   8450    536  -1310  -2781       N  
ATOM   2219  CA  ASP A 296      16.343  38.431  17.488  1.00 64.37           C  
ANISOU 2219  CA  ASP A 296     8333   8153   7972    603  -1455  -2981       C  
ATOM   2220  C   ASP A 296      16.171  39.505  16.416  1.00 67.92           C  
ANISOU 2220  C   ASP A 296     8803   8382   8623    526  -1502  -2996       C  
ATOM   2221  O   ASP A 296      16.075  39.221  15.218  1.00 68.97           O  
ANISOU 2221  O   ASP A 296     8943   8416   8848    413  -1429  -2850       O  
ATOM   2222  CB  ASP A 296      17.738  38.514  18.107  1.00 57.71           C  
ANISOU 2222  CB  ASP A 296     7467   7309   7153    590  -1556  -3063       C  
ATOM   2223  CG  ASP A 296      17.874  39.660  19.091  1.00 71.33           C  
ANISOU 2223  CG  ASP A 296     9195   9026   8883    700  -1705  -3291       C  
ATOM   2224  OD1 ASP A 296      17.138  39.668  20.100  1.00 67.33           O  
ANISOU 2224  OD1 ASP A 296     8691   8675   8214    847  -1705  -3383       O  
ATOM   2225  OD2 ASP A 296      18.717  40.551  18.855  1.00 74.16           O  
ANISOU 2225  OD2 ASP A 296     9548   9222   9406    640  -1823  -3378       O  
ATOM   2226  N   GLU A 297      16.388  40.767  16.788  1.00 70.38           N  
ANISOU 2226  N   GLU A 297     9126   8615   9000    594  -1629  -3176       N  
ATOM   2227  CA  GLU A 297      16.355  41.861  15.788  1.00 82.44           C  
ANISOU 2227  CA  GLU A 297    10674   9921  10729    525  -1692  -3201       C  
ATOM   2228  C   GLU A 297      17.608  41.834  14.917  1.00 80.05           C  
ANISOU 2228  C   GLU A 297    10356   9465  10596    364  -1716  -3115       C  
ATOM   2229  O   GLU A 297      18.690  41.627  15.443  1.00 80.02           O  
ANISOU 2229  O   GLU A 297    10326   9471  10607    342  -1783  -3164       O  
ATOM   2230  CB  GLU A 297      16.201  43.229  16.448  1.00 96.15           C  
ANISOU 2230  CB  GLU A 297    12424  11599  12511    630  -1840  -3424       C  
ATOM   2231  CG  GLU A 297      14.891  43.909  16.100  1.00108.29           C  
ANISOU 2231  CG  GLU A 297    13993  13043  14109    675  -1847  -3463       C  
ATOM   2232  CD  GLU A 297      14.872  44.624  14.759  1.00117.14           C  
ANISOU 2232  CD  GLU A 297    15127  13921  15461    541  -1877  -3391       C  
ATOM   2233  OE1 GLU A 297      13.765  44.839  14.225  1.00118.31           O  
ANISOU 2233  OE1 GLU A 297    15301  13994  15659    541  -1842  -3354       O  
ATOM   2234  OE2 GLU A 297      15.961  44.971  14.256  1.00119.54           O  
ANISOU 2234  OE2 GLU A 297    15410  14118  15892    439  -1930  -3358       O  
ATOM   2235  N   MET A 298      17.432  41.999  13.601  1.00 80.68           N  
ANISOU 2235  N   MET A 298    10447   9411  10796    256  -1657  -2982       N  
ATOM   2236  CA  MET A 298      18.577  41.984  12.650  1.00 88.80           C  
ANISOU 2236  CA  MET A 298    11458  10298  11983    103  -1666  -2882       C  
ATOM   2237  C   MET A 298      19.462  43.203  12.924  1.00103.73           C  
ANISOU 2237  C   MET A 298    13335  12054  14023     82  -1824  -3026       C  
ATOM   2238  O   MET A 298      18.905  44.310  13.069  1.00111.35           O  
ANISOU 2238  O   MET A 298    14320  12945  15044    150  -1915  -3157       O  
ATOM   2239  CB  MET A 298      18.060  42.052  11.209  1.00 86.03           C  
ANISOU 2239  CB  MET A 298    11127   9814  11745     13  -1598  -2747       C  
ATOM   2240  CG  MET A 298      18.866  41.227  10.227  1.00 82.93           C  
ANISOU 2240  CG  MET A 298    10716   9269  11523   -143  -1604  -2638       C  
ATOM   2241  SD  MET A 298      19.109  42.104   8.663  1.00 88.22           S  
ANISOU 2241  SD  MET A 298    11393   9939  12187   -244  -1443  -2400       S  
ATOM   2242  CE  MET A 298      20.763  42.751   8.899  1.00 88.12           C  
ANISOU 2242  CE  MET A 298    11421   9786  12275   -232  -1450  -2402       C  
ATOM   2243  N   ASP A 301      23.052  48.038  10.845  1.00 96.73           N  
ANISOU 2243  N   ASP A 301    12352  10357  14043   -339  -2151  -2904       N  
ATOM   2244  CA  ASP A 301      23.881  48.185   9.627  1.00 94.06           C  
ANISOU 2244  CA  ASP A 301    11991   9896  13852   -489  -2110  -2741       C  
ATOM   2245  C   ASP A 301      25.164  47.379   9.728  1.00 89.60           C  
ANISOU 2245  C   ASP A 301    11370   9386  13289   -568  -2107  -2701       C  
ATOM   2246  O   ASP A 301      25.794  47.446  10.794  1.00 80.78           O  
ANISOU 2246  O   ASP A 301    10221   8317  12153   -531  -2188  -2807       O  
ATOM   2247  CB  ASP A 301      24.186  49.644   9.281  1.00101.68           C  
ANISOU 2247  CB  ASP A 301    12952  10691  14989   -525  -2180  -2735       C  
ATOM   2248  CG  ASP A 301      22.974  50.557   9.250  1.00103.46           C  
ANISOU 2248  CG  ASP A 301    13233  10847  15232   -460  -2178  -2752       C  
ATOM   2249  OD1 ASP A 301      22.085  50.323   8.414  1.00102.82           O  
ANISOU 2249  OD1 ASP A 301    13187  10862  15017   -351  -2155  -2827       O  
ATOM   2250  OD2 ASP A 301      22.938  51.499  10.064  1.00104.35           O  
ANISOU 2250  OD2 ASP A 301    13348  10810  15488   -515  -2199  -2690       O  
ATOM   2251  N   LEU A 302      25.490  46.621   8.669  1.00 88.87           N  
ANISOU 2251  N   LEU A 302    11263   9290  13215   -672  -2016  -2548       N  
ATOM   2252  CA  LEU A 302      26.726  45.863   8.584  1.00 76.56           C  
ANISOU 2252  CA  LEU A 302     9648   7778  11664   -756  -2000  -2488       C  
ATOM   2253  C   LEU A 302      27.490  46.239   7.322  1.00 71.51           C  
ANISOU 2253  C   LEU A 302     8975   7016  11180   -896  -1964  -2326       C  
ATOM   2254  O   LEU A 302      26.888  46.658   6.328  1.00 77.63           O  
ANISOU 2254  O   LEU A 302     9779   7698  12017   -931  -1913  -2229       O  
ATOM   2255  CB  LEU A 302      26.465  44.351   8.565  1.00 78.77           C  
ANISOU 2255  CB  LEU A 302     9932   8195  11802   -746  -1917  -2452       C  
ATOM   2256  CG  LEU A 302      26.460  43.610   9.899  1.00 79.58           C  
ANISOU 2256  CG  LEU A 302    10032   8462  11743   -641  -1953  -2589       C  
ATOM   2257  CD1 LEU A 302      25.072  43.664  10.484  1.00 81.14           C  
ANISOU 2257  CD1 LEU A 302    10287   8722  11820   -511  -1949  -2688       C  
ATOM   2258  CD2 LEU A 302      26.908  42.170   9.714  1.00 76.85           C  
ANISOU 2258  CD2 LEU A 302     9660   8224  11316   -685  -1886  -2519       C  
ATOM   2259  N   PRO A 303      28.816  46.104   7.331  1.00 62.97           N  
ANISOU 2259  N   PRO A 303     7830   5937  10157   -973  -1986  -2291       N  
ATOM   2260  CA  PRO A 303      29.580  46.272   6.091  1.00 69.92           C  
ANISOU 2260  CA  PRO A 303     8673   6730  11165  -1106  -1934  -2123       C  
ATOM   2261  C   PRO A 303      29.104  45.314   5.007  1.00 66.57           C  
ANISOU 2261  C   PRO A 303     8266   6334  10692  -1151  -1809  -1978       C  
ATOM   2262  O   PRO A 303      28.456  44.299   5.274  1.00 57.32           O  
ANISOU 2262  O   PRO A 303     7122   5264   9392  -1098  -1764  -2003       O  
ATOM   2263  CB  PRO A 303      31.020  45.960   6.516  1.00 71.91           C  
ANISOU 2263  CB  PRO A 303     8850   7028  11443  -1158  -1976  -2134       C  
ATOM   2264  CG  PRO A 303      31.057  46.274   7.972  1.00 72.80           C  
ANISOU 2264  CG  PRO A 303     8965   7194  11502  -1057  -2085  -2322       C  
ATOM   2265  CD  PRO A 303      29.688  45.958   8.511  1.00 63.05           C  
ANISOU 2265  CD  PRO A 303     7799   6028  10130   -936  -2071  -2412       C  
ATOM   2266  N   SER A 304      29.434  45.657   3.764  1.00 71.65           N  
ANISOU 2266  N   SER A 304     8894   6889  11441  -1250  -1753  -1823       N  
ATOM   2267  CA  SER A 304      29.043  44.834   2.630  1.00 71.13           C  
ANISOU 2267  CA  SER A 304     8842   6843  11339  -1296  -1634  -1674       C  
ATOM   2268  C   SER A 304      29.711  43.475   2.723  1.00 76.22           C  
ANISOU 2268  C   SER A 304     9446   7606  11908  -1325  -1588  -1640       C  
ATOM   2269  O   SER A 304      30.918  43.378   2.972  1.00 84.82           O  
ANISOU 2269  O   SER A 304    10472   8718  13037  -1374  -1621  -1639       O  
ATOM   2270  CB  SER A 304      29.436  45.518   1.324  1.00 71.21           C  
ANISOU 2270  CB  SER A 304     8835   6748  11473  -1392  -1589  -1516       C  
ATOM   2271  OG  SER A 304      30.847  45.520   1.143  1.00 72.03           O  
ANISOU 2271  OG  SER A 304     8865   6853  11651  -1478  -1599  -1457       O  
ATOM   2272  N   LEU A 305      28.924  42.418   2.522  1.00 69.94           N  
ANISOU 2272  N   LEU A 305     8685   6884  11006  -1295  -1514  -1613       N  
ATOM   2273  CA  LEU A 305      29.510  41.089   2.621  1.00 72.91           C  
ANISOU 2273  CA  LEU A 305     9023   7370  11309  -1318  -1473  -1583       C  
ATOM   2274  C   LEU A 305      30.378  40.770   1.413  1.00 69.14           C  
ANISOU 2274  C   LEU A 305     8497   6874  10900  -1426  -1395  -1408       C  
ATOM   2275  O   LEU A 305      31.179  39.828   1.462  1.00 65.42           O  
ANISOU 2275  O   LEU A 305     7977   6482  10399  -1459  -1372  -1377       O  
ATOM   2276  CB  LEU A 305      28.443  40.010   2.813  1.00 78.26           C  
ANISOU 2276  CB  LEU A 305     9754   8166  11814  -1235  -1392  -1582       C  
ATOM   2277  CG  LEU A 305      28.975  38.738   3.473  1.00 79.69           C  
ANISOU 2277  CG  LEU A 305     9913   8519  11847  -1196  -1350  -1579       C  
ATOM   2278  CD1 LEU A 305      29.725  39.142   4.714  1.00 85.45           C  
ANISOU 2278  CD1 LEU A 305    10606   9269  12594  -1165  -1472  -1732       C  
ATOM   2279  CD2 LEU A 305      27.861  37.744   3.794  1.00 74.92           C  
ANISOU 2279  CD2 LEU A 305     9367   8048  11051  -1099  -1262  -1569       C  
ATOM   2280  N   ALA A 306      30.249  41.541   0.336  1.00 70.28           N  
ANISOU 2280  N   ALA A 306     8653   6922  11130  -1478  -1355  -1295       N  
ATOM   2281  CA  ALA A 306      31.113  41.336  -0.814  1.00 69.81           C  
ANISOU 2281  CA  ALA A 306     8543   6853  11128  -1573  -1283  -1131       C  
ATOM   2282  C   ALA A 306      32.543  41.787  -0.549  1.00 63.05           C  
ANISOU 2282  C   ALA A 306     7610   5986  10360  -1632  -1339  -1136       C  
ATOM   2283  O   ALA A 306      33.458  41.383  -1.279  1.00 69.98           O  
ANISOU 2283  O   ALA A 306     8431   6890  11268  -1705  -1285  -1018       O  
ATOM   2284  CB  ALA A 306      30.562  42.073  -2.037  1.00 68.64           C  
ANISOU 2284  CB  ALA A 306     8429   6614  11037  -1604  -1226  -1011       C  
ATOM   2285  N   ALA A 307      32.765  42.602   0.478  1.00 60.39           N  
ANISOU 2285  N   ALA A 307     7266   5615  10063  -1599  -1449  -1271       N  
ATOM   2286  CA  ALA A 307      34.101  43.147   0.683  1.00 60.63           C  
ANISOU 2286  CA  ALA A 307     7223   5623  10192  -1659  -1507  -1273       C  
ATOM   2287  C   ALA A 307      35.071  42.071   1.161  1.00 61.33           C  
ANISOU 2287  C   ALA A 307     7247   5825  10231  -1674  -1509  -1290       C  
ATOM   2288  O   ALA A 307      36.177  41.946   0.627  1.00 56.15           O  
ANISOU 2288  O   ALA A 307     6519   5180   9634  -1753  -1483  -1195       O  
ATOM   2289  CB  ALA A 307      34.057  44.323   1.660  1.00 65.83           C  
ANISOU 2289  CB  ALA A 307     7892   6211  10909  -1615  -1628  -1418       C  
ATOM   2290  N   ASP A 308      34.670  41.267   2.151  1.00 63.63           N  
ANISOU 2290  N   ASP A 308     7560   6207  10409  -1597  -1538  -1406       N  
ATOM   2291  CA  ASP A 308      35.571  40.265   2.716  1.00 56.90           C  
ANISOU 2291  CA  ASP A 308     6647   5467   9507  -1601  -1553  -1436       C  
ATOM   2292  C   ASP A 308      35.531  38.925   1.989  1.00 53.06           C  
ANISOU 2292  C   ASP A 308     6151   5058   8953  -1625  -1447  -1323       C  
ATOM   2293  O   ASP A 308      36.491  38.154   2.097  1.00 49.21           O  
ANISOU 2293  O   ASP A 308     5599   4654   8446  -1650  -1437  -1297       O  
ATOM   2294  CB  ASP A 308      35.255  40.034   4.200  1.00 56.17           C  
ANISOU 2294  CB  ASP A 308     6577   5448   9317  -1499  -1642  -1622       C  
ATOM   2295  CG  ASP A 308      35.772  41.150   5.091  1.00 72.38           C  
ANISOU 2295  CG  ASP A 308     8609   7455  11436  -1479  -1760  -1743       C  
ATOM   2296  OD1 ASP A 308      36.406  42.088   4.563  1.00 78.16           O  
ANISOU 2296  OD1 ASP A 308     9307   8093  12299  -1551  -1776  -1682       O  
ATOM   2297  OD2 ASP A 308      35.547  41.091   6.320  1.00 75.41           O  
ANISOU 2297  OD2 ASP A 308     9011   7902  11740  -1388  -1838  -1898       O  
ATOM   2298  N   PHE A 309      34.459  38.627   1.253  1.00 43.27           N  
ANISOU 2298  N   PHE A 309     4974   3801   7666  -1611  -1363  -1250       N  
ATOM   2299  CA  PHE A 309      34.289  37.316   0.646  1.00 41.83           C  
ANISOU 2299  CA  PHE A 309     4811   3737   7346  -1589  -1229  -1127       C  
ATOM   2300  C   PHE A 309      34.258  37.320  -0.877  1.00 47.99           C  
ANISOU 2300  C   PHE A 309     5586   4460   8189  -1666  -1135   -958       C  
ATOM   2301  O   PHE A 309      34.370  36.243  -1.475  1.00 45.84           O  
ANISOU 2301  O   PHE A 309     5313   4281   7822  -1661  -1031   -851       O  
ATOM   2302  CB  PHE A 309      33.002  36.650   1.165  1.00 50.64           C  
ANISOU 2302  CB  PHE A 309     6014   4938   8287  -1477  -1182  -1173       C  
ATOM   2303  CG  PHE A 309      33.019  36.357   2.642  1.00 48.12           C  
ANISOU 2303  CG  PHE A 309     5703   4717   7864  -1386  -1249  -1318       C  
ATOM   2304  CD1 PHE A 309      33.758  35.298   3.142  1.00 53.13           C  
ANISOU 2304  CD1 PHE A 309     6305   5484   8397  -1358  -1227  -1310       C  
ATOM   2305  CD2 PHE A 309      32.296  37.138   3.528  1.00 44.33           C  
ANISOU 2305  CD2 PHE A 309     5263   4200   7382  -1322  -1335  -1462       C  
ATOM   2306  CE1 PHE A 309      33.779  35.026   4.498  1.00 47.45           C  
ANISOU 2306  CE1 PHE A 309     5592   4861   7575  -1271  -1287  -1436       C  
ATOM   2307  CE2 PHE A 309      32.314  36.869   4.886  1.00 44.39           C  
ANISOU 2307  CE2 PHE A 309     5276   4308   7283  -1231  -1394  -1594       C  
ATOM   2308  CZ  PHE A 309      33.057  35.813   5.370  1.00 41.96           C  
ANISOU 2308  CZ  PHE A 309     4935   4135   6873  -1206  -1370  -1578       C  
ATOM   2309  N   VAL A 310      34.117  38.480  -1.525  1.00 48.42           N  
ANISOU 2309  N   VAL A 310     5641   4380   8375  -1722  -1158   -922       N  
ATOM   2310  CA  VAL A 310      33.944  38.562  -2.970  1.00 55.83           C  
ANISOU 2310  CA  VAL A 310     6590   5284   9338  -1771  -1058   -756       C  
ATOM   2311  C   VAL A 310      34.991  39.460  -3.618  1.00 60.95           C  
ANISOU 2311  C   VAL A 310     7179   5880  10100  -1847  -1061   -671       C  
ATOM   2312  O   VAL A 310      35.679  39.052  -4.558  1.00 60.43           O  
ANISOU 2312  O   VAL A 310     7066   5849  10046  -1903   -986   -538       O  
ATOM   2313  CB  VAL A 310      32.519  39.033  -3.343  1.00 57.76           C  
ANISOU 2313  CB  VAL A 310     6923   5464   9560  -1726  -1034   -755       C  
ATOM   2314  CG1 VAL A 310      32.363  39.104  -4.857  1.00 57.90           C  
ANISOU 2314  CG1 VAL A 310     6950   5456   9593  -1771   -933   -585       C  
ATOM   2315  CG2 VAL A 310      31.470  38.112  -2.732  1.00 55.57           C  
ANISOU 2315  CG2 VAL A 310     6704   5257   9152  -1644  -1017   -829       C  
ATOM   2316  N   GLU A 311      35.117  40.699  -3.141  1.00 61.42           N  
ANISOU 2316  N   GLU A 311     7238   5855  10244  -1849  -1146   -744       N  
ATOM   2317  CA  GLU A 311      35.944  41.685  -3.824  1.00 63.05           C  
ANISOU 2317  CA  GLU A 311     7396   5992  10567  -1922  -1149   -658       C  
ATOM   2318  C   GLU A 311      37.368  41.778  -3.288  1.00 60.29           C  
ANISOU 2318  C   GLU A 311     6955   5670  10284  -1971  -1208   -688       C  
ATOM   2319  O   GLU A 311      38.223  42.356  -3.966  1.00 64.28           O  
ANISOU 2319  O   GLU A 311     7403   6140  10879  -2042  -1193   -594       O  
ATOM   2320  CB  GLU A 311      35.289  43.070  -3.757  1.00 62.91           C  
ANISOU 2320  CB  GLU A 311     7428   5851  10622  -1905  -1206   -703       C  
ATOM   2321  CG  GLU A 311      33.783  43.058  -3.966  1.00 77.04           C  
ANISOU 2321  CG  GLU A 311     9311   7615  12347  -1840  -1175   -716       C  
ATOM   2322  CD  GLU A 311      33.108  44.253  -3.329  1.00 88.71           C  
ANISOU 2322  CD  GLU A 311    10836   8992  13877  -1794  -1265   -828       C  
ATOM   2323  OE1 GLU A 311      32.048  44.682  -3.832  1.00 89.19           O  
ANISOU 2323  OE1 GLU A 311    10960   8997  13931  -1763  -1239   -802       O  
ATOM   2324  OE2 GLU A 311      33.645  44.770  -2.327  1.00 92.12           O  
ANISOU 2324  OE2 GLU A 311    11241   9404  14357  -1785  -1364   -944       O  
ATOM   2325  N   SER A 312      37.649  41.231  -2.108  1.00 62.51           N  
ANISOU 2325  N   SER A 312     7216   6015  10519  -1933  -1275   -815       N  
ATOM   2326  CA  SER A 312      39.003  41.283  -1.576  1.00 62.32           C  
ANISOU 2326  CA  SER A 312     7101   6024  10553  -1975  -1335   -848       C  
ATOM   2327  C   SER A 312      39.940  40.414  -2.407  1.00 63.64           C  
ANISOU 2327  C   SER A 312     7193   6272  10715  -2036  -1249   -712       C  
ATOM   2328  O   SER A 312      39.532  39.413  -3.003  1.00 69.54           O  
ANISOU 2328  O   SER A 312     7960   7081  11380  -2023  -1159   -635       O  
ATOM   2329  CB  SER A 312      39.027  40.828  -0.117  1.00 56.87           C  
ANISOU 2329  CB  SER A 312     6411   5398   9800  -1908  -1426  -1019       C  
ATOM   2330  OG  SER A 312      40.354  40.599   0.323  1.00 57.05           O  
ANISOU 2330  OG  SER A 312     6339   5477   9859  -1946  -1472  -1039       O  
ATOM   2331  N   LYS A 313      41.215  40.802  -2.433  1.00 60.59           N  
ANISOU 2331  N   LYS A 313     6716   5886  10418  -2101  -1280   -685       N  
ATOM   2332  CA  LYS A 313      42.217  40.061  -3.190  1.00 63.67           C  
ANISOU 2332  CA  LYS A 313     7022   6358  10811  -2157  -1204   -559       C  
ATOM   2333  C   LYS A 313      42.746  38.838  -2.451  1.00 59.20           C  
ANISOU 2333  C   LYS A 313     6408   5913  10174  -2130  -1222   -619       C  
ATOM   2334  O   LYS A 313      43.410  38.002  -3.073  1.00 52.99           O  
ANISOU 2334  O   LYS A 313     5559   5207   9367  -2161  -1149   -517       O  
ATOM   2335  CB  LYS A 313      43.392  40.975  -3.553  1.00 63.62           C  
ANISOU 2335  CB  LYS A 313     6931   6308  10933  -2240  -1227   -500       C  
ATOM   2336  CG  LYS A 313      43.061  42.048  -4.574  1.00 66.47           C  
ANISOU 2336  CG  LYS A 313     7322   6565  11369  -2280  -1187   -397       C  
ATOM   2337  CD  LYS A 313      44.241  42.985  -4.784  1.00 68.59           C  
ANISOU 2337  CD  LYS A 313     7502   6785  11772  -2362  -1223   -353       C  
ATOM   2338  CE  LYS A 313      43.876  44.411  -4.417  1.00 77.15           C  
ANISOU 2338  CE  LYS A 313     8627   7731  12955  -2365  -1311   -422       C  
ATOM   2339  NZ  LYS A 313      43.242  44.473  -3.072  1.00 81.25           N  
ANISOU 2339  NZ  LYS A 313     9203   8233  13436  -2290  -1413   -606       N  
ATOM   2340  N   ASP A 314      42.475  38.712  -1.151  1.00 53.47           N  
ANISOU 2340  N   ASP A 314     5706   5204   9404  -2068  -1316   -780       N  
ATOM   2341  CA  ASP A 314      43.007  37.628  -0.337  1.00 46.96           C  
ANISOU 2341  CA  ASP A 314     4834   4495   8515  -2036  -1348   -852       C  
ATOM   2342  C   ASP A 314      41.981  36.532  -0.071  1.00 45.38           C  
ANISOU 2342  C   ASP A 314     4702   4353   8187  -1962  -1314   -889       C  
ATOM   2343  O   ASP A 314      42.156  35.748   0.869  1.00 49.82           O  
ANISOU 2343  O   ASP A 314     5270   5031   8627  -1883  -1334   -970       O  
ATOM   2344  CB  ASP A 314      43.528  38.176   0.990  1.00 52.50           C  
ANISOU 2344  CB  ASP A 314     5507   5195   9246  -2010  -1483  -1012       C  
ATOM   2345  CG  ASP A 314      44.483  39.335   0.808  1.00 61.64           C  
ANISOU 2345  CG  ASP A 314     6600   6282  10539  -2084  -1528   -987       C  
ATOM   2346  OD1 ASP A 314      44.904  39.596  -0.339  1.00 65.78           O  
ANISOU 2346  OD1 ASP A 314     7087   6777  11130  -2158  -1451   -839       O  
ATOM   2347  OD2 ASP A 314      44.805  39.990   1.819  1.00 59.73           O  
ANISOU 2347  OD2 ASP A 314     6345   6016  10334  -2065  -1640  -1116       O  
ATOM   2348  N   VAL A 315      40.916  36.464  -0.872  1.00 44.64           N  
ANISOU 2348  N   VAL A 315     4688   4221   8053  -1948  -1229   -812       N  
ATOM   2349  CA  VAL A 315      39.874  35.465  -0.644  1.00 44.95           C  
ANISOU 2349  CA  VAL A 315     4826   4353   7900  -1840  -1156   -824       C  
ATOM   2350  C   VAL A 315      40.455  34.059  -0.728  1.00 49.30           C  
ANISOU 2350  C   VAL A 315     5354   5058   8320  -1801  -1075   -759       C  
ATOM   2351  O   VAL A 315      40.182  33.203   0.122  1.00 43.54           O  
ANISOU 2351  O   VAL A 315     4666   4433   7445  -1709  -1072   -825       O  
ATOM   2352  CB  VAL A 315      38.717  35.656  -1.641  1.00 42.15           C  
ANISOU 2352  CB  VAL A 315     4549   3929   7538  -1844  -1077   -738       C  
ATOM   2353  CG1 VAL A 315      37.736  34.498  -1.542  1.00 42.76           C  
ANISOU 2353  CG1 VAL A 315     4715   4110   7422  -1744   -990   -729       C  
ATOM   2354  CG2 VAL A 315      38.014  36.980  -1.393  1.00 47.18           C  
ANISOU 2354  CG2 VAL A 315     5222   4420   8285  -1860  -1163   -821       C  
ATOM   2355  N   CYS A 316      41.283  33.802  -1.744  1.00 48.46           N  
ANISOU 2355  N   CYS A 316     5178   4969   8265  -1868  -1009   -627       N  
ATOM   2356  CA  CYS A 316      41.778  32.445  -1.953  1.00 43.73           C  
ANISOU 2356  CA  CYS A 316     4563   4511   7542  -1826   -925   -558       C  
ATOM   2357  C   CYS A 316      42.772  32.037  -0.872  1.00 42.01           C  
ANISOU 2357  C   CYS A 316     4282   4384   7294  -1795   -995   -645       C  
ATOM   2358  O   CYS A 316      42.736  30.900  -0.390  1.00 45.85           O  
ANISOU 2358  O   CYS A 316     4799   4989   7633  -1711   -960   -660       O  
ATOM   2359  CB  CYS A 316      42.401  32.323  -3.346  1.00 47.11           C  
ANISOU 2359  CB  CYS A 316     4931   4940   8031  -1898   -837   -398       C  
ATOM   2360  SG  CYS A 316      41.192  32.376  -4.686  1.00 46.11           S  
ANISOU 2360  SG  CYS A 316     4889   4751   7881  -1904   -730   -281       S  
ATOM   2361  N   LYS A 317      43.656  32.949  -0.465  1.00 46.08           N  
ANISOU 2361  N   LYS A 317     4711   4847   7952  -1861  -1097   -703       N  
ATOM   2362  CA  LYS A 317      44.644  32.583   0.546  1.00 50.96           C  
ANISOU 2362  CA  LYS A 317     5262   5555   8544  -1833  -1169   -787       C  
ATOM   2363  C   LYS A 317      44.000  32.439   1.923  1.00 51.19           C  
ANISOU 2363  C   LYS A 317     5362   5623   8464  -1732  -1241   -940       C  
ATOM   2364  O   LYS A 317      44.377  31.554   2.702  1.00 46.98           O  
ANISOU 2364  O   LYS A 317     4823   5212   7814  -1658  -1250   -984       O  
ATOM   2365  CB  LYS A 317      45.787  33.602   0.564  1.00 58.39           C  
ANISOU 2365  CB  LYS A 317     6083   6428   9675  -1937  -1262   -805       C  
ATOM   2366  CG  LYS A 317      45.453  34.958   1.165  1.00 66.43           C  
ANISOU 2366  CG  LYS A 317     7109   7310  10821  -1973  -1386   -925       C  
ATOM   2367  CD  LYS A 317      46.726  35.747   1.434  1.00 70.02           C  
ANISOU 2367  CD  LYS A 317     7439   7724  11440  -2060  -1489   -962       C  
ATOM   2368  CE  LYS A 317      46.486  36.885   2.413  1.00 76.37           C  
ANISOU 2368  CE  LYS A 317     8286   8452  12280  -2033  -1605  -1106       C  
ATOM   2369  NZ  LYS A 317      45.735  36.447   3.622  1.00 76.30           N  
ANISOU 2369  NZ  LYS A 317     8341   8490  12159  -1929  -1675  -1267       N  
ATOM   2370  N   ASN A 318      43.007  33.277   2.231  1.00 51.09           N  
ANISOU 2370  N   ASN A 318     5417   5514   8480  -1721  -1290  -1018       N  
ATOM   2371  CA  ASN A 318      42.274  33.116   3.482  1.00 55.75           C  
ANISOU 2371  CA  ASN A 318     6079   6151   8950  -1616  -1345  -1155       C  
ATOM   2372  C   ASN A 318      41.484  31.814   3.483  1.00 57.70           C  
ANISOU 2372  C   ASN A 318     6412   6509   9005  -1522  -1238  -1105       C  
ATOM   2373  O   ASN A 318      41.389  31.136   4.513  1.00 58.52           O  
ANISOU 2373  O   ASN A 318     6542   6717   8975  -1429  -1259  -1178       O  
ATOM   2374  CB  ASN A 318      41.343  34.308   3.707  1.00 59.35           C  
ANISOU 2374  CB  ASN A 318     6590   6480   9482  -1622  -1413  -1244       C  
ATOM   2375  CG  ASN A 318      42.097  35.594   3.969  1.00 60.59           C  
ANISOU 2375  CG  ASN A 318     6669   6525   9827  -1702  -1543  -1324       C  
ATOM   2376  OD1 ASN A 318      43.184  35.582   4.546  1.00 68.84           O  
ANISOU 2376  OD1 ASN A 318     7631   7615  10909  -1717  -1616  -1378       O  
ATOM   2377  ND2 ASN A 318      41.527  36.715   3.540  1.00 63.81           N  
ANISOU 2377  ND2 ASN A 318     7102   6783  10361  -1755  -1575  -1333       N  
ATOM   2378  N   TYR A 319      40.915  31.449   2.332  1.00 46.46           N  
ANISOU 2378  N   TYR A 319     5029   5062   7564  -1544  -1126   -977       N  
ATOM   2379  CA  TYR A 319      40.178  30.195   2.225  1.00 42.02           C  
ANISOU 2379  CA  TYR A 319     4541   4591   6832  -1464  -1024   -920       C  
ATOM   2380  C   TYR A 319      41.108  28.994   2.348  1.00 42.83           C  
ANISOU 2380  C   TYR A 319     4601   4821   6851  -1432   -986   -874       C  
ATOM   2381  O   TYR A 319      40.738  27.974   2.940  1.00 52.29           O  
ANISOU 2381  O   TYR A 319     5850   6117   7900  -1343   -954   -887       O  
ATOM   2382  CB  TYR A 319      39.420  30.158   0.898  1.00 40.17           C  
ANISOU 2382  CB  TYR A 319     4353   4295   6614  -1501   -922   -799       C  
ATOM   2383  CG  TYR A 319      38.677  28.871   0.629  1.00 46.29           C  
ANISOU 2383  CG  TYR A 319     5202   5153   7234  -1431   -817   -732       C  
ATOM   2384  CD1 TYR A 319      37.581  28.504   1.399  1.00 54.53           C  
ANISOU 2384  CD1 TYR A 319     6329   6234   8158  -1346   -814   -795       C  
ATOM   2385  CD2 TYR A 319      39.063  28.029  -0.405  1.00 42.44           C  
ANISOU 2385  CD2 TYR A 319     4698   4706   6722  -1450   -721   -606       C  
ATOM   2386  CE1 TYR A 319      36.894  27.330   1.150  1.00 50.49           C  
ANISOU 2386  CE1 TYR A 319     5880   5789   7515  -1290   -721   -729       C  
ATOM   2387  CE2 TYR A 319      38.383  26.854  -0.662  1.00 42.20           C  
ANISOU 2387  CE2 TYR A 319     4735   4740   6560  -1388   -633   -549       C  
ATOM   2388  CZ  TYR A 319      37.301  26.509   0.120  1.00 43.90           C  
ANISOU 2388  CZ  TYR A 319     5030   4982   6666  -1313   -634   -610       C  
ATOM   2389  OH  TYR A 319      36.622  25.341  -0.132  1.00 47.92           O  
ANISOU 2389  OH  TYR A 319     5603   5549   7055  -1258   -550   -550       O  
ATOM   2390  N   ALA A 320      42.320  29.096   1.800  1.00 48.06           N  
ANISOU 2390  N   ALA A 320     5166   5484   7609  -1502   -989   -816       N  
ATOM   2391  CA  ALA A 320      43.255  27.978   1.848  1.00 46.33           C  
ANISOU 2391  CA  ALA A 320     4901   5385   7317  -1471   -953   -769       C  
ATOM   2392  C   ALA A 320      43.925  27.841   3.209  1.00 50.32           C  
ANISOU 2392  C   ALA A 320     5368   5971   7782  -1417  -1050   -885       C  
ATOM   2393  O   ALA A 320      44.345  26.738   3.577  1.00 57.97           O  
ANISOU 2393  O   ALA A 320     6333   7053   8639  -1351  -1023   -869       O  
ATOM   2394  CB  ALA A 320      44.317  28.132   0.758  1.00 54.47           C  
ANISOU 2394  CB  ALA A 320     5835   6401   8461  -1560   -918   -663       C  
ATOM   2395  N   GLU A 321      44.039  28.934   3.967  1.00 45.49           N  
ANISOU 2395  N   GLU A 321     4729   5300   7255  -1440  -1166  -1004       N  
ATOM   2396  CA  GLU A 321      44.698  28.866   5.267  1.00 53.53           C  
ANISOU 2396  CA  GLU A 321     5708   6396   8235  -1386  -1268  -1123       C  
ATOM   2397  C   GLU A 321      43.797  28.269   6.341  1.00 51.80           C  
ANISOU 2397  C   GLU A 321     5582   6255   7846  -1266  -1273  -1199       C  
ATOM   2398  O   GLU A 321      44.290  27.587   7.246  1.00 59.94           O  
ANISOU 2398  O   GLU A 321     6597   7399   8780  -1193  -1306  -1246       O  
ATOM   2399  CB  GLU A 321      45.172  30.256   5.692  1.00 47.97           C  
ANISOU 2399  CB  GLU A 321     4939   5600   7688  -1452  -1398  -1230       C  
ATOM   2400  CG  GLU A 321      46.401  30.746   4.943  1.00 64.05           C  
ANISOU 2400  CG  GLU A 321     6854   7592   9890  -1566  -1415  -1167       C  
ATOM   2401  CD  GLU A 321      46.728  32.195   5.244  1.00 75.73           C  
ANISOU 2401  CD  GLU A 321     8276   8952  11545  -1644  -1542  -1263       C  
ATOM   2402  OE1 GLU A 321      47.375  32.845   4.396  1.00 83.19           O  
ANISOU 2402  OE1 GLU A 321     9140   9817  12653  -1756  -1542  -1192       O  
ATOM   2403  OE2 GLU A 321      46.343  32.683   6.327  1.00 79.76           O  
ANISOU 2403  OE2 GLU A 321     8820   9450  12034  -1591  -1642  -1411       O  
ATOM   2404  N   ALA A 322      42.488  28.513   6.265  1.00 45.68           N  
ANISOU 2404  N   ALA A 322     4899   5426   7032  -1242  -1241  -1209       N  
ATOM   2405  CA  ALA A 322      41.536  27.949   7.225  1.00 55.17           C  
ANISOU 2405  CA  ALA A 322     6187   6704   8071  -1130  -1235  -1268       C  
ATOM   2406  C   ALA A 322      40.222  27.727   6.472  1.00 58.69           C  
ANISOU 2406  C   ALA A 322     6724   7103   8474  -1125  -1133  -1190       C  
ATOM   2407  O   ALA A 322      39.363  28.609   6.428  1.00 67.72           O  
ANISOU 2407  O   ALA A 322     7907   8159   9663  -1139  -1156  -1237       O  
ATOM   2408  CB  ALA A 322      41.351  28.855   8.433  1.00 52.61           C  
ANISOU 2408  CB  ALA A 322     5866   6370   7753  -1089  -1359  -1433       C  
ATOM   2409  N   LYS A 323      40.082  26.534   5.890  1.00 53.92           N  
ANISOU 2409  N   LYS A 323     6149   6557   7783  -1104  -1026  -1074       N  
ATOM   2410  CA  LYS A 323      38.970  26.264   4.983  1.00 47.71           C  
ANISOU 2410  CA  LYS A 323     5435   5723   6969  -1113   -926   -986       C  
ATOM   2411  C   LYS A 323      37.630  26.311   5.708  1.00 47.72           C  
ANISOU 2411  C   LYS A 323     5523   5736   6874  -1039   -927  -1049       C  
ATOM   2412  O   LYS A 323      36.777  27.155   5.409  1.00 47.36           O  
ANISOU 2412  O   LYS A 323     5511   5601   6881  -1064   -933  -1072       O  
ATOM   2413  CB  LYS A 323      39.170  24.908   4.304  1.00 52.60           C  
ANISOU 2413  CB  LYS A 323     6065   6408   7512  -1097   -822   -863       C  
ATOM   2414  CG  LYS A 323      38.334  24.712   3.049  1.00 49.01           C  
ANISOU 2414  CG  LYS A 323     5661   5891   7068  -1131   -723   -758       C  
ATOM   2415  CD  LYS A 323      38.771  23.474   2.281  1.00 62.86           C  
ANISOU 2415  CD  LYS A 323     7411   7701   8771  -1124   -634   -644       C  
ATOM   2416  CE  LYS A 323      40.230  23.566   1.861  1.00 74.18           C  
ANISOU 2416  CE  LYS A 323     8747   9150  10290  -1175   -653   -613       C  
ATOM   2417  NZ  LYS A 323      40.442  24.558   0.769  1.00 75.55           N  
ANISOU 2417  NZ  LYS A 323     8877   9224  10605  -1273   -646   -567       N  
ATOM   2418  N   ASP A 324      37.421  25.401   6.663  1.00 56.91           N  
ANISOU 2418  N   ASP A 324     6719   7013   7891   -946   -919  -1072       N  
ATOM   2419  CA  ASP A 324      36.117  25.301   7.309  1.00 53.82           C  
ANISOU 2419  CA  ASP A 324     6405   6650   7394   -873   -903  -1112       C  
ATOM   2420  C   ASP A 324      35.823  26.509   8.191  1.00 40.50           C  
ANISOU 2420  C   ASP A 324     4717   4932   5739   -851  -1007  -1256       C  
ATOM   2421  O   ASP A 324      34.653  26.855   8.393  1.00 47.15           O  
ANISOU 2421  O   ASP A 324     5617   5754   6545   -816   -997  -1291       O  
ATOM   2422  CB  ASP A 324      36.033  24.008   8.120  1.00 58.68           C  
ANISOU 2422  CB  ASP A 324     7051   7398   7848   -780   -868  -1089       C  
ATOM   2423  CG  ASP A 324      35.798  22.790   7.247  1.00 63.42           C  
ANISOU 2423  CG  ASP A 324     7683   8013   8399   -787   -755   -950       C  
ATOM   2424  OD1 ASP A 324      34.758  22.743   6.557  1.00 64.93           O  
ANISOU 2424  OD1 ASP A 324     7928   8153   8590   -804   -688   -897       O  
ATOM   2425  OD2 ASP A 324      36.655  21.883   7.245  1.00 71.65           O  
ANISOU 2425  OD2 ASP A 324     8698   9119   9407   -772   -736   -899       O  
ATOM   2426  N   VAL A 325      36.858  27.163   8.718  1.00 43.21           N  
ANISOU 2426  N   VAL A 325     4993   5272   6155   -868  -1110  -1345       N  
ATOM   2427  CA  VAL A 325      36.640  28.384   9.487  1.00 48.84           C  
ANISOU 2427  CA  VAL A 325     5701   5939   6915   -851  -1220  -1491       C  
ATOM   2428  C   VAL A 325      36.178  29.511   8.571  1.00 56.57           C  
ANISOU 2428  C   VAL A 325     6688   6766   8042   -934  -1226  -1486       C  
ATOM   2429  O   VAL A 325      35.252  30.261   8.904  1.00 40.70           O  
ANISOU 2429  O   VAL A 325     4721   4710   6032   -903  -1260  -1565       O  
ATOM   2430  CB  VAL A 325      37.917  28.764  10.258  1.00 45.73           C  
ANISOU 2430  CB  VAL A 325     5229   5578   6568   -853  -1335  -1588       C  
ATOM   2431  CG1 VAL A 325      37.772  30.142  10.887  1.00 48.60           C  
ANISOU 2431  CG1 VAL A 325     5583   5869   7013   -850  -1458  -1743       C  
ATOM   2432  CG2 VAL A 325      38.224  27.717  11.318  1.00 55.44           C  
ANISOU 2432  CG2 VAL A 325     6462   6966   7635   -752  -1337  -1607       C  
ATOM   2433  N   PHE A 326      36.812  29.645   7.403  1.00 54.47           N  
ANISOU 2433  N   PHE A 326     6378   6421   7898  -1035  -1192  -1390       N  
ATOM   2434  CA  PHE A 326      36.404  30.667   6.445  1.00 46.60           C  
ANISOU 2434  CA  PHE A 326     5387   5278   7041  -1115  -1190  -1365       C  
ATOM   2435  C   PHE A 326      34.987  30.420   5.946  1.00 39.66           C  
ANISOU 2435  C   PHE A 326     4593   4381   6095  -1087  -1101  -1308       C  
ATOM   2436  O   PHE A 326      34.191  31.359   5.822  1.00 43.63           O  
ANISOU 2436  O   PHE A 326     5128   4792   6656  -1095  -1129  -1355       O  
ATOM   2437  CB  PHE A 326      37.388  30.701   5.274  1.00 49.50           C  
ANISOU 2437  CB  PHE A 326     5687   5589   7532  -1222  -1157  -1253       C  
ATOM   2438  CG  PHE A 326      37.216  31.882   4.367  1.00 47.47           C  
ANISOU 2438  CG  PHE A 326     5419   5178   7438  -1313  -1174  -1230       C  
ATOM   2439  CD1 PHE A 326      37.495  33.161   4.813  1.00 43.18           C  
ANISOU 2439  CD1 PHE A 326     4841   4541   7022  -1347  -1293  -1340       C  
ATOM   2440  CD2 PHE A 326      36.782  31.710   3.063  1.00 46.21           C  
ANISOU 2440  CD2 PHE A 326     5283   4968   7306  -1363  -1074  -1098       C  
ATOM   2441  CE1 PHE A 326      37.340  34.250   3.976  1.00 53.88           C  
ANISOU 2441  CE1 PHE A 326     6189   5749   8535  -1431  -1309  -1310       C  
ATOM   2442  CE2 PHE A 326      36.626  32.793   2.222  1.00 40.72           C  
ANISOU 2442  CE2 PHE A 326     4579   4135   6758  -1443  -1088  -1067       C  
ATOM   2443  CZ  PHE A 326      36.905  34.065   2.679  1.00 41.30           C  
ANISOU 2443  CZ  PHE A 326     4620   4110   6964  -1479  -1205  -1169       C  
ATOM   2444  N   LEU A 327      34.652  29.161   5.653  1.00 38.07           N  
ANISOU 2444  N   LEU A 327     4427   4263   5775  -1053   -998  -1210       N  
ATOM   2445  CA  LEU A 327      33.301  28.843   5.202  1.00 37.09           C  
ANISOU 2445  CA  LEU A 327     4378   4129   5585  -1026   -914  -1156       C  
ATOM   2446  C   LEU A 327      32.284  29.065   6.315  1.00 46.24           C  
ANISOU 2446  C   LEU A 327     5588   5332   6648   -934   -950  -1262       C  
ATOM   2447  O   LEU A 327      31.161  29.513   6.056  1.00 39.42           O  
ANISOU 2447  O   LEU A 327     4773   4417   5788   -924   -929  -1270       O  
ATOM   2448  CB  LEU A 327      33.242  27.402   4.697  1.00 37.62           C  
ANISOU 2448  CB  LEU A 327     4467   4274   5552  -1011   -805  -1033       C  
ATOM   2449  CG  LEU A 327      33.803  27.166   3.294  1.00 44.55           C  
ANISOU 2449  CG  LEU A 327     5316   5100   6511  -1094   -741   -909       C  
ATOM   2450  CD1 LEU A 327      33.791  25.684   2.954  1.00 47.42           C  
ANISOU 2450  CD1 LEU A 327     5702   5548   6767  -1063   -646   -808       C  
ATOM   2451  CD2 LEU A 327      33.022  27.964   2.261  1.00 44.13           C  
ANISOU 2451  CD2 LEU A 327     5290   4931   6545  -1148   -713   -870       C  
ATOM   2452  N   GLY A 328      32.658  28.757   7.558  1.00 47.74           N  
ANISOU 2452  N   GLY A 328     5765   5626   6748   -861  -1003  -1345       N  
ATOM   2453  CA  GLY A 328      31.759  29.011   8.671  1.00 46.15           C  
ANISOU 2453  CA  GLY A 328     5606   5480   6450   -766  -1041  -1452       C  
ATOM   2454  C   GLY A 328      31.499  30.490   8.880  1.00 57.00           C  
ANISOU 2454  C   GLY A 328     6976   6752   7928   -777  -1137  -1574       C  
ATOM   2455  O   GLY A 328      30.369  30.897   9.163  1.00 51.23           O  
ANISOU 2455  O   GLY A 328     6295   6014   7158   -725  -1137  -1625       O  
ATOM   2456  N   MET A 329      32.541  31.314   8.740  1.00 50.55           N  
ANISOU 2456  N   MET A 329     6100   5854   7252   -844  -1223  -1621       N  
ATOM   2457  CA  MET A 329      32.363  32.758   8.848  1.00 47.62           C  
ANISOU 2457  CA  MET A 329     5726   5365   7004   -864  -1322  -1732       C  
ATOM   2458  C   MET A 329      31.455  33.283   7.744  1.00 49.51           C  
ANISOU 2458  C   MET A 329     6003   5484   7322   -915  -1268  -1664       C  
ATOM   2459  O   MET A 329      30.620  34.163   7.982  1.00 48.93           O  
ANISOU 2459  O   MET A 329     5966   5351   7276   -882  -1313  -1749       O  
ATOM   2460  CB  MET A 329      33.720  33.462   8.805  1.00 52.05           C  
ANISOU 2460  CB  MET A 329     6208   5855   7715   -941  -1419  -1775       C  
ATOM   2461  CG  MET A 329      34.555  33.289  10.062  1.00 69.63           C  
ANISOU 2461  CG  MET A 329     8393   8183   9879   -882  -1509  -1887       C  
ATOM   2462  SD  MET A 329      35.975  34.401  10.110  1.00 86.48           S  
ANISOU 2462  SD  MET A 329    10433  10212  12212   -972  -1649  -1971       S  
ATOM   2463  CE  MET A 329      36.911  33.822   8.696  1.00 84.51           C  
ANISOU 2463  CE  MET A 329    10126   9929  12055  -1095  -1556  -1782       C  
ATOM   2464  N   PHE A 330      31.602  32.753   6.527  1.00 39.61           N  
ANISOU 2464  N   PHE A 330     4744   4199   6105   -989  -1174  -1514       N  
ATOM   2465  CA  PHE A 330      30.724  33.152   5.431  1.00 39.37           C  
ANISOU 2465  CA  PHE A 330     4753   4068   6137  -1032  -1116  -1439       C  
ATOM   2466  C   PHE A 330      29.276  32.794   5.735  1.00 42.02           C  
ANISOU 2466  C   PHE A 330     5161   4461   6345   -946  -1062  -1451       C  
ATOM   2467  O   PHE A 330      28.370  33.621   5.575  1.00 41.38           O  
ANISOU 2467  O   PHE A 330     5114   4302   6306   -935  -1080  -1492       O  
ATOM   2468  CB  PHE A 330      31.181  32.490   4.129  1.00 38.11           C  
ANISOU 2468  CB  PHE A 330     4574   3892   6013  -1112  -1021  -1277       C  
ATOM   2469  CG  PHE A 330      30.219  32.665   2.988  1.00 44.58           C  
ANISOU 2469  CG  PHE A 330     5439   4636   6866  -1143   -947  -1188       C  
ATOM   2470  CD1 PHE A 330      30.237  33.819   2.221  1.00 49.63           C  
ANISOU 2470  CD1 PHE A 330     6066   5132   7658  -1215   -982  -1176       C  
ATOM   2471  CD2 PHE A 330      29.299  31.675   2.678  1.00 45.79           C  
ANISOU 2471  CD2 PHE A 330     5643   4857   6898  -1102   -847  -1113       C  
ATOM   2472  CE1 PHE A 330      29.355  33.984   1.172  1.00 46.28           C  
ANISOU 2472  CE1 PHE A 330     5683   4643   7259  -1238   -917  -1092       C  
ATOM   2473  CE2 PHE A 330      28.413  31.836   1.630  1.00 44.99           C  
ANISOU 2473  CE2 PHE A 330     5580   4689   6823  -1128   -784  -1036       C  
ATOM   2474  CZ  PHE A 330      28.443  32.992   0.876  1.00 44.30           C  
ANISOU 2474  CZ  PHE A 330     5483   4468   6883  -1193   -819  -1026       C  
ATOM   2475  N   LEU A 331      29.039  31.554   6.168  1.00 45.32           N  
ANISOU 2475  N   LEU A 331     5598   5013   6608   -885   -994  -1411       N  
ATOM   2476  CA  LEU A 331      27.684  31.126   6.500  1.00 39.65           C  
ANISOU 2476  CA  LEU A 331     4939   4360   5765   -806   -937  -1413       C  
ATOM   2477  C   LEU A 331      27.124  31.925   7.669  1.00 38.92           C  
ANISOU 2477  C   LEU A 331     4863   4289   5635   -721  -1021  -1567       C  
ATOM   2478  O   LEU A 331      25.943  32.292   7.671  1.00 38.11           O  
ANISOU 2478  O   LEU A 331     4803   4171   5507   -679  -1005  -1592       O  
ATOM   2479  CB  LEU A 331      27.680  29.632   6.820  1.00 40.89           C  
ANISOU 2479  CB  LEU A 331     5107   4655   5773   -762   -857  -1338       C  
ATOM   2480  CG  LEU A 331      26.329  28.947   7.014  1.00 42.33           C  
ANISOU 2480  CG  LEU A 331     5344   4913   5828   -696   -778  -1304       C  
ATOM   2481  CD1 LEU A 331      25.394  29.247   5.853  1.00 42.15           C  
ANISOU 2481  CD1 LEU A 331     5353   4797   5866   -741   -721  -1235       C  
ATOM   2482  CD2 LEU A 331      26.538  27.452   7.169  1.00 35.00           C  
ANISOU 2482  CD2 LEU A 331     4419   4096   4784   -674   -702  -1211       C  
ATOM   2483  N   TYR A 332      27.958  32.209   8.670  1.00 39.40           N  
ANISOU 2483  N   TYR A 332     4889   4390   5692   -689  -1115  -1674       N  
ATOM   2484  CA  TYR A 332      27.502  32.984   9.819  1.00 47.73           C  
ANISOU 2484  CA  TYR A 332     5957   5471   6708   -599  -1204  -1834       C  
ATOM   2485  C   TYR A 332      27.142  34.409   9.412  1.00 57.01           C  
ANISOU 2485  C   TYR A 332     7140   6492   8027   -632  -1274  -1906       C  
ATOM   2486  O   TYR A 332      26.095  34.934   9.810  1.00 59.93           O  
ANISOU 2486  O   TYR A 332     7549   6862   8360   -561  -1292  -1983       O  
ATOM   2487  CB  TYR A 332      28.576  32.978  10.909  1.00 48.27           C  
ANISOU 2487  CB  TYR A 332     5981   5612   6746   -563  -1296  -1934       C  
ATOM   2488  CG  TYR A 332      28.588  34.209  11.787  1.00 53.95           C  
ANISOU 2488  CG  TYR A 332     6694   6292   7512   -512  -1430  -2116       C  
ATOM   2489  CD1 TYR A 332      27.704  34.336  12.851  1.00 56.65           C  
ANISOU 2489  CD1 TYR A 332     7070   6727   7726   -389  -1454  -2224       C  
ATOM   2490  CD2 TYR A 332      29.491  35.239  11.558  1.00 46.27           C  
ANISOU 2490  CD2 TYR A 332     5679   5190   6712   -586  -1535  -2181       C  
ATOM   2491  CE1 TYR A 332      27.714  35.458  13.658  1.00 55.62           C  
ANISOU 2491  CE1 TYR A 332     6936   6562   7635   -334  -1582  -2401       C  
ATOM   2492  CE2 TYR A 332      29.507  36.364  12.358  1.00 54.02           C  
ANISOU 2492  CE2 TYR A 332     6655   6126   7744   -540  -1666  -2355       C  
ATOM   2493  CZ  TYR A 332      28.619  36.468  13.406  1.00 55.21           C  
ANISOU 2493  CZ  TYR A 332     6845   6371   7761   -410  -1691  -2469       C  
ATOM   2494  OH  TYR A 332      28.637  37.589  14.200  1.00 57.68           O  
ANISOU 2494  OH  TYR A 332     7155   6639   8121   -356  -1826  -2652       O  
ATOM   2495  N   GLU A 333      27.996  35.049   8.608  1.00 53.94           N  
ANISOU 2495  N   GLU A 333     6716   5972   7809   -737  -1314  -1877       N  
ATOM   2496  CA  GLU A 333      27.728  36.423   8.197  1.00 52.60           C  
ANISOU 2496  CA  GLU A 333     6553   5643   7791   -774  -1386  -1937       C  
ATOM   2497  C   GLU A 333      26.559  36.506   7.223  1.00 53.01           C  
ANISOU 2497  C   GLU A 333     6654   5634   7855   -788  -1302  -1849       C  
ATOM   2498  O   GLU A 333      25.818  37.495   7.232  1.00 44.18           O  
ANISOU 2498  O   GLU A 333     5564   4429   6793   -763  -1351  -1923       O  
ATOM   2499  CB  GLU A 333      28.979  37.045   7.576  1.00 46.80           C  
ANISOU 2499  CB  GLU A 333     5759   4785   7238   -890  -1445  -1912       C  
ATOM   2500  CG  GLU A 333      30.153  37.192   8.535  1.00 53.11           C  
ANISOU 2500  CG  GLU A 333     6503   5623   8055   -882  -1551  -2019       C  
ATOM   2501  CD  GLU A 333      30.009  38.376   9.473  1.00 60.00           C  
ANISOU 2501  CD  GLU A 333     7380   6439   8980   -827  -1690  -2207       C  
ATOM   2502  OE1 GLU A 333      29.097  39.202   9.260  1.00 60.13           O  
ANISOU 2502  OE1 GLU A 333     7438   6362   9047   -809  -1710  -2248       O  
ATOM   2503  OE2 GLU A 333      30.813  38.480  10.424  1.00 57.96           O  
ANISOU 2503  OE2 GLU A 333     7082   6229   8711   -798  -1784  -2317       O  
ATOM   2504  N   TYR A 334      26.374  35.489   6.379  1.00 39.64           N  
ANISOU 2504  N   TYR A 334     4971   3984   6108   -824  -1182  -1697       N  
ATOM   2505  CA  TYR A 334      25.248  35.510   5.451  1.00 40.94           C  
ANISOU 2505  CA  TYR A 334     5180   4100   6276   -834  -1104  -1615       C  
ATOM   2506  C   TYR A 334      23.934  35.226   6.168  1.00 44.12           C  
ANISOU 2506  C   TYR A 334     5629   4599   6535   -723  -1073  -1668       C  
ATOM   2507  O   TYR A 334      22.928  35.901   5.921  1.00 45.88           O  
ANISOU 2507  O   TYR A 334     5887   4761   6786   -698  -1077  -1695       O  
ATOM   2508  CB  TYR A 334      25.470  34.501   4.323  1.00 38.65           C  
ANISOU 2508  CB  TYR A 334     4885   3827   5973   -902   -991  -1445       C  
ATOM   2509  CG  TYR A 334      24.909  34.947   2.990  1.00 52.69           C  
ANISOU 2509  CG  TYR A 334     6685   5492   7844   -963   -945  -1352       C  
ATOM   2510  CD1 TYR A 334      23.552  35.198   2.835  1.00 51.87           C  
ANISOU 2510  CD1 TYR A 334     6631   5374   7705   -914   -917  -1362       C  
ATOM   2511  CD2 TYR A 334      25.737  35.120   1.889  1.00 61.85           C  
ANISOU 2511  CD2 TYR A 334     7813   6566   9123  -1065   -930  -1252       C  
ATOM   2512  CE1 TYR A 334      23.035  35.606   1.620  1.00 57.79           C  
ANISOU 2512  CE1 TYR A 334     7401   6024   8534   -965   -878  -1277       C  
ATOM   2513  CE2 TYR A 334      25.228  35.528   0.670  1.00 64.48           C  
ANISOU 2513  CE2 TYR A 334     8166   6802   9532  -1115   -887  -1163       C  
ATOM   2514  CZ  TYR A 334      23.877  35.770   0.542  1.00 64.31           C  
ANISOU 2514  CZ  TYR A 334     8197   6765   9473  -1064   -864  -1177       C  
ATOM   2515  OH  TYR A 334      23.366  36.176  -0.670  1.00 71.47           O  
ANISOU 2515  OH  TYR A 334     9124   7580  10451  -1109   -825  -1089       O  
ATOM   2516  N   ALA A 335      23.924  34.231   7.060  1.00 51.85           N  
ANISOU 2516  N   ALA A 335     6608   5731   7361   -655  -1042  -1679       N  
ATOM   2517  CA  ALA A 335      22.692  33.869   7.753  1.00 48.25           C  
ANISOU 2517  CA  ALA A 335     6189   5382   6761   -552  -1002  -1714       C  
ATOM   2518  C   ALA A 335      22.257  34.944   8.740  1.00 46.73           C  
ANISOU 2518  C   ALA A 335     6006   5182   6567   -466  -1102  -1883       C  
ATOM   2519  O   ALA A 335      21.055  35.131   8.958  1.00 41.48           O  
ANISOU 2519  O   ALA A 335     5373   4548   5839   -396  -1080  -1916       O  
ATOM   2520  CB  ALA A 335      22.865  32.532   8.473  1.00 40.81           C  
ANISOU 2520  CB  ALA A 335     5240   4604   5660   -503   -945  -1673       C  
ATOM   2521  N   ARG A 336      23.210  35.659   9.344  1.00 47.72           N  
ANISOU 2521  N   ARG A 336     6102   5270   6761   -468  -1215  -1995       N  
ATOM   2522  CA  ARG A 336      22.859  36.685  10.319  1.00 48.26           C  
ANISOU 2522  CA  ARG A 336     6179   5329   6827   -380  -1321  -2170       C  
ATOM   2523  C   ARG A 336      22.129  37.863   9.686  1.00 50.90           C  
ANISOU 2523  C   ARG A 336     6540   5514   7285   -395  -1357  -2206       C  
ATOM   2524  O   ARG A 336      21.443  38.603  10.398  1.00 50.78           O  
ANISOU 2524  O   ARG A 336     6546   5504   7244   -303  -1419  -2338       O  
ATOM   2525  CB  ARG A 336      24.112  37.178  11.044  1.00 43.91           C  
ANISOU 2525  CB  ARG A 336     5587   4760   6336   -386  -1442  -2283       C  
ATOM   2526  CG  ARG A 336      24.940  38.170  10.244  1.00 55.79           C  
ANISOU 2526  CG  ARG A 336     7066   6078   8055   -498  -1516  -2285       C  
ATOM   2527  CD  ARG A 336      26.311  38.384  10.861  1.00 53.54           C  
ANISOU 2527  CD  ARG A 336     6728   5791   7825   -523  -1619  -2365       C  
ATOM   2528  NE  ARG A 336      26.231  38.964  12.197  1.00 62.59           N  
ANISOU 2528  NE  ARG A 336     7876   6989   8915   -414  -1732  -2556       N  
ATOM   2529  CZ  ARG A 336      27.167  39.745  12.726  1.00 64.06           C  
ANISOU 2529  CZ  ARG A 336     8025   7115   9201   -427  -1866  -2682       C  
ATOM   2530  NH1 ARG A 336      28.259  40.039  12.031  1.00 61.32           N  
ANISOU 2530  NH1 ARG A 336     7630   6651   9016   -551  -1900  -2628       N  
ATOM   2531  NH2 ARG A 336      27.016  40.230  13.950  1.00 54.00           N  
ANISOU 2531  NH2 ARG A 336     6758   5899   7861   -315  -1967  -2861       N  
ATOM   2532  N   ARG A 337      22.254  38.050   8.374  1.00 60.60           N  
ANISOU 2532  N   ARG A 337     7770   6614   8641   -501  -1318  -2091       N  
ATOM   2533  CA  ARG A 337      21.600  39.148   7.678  1.00 55.91           C  
ANISOU 2533  CA  ARG A 337     7202   5871   8171   -521  -1349  -2107       C  
ATOM   2534  C   ARG A 337      20.376  38.714   6.890  1.00 46.80           C  
ANISOU 2534  C   ARG A 337     6084   4735   6963   -513  -1238  -2000       C  
ATOM   2535  O   ARG A 337      19.687  39.571   6.327  1.00 44.59           O  
ANISOU 2535  O   ARG A 337     5830   4344   6768   -516  -1257  -2010       O  
ATOM   2536  CB  ARG A 337      22.577  39.836   6.724  1.00 58.32           C  
ANISOU 2536  CB  ARG A 337     7479   6006   8672   -647  -1394  -2054       C  
ATOM   2537  CG  ARG A 337      23.931  40.131   7.310  1.00 64.07           C  
ANISOU 2537  CG  ARG A 337     8159   6713   9470   -681  -1492  -2129       C  
ATOM   2538  CD  ARG A 337      24.908  40.445   6.201  1.00 71.13           C  
ANISOU 2538  CD  ARG A 337     9017   7474  10536   -819  -1496  -2024       C  
ATOM   2539  NE  ARG A 337      26.269  40.572   6.699  1.00 74.17           N  
ANISOU 2539  NE  ARG A 337     9345   7853  10986   -863  -1578  -2077       N  
ATOM   2540  CZ  ARG A 337      27.213  41.283   6.097  1.00 87.32           C  
ANISOU 2540  CZ  ARG A 337    10966   9379  12831   -970  -1635  -2048       C  
ATOM   2541  NH1 ARG A 337      26.941  41.933   4.973  1.00 86.81           N  
ANISOU 2541  NH1 ARG A 337    10915   9181  12887  -1039  -1607  -1952       N  
ATOM   2542  NH2 ARG A 337      28.426  41.346   6.621  1.00102.67           N  
ANISOU 2542  NH2 ARG A 337    12852  11332  14825  -1004  -1710  -2101       N  
ATOM   2543  N   HIS A 338      20.091  37.417   6.820  1.00 39.69           N  
ANISOU 2543  N   HIS A 338     5187   3965   5929   -503  -1129  -1898       N  
ATOM   2544  CA  HIS A 338      18.988  36.899   6.012  1.00 38.63           C  
ANISOU 2544  CA  HIS A 338     5081   3849   5747   -505  -1022  -1788       C  
ATOM   2545  C   HIS A 338      18.155  35.912   6.820  1.00 48.10           C  
ANISOU 2545  C   HIS A 338     6290   5225   6760   -413   -954  -1789       C  
ATOM   2546  O   HIS A 338      18.196  34.700   6.578  1.00 41.26           O  
ANISOU 2546  O   HIS A 338     5421   4446   5813   -437   -862  -1677       O  
ATOM   2547  CB  HIS A 338      19.514  36.250   4.732  1.00 53.47           C  
ANISOU 2547  CB  HIS A 338     6951   5683   7683   -617   -945  -1624       C  
ATOM   2548  CG  HIS A 338      19.899  37.235   3.672  1.00 54.30           C  
ANISOU 2548  CG  HIS A 338     7053   5614   7965   -704   -984  -1590       C  
ATOM   2549  ND1 HIS A 338      21.203  37.622   3.454  1.00 53.33           N  
ANISOU 2549  ND1 HIS A 338     6894   5410   7960   -784  -1041  -1584       N  
ATOM   2550  CD2 HIS A 338      19.149  37.915   2.773  1.00 51.20           C  
ANISOU 2550  CD2 HIS A 338     6687   5116   7652   -723   -975  -1553       C  
ATOM   2551  CE1 HIS A 338      21.241  38.496   2.464  1.00 53.87           C  
ANISOU 2551  CE1 HIS A 338     6965   5329   8173   -851  -1061  -1540       C  
ATOM   2552  NE2 HIS A 338      20.008  38.690   2.032  1.00 49.67           N  
ANISOU 2552  NE2 HIS A 338     6474   4779   7620   -814  -1023  -1521       N  
ATOM   2553  N   PRO A 339      17.374  36.401   7.790  1.00 52.49           N  
ANISOU 2553  N   PRO A 339     6859   5840   7246   -304   -995  -1913       N  
ATOM   2554  CA  PRO A 339      16.349  35.543   8.400  1.00 51.69           C  
ANISOU 2554  CA  PRO A 339     6766   5900   6974   -218   -917  -1895       C  
ATOM   2555  C   PRO A 339      15.188  35.257   7.467  1.00 47.55           C  
ANISOU 2555  C   PRO A 339     6262   5361   6443   -235   -826  -1793       C  
ATOM   2556  O   PRO A 339      14.379  34.369   7.764  1.00 45.19           O  
ANISOU 2556  O   PRO A 339     5964   5191   6016   -188   -745  -1743       O  
ATOM   2557  CB  PRO A 339      15.898  36.348   9.624  1.00 55.06           C  
ANISOU 2557  CB  PRO A 339     7197   6380   7344    -95   -998  -2066       C  
ATOM   2558  CG  PRO A 339      16.153  37.764   9.249  1.00 52.68           C  
ANISOU 2558  CG  PRO A 339     6904   5904   7207   -121  -1103  -2156       C  
ATOM   2559  CD  PRO A 339      17.374  37.758   8.368  1.00 52.33           C  
ANISOU 2559  CD  PRO A 339     6844   5741   7298   -251  -1117  -2074       C  
ATOM   2560  N   ASP A 340      15.081  35.986   6.354  1.00 41.07           N  
ANISOU 2560  N   ASP A 340     5456   4390   5759   -300   -840  -1758       N  
ATOM   2561  CA  ASP A 340      14.081  35.711   5.332  1.00 40.06           C  
ANISOU 2561  CA  ASP A 340     5345   4239   5636   -325   -758  -1654       C  
ATOM   2562  C   ASP A 340      14.462  34.542   4.435  1.00 40.66           C  
ANISOU 2562  C   ASP A 340     5416   4331   5702   -414   -666  -1496       C  
ATOM   2563  O   ASP A 340      13.601  34.035   3.708  1.00 50.69           O  
ANISOU 2563  O   ASP A 340     6697   5616   6946   -427   -589  -1406       O  
ATOM   2564  CB  ASP A 340      13.848  36.959   4.476  1.00 49.88           C  
ANISOU 2564  CB  ASP A 340     6608   5317   7028   -356   -811  -1675       C  
ATOM   2565  CG  ASP A 340      15.115  37.444   3.792  1.00 56.35           C  
ANISOU 2565  CG  ASP A 340     7417   5998   7995   -458   -862  -1644       C  
ATOM   2566  OD1 ASP A 340      16.187  37.423   4.434  1.00 47.12           O  
ANISOU 2566  OD1 ASP A 340     6226   4843   6835   -470   -914  -1694       O  
ATOM   2567  OD2 ASP A 340      15.040  37.847   2.612  1.00 54.07           O  
ANISOU 2567  OD2 ASP A 340     7140   5591   7812   -525   -849  -1566       O  
ATOM   2568  N   TYR A 341      15.721  34.112   4.460  1.00 46.53           N  
ANISOU 2568  N   TYR A 341     6140   5072   6467   -471   -677  -1465       N  
ATOM   2569  CA  TYR A 341      16.163  32.952   3.700  1.00 44.02           C  
ANISOU 2569  CA  TYR A 341     5816   4778   6131   -544   -595  -1326       C  
ATOM   2570  C   TYR A 341      15.935  31.689   4.515  1.00 40.57           C  
ANISOU 2570  C   TYR A 341     5372   4501   5541   -494   -534  -1299       C  
ATOM   2571  O   TYR A 341      16.072  31.694   5.742  1.00 36.84           O  
ANISOU 2571  O   TYR A 341     4890   4118   4990   -423   -571  -1387       O  
ATOM   2572  CB  TYR A 341      17.647  33.062   3.340  1.00 42.95           C  
ANISOU 2572  CB  TYR A 341     5658   4572   6090   -624   -634  -1302       C  
ATOM   2573  CG  TYR A 341      17.980  34.029   2.224  1.00 34.81           C  
ANISOU 2573  CG  TYR A 341     4629   3382   5217   -701   -667  -1273       C  
ATOM   2574  CD1 TYR A 341      17.040  34.934   1.749  1.00 43.23           C  
ANISOU 2574  CD1 TYR A 341     5720   4365   6342   -686   -683  -1295       C  
ATOM   2575  CD2 TYR A 341      19.244  34.036   1.648  1.00 38.27           C  
ANISOU 2575  CD2 TYR A 341     5041   3756   5745   -787   -682  -1219       C  
ATOM   2576  CE1 TYR A 341      17.350  35.819   0.732  1.00 48.63           C  
ANISOU 2576  CE1 TYR A 341     6405   4902   7169   -755   -713  -1259       C  
ATOM   2577  CE2 TYR A 341      19.563  34.914   0.631  1.00 45.45           C  
ANISOU 2577  CE2 TYR A 341     5947   4525   6798   -858   -708  -1181       C  
ATOM   2578  CZ  TYR A 341      18.613  35.803   0.176  1.00 52.31           C  
ANISOU 2578  CZ  TYR A 341     6843   5309   7722   -843   -724  -1198       C  
ATOM   2579  OH  TYR A 341      18.927  36.680  -0.837  1.00 60.28           O  
ANISOU 2579  OH  TYR A 341     7852   6178   8875   -913   -749  -1151       O  
ATOM   2580  N   SER A 342      15.588  30.604   3.830  1.00 37.77           N  
ANISOU 2580  N   SER A 342     5024   4182   5143   -530   -442  -1176       N  
ATOM   2581  CA  SER A 342      15.557  29.316   4.497  1.00 38.70           C  
ANISOU 2581  CA  SER A 342     5135   4435   5134   -500   -383  -1130       C  
ATOM   2582  C   SER A 342      16.973  28.903   4.888  1.00 45.36           C  
ANISOU 2582  C   SER A 342     5959   5299   5978   -525   -412  -1129       C  
ATOM   2583  O   SER A 342      17.965  29.388   4.335  1.00 32.84           O  
ANISOU 2583  O   SER A 342     4362   3618   4496   -588   -454  -1129       O  
ATOM   2584  CB  SER A 342      14.926  28.253   3.597  1.00 31.61           C  
ANISOU 2584  CB  SER A 342     4248   3552   4209   -540   -287  -1000       C  
ATOM   2585  OG  SER A 342      15.743  27.980   2.474  1.00 30.99           O  
ANISOU 2585  OG  SER A 342     4170   3392   4211   -628   -271   -917       O  
ATOM   2586  N   VAL A 343      17.062  28.010   5.873  1.00 32.87           N  
ANISOU 2586  N   VAL A 343     4368   3844   4275   -474   -388  -1126       N  
ATOM   2587  CA  VAL A 343      18.366  27.481   6.258  1.00 32.97           C  
ANISOU 2587  CA  VAL A 343     4361   3889   4275   -492   -409  -1116       C  
ATOM   2588  C   VAL A 343      18.950  26.639   5.131  1.00 37.54           C  
ANISOU 2588  C   VAL A 343     4941   4421   4901   -577   -353   -992       C  
ATOM   2589  O   VAL A 343      20.159  26.676   4.871  1.00 37.24           O  
ANISOU 2589  O   VAL A 343     4883   4341   4924   -625   -384   -984       O  
ATOM   2590  CB  VAL A 343      18.254  26.679   7.568  1.00 34.35           C  
ANISOU 2590  CB  VAL A 343     4530   4217   4303   -410   -393  -1132       C  
ATOM   2591  CG1 VAL A 343      19.605  26.092   7.945  1.00 33.87           C  
ANISOU 2591  CG1 VAL A 343     4449   4191   4227   -425   -415  -1119       C  
ATOM   2592  CG2 VAL A 343      17.724  27.560   8.685  1.00 34.37           C  
ANISOU 2592  CG2 VAL A 343     4530   4275   4253   -317   -452  -1265       C  
ATOM   2593  N   VAL A 344      18.102  25.879   4.433  1.00 31.24           N  
ANISOU 2593  N   VAL A 344     4163   3631   4078   -596   -272   -896       N  
ATOM   2594  CA  VAL A 344      18.597  25.020   3.363  1.00 30.41           C  
ANISOU 2594  CA  VAL A 344     4061   3487   4007   -667   -219   -783       C  
ATOM   2595  C   VAL A 344      19.091  25.849   2.181  1.00 38.24           C  
ANISOU 2595  C   VAL A 344     5048   4350   5130   -739   -244   -772       C  
ATOM   2596  O   VAL A 344      20.032  25.448   1.485  1.00 31.99           O  
ANISOU 2596  O   VAL A 344     4246   3526   4384   -794   -231   -710       O  
ATOM   2597  CB  VAL A 344      17.511  24.009   2.947  1.00 42.39           C  
ANISOU 2597  CB  VAL A 344     5599   5042   5464   -665   -134   -693       C  
ATOM   2598  CG1 VAL A 344      16.257  24.726   2.476  1.00 39.05           C  
ANISOU 2598  CG1 VAL A 344     5190   4576   5071   -659   -125   -711       C  
ATOM   2599  CG2 VAL A 344      18.036  23.064   1.877  1.00 37.85           C  
ANISOU 2599  CG2 VAL A 344     5029   4431   4919   -729    -84   -586       C  
ATOM   2600  N   LEU A 345      18.486  27.016   1.936  1.00 31.45           N  
ANISOU 2600  N   LEU A 345     4196   3419   4334   -736   -280   -827       N  
ATOM   2601  CA  LEU A 345      18.996  27.891   0.884  1.00 34.09           C  
ANISOU 2601  CA  LEU A 345     4525   3629   4798   -803   -309   -813       C  
ATOM   2602  C   LEU A 345      20.339  28.489   1.278  1.00 35.90           C  
ANISOU 2602  C   LEU A 345     4722   3825   5092   -826   -383   -869       C  
ATOM   2603  O   LEU A 345      21.260  28.554   0.457  1.00 33.22           O  
ANISOU 2603  O   LEU A 345     4363   3424   4833   -895   -384   -815       O  
ATOM   2604  CB  LEU A 345      17.990  29.000   0.571  1.00 32.27           C  
ANISOU 2604  CB  LEU A 345     4313   3327   4622   -790   -333   -858       C  
ATOM   2605  CG  LEU A 345      18.522  30.182  -0.250  1.00 31.25           C  
ANISOU 2605  CG  LEU A 345     4177   3064   4635   -848   -384   -865       C  
ATOM   2606  CD1 LEU A 345      18.923  29.735  -1.650  1.00 30.55           C  
ANISOU 2606  CD1 LEU A 345     4088   2925   4596   -923   -330   -744       C  
ATOM   2607  CD2 LEU A 345      17.499  31.308  -0.318  1.00 31.69           C  
ANISOU 2607  CD2 LEU A 345     4253   3054   4735   -817   -419   -926       C  
ATOM   2608  N   LEU A 346      20.468  28.929   2.532  1.00 32.11           N  
ANISOU 2608  N   LEU A 346     4232   3390   4577   -768   -447   -979       N  
ATOM   2609  CA  LEU A 346      21.742  29.465   3.001  1.00 32.85           C  
ANISOU 2609  CA  LEU A 346     4291   3460   4732   -787   -525  -1042       C  
ATOM   2610  C   LEU A 346      22.847  28.420   2.903  1.00 37.37           C  
ANISOU 2610  C   LEU A 346     4838   4083   5276   -819   -495   -971       C  
ATOM   2611  O   LEU A 346      23.974  28.733   2.501  1.00 41.35           O  
ANISOU 2611  O   LEU A 346     5309   4533   5871   -878   -528   -959       O  
ATOM   2612  CB  LEU A 346      21.597  29.972   4.436  1.00 33.80           C  
ANISOU 2612  CB  LEU A 346     4407   3639   4795   -704   -598  -1177       C  
ATOM   2613  CG  LEU A 346      20.784  31.259   4.606  1.00 38.90           C  
ANISOU 2613  CG  LEU A 346     5070   4218   5494   -670   -656  -1275       C  
ATOM   2614  CD1 LEU A 346      20.288  31.401   6.036  1.00 38.34           C  
ANISOU 2614  CD1 LEU A 346     5004   4248   5317   -564   -696  -1393       C  
ATOM   2615  CD2 LEU A 346      21.602  32.478   4.193  1.00 35.17           C  
ANISOU 2615  CD2 LEU A 346     4576   3608   5179   -731   -740  -1321       C  
ATOM   2616  N   LEU A 347      22.544  27.170   3.268  1.00 31.96           N  
ANISOU 2616  N   LEU A 347     4166   3504   4471   -781   -432   -920       N  
ATOM   2617  CA  LEU A 347      23.508  26.090   3.079  1.00 33.42           C  
ANISOU 2617  CA  LEU A 347     4334   3734   4630   -807   -397   -844       C  
ATOM   2618  C   LEU A 347      23.789  25.857   1.604  1.00 30.87           C  
ANISOU 2618  C   LEU A 347     4010   3337   4383   -884   -346   -740       C  
ATOM   2619  O   LEU A 347      24.905  25.475   1.234  1.00 30.81           O  
ANISOU 2619  O   LEU A 347     3974   3327   4407   -924   -343   -695       O  
ATOM   2620  CB  LEU A 347      22.993  24.800   3.719  1.00 31.18           C  
ANISOU 2620  CB  LEU A 347     4070   3566   4209   -749   -338   -804       C  
ATOM   2621  CG  LEU A 347      22.872  24.800   5.240  1.00 32.72           C  
ANISOU 2621  CG  LEU A 347     4261   3864   4305   -665   -378   -891       C  
ATOM   2622  CD1 LEU A 347      22.141  23.557   5.727  1.00 31.52           C  
ANISOU 2622  CD1 LEU A 347     4133   3818   4025   -614   -307   -829       C  
ATOM   2623  CD2 LEU A 347      24.249  24.898   5.863  1.00 33.81           C  
ANISOU 2623  CD2 LEU A 347     4362   4027   4456   -663   -444   -941       C  
ATOM   2624  N   ARG A 348      22.782  26.079   0.759  1.00 30.41           N  
ANISOU 2624  N   ARG A 348     3981   3224   4349   -901   -307   -700       N  
ATOM   2625  CA  ARG A 348      22.948  25.931  -0.681  1.00 29.83           C  
ANISOU 2625  CA  ARG A 348     3910   3084   4340   -966   -260   -604       C  
ATOM   2626  C   ARG A 348      23.862  27.008  -1.246  1.00 39.60           C  
ANISOU 2626  C   ARG A 348     5113   4228   5707  -1028   -311   -615       C  
ATOM   2627  O   ARG A 348      24.685  26.732  -2.127  1.00 30.14           O  
ANISOU 2627  O   ARG A 348     3892   3005   4553  -1081   -285   -540       O  
ATOM   2628  CB  ARG A 348      21.580  25.984  -1.355  1.00 29.32           C  
ANISOU 2628  CB  ARG A 348     3884   2990   4267   -961   -215   -571       C  
ATOM   2629  CG  ARG A 348      21.605  25.777  -2.848  1.00 39.72           C  
ANISOU 2629  CG  ARG A 348     5208   4250   5635  -1017   -164   -473       C  
ATOM   2630  CD  ARG A 348      20.191  25.506  -3.400  1.00 47.64           C  
ANISOU 2630  CD  ARG A 348     6250   5250   6601  -1001   -113   -438       C  
ATOM   2631  NE  ARG A 348      19.506  24.432  -2.672  1.00 38.84           N  
ANISOU 2631  NE  ARG A 348     5153   4227   5377   -951    -76   -435       N  
ATOM   2632  CZ  ARG A 348      18.324  24.539  -2.062  1.00 46.90           C  
ANISOU 2632  CZ  ARG A 348     6191   5283   6346   -904    -72   -474       C  
ATOM   2633  NH1 ARG A 348      17.645  25.683  -2.062  1.00 34.32           N  
ANISOU 2633  NH1 ARG A 348     4604   3640   4798   -892   -107   -531       N  
ATOM   2634  NH2 ARG A 348      17.827  23.483  -1.433  1.00 45.57           N  
ANISOU 2634  NH2 ARG A 348     6031   5200   6082   -867    -33   -455       N  
ATOM   2635  N   LEU A 349      23.721  28.244  -0.761  1.00 31.11           N  
ANISOU 2635  N   LEU A 349     4032   3096   4692  -1021   -384   -705       N  
ATOM   2636  CA  LEU A 349      24.606  29.317  -1.203  1.00 31.77           C  
ANISOU 2636  CA  LEU A 349     4079   3082   4909  -1083   -440   -716       C  
ATOM   2637  C   LEU A 349      26.031  29.090  -0.713  1.00 35.84           C  
ANISOU 2637  C   LEU A 349     4544   3634   5442  -1103   -478   -733       C  
ATOM   2638  O   LEU A 349      26.993  29.343  -1.446  1.00 39.02           O  
ANISOU 2638  O   LEU A 349     4906   3986   5934  -1170   -482   -680       O  
ATOM   2639  CB  LEU A 349      24.074  30.666  -0.716  1.00 33.69           C  
ANISOU 2639  CB  LEU A 349     4332   3253   5217  -1064   -518   -819       C  
ATOM   2640  CG  LEU A 349      22.628  30.999  -1.094  1.00 36.10           C  
ANISOU 2640  CG  LEU A 349     4685   3525   5508  -1035   -490   -817       C  
ATOM   2641  CD1 LEU A 349      22.188  32.308  -0.456  1.00 34.90           C  
ANISOU 2641  CD1 LEU A 349     4540   3308   5413  -1003   -576   -933       C  
ATOM   2642  CD2 LEU A 349      22.466  31.053  -2.606  1.00 32.58           C  
ANISOU 2642  CD2 LEU A 349     4247   3007   5124  -1096   -436   -704       C  
ATOM   2643  N   ALA A 350      26.183  28.610   0.525  1.00 36.60           N  
ANISOU 2643  N   ALA A 350     4636   3822   5448  -1042   -504   -801       N  
ATOM   2644  CA  ALA A 350      27.512  28.307   1.045  1.00 32.90           C  
ANISOU 2644  CA  ALA A 350     4118   3399   4983  -1052   -540   -818       C  
ATOM   2645  C   ALA A 350      28.183  27.206   0.234  1.00 32.22           C  
ANISOU 2645  C   ALA A 350     4016   3350   4875  -1085   -468   -703       C  
ATOM   2646  O   ALA A 350      29.391  27.260  -0.020  1.00 41.07           O  
ANISOU 2646  O   ALA A 350     5085   4461   6058  -1131   -487   -681       O  
ATOM   2647  CB  ALA A 350      27.420  27.912   2.519  1.00 33.25           C  
ANISOU 2647  CB  ALA A 350     4169   3548   4917   -969   -575   -907       C  
ATOM   2648  N   LYS A 351      27.414  26.195  -0.180  1.00 33.56           N  
ANISOU 2648  N   LYS A 351     4228   3563   4960  -1061   -386   -632       N  
ATOM   2649  CA  LYS A 351      27.975  25.142  -1.020  1.00 32.96           C  
ANISOU 2649  CA  LYS A 351     4143   3515   4864  -1086   -318   -527       C  
ATOM   2650  C   LYS A 351      28.384  25.687  -2.383  1.00 32.48           C  
ANISOU 2650  C   LYS A 351     4060   3371   4910  -1161   -299   -457       C  
ATOM   2651  O   LYS A 351      29.430  25.306  -2.921  1.00 30.69           O  
ANISOU 2651  O   LYS A 351     3793   3157   4710  -1195   -281   -400       O  
ATOM   2652  CB  LYS A 351      26.970  24.001  -1.177  1.00 29.84           C  
ANISOU 2652  CB  LYS A 351     3802   3172   4365  -1045   -243   -473       C  
ATOM   2653  CG  LYS A 351      27.523  22.794  -1.917  1.00 30.73           C  
ANISOU 2653  CG  LYS A 351     3911   3320   4446  -1057   -180   -379       C  
ATOM   2654  CD  LYS A 351      28.741  22.229  -1.203  1.00 54.00           C  
ANISOU 2654  CD  LYS A 351     6819   6335   7364  -1039   -205   -392       C  
ATOM   2655  CE  LYS A 351      29.622  21.431  -2.152  1.00 64.29           C  
ANISOU 2655  CE  LYS A 351     8100   7650   8679  -1065   -159   -306       C  
ATOM   2656  NZ  LYS A 351      30.554  22.306  -2.915  1.00 58.80           N  
ANISOU 2656  NZ  LYS A 351     7350   6899   8095  -1130   -181   -289       N  
ATOM   2657  N   THR A 352      27.571  26.577  -2.955  1.00 34.14           N  
ANISOU 2657  N   THR A 352     4293   3499   5180  -1184   -302   -457       N  
ATOM   2658  CA  THR A 352      27.937  27.207  -4.219  1.00 35.52           C  
ANISOU 2658  CA  THR A 352     4446   3592   5458  -1253   -287   -387       C  
ATOM   2659  C   THR A 352      29.173  28.082  -4.056  1.00 33.61           C  
ANISOU 2659  C   THR A 352     4137   3306   5325  -1305   -353   -413       C  
ATOM   2660  O   THR A 352      30.062  28.080  -4.916  1.00 37.00           O  
ANISOU 2660  O   THR A 352     4523   3721   5814  -1360   -330   -337       O  
ATOM   2661  CB  THR A 352      26.764  28.030  -4.755  1.00 35.65           C  
ANISOU 2661  CB  THR A 352     4503   3529   5514  -1259   -284   -387       C  
ATOM   2662  OG1 THR A 352      25.627  27.177  -4.940  1.00 38.34           O  
ANISOU 2662  OG1 THR A 352     4898   3914   5757  -1214   -223   -359       O  
ATOM   2663  CG2 THR A 352      27.124  28.681  -6.084  1.00 36.86           C  
ANISOU 2663  CG2 THR A 352     4634   3601   5770  -1328   -266   -303       C  
ATOM   2664  N   TYR A 353      29.251  28.828  -2.951  1.00 35.74           N  
ANISOU 2664  N   TYR A 353     4395   3560   5622  -1288   -437   -522       N  
ATOM   2665  CA  TYR A 353      30.421  29.662  -2.695  1.00 39.95           C  
ANISOU 2665  CA  TYR A 353     4863   4051   6267  -1339   -511   -559       C  
ATOM   2666  C   TYR A 353      31.681  28.817  -2.555  1.00 40.49           C  
ANISOU 2666  C   TYR A 353     4877   4200   6307  -1347   -499   -527       C  
ATOM   2667  O   TYR A 353      32.748  29.190  -3.056  1.00 45.02           O  
ANISOU 2667  O   TYR A 353     5387   4744   6976  -1412   -513   -486       O  
ATOM   2668  CB  TYR A 353      30.197  30.503  -1.438  1.00 36.87           C  
ANISOU 2668  CB  TYR A 353     4477   3639   5895  -1304   -609   -697       C  
ATOM   2669  CG  TYR A 353      31.349  31.422  -1.100  1.00 37.50           C  
ANISOU 2669  CG  TYR A 353     4488   3664   6097  -1357   -699   -750       C  
ATOM   2670  CD1 TYR A 353      31.673  32.492  -1.924  1.00 41.48           C  
ANISOU 2670  CD1 TYR A 353     4961   4049   6752  -1438   -724   -712       C  
ATOM   2671  CD2 TYR A 353      32.111  31.221   0.044  1.00 42.74           C  
ANISOU 2671  CD2 TYR A 353     5115   4395   6729  -1326   -762   -836       C  
ATOM   2672  CE1 TYR A 353      32.725  33.336  -1.620  1.00 45.22           C  
ANISOU 2672  CE1 TYR A 353     5366   4466   7349  -1494   -811   -757       C  
ATOM   2673  CE2 TYR A 353      33.166  32.060   0.357  1.00 48.39           C  
ANISOU 2673  CE2 TYR A 353     5763   5059   7562  -1377   -852   -890       C  
ATOM   2674  CZ  TYR A 353      33.468  33.116  -0.479  1.00 47.51           C  
ANISOU 2674  CZ  TYR A 353     5619   4824   7609  -1464   -876   -850       C  
ATOM   2675  OH  TYR A 353      34.515  33.954  -0.175  1.00 44.35           O  
ANISOU 2675  OH  TYR A 353     5146   4366   7337  -1522   -968   -899       O  
ATOM   2676  N   GLU A 354      31.577  27.673  -1.875  1.00 33.53           N  
ANISOU 2676  N   GLU A 354     4018   3424   5299  -1281   -473   -542       N  
ATOM   2677  CA  GLU A 354      32.717  26.769  -1.764  1.00 35.97           C  
ANISOU 2677  CA  GLU A 354     4281   3813   5572  -1278   -457   -508       C  
ATOM   2678  C   GLU A 354      33.109  26.215  -3.128  1.00 44.80           C  
ANISOU 2678  C   GLU A 354     5384   4931   6707  -1319   -377   -383       C  
ATOM   2679  O   GLU A 354      34.286  26.228  -3.502  1.00 42.31           O  
ANISOU 2679  O   GLU A 354     5001   4626   6449  -1362   -380   -343       O  
ATOM   2680  CB  GLU A 354      32.389  25.635  -0.791  1.00 36.81           C  
ANISOU 2680  CB  GLU A 354     4424   4026   5536  -1195   -441   -539       C  
ATOM   2681  CG  GLU A 354      33.393  24.494  -0.792  1.00 39.88           C  
ANISOU 2681  CG  GLU A 354     4780   4501   5872  -1180   -411   -489       C  
ATOM   2682  CD  GLU A 354      32.965  23.343   0.100  1.00 55.87           C  
ANISOU 2682  CD  GLU A 354     6849   6621   7758  -1097   -390   -505       C  
ATOM   2683  OE1 GLU A 354      33.772  22.914   0.952  1.00 54.44           O  
ANISOU 2683  OE1 GLU A 354     6637   6513   7536  -1063   -425   -540       O  
ATOM   2684  OE2 GLU A 354      31.819  22.868  -0.051  1.00 50.43           O  
ANISOU 2684  OE2 GLU A 354     6224   5936   7003  -1067   -338   -479       O  
ATOM   2685  N   THR A 355      32.125  25.729  -3.891  1.00 43.87           N  
ANISOU 2685  N   THR A 355     5324   4806   6537  -1304   -305   -322       N  
ATOM   2686  CA  THR A 355      32.410  25.166  -5.207  1.00 41.79           C  
ANISOU 2686  CA  THR A 355     5053   4550   6277  -1331   -228   -210       C  
ATOM   2687  C   THR A 355      33.010  26.214  -6.139  1.00 38.26           C  
ANISOU 2687  C   THR A 355     4552   4026   5958  -1410   -237   -160       C  
ATOM   2688  O   THR A 355      33.940  25.920  -6.899  1.00 40.81           O  
ANISOU 2688  O   THR A 355     4824   4374   6305  -1441   -202    -85       O  
ATOM   2689  CB  THR A 355      31.134  24.572  -5.808  1.00 37.62           C  
ANISOU 2689  CB  THR A 355     4598   4018   5676  -1299   -162   -169       C  
ATOM   2690  OG1 THR A 355      30.689  23.478  -4.997  1.00 40.52           O  
ANISOU 2690  OG1 THR A 355     5007   4461   5928  -1232   -147   -198       O  
ATOM   2691  CG2 THR A 355      31.382  24.072  -7.226  1.00 32.55           C  
ANISOU 2691  CG2 THR A 355     3950   3381   5036  -1323    -89    -61       C  
ATOM   2692  N   THR A 356      32.498  27.446  -6.085  1.00 39.04           N  
ANISOU 2692  N   THR A 356     4659   4032   6140  -1442   -284   -198       N  
ATOM   2693  CA  THR A 356      33.047  28.512  -6.919  1.00 40.29           C  
ANISOU 2693  CA  THR A 356     4767   4109   6432  -1521   -298   -145       C  
ATOM   2694  C   THR A 356      34.485  28.831  -6.531  1.00 43.15           C  
ANISOU 2694  C   THR A 356     5040   4483   6872  -1565   -349   -160       C  
ATOM   2695  O   THR A 356      35.345  29.019  -7.401  1.00 40.24           O  
ANISOU 2695  O   THR A 356     4610   4107   6574  -1623   -323    -74       O  
ATOM   2696  CB  THR A 356      32.172  29.762  -6.816  1.00 40.93           C  
ANISOU 2696  CB  THR A 356     4881   4081   6590  -1539   -348   -192       C  
ATOM   2697  OG1 THR A 356      30.916  29.522  -7.463  1.00 43.48           O  
ANISOU 2697  OG1 THR A 356     5274   4390   6854  -1508   -291   -155       O  
ATOM   2698  CG2 THR A 356      32.854  30.955  -7.477  1.00 42.10           C  
ANISOU 2698  CG2 THR A 356     4969   4134   6891  -1625   -379   -145       C  
ATOM   2699  N   LEU A 357      34.768  28.890  -5.227  1.00 39.36           N  
ANISOU 2699  N   LEU A 357     4547   4029   6379  -1537   -423   -267       N  
ATOM   2700  CA  LEU A 357      36.130  29.159  -4.778  1.00 35.26           C  
ANISOU 2700  CA  LEU A 357     3939   3526   5931  -1576   -480   -292       C  
ATOM   2701  C   LEU A 357      37.078  28.042  -5.192  1.00 34.99           C  
ANISOU 2701  C   LEU A 357     3860   3593   5841  -1567   -420   -217       C  
ATOM   2702  O   LEU A 357      38.213  28.306  -5.604  1.00 43.81           O  
ANISOU 2702  O   LEU A 357     4893   4713   7041  -1625   -425   -169       O  
ATOM   2703  CB  LEU A 357      36.159  29.347  -3.261  1.00 43.79           C  
ANISOU 2703  CB  LEU A 357     5022   4628   6989  -1532   -572   -429       C  
ATOM   2704  CG  LEU A 357      35.682  30.693  -2.714  1.00 47.39           C  
ANISOU 2704  CG  LEU A 357     5490   4979   7538  -1552   -662   -525       C  
ATOM   2705  CD1 LEU A 357      36.132  30.866  -1.271  1.00 48.75           C  
ANISOU 2705  CD1 LEU A 357     5638   5187   7698  -1515   -761   -658       C  
ATOM   2706  CD2 LEU A 357      36.183  31.839  -3.578  1.00 45.19           C  
ANISOU 2706  CD2 LEU A 357     5157   4588   7427  -1651   -684   -468       C  
ATOM   2707  N   GLU A 358      36.633  26.787  -5.090  1.00 34.05           N  
ANISOU 2707  N   GLU A 358     3795   3557   5585  -1495   -363   -205       N  
ATOM   2708  CA  GLU A 358      37.480  25.671  -5.498  1.00 40.40           C  
ANISOU 2708  CA  GLU A 358     4564   4454   6332  -1476   -306   -138       C  
ATOM   2709  C   GLU A 358      37.856  25.773  -6.970  1.00 46.24           C  
ANISOU 2709  C   GLU A 358     5268   5176   7124  -1528   -238    -18       C  
ATOM   2710  O   GLU A 358      38.978  25.434  -7.359  1.00 41.82           O  
ANISOU 2710  O   GLU A 358     4637   4672   6583  -1546   -217     35       O  
ATOM   2711  CB  GLU A 358      36.776  24.342  -5.222  1.00 46.11           C  
ANISOU 2711  CB  GLU A 358     5363   5249   6909  -1392   -257   -140       C  
ATOM   2712  CG  GLU A 358      36.518  24.059  -3.752  1.00 54.41           C  
ANISOU 2712  CG  GLU A 358     6442   6342   7889  -1331   -313   -243       C  
ATOM   2713  CD  GLU A 358      37.728  23.485  -3.042  1.00 61.84           C  
ANISOU 2713  CD  GLU A 358     7323   7368   8805  -1308   -345   -267       C  
ATOM   2714  OE1 GLU A 358      38.483  22.716  -3.673  1.00 61.91           O  
ANISOU 2714  OE1 GLU A 358     7297   7429   8795  -1305   -296   -195       O  
ATOM   2715  OE2 GLU A 358      37.922  23.802  -1.850  1.00 66.28           O  
ANISOU 2715  OE2 GLU A 358     7872   7948   9364  -1286   -421   -360       O  
ATOM   2716  N   LYS A 359      36.940  26.253  -7.803  1.00 45.90           N  
ANISOU 2716  N   LYS A 359     5273   5065   7104  -1549   -204     26       N  
ATOM   2717  CA  LYS A 359      37.217  26.267  -9.233  1.00 52.15           C  
ANISOU 2717  CA  LYS A 359     6036   5852   7925  -1587   -133    145       C  
ATOM   2718  C   LYS A 359      38.027  27.493  -9.642  1.00 53.04           C  
ANISOU 2718  C   LYS A 359     6065   5902   8187  -1677   -165    186       C  
ATOM   2719  O   LYS A 359      38.985  27.385 -10.417  1.00 51.97           O  
ANISOU 2719  O   LYS A 359     5857   5806   8084  -1711   -124    272       O  
ATOM   2720  CB  LYS A 359      35.908  26.208 -10.010  1.00 59.31           C  
ANISOU 2720  CB  LYS A 359     7027   6719   8788  -1566    -81    182       C  
ATOM   2721  CG  LYS A 359      36.071  26.379 -11.496  1.00 65.07           C  
ANISOU 2721  CG  LYS A 359     7735   7440   9549  -1602    -13    301       C  
ATOM   2722  CD  LYS A 359      34.720  26.324 -12.171  1.00 67.45           C  
ANISOU 2722  CD  LYS A 359     8122   7704   9802  -1576     28    325       C  
ATOM   2723  CE  LYS A 359      33.947  27.623 -11.950  1.00 68.80           C  
ANISOU 2723  CE  LYS A 359     8318   7763  10059  -1613    -25    289       C  
ATOM   2724  NZ  LYS A 359      34.533  28.728 -12.748  1.00 69.17           N  
ANISOU 2724  NZ  LYS A 359     8304   7747  10231  -1691    -27    368       N  
ATOM   2725  N   CYS A 360      37.651  28.671  -9.142  1.00 48.56           N  
ANISOU 2725  N   CYS A 360     5503   5234   7713  -1717   -237    127       N  
ATOM   2726  CA  CYS A 360      38.263  29.905  -9.622  1.00 48.14           C  
ANISOU 2726  CA  CYS A 360     5379   5098   7814  -1809   -268    175       C  
ATOM   2727  C   CYS A 360      39.609  30.189  -8.962  1.00 58.06           C  
ANISOU 2727  C   CYS A 360     6533   6375   9152  -1853   -331    141       C  
ATOM   2728  O   CYS A 360      40.474  30.818  -9.585  1.00 53.98           O  
ANISOU 2728  O   CYS A 360     5930   5831   8747  -1930   -329    218       O  
ATOM   2729  CB  CYS A 360      37.318  31.084  -9.401  1.00 52.43           C  
ANISOU 2729  CB  CYS A 360     5971   5515   8436  -1833   -325    125       C  
ATOM   2730  SG  CYS A 360      35.823  31.052 -10.423  1.00 58.50           S  
ANISOU 2730  SG  CYS A 360     6839   6243   9146  -1803   -253    187       S  
ATOM   2731  N   CYS A 361      39.810  29.748  -7.714  1.00 48.53           N  
ANISOU 2731  N   CYS A 361     5330   5218   7892  -1805   -389     31       N  
ATOM   2732  CA  CYS A 361      41.105  29.945  -7.067  1.00 49.96           C  
ANISOU 2732  CA  CYS A 361     5411   5428   8142  -1841   -453     -6       C  
ATOM   2733  C   CYS A 361      42.213  29.198  -7.794  1.00 47.33           C  
ANISOU 2733  C   CYS A 361     5000   5194   7791  -1851   -385     93       C  
ATOM   2734  O   CYS A 361      43.377  29.606  -7.735  1.00 46.49           O  
ANISOU 2734  O   CYS A 361     4788   5096   7781  -1910   -421    109       O  
ATOM   2735  CB  CYS A 361      41.044  29.499  -5.609  1.00 41.04           C  
ANISOU 2735  CB  CYS A 361     4308   4349   6936  -1772   -521   -141       C  
ATOM   2736  SG  CYS A 361      40.157  30.633  -4.530  1.00 42.38           S  
ANISOU 2736  SG  CYS A 361     4531   4410   7160  -1769   -631   -281       S  
ATOM   2737  N   ALA A 362      41.875  28.111  -8.479  1.00 57.29           N  
ANISOU 2737  N   ALA A 362     6308   6529   8931  -1793   -291    158       N  
ATOM   2738  CA  ALA A 362      42.843  27.335  -9.239  1.00 59.41           C  
ANISOU 2738  CA  ALA A 362     6509   6896   9167  -1788   -221    251       C  
ATOM   2739  C   ALA A 362      42.955  27.784 -10.690  1.00 51.54           C  
ANISOU 2739  C   ALA A 362     5478   5875   8230  -1845   -150    385       C  
ATOM   2740  O   ALA A 362      43.741  27.201 -11.445  1.00 51.08           O  
ANISOU 2740  O   ALA A 362     5361   5904   8145  -1839    -84    471       O  
ATOM   2741  CB  ALA A 362      42.479  25.847  -9.185  1.00 61.15           C  
ANISOU 2741  CB  ALA A 362     6797   7213   9224  -1687   -163    244       C  
ATOM   2742  N   ALA A 363      42.198  28.801 -11.097  1.00 59.64           N  
ANISOU 2742  N   ALA A 363     6539   6790   9332  -1893   -160    407       N  
ATOM   2743  CA  ALA A 363      42.199  29.257 -12.478  1.00 65.63           C  
ANISOU 2743  CA  ALA A 363     7273   7524  10139  -1942    -91    540       C  
ATOM   2744  C   ALA A 363      43.238  30.361 -12.680  1.00 75.14           C  
ANISOU 2744  C   ALA A 363     8359   8679  11509  -2048   -127    596       C  
ATOM   2745  O   ALA A 363      44.000  30.711 -11.775  1.00 71.80           O  
ANISOU 2745  O   ALA A 363     7871   8247  11162  -2082   -206    528       O  
ATOM   2746  CB  ALA A 363      40.805  29.731 -12.885  1.00 66.06           C  
ANISOU 2746  CB  ALA A 363     7429   7487  10185  -1934    -79    545       C  
ATOM   2747  N   ALA A 364      43.263  30.920 -13.892  1.00 89.57           N  
ANISOU 2747  N   ALA A 364    10160  10478  13396  -2100    -69    726       N  
ATOM   2748  CA  ALA A 364      44.246  31.931 -14.268  1.00 94.81           C  
ANISOU 2748  CA  ALA A 364    10726  11114  14185  -2182    -81    792       C  
ATOM   2749  C   ALA A 364      44.102  33.194 -13.428  1.00 96.68           C  
ANISOU 2749  C   ALA A 364    10983  11230  14523  -2219   -184    695       C  
ATOM   2750  O   ALA A 364      44.911  33.441 -12.528  1.00104.80           O  
ANISOU 2750  O   ALA A 364    11943  12255  15622  -2252   -261    625       O  
ATOM   2751  CB  ALA A 364      44.119  32.269 -15.755  1.00 97.00           C  
ANISOU 2751  CB  ALA A 364    11016  11403  14435  -2181     13    927       C  
ATOM   2752  N   ASP A 365      43.084  34.005 -13.722  1.00 89.31           N  
ANISOU 2752  N   ASP A 365    10140  10199  13596  -2211   -190    689       N  
ATOM   2753  CA  ASP A 365      42.801  35.206 -12.950  1.00 81.07           C  
ANISOU 2753  CA  ASP A 365     9126   9036  12640  -2236   -287    595       C  
ATOM   2754  C   ASP A 365      41.695  34.890 -11.954  1.00 65.85           C  
ANISOU 2754  C   ASP A 365     7287   7066  10665  -2185   -344    467       C  
ATOM   2755  O   ASP A 365      40.512  34.887 -12.329  1.00 62.52           O  
ANISOU 2755  O   ASP A 365     6959   6607  10188  -2146   -314    473       O  
ATOM   2756  CB  ASP A 365      42.390  36.361 -13.868  1.00 83.89           C  
ANISOU 2756  CB  ASP A 365     9523   9311  13041  -2256   -262    670       C  
ATOM   2757  CG  ASP A 365      42.288  37.687 -13.133  1.00 89.23           C  
ANISOU 2757  CG  ASP A 365    10215   9865  13825  -2288   -363    584       C  
ATOM   2758  OD1 ASP A 365      42.639  37.739 -11.935  1.00 91.05           O  
ANISOU 2758  OD1 ASP A 365    10420  10080  14096  -2295   -453    468       O  
ATOM   2759  OD2 ASP A 365      41.857  38.680 -13.756  1.00 90.96           O  
ANISOU 2759  OD2 ASP A 365    10471  10002  14086  -2301   -356    633       O  
ATOM   2760  N   PRO A 366      42.013  34.619 -10.685  1.00 54.20           N  
ANISOU 2760  N   PRO A 366     5786   5601   9208  -2181   -428    348       N  
ATOM   2761  CA  PRO A 366      40.949  34.220  -9.749  1.00 52.71           C  
ANISOU 2761  CA  PRO A 366     5679   5385   8965  -2126   -477    229       C  
ATOM   2762  C   PRO A 366      40.025  35.362  -9.372  1.00 49.70           C  
ANISOU 2762  C   PRO A 366     5376   4887   8622  -2115   -539    151       C  
ATOM   2763  O   PRO A 366      38.809  35.154  -9.279  1.00 52.69           O  
ANISOU 2763  O   PRO A 366     5845   5238   8939  -2065   -531    114       O  
ATOM   2764  CB  PRO A 366      41.728  33.690  -8.533  1.00 45.10           C  
ANISOU 2764  CB  PRO A 366     4656   4481   8000  -2117   -550    125       C  
ATOM   2765  CG  PRO A 366      43.164  33.573  -8.983  1.00 56.18           C  
ANISOU 2765  CG  PRO A 366     5934   5947   9466  -2177   -526    212       C  
ATOM   2766  CD  PRO A 366      43.338  34.599 -10.049  1.00 49.59           C  
ANISOU 2766  CD  PRO A 366     5093   5061   8688  -2221   -481    315       C  
ATOM   2767  N   HIS A 367      40.566  36.566  -9.158  1.00 45.48           N  
ANISOU 2767  N   HIS A 367     4807   4281   8190  -2158   -601    127       N  
ATOM   2768  CA  HIS A 367      39.751  37.676  -8.671  1.00 61.10           C  
ANISOU 2768  CA  HIS A 367     6855   6147  10213  -2143   -673     41       C  
ATOM   2769  C   HIS A 367      38.592  37.970  -9.616  1.00 70.85           C  
ANISOU 2769  C   HIS A 367     8175   7334  11411  -2118   -609    111       C  
ATOM   2770  O   HIS A 367      37.446  38.121  -9.180  1.00 60.97           O  
ANISOU 2770  O   HIS A 367     7006   6034  10126  -2068   -639     33       O  
ATOM   2771  CB  HIS A 367      40.614  38.923  -8.479  1.00 64.25           C  
ANISOU 2771  CB  HIS A 367     7197   6478  10739  -2200   -741     28       C  
ATOM   2772  CG  HIS A 367      39.877  40.077  -7.874  1.00 74.01           C  
ANISOU 2772  CG  HIS A 367     8496   7596  12029  -2182   -826    -70       C  
ATOM   2773  ND1 HIS A 367      39.011  40.870  -8.597  1.00 79.32           N  
ANISOU 2773  ND1 HIS A 367     9234   8186  12719  -2175   -799    -19       N  
ATOM   2774  CD2 HIS A 367      39.872  40.568  -6.613  1.00 77.59           C  
ANISOU 2774  CD2 HIS A 367     8955   8005  12520  -2163   -939   -220       C  
ATOM   2775  CE1 HIS A 367      38.507  41.802  -7.807  1.00 82.47           C  
ANISOU 2775  CE1 HIS A 367     9675   8491  13168  -2153   -891   -131       C  
ATOM   2776  NE2 HIS A 367      39.013  41.641  -6.598  1.00 78.84           N  
ANISOU 2776  NE2 HIS A 367     9181   8054  12720  -2144   -977   -255       N  
ATOM   2777  N   GLU A 368      38.872  38.052 -10.918  1.00 75.50           N  
ANISOU 2777  N   GLU A 368     8742   7940  12003  -2147   -522    256       N  
ATOM   2778  CA  GLU A 368      37.804  38.274 -11.886  1.00 83.47           C  
ANISOU 2778  CA  GLU A 368     9830   8916  12971  -2120   -460    327       C  
ATOM   2779  C   GLU A 368      36.839  37.099 -11.960  1.00 74.00           C  
ANISOU 2779  C   GLU A 368     8693   7774  11649  -2059   -408    318       C  
ATOM   2780  O   GLU A 368      35.711  37.265 -12.439  1.00 76.15           O  
ANISOU 2780  O   GLU A 368     9043   8009  11881  -2023   -380    335       O  
ATOM   2781  CB  GLU A 368      38.393  38.544 -13.272  1.00100.72           C  
ANISOU 2781  CB  GLU A 368    11970  11122  15176  -2160   -379    485       C  
ATOM   2782  CG  GLU A 368      38.842  37.295 -14.014  1.00112.78           C  
ANISOU 2782  CG  GLU A 368    13459  12773  16618  -2151   -283    580       C  
ATOM   2783  CD  GLU A 368      38.824  37.470 -15.521  1.00121.77           C  
ANISOU 2783  CD  GLU A 368    14599  13934  17736  -2158   -190    729       C  
ATOM   2784  OE1 GLU A 368      38.052  38.319 -16.014  1.00123.74           O  
ANISOU 2784  OE1 GLU A 368    14905  14104  18005  -2150   -191    754       O  
ATOM   2785  OE2 GLU A 368      39.581  36.756 -16.212  1.00124.41           O  
ANISOU 2785  OE2 GLU A 368    14872  14366  18031  -2166   -118    821       O  
ATOM   2786  N   CYS A 369      37.248  35.921 -11.488  1.00 64.63           N  
ANISOU 2786  N   CYS A 369     7473   6676  10407  -2047   -398    293       N  
ATOM   2787  CA  CYS A 369      36.389  34.745 -11.574  1.00 62.20           C  
ANISOU 2787  CA  CYS A 369     7221   6422   9989  -1994   -347    292       C  
ATOM   2788  C   CYS A 369      35.378  34.713 -10.430  1.00 52.48           C  
ANISOU 2788  C   CYS A 369     6057   5147   8734  -1947   -417    153       C  
ATOM   2789  O   CYS A 369      34.164  34.663 -10.659  1.00 46.22           O  
ANISOU 2789  O   CYS A 369     5346   4327   7891  -1906   -394    147       O  
ATOM   2790  CB  CYS A 369      37.245  33.474 -11.589  1.00 65.45           C  
ANISOU 2790  CB  CYS A 369     7568   6945  10355  -1998   -305    331       C  
ATOM   2791  SG  CYS A 369      36.375  31.986 -12.137  1.00 66.73           S  
ANISOU 2791  SG  CYS A 369     7815   7221  10319  -1900   -200    362       S  
ATOM   2792  N   TYR A 370      35.858  34.748  -9.186  1.00 43.99           N  
ANISOU 2792  N   TYR A 370     4949   4072   7693  -1949   -503     38       N  
ATOM   2793  CA  TYR A 370      34.944  34.691  -8.052  1.00 48.72           C  
ANISOU 2793  CA  TYR A 370     5620   4667   8223  -1876   -558   -103       C  
ATOM   2794  C   TYR A 370      34.245  36.018  -7.776  1.00 59.14           C  
ANISOU 2794  C   TYR A 370     6977   5855   9637  -1886   -634   -168       C  
ATOM   2795  O   TYR A 370      33.402  36.075  -6.875  1.00 43.05           O  
ANISOU 2795  O   TYR A 370     4996   3803   7560  -1829   -684   -285       O  
ATOM   2796  CB  TYR A 370      35.672  34.200  -6.788  1.00 41.37           C  
ANISOU 2796  CB  TYR A 370     4654   3813   7251  -1846   -616   -210       C  
ATOM   2797  CG  TYR A 370      36.851  35.030  -6.311  1.00 46.40           C  
ANISOU 2797  CG  TYR A 370     5199   4399   8032  -1918   -707   -248       C  
ATOM   2798  CD1 TYR A 370      36.667  36.285  -5.747  1.00 46.09           C  
ANISOU 2798  CD1 TYR A 370     5165   4246   8100  -1939   -806   -337       C  
ATOM   2799  CD2 TYR A 370      38.148  34.534  -6.384  1.00 39.88           C  
ANISOU 2799  CD2 TYR A 370     4284   3650   7218  -1952   -693   -203       C  
ATOM   2800  CE1 TYR A 370      37.737  37.033  -5.301  1.00 41.88           C  
ANISOU 2800  CE1 TYR A 370     4563   3691   7657  -1980   -877   -374       C  
ATOM   2801  CE2 TYR A 370      39.228  35.281  -5.938  1.00 41.67           C  
ANISOU 2801  CE2 TYR A 370     4420   3832   7580  -2020   -779   -240       C  
ATOM   2802  CZ  TYR A 370      39.013  36.529  -5.396  1.00 42.21           C  
ANISOU 2802  CZ  TYR A 370     4511   3804   7722  -2025   -865   -325       C  
ATOM   2803  OH  TYR A 370      40.070  37.286  -4.945  1.00 50.22           O  
ANISOU 2803  OH  TYR A 370     5454   4796   8830  -2068   -938   -364       O  
ATOM   2804  N   ALA A 371      34.561  37.080  -8.523  1.00 54.95           N  
ANISOU 2804  N   ALA A 371     6433   5264   9182  -1927   -625    -96       N  
ATOM   2805  CA  ALA A 371      33.830  38.334  -8.377  1.00 49.01           C  
ANISOU 2805  CA  ALA A 371     5733   4407   8484  -1912   -679   -147       C  
ATOM   2806  C   ALA A 371      32.413  38.251  -8.927  1.00 54.47           C  
ANISOU 2806  C   ALA A 371     6510   5074   9111  -1864   -631   -123       C  
ATOM   2807  O   ALA A 371      31.611  39.154  -8.663  1.00 59.72           O  
ANISOU 2807  O   ALA A 371     7226   5658   9807  -1836   -679   -183       O  
ATOM   2808  CB  ALA A 371      34.584  39.474  -9.064  1.00 57.42           C  
ANISOU 2808  CB  ALA A 371     6754   5410   9653  -1971   -682    -68       C  
ATOM   2809  N   LYS A 372      32.088  37.200  -9.678  1.00 52.95           N  
ANISOU 2809  N   LYS A 372     6334   4951   8834  -1851   -540    -38       N  
ATOM   2810  CA  LYS A 372      30.749  36.985 -10.207  1.00 54.82           C  
ANISOU 2810  CA  LYS A 372     6648   5177   9005  -1805   -493    -15       C  
ATOM   2811  C   LYS A 372      29.923  36.043  -9.339  1.00 48.89           C  
ANISOU 2811  C   LYS A 372     5940   4469   8168  -1748   -505   -110       C  
ATOM   2812  O   LYS A 372      28.829  35.641  -9.750  1.00 60.50           O  
ANISOU 2812  O   LYS A 372     7475   5963   9551  -1697   -452    -90       O  
ATOM   2813  CB  LYS A 372      30.826  36.432 -11.631  1.00 54.01           C  
ANISOU 2813  CB  LYS A 372     6542   5126   8854  -1819   -387    136       C  
ATOM   2814  CG  LYS A 372      31.619  37.283 -12.606  1.00 59.46           C  
ANISOU 2814  CG  LYS A 372     7189   5789   9614  -1870   -362    243       C  
ATOM   2815  CD  LYS A 372      31.936  36.498 -13.870  1.00 59.36           C  
ANISOU 2815  CD  LYS A 372     7157   5858   9541  -1878   -258    381       C  
ATOM   2816  CE  LYS A 372      32.636  37.364 -14.904  1.00 66.72           C  
ANISOU 2816  CE  LYS A 372     8047   6766  10536  -1924   -229    493       C  
ATOM   2817  NZ  LYS A 372      33.859  38.011 -14.356  1.00 73.43           N  
ANISOU 2817  NZ  LYS A 372     8821   7593  11485  -1979   -285    470       N  
ATOM   2818  N   VAL A 373      30.417  35.685  -8.151  1.00 53.33           N  
ANISOU 2818  N   VAL A 373     6480   5087   8695  -1722   -554   -214       N  
ATOM   2819  CA  VAL A 373      29.744  34.685  -7.330  1.00 55.37           C  
ANISOU 2819  CA  VAL A 373     6789   5449   8801  -1634   -536   -292       C  
ATOM   2820  C   VAL A 373      28.382  35.166  -6.841  1.00 51.18           C  
ANISOU 2820  C   VAL A 373     6330   4874   8244  -1574   -569   -378       C  
ATOM   2821  O   VAL A 373      27.507  34.342  -6.549  1.00 48.02           O  
ANISOU 2821  O   VAL A 373     5980   4551   7714  -1504   -527   -404       O  
ATOM   2822  CB  VAL A 373      30.644  34.274  -6.145  1.00 61.39           C  
ANISOU 2822  CB  VAL A 373     7508   6281   9536  -1619   -587   -380       C  
ATOM   2823  CG1 VAL A 373      30.659  35.353  -5.074  1.00 63.20           C  
ANISOU 2823  CG1 VAL A 373     7730   6433   9848  -1616   -704   -513       C  
ATOM   2824  CG2 VAL A 373      30.197  32.937  -5.569  1.00 62.66           C  
ANISOU 2824  CG2 VAL A 373     7708   6571   9527  -1538   -538   -410       C  
ATOM   2825  N   PHE A 374      28.169  36.479  -6.749  1.00 38.32           N  
ANISOU 2825  N   PHE A 374     4703   3119   6737  -1599   -643   -422       N  
ATOM   2826  CA  PHE A 374      26.864  36.986  -6.350  1.00 45.05           C  
ANISOU 2826  CA  PHE A 374     5621   3928   7568  -1537   -674   -503       C  
ATOM   2827  C   PHE A 374      25.856  36.950  -7.489  1.00 46.73           C  
ANISOU 2827  C   PHE A 374     5881   4117   7757  -1529   -603   -409       C  
ATOM   2828  O   PHE A 374      24.648  36.931  -7.229  1.00 56.50           O  
ANISOU 2828  O   PHE A 374     7175   5363   8928  -1463   -599   -461       O  
ATOM   2829  CB  PHE A 374      26.989  38.411  -5.807  1.00 60.75           C  
ANISOU 2829  CB  PHE A 374     7598   5786   9699  -1558   -789   -595       C  
ATOM   2830  CG  PHE A 374      27.232  38.473  -4.325  1.00 66.65           C  
ANISOU 2830  CG  PHE A 374     8336   6569  10420  -1511   -873   -750       C  
ATOM   2831  CD1 PHE A 374      26.892  37.405  -3.511  1.00 76.73           C  
ANISOU 2831  CD1 PHE A 374     9634   7983  11536  -1433   -842   -806       C  
ATOM   2832  CD2 PHE A 374      27.802  39.594  -3.747  1.00 71.34           C  
ANISOU 2832  CD2 PHE A 374     8900   7070  11135  -1536   -980   -835       C  
ATOM   2833  CE1 PHE A 374      27.115  37.455  -2.148  1.00 79.20           C  
ANISOU 2833  CE1 PHE A 374     9938   8340  11814  -1383   -918   -944       C  
ATOM   2834  CE2 PHE A 374      28.027  39.649  -2.383  1.00 75.45           C  
ANISOU 2834  CE2 PHE A 374     9409   7620  11637  -1492  -1069   -988       C  
ATOM   2835  CZ  PHE A 374      27.683  38.578  -1.583  1.00 73.43           C  
ANISOU 2835  CZ  PHE A 374     9176   7512  11211  -1409  -1033  -1040       C  
ATOM   2836  N   ASP A 375      26.323  36.930  -8.740  1.00 38.08           N  
ANISOU 2836  N   ASP A 375     4761   2998   6708  -1592   -547   -272       N  
ATOM   2837  CA  ASP A 375      25.406  36.804  -9.867  1.00 42.36           C  
ANISOU 2837  CA  ASP A 375     5347   3532   7216  -1579   -477   -180       C  
ATOM   2838  C   ASP A 375      24.874  35.384 -10.001  1.00 46.71           C  
ANISOU 2838  C   ASP A 375     5930   4214   7605  -1524   -393   -157       C  
ATOM   2839  O   ASP A 375      23.718  35.193 -10.396  1.00 41.67           O  
ANISOU 2839  O   ASP A 375     5343   3585   6905  -1480   -356   -144       O  
ATOM   2840  CB  ASP A 375      26.095  37.235 -11.161  1.00 48.88           C  
ANISOU 2840  CB  ASP A 375     6140   4323   8108  -1643   -434    -40       C  
ATOM   2841  CG  ASP A 375      26.531  38.686 -11.134  1.00 56.57           C  
ANISOU 2841  CG  ASP A 375     7098   5208   9188  -1669   -493    -50       C  
ATOM   2842  OD1 ASP A 375      25.789  39.521 -10.574  1.00 62.02           O  
ANISOU 2842  OD1 ASP A 375     7826   5825   9914  -1634   -556   -138       O  
ATOM   2843  OD2 ASP A 375      27.615  38.991 -11.672  1.00 64.31           O  
ANISOU 2843  OD2 ASP A 375     8027   6191  10218  -1722   -476     29       O  
ATOM   2844  N   GLU A 376      25.693  34.379  -9.687  1.00 43.34           N  
ANISOU 2844  N   GLU A 376     5470   3885   7111  -1525   -364   -151       N  
ATOM   2845  CA  GLU A 376      25.215  33.003  -9.715  1.00 44.28           C  
ANISOU 2845  CA  GLU A 376     5620   4120   7084  -1473   -292   -136       C  
ATOM   2846  C   GLU A 376      24.380  32.655  -8.489  1.00 44.74           C  
ANISOU 2846  C   GLU A 376     5717   4228   7056  -1400   -319   -251       C  
ATOM   2847  O   GLU A 376      23.632  31.673  -8.525  1.00 47.81           O  
ANISOU 2847  O   GLU A 376     6141   4692   7332  -1353   -264   -241       O  
ATOM   2848  CB  GLU A 376      26.392  32.034  -9.850  1.00 55.66           C  
ANISOU 2848  CB  GLU A 376     7014   5646   8487  -1495   -252    -84       C  
ATOM   2849  CG  GLU A 376      27.267  31.921  -8.616  1.00 72.09           C  
ANISOU 2849  CG  GLU A 376     9057   7764  10572  -1492   -309   -170       C  
ATOM   2850  CD  GLU A 376      28.494  31.063  -8.854  1.00 81.01           C  
ANISOU 2850  CD  GLU A 376    10133   8969  11677  -1516   -271   -111       C  
ATOM   2851  OE1 GLU A 376      29.613  31.617  -8.878  1.00 84.11           O  
ANISOU 2851  OE1 GLU A 376    10462   9330  12165  -1573   -306    -96       O  
ATOM   2852  OE2 GLU A 376      28.339  29.834  -9.018  1.00 80.49           O  
ANISOU 2852  OE2 GLU A 376    10088   8993  11500  -1477   -208    -80       O  
ATOM   2853  N   PHE A 377      24.490  33.437  -7.410  1.00 41.75           N  
ANISOU 2853  N   PHE A 377     5329   3809   6726  -1388   -403   -360       N  
ATOM   2854  CA  PHE A 377      23.574  33.279  -6.285  1.00 32.42           C  
ANISOU 2854  CA  PHE A 377     4185   2673   5463  -1312   -429   -469       C  
ATOM   2855  C   PHE A 377      22.165  33.722  -6.653  1.00 38.86           C  
ANISOU 2855  C   PHE A 377     5052   3446   6269  -1276   -418   -474       C  
ATOM   2856  O   PHE A 377      21.192  33.258  -6.048  1.00 43.96           O  
ANISOU 2856  O   PHE A 377     5732   4155   6818  -1209   -403   -527       O  
ATOM   2857  CB  PHE A 377      24.061  34.083  -5.079  1.00 40.50           C  
ANISOU 2857  CB  PHE A 377     5183   3663   6541  -1302   -528   -591       C  
ATOM   2858  CG  PHE A 377      25.182  33.434  -4.318  1.00 46.04           C  
ANISOU 2858  CG  PHE A 377     5842   4443   7208  -1306   -543   -619       C  
ATOM   2859  CD1 PHE A 377      25.717  32.225  -4.730  1.00 40.19           C  
ANISOU 2859  CD1 PHE A 377     5086   3789   6395  -1318   -471   -536       C  
ATOM   2860  CD2 PHE A 377      25.700  34.039  -3.184  1.00 43.16           C  
ANISOU 2860  CD2 PHE A 377     5452   4065   6881  -1293   -635   -735       C  
ATOM   2861  CE1 PHE A 377      26.750  31.633  -4.024  1.00 48.95           C  
ANISOU 2861  CE1 PHE A 377     6156   4971   7473  -1316   -487   -561       C  
ATOM   2862  CE2 PHE A 377      26.730  33.452  -2.475  1.00 50.81           C  
ANISOU 2862  CE2 PHE A 377     6380   5110   7816  -1293   -653   -762       C  
ATOM   2863  CZ  PHE A 377      27.256  32.248  -2.896  1.00 51.80           C  
ANISOU 2863  CZ  PHE A 377     6490   5322   7870  -1304   -578   -673       C  
ATOM   2864  N   LYS A 378      22.042  34.615  -7.638  1.00 33.58           N  
ANISOU 2864  N   LYS A 378     4386   2673   5700  -1317   -424   -416       N  
ATOM   2865  CA  LYS A 378      20.743  35.200  -7.967  1.00 43.70           C  
ANISOU 2865  CA  LYS A 378     5714   3903   6988  -1281   -426   -427       C  
ATOM   2866  C   LYS A 378      19.706  34.163  -8.387  1.00 37.79           C  
ANISOU 2866  C   LYS A 378     5002   3240   6118  -1238   -346   -384       C  
ATOM   2867  O   LYS A 378      18.600  34.172  -7.819  1.00 32.26           O  
ANISOU 2867  O   LYS A 378     4333   2565   5360  -1175   -354   -452       O  
ATOM   2868  CB  LYS A 378      20.929  36.284  -9.035  1.00 59.08           C  
ANISOU 2868  CB  LYS A 378     7656   5726   9067  -1339   -443   -353       C  
ATOM   2869  CG  LYS A 378      19.707  36.524  -9.907  1.00 69.31           C  
ANISOU 2869  CG  LYS A 378     8995   6988  10350  -1312   -409   -306       C  
ATOM   2870  CD  LYS A 378      18.658  37.337  -9.171  1.00 75.88           C  
ANISOU 2870  CD  LYS A 378     9862   7773  11196  -1251   -470   -415       C  
ATOM   2871  CE  LYS A 378      18.875  38.826  -9.365  1.00 84.93           C  
ANISOU 2871  CE  LYS A 378    11004   8768  12496  -1283   -547   -427       C  
ATOM   2872  NZ  LYS A 378      18.029  39.631  -8.442  1.00 90.45           N  
ANISOU 2872  NZ  LYS A 378    11732   9423  13211  -1216   -621   -558       N  
ATOM   2873  N   PRO A 379      19.964  33.264  -9.347  1.00 41.25           N  
ANISOU 2873  N   PRO A 379     5435   3725   6512  -1265   -272   -279       N  
ATOM   2874  CA  PRO A 379      18.934  32.264  -9.669  1.00 36.87           C  
ANISOU 2874  CA  PRO A 379     4915   3246   5847  -1222   -206   -251       C  
ATOM   2875  C   PRO A 379      18.691  31.282  -8.539  1.00 42.65           C  
ANISOU 2875  C   PRO A 379     5652   4082   6471  -1173   -195   -316       C  
ATOM   2876  O   PRO A 379      17.582  30.744  -8.427  1.00 40.52           O  
ANISOU 2876  O   PRO A 379     5410   3862   6123  -1127   -164   -327       O  
ATOM   2877  CB  PRO A 379      19.493  31.567 -10.917  1.00 29.43           C  
ANISOU 2877  CB  PRO A 379     3962   2327   4893  -1264   -140   -131       C  
ATOM   2878  CG  PRO A 379      20.958  31.743 -10.814  1.00 34.23           C  
ANISOU 2878  CG  PRO A 379     4522   2921   5564  -1316   -161   -113       C  
ATOM   2879  CD  PRO A 379      21.162  33.095 -10.192  1.00 36.39           C  
ANISOU 2879  CD  PRO A 379     4782   3100   5945  -1331   -244   -182       C  
ATOM   2880  N   LEU A 380      19.694  31.034  -7.693  1.00 36.11           N  
ANISOU 2880  N   LEU A 380     4793   3289   5637  -1181   -221   -355       N  
ATOM   2881  CA  LEU A 380      19.505  30.118  -6.575  1.00 41.71           C  
ANISOU 2881  CA  LEU A 380     5507   4100   6242  -1130   -212   -411       C  
ATOM   2882  C   LEU A 380      18.592  30.712  -5.511  1.00 41.63           C  
ANISOU 2882  C   LEU A 380     5514   4094   6209  -1069   -259   -518       C  
ATOM   2883  O   LEU A 380      17.933  29.967  -4.779  1.00 34.97           O  
ANISOU 2883  O   LEU A 380     4683   3337   5265  -1017   -235   -549       O  
ATOM   2884  CB  LEU A 380      20.858  29.745  -5.969  1.00 40.96           C  
ANISOU 2884  CB  LEU A 380     5373   4042   6147  -1150   -232   -425       C  
ATOM   2885  CG  LEU A 380      21.765  28.890  -6.854  1.00 38.12           C  
ANISOU 2885  CG  LEU A 380     4993   3708   5781  -1195   -179   -325       C  
ATOM   2886  CD1 LEU A 380      23.168  28.826  -6.278  1.00 29.66           C  
ANISOU 2886  CD1 LEU A 380     3876   2659   4736  -1218   -213   -345       C  
ATOM   2887  CD2 LEU A 380      21.185  27.491  -7.021  1.00 41.00           C  
ANISOU 2887  CD2 LEU A 380     5386   4159   6036  -1163   -109   -281       C  
ATOM   2888  N   VAL A 381      18.544  32.040  -5.407  1.00 30.60           N  
ANISOU 2888  N   VAL A 381     4115   2605   4905  -1073   -325   -574       N  
ATOM   2889  CA  VAL A 381      17.618  32.682  -4.481  1.00 37.51           C  
ANISOU 2889  CA  VAL A 381     5009   3481   5761  -1007   -371   -681       C  
ATOM   2890  C   VAL A 381      16.215  32.732  -5.074  1.00 46.79           C  
ANISOU 2890  C   VAL A 381     6218   4650   6910   -976   -334   -655       C  
ATOM   2891  O   VAL A 381      15.226  32.452  -4.386  1.00 34.49           O  
ANISOU 2891  O   VAL A 381     4674   3162   5270   -911   -323   -706       O  
ATOM   2892  CB  VAL A 381      18.129  34.086  -4.109  1.00 35.73           C  
ANISOU 2892  CB  VAL A 381     4771   3153   5653  -1018   -466   -760       C  
ATOM   2893  CG1 VAL A 381      17.012  34.923  -3.503  1.00 44.13           C  
ANISOU 2893  CG1 VAL A 381     5860   4193   6713   -948   -512   -860       C  
ATOM   2894  CG2 VAL A 381      19.307  33.989  -3.151  1.00 37.66           C  
ANISOU 2894  CG2 VAL A 381     4981   3430   5900  -1026   -514   -820       C  
ATOM   2895  N   GLU A 382      16.106  33.073  -6.361  1.00 32.36           N  
ANISOU 2895  N   GLU A 382     4400   2748   5149  -1019   -313   -572       N  
ATOM   2896  CA  GLU A 382      14.800  33.208  -6.995  1.00 36.01           C  
ANISOU 2896  CA  GLU A 382     4890   3197   5593   -990   -285   -548       C  
ATOM   2897  C   GLU A 382      14.085  31.875  -7.170  1.00 30.44           C  
ANISOU 2897  C   GLU A 382     4195   2595   4775   -970   -208   -500       C  
ATOM   2898  O   GLU A 382      12.854  31.861  -7.283  1.00 36.25           O  
ANISOU 2898  O   GLU A 382     4949   3351   5474   -929   -189   -509       O  
ATOM   2899  CB  GLU A 382      14.943  33.888  -8.358  1.00 39.43           C  
ANISOU 2899  CB  GLU A 382     5331   3528   6123  -1041   -282   -465       C  
ATOM   2900  CG  GLU A 382      15.444  35.319  -8.294  1.00 50.02           C  
ANISOU 2900  CG  GLU A 382     6665   4747   7593  -1063   -360   -503       C  
ATOM   2901  CD  GLU A 382      15.492  35.975  -9.659  1.00 60.62           C  
ANISOU 2901  CD  GLU A 382     8015   5993   9025  -1110   -352   -407       C  
ATOM   2902  OE1 GLU A 382      15.534  35.241 -10.670  1.00 67.51           O  
ANISOU 2902  OE1 GLU A 382     8890   6901   9861  -1137   -285   -305       O  
ATOM   2903  OE2 GLU A 382      15.484  37.222  -9.722  1.00 66.86           O  
ANISOU 2903  OE2 GLU A 382     8811   6672   9922  -1116   -414   -433       O  
ATOM   2904  N   GLU A 383      14.819  30.757  -7.198  1.00 30.65           N  
ANISOU 2904  N   GLU A 383     4209   2686   4751   -997   -165   -450       N  
ATOM   2905  CA  GLU A 383      14.174  29.472  -7.468  1.00 28.25           C  
ANISOU 2905  CA  GLU A 383     3916   2465   4354   -985    -96   -398       C  
ATOM   2906  C   GLU A 383      13.223  29.052  -6.352  1.00 35.73           C  
ANISOU 2906  C   GLU A 383     4865   3497   5212   -922    -90   -461       C  
ATOM   2907  O   GLU A 383      12.063  28.719  -6.655  1.00 37.85           O  
ANISOU 2907  O   GLU A 383     5146   3794   5440   -898    -55   -443       O  
ATOM   2908  CB  GLU A 383      15.235  28.404  -7.754  1.00 37.23           C  
ANISOU 2908  CB  GLU A 383     5040   3643   5465  -1024    -59   -334       C  
ATOM   2909  CG  GLU A 383      14.814  27.372  -8.789  1.00 54.90           C  
ANISOU 2909  CG  GLU A 383     7292   5909   7658  -1038      6   -248       C  
ATOM   2910  CD  GLU A 383      15.892  26.341  -9.058  1.00 73.19           C  
ANISOU 2910  CD  GLU A 383     9596   8262   9949  -1069     39   -192       C  
ATOM   2911  OE1 GLU A 383      16.256  25.601  -8.120  1.00 83.78           O  
ANISOU 2911  OE1 GLU A 383    10929   9668  11236  -1052     43   -217       O  
ATOM   2912  OE2 GLU A 383      16.377  26.269 -10.207  1.00 81.96           O  
ANISOU 2912  OE2 GLU A 383    10707   9342  11093  -1104     61   -122       O  
ATOM   2913  N   PRO A 384      13.615  29.034  -5.071  1.00 38.94           N  
ANISOU 2913  N   PRO A 384     5258   3953   5584   -890   -120   -533       N  
ATOM   2914  CA  PRO A 384      12.622  28.707  -4.035  1.00 36.95           C  
ANISOU 2914  CA  PRO A 384     5007   3790   5244   -824   -109   -587       C  
ATOM   2915  C   PRO A 384      11.562  29.779  -3.869  1.00 40.07           C  
ANISOU 2915  C   PRO A 384     5410   4153   5661   -776   -143   -654       C  
ATOM   2916  O   PRO A 384      10.427  29.455  -3.498  1.00 31.44           O  
ANISOU 2916  O   PRO A 384     4317   3129   4501   -728   -115   -667       O  
ATOM   2917  CB  PRO A 384      13.471  28.548  -2.766  1.00 40.41           C  
ANISOU 2917  CB  PRO A 384     5427   4284   5642   -801   -140   -648       C  
ATOM   2918  CG  PRO A 384      14.681  29.364  -3.023  1.00 32.03           C  
ANISOU 2918  CG  PRO A 384     4356   3136   4678   -845   -195   -664       C  
ATOM   2919  CD  PRO A 384      14.958  29.209  -4.488  1.00 37.38           C  
ANISOU 2919  CD  PRO A 384     5040   3748   5415   -910   -160   -565       C  
ATOM   2920  N   GLN A 385      11.894  31.046  -4.128  1.00 33.54           N  
ANISOU 2920  N   GLN A 385     4588   3225   4932   -786   -204   -694       N  
ATOM   2921  CA  GLN A 385      10.885  32.098  -4.055  1.00 32.68           C  
ANISOU 2921  CA  GLN A 385     4491   3075   4853   -736   -240   -757       C  
ATOM   2922  C   GLN A 385       9.789  31.877  -5.087  1.00 38.13           C  
ANISOU 2922  C   GLN A 385     5193   3757   5536   -739   -192   -690       C  
ATOM   2923  O   GLN A 385       8.601  32.051  -4.791  1.00 35.34           O  
ANISOU 2923  O   GLN A 385     4842   3443   5144   -682   -186   -728       O  
ATOM   2924  CB  GLN A 385      11.535  33.467  -4.249  1.00 36.32           C  
ANISOU 2924  CB  GLN A 385     4956   3410   5434   -756   -316   -801       C  
ATOM   2925  CG  GLN A 385      12.462  33.877  -3.119  1.00 51.92           C  
ANISOU 2925  CG  GLN A 385     6916   5387   7424   -742   -381   -893       C  
ATOM   2926  CD  GLN A 385      13.110  35.225  -3.358  1.00 51.56           C  
ANISOU 2926  CD  GLN A 385     6872   5205   7512   -770   -462   -932       C  
ATOM   2927  OE1 GLN A 385      13.110  35.737  -4.478  1.00 48.35           O  
ANISOU 2927  OE1 GLN A 385     6477   4701   7193   -816   -460   -866       O  
ATOM   2928  NE2 GLN A 385      13.669  35.808  -2.304  1.00 49.67           N  
ANISOU 2928  NE2 GLN A 385     6622   4958   7294   -743   -535  -1039       N  
ATOM   2929  N   ASN A 386      10.168  31.491  -6.308  1.00 37.47           N  
ANISOU 2929  N   ASN A 386     5118   3633   5488   -802   -157   -592       N  
ATOM   2930  CA  ASN A 386       9.173  31.205  -7.335  1.00 34.84           C  
ANISOU 2930  CA  ASN A 386     4796   3298   5144   -805   -115   -528       C  
ATOM   2931  C   ASN A 386       8.402  29.931  -7.014  1.00 28.04           C  
ANISOU 2931  C   ASN A 386     3926   2550   4179   -784    -55   -506       C  
ATOM   2932  O   ASN A 386       7.186  29.865  -7.227  1.00 34.91           O  
ANISOU 2932  O   ASN A 386     4796   3448   5022   -753    -35   -503       O  
ATOM   2933  CB  ASN A 386       9.846  31.091  -8.704  1.00 28.21           C  
ANISOU 2933  CB  ASN A 386     3966   2395   4359   -871    -95   -431       C  
ATOM   2934  CG  ASN A 386      10.372  32.421  -9.210  1.00 51.27           C  
ANISOU 2934  CG  ASN A 386     6894   5197   7391   -893   -148   -434       C  
ATOM   2935  OD1 ASN A 386      10.200  33.456  -8.567  1.00 54.87           O  
ANISOU 2935  OD1 ASN A 386     7352   5606   7891   -860   -206   -513       O  
ATOM   2936  ND2 ASN A 386      11.021  32.397 -10.369  1.00 53.32           N  
ANISOU 2936  ND2 ASN A 386     7156   5405   7697   -949   -130   -345       N  
ATOM   2937  N   LEU A 387       9.093  28.909  -6.500  1.00 31.92           N  
ANISOU 2937  N   LEU A 387     4406   3105   4616   -802    -28   -486       N  
ATOM   2938  CA  LEU A 387       8.431  27.647  -6.183  1.00 32.89           C  
ANISOU 2938  CA  LEU A 387     4520   3327   4649   -790     28   -455       C  
ATOM   2939  C   LEU A 387       7.384  27.828  -5.092  1.00 37.80           C  
ANISOU 2939  C   LEU A 387     5126   4022   5212   -721     25   -523       C  
ATOM   2940  O   LEU A 387       6.276  27.286  -5.188  1.00 36.63           O  
ANISOU 2940  O   LEU A 387     4968   3929   5019   -704     64   -499       O  
ATOM   2941  CB  LEU A 387       9.466  26.604  -5.760  1.00 37.82           C  
ANISOU 2941  CB  LEU A 387     5138   3998   5234   -817     50   -424       C  
ATOM   2942  CG  LEU A 387       8.900  25.266  -5.279  1.00 33.95           C  
ANISOU 2942  CG  LEU A 387     4638   3605   4655   -805    104   -390       C  
ATOM   2943  CD1 LEU A 387       8.617  24.348  -6.460  1.00 37.70           C  
ANISOU 2943  CD1 LEU A 387     5123   4067   5133   -848    148   -304       C  
ATOM   2944  CD2 LEU A 387       9.844  24.601  -4.289  1.00 27.46           C  
ANISOU 2944  CD2 LEU A 387     3807   2840   3785   -802    105   -397       C  
ATOM   2945  N   ILE A 388       7.717  28.585  -4.046  1.00 32.97           N  
ANISOU 2945  N   ILE A 388     4509   3419   4601   -679    -22   -610       N  
ATOM   2946  CA  ILE A 388       6.764  28.811  -2.965  1.00 28.92           C  
ANISOU 2946  CA  ILE A 388     3979   2985   4023   -603    -27   -680       C  
ATOM   2947  C   ILE A 388       5.627  29.709  -3.437  1.00 38.64           C  
ANISOU 2947  C   ILE A 388     5214   4179   5290   -567    -43   -709       C  
ATOM   2948  O   ILE A 388       4.461  29.497  -3.081  1.00 33.74           O  
ANISOU 2948  O   ILE A 388     4574   3634   4612   -520    -15   -721       O  
ATOM   2949  CB  ILE A 388       7.480  29.400  -1.736  1.00 30.99           C  
ANISOU 2949  CB  ILE A 388     4236   3267   4272   -560    -80   -775       C  
ATOM   2950  CG1 ILE A 388       8.555  28.442  -1.216  1.00 29.37           C  
ANISOU 2950  CG1 ILE A 388     4024   3113   4022   -589    -63   -744       C  
ATOM   2951  CG2 ILE A 388       6.485  29.682  -0.635  1.00 38.21           C  
ANISOU 2951  CG2 ILE A 388     5133   4273   5114   -471    -85   -852       C  
ATOM   2952  CD1 ILE A 388       8.137  26.986  -1.202  1.00 46.36           C  
ANISOU 2952  CD1 ILE A 388     6166   5354   6095   -603     12   -660       C  
ATOM   2953  N   LYS A 389       5.945  30.723  -4.249  1.00 32.15           N  
ANISOU 2953  N   LYS A 389     4412   3239   4564   -589    -87   -717       N  
ATOM   2954  CA  LYS A 389       4.913  31.624  -4.754  1.00 37.03           C  
ANISOU 2954  CA  LYS A 389     5037   3810   5222   -553   -108   -741       C  
ATOM   2955  C   LYS A 389       3.884  30.876  -5.593  1.00 31.86           C  
ANISOU 2955  C   LYS A 389     4375   3193   4538   -567    -50   -665       C  
ATOM   2956  O   LYS A 389       2.677  31.102  -5.454  1.00 39.95           O  
ANISOU 2956  O   LYS A 389     5385   4258   5535   -514    -44   -693       O  
ATOM   2957  CB  LYS A 389       5.552  32.748  -5.570  1.00 44.21           C  
ANISOU 2957  CB  LYS A 389     5972   4580   6247   -584   -162   -741       C  
ATOM   2958  CG  LYS A 389       4.562  33.761  -6.121  1.00 46.73           C  
ANISOU 2958  CG  LYS A 389     6301   4837   6615   -545   -191   -764       C  
ATOM   2959  CD  LYS A 389       5.275  35.024  -6.579  1.00 44.02           C  
ANISOU 2959  CD  LYS A 389     5983   4354   6390   -565   -258   -781       C  
ATOM   2960  CE  LYS A 389       4.293  36.062  -7.097  1.00 49.56           C  
ANISOU 2960  CE  LYS A 389     6699   4989   7144   -519   -290   -804       C  
ATOM   2961  NZ  LYS A 389       3.506  35.555  -8.255  1.00 56.33           N  
ANISOU 2961  NZ  LYS A 389     7557   5860   7985   -537   -239   -713       N  
ATOM   2962  N   GLN A 390       4.342  29.974  -6.462  1.00 31.57           N  
ANISOU 2962  N   GLN A 390     4345   3145   4504   -634    -11   -574       N  
ATOM   2963  CA  GLN A 390       3.418  29.244  -7.323  1.00 29.81           C  
ANISOU 2963  CA  GLN A 390     4116   2950   4259   -650     36   -507       C  
ATOM   2964  C   GLN A 390       2.593  28.230  -6.535  1.00 35.82           C  
ANISOU 2964  C   GLN A 390     4846   3833   4932   -625     83   -504       C  
ATOM   2965  O   GLN A 390       1.390  28.081  -6.777  1.00 37.13           O  
ANISOU 2965  O   GLN A 390     4993   4038   5077   -603    104   -494       O  
ATOM   2966  CB  GLN A 390       4.190  28.553  -8.447  1.00 27.25           C  
ANISOU 2966  CB  GLN A 390     3809   2583   3961   -722     60   -419       C  
ATOM   2967  CG  GLN A 390       4.808  29.515  -9.456  1.00 43.20           C  
ANISOU 2967  CG  GLN A 390     5856   4491   6069   -749     24   -399       C  
ATOM   2968  CD  GLN A 390       5.740  28.822 -10.432  1.00 61.14           C  
ANISOU 2968  CD  GLN A 390     8140   6735   8355   -813     50   -316       C  
ATOM   2969  OE1 GLN A 390       6.042  27.639 -10.286  1.00 70.81           O  
ANISOU 2969  OE1 GLN A 390     9359   8018   9529   -837     88   -283       O  
ATOM   2970  NE2 GLN A 390       6.204  29.561 -11.435  1.00 67.52           N  
ANISOU 2970  NE2 GLN A 390     8967   7457   9232   -838     29   -281       N  
ATOM   2971  N   ASN A 391       3.218  27.519  -5.594  1.00 27.79           N  
ANISOU 2971  N   ASN A 391     3819   2878   3862   -630    100   -507       N  
ATOM   2972  CA  ASN A 391       2.501  26.458  -4.890  1.00 33.42           C  
ANISOU 2972  CA  ASN A 391     4501   3704   4493   -615    151   -484       C  
ATOM   2973  C   ASN A 391       1.560  27.014  -3.832  1.00 28.48           C  
ANISOU 2973  C   ASN A 391     3846   3155   3818   -535    144   -557       C  
ATOM   2974  O   ASN A 391       0.557  26.373  -3.494  1.00 31.84           O  
ANISOU 2974  O   ASN A 391     4238   3671   4189   -516    187   -534       O  
ATOM   2975  CB  ASN A 391       3.492  25.478  -4.266  1.00 34.52           C  
ANISOU 2975  CB  ASN A 391     4642   3885   4590   -643    172   -454       C  
ATOM   2976  CG  ASN A 391       3.949  24.417  -5.247  1.00 35.29           C  
ANISOU 2976  CG  ASN A 391     4754   3949   4705   -713    203   -366       C  
ATOM   2977  OD1 ASN A 391       3.271  23.410  -5.439  1.00 41.34           O  
ANISOU 2977  OD1 ASN A 391     5506   4761   5441   -731    246   -311       O  
ATOM   2978  ND2 ASN A 391       5.097  24.639  -5.876  1.00 29.58           N  
ANISOU 2978  ND2 ASN A 391     4058   3149   4033   -752    180   -352       N  
ATOM   2979  N   CYS A 392       1.868  28.199  -3.303  1.00 29.06           N  
ANISOU 2979  N   CYS A 392     3930   3196   3914   -486     90   -644       N  
ATOM   2980  CA  CYS A 392       0.955  28.858  -2.379  1.00 29.84           C  
ANISOU 2980  CA  CYS A 392     4003   3363   3970   -399     77   -725       C  
ATOM   2981  C   CYS A 392      -0.240  29.444  -3.131  1.00 31.32           C  
ANISOU 2981  C   CYS A 392     4183   3525   4192   -374     73   -729       C  
ATOM   2982  O   CYS A 392      -1.355  29.505  -2.595  1.00 32.42           O  
ANISOU 2982  O   CYS A 392     4286   3751   4279   -313     91   -758       O  
ATOM   2983  CB  CYS A 392       1.682  29.952  -1.601  1.00 30.50           C  
ANISOU 2983  CB  CYS A 392     4104   3412   4072   -351     10   -827       C  
ATOM   2984  SG  CYS A 392       2.695  29.373  -0.184  1.00 39.97           S  
ANISOU 2984  SG  CYS A 392     5295   4699   5192   -335     11   -857       S  
ATOM   2985  N   GLU A 393      -0.015  29.933  -4.360  1.00 38.32           N  
ANISOU 2985  N   GLU A 393     5100   4296   5164   -415     47   -701       N  
ATOM   2986  CA  GLU A 393      -1.125  30.266  -5.245  1.00 33.99           C  
ANISOU 2986  CA  GLU A 393     4545   3726   4645   -402     49   -684       C  
ATOM   2987  C   GLU A 393      -1.974  29.039  -5.533  1.00 29.24           C  
ANISOU 2987  C   GLU A 393     3909   3207   3994   -430    113   -610       C  
ATOM   2988  O   GLU A 393      -3.199  29.136  -5.556  1.00 29.54           O  
ANISOU 2988  O   GLU A 393     3914   3298   4012   -389    127   -620       O  
ATOM   2989  CB  GLU A 393      -0.600  30.864  -6.548  1.00 37.79           C  
ANISOU 2989  CB  GLU A 393     5066   4075   5218   -447     16   -651       C  
ATOM   2990  CG  GLU A 393      -0.136  32.311  -6.436  1.00 45.50           C  
ANISOU 2990  CG  GLU A 393     6070   4953   6264   -413    -54   -723       C  
ATOM   2991  CD  GLU A 393       0.531  32.827  -7.700  1.00 57.93           C  
ANISOU 2991  CD  GLU A 393     7682   6398   7930   -467    -81   -672       C  
ATOM   2992  OE1 GLU A 393       1.306  33.805  -7.609  1.00 59.98           O  
ANISOU 2992  OE1 GLU A 393     7966   6567   8257   -466   -136   -711       O  
ATOM   2993  OE2 GLU A 393       0.280  32.261  -8.780  1.00 63.08           O  
ANISOU 2993  OE2 GLU A 393     8337   7043   8588   -510    -49   -591       O  
ATOM   2994  N   LEU A 394      -1.344  27.887  -5.797  1.00 28.60           N  
ANISOU 2994  N   LEU A 394     3834   3134   3899   -499    149   -537       N  
ATOM   2995  CA  LEU A 394      -2.103  26.656  -6.011  1.00 35.68           C  
ANISOU 2995  CA  LEU A 394     4698   4102   4756   -530    204   -468       C  
ATOM   2996  C   LEU A 394      -2.871  26.256  -4.754  1.00 40.55           C  
ANISOU 2996  C   LEU A 394     5265   4848   5294   -482    239   -487       C  
ATOM   2997  O   LEU A 394      -3.998  25.751  -4.835  1.00 38.77           O  
ANISOU 2997  O   LEU A 394     4998   4690   5045   -478    274   -457       O  
ATOM   2998  CB  LEU A 394      -1.162  25.536  -6.450  1.00 28.84           C  
ANISOU 2998  CB  LEU A 394     3853   3211   3893   -607    229   -395       C  
ATOM   2999  CG  LEU A 394      -1.826  24.221  -6.860  1.00 42.88           C  
ANISOU 2999  CG  LEU A 394     5606   5037   5651   -650    276   -320       C  
ATOM   3000  CD1 LEU A 394      -2.707  24.414  -8.088  1.00 41.97           C  
ANISOU 3000  CD1 LEU A 394     5488   4883   5578   -660    267   -301       C  
ATOM   3001  CD2 LEU A 394      -0.784  23.143  -7.111  1.00 34.71           C  
ANISOU 3001  CD2 LEU A 394     4596   3978   4616   -714    294   -260       C  
ATOM   3002  N   PHE A 395      -2.276  26.478  -3.579  1.00 36.61           N  
ANISOU 3002  N   PHE A 395     4767   4392   4752   -444    230   -537       N  
ATOM   3003  CA  PHE A 395      -2.968  26.172  -2.331  1.00 36.23           C  
ANISOU 3003  CA  PHE A 395     4670   4477   4617   -388    265   -556       C  
ATOM   3004  C   PHE A 395      -4.225  27.019  -2.183  1.00 36.53           C  
ANISOU 3004  C   PHE A 395     4674   4559   4647   -313    256   -613       C  
ATOM   3005  O   PHE A 395      -5.313  26.497  -1.915  1.00 33.51           O  
ANISOU 3005  O   PHE A 395     4239   4275   4220   -296    301   -583       O  
ATOM   3006  CB  PHE A 395      -2.035  26.385  -1.139  1.00 34.89           C  
ANISOU 3006  CB  PHE A 395     4513   4343   4401   -351    247   -609       C  
ATOM   3007  CG  PHE A 395      -2.751  26.462   0.183  1.00 36.76           C  
ANISOU 3007  CG  PHE A 395     4703   4717   4546   -267    269   -653       C  
ATOM   3008  CD1 PHE A 395      -3.260  25.320   0.778  1.00 35.10           C  
ANISOU 3008  CD1 PHE A 395     4449   4625   4264   -276    335   -584       C  
ATOM   3009  CD2 PHE A 395      -2.923  27.678   0.824  1.00 31.76           C  
ANISOU 3009  CD2 PHE A 395     4070   4097   3900   -178    223   -763       C  
ATOM   3010  CE1 PHE A 395      -3.920  25.389   1.991  1.00 40.19           C  
ANISOU 3010  CE1 PHE A 395     5046   5407   4816   -196    361   -616       C  
ATOM   3011  CE2 PHE A 395      -3.583  27.753   2.036  1.00 42.10           C  
ANISOU 3011  CE2 PHE A 395     5336   5545   5117    -91    245   -807       C  
ATOM   3012  CZ  PHE A 395      -4.082  26.607   2.619  1.00 41.89           C  
ANISOU 3012  CZ  PHE A 395     5262   5645   5010   -100    316   -730       C  
ATOM   3013  N   GLU A 396      -4.095  28.336  -2.363  1.00 30.77           N  
ANISOU 3013  N   GLU A 396     3972   3754   3964   -266    196   -693       N  
ATOM   3014  CA  GLU A 396      -5.246  29.224  -2.252  1.00 46.45           C  
ANISOU 3014  CA  GLU A 396     5931   5773   5947   -186    180   -755       C  
ATOM   3015  C   GLU A 396      -6.278  28.978  -3.346  1.00 42.99           C  
ANISOU 3015  C   GLU A 396     5470   5322   5543   -214    199   -699       C  
ATOM   3016  O   GLU A 396      -7.420  29.432  -3.216  1.00 41.01           O  
ANISOU 3016  O   GLU A 396     5180   5127   5276   -150    202   -734       O  
ATOM   3017  CB  GLU A 396      -4.785  30.682  -2.283  1.00 59.92           C  
ANISOU 3017  CB  GLU A 396     7679   7379   7709   -136    103   -851       C  
ATOM   3018  CG  GLU A 396      -3.834  31.048  -1.154  1.00 71.11           C  
ANISOU 3018  CG  GLU A 396     9113   8810   9095    -99     72   -924       C  
ATOM   3019  CD  GLU A 396      -3.252  32.440  -1.307  1.00 77.73           C  
ANISOU 3019  CD  GLU A 396     9997   9525  10011    -67    -11  -1012       C  
ATOM   3020  OE1 GLU A 396      -3.377  33.021  -2.405  1.00 76.63           O  
ANISOU 3020  OE1 GLU A 396     9884   9276   9956    -91    -40   -995       O  
ATOM   3021  OE2 GLU A 396      -2.671  32.952  -0.327  1.00 81.24           O  
ANISOU 3021  OE2 GLU A 396    10451   9982  10433    -17    -51  -1097       O  
ATOM   3022  N   GLN A 397      -5.904  28.272  -4.416  1.00 45.37           N  
ANISOU 3022  N   GLN A 397     5793   5555   5889   -302    212   -619       N  
ATOM   3023  CA  GLN A 397      -6.859  27.941  -5.467  1.00 38.56           C  
ANISOU 3023  CA  GLN A 397     4909   4687   5055   -330    227   -567       C  
ATOM   3024  C   GLN A 397      -7.682  26.705  -5.127  1.00 43.89           C  
ANISOU 3024  C   GLN A 397     5523   5476   5678   -355    290   -505       C  
ATOM   3025  O   GLN A 397      -8.834  26.594  -5.564  1.00 36.71           O  
ANISOU 3025  O   GLN A 397     4569   4604   4773   -346    303   -487       O  
ATOM   3026  CB  GLN A 397      -6.129  27.717  -6.794  1.00 39.75           C  
ANISOU 3026  CB  GLN A 397     5109   4721   5272   -406    210   -511       C  
ATOM   3027  CG  GLN A 397      -5.655  28.985  -7.484  1.00 44.00           C  
ANISOU 3027  CG  GLN A 397     5698   5140   5879   -387    150   -551       C  
ATOM   3028  CD  GLN A 397      -5.154  28.725  -8.892  1.00 53.90           C  
ANISOU 3028  CD  GLN A 397     6990   6301   7188   -456    142   -485       C  
ATOM   3029  OE1 GLN A 397      -4.563  27.682  -9.170  1.00 52.25           O  
ANISOU 3029  OE1 GLN A 397     6790   6093   6970   -522    170   -425       O  
ATOM   3030  NE2 GLN A 397      -5.390  29.675  -9.788  1.00 61.84           N  
ANISOU 3030  NE2 GLN A 397     8020   7229   8250   -435    102   -496       N  
ATOM   3031  N   LEU A 398      -7.121  25.776  -4.349  1.00 40.46           N  
ANISOU 3031  N   LEU A 398     5080   5096   5195   -385    327   -468       N  
ATOM   3032  CA  LEU A 398      -7.720  24.463  -4.165  1.00 38.40           C  
ANISOU 3032  CA  LEU A 398     4769   4920   4901   -429    385   -389       C  
ATOM   3033  C   LEU A 398      -8.199  24.173  -2.750  1.00 43.26           C  
ANISOU 3033  C   LEU A 398     5328   5677   5432   -380    429   -394       C  
ATOM   3034  O   LEU A 398      -9.092  23.336  -2.583  1.00 49.70           O  
ANISOU 3034  O   LEU A 398     6084   6577   6225   -400    477   -334       O  
ATOM   3035  CB  LEU A 398      -6.721  23.368  -4.567  1.00 29.63           C  
ANISOU 3035  CB  LEU A 398     3695   3754   3808   -517    399   -318       C  
ATOM   3036  CG  LEU A 398      -6.176  23.389  -5.994  1.00 37.08           C  
ANISOU 3036  CG  LEU A 398     4691   4573   4825   -574    366   -296       C  
ATOM   3037  CD1 LEU A 398      -5.082  22.345  -6.155  1.00 42.65           C  
ANISOU 3037  CD1 LEU A 398     5431   5240   5535   -643    380   -238       C  
ATOM   3038  CD2 LEU A 398      -7.291  23.163  -7.005  1.00 45.25           C  
ANISOU 3038  CD2 LEU A 398     5696   5603   5895   -594    368   -267       C  
ATOM   3039  N   GLY A 399      -7.640  24.826  -1.736  1.00 46.07           N  
ANISOU 3039  N   GLY A 399     5700   6064   5741   -315    414   -461       N  
ATOM   3040  CA  GLY A 399      -7.841  24.407  -0.365  1.00 44.16           C  
ANISOU 3040  CA  GLY A 399     5412   5960   5408   -272    458   -455       C  
ATOM   3041  C   GLY A 399      -6.952  23.225  -0.026  1.00 38.78           C  
ANISOU 3041  C   GLY A 399     4747   5285   4703   -337    489   -380       C  
ATOM   3042  O   GLY A 399      -6.365  22.577  -0.892  1.00 38.32           O  
ANISOU 3042  O   GLY A 399     4725   5136   4700   -419    485   -324       O  
ATOM   3043  N   GLU A 400      -6.862  22.927   1.274  1.00 33.99           N  
ANISOU 3043  N   GLU A 400     4113   4795   4008   -292    522   -378       N  
ATOM   3044  CA  GLU A 400      -5.865  21.963   1.734  1.00 42.05           C  
ANISOU 3044  CA  GLU A 400     5156   5820   5000   -338    543   -318       C  
ATOM   3045  C   GLU A 400      -6.120  20.568   1.173  1.00 33.15           C  
ANISOU 3045  C   GLU A 400     4011   4680   3904   -432    588   -199       C  
ATOM   3046  O   GLU A 400      -5.181  19.881   0.755  1.00 38.97           O  
ANISOU 3046  O   GLU A 400     4793   5340   4675   -497    581   -154       O  
ATOM   3047  CB  GLU A 400      -5.823  21.914   3.260  1.00 43.04           C  
ANISOU 3047  CB  GLU A 400     5251   6086   5016   -263    572   -335       C  
ATOM   3048  CG  GLU A 400      -4.747  20.968   3.786  1.00 42.22           C  
ANISOU 3048  CG  GLU A 400     5173   5989   4879   -301    589   -276       C  
ATOM   3049  CD  GLU A 400      -4.909  20.628   5.252  1.00 57.73           C  
ANISOU 3049  CD  GLU A 400     7095   8113   6727   -236    633   -258       C  
ATOM   3050  OE1 GLU A 400      -5.967  20.081   5.627  1.00 66.91           O  
ANISOU 3050  OE1 GLU A 400     8190   9383   7847   -229    693   -193       O  
ATOM   3051  OE2 GLU A 400      -3.969  20.896   6.030  1.00 65.34           O  
ANISOU 3051  OE2 GLU A 400     8089   9098   7639   -191    608   -308       O  
ATOM   3052  N   TYR A 401      -7.381  20.128   1.157  1.00 45.31           N  
ANISOU 3052  N   TYR A 401     5483   6295   5437   -439    632   -148       N  
ATOM   3053  CA  TYR A 401      -7.680  18.767   0.720  1.00 39.89           C  
ANISOU 3053  CA  TYR A 401     4773   5598   4783   -529    671    -35       C  
ATOM   3054  C   TYR A 401      -7.354  18.576  -0.756  1.00 37.18           C  
ANISOU 3054  C   TYR A 401     4478   5110   4538   -604    633    -24       C  
ATOM   3055  O   TYR A 401      -6.664  17.622  -1.132  1.00 35.68           O  
ANISOU 3055  O   TYR A 401     4320   4858   4378   -674    636     36       O  
ATOM   3056  CB  TYR A 401      -9.146  18.433   0.999  1.00 34.29           C  
ANISOU 3056  CB  TYR A 401     3973   5001   4055   -521    721     13       C  
ATOM   3057  CG  TYR A 401      -9.595  17.120   0.396  1.00 40.46           C  
ANISOU 3057  CG  TYR A 401     4726   5756   4893   -620    751    122       C  
ATOM   3058  CD1 TYR A 401      -9.012  15.921   0.782  1.00 37.31           C  
ANISOU 3058  CD1 TYR A 401     4337   5356   4485   -676    781    211       C  
ATOM   3059  CD2 TYR A 401     -10.602  17.081  -0.560  1.00 43.71           C  
ANISOU 3059  CD2 TYR A 401     5101   6139   5369   -655    744    132       C  
ATOM   3060  CE1 TYR A 401      -9.419  14.718   0.233  1.00 44.52           C  
ANISOU 3060  CE1 TYR A 401     5225   6233   5458   -766    801    306       C  
ATOM   3061  CE2 TYR A 401     -11.018  15.884  -1.114  1.00 44.65           C  
ANISOU 3061  CE2 TYR A 401     5192   6228   5545   -746    762    224       C  
ATOM   3062  CZ  TYR A 401     -10.422  14.705  -0.715  1.00 52.34           C  
ANISOU 3062  CZ  TYR A 401     6178   7194   6515   -802    790    309       C  
ATOM   3063  OH  TYR A 401     -10.832  13.511  -1.265  1.00 50.14           O  
ANISOU 3063  OH  TYR A 401     5873   6875   6302   -893    802    396       O  
ATOM   3064  N   LYS A 402      -7.841  19.478  -1.612  1.00 32.22           N  
ANISOU 3064  N   LYS A 402     3856   4431   3957   -586    596    -82       N  
ATOM   3065  CA  LYS A 402      -7.549  19.365  -3.037  1.00 42.48           C  
ANISOU 3065  CA  LYS A 402     5199   5602   5339   -648    560    -74       C  
ATOM   3066  C   LYS A 402      -6.082  19.648  -3.335  1.00 41.34           C  
ANISOU 3066  C   LYS A 402     5135   5359   5214   -660    522   -103       C  
ATOM   3067  O   LYS A 402      -5.521  19.073  -4.275  1.00 31.84           O  
ANISOU 3067  O   LYS A 402     3971   4067   4062   -724    508    -67       O  
ATOM   3068  CB  LYS A 402      -8.453  20.304  -3.834  1.00 40.79           C  
ANISOU 3068  CB  LYS A 402     4970   5365   5164   -617    530   -125       C  
ATOM   3069  CG  LYS A 402      -9.935  19.982  -3.710  1.00 45.16           C  
ANISOU 3069  CG  LYS A 402     5437   6012   5709   -613    565    -93       C  
ATOM   3070  CD  LYS A 402     -10.694  20.371  -4.968  1.00 51.62           C  
ANISOU 3070  CD  LYS A 402     6249   6773   6590   -624    532   -110       C  
ATOM   3071  CE  LYS A 402     -10.574  21.861  -5.246  1.00 53.12           C  
ANISOU 3071  CE  LYS A 402     6475   6918   6790   -552    484   -202       C  
ATOM   3072  NZ  LYS A 402     -11.090  22.676  -4.112  1.00 46.94           N  
ANISOU 3072  NZ  LYS A 402     5651   6237   5946   -459    496   -261       N  
ATOM   3073  N   PHE A 403      -5.445  20.526  -2.552  1.00 30.47           N  
ANISOU 3073  N   PHE A 403     3780   3999   3799   -599    502   -171       N  
ATOM   3074  CA  PHE A 403      -4.007  20.739  -2.697  1.00 28.80           C  
ANISOU 3074  CA  PHE A 403     3634   3704   3604   -613    468   -193       C  
ATOM   3075  C   PHE A 403      -3.232  19.473  -2.356  1.00 31.93           C  
ANISOU 3075  C   PHE A 403     4042   4108   3980   -664    497   -121       C  
ATOM   3076  O   PHE A 403      -2.196  19.186  -2.967  1.00 33.91           O  
ANISOU 3076  O   PHE A 403     4343   4274   4268   -708    477   -106       O  
ATOM   3077  CB  PHE A 403      -3.559  21.902  -1.810  1.00 29.22           C  
ANISOU 3077  CB  PHE A 403     3700   3781   3622   -536    437   -285       C  
ATOM   3078  CG  PHE A 403      -2.110  22.267  -1.962  1.00 31.60           C  
ANISOU 3078  CG  PHE A 403     4062   3995   3950   -550    396   -315       C  
ATOM   3079  CD1 PHE A 403      -1.602  22.658  -3.189  1.00 33.37           C  
ANISOU 3079  CD1 PHE A 403     4329   4099   4251   -591    360   -318       C  
ATOM   3080  CD2 PHE A 403      -1.260  22.239  -0.868  1.00 37.80           C  
ANISOU 3080  CD2 PHE A 403     4856   4826   4682   -521    393   -340       C  
ATOM   3081  CE1 PHE A 403      -0.270  23.004  -3.326  1.00 29.09           C  
ANISOU 3081  CE1 PHE A 403     3834   3483   3738   -607    325   -341       C  
ATOM   3082  CE2 PHE A 403       0.073  22.584  -0.997  1.00 35.07           C  
ANISOU 3082  CE2 PHE A 403     4558   4403   4366   -536    352   -369       C  
ATOM   3083  CZ  PHE A 403       0.569  22.967  -2.228  1.00 33.02           C  
ANISOU 3083  CZ  PHE A 403     4336   4023   4188   -582    320   -367       C  
ATOM   3084  N   GLN A 404      -3.720  18.702  -1.379  1.00 36.64           N  
ANISOU 3084  N   GLN A 404     4593   4810   4518   -656    546    -72       N  
ATOM   3085  CA  GLN A 404      -3.096  17.419  -1.069  1.00 33.92           C  
ANISOU 3085  CA  GLN A 404     4258   4472   4159   -705    574      8       C  
ATOM   3086  C   GLN A 404      -3.240  16.446  -2.232  1.00 31.97           C  
ANISOU 3086  C   GLN A 404     4021   4146   3981   -787    578     75       C  
ATOM   3087  O   GLN A 404      -2.297  15.717  -2.562  1.00 31.85           O  
ANISOU 3087  O   GLN A 404     4047   4068   3987   -832    571    111       O  
ATOM   3088  CB  GLN A 404      -3.708  16.826   0.200  1.00 29.74           C  
ANISOU 3088  CB  GLN A 404     3671   4075   3552   -678    628     57       C  
ATOM   3089  CG  GLN A 404      -3.146  17.384   1.500  1.00 30.81           C  
ANISOU 3089  CG  GLN A 404     3809   4293   3603   -601    627      7       C  
ATOM   3090  CD  GLN A 404      -3.984  16.992   2.700  1.00 38.98           C  
ANISOU 3090  CD  GLN A 404     4779   5478   4554   -559    683     51       C  
ATOM   3091  OE1 GLN A 404      -5.153  16.636   2.561  1.00 34.98           O  
ANISOU 3091  OE1 GLN A 404     4215   5019   4056   -576    720     99       O  
ATOM   3092  NE2 GLN A 404      -3.389  17.054   3.887  1.00 39.63           N  
ANISOU 3092  NE2 GLN A 404     4864   5642   4552   -503    691     35       N  
ATOM   3093  N   ASN A 405      -4.419  16.416  -2.860  1.00 31.24           N  
ANISOU 3093  N   ASN A 405     3890   4056   3923   -805    585     88       N  
ATOM   3094  CA  ASN A 405      -4.623  15.546  -4.015  1.00 32.29           C  
ANISOU 3094  CA  ASN A 405     4032   4114   4123   -878    579    139       C  
ATOM   3095  C   ASN A 405      -3.739  15.963  -5.183  1.00 32.70           C  
ANISOU 3095  C   ASN A 405     4149   4050   4225   -895    531    101       C  
ATOM   3096  O   ASN A 405      -3.214  15.109  -5.909  1.00 28.15           O  
ANISOU 3096  O   ASN A 405     3604   3405   3686   -949    524    140       O  
ATOM   3097  CB  ASN A 405      -6.096  15.558  -4.426  1.00 34.15           C  
ANISOU 3097  CB  ASN A 405     4207   4383   4384   -886    589    150       C  
ATOM   3098  CG  ASN A 405      -7.018  15.100  -3.311  1.00 33.78           C  
ANISOU 3098  CG  ASN A 405     4086   4459   4291   -873    642    199       C  
ATOM   3099  OD1 ASN A 405      -6.592  14.417  -2.380  1.00 38.27           O  
ANISOU 3099  OD1 ASN A 405     4650   5074   4817   -878    674    249       O  
ATOM   3100  ND2 ASN A 405      -8.290  15.476  -3.401  1.00 30.89           N  
ANISOU 3100  ND2 ASN A 405     3658   4149   3930   -855    652    188       N  
ATOM   3101  N   ALA A 406      -3.564  17.271  -5.384  1.00 35.69           N  
ANISOU 3101  N   ALA A 406     4547   4406   4606   -848    499     27       N  
ATOM   3102  CA  ALA A 406      -2.691  17.740  -6.454  1.00 26.70           C  
ANISOU 3102  CA  ALA A 406     3467   3164   3514   -863    458     -1       C  
ATOM   3103  C   ALA A 406      -1.248  17.319  -6.208  1.00 37.17           C  
ANISOU 3103  C   ALA A 406     4838   4456   4830   -881    455     13       C  
ATOM   3104  O   ALA A 406      -0.537  16.934  -7.143  1.00 37.92           O  
ANISOU 3104  O   ALA A 406     4972   4475   4962   -919    439     32       O  
ATOM   3105  CB  ALA A 406      -2.795  19.259  -6.591  1.00 32.41           C  
ANISOU 3105  CB  ALA A 406     4200   3869   4246   -809    424    -77       C  
ATOM   3106  N   LEU A 407      -0.799  17.382  -4.953  1.00 26.66           N  
ANISOU 3106  N   LEU A 407     3500   3186   3445   -848    468      2       N  
ATOM   3107  CA  LEU A 407       0.544  16.914  -4.627  1.00 26.41           C  
ANISOU 3107  CA  LEU A 407     3503   3131   3400   -862    465     18       C  
ATOM   3108  C   LEU A 407       0.619  15.393  -4.675  1.00 27.35           C  
ANISOU 3108  C   LEU A 407     3621   3250   3520   -912    495    100       C  
ATOM   3109  O   LEU A 407       1.649  14.828  -5.062  1.00 30.27           O  
ANISOU 3109  O   LEU A 407     4029   3566   3907   -941    485    122       O  
ATOM   3110  CB  LEU A 407       0.957  17.433  -3.251  1.00 32.68           C  
ANISOU 3110  CB  LEU A 407     4288   3997   4132   -807    467    -22       C  
ATOM   3111  CG  LEU A 407       1.111  18.952  -3.158  1.00 34.97           C  
ANISOU 3111  CG  LEU A 407     4587   4270   4428   -756    426   -112       C  
ATOM   3112  CD1 LEU A 407       1.413  19.378  -1.733  1.00 39.08           C  
ANISOU 3112  CD1 LEU A 407     5094   4871   4881   -695    424   -158       C  
ATOM   3113  CD2 LEU A 407       2.193  19.438  -4.108  1.00 33.72           C  
ANISOU 3113  CD2 LEU A 407     4477   4007   4329   -782    386   -133       C  
ATOM   3114  N   LEU A 408      -0.463  14.721  -4.275  1.00 35.14           N  
ANISOU 3114  N   LEU A 408     4561   4297   4491   -923    529    147       N  
ATOM   3115  CA  LEU A 408      -0.551  13.271  -4.403  1.00 31.24           C  
ANISOU 3115  CA  LEU A 408     4063   3791   4015   -977    552    228       C  
ATOM   3116  C   LEU A 408      -0.281  12.836  -5.837  1.00 26.49           C  
ANISOU 3116  C   LEU A 408     3498   3087   3479  -1024    525    235       C  
ATOM   3117  O   LEU A 408       0.576  11.982  -6.093  1.00 31.01           O  
ANISOU 3117  O   LEU A 408     4104   3611   4065  -1053    521    268       O  
ATOM   3118  CB  LEU A 408      -1.934  12.803  -3.950  1.00 46.33           C  
ANISOU 3118  CB  LEU A 408     5911   5775   5917   -986    589    274       C  
ATOM   3119  CG  LEU A 408      -2.123  11.408  -3.360  1.00 60.97           C  
ANISOU 3119  CG  LEU A 408     7741   7659   7765  -1025    626    367       C  
ATOM   3120  CD1 LEU A 408      -1.162  11.146  -2.216  1.00 53.55           C  
ANISOU 3120  CD1 LEU A 408     6819   6765   6764   -996    643    389       C  
ATOM   3121  CD2 LEU A 408      -3.554  11.258  -2.894  1.00 52.36           C  
ANISOU 3121  CD2 LEU A 408     6576   6651   6665  -1028    662    405       C  
ATOM   3122  N   VAL A 409      -1.010  13.422  -6.789  1.00 33.01           N  
ANISOU 3122  N   VAL A 409     4316   3884   4342  -1027    505    204       N  
ATOM   3123  CA  VAL A 409      -0.752  13.150  -8.200  1.00 38.87           C  
ANISOU 3123  CA  VAL A 409     5093   4538   5136  -1061    476    202       C  
ATOM   3124  C   VAL A 409       0.691  13.493  -8.548  1.00 34.85           C  
ANISOU 3124  C   VAL A 409     4639   3975   4627  -1051    454    177       C  
ATOM   3125  O   VAL A 409       1.413  12.680  -9.134  1.00 29.18           O  
ANISOU 3125  O   VAL A 409     3955   3205   3929  -1079    447    203       O  
ATOM   3126  CB  VAL A 409      -1.746  13.924  -9.086  1.00 37.88           C  
ANISOU 3126  CB  VAL A 409     4951   4401   5041  -1052    456    166       C  
ATOM   3127  CG1 VAL A 409      -1.323  13.851 -10.547  1.00 42.77           C  
ANISOU 3127  CG1 VAL A 409     5613   4937   5701  -1073    423    157       C  
ATOM   3128  CG2 VAL A 409      -3.154  13.380  -8.907  1.00 39.07           C  
ANISOU 3128  CG2 VAL A 409     5042   4600   5203  -1072    475    198       C  
ATOM   3129  N   ARG A 410       1.142  14.687  -8.154  1.00 27.10           N  
ANISOU 3129  N   ARG A 410     3665   3006   3625  -1011    443    127       N  
ATOM   3130  CA  ARG A 410       2.460  15.165  -8.568  1.00 24.73           C  
ANISOU 3130  CA  ARG A 410     3409   2652   3335  -1005    420    103       C  
ATOM   3131  C   ARG A 410       3.570  14.207  -8.151  1.00 33.87           C  
ANISOU 3131  C   ARG A 410     4588   3805   4475  -1021    430    138       C  
ATOM   3132  O   ARG A 410       4.482  13.925  -8.938  1.00 26.86           O  
ANISOU 3132  O   ARG A 410     3734   2862   3609  -1037    416    146       O  
ATOM   3133  CB  ARG A 410       2.721  16.557  -7.992  1.00 27.94           C  
ANISOU 3133  CB  ARG A 410     3813   3075   3727   -961    403     44       C  
ATOM   3134  CG  ARG A 410       4.100  17.109  -8.331  1.00 27.10           C  
ANISOU 3134  CG  ARG A 410     3743   2916   3638   -961    378     23       C  
ATOM   3135  CD  ARG A 410       4.335  18.469  -7.692  1.00 24.83           C  
ANISOU 3135  CD  ARG A 410     3452   2637   3347   -920    355    -39       C  
ATOM   3136  NE  ARG A 410       3.257  19.404  -7.995  1.00 28.49           N  
ANISOU 3136  NE  ARG A 410     3900   3097   3828   -897    342    -73       N  
ATOM   3137  CZ  ARG A 410       3.173  20.634  -7.500  1.00 33.28           C  
ANISOU 3137  CZ  ARG A 410     4501   3707   4437   -855    317   -134       C  
ATOM   3138  NH1 ARG A 410       4.106  21.083  -6.672  1.00 30.23           N  
ANISOU 3138  NH1 ARG A 410     4122   3327   4038   -836    300   -170       N  
ATOM   3139  NH2 ARG A 410       2.155  21.415  -7.831  1.00 37.08           N  
ANISOU 3139  NH2 ARG A 410     4969   4184   4937   -830    305   -162       N  
ATOM   3140  N   TYR A 411       3.509  13.688  -6.924  1.00 31.69           N  
ANISOU 3140  N   TYR A 411     4292   3592   4158  -1011    454    162       N  
ATOM   3141  CA  TYR A 411       4.607  12.883  -6.404  1.00 27.96           C  
ANISOU 3141  CA  TYR A 411     3840   3120   3665  -1016    461    193       C  
ATOM   3142  C   TYR A 411       4.509  11.415  -6.793  1.00 24.92           C  
ANISOU 3142  C   TYR A 411     3464   2705   3300  -1056    474    256       C  
ATOM   3143  O   TYR A 411       5.546  10.752  -6.926  1.00 26.18           O  
ANISOU 3143  O   TYR A 411     3653   2833   3462  -1064    468    276       O  
ATOM   3144  CB  TYR A 411       4.689  13.027  -4.880  1.00 28.17           C  
ANISOU 3144  CB  TYR A 411     3843   3229   3630   -979    478    190       C  
ATOM   3145  CG  TYR A 411       5.585  14.177  -4.476  1.00 34.74           C  
ANISOU 3145  CG  TYR A 411     4687   4068   4446   -942    452    126       C  
ATOM   3146  CD1 TYR A 411       5.134  15.489  -4.548  1.00 27.30           C  
ANISOU 3146  CD1 TYR A 411     3733   3127   3512   -915    433     63       C  
ATOM   3147  CD2 TYR A 411       6.891  13.954  -4.057  1.00 27.96           C  
ANISOU 3147  CD2 TYR A 411     3848   3206   3569   -935    442    126       C  
ATOM   3148  CE1 TYR A 411       5.951  16.548  -4.198  1.00 31.20           C  
ANISOU 3148  CE1 TYR A 411     4237   3614   4002   -885    402      2       C  
ATOM   3149  CE2 TYR A 411       7.716  15.007  -3.705  1.00 34.59           C  
ANISOU 3149  CE2 TYR A 411     4694   4047   4403   -906    412     65       C  
ATOM   3150  CZ  TYR A 411       7.240  16.301  -3.777  1.00 29.42           C  
ANISOU 3150  CZ  TYR A 411     4028   3387   3762   -883    391      3       C  
ATOM   3151  OH  TYR A 411       8.052  17.353  -3.428  1.00 37.56           O  
ANISOU 3151  OH  TYR A 411     5065   4409   4799   -858    355    -60       O  
ATOM   3152  N   THR A 412       3.299  10.883  -6.981  1.00 25.23           N  
ANISOU 3152  N   THR A 412     3476   2752   3359  -1080    487    287       N  
ATOM   3153  CA  THR A 412       3.185   9.542  -7.543  1.00 30.62           C  
ANISOU 3153  CA  THR A 412     4169   3387   4077  -1123    488    338       C  
ATOM   3154  C   THR A 412       3.713   9.504  -8.972  1.00 30.49           C  
ANISOU 3154  C   THR A 412     4193   3292   4101  -1135    456    314       C  
ATOM   3155  O   THR A 412       4.211   8.467  -9.424  1.00 32.85           O  
ANISOU 3155  O   THR A 412     4517   3542   4420  -1155    448    341       O  
ATOM   3156  CB  THR A 412       1.733   9.059  -7.494  1.00 28.64           C  
ANISOU 3156  CB  THR A 412     3875   3159   3849  -1151    503    373       C  
ATOM   3157  OG1 THR A 412       1.204   9.255  -6.176  1.00 34.77           O  
ANISOU 3157  OG1 THR A 412     4609   4024   4580  -1131    537    394       O  
ATOM   3158  CG2 THR A 412       1.652   7.579  -7.841  1.00 25.85           C  
ANISOU 3158  CG2 THR A 412     3531   2754   3538  -1197    501    430       C  
ATOM   3159  N   LYS A 413       3.626  10.626  -9.690  1.00 32.57           N  
ANISOU 3159  N   LYS A 413     4460   3542   4372  -1119    438    264       N  
ATOM   3160  CA  LYS A 413       4.222  10.708 -11.021  1.00 29.11           C  
ANISOU 3160  CA  LYS A 413     4058   3041   3961  -1123    412    244       C  
ATOM   3161  C   LYS A 413       5.740  10.624 -10.947  1.00 29.00           C  
ANISOU 3161  C   LYS A 413     4076   3010   3931  -1110    409    243       C  
ATOM   3162  O   LYS A 413       6.370   9.890 -11.717  1.00 34.83           O  
ANISOU 3162  O   LYS A 413     4844   3705   4684  -1118    398    254       O  
ATOM   3163  CB  LYS A 413       3.802  12.007 -11.702  1.00 31.90           C  
ANISOU 3163  CB  LYS A 413     4406   3390   4324  -1106    397    200       C  
ATOM   3164  CG  LYS A 413       2.314  12.162 -11.878  1.00 41.53           C  
ANISOU 3164  CG  LYS A 413     5591   4629   5559  -1113    397    196       C  
ATOM   3165  CD  LYS A 413       1.981  12.557 -13.279  1.00 59.03           C  
ANISOU 3165  CD  LYS A 413     7821   6805   7802  -1113    370    173       C  
ATOM   3166  CE  LYS A 413       1.642  14.027 -13.343  1.00 61.98           C  
ANISOU 3166  CE  LYS A 413     8184   7192   8172  -1082    362    136       C  
ATOM   3167  NZ  LYS A 413       0.232  14.267 -12.943  1.00 71.29           N  
ANISOU 3167  NZ  LYS A 413     9318   8415   9355  -1078    368    128       N  
ATOM   3168  N   LYS A 414       6.343  11.382 -10.028  1.00 32.07           N  
ANISOU 3168  N   LYS A 414     4459   3435   4291  -1086    415    225       N  
ATOM   3169  CA  LYS A 414       7.797  11.403  -9.915  1.00 23.67           C  
ANISOU 3169  CA  LYS A 414     3418   2360   3215  -1074    409    222       C  
ATOM   3170  C   LYS A 414       8.345  10.019  -9.598  1.00 27.19           C  
ANISOU 3170  C   LYS A 414     3878   2800   3652  -1082    418    265       C  
ATOM   3171  O   LYS A 414       9.303   9.557 -10.229  1.00 36.84           O  
ANISOU 3171  O   LYS A 414     5127   3988   4884  -1081    408    270       O  
ATOM   3172  CB  LYS A 414       8.229  12.397  -8.834  1.00 31.26           C  
ANISOU 3172  CB  LYS A 414     4364   3366   4148  -1047    408    191       C  
ATOM   3173  CG  LYS A 414       7.874  13.851  -9.097  1.00 30.88           C  
ANISOU 3173  CG  LYS A 414     4306   3313   4115  -1034    393    143       C  
ATOM   3174  CD  LYS A 414       8.194  14.698  -7.868  1.00 27.61           C  
ANISOU 3174  CD  LYS A 414     3874   2944   3671  -1004    387    106       C  
ATOM   3175  CE  LYS A 414       7.768  16.144  -8.047  1.00 30.01           C  
ANISOU 3175  CE  LYS A 414     4169   3237   3996   -987    366     55       C  
ATOM   3176  NZ  LYS A 414       8.764  16.913  -8.837  1.00 26.14           N  
ANISOU 3176  NZ  LYS A 414     3697   2691   3544   -994    342     38       N  
ATOM   3177  N   VAL A 415       7.751   9.343  -8.619  1.00 27.86           N  
ANISOU 3177  N   VAL A 415     3945   2920   3720  -1088    437    300       N  
ATOM   3178  CA  VAL A 415       8.338   8.123  -8.070  1.00 29.60           C  
ANISOU 3178  CA  VAL A 415     4179   3138   3929  -1090    445    346       C  
ATOM   3179  C   VAL A 415       7.250   7.080  -7.824  1.00 31.93           C  
ANISOU 3179  C   VAL A 415     4459   3431   4241  -1118    460    398       C  
ATOM   3180  O   VAL A 415       6.961   6.737  -6.667  1.00 30.22           O  
ANISOU 3180  O   VAL A 415     4222   3265   3996  -1115    483    437       O  
ATOM   3181  CB  VAL A 415       9.133   8.443  -6.793  1.00 32.57           C  
ANISOU 3181  CB  VAL A 415     4547   3572   4256  -1059    454    345       C  
ATOM   3182  CG1 VAL A 415      10.429   9.162  -7.161  1.00 24.17           C  
ANISOU 3182  CG1 VAL A 415     3499   2493   3191  -1040    433    303       C  
ATOM   3183  CG2 VAL A 415       8.312   9.318  -5.848  1.00 27.76           C  
ANISOU 3183  CG2 VAL A 415     3902   3030   3614  -1043    467    326       C  
ATOM   3184  N   PRO A 416       6.645   6.523  -8.879  1.00 35.55           N  
ANISOU 3184  N   PRO A 416     4926   3835   4747  -1147    446    402       N  
ATOM   3185  CA  PRO A 416       5.484   5.635  -8.690  1.00 25.16           C  
ANISOU 3185  CA  PRO A 416     3587   2514   3460  -1182    456    449       C  
ATOM   3186  C   PRO A 416       5.802   4.300  -8.032  1.00 29.27           C  
ANISOU 3186  C   PRO A 416     4118   3018   3986  -1195    465    514       C  
ATOM   3187  O   PRO A 416       4.863   3.599  -7.633  1.00 30.18           O  
ANISOU 3187  O   PRO A 416     4206   3136   4124  -1226    478    566       O  
ATOM   3188  CB  PRO A 416       4.963   5.431 -10.119  1.00 33.69           C  
ANISOU 3188  CB  PRO A 416     4679   3531   4591  -1205    427    423       C  
ATOM   3189  CG  PRO A 416       6.139   5.690 -10.991  1.00 33.35           C  
ANISOU 3189  CG  PRO A 416     4677   3452   4542  -1180    406    384       C  
ATOM   3190  CD  PRO A 416       6.957   6.737 -10.302  1.00 27.06           C  
ANISOU 3190  CD  PRO A 416     3877   2705   3699  -1147    419    363       C  
ATOM   3191  N   GLN A 417       7.073   3.912  -7.913  1.00 32.43           N  
ANISOU 3191  N   GLN A 417     4553   3400   4370  -1171    457    518       N  
ATOM   3192  CA  GLN A 417       7.394   2.661  -7.236  1.00 27.27           C  
ANISOU 3192  CA  GLN A 417     3911   2730   3721  -1177    464    584       C  
ATOM   3193  C   GLN A 417       7.262   2.764  -5.724  1.00 37.60           C  
ANISOU 3193  C   GLN A 417     5190   4119   4977  -1163    499    631       C  
ATOM   3194  O   GLN A 417       7.171   1.730  -5.052  1.00 40.08           O  
ANISOU 3194  O   GLN A 417     5502   4429   5297  -1175    511    703       O  
ATOM   3195  CB  GLN A 417       8.810   2.204  -7.590  1.00 35.35           C  
ANISOU 3195  CB  GLN A 417     4978   3712   4740  -1149    444    571       C  
ATOM   3196  CG  GLN A 417       8.999   1.839  -9.052  1.00 48.46           C  
ANISOU 3196  CG  GLN A 417     6671   5296   6447  -1155    410    534       C  
ATOM   3197  CD  GLN A 417       9.573   2.983  -9.858  1.00 50.22           C  
ANISOU 3197  CD  GLN A 417     6900   5532   6650  -1131    401    467       C  
ATOM   3198  OE1 GLN A 417      10.242   3.861  -9.317  1.00 57.31           O  
ANISOU 3198  OE1 GLN A 417     7788   6480   7505  -1106    413    449       O  
ATOM   3199  NE2 GLN A 417       9.317   2.978 -11.160  1.00 63.60           N  
ANISOU 3199  NE2 GLN A 417     8610   7181   8376  -1138    378    431       N  
ATOM   3200  N   VAL A 418       7.249   3.983  -5.179  1.00 34.36           N  
ANISOU 3200  N   VAL A 418     4756   3783   4517  -1135    512    592       N  
ATOM   3201  CA  VAL A 418       7.128   4.162  -3.738  1.00 30.30           C  
ANISOU 3201  CA  VAL A 418     4214   3359   3941  -1111    543    626       C  
ATOM   3202  C   VAL A 418       5.821   3.551  -3.250  1.00 35.19           C  
ANISOU 3202  C   VAL A 418     4793   4003   4574  -1144    572    695       C  
ATOM   3203  O   VAL A 418       4.781   3.640  -3.916  1.00 37.95           O  
ANISOU 3203  O   VAL A 418     5122   4330   4968  -1178    570    687       O  
ATOM   3204  CB  VAL A 418       7.220   5.657  -3.385  1.00 28.37           C  
ANISOU 3204  CB  VAL A 418     3951   3181   3649  -1074    543    556       C  
ATOM   3205  CG1 VAL A 418       6.994   5.880  -1.897  1.00 27.53           C  
ANISOU 3205  CG1 VAL A 418     3812   3177   3471  -1040    573    582       C  
ATOM   3206  CG2 VAL A 418       8.570   6.217  -3.812  1.00 28.08           C  
ANISOU 3206  CG2 VAL A 418     3946   3118   3606  -1048    514    498       C  
ATOM   3207  N   SER A 419       5.878   2.906  -2.084  1.00 35.21           N  
ANISOU 3207  N   SER A 419     4783   4055   4538  -1133    600    769       N  
ATOM   3208  CA  SER A 419       4.691   2.291  -1.506  1.00 35.67           C  
ANISOU 3208  CA  SER A 419     4797   4147   4607  -1165    634    850       C  
ATOM   3209  C   SER A 419       3.580   3.321  -1.349  1.00 30.81           C  
ANISOU 3209  C   SER A 419     4130   3605   3969  -1161    654    817       C  
ATOM   3210  O   SER A 419       3.831   4.488  -1.037  1.00 34.21           O  
ANISOU 3210  O   SER A 419     4557   4097   4346  -1114    653    749       O  
ATOM   3211  CB  SER A 419       5.024   1.663  -0.152  1.00 47.19           C  
ANISOU 3211  CB  SER A 419     6249   5672   6010  -1140    665    934       C  
ATOM   3212  OG  SER A 419       4.631   2.513   0.911  1.00 50.16           O  
ANISOU 3212  OG  SER A 419     6583   6172   6303  -1099    698    927       O  
ATOM   3213  N   THR A 420       2.344   2.880  -1.581  1.00 30.18           N  
ANISOU 3213  N   THR A 420     4011   3517   3939  -1209    669    862       N  
ATOM   3214  CA  THR A 420       1.205   3.796  -1.536  1.00 29.13           C  
ANISOU 3214  CA  THR A 420     3825   3452   3793  -1205    687    830       C  
ATOM   3215  C   THR A 420       1.042   4.481  -0.182  1.00 47.55           C  
ANISOU 3215  C   THR A 420     6119   5917   6029  -1149    727    837       C  
ATOM   3216  O   THR A 420       0.821   5.705  -0.163  1.00 34.33           O  
ANISOU 3216  O   THR A 420     4431   4294   4320  -1110    723    759       O  
ATOM   3217  CB  THR A 420      -0.067   3.048  -1.954  1.00 34.07           C  
ANISOU 3217  CB  THR A 420     4408   4047   4491  -1270    696    889       C  
ATOM   3218  OG1 THR A 420       0.029   2.680  -3.337  1.00 38.27           O  
ANISOU 3218  OG1 THR A 420     4975   4462   5105  -1310    649    852       O  
ATOM   3219  CG2 THR A 420      -1.297   3.918  -1.755  1.00 39.70           C  
ANISOU 3219  CG2 THR A 420     5055   4845   5184  -1261    721    867       C  
ATOM   3220  N   PRO A 421       1.134   3.791   0.966  1.00 42.69           N  
ANISOU 3220  N   PRO A 421     5487   5364   5367  -1138    763    924       N  
ATOM   3221  CA  PRO A 421       1.026   4.522   2.244  1.00 40.42           C  
ANISOU 3221  CA  PRO A 421     5167   5216   4977  -1072    797    919       C  
ATOM   3222  C   PRO A 421       2.092   5.590   2.420  1.00 35.34           C  
ANISOU 3222  C   PRO A 421     4560   4592   4274  -1007    767    817       C  
ATOM   3223  O   PRO A 421       1.813   6.646   3.001  1.00 49.50           O  
ANISOU 3223  O   PRO A 421     6327   6477   6005   -953    776    760       O  
ATOM   3224  CB  PRO A 421       1.153   3.409   3.295  1.00 48.69           C  
ANISOU 3224  CB  PRO A 421     6202   6309   5989  -1074    835   1040       C  
ATOM   3225  CG  PRO A 421       0.722   2.174   2.591  1.00 49.20           C  
ANISOU 3225  CG  PRO A 421     6267   6270   6155  -1155    832   1120       C  
ATOM   3226  CD  PRO A 421       1.212   2.334   1.186  1.00 43.73           C  
ANISOU 3226  CD  PRO A 421     5626   5451   5537  -1181    776   1036       C  
ATOM   3227  N   THR A 422       3.309   5.346   1.928  1.00 31.90           N  
ANISOU 3227  N   THR A 422     4183   4075   3864  -1010    730    792       N  
ATOM   3228  CA  THR A 422       4.363   6.352   2.025  1.00 35.04           C  
ANISOU 3228  CA  THR A 422     4612   4483   4220   -958    698    697       C  
ATOM   3229  C   THR A 422       4.034   7.579   1.182  1.00 38.40           C  
ANISOU 3229  C   THR A 422     5035   4881   4675   -955    671    598       C  
ATOM   3230  O   THR A 422       4.238   8.716   1.624  1.00 34.20           O  
ANISOU 3230  O   THR A 422     4497   4403   4095   -903    659    522       O  
ATOM   3231  CB  THR A 422       5.704   5.748   1.603  1.00 40.10           C  
ANISOU 3231  CB  THR A 422     5307   5042   4886   -966    667    700       C  
ATOM   3232  OG1 THR A 422       6.023   4.646   2.461  1.00 41.00           O  
ANISOU 3232  OG1 THR A 422     5425   5184   4969   -960    689    794       O  
ATOM   3233  CG2 THR A 422       6.818   6.786   1.693  1.00 31.21           C  
ANISOU 3233  CG2 THR A 422     4206   3927   3726   -918    632    606       C  
ATOM   3234  N   LEU A 423       3.516   7.372  -0.033  1.00 30.51           N  
ANISOU 3234  N   LEU A 423     4042   3796   3756  -1008    658    596       N  
ATOM   3235  CA  LEU A 423       3.156   8.503  -0.882  1.00 30.83           C  
ANISOU 3235  CA  LEU A 423     4080   3807   3825  -1005    633    511       C  
ATOM   3236  C   LEU A 423       1.988   9.291  -0.304  1.00 28.16           C  
ANISOU 3236  C   LEU A 423     3689   3560   3450   -976    657    491       C  
ATOM   3237  O   LEU A 423       1.933  10.516  -0.457  1.00 30.28           O  
ANISOU 3237  O   LEU A 423     3957   3840   3710   -941    636    408       O  
ATOM   3238  CB  LEU A 423       2.817   8.022  -2.293  1.00 30.08           C  
ANISOU 3238  CB  LEU A 423     4002   3611   3817  -1063    614    518       C  
ATOM   3239  CG  LEU A 423       3.989   7.683  -3.217  1.00 33.13           C  
ANISOU 3239  CG  LEU A 423     4445   3901   4243  -1078    579    500       C  
ATOM   3240  CD1 LEU A 423       3.506   6.849  -4.394  1.00 32.42           C  
ANISOU 3240  CD1 LEU A 423     4365   3725   4228  -1132    566    525       C  
ATOM   3241  CD2 LEU A 423       4.688   8.948  -3.699  1.00 26.57           C  
ANISOU 3241  CD2 LEU A 423     3637   3051   3407  -1048    548    412       C  
ATOM   3242  N   VAL A 424       1.047   8.609   0.353  1.00 28.86           N  
ANISOU 3242  N   VAL A 424     3730   3714   3521   -988    700    568       N  
ATOM   3243  CA  VAL A 424      -0.090   9.299   0.954  1.00 39.99           C  
ANISOU 3243  CA  VAL A 424     5081   5225   4889   -955    728    554       C  
ATOM   3244  C   VAL A 424       0.355  10.110   2.166  1.00 35.64           C  
ANISOU 3244  C   VAL A 424     4524   4776   4241   -874    734    508       C  
ATOM   3245  O   VAL A 424      -0.080  11.252   2.358  1.00 29.85           O  
ANISOU 3245  O   VAL A 424     3770   4093   3478   -826    726    432       O  
ATOM   3246  CB  VAL A 424      -1.192   8.288   1.320  1.00 40.13           C  
ANISOU 3246  CB  VAL A 424     5042   5289   4916   -994    776    660       C  
ATOM   3247  CG1 VAL A 424      -2.247   8.934   2.215  1.00 30.88           C  
ANISOU 3247  CG1 VAL A 424     3802   4251   3680   -946    815    656       C  
ATOM   3248  CG2 VAL A 424      -1.829   7.720   0.060  1.00 42.00           C  
ANISOU 3248  CG2 VAL A 424     5276   5427   5253  -1068    760    681       C  
ATOM   3249  N   GLU A 425       1.228   9.539   2.999  1.00 35.43           N  
ANISOU 3249  N   GLU A 425     4516   4782   4164   -855    743    548       N  
ATOM   3250  CA  GLU A 425       1.691  10.251   4.187  1.00 35.56           C  
ANISOU 3250  CA  GLU A 425     4527   4900   4083   -775    743    501       C  
ATOM   3251  C   GLU A 425       2.540  11.459   3.813  1.00 33.63           C  
ANISOU 3251  C   GLU A 425     4322   4608   3848   -742    687    380       C  
ATOM   3252  O   GLU A 425       2.393  12.537   4.403  1.00 35.10           O  
ANISOU 3252  O   GLU A 425     4492   4862   3983   -678    675    302       O  
ATOM   3253  CB  GLU A 425       2.476   9.301   5.092  1.00 40.47           C  
ANISOU 3253  CB  GLU A 425     5163   5562   4652   -762    762    576       C  
ATOM   3254  CG  GLU A 425       3.359   9.997   6.117  1.00 44.60           C  
ANISOU 3254  CG  GLU A 425     5698   6163   5084   -682    742    512       C  
ATOM   3255  CD  GLU A 425       2.673  10.170   7.459  1.00 67.17           C  
ANISOU 3255  CD  GLU A 425     8505   9181   7835   -614    784    533       C  
ATOM   3256  OE1 GLU A 425       1.481   9.811   7.571  1.00 76.06           O  
ANISOU 3256  OE1 GLU A 425     9581  10359   8960   -632    832    599       O  
ATOM   3257  OE2 GLU A 425       3.326  10.665   8.402  1.00 72.40           O  
ANISOU 3257  OE2 GLU A 425     9174   9922   8413   -541    768    482       O  
ATOM   3258  N   VAL A 426       3.426  11.303   2.830  1.00 33.82           N  
ANISOU 3258  N   VAL A 426     4394   4516   3940   -784    651    365       N  
ATOM   3259  CA  VAL A 426       4.287  12.407   2.420  1.00 36.03           C  
ANISOU 3259  CA  VAL A 426     4707   4744   4239   -762    599    263       C  
ATOM   3260  C   VAL A 426       3.463  13.520   1.782  1.00 38.51           C  
ANISOU 3260  C   VAL A 426     5008   5037   4589   -756    583    193       C  
ATOM   3261  O   VAL A 426       3.626  14.700   2.112  1.00 37.45           O  
ANISOU 3261  O   VAL A 426     4873   4925   4433   -705    553    105       O  
ATOM   3262  CB  VAL A 426       5.391  11.899   1.474  1.00 33.75           C  
ANISOU 3262  CB  VAL A 426     4467   4344   4013   -810    572    275       C  
ATOM   3263  CG1 VAL A 426       5.951  13.040   0.636  1.00 29.48           C  
ANISOU 3263  CG1 VAL A 426     3951   3729   3519   -809    524    186       C  
ATOM   3264  CG2 VAL A 426       6.494  11.225   2.275  1.00 40.80           C  
ANISOU 3264  CG2 VAL A 426     5377   5266   4858   -790    571    309       C  
ATOM   3265  N   SER A 427       2.552  13.162   0.874  1.00 33.85           N  
ANISOU 3265  N   SER A 427     4404   4401   4056   -804    597    230       N  
ATOM   3266  CA  SER A 427       1.785  14.186   0.171  1.00 39.30           C  
ANISOU 3266  CA  SER A 427     5083   5066   4784   -798    579    168       C  
ATOM   3267  C   SER A 427       0.848  14.928   1.116  1.00 31.25           C  
ANISOU 3267  C   SER A 427     4016   4156   3703   -735    597    131       C  
ATOM   3268  O   SER A 427       0.665  16.143   0.983  1.00 39.13           O  
ANISOU 3268  O   SER A 427     5015   5147   4707   -695    567     46       O  
ATOM   3269  CB  SER A 427       1.003  13.562  -0.984  1.00 38.61           C  
ANISOU 3269  CB  SER A 427     4989   4915   4766   -861    588    216       C  
ATOM   3270  OG  SER A 427       1.813  12.654  -1.711  1.00 38.44           O  
ANISOU 3270  OG  SER A 427     5008   4808   4789   -913    578    258       O  
ATOM   3271  N   ARG A 428       0.240  14.216   2.068  1.00 37.73           N  
ANISOU 3271  N   ARG A 428     4794   5078   4464   -721    645    196       N  
ATOM   3272  CA  ARG A 428      -0.625  14.881   3.036  1.00 38.76           C  
ANISOU 3272  CA  ARG A 428     4875   5330   4523   -651    667    164       C  
ATOM   3273  C   ARG A 428       0.170  15.844   3.910  1.00 30.44           C  
ANISOU 3273  C   ARG A 428     3839   4320   3406   -574    634     73       C  
ATOM   3274  O   ARG A 428      -0.318  16.925   4.262  1.00 30.83           O  
ANISOU 3274  O   ARG A 428     3870   4418   3427   -510    619     -9       O  
ATOM   3275  CB  ARG A 428      -1.349  13.845   3.897  1.00 30.93           C  
ANISOU 3275  CB  ARG A 428     3830   4445   3477   -655    731    266       C  
ATOM   3276  CG  ARG A 428      -2.510  13.160   3.195  1.00 37.87           C  
ANISOU 3276  CG  ARG A 428     4668   5304   4415   -719    762    340       C  
ATOM   3277  CD  ARG A 428      -3.137  12.093   4.079  1.00 33.29           C  
ANISOU 3277  CD  ARG A 428     4034   4824   3789   -730    826    454       C  
ATOM   3278  NE  ARG A 428      -3.525  12.622   5.383  1.00 35.81           N  
ANISOU 3278  NE  ARG A 428     4309   5297   4001   -643    857    436       N  
ATOM   3279  CZ  ARG A 428      -4.603  13.369   5.597  1.00 38.99           C  
ANISOU 3279  CZ  ARG A 428     4657   5783   4376   -597    874    397       C  
ATOM   3280  NH1 ARG A 428      -5.411  13.680   4.592  1.00 42.11           N  
ANISOU 3280  NH1 ARG A 428     5034   6120   4845   -631    861    374       N  
ATOM   3281  NH2 ARG A 428      -4.874  13.805   6.819  1.00 49.74           N  
ANISOU 3281  NH2 ARG A 428     5979   7290   5629   -510    902    378       N  
ATOM   3282  N   ASN A 429       1.400  15.471   4.265  1.00 32.17           N  
ANISOU 3282  N   ASN A 429     4095   4522   3606   -576    618     81       N  
ATOM   3283  CA  ASN A 429       2.235  16.357   5.068  1.00 35.49           C  
ANISOU 3283  CA  ASN A 429     4533   4978   3974   -506    578    -10       C  
ATOM   3284  C   ASN A 429       2.704  17.555   4.256  1.00 37.36           C  
ANISOU 3284  C   ASN A 429     4804   5112   4281   -507    515   -111       C  
ATOM   3285  O   ASN A 429       2.826  18.663   4.790  1.00 33.19           O  
ANISOU 3285  O   ASN A 429     4275   4612   3725   -442    478   -210       O  
ATOM   3286  CB  ASN A 429       3.423  15.583   5.636  1.00 36.79           C  
ANISOU 3286  CB  ASN A 429     4723   5154   4102   -510    576     30       C  
ATOM   3287  CG  ASN A 429       3.019  14.663   6.769  1.00 32.58           C  
ANISOU 3287  CG  ASN A 429     4155   4748   3478   -482    633    116       C  
ATOM   3288  OD1 ASN A 429       1.915  14.774   7.299  1.00 31.97           O  
ANISOU 3288  OD1 ASN A 429     4029   4768   3350   -447    671    130       O  
ATOM   3289  ND2 ASN A 429       3.905  13.747   7.141  1.00 36.92           N  
ANISOU 3289  ND2 ASN A 429     4725   5300   4004   -496    639    178       N  
ATOM   3290  N   LEU A 430       2.973  17.351   2.963  1.00 31.14           N  
ANISOU 3290  N   LEU A 430     4045   4202   3584   -579    501    -88       N  
ATOM   3291  CA  LEU A 430       3.311  18.471   2.091  1.00 38.37           C  
ANISOU 3291  CA  LEU A 430     4990   5019   4571   -585    448   -167       C  
ATOM   3292  C   LEU A 430       2.168  19.474   2.021  1.00 38.87           C  
ANISOU 3292  C   LEU A 430     5027   5104   4639   -543    441   -226       C  
ATOM   3293  O   LEU A 430       2.397  20.690   2.017  1.00 37.26           O  
ANISOU 3293  O   LEU A 430     4836   4866   4455   -505    393   -318       O  
ATOM   3294  CB  LEU A 430       3.659  17.960   0.694  1.00 35.91           C  
ANISOU 3294  CB  LEU A 430     4708   4591   4344   -665    444   -117       C  
ATOM   3295  CG  LEU A 430       4.956  17.166   0.563  1.00 46.05           C  
ANISOU 3295  CG  LEU A 430     6025   5832   5639   -702    439    -76       C  
ATOM   3296  CD1 LEU A 430       5.053  16.529  -0.811  1.00 40.48           C  
ANISOU 3296  CD1 LEU A 430     5343   5032   5007   -772    443    -22       C  
ATOM   3297  CD2 LEU A 430       6.145  18.064   0.827  1.00 47.27           C  
ANISOU 3297  CD2 LEU A 430     6202   5958   5799   -677    387   -152       C  
ATOM   3298  N   GLY A 431       0.928  18.984   1.968  1.00 31.01           N  
ANISOU 3298  N   GLY A 431     3991   4162   3629   -550    488   -173       N  
ATOM   3299  CA  GLY A 431      -0.212  19.886   1.965  1.00 32.15           C  
ANISOU 3299  CA  GLY A 431     4104   4341   3772   -502    484   -227       C  
ATOM   3300  C   GLY A 431      -0.343  20.657   3.263  1.00 42.09           C  
ANISOU 3300  C   GLY A 431     5341   5705   4947   -406    475   -304       C  
ATOM   3301  O   GLY A 431      -0.749  21.822   3.266  1.00 33.97           O  
ANISOU 3301  O   GLY A 431     4308   4670   3928   -352    441   -393       O  
ATOM   3302  N   LYS A 432       0.002  20.017   4.385  1.00 43.45           N  
ANISOU 3302  N   LYS A 432     5498   5975   5034   -379    503   -273       N  
ATOM   3303  CA  LYS A 432      -0.023  20.702   5.674  1.00 38.86           C  
ANISOU 3303  CA  LYS A 432     4898   5504   4362   -280    491   -351       C  
ATOM   3304  C   LYS A 432       1.007  21.823   5.734  1.00 40.33           C  
ANISOU 3304  C   LYS A 432     5129   5621   4576   -246    414   -466       C  
ATOM   3305  O   LYS A 432       0.777  22.838   6.401  1.00 42.22           O  
ANISOU 3305  O   LYS A 432     5358   5909   4776   -162    381   -567       O  
ATOM   3306  CB  LYS A 432       0.218  19.703   6.807  1.00 41.79           C  
ANISOU 3306  CB  LYS A 432     5248   5994   4635   -260    537   -282       C  
ATOM   3307  CG  LYS A 432      -0.903  18.692   7.001  1.00 50.09           C  
ANISOU 3307  CG  LYS A 432     6245   7136   5651   -280    615   -170       C  
ATOM   3308  CD  LYS A 432      -0.583  17.727   8.134  1.00 64.73           C  
ANISOU 3308  CD  LYS A 432     8083   9104   7410   -259    659    -94       C  
ATOM   3309  CE  LYS A 432      -1.675  16.681   8.297  1.00 75.03           C  
ANISOU 3309  CE  LYS A 432     9329  10488   8690   -290    738     31       C  
ATOM   3310  NZ  LYS A 432      -2.930  17.265   8.847  1.00 79.75           N  
ANISOU 3310  NZ  LYS A 432     9863  11210   9228   -219    769      2       N  
ATOM   3311  N   VAL A 433       2.146  21.658   5.054  1.00 48.39           N  
ANISOU 3311  N   VAL A 433     6194   6529   5664   -310    382   -454       N  
ATOM   3312  CA  VAL A 433       3.144  22.723   5.004  1.00 43.91           C  
ANISOU 3312  CA  VAL A 433     5662   5882   5138   -292    307   -554       C  
ATOM   3313  C   VAL A 433       2.572  23.949   4.304  1.00 41.25           C  
ANISOU 3313  C   VAL A 433     5332   5469   4872   -277    267   -628       C  
ATOM   3314  O   VAL A 433       2.814  25.090   4.716  1.00 40.18           O  
ANISOU 3314  O   VAL A 433     5206   5317   4742   -219    208   -737       O  
ATOM   3315  CB  VAL A 433       4.429  22.223   4.317  1.00 45.32           C  
ANISOU 3315  CB  VAL A 433     5879   5960   5379   -370    290   -511       C  
ATOM   3316  CG1 VAL A 433       5.453  23.344   4.217  1.00 52.84           C  
ANISOU 3316  CG1 VAL A 433     6861   6827   6387   -361    212   -608       C  
ATOM   3317  CG2 VAL A 433       5.009  21.039   5.072  1.00 44.77           C  
ANISOU 3317  CG2 VAL A 433     5805   5967   5239   -376    325   -442       C  
ATOM   3318  N   GLY A 434       1.795  23.732   3.241  1.00 43.78           N  
ANISOU 3318  N   GLY A 434     5647   5738   5248   -326    294   -572       N  
ATOM   3319  CA  GLY A 434       1.159  24.850   2.564  1.00 39.91           C  
ANISOU 3319  CA  GLY A 434     5162   5181   4821   -307    259   -633       C  
ATOM   3320  C   GLY A 434       0.144  25.563   3.437  1.00 36.14           C  
ANISOU 3320  C   GLY A 434     4649   4803   4282   -209    258   -708       C  
ATOM   3321  O   GLY A 434       0.114  26.795   3.488  1.00 45.45           O  
ANISOU 3321  O   GLY A 434     5841   5939   5491   -156    200   -809       O  
ATOM   3322  N   SER A 435      -0.697  24.801   4.142  1.00 44.42           N  
ANISOU 3322  N   SER A 435     5649   5985   5243   -181    320   -659       N  
ATOM   3323  CA  SER A 435      -1.703  25.415   5.004  1.00 48.18           C  
ANISOU 3323  CA  SER A 435     6083   6574   5647    -80    327   -725       C  
ATOM   3324  C   SER A 435      -1.068  26.233   6.119  1.00 36.39           C  
ANISOU 3324  C   SER A 435     4603   5125   4100      9    275   -839       C  
ATOM   3325  O   SER A 435      -1.647  27.229   6.566  1.00 45.17           O  
ANISOU 3325  O   SER A 435     5700   6273   5188     98    244   -938       O  
ATOM   3326  CB  SER A 435      -2.617  24.341   5.597  1.00 53.46           C  
ANISOU 3326  CB  SER A 435     6693   7389   6231    -73    410   -634       C  
ATOM   3327  OG  SER A 435      -3.443  23.764   4.604  1.00 64.33           O  
ANISOU 3327  OG  SER A 435     8049   8732   7662   -141    450   -549       O  
ATOM   3328  N   LYS A 436       0.120  25.839   6.574  1.00 39.80           N  
ANISOU 3328  N   LYS A 436     5060   5552   4510    -11    259   -833       N  
ATOM   3329  CA  LYS A 436       0.776  26.519   7.684  1.00 49.59           C  
ANISOU 3329  CA  LYS A 436     6309   6840   5692     73    206   -942       C  
ATOM   3330  C   LYS A 436       1.592  27.729   7.233  1.00 47.49           C  
ANISOU 3330  C   LYS A 436     6089   6431   5525     69    112  -1047       C  
ATOM   3331  O   LYS A 436       1.517  28.794   7.851  1.00 49.75           O  
ANISOU 3331  O   LYS A 436     6377   6732   5795    156     55  -1171       O  
ATOM   3332  CB  LYS A 436       1.672  25.533   8.443  1.00 42.45           C  
ANISOU 3332  CB  LYS A 436     5406   6006   4716     59    229   -888       C  
ATOM   3333  CG  LYS A 436       2.519  26.181   9.528  1.00 54.67           C  
ANISOU 3333  CG  LYS A 436     6967   7596   6209    138    165  -1002       C  
ATOM   3334  CD  LYS A 436       3.564  25.223  10.073  1.00 57.56           C  
ANISOU 3334  CD  LYS A 436     7341   8005   6523    112    179   -944       C  
ATOM   3335  CE  LYS A 436       4.108  25.710  11.408  1.00 64.76           C  
ANISOU 3335  CE  LYS A 436     8250   9015   7341    213    130  -1050       C  
ATOM   3336  NZ  LYS A 436       3.047  25.770  12.451  1.00 68.36           N  
ANISOU 3336  NZ  LYS A 436     8662   9643   7669    323    169  -1075       N  
ATOM   3337  N   CYS A 437       2.371  27.585   6.161  1.00 38.84           N  
ANISOU 3337  N   CYS A 437     5029   5197   4532    -29     96   -998       N  
ATOM   3338  CA  CYS A 437       3.365  28.595   5.814  1.00 45.16           C  
ANISOU 3338  CA  CYS A 437     5869   5866   5425    -44     10  -1080       C  
ATOM   3339  C   CYS A 437       2.851  29.642   4.836  1.00 44.76           C  
ANISOU 3339  C   CYS A 437     5834   5696   5477    -52    -27  -1118       C  
ATOM   3340  O   CYS A 437       3.293  30.796   4.892  1.00 45.65           O  
ANISOU 3340  O   CYS A 437     5969   5725   5650    -24   -106  -1218       O  
ATOM   3341  CB  CYS A 437       4.610  27.925   5.231  1.00 38.80           C  
ANISOU 3341  CB  CYS A 437     5089   4982   4673   -141     11  -1007       C  
ATOM   3342  SG  CYS A 437       5.329  26.633   6.278  1.00 44.50           S  
ANISOU 3342  SG  CYS A 437     5796   5828   5283   -138     52   -951       S  
ATOM   3343  N   CYS A 438       1.926  29.268   3.946  1.00 45.74           N  
ANISOU 3343  N   CYS A 438     5948   5807   5626    -89     23  -1039       N  
ATOM   3344  CA  CYS A 438       1.442  30.190   2.927  1.00 40.59           C  
ANISOU 3344  CA  CYS A 438     5311   5041   5069    -99    -10  -1062       C  
ATOM   3345  C   CYS A 438       0.738  31.400   3.530  1.00 51.29           C  
ANISOU 3345  C   CYS A 438     6659   6416   6413      7    -59  -1185       C  
ATOM   3346  O   CYS A 438       0.645  32.431   2.859  1.00 48.92           O  
ANISOU 3346  O   CYS A 438     6383   6001   6206     10   -112  -1230       O  
ATOM   3347  CB  CYS A 438       0.506  29.465   1.950  1.00 32.22           C  
ANISOU 3347  CB  CYS A 438     4236   3985   4023   -150     55   -957       C  
ATOM   3348  SG  CYS A 438       1.363  28.253   0.863  1.00 39.15           S  
ANISOU 3348  SG  CYS A 438     5135   4793   4948   -278     94   -824       S  
ATOM   3349  N   LYS A 439       0.213  31.292   4.758  1.00 49.35           N  
ANISOU 3349  N   LYS A 439     6378   6316   6055     99    -41  -1236       N  
ATOM   3350  CA  LYS A 439      -0.431  32.415   5.427  1.00 46.70           C  
ANISOU 3350  CA  LYS A 439     6034   6013   5696    213    -89  -1363       C  
ATOM   3351  C   LYS A 439       0.559  33.385   6.056  1.00 53.87           C  
ANISOU 3351  C   LYS A 439     6974   6862   6634    256   -183  -1489       C  
ATOM   3352  O   LYS A 439       0.159  34.492   6.422  1.00 55.34           O  
ANISOU 3352  O   LYS A 439     7164   7032   6832    345   -243  -1608       O  
ATOM   3353  CB  LYS A 439      -1.385  31.885   6.494  1.00 50.49           C  
ANISOU 3353  CB  LYS A 439     6459   6687   6036    299    -29  -1365       C  
ATOM   3354  CG  LYS A 439      -0.692  31.234   7.683  1.00 58.53           C  
ANISOU 3354  CG  LYS A 439     7467   7822   6949    326    -13  -1370       C  
ATOM   3355  CD  LYS A 439      -1.700  30.732   8.704  1.00 72.38           C  
ANISOU 3355  CD  LYS A 439     9164   9776   8563    413     53  -1359       C  
ATOM   3356  CE  LYS A 439      -1.325  29.356   9.233  1.00 79.36           C  
ANISOU 3356  CE  LYS A 439    10027  10766   9361    372    123  -1250       C  
ATOM   3357  NZ  LYS A 439      -0.116  29.406  10.103  1.00 83.89           N  
ANISOU 3357  NZ  LYS A 439    10625  11358   9891    398     76  -1309       N  
ATOM   3358  N   HIS A 440       1.825  33.000   6.197  1.00 50.47           N  
ANISOU 3358  N   HIS A 440     6563   6398   6217    199   -201  -1470       N  
ATOM   3359  CA  HIS A 440       2.809  33.841   6.852  1.00 59.66           C  
ANISOU 3359  CA  HIS A 440     7750   7512   7407    235   -293  -1589       C  
ATOM   3360  C   HIS A 440       3.195  35.018   5.962  1.00 68.66           C  
ANISOU 3360  C   HIS A 440     8927   8461   8699    198   -374  -1637       C  
ATOM   3361  O   HIS A 440       3.019  34.974   4.741  1.00 60.07           O  
ANISOU 3361  O   HIS A 440     7853   7276   7696    122   -351  -1552       O  
ATOM   3362  CB  HIS A 440       4.052  33.024   7.193  1.00 53.84           C  
ANISOU 3362  CB  HIS A 440     7017   6796   6644    177   -286  -1544       C  
ATOM   3363  CG  HIS A 440       3.844  32.031   8.294  1.00 61.28           C  
ANISOU 3363  CG  HIS A 440     7926   7923   7435    229   -226  -1517       C  
ATOM   3364  ND1 HIS A 440       2.786  32.104   9.174  1.00 66.99           N  
ANISOU 3364  ND1 HIS A 440     8616   8790   8046    338   -199  -1565       N  
ATOM   3365  CD2 HIS A 440       4.562  30.942   8.659  1.00 61.23           C  
ANISOU 3365  CD2 HIS A 440     7913   7983   7368    189   -186  -1443       C  
ATOM   3366  CE1 HIS A 440       2.860  31.103  10.033  1.00 66.07           C  
ANISOU 3366  CE1 HIS A 440     8473   8822   7807    360   -143  -1515       C  
ATOM   3367  NE2 HIS A 440       3.929  30.383   9.742  1.00 61.48           N  
ANISOU 3367  NE2 HIS A 440     7910   8193   7256    271   -136  -1441       N  
ATOM   3368  N   PRO A 441       3.709  36.094   6.556  1.00 77.49           N  
ANISOU 3368  N   PRO A 441    10063   9525   9856    254   -471  -1772       N  
ATOM   3369  CA  PRO A 441       4.317  37.156   5.750  1.00 81.22           C  
ANISOU 3369  CA  PRO A 441    10571   9804  10486    204   -552  -1806       C  
ATOM   3370  C   PRO A 441       5.542  36.633   5.019  1.00 89.11           C  
ANISOU 3370  C   PRO A 441    11583  10716  11558     77   -544  -1709       C  
ATOM   3371  O   PRO A 441       6.190  35.677   5.449  1.00 90.24           O  
ANISOU 3371  O   PRO A 441    11713  10941  11634     48   -507  -1663       O  
ATOM   3372  CB  PRO A 441       4.692  38.224   6.786  1.00 72.11           C  
ANISOU 3372  CB  PRO A 441     9426   8634   9339    295   -658  -1977       C  
ATOM   3373  CG  PRO A 441       4.686  37.512   8.106  1.00 72.10           C  
ANISOU 3373  CG  PRO A 441     9396   8820   9178    370   -629  -2015       C  
ATOM   3374  CD  PRO A 441       3.655  36.440   7.986  1.00 73.54           C  
ANISOU 3374  CD  PRO A 441     9548   9139   9256    374   -513  -1904       C  
ATOM   3375  N   GLU A 442       5.836  37.226   3.856  1.00 90.49           N  
ANISOU 3375  N   GLU A 442    11783  10727  11873      5   -577  -1675       N  
ATOM   3376  CA  GLU A 442       6.944  36.717   2.996  1.00 85.10           C  
ANISOU 3376  CA  GLU A 442    11108   9966  11259   -115   -560  -1570       C  
ATOM   3377  C   GLU A 442       8.294  36.802   3.713  1.00 75.15           C  
ANISOU 3377  C   GLU A 442     9846   8678  10028   -135   -625  -1630       C  
ATOM   3378  O   GLU A 442       9.234  36.108   3.279  1.00 70.33           O  
ANISOU 3378  O   GLU A 442     9234   8040   9449   -225   -604  -1548       O  
ATOM   3379  CB  GLU A 442       6.979  37.482   1.672  1.00 87.91           C  
ANISOU 3379  CB  GLU A 442    11487  10162  11751   -181   -575  -1511       C  
ATOM   3380  CG  GLU A 442       5.604  37.697   1.068  1.00 92.14           C  
ANISOU 3380  CG  GLU A 442    12025  10709  12273   -150   -529  -1470       C  
ATOM   3381  CD  GLU A 442       4.829  36.421   0.790  1.00 95.58           C  
ANISOU 3381  CD  GLU A 442    12440  11266  12609   -173   -422  -1361       C  
ATOM   3382  OE1 GLU A 442       3.808  36.192   1.471  1.00 98.51           O  
ANISOU 3382  OE1 GLU A 442    12813  11623  12993   -181   -384  -1300       O  
ATOM   3383  OE2 GLU A 442       5.248  35.661  -0.105  1.00 95.96           O  
ANISOU 3383  OE2 GLU A 442    12471  11421  12570   -183   -380  -1334       O  
ATOM   3384  N   ALA A 443       8.378  37.602   4.779  1.00 78.04           N  
ANISOU 3384  N   ALA A 443    10212   9058  10381    -51   -707  -1776       N  
ATOM   3385  CA  ALA A 443       9.648  37.757   5.525  1.00 90.79           C  
ANISOU 3385  CA  ALA A 443    11819  10675  12000    -57   -769  -1844       C  
ATOM   3386  C   ALA A 443       9.917  36.503   6.365  1.00 92.39           C  
ANISOU 3386  C   ALA A 443    11999  11045  12061    -43   -706  -1805       C  
ATOM   3387  O   ALA A 443      11.025  36.398   6.925  1.00 97.19           O  
ANISOU 3387  O   ALA A 443    12597  11662  12669    -67   -743  -1829       O  
ATOM   3388  CB  ALA A 443       9.593  38.998   6.379  1.00 95.78           C  
ANISOU 3388  CB  ALA A 443    12458  11283  12651     40   -879  -2022       C  
ATOM   3389  N   LYS A 444       8.941  35.593   6.446  1.00 84.43           N  
ANISOU 3389  N   LYS A 444    10978  10166  10935     -8   -614  -1740       N  
ATOM   3390  CA  LYS A 444       9.094  34.362   7.263  1.00 71.80           C  
ANISOU 3390  CA  LYS A 444     9357   8724   9200      8   -552  -1693       C  
ATOM   3391  C   LYS A 444       8.453  33.169   6.549  1.00 61.00           C  
ANISOU 3391  C   LYS A 444     7982   7409   7787    -48   -439  -1538       C  
ATOM   3392  O   LYS A 444       8.395  32.092   7.175  1.00 51.79           O  
ANISOU 3392  O   LYS A 444     6798   6366   6513    -40   -381  -1484       O  
ATOM   3393  CB  LYS A 444       8.393  34.544   8.611  1.00 66.52           C  
ANISOU 3393  CB  LYS A 444     8672   8205   8397    142   -562  -1799       C  
ATOM   3394  CG  LYS A 444       9.276  35.029   9.752  1.00 73.94           C  
ANISOU 3394  CG  LYS A 444     9611   9156   9327    202   -662  -1942       C  
ATOM   3395  CD  LYS A 444       8.637  36.131  10.567  1.00 72.96           C  
ANISOU 3395  CD  LYS A 444     9484   9091   9144    337   -712  -2088       C  
ATOM   3396  CE  LYS A 444       9.060  37.515  10.127  1.00 73.95           C  
ANISOU 3396  CE  LYS A 444     9624   9130   9345    374   -845  -2249       C  
ATOM   3397  NZ  LYS A 444       7.935  38.265   9.521  1.00 75.58           N  
ANISOU 3397  NZ  LYS A 444     9840   9308   9567    477   -908  -2383       N  
ATOM   3398  N   ARG A 445       7.995  33.331   5.300  1.00 49.01           N  
ANISOU 3398  N   ARG A 445     6475   5798   6347   -104   -409  -1466       N  
ATOM   3399  CA  ARG A 445       7.295  32.210   4.681  1.00 39.62           C  
ANISOU 3399  CA  ARG A 445     5278   4666   5111   -144   -309  -1336       C  
ATOM   3400  C   ARG A 445       8.257  31.198   4.067  1.00 46.26           C  
ANISOU 3400  C   ARG A 445     6122   5482   5973   -243   -269  -1223       C  
ATOM   3401  O   ARG A 445       8.014  29.989   4.141  1.00 46.19           O  
ANISOU 3401  O   ARG A 445     6101   5565   5886   -258   -194  -1135       O  
ATOM   3402  CB  ARG A 445       6.314  32.725   3.627  1.00 42.65           C  
ANISOU 3402  CB  ARG A 445     5671   4971   5563   -157   -296  -1308       C  
ATOM   3403  CG  ARG A 445       5.584  31.623   2.886  1.00 47.64           C  
ANISOU 3403  CG  ARG A 445     6292   5648   6161   -204   -202  -1180       C  
ATOM   3404  CD  ARG A 445       5.189  32.055   1.494  1.00 43.68           C  
ANISOU 3404  CD  ARG A 445     5810   5028   5761   -256   -201  -1129       C  
ATOM   3405  NE  ARG A 445       3.935  32.801   1.475  1.00 55.17           N  
ANISOU 3405  NE  ARG A 445     7259   6489   7216   -187   -211  -1181       N  
ATOM   3406  CZ  ARG A 445       3.258  33.085   0.368  1.00 64.72           C  
ANISOU 3406  CZ  ARG A 445     8477   7627   8487   -212   -199  -1135       C  
ATOM   3407  NH1 ARG A 445       3.717  32.689  -0.812  1.00 58.25           N  
ANISOU 3407  NH1 ARG A 445     7674   6727   7731   -303   -177  -1038       N  
ATOM   3408  NH2 ARG A 445       2.125  33.770   0.437  1.00 73.56           N  
ANISOU 3408  NH2 ARG A 445     9587   8760   9601   -140   -212  -1189       N  
ATOM   3409  N   MET A 446       9.348  31.661   3.456  1.00 55.84           N  
ANISOU 3409  N   MET A 446     7351   6574   7293   -310   -317  -1222       N  
ATOM   3410  CA  MET A 446      10.286  30.731   2.833  1.00 51.01           C  
ANISOU 3410  CA  MET A 446     6739   5940   6700   -398   -280  -1118       C  
ATOM   3411  C   MET A 446      11.046  29.907   3.872  1.00 43.21           C  
ANISOU 3411  C   MET A 446     5737   5058   5624   -379   -273  -1123       C  
ATOM   3412  O   MET A 446      11.249  28.705   3.655  1.00 52.44           O  
ANISOU 3412  O   MET A 446     6902   6276   6748   -418   -209  -1024       O  
ATOM   3413  CB  MET A 446      11.270  31.465   1.919  1.00 56.85           C  
ANISOU 3413  CB  MET A 446     7491   6532   7576   -473   -330  -1110       C  
ATOM   3414  CG  MET A 446      11.938  30.542   0.909  1.00 63.51           C  
ANISOU 3414  CG  MET A 446     8337   7346   8447   -563   -277   -985       C  
ATOM   3415  SD  MET A 446      13.712  30.806   0.731  1.00 68.30           S  
ANISOU 3415  SD  MET A 446     8934   7874   9142   -632   -331   -986       S  
ATOM   3416  CE  MET A 446      13.739  32.413  -0.053  1.00 70.63           C  
ANISOU 3416  CE  MET A 446     9241   8006   9587   -659   -401  -1027       C  
ATOM   3417  N   PRO A 447      11.500  30.488   4.993  1.00 42.35           N  
ANISOU 3417  N   PRO A 447     5620   4986   5487   -317   -339  -1235       N  
ATOM   3418  CA  PRO A 447      12.040  29.627   6.059  1.00 51.12           C  
ANISOU 3418  CA  PRO A 447     6714   6219   6490   -284   -325  -1236       C  
ATOM   3419  C   PRO A 447      11.047  28.579   6.523  1.00 47.12           C  
ANISOU 3419  C   PRO A 447     6196   5850   5856   -241   -241  -1172       C  
ATOM   3420  O   PRO A 447      11.435  27.439   6.805  1.00 51.23           O  
ANISOU 3420  O   PRO A 447     6710   6444   6310   -257   -194  -1098       O  
ATOM   3421  CB  PRO A 447      12.380  30.624   7.175  1.00 51.76           C  
ANISOU 3421  CB  PRO A 447     6789   6319   6557   -206   -418  -1386       C  
ATOM   3422  CG  PRO A 447      12.644  31.889   6.469  1.00 45.00           C  
ANISOU 3422  CG  PRO A 447     5946   5307   5844   -242   -490  -1443       C  
ATOM   3423  CD  PRO A 447      11.689  31.916   5.314  1.00 37.38           C  
ANISOU 3423  CD  PRO A 447     4996   4279   4929   -280   -437  -1365       C  
ATOM   3424  N   CYS A 448       9.763  28.933   6.597  1.00 36.64           N  
ANISOU 3424  N   CYS A 448     4866   4557   4499   -188   -220  -1197       N  
ATOM   3425  CA  CYS A 448       8.739  27.960   6.962  1.00 42.44           C  
ANISOU 3425  CA  CYS A 448     5582   5419   5125   -155   -136  -1127       C  
ATOM   3426  C   CYS A 448       8.587  26.896   5.881  1.00 32.31           C  
ANISOU 3426  C   CYS A 448     4304   4100   3871   -245    -62   -985       C  
ATOM   3427  O   CYS A 448       8.747  25.697   6.141  1.00 34.58           O  
ANISOU 3427  O   CYS A 448     4584   4462   4094   -262     -7   -900       O  
ATOM   3428  CB  CYS A 448       7.408  28.677   7.209  1.00 42.05           C  
ANISOU 3428  CB  CYS A 448     5521   5409   5047    -79   -135  -1189       C  
ATOM   3429  SG  CYS A 448       6.078  27.639   7.879  1.00 42.17           S  
ANISOU 3429  SG  CYS A 448     5500   5602   4921    -24    -37  -1117       S  
ATOM   3430  N   ALA A 449       8.283  27.322   4.655  1.00 31.79           N  
ANISOU 3430  N   ALA A 449     4254   3921   3906   -300    -63   -959       N  
ATOM   3431  CA  ALA A 449       7.913  26.380   3.604  1.00 36.02           C  
ANISOU 3431  CA  ALA A 449     4792   4429   4463   -371      4   -837       C  
ATOM   3432  C   ALA A 449       9.081  25.482   3.214  1.00 39.45           C  
ANISOU 3432  C   ALA A 449     5238   4833   4917   -442     19   -761       C  
ATOM   3433  O   ALA A 449       8.933  24.256   3.141  1.00 34.24           O  
ANISOU 3433  O   ALA A 449     4574   4225   4212   -468     80   -669       O  
ATOM   3434  CB  ALA A 449       7.385  27.138   2.386  1.00 36.68           C  
ANISOU 3434  CB  ALA A 449     4891   4400   4645   -405     -9   -834       C  
ATOM   3435  N   GLU A 450      10.252  26.068   2.958  1.00 30.29           N  
ANISOU 3435  N   GLU A 450     4091   3588   3830   -474    -38   -798       N  
ATOM   3436  CA  GLU A 450      11.347  25.284   2.395  1.00 30.18           C  
ANISOU 3436  CA  GLU A 450     4084   3536   3846   -543    -23   -723       C  
ATOM   3437  C   GLU A 450      12.037  24.406   3.432  1.00 33.17           C  
ANISOU 3437  C   GLU A 450     4453   4013   4139   -518    -13   -712       C  
ATOM   3438  O   GLU A 450      12.490  23.307   3.096  1.00 30.76           O  
ANISOU 3438  O   GLU A 450     4151   3716   3821   -560     28   -625       O  
ATOM   3439  CB  GLU A 450      12.372  26.199   1.723  1.00 30.97           C  
ANISOU 3439  CB  GLU A 450     4194   3517   4057   -589    -83   -756       C  
ATOM   3440  CG  GLU A 450      13.224  25.471   0.694  1.00 46.75           C  
ANISOU 3440  CG  GLU A 450     6200   5462   6103   -668    -55   -662       C  
ATOM   3441  CD  GLU A 450      14.142  26.392  -0.085  1.00 52.24           C  
ANISOU 3441  CD  GLU A 450     6897   6041   6911   -719   -104   -678       C  
ATOM   3442  OE1 GLU A 450      14.418  27.513   0.392  1.00 44.71           O  
ANISOU 3442  OE1 GLU A 450     5938   5051   6000   -696   -172   -769       O  
ATOM   3443  OE2 GLU A 450      14.593  25.986  -1.177  1.00 55.44           O  
ANISOU 3443  OE2 GLU A 450     7308   6393   7363   -781    -77   -599       O  
ATOM   3444  N   ASP A 451      12.140  24.861   4.682  1.00 30.71           N  
ANISOU 3444  N   ASP A 451     4128   3774   3765   -446    -53   -800       N  
ATOM   3445  CA  ASP A 451      12.772  24.029   5.698  1.00 37.85           C  
ANISOU 3445  CA  ASP A 451     5022   4779   4580   -415    -44   -787       C  
ATOM   3446  C   ASP A 451      11.862  22.891   6.143  1.00 30.89           C  
ANISOU 3446  C   ASP A 451     4132   4007   3597   -389     33   -707       C  
ATOM   3447  O   ASP A 451      12.349  21.792   6.429  1.00 42.25           O  
ANISOU 3447  O   ASP A 451     5570   5496   4987   -400     66   -635       O  
ATOM   3448  CB  ASP A 451      13.196  24.884   6.893  1.00 39.79           C  
ANISOU 3448  CB  ASP A 451     5257   5075   4787   -341   -116   -911       C  
ATOM   3449  CG  ASP A 451      14.390  25.766   6.577  1.00 47.32           C  
ANISOU 3449  CG  ASP A 451     6213   5926   5843   -378   -196   -977       C  
ATOM   3450  OD1 ASP A 451      15.175  25.399   5.676  1.00 40.66           O  
ANISOU 3450  OD1 ASP A 451     5374   5006   5069   -455   -185   -910       O  
ATOM   3451  OD2 ASP A 451      14.544  26.825   7.220  1.00 35.00           O  
ANISOU 3451  OD2 ASP A 451     4646   4358   4292   -328   -269  -1095       O  
ATOM   3452  N   TYR A 452      10.548  23.128   6.202  1.00 31.06           N  
ANISOU 3452  N   TYR A 452     4145   4066   3591   -356     62   -713       N  
ATOM   3453  CA  TYR A 452       9.617  22.028   6.426  1.00 31.05           C  
ANISOU 3453  CA  TYR A 452     4130   4154   3515   -348    141   -620       C  
ATOM   3454  C   TYR A 452       9.590  21.080   5.236  1.00 35.30           C  
ANISOU 3454  C   TYR A 452     4682   4620   4112   -436    189   -508       C  
ATOM   3455  O   TYR A 452       9.396  19.871   5.409  1.00 29.89           O  
ANISOU 3455  O   TYR A 452     3990   3988   3378   -450    244   -415       O  
ATOM   3456  CB  TYR A 452       8.214  22.569   6.703  1.00 31.41           C  
ANISOU 3456  CB  TYR A 452     4155   4255   3525   -294    159   -656       C  
ATOM   3457  CG  TYR A 452       7.894  22.716   8.173  1.00 47.06           C  
ANISOU 3457  CG  TYR A 452     6112   6381   5387   -194    157   -712       C  
ATOM   3458  CD1 TYR A 452       8.296  21.755   9.091  1.00 49.87           C  
ANISOU 3458  CD1 TYR A 452     6458   6842   5648   -169    187   -660       C  
ATOM   3459  CD2 TYR A 452       7.192  23.818   8.643  1.00 43.59           C  
ANISOU 3459  CD2 TYR A 452     5660   5976   4927   -118    125   -816       C  
ATOM   3460  CE1 TYR A 452       8.005  21.885  10.436  1.00 58.47           C  
ANISOU 3460  CE1 TYR A 452     7524   8075   6617    -70    187   -707       C  
ATOM   3461  CE2 TYR A 452       6.898  23.958   9.987  1.00 54.73           C  
ANISOU 3461  CE2 TYR A 452     7047   7529   6218    -17    123   -872       C  
ATOM   3462  CZ  TYR A 452       7.306  22.988  10.879  1.00 60.25           C  
ANISOU 3462  CZ  TYR A 452     7735   8339   6818      7    156   -815       C  
ATOM   3463  OH  TYR A 452       7.015  23.122  12.217  1.00 74.24           O  
ANISOU 3463  OH  TYR A 452     9482  10263   8462    113    156   -867       O  
ATOM   3464  N   LEU A 453       9.782  21.614   4.027  1.00 34.04           N  
ANISOU 3464  N   LEU A 453     4540   4338   4056   -492    166   -514       N  
ATOM   3465  CA  LEU A 453       9.863  20.779   2.832  1.00 28.65           C  
ANISOU 3465  CA  LEU A 453     3873   3585   3430   -569    203   -419       C  
ATOM   3466  C   LEU A 453      10.988  19.758   2.955  1.00 33.93           C  
ANISOU 3466  C   LEU A 453     4550   4260   4080   -596    213   -362       C  
ATOM   3467  O   LEU A 453      10.803  18.572   2.655  1.00 32.44           O  
ANISOU 3467  O   LEU A 453     4366   4082   3878   -628    262   -271       O  
ATOM   3468  CB  LEU A 453      10.059  21.670   1.602  1.00 28.25           C  
ANISOU 3468  CB  LEU A 453     3839   3410   3485   -614    170   -444       C  
ATOM   3469  CG  LEU A 453      10.009  21.103   0.182  1.00 46.01           C  
ANISOU 3469  CG  LEU A 453     6105   5580   5798   -685    200   -364       C  
ATOM   3470  CD1 LEU A 453       9.017  19.966   0.065  1.00 41.39           C  
ANISOU 3470  CD1 LEU A 453     5513   5042   5173   -696    261   -285       C  
ATOM   3471  CD2 LEU A 453       9.672  22.212  -0.811  1.00 34.37           C  
ANISOU 3471  CD2 LEU A 453     4640   4012   4405   -703    171   -398       C  
ATOM   3472  N   SER A 454      12.162  20.198   3.413  1.00 28.68           N  
ANISOU 3472  N   SER A 454     3887   3590   3421   -582    163   -417       N  
ATOM   3473  CA  SER A 454      13.271  19.269   3.603  1.00 36.46           C  
ANISOU 3473  CA  SER A 454     4877   4590   4387   -599    168   -369       C  
ATOM   3474  C   SER A 454      12.977  18.260   4.705  1.00 31.66           C  
ANISOU 3474  C   SER A 454     4259   4098   3672   -555    206   -322       C  
ATOM   3475  O   SER A 454      13.461  17.124   4.650  1.00 31.93           O  
ANISOU 3475  O   SER A 454     4301   4140   3689   -576    234   -244       O  
ATOM   3476  CB  SER A 454      14.555  20.039   3.914  1.00 44.66           C  
ANISOU 3476  CB  SER A 454     5911   5604   5454   -591    101   -445       C  
ATOM   3477  OG  SER A 454      14.475  20.674   5.176  1.00 44.81           O  
ANISOU 3477  OG  SER A 454     5915   5702   5409   -518     63   -531       O  
ATOM   3478  N   VAL A 455      12.191  18.651   5.709  1.00 29.60           N  
ANISOU 3478  N   VAL A 455     3980   3928   3338   -489    209   -366       N  
ATOM   3479  CA  VAL A 455      11.817  17.719   6.767  1.00 30.08           C  
ANISOU 3479  CA  VAL A 455     4027   4109   3292   -444    252   -310       C  
ATOM   3480  C   VAL A 455      10.908  16.626   6.214  1.00 37.55           C  
ANISOU 3480  C   VAL A 455     4973   5049   4244   -488    322   -196       C  
ATOM   3481  O   VAL A 455      11.105  15.435   6.485  1.00 29.70           O  
ANISOU 3481  O   VAL A 455     3982   4089   3213   -498    358   -108       O  
ATOM   3482  CB  VAL A 455      11.152  18.476   7.932  1.00 39.70           C  
ANISOU 3482  CB  VAL A 455     5222   5434   4427   -358    239   -387       C  
ATOM   3483  CG1 VAL A 455      10.372  17.523   8.807  1.00 31.45           C  
ANISOU 3483  CG1 VAL A 455     4157   4515   3279   -319    303   -308       C  
ATOM   3484  CG2 VAL A 455      12.197  19.225   8.750  1.00 31.54           C  
ANISOU 3484  CG2 VAL A 455     4188   4429   3367   -306    168   -490       C  
ATOM   3485  N   VAL A 456       9.904  17.014   5.424  1.00 29.38           N  
ANISOU 3485  N   VAL A 456     3936   3968   3260   -515    338   -198       N  
ATOM   3486  CA  VAL A 456       8.982  16.035   4.855  1.00 33.75           C  
ANISOU 3486  CA  VAL A 456     4484   4512   3828   -560    397    -99       C  
ATOM   3487  C   VAL A 456       9.697  15.155   3.836  1.00 36.49           C  
ANISOU 3487  C   VAL A 456     4859   4764   4240   -629    402    -32       C  
ATOM   3488  O   VAL A 456       9.459  13.942   3.768  1.00 32.20           O  
ANISOU 3488  O   VAL A 456     4317   4229   3688   -656    444     61       O  
ATOM   3489  CB  VAL A 456       7.764  16.744   4.235  1.00 31.10           C  
ANISOU 3489  CB  VAL A 456     4135   4150   3531   -567    405   -127       C  
ATOM   3490  CG1 VAL A 456       6.829  15.731   3.587  1.00 32.32           C  
ANISOU 3490  CG1 VAL A 456     4281   4289   3710   -619    459    -28       C  
ATOM   3491  CG2 VAL A 456       7.028  17.552   5.291  1.00 29.77           C  
ANISOU 3491  CG2 VAL A 456     3936   4084   3290   -488    402   -193       C  
ATOM   3492  N   LEU A 457      10.579  15.747   3.027  1.00 29.65           N  
ANISOU 3492  N   LEU A 457     4014   3808   3444   -658    360    -78       N  
ATOM   3493  CA  LEU A 457      11.336  14.961   2.058  1.00 27.30           C  
ANISOU 3493  CA  LEU A 457     3741   3430   3201   -714    364    -23       C  
ATOM   3494  C   LEU A 457      12.252  13.959   2.745  1.00 36.52           C  
ANISOU 3494  C   LEU A 457     4916   4639   4323   -700    370     25       C  
ATOM   3495  O   LEU A 457      12.471  12.860   2.222  1.00 29.46           O  
ANISOU 3495  O   LEU A 457     4037   3707   3449   -736    393     99       O  
ATOM   3496  CB  LEU A 457      12.147  15.883   1.146  1.00 34.16           C  
ANISOU 3496  CB  LEU A 457     4624   4210   4147   -740    319    -80       C  
ATOM   3497  CG  LEU A 457      11.373  16.627   0.057  1.00 29.94           C  
ANISOU 3497  CG  LEU A 457     4093   3605   3678   -769    316   -100       C  
ATOM   3498  CD1 LEU A 457      12.273  17.629  -0.665  1.00 26.34           C  
ANISOU 3498  CD1 LEU A 457     3646   3070   3292   -790    270   -152       C  
ATOM   3499  CD2 LEU A 457      10.761  15.646  -0.926  1.00 30.32           C  
ANISOU 3499  CD2 LEU A 457     4152   3613   3755   -815    355    -22       C  
ATOM   3500  N   ASN A 458      12.795  14.315   3.913  1.00 28.06           N  
ANISOU 3500  N   ASN A 458     3832   3643   3186   -645    346    -20       N  
ATOM   3501  CA  ASN A 458      13.588  13.354   4.672  1.00 36.94           C  
ANISOU 3501  CA  ASN A 458     4960   4820   4255   -623    352     29       C  
ATOM   3502  C   ASN A 458      12.737  12.190   5.162  1.00 37.48           C  
ANISOU 3502  C   ASN A 458     5024   4946   4272   -618    409    127       C  
ATOM   3503  O   ASN A 458      13.236  11.065   5.278  1.00 28.80           O  
ANISOU 3503  O   ASN A 458     3938   3847   3160   -626    425    201       O  
ATOM   3504  CB  ASN A 458      14.270  14.034   5.857  1.00 28.99           C  
ANISOU 3504  CB  ASN A 458     3939   3892   3184   -558    311    -46       C  
ATOM   3505  CG  ASN A 458      15.188  13.093   6.610  1.00 30.18           C  
ANISOU 3505  CG  ASN A 458     4093   4096   3276   -531    311      1       C  
ATOM   3506  OD1 ASN A 458      16.227  12.683   6.096  1.00 35.20           O  
ANISOU 3506  OD1 ASN A 458     4744   4677   3954   -558    294     18       O  
ATOM   3507  ND2 ASN A 458      14.800  12.732   7.830  1.00 30.04           N  
ANISOU 3507  ND2 ASN A 458     4062   4191   3159   -473    332     26       N  
ATOM   3508  N   GLN A 459      11.460  12.438   5.458  1.00 28.94           N  
ANISOU 3508  N   GLN A 459     3920   3914   3162   -604    439    131       N  
ATOM   3509  CA  GLN A 459      10.562  11.345   5.810  1.00 35.42           C  
ANISOU 3509  CA  GLN A 459     4728   4781   3947   -612    496    234       C  
ATOM   3510  C   GLN A 459      10.431  10.357   4.656  1.00 35.01           C  
ANISOU 3510  C   GLN A 459     4698   4629   3976   -684    516    310       C  
ATOM   3511  O   GLN A 459      10.478   9.139   4.856  1.00 33.82           O  
ANISOU 3511  O   GLN A 459     4554   4482   3815   -698    544    402       O  
ATOM   3512  CB  GLN A 459       9.195  11.905   6.208  1.00 31.56           C  
ANISOU 3512  CB  GLN A 459     4205   4362   3424   -587    524    218       C  
ATOM   3513  CG  GLN A 459       8.175  10.854   6.607  1.00 49.50           C  
ANISOU 3513  CG  GLN A 459     6453   6692   5663   -598    586    329       C  
ATOM   3514  CD  GLN A 459       6.828  11.454   6.965  1.00 59.27           C  
ANISOU 3514  CD  GLN A 459     7648   8005   6867   -571    614    311       C  
ATOM   3515  OE1 GLN A 459       6.368  12.401   6.326  1.00 61.88           O  
ANISOU 3515  OE1 GLN A 459     7974   8295   7243   -578    594    238       O  
ATOM   3516  NE2 GLN A 459       6.187  10.903   7.990  1.00 49.38           N  
ANISOU 3516  NE2 GLN A 459     6361   6867   5534   -538    663    382       N  
ATOM   3517  N   LEU A 460      10.271  10.870   3.433  1.00 31.46           N  
ANISOU 3517  N   LEU A 460     4260   4088   3607   -728    499    271       N  
ATOM   3518  CA  LEU A 460      10.173   9.997   2.265  1.00 27.54           C  
ANISOU 3518  CA  LEU A 460     3784   3495   3184   -790    511    328       C  
ATOM   3519  C   LEU A 460      11.429   9.157   2.110  1.00 27.37           C  
ANISOU 3519  C   LEU A 460     3793   3434   3174   -797    497    361       C  
ATOM   3520  O   LEU A 460      11.359   7.958   1.805  1.00 33.62           O  
ANISOU 3520  O   LEU A 460     4599   4188   3989   -827    516    439       O  
ATOM   3521  CB  LEU A 460       9.934  10.834   1.008  1.00 29.52           C  
ANISOU 3521  CB  LEU A 460     4043   3665   3508   -823    489    271       C  
ATOM   3522  CG  LEU A 460      10.188  10.122  -0.323  1.00 34.20           C  
ANISOU 3522  CG  LEU A 460     4664   4157   4175   -877    486    306       C  
ATOM   3523  CD1 LEU A 460       9.155   9.027  -0.528  1.00 29.01           C  
ANISOU 3523  CD1 LEU A 460     4000   3487   3534   -912    521    385       C  
ATOM   3524  CD2 LEU A 460      10.172  11.113  -1.473  1.00 25.84           C  
ANISOU 3524  CD2 LEU A 460     3614   3031   3175   -897    461    244       C  
ATOM   3525  N   CYS A 461      12.585   9.777   2.356  1.00 27.32           N  
ANISOU 3525  N   CYS A 461     3792   3435   3152   -769    460    301       N  
ATOM   3526  CA  CYS A 461      13.872   9.118   2.157  1.00 27.16           C  
ANISOU 3526  CA  CYS A 461     3796   3380   3145   -771    442    321       C  
ATOM   3527  C   CYS A 461      14.082   7.984   3.163  1.00 30.88           C  
ANISOU 3527  C   CYS A 461     4269   3908   3555   -742    463    398       C  
ATOM   3528  O   CYS A 461      14.534   6.894   2.805  1.00 32.96           O  
ANISOU 3528  O   CYS A 461     4555   4125   3843   -759    468    459       O  
ATOM   3529  CB  CYS A 461      15.004  10.142   2.271  1.00 27.09           C  
ANISOU 3529  CB  CYS A 461     3782   3376   3135   -747    396    237       C  
ATOM   3530  SG  CYS A 461      15.065  11.359   0.928  1.00 31.99           S  
ANISOU 3530  SG  CYS A 461     4405   3909   3842   -787    368    164       S  
ATOM   3531  N   VAL A 462      13.843   8.251   4.446  1.00 34.43           N  
ANISOU 3531  N   VAL A 462     4696   4462   3923   -692    470    394       N  
ATOM   3532  CA  VAL A 462      14.043   7.239   5.478  1.00 29.00           C  
ANISOU 3532  CA  VAL A 462     4010   3840   3170   -658    491    472       C  
ATOM   3533  C   VAL A 462      13.013   6.126   5.344  1.00 35.39           C  
ANISOU 3533  C   VAL A 462     4819   4630   3996   -694    539    579       C  
ATOM   3534  O   VAL A 462      13.323   4.960   5.587  1.00 35.11           O  
ANISOU 3534  O   VAL A 462     4800   4585   3955   -695    552    664       O  
ATOM   3535  CB  VAL A 462      14.017   7.886   6.882  1.00 43.81           C  
ANISOU 3535  CB  VAL A 462     5858   5843   4943   -588    486    435       C  
ATOM   3536  CG1 VAL A 462      15.117   8.928   7.010  1.00 32.84           C  
ANISOU 3536  CG1 VAL A 462     4467   4461   3548   -557    429    328       C  
ATOM   3537  CG2 VAL A 462      12.654   8.485   7.201  1.00 41.08           C  
ANISOU 3537  CG2 VAL A 462     5483   5555   4571   -580    515    423       C  
ATOM   3538  N   LEU A 463      11.770   6.461   4.975  1.00 29.54           N  
ANISOU 3538  N   LEU A 463     4059   3883   3281   -724    563    578       N  
ATOM   3539  CA  LEU A 463      10.765   5.419   4.780  1.00 29.36           C  
ANISOU 3539  CA  LEU A 463     4030   3835   3288   -767    604    677       C  
ATOM   3540  C   LEU A 463      11.082   4.573   3.551  1.00 41.67           C  
ANISOU 3540  C   LEU A 463     5625   5268   4940   -823    591    706       C  
ATOM   3541  O   LEU A 463      10.841   3.360   3.540  1.00 38.64           O  
ANISOU 3541  O   LEU A 463     5251   4850   4581   -849    610    798       O  
ATOM   3542  CB  LEU A 463       9.377   6.045   4.671  1.00 29.42           C  
ANISOU 3542  CB  LEU A 463     4003   3874   3302   -783    629    661       C  
ATOM   3543  CG  LEU A 463       8.820   6.696   5.940  1.00 34.62           C  
ANISOU 3543  CG  LEU A 463     4621   4669   3864   -724    652    648       C  
ATOM   3544  CD1 LEU A 463       7.452   7.304   5.667  1.00 30.15           C  
ANISOU 3544  CD1 LEU A 463     4018   4123   3315   -741    675    628       C  
ATOM   3545  CD2 LEU A 463       8.752   5.695   7.086  1.00 36.62           C  
ANISOU 3545  CD2 LEU A 463     4862   5005   4048   -698    690    755       C  
ATOM   3546  N   HIS A 464      11.636   5.195   2.509  1.00 33.19           N  
ANISOU 3546  N   HIS A 464     4569   4123   3917   -839    556    628       N  
ATOM   3547  CA  HIS A 464      12.036   4.446   1.324  1.00 30.73           C  
ANISOU 3547  CA  HIS A 464     4291   3702   3682   -879    541    645       C  
ATOM   3548  C   HIS A 464      13.320   3.661   1.558  1.00 44.92           C  
ANISOU 3548  C   HIS A 464     6116   5483   5467   -854    524    672       C  
ATOM   3549  O   HIS A 464      13.501   2.592   0.966  1.00 39.53           O  
ANISOU 3549  O   HIS A 464     5461   4725   4832   -877    521    721       O  
ATOM   3550  CB  HIS A 464      12.199   5.397   0.136  1.00 27.37           C  
ANISOU 3550  CB  HIS A 464     3873   3218   3307   -899    514    559       C  
ATOM   3551  CG  HIS A 464      12.690   4.735  -1.114  1.00 33.88           C  
ANISOU 3551  CG  HIS A 464     4731   3943   4199   -929    497    565       C  
ATOM   3552  ND1 HIS A 464      14.029   4.632  -1.424  1.00 39.90           N  
ANISOU 3552  ND1 HIS A 464     5515   4679   4966   -910    472    542       N  
ATOM   3553  CD2 HIS A 464      12.021   4.159  -2.141  1.00 35.68           C  
ANISOU 3553  CD2 HIS A 464     4972   4096   4490   -972    499    586       C  
ATOM   3554  CE1 HIS A 464      14.164   4.014  -2.583  1.00 38.47           C  
ANISOU 3554  CE1 HIS A 464     5360   4414   4842   -936    462    549       C  
ATOM   3555  NE2 HIS A 464      12.961   3.716  -3.040  1.00 35.37           N  
ANISOU 3555  NE2 HIS A 464     4964   3988   4485   -973    475    573       N  
ATOM   3556  N   GLU A 465      14.208   4.163   2.421  1.00 27.98           N  
ANISOU 3556  N   GLU A 465     3964   3408   3258   -803    509    639       N  
ATOM   3557  CA  GLU A 465      15.470   3.474   2.674  1.00 35.06           C  
ANISOU 3557  CA  GLU A 465     4882   4298   4140   -773    490    661       C  
ATOM   3558  C   GLU A 465      15.255   2.126   3.353  1.00 38.56           C  
ANISOU 3558  C   GLU A 465     5337   4750   4564   -765    514    771       C  
ATOM   3559  O   GLU A 465      16.076   1.216   3.194  1.00 45.30           O  
ANISOU 3559  O   GLU A 465     6218   5559   5435   -755    500    807       O  
ATOM   3560  CB  GLU A 465      16.386   4.361   3.520  1.00 49.50           C  
ANISOU 3560  CB  GLU A 465     6695   6209   5904   -719    464    598       C  
ATOM   3561  CG  GLU A 465      17.771   3.785   3.761  1.00 64.04           C  
ANISOU 3561  CG  GLU A 465     8551   8051   7729   -684    439    609       C  
ATOM   3562  CD  GLU A 465      18.582   4.607   4.743  1.00 69.36           C  
ANISOU 3562  CD  GLU A 465     9203   8815   8334   -630    411    550       C  
ATOM   3563  OE1 GLU A 465      18.247   5.793   4.947  1.00 70.55           O  
ANISOU 3563  OE1 GLU A 465     9330   9006   8469   -625    401    477       O  
ATOM   3564  OE2 GLU A 465      19.553   4.066   5.312  1.00 69.32           O  
ANISOU 3564  OE2 GLU A 465     9204   8841   8293   -589    395    572       O  
ATOM   3565  N   LYS A 466      14.164   1.975   4.108  1.00 36.11           N  
ANISOU 3565  N   LYS A 466     5003   4496   4219   -769    550    828       N  
ATOM   3566  CA  LYS A 466      13.877   0.686   4.728  1.00 44.59           C  
ANISOU 3566  CA  LYS A 466     6085   5573   5283   -769    576    946       C  
ATOM   3567  C   LYS A 466      13.610  -0.390   3.683  1.00 45.33           C  
ANISOU 3567  C   LYS A 466     6207   5541   5473   -825    573    995       C  
ATOM   3568  O   LYS A 466      13.965  -1.556   3.891  1.00 49.59           O  
ANISOU 3568  O   LYS A 466     6772   6043   6028   -820    572   1074       O  
ATOM   3569  CB  LYS A 466      12.686   0.808   5.679  1.00 41.80           C  
ANISOU 3569  CB  LYS A 466     5692   5312   4876   -766    621   1001       C  
ATOM   3570  CG  LYS A 466      12.391  -0.465   6.457  1.00 31.72           C  
ANISOU 3570  CG  LYS A 466     4418   4052   3583   -765    653   1136       C  
ATOM   3571  CD  LYS A 466      11.098  -0.353   7.243  1.00 42.88           C  
ANISOU 3571  CD  LYS A 466     5785   5556   4953   -771    704   1198       C  
ATOM   3572  CE  LYS A 466      10.615  -1.725   7.690  1.00 52.05           C  
ANISOU 3572  CE  LYS A 466     6945   6700   6133   -796    737   1347       C  
ATOM   3573  NZ  LYS A 466       9.158  -1.728   7.983  1.00 58.17           N  
ANISOU 3573  NZ  LYS A 466     7670   7525   6909   -831    788   1411       N  
ATOM   3574  N   THR A 467      12.997  -0.023   2.560  1.00 47.26           N  
ANISOU 3574  N   THR A 467     6451   5720   5786   -873    567    947       N  
ATOM   3575  CA  THR A 467      12.700  -0.970   1.484  1.00 41.83           C  
ANISOU 3575  CA  THR A 467     5790   4913   5191   -923    557    978       C  
ATOM   3576  C   THR A 467      12.848  -0.254   0.151  1.00 38.80           C  
ANISOU 3576  C   THR A 467     5417   4470   4856   -944    530    881       C  
ATOM   3577  O   THR A 467      11.859   0.140  -0.480  1.00 42.21           O  
ANISOU 3577  O   THR A 467     5833   4881   5326   -984    536    858       O  
ATOM   3578  CB  THR A 467      11.295  -1.556   1.634  1.00 46.67           C  
ANISOU 3578  CB  THR A 467     6380   5515   5838   -973    588   1058       C  
ATOM   3579  OG1 THR A 467      11.099  -1.997   2.984  1.00 49.48           O  
ANISOU 3579  OG1 THR A 467     6716   5951   6133   -949    621   1150       O  
ATOM   3580  CG2 THR A 467      11.104  -2.729   0.690  1.00 47.27           C  
ANISOU 3580  CG2 THR A 467     6486   5462   6011  -1019    569   1096       C  
ATOM   3581  N   PRO A 468      14.083  -0.067  -0.314  1.00 38.38           N  
ANISOU 3581  N   PRO A 468     5387   4393   4802   -915    500    826       N  
ATOM   3582  CA  PRO A 468      14.298   0.709  -1.545  1.00 37.97           C  
ANISOU 3582  CA  PRO A 468     5341   4299   4787   -929    479    740       C  
ATOM   3583  C   PRO A 468      13.704   0.006  -2.757  1.00 44.14           C  
ANISOU 3583  C   PRO A 468     6144   4980   5647   -972    469    748       C  
ATOM   3584  O   PRO A 468      13.869  -1.201  -2.942  1.00 56.61           O  
ANISOU 3584  O   PRO A 468     7751   6496   7263   -977    459    797       O  
ATOM   3585  CB  PRO A 468      15.825   0.819  -1.639  1.00 35.36           C  
ANISOU 3585  CB  PRO A 468     5026   3971   4437   -886    453    702       C  
ATOM   3586  CG  PRO A 468      16.358  -0.268  -0.777  1.00 44.94           C  
ANISOU 3586  CG  PRO A 468     6256   5195   5626   -856    454    774       C  
ATOM   3587  CD  PRO A 468      15.343  -0.529   0.291  1.00 46.39           C  
ANISOU 3587  CD  PRO A 468     6419   5428   5777   -865    486    845       C  
ATOM   3588  N   VAL A 469      12.999   0.778  -3.581  1.00 39.10           N  
ANISOU 3588  N   VAL A 469     5492   4327   5036  -1002    467    697       N  
ATOM   3589  CA  VAL A 469      12.273   0.232  -4.722  1.00 43.93           C  
ANISOU 3589  CA  VAL A 469     6119   4855   5718  -1042    455    697       C  
ATOM   3590  C   VAL A 469      12.483   1.109  -5.948  1.00 51.18           C  
ANISOU 3590  C   VAL A 469     7043   5751   6654  -1043    437    616       C  
ATOM   3591  O   VAL A 469      12.183   0.699  -7.075  1.00 45.34           O  
ANISOU 3591  O   VAL A 469     6321   4942   5964  -1063    418    599       O  
ATOM   3592  CB  VAL A 469      10.773   0.098  -4.406  1.00 44.52           C  
ANISOU 3592  CB  VAL A 469     6164   4940   5813  -1085    477    740       C  
ATOM   3593  CG1 VAL A 469      10.526  -1.059  -3.447  1.00 41.20           C  
ANISOU 3593  CG1 VAL A 469     5742   4518   5394  -1093    494    837       C  
ATOM   3594  CG2 VAL A 469      10.241   1.404  -3.832  1.00 44.89           C  
ANISOU 3594  CG2 VAL A 469     6171   5075   5811  -1078    500    708       C  
ATOM   3595  N   SER A 470      12.992   2.322  -5.743  1.00 42.96           N  
ANISOU 3595  N   SER A 470     5985   4767   5572  -1021    440    567       N  
ATOM   3596  CA  SER A 470      13.109   3.296  -6.822  1.00 38.58           C  
ANISOU 3596  CA  SER A 470     5429   4197   5032  -1025    427    501       C  
ATOM   3597  C   SER A 470      14.487   3.935  -6.775  1.00 50.43           C  
ANISOU 3597  C   SER A 470     6930   5725   6504   -991    417    464       C  
ATOM   3598  O   SER A 470      14.826   4.612  -5.799  1.00 43.60           O  
ANISOU 3598  O   SER A 470     6044   4921   5599   -972    422    453       O  
ATOM   3599  CB  SER A 470      12.016   4.364  -6.715  1.00 40.87           C  
ANISOU 3599  CB  SER A 470     5688   4521   5318  -1044    439    476       C  
ATOM   3600  OG  SER A 470      12.428   5.584  -7.303  1.00 37.50           O  
ANISOU 3600  OG  SER A 470     5256   4103   4890  -1035    429    416       O  
ATOM   3601  N   ASP A 471      15.275   3.724  -7.833  1.00 39.35           N  
ANISOU 3601  N   ASP A 471     5548   4280   5123   -981    401    442       N  
ATOM   3602  CA  ASP A 471      16.593   4.340  -7.916  1.00 40.99           C  
ANISOU 3602  CA  ASP A 471     5749   4514   5312   -953    392    410       C  
ATOM   3603  C   ASP A 471      16.515   5.855  -8.027  1.00 31.93           C  
ANISOU 3603  C   ASP A 471     4575   3396   4161   -963    392    364       C  
ATOM   3604  O   ASP A 471      17.512   6.534  -7.758  1.00 34.26           O  
ANISOU 3604  O   ASP A 471     4853   3722   4441   -946    385    340       O  
ATOM   3605  CB  ASP A 471      17.370   3.778  -9.108  1.00 60.40           C  
ANISOU 3605  CB  ASP A 471     8230   6927   7791   -938    379    400       C  
ATOM   3606  CG  ASP A 471      17.565   2.278  -9.022  1.00 67.81           C  
ANISOU 3606  CG  ASP A 471     9199   7827   8739   -921    372    438       C  
ATOM   3607  OD1 ASP A 471      17.059   1.666  -8.058  1.00 71.66           O  
ANISOU 3607  OD1 ASP A 471     9689   8318   9221   -928    378    481       O  
ATOM   3608  OD2 ASP A 471      18.227   1.713  -9.917  1.00 70.68           O  
ANISOU 3608  OD2 ASP A 471     9583   8157   9116   -899    359    426       O  
ATOM   3609  N   ARG A 472      15.361   6.397  -8.421  1.00 26.98           N  
ANISOU 3609  N   ARG A 472     3942   2758   3553   -989    398    351       N  
ATOM   3610  CA  ARG A 472      15.213   7.847  -8.478  1.00 34.57           C  
ANISOU 3610  CA  ARG A 472     4880   3740   4514   -996    395    309       C  
ATOM   3611  C   ARG A 472      15.136   8.445  -7.078  1.00 36.46           C  
ANISOU 3611  C   ARG A 472     5095   4038   4718   -983    397    299       C  
ATOM   3612  O   ARG A 472      15.728   9.499  -6.816  1.00 30.86           O  
ANISOU 3612  O   ARG A 472     4369   3352   4005   -974    384    260       O  
ATOM   3613  CB  ARG A 472      13.977   8.216  -9.299  1.00 27.82           C  
ANISOU 3613  CB  ARG A 472     4027   2857   3687  -1020    397    299       C  
ATOM   3614  CG  ARG A 472      14.184   8.110 -10.803  1.00 33.31           C  
ANISOU 3614  CG  ARG A 472     4741   3506   4411  -1025    389    290       C  
ATOM   3615  CD  ARG A 472      12.916   7.661 -11.516  1.00 27.87           C  
ANISOU 3615  CD  ARG A 472     4061   2782   3744  -1046    388    297       C  
ATOM   3616  NE  ARG A 472      11.887   8.698 -11.523  1.00 29.02           N  
ANISOU 3616  NE  ARG A 472     4187   2940   3897  -1059    390    276       N  
ATOM   3617  CZ  ARG A 472      11.886   9.747 -12.340  1.00 30.36           C  
ANISOU 3617  CZ  ARG A 472     4354   3102   4080  -1059    383    249       C  
ATOM   3618  NH1 ARG A 472      12.861   9.903 -13.223  1.00 28.27           N  
ANISOU 3618  NH1 ARG A 472     4101   2822   3820  -1048    378    244       N  
ATOM   3619  NH2 ARG A 472      10.907  10.640 -12.275  1.00 30.43           N  
ANISOU 3619  NH2 ARG A 472     4345   3120   4097  -1067    383    230       N  
ATOM   3620  N   VAL A 473      14.412   7.788  -6.166  1.00 29.87           N  
ANISOU 3620  N   VAL A 473     4258   3230   3860   -981    412    333       N  
ATOM   3621  CA  VAL A 473      14.404   8.225  -4.771  1.00 26.11           C  
ANISOU 3621  CA  VAL A 473     3761   2824   3337   -957    415    325       C  
ATOM   3622  C   VAL A 473      15.799   8.097  -4.177  1.00 35.98           C  
ANISOU 3622  C   VAL A 473     5010   4101   4560   -927    401    321       C  
ATOM   3623  O   VAL A 473      16.304   9.017  -3.524  1.00 28.92           O  
ANISOU 3623  O   VAL A 473     4095   3249   3643   -908    385    278       O  
ATOM   3624  CB  VAL A 473      13.378   7.418  -3.954  1.00 34.85           C  
ANISOU 3624  CB  VAL A 473     4862   3961   4420   -960    440    378       C  
ATOM   3625  CG1 VAL A 473      13.467   7.792  -2.481  1.00 31.04           C  
ANISOU 3625  CG1 VAL A 473     4357   3563   3874   -924    445    373       C  
ATOM   3626  CG2 VAL A 473      11.978   7.645  -4.471  1.00 30.33           C  
ANISOU 3626  CG2 VAL A 473     4279   3370   3874   -989    452    378       C  
ATOM   3627  N   THR A 474      16.441   6.948  -4.403  1.00 31.09           N  
ANISOU 3627  N   THR A 474     4412   3456   3944   -921    401    361       N  
ATOM   3628  CA  THR A 474      17.759   6.694  -3.832  1.00 34.24           C  
ANISOU 3628  CA  THR A 474     4809   3885   4317   -889    387    362       C  
ATOM   3629  C   THR A 474      18.769   7.747  -4.272  1.00 37.76           C  
ANISOU 3629  C   THR A 474     5237   4331   4779   -886    365    307       C  
ATOM   3630  O   THR A 474      19.583   8.210  -3.466  1.00 40.64           O  
ANISOU 3630  O   THR A 474     5582   4743   5117   -863    347    282       O  
ATOM   3631  CB  THR A 474      18.235   5.295  -4.225  1.00 34.14           C  
ANISOU 3631  CB  THR A 474     4824   3832   4316   -881    389    411       C  
ATOM   3632  OG1 THR A 474      17.369   4.313  -3.641  1.00 39.80           O  
ANISOU 3632  OG1 THR A 474     5554   4547   5021   -885    407    470       O  
ATOM   3633  CG2 THR A 474      19.659   5.055  -3.750  1.00 35.65           C  
ANISOU 3633  CG2 THR A 474     5011   4053   4482   -843    373    409       C  
ATOM   3634  N   LYS A 475      18.722   8.150  -5.544  1.00 30.32           N  
ANISOU 3634  N   LYS A 475     4299   3339   3881   -911    364    290       N  
ATOM   3635  CA  LYS A 475      19.682   9.130  -6.040  1.00 28.35           C  
ANISOU 3635  CA  LYS A 475     4029   3087   3655   -915    347    250       C  
ATOM   3636  C   LYS A 475      19.445  10.502  -5.421  1.00 24.44           C  
ANISOU 3636  C   LYS A 475     3507   2617   3160   -920    331    201       C  
ATOM   3637  O   LYS A 475      20.392  11.176  -5.000  1.00 30.64           O  
ANISOU 3637  O   LYS A 475     4268   3427   3946   -911    307    169       O  
ATOM   3638  CB  LYS A 475      19.613   9.214  -7.566  1.00 28.86           C  
ANISOU 3638  CB  LYS A 475     4105   3098   3762   -937    354    253       C  
ATOM   3639  CG  LYS A 475      20.406  10.375  -8.151  1.00 35.15           C  
ANISOU 3639  CG  LYS A 475     4876   3890   4589   -949    341    223       C  
ATOM   3640  CD  LYS A 475      20.462  10.311  -9.667  1.00 45.47           C  
ANISOU 3640  CD  LYS A 475     6194   5157   5925   -961    352    236       C  
ATOM   3641  CE  LYS A 475      21.323  11.429 -10.232  1.00 52.20           C  
ANISOU 3641  CE  LYS A 475     7016   6009   6810   -975    344    221       C  
ATOM   3642  NZ  LYS A 475      20.693  12.764 -10.042  1.00 56.85           N  
ANISOU 3642  NZ  LYS A 475     7591   6585   7424   -998    332    191       N  
ATOM   3643  N   CYS A 476      18.185  10.941  -5.365  1.00 29.42           N  
ANISOU 3643  N   CYS A 476     4142   3244   3793   -933    340    192       N  
ATOM   3644  CA  CYS A 476      17.898  12.264  -4.817  1.00 35.88           C  
ANISOU 3644  CA  CYS A 476     4938   4081   4613   -931    321    138       C  
ATOM   3645  C   CYS A 476      18.107  12.308  -3.308  1.00 32.22           C  
ANISOU 3645  C   CYS A 476     4460   3687   4097   -896    308    118       C  
ATOM   3646  O   CYS A 476      18.438  13.366  -2.758  1.00 28.88           O  
ANISOU 3646  O   CYS A 476     4015   3283   3674   -885    279     62       O  
ATOM   3647  CB  CYS A 476      16.469  12.682  -5.163  1.00 41.20           C  
ANISOU 3647  CB  CYS A 476     5617   4736   5300   -946    334    132       C  
ATOM   3648  SG  CYS A 476      16.250  13.273  -6.858  1.00 58.14           S  
ANISOU 3648  SG  CYS A 476     7772   6809   7508   -980    334    131       S  
ATOM   3649  N   CYS A 477      17.930  11.169  -2.630  1.00 25.87           N  
ANISOU 3649  N   CYS A 477     3667   2919   3246   -875    327    164       N  
ATOM   3650  CA  CYS A 477      18.068  11.101  -1.180  1.00 29.58           C  
ANISOU 3650  CA  CYS A 477     4123   3465   3653   -835    320    155       C  
ATOM   3651  C   CYS A 477      19.519  10.957  -0.733  1.00 42.58           C  
ANISOU 3651  C   CYS A 477     5758   5136   5283   -811    293    144       C  
ATOM   3652  O   CYS A 477      19.814  11.211   0.440  1.00 39.71           O  
ANISOU 3652  O   CYS A 477     5380   4840   4870   -774    274    116       O  
ATOM   3653  CB  CYS A 477      17.247   9.932  -0.615  1.00 32.02           C  
ANISOU 3653  CB  CYS A 477     4445   3803   3918   -824    354    222       C  
ATOM   3654  SG  CYS A 477      15.440  10.175  -0.673  1.00 32.35           S  
ANISOU 3654  SG  CYS A 477     4483   3848   3960   -841    384    231       S  
ATOM   3655  N   THR A 478      20.417  10.515  -1.622  1.00 34.24           N  
ANISOU 3655  N   THR A 478     4709   4037   4265   -827    291    164       N  
ATOM   3656  CA  THR A 478      21.820  10.323  -1.293  1.00 33.69           C  
ANISOU 3656  CA  THR A 478     4623   3992   4184   -805    267    157       C  
ATOM   3657  C   THR A 478      22.764  11.238  -2.060  1.00 35.39           C  
ANISOU 3657  C   THR A 478     4815   4176   4457   -829    242    116       C  
ATOM   3658  O   THR A 478      23.973  11.190  -1.811  1.00 48.66           O  
ANISOU 3658  O   THR A 478     6472   5880   6135   -813    219    106       O  
ATOM   3659  CB  THR A 478      22.217   8.866  -1.550  1.00 33.59           C  
ANISOU 3659  CB  THR A 478     4635   3968   4160   -792    286    222       C  
ATOM   3660  OG1 THR A 478      22.124   8.586  -2.952  1.00 33.69           O  
ANISOU 3660  OG1 THR A 478     4664   3912   4224   -823    303    242       O  
ATOM   3661  CG2 THR A 478      21.307   7.914  -0.782  1.00 33.66           C  
ANISOU 3661  CG2 THR A 478     4666   4002   4121   -774    311    275       C  
ATOM   3662  N   GLU A 479      22.261  12.058  -2.984  1.00 27.80           N  
ANISOU 3662  N   GLU A 479     3852   3163   3546   -865    246     99       N  
ATOM   3663  CA  GLU A 479      23.124  12.950  -3.747  1.00 46.52           C  
ANISOU 3663  CA  GLU A 479     6197   5502   5976   -892    226     73       C  
ATOM   3664  C   GLU A 479      23.803  13.940  -2.813  1.00 61.30           C  
ANISOU 3664  C   GLU A 479     8033   7408   7851   -883    180     12       C  
ATOM   3665  O   GLU A 479      25.014  13.860  -2.587  1.00 69.66           O  
ANISOU 3665  O   GLU A 479     9064   8490   8914   -874    158      5       O  
ATOM   3666  CB  GLU A 479      22.327  13.688  -4.823  1.00 56.73           C  
ANISOU 3666  CB  GLU A 479     7499   6737   7319   -929    238     70       C  
ATOM   3667  CG  GLU A 479      23.175  14.609  -5.689  1.00 70.84           C  
ANISOU 3667  CG  GLU A 479     9258   8488   9170   -961    223     59       C  
ATOM   3668  CD  GLU A 479      22.809  14.537  -7.159  1.00 81.01           C  
ANISOU 3668  CD  GLU A 479    10563   9726  10490   -987    252     97       C  
ATOM   3669  OE1 GLU A 479      21.916  13.739  -7.511  1.00 84.53           O  
ANISOU 3669  OE1 GLU A 479    11043  10163  10913   -980    279    125       O  
ATOM   3670  OE2 GLU A 479      23.416  15.277  -7.962  1.00 86.94           O  
ANISOU 3670  OE2 GLU A 479    11291  10450  11291  -1013    247    100       O  
ATOM   3671  N   SER A 480      23.028  14.868  -2.260  1.00 57.04           N  
ANISOU 3671  N   SER A 480     7491   6870   7311   -881    162    -37       N  
ATOM   3672  CA  SER A 480      23.546  15.822  -1.293  1.00 45.12           C  
ANISOU 3672  CA  SER A 480     5951   5390   5803   -866    111   -108       C  
ATOM   3673  C   SER A 480      22.369  16.387  -0.515  1.00 34.90           C  
ANISOU 3673  C   SER A 480     4667   4116   4475   -843    104   -152       C  
ATOM   3674  O   SER A 480      21.295  16.606  -1.082  1.00 39.50           O  
ANISOU 3674  O   SER A 480     5270   4663   5074   -859    128   -140       O  
ATOM   3675  CB  SER A 480      24.336  16.947  -1.972  1.00 58.96           C  
ANISOU 3675  CB  SER A 480     7671   7090   7641   -908     79   -138       C  
ATOM   3676  OG  SER A 480      23.520  18.081  -2.202  1.00 58.72           O  
ANISOU 3676  OG  SER A 480     7646   7013   7654   -927     65   -176       O  
ATOM   3677  N   LEU A 481      22.576  16.612   0.784  1.00 32.15           N  
ANISOU 3677  N   LEU A 481     4305   3834   4077   -799     69   -203       N  
ATOM   3678  CA  LEU A 481      21.481  17.064   1.637  1.00 36.56           C  
ANISOU 3678  CA  LEU A 481     4872   4431   4590   -764     65   -247       C  
ATOM   3679  C   LEU A 481      20.933  18.409   1.177  1.00 36.93           C  
ANISOU 3679  C   LEU A 481     4915   4416   4702   -787     40   -303       C  
ATOM   3680  O   LEU A 481      19.718  18.638   1.223  1.00 43.44           O  
ANISOU 3680  O   LEU A 481     5755   5243   5509   -775     59   -310       O  
ATOM   3681  CB  LEU A 481      21.946  17.141   3.091  1.00 41.31           C  
ANISOU 3681  CB  LEU A 481     5455   5118   5122   -706     25   -300       C  
ATOM   3682  CG  LEU A 481      20.850  17.147   4.159  1.00 52.60           C  
ANISOU 3682  CG  LEU A 481     6894   6624   6467   -650     36   -323       C  
ATOM   3683  CD1 LEU A 481      21.291  16.355   5.375  1.00 53.82           C  
ANISOU 3683  CD1 LEU A 481     7043   6881   6526   -592     32   -311       C  
ATOM   3684  CD2 LEU A 481      20.483  18.569   4.554  1.00 67.38           C  
ANISOU 3684  CD2 LEU A 481     8753   8487   8360   -632    -14   -426       C  
ATOM   3685  N   VAL A 482      21.807  19.312   0.726  1.00 40.17           N  
ANISOU 3685  N   VAL A 482     5302   4769   5191   -820     -3   -340       N  
ATOM   3686  CA  VAL A 482      21.336  20.642   0.349  1.00 50.09           C  
ANISOU 3686  CA  VAL A 482     6555   5959   6516   -841    -33   -393       C  
ATOM   3687  C   VAL A 482      20.649  20.623  -1.015  1.00 48.44           C  
ANISOU 3687  C   VAL A 482     6368   5682   6356   -884     10   -334       C  
ATOM   3688  O   VAL A 482      19.756  21.440  -1.271  1.00 61.18           O  
ANISOU 3688  O   VAL A 482     7992   7256   7999   -886      4   -362       O  
ATOM   3689  CB  VAL A 482      22.488  21.665   0.386  1.00 54.58           C  
ANISOU 3689  CB  VAL A 482     7090   6486   7161   -865    -98   -451       C  
ATOM   3690  CG1 VAL A 482      23.282  21.531   1.678  1.00 56.46           C  
ANISOU 3690  CG1 VAL A 482     7305   6800   7348   -821   -143   -507       C  
ATOM   3691  CG2 VAL A 482      23.398  21.521  -0.826  1.00 61.36           C  
ANISOU 3691  CG2 VAL A 482     7934   7288   8093   -925    -82   -388       C  
ATOM   3692  N   ASN A 483      21.030  19.705  -1.903  1.00 35.96           N  
ANISOU 3692  N   ASN A 483     4795   4088   4781   -912     52   -256       N  
ATOM   3693  CA  ASN A 483      20.405  19.590  -3.214  1.00 34.76           C  
ANISOU 3693  CA  ASN A 483     4664   3879   4665   -947     92   -201       C  
ATOM   3694  C   ASN A 483      19.284  18.560  -3.241  1.00 41.49           C  
ANISOU 3694  C   ASN A 483     5545   4763   5457   -929    141   -156       C  
ATOM   3695  O   ASN A 483      18.841  18.173  -4.328  1.00 30.99           O  
ANISOU 3695  O   ASN A 483     4234   3396   4147   -954    175   -105       O  
ATOM   3696  CB  ASN A 483      21.454  19.239  -4.273  1.00 42.57           C  
ANISOU 3696  CB  ASN A 483     5642   4836   5697   -985    106   -146       C  
ATOM   3697  CG  ASN A 483      22.484  20.334  -4.456  1.00 43.02           C  
ANISOU 3697  CG  ASN A 483     5662   4851   5831  -1016     62   -176       C  
ATOM   3698  OD1 ASN A 483      22.197  21.512  -4.249  1.00 43.83           O  
ANISOU 3698  OD1 ASN A 483     5758   4916   5979  -1023     23   -229       O  
ATOM   3699  ND2 ASN A 483      23.694  19.949  -4.845  1.00 42.11           N  
ANISOU 3699  ND2 ASN A 483     5523   4743   5735  -1035     66   -142       N  
ATOM   3700  N   ARG A 484      18.819  18.112  -2.073  1.00 34.69           N  
ANISOU 3700  N   ARG A 484     4686   3971   4523   -886    145   -172       N  
ATOM   3701  CA  ARG A 484      17.749  17.122  -2.026  1.00 30.40           C  
ANISOU 3701  CA  ARG A 484     4164   3457   3928   -874    192   -123       C  
ATOM   3702  C   ARG A 484      16.468  17.668  -2.646  1.00 30.55           C  
ANISOU 3702  C   ARG A 484     4194   3441   3974   -886    206   -128       C  
ATOM   3703  O   ARG A 484      15.895  17.058  -3.556  1.00 31.26           O  
ANISOU 3703  O   ARG A 484     4301   3502   4076   -910    240    -75       O  
ATOM   3704  CB  ARG A 484      17.508  16.688  -0.580  1.00 42.36           C  
ANISOU 3704  CB  ARG A 484     5673   5061   5360   -823    193   -137       C  
ATOM   3705  CG  ARG A 484      16.812  15.350  -0.436  1.00 39.38           C  
ANISOU 3705  CG  ARG A 484     5312   4720   4931   -816    242    -64       C  
ATOM   3706  CD  ARG A 484      16.753  14.928   1.022  1.00 43.54           C  
ANISOU 3706  CD  ARG A 484     5829   5342   5372   -764    244    -67       C  
ATOM   3707  NE  ARG A 484      17.698  13.857   1.321  1.00 34.34           N  
ANISOU 3707  NE  ARG A 484     4669   4201   4177   -755    250    -20       N  
ATOM   3708  CZ  ARG A 484      17.749  13.211   2.481  1.00 35.33           C  
ANISOU 3708  CZ  ARG A 484     4790   4407   4225   -711    258      1       C  
ATOM   3709  NH1 ARG A 484      16.912  13.532   3.458  1.00 27.66           N  
ANISOU 3709  NH1 ARG A 484     3808   3508   3193   -671    263    -21       N  
ATOM   3710  NH2 ARG A 484      18.640  12.246   2.665  1.00 27.26           N  
ANISOU 3710  NH2 ARG A 484     3775   3399   3182   -702    260     47       N  
ATOM   3711  N   ARG A 485      16.009  18.825  -2.167  1.00 28.44           N  
ANISOU 3711  N   ARG A 485     3916   3174   3716   -866    175   -195       N  
ATOM   3712  CA  ARG A 485      14.776  19.410  -2.691  1.00 32.69           C  
ANISOU 3712  CA  ARG A 485     4461   3681   4277   -870    184   -205       C  
ATOM   3713  C   ARG A 485      14.871  19.768  -4.171  1.00 37.05           C  
ANISOU 3713  C   ARG A 485     5025   4149   4905   -916    187   -176       C  
ATOM   3714  O   ARG A 485      13.924  19.458  -4.915  1.00 35.94           O  
ANISOU 3714  O   ARG A 485     4897   3990   4767   -927    217   -140       O  
ATOM   3715  CB  ARG A 485      14.380  20.624  -1.842  1.00 28.26           C  
ANISOU 3715  CB  ARG A 485     3888   3136   3714   -830    144   -291       C  
ATOM   3716  CG  ARG A 485      12.910  21.008  -1.941  1.00 30.90           C  
ANISOU 3716  CG  ARG A 485     4224   3475   4040   -811    159   -304       C  
ATOM   3717  CD  ARG A 485      12.645  21.989  -3.077  1.00 35.28           C  
ANISOU 3717  CD  ARG A 485     4788   3939   4677   -840    141   -314       C  
ATOM   3718  NE  ARG A 485      13.623  23.071  -3.115  1.00 37.03           N  
ANISOU 3718  NE  ARG A 485     5005   4103   4962   -850     87   -365       N  
ATOM   3719  CZ  ARG A 485      14.005  23.694  -4.226  1.00 41.58           C  
ANISOU 3719  CZ  ARG A 485     5587   4592   5619   -892     73   -346       C  
ATOM   3720  NH1 ARG A 485      13.493  23.342  -5.398  1.00 32.31           N  
ANISOU 3720  NH1 ARG A 485     4427   3385   4463   -921    108   -284       N  
ATOM   3721  NH2 ARG A 485      14.901  24.670  -4.166  1.00 38.01           N  
ANISOU 3721  NH2 ARG A 485     5124   4088   5230   -906     22   -388       N  
ATOM   3722  N   PRO A 486      15.933  20.419  -4.664  1.00 41.61           N  
ANISOU 3722  N   PRO A 486     5594   4674   5541   -942    158   -186       N  
ATOM   3723  CA  PRO A 486      16.020  20.635  -6.118  1.00 37.87           C  
ANISOU 3723  CA  PRO A 486     5130   4131   5127   -982    169   -143       C  
ATOM   3724  C   PRO A 486      16.057  19.344  -6.916  1.00 32.71           C  
ANISOU 3724  C   PRO A 486     4493   3485   4451   -999    214    -71       C  
ATOM   3725  O   PRO A 486      15.543  19.310  -8.041  1.00 34.01           O  
ANISOU 3725  O   PRO A 486     4672   3613   4639  -1017    232    -37       O  
ATOM   3726  CB  PRO A 486      17.319  21.438  -6.277  1.00 35.63           C  
ANISOU 3726  CB  PRO A 486     4826   3807   4904  -1007    132   -160       C  
ATOM   3727  CG  PRO A 486      17.498  22.117  -4.973  1.00 36.91           C  
ANISOU 3727  CG  PRO A 486     4973   3996   5058   -977     87   -238       C  
ATOM   3728  CD  PRO A 486      17.004  21.139  -3.950  1.00 42.09           C  
ANISOU 3728  CD  PRO A 486     5635   4736   5624   -936    109   -241       C  
ATOM   3729  N   CYS A 487      16.647  18.279  -6.368  1.00 33.61           N  
ANISOU 3729  N   CYS A 487     4606   3646   4520   -988    227    -50       N  
ATOM   3730  CA  CYS A 487      16.658  16.998  -7.067  1.00 35.78           C  
ANISOU 3730  CA  CYS A 487     4898   3923   4776   -998    264     12       C  
ATOM   3731  C   CYS A 487      15.242  16.468  -7.259  1.00 37.80           C  
ANISOU 3731  C   CYS A 487     5170   4183   5008   -994    291     32       C  
ATOM   3732  O   CYS A 487      14.873  16.033  -8.356  1.00 30.29           O  
ANISOU 3732  O   CYS A 487     4235   3200   4073  -1012    309     67       O  
ATOM   3733  CB  CYS A 487      17.515  15.989  -6.303  1.00 36.31           C  
ANISOU 3733  CB  CYS A 487     4961   4036   4799   -981    268     28       C  
ATOM   3734  SG  CYS A 487      17.866  14.460  -7.206  1.00 37.61           S  
ANISOU 3734  SG  CYS A 487     5148   4190   4952   -989    302     96       S  
ATOM   3735  N   PHE A 488      14.431  16.494  -6.197  1.00 37.38           N  
ANISOU 3735  N   PHE A 488     5111   4175   4916   -970    292      9       N  
ATOM   3736  CA  PHE A 488      13.051  16.030  -6.312  1.00 33.26           C  
ANISOU 3736  CA  PHE A 488     4596   3665   4378   -969    318     29       C  
ATOM   3737  C   PHE A 488      12.223  16.967  -7.183  1.00 36.22           C  
ANISOU 3737  C   PHE A 488     4973   3996   4795   -979    310     11       C  
ATOM   3738  O   PHE A 488      11.333  16.518  -7.916  1.00 26.81           O  
ANISOU 3738  O   PHE A 488     3789   2789   3609   -992    329     39       O  
ATOM   3739  CB  PHE A 488      12.422  15.900  -4.925  1.00 29.55           C  
ANISOU 3739  CB  PHE A 488     4110   3265   3851   -936    324     13       C  
ATOM   3740  CG  PHE A 488      12.769  14.621  -4.216  1.00 30.98           C  
ANISOU 3740  CG  PHE A 488     4294   3491   3985   -927    345     58       C  
ATOM   3741  CD1 PHE A 488      12.171  13.426  -4.582  1.00 37.99           C  
ANISOU 3741  CD1 PHE A 488     5193   4373   4867   -945    376    118       C  
ATOM   3742  CD2 PHE A 488      13.686  14.615  -3.177  1.00 32.31           C  
ANISOU 3742  CD2 PHE A 488     4454   3705   4116   -900    330     40       C  
ATOM   3743  CE1 PHE A 488      12.486  12.247  -3.928  1.00 32.51           C  
ANISOU 3743  CE1 PHE A 488     4503   3711   4136   -937    393    166       C  
ATOM   3744  CE2 PHE A 488      14.004  13.441  -2.519  1.00 28.11           C  
ANISOU 3744  CE2 PHE A 488     3927   3215   3540   -888    348     87       C  
ATOM   3745  CZ  PHE A 488      13.404  12.256  -2.895  1.00 32.91           C  
ANISOU 3745  CZ  PHE A 488     4548   3811   4147   -907    381    153       C  
ATOM   3746  N   SER A 489      12.502  18.272  -7.114  1.00 35.85           N  
ANISOU 3746  N   SER A 489     4917   3926   4780   -973    279    -37       N  
ATOM   3747  CA  SER A 489      11.751  19.241  -7.905  1.00 32.59           C  
ANISOU 3747  CA  SER A 489     4507   3467   4409   -978    268    -53       C  
ATOM   3748  C   SER A 489      11.928  19.011  -9.400  1.00 35.60           C  
ANISOU 3748  C   SER A 489     4905   3797   4826  -1008    279     -7       C  
ATOM   3749  O   SER A 489      10.995  19.240 -10.177  1.00 31.11           O  
ANISOU 3749  O   SER A 489     4343   3206   4272  -1011    284      1       O  
ATOM   3750  CB  SER A 489      12.181  20.664  -7.539  1.00 37.98           C  
ANISOU 3750  CB  SER A 489     5180   4122   5130   -968    226   -111       C  
ATOM   3751  OG  SER A 489      11.756  21.014  -6.234  1.00 39.23           O  
ANISOU 3751  OG  SER A 489     5324   4330   5252   -929    211   -166       O  
ATOM   3752  N   ALA A 490      13.113  18.562  -9.822  1.00 28.02           N  
ANISOU 3752  N   ALA A 490     3949   2825   3873  -1026    283     22       N  
ATOM   3753  CA  ALA A 490      13.376  18.356 -11.241  1.00 35.68           C  
ANISOU 3753  CA  ALA A 490     4933   3757   4868  -1046    294     65       C  
ATOM   3754  C   ALA A 490      12.640  17.147 -11.801  1.00 44.07           C  
ANISOU 3754  C   ALA A 490     6011   4830   5902  -1047    320     98       C  
ATOM   3755  O   ALA A 490      12.455  17.060 -13.020  1.00 38.86           O  
ANISOU 3755  O   ALA A 490     5366   4144   5257  -1055    326    123       O  
ATOM   3756  CB  ALA A 490      14.878  18.203 -11.482  1.00 38.49           C  
ANISOU 3756  CB  ALA A 490     5282   4108   5235  -1059    293     85       C  
ATOM   3757  N   LEU A 491      12.228  16.214 -10.948  1.00 23.33           N  
ANISOU 3757  N   LEU A 491     3384   2242   3238  -1039    333    101       N  
ATOM   3758  CA  LEU A 491      11.498  15.046 -11.415  1.00 30.45           C  
ANISOU 3758  CA  LEU A 491     4300   3145   4125  -1045    351    132       C  
ATOM   3759  C   LEU A 491      10.112  15.447 -11.902  1.00 35.58           C  
ANISOU 3759  C   LEU A 491     4946   3784   4787  -1047    350    123       C  
ATOM   3760  O   LEU A 491       9.476  16.348 -11.350  1.00 34.46           O  
ANISOU 3760  O   LEU A 491     4789   3655   4649  -1035    342     92       O  
ATOM   3761  CB  LEU A 491      11.382  14.006 -10.300  1.00 31.57           C  
ANISOU 3761  CB  LEU A 491     4437   3328   4230  -1039    365    146       C  
ATOM   3762  CG  LEU A 491      12.682  13.420  -9.744  1.00 39.14           C  
ANISOU 3762  CG  LEU A 491     5399   4302   5170  -1032    366    158       C  
ATOM   3763  CD1 LEU A 491      12.386  12.266  -8.797  1.00 38.33           C  
ANISOU 3763  CD1 LEU A 491     5296   4234   5032  -1025    382    186       C  
ATOM   3764  CD2 LEU A 491      13.602  12.972 -10.871  1.00 44.44           C  
ANISOU 3764  CD2 LEU A 491     6088   4941   5858  -1038    366    180       C  
ATOM   3765  N   GLU A 492       9.651  14.776 -12.954  1.00 34.03           N  
ANISOU 3765  N   GLU A 492     4765   3567   4598  -1057    355    146       N  
ATOM   3766  CA  GLU A 492       8.310  15.008 -13.473  1.00 33.63           C  
ANISOU 3766  CA  GLU A 492     4709   3511   4559  -1058    351    139       C  
ATOM   3767  C   GLU A 492       7.535  13.699 -13.502  1.00 39.14           C  
ANISOU 3767  C   GLU A 492     5406   4216   5248  -1071    361    161       C  
ATOM   3768  O   GLU A 492       6.696  13.448 -12.630  1.00 29.43           O  
ANISOU 3768  O   GLU A 492     4155   3018   4008  -1074    371    162       O  
ATOM   3769  CB  GLU A 492       8.371  15.637 -14.868  1.00 45.45           C  
ANISOU 3769  CB  GLU A 492     6220   4972   6078  -1056    339    142       C  
ATOM   3770  CG  GLU A 492       7.013  16.010 -15.444  1.00 48.85           C  
ANISOU 3770  CG  GLU A 492     6644   5398   6521  -1052    330    131       C  
ATOM   3771  CD  GLU A 492       6.534  17.376 -14.989  1.00 51.27           C  
ANISOU 3771  CD  GLU A 492     6934   5705   6842  -1037    319    102       C  
ATOM   3772  OE1 GLU A 492       7.172  17.971 -14.095  1.00 50.66           O  
ANISOU 3772  OE1 GLU A 492     6850   5633   6765  -1031    317     84       O  
ATOM   3773  OE2 GLU A 492       5.515  17.856 -15.528  1.00 54.09           O  
ANISOU 3773  OE2 GLU A 492     7285   6056   7210  -1027    309     93       O  
ATOM   3774  N   VAL A 493       7.819  12.856 -14.495  1.00 24.64           N  
ANISOU 3774  N   VAL A 493     3592   2353   3417  -1078    357    179       N  
ATOM   3775  CA  VAL A 493       7.177  11.556 -14.646  1.00 26.24           C  
ANISOU 3775  CA  VAL A 493     3798   2548   3624  -1094    358    197       C  
ATOM   3776  C   VAL A 493       8.257  10.504 -14.853  1.00 27.28           C  
ANISOU 3776  C   VAL A 493     3956   2662   3749  -1092    358    216       C  
ATOM   3777  O   VAL A 493       9.165  10.694 -15.669  1.00 35.17           O  
ANISOU 3777  O   VAL A 493     4973   3646   4745  -1078    353    212       O  
ATOM   3778  CB  VAL A 493       6.183  11.540 -15.823  1.00 31.96           C  
ANISOU 3778  CB  VAL A 493     4525   3253   4368  -1098    341    187       C  
ATOM   3779  CG1 VAL A 493       5.494  10.184 -15.921  1.00 38.63           C  
ANISOU 3779  CG1 VAL A 493     5368   4082   5226  -1119    334    202       C  
ATOM   3780  CG2 VAL A 493       5.163  12.652 -15.673  1.00 32.84           C  
ANISOU 3780  CG2 VAL A 493     4611   3383   4486  -1092    338    168       C  
ATOM   3781  N   ASP A 494       8.157   9.397 -14.121  1.00 34.51           N  
ANISOU 3781  N   ASP A 494     4871   3579   4663  -1104    366    239       N  
ATOM   3782  CA  ASP A 494       9.057   8.260 -14.308  1.00 32.02           C  
ANISOU 3782  CA  ASP A 494     4582   3240   4346  -1099    362    256       C  
ATOM   3783  C   ASP A 494       8.701   7.581 -15.623  1.00 28.35           C  
ANISOU 3783  C   ASP A 494     4137   2734   3901  -1100    340    247       C  
ATOM   3784  O   ASP A 494       7.748   6.803 -15.698  1.00 26.95           O  
ANISOU 3784  O   ASP A 494     3957   2536   3748  -1121    329    254       O  
ATOM   3785  CB  ASP A 494       8.942   7.292 -13.135  1.00 32.32           C  
ANISOU 3785  CB  ASP A 494     4614   3287   4381  -1111    373    290       C  
ATOM   3786  CG  ASP A 494      10.049   6.249 -13.118  1.00 39.66           C  
ANISOU 3786  CG  ASP A 494     5570   4194   5306  -1097    369    309       C  
ATOM   3787  OD1 ASP A 494      10.715   6.049 -14.157  1.00 36.27           O  
ANISOU 3787  OD1 ASP A 494     5164   3738   4880  -1080    355    292       O  
ATOM   3788  OD2 ASP A 494      10.248   5.620 -12.058  1.00 36.96           O  
ANISOU 3788  OD2 ASP A 494     5225   3865   4955  -1099    380    341       O  
ATOM   3789  N   GLU A 495       9.475   7.871 -16.670  1.00 30.43           N  
ANISOU 3789  N   GLU A 495     4419   2988   4153  -1076    332    231       N  
ATOM   3790  CA  GLU A 495       9.181   7.349 -17.999  1.00 32.48           C  
ANISOU 3790  CA  GLU A 495     4700   3219   4421  -1066    309    213       C  
ATOM   3791  C   GLU A 495       9.495   5.865 -18.141  1.00 45.68           C  
ANISOU 3791  C   GLU A 495     6398   4857   6104  -1061    293    217       C  
ATOM   3792  O   GLU A 495       9.090   5.260 -19.139  1.00 48.50           O  
ANISOU 3792  O   GLU A 495     6771   5184   6472  -1053    265    195       O  
ATOM   3793  CB  GLU A 495       9.950   8.155 -19.049  1.00 23.18           C  
ANISOU 3793  CB  GLU A 495     3532   2056   3221  -1036    310    202       C  
ATOM   3794  CG  GLU A 495       9.511   9.614 -19.133  1.00 31.05           C  
ANISOU 3794  CG  GLU A 495     4508   3071   4217  -1041    317    198       C  
ATOM   3795  CD  GLU A 495      10.585  10.530 -19.690  1.00 33.12           C  
ANISOU 3795  CD  GLU A 495     4772   3350   4463  -1020    329    206       C  
ATOM   3796  OE1 GLU A 495      11.759  10.398 -19.283  1.00 36.53           O  
ANISOU 3796  OE1 GLU A 495     5203   3791   4884  -1013    342    218       O  
ATOM   3797  OE2 GLU A 495      10.252  11.388 -20.535  1.00 29.96           O  
ANISOU 3797  OE2 GLU A 495     4370   2953   4061  -1011    324    204       O  
ATOM   3798  N   THR A 496      10.190   5.265 -17.176  1.00 33.85           N  
ANISOU 3798  N   THR A 496     4903   3357   4603  -1061    305    241       N  
ATOM   3799  CA  THR A 496      10.547   3.853 -17.231  1.00 41.87           C  
ANISOU 3799  CA  THR A 496     5944   4332   5633  -1053    287    248       C  
ATOM   3800  C   THR A 496       9.587   2.961 -16.452  1.00 44.30           C  
ANISOU 3800  C   THR A 496     6244   4609   5978  -1090    281    275       C  
ATOM   3801  O   THR A 496       9.740   1.736 -16.481  1.00 45.72           O  
ANISOU 3801  O   THR A 496     6446   4742   6182  -1089    261    284       O  
ATOM   3802  CB  THR A 496      11.973   3.648 -16.706  1.00 42.89           C  
ANISOU 3802  CB  THR A 496     6083   4476   5736  -1025    302    263       C  
ATOM   3803  OG1 THR A 496      12.024   3.975 -15.312  1.00 56.64           O  
ANISOU 3803  OG1 THR A 496     7802   6248   7470  -1042    325    293       O  
ATOM   3804  CG2 THR A 496      12.952   4.531 -17.465  1.00 53.80           C  
ANISOU 3804  CG2 THR A 496     7464   5891   7086   -993    311    244       C  
ATOM   3805  N   TYR A 497       8.602   3.538 -15.770  1.00 43.75           N  
ANISOU 3805  N   TYR A 497     6141   4566   5916  -1122    296    290       N  
ATOM   3806  CA  TYR A 497       7.693   2.762 -14.937  1.00 44.38           C  
ANISOU 3806  CA  TYR A 497     6204   4630   6030  -1160    298    328       C  
ATOM   3807  C   TYR A 497       6.636   2.074 -15.795  1.00 44.68           C  
ANISOU 3807  C   TYR A 497     6242   4617   6116  -1185    264    312       C  
ATOM   3808  O   TYR A 497       6.043   2.696 -16.682  1.00 50.56           O  
ANISOU 3808  O   TYR A 497     6979   5369   6861  -1183    249    275       O  
ATOM   3809  CB  TYR A 497       7.028   3.669 -13.903  1.00 41.75           C  
ANISOU 3809  CB  TYR A 497     5829   4355   5679  -1178    330    348       C  
ATOM   3810  CG  TYR A 497       5.984   2.985 -13.051  1.00 39.48           C  
ANISOU 3810  CG  TYR A 497     5513   4067   5422  -1218    339    394       C  
ATOM   3811  CD1 TYR A 497       6.352   2.113 -12.036  1.00 33.74           C  
ANISOU 3811  CD1 TYR A 497     4790   3336   4695  -1224    353    448       C  
ATOM   3812  CD2 TYR A 497       4.631   3.219 -13.254  1.00 38.89           C  
ANISOU 3812  CD2 TYR A 497     5404   4000   5374  -1248    336    391       C  
ATOM   3813  CE1 TYR A 497       5.403   1.488 -11.251  1.00 45.36           C  
ANISOU 3813  CE1 TYR A 497     6230   4810   6194  -1262    367    503       C  
ATOM   3814  CE2 TYR A 497       3.675   2.599 -12.476  1.00 30.58           C  
ANISOU 3814  CE2 TYR A 497     4316   2953   4351  -1287    348    441       C  
ATOM   3815  CZ  TYR A 497       4.066   1.735 -11.476  1.00 44.10           C  
ANISOU 3815  CZ  TYR A 497     6032   4661   6063  -1296    365    500       C  
ATOM   3816  OH  TYR A 497       3.116   1.116 -10.696  1.00 47.03           O  
ANISOU 3816  OH  TYR A 497     6364   5040   6463  -1337    382    561       O  
ATOM   3817  N   VAL A 498       6.403   0.792 -15.530  1.00 48.39           N  
ANISOU 3817  N   VAL A 498     6721   5035   6631  -1209    247    341       N  
ATOM   3818  CA  VAL A 498       5.351   0.046 -16.219  1.00 57.49           C  
ANISOU 3818  CA  VAL A 498     7868   6132   7842  -1240    208    327       C  
ATOM   3819  C   VAL A 498       4.077   0.151 -15.388  1.00 58.63           C  
ANISOU 3819  C   VAL A 498     7961   6300   8015  -1292    227    370       C  
ATOM   3820  O   VAL A 498       4.121  -0.022 -14.160  1.00 57.85           O  
ANISOU 3820  O   VAL A 498     7844   6226   7910  -1308    260    428       O  
ATOM   3821  CB  VAL A 498       5.761  -1.417 -16.469  1.00 60.62           C  
ANISOU 3821  CB  VAL A 498     8302   6448   8284  -1239    171    331       C  
ATOM   3822  CG1 VAL A 498       6.127  -2.121 -15.167  1.00 57.08           C  
ANISOU 3822  CG1 VAL A 498     7853   5989   7846  -1255    195    402       C  
ATOM   3823  CG2 VAL A 498       4.655  -2.170 -17.204  1.00 58.81           C  
ANISOU 3823  CG2 VAL A 498     8066   6155   8124  -1275    122    309       C  
ATOM   3824  N   PRO A 499       2.935   0.462 -16.001  1.00 55.29           N  
ANISOU 3824  N   PRO A 499     7509   5879   7618  -1315    208    344       N  
ATOM   3825  CA  PRO A 499       1.706   0.659 -15.222  1.00 50.03           C  
ANISOU 3825  CA  PRO A 499     6785   5249   6975  -1360    230    384       C  
ATOM   3826  C   PRO A 499       1.322  -0.580 -14.425  1.00 50.80           C  
ANISOU 3826  C   PRO A 499     6866   5305   7129  -1408    232    451       C  
ATOM   3827  O   PRO A 499       1.502  -1.715 -14.871  1.00 46.12           O  
ANISOU 3827  O   PRO A 499     6303   4633   6590  -1421    192    450       O  
ATOM   3828  CB  PRO A 499       0.659   0.983 -16.292  1.00 46.49           C  
ANISOU 3828  CB  PRO A 499     6315   4794   6554  -1372    195    335       C  
ATOM   3829  CG  PRO A 499       1.441   1.553 -17.423  1.00 44.87           C  
ANISOU 3829  CG  PRO A 499     6154   4587   6308  -1319    175    272       C  
ATOM   3830  CD  PRO A 499       2.766   0.846 -17.414  1.00 48.99           C  
ANISOU 3830  CD  PRO A 499     6726   5069   6816  -1292    171    276       C  
ATOM   3831  N   LYS A 500       0.791  -0.345 -13.228  1.00 60.93           N  
ANISOU 3831  N   LYS A 500     8102   6646   8401  -1432    277    511       N  
ATOM   3832  CA  LYS A 500       0.320  -1.411 -12.357  1.00 67.41           C  
ANISOU 3832  CA  LYS A 500     8898   7443   9273  -1481    288    592       C  
ATOM   3833  C   LYS A 500      -1.144  -1.706 -12.656  1.00 60.06           C  
ANISOU 3833  C   LYS A 500     7911   6497   8411  -1539    269    603       C  
ATOM   3834  O   LYS A 500      -1.962  -0.785 -12.754  1.00 57.57           O  
ANISOU 3834  O   LYS A 500     7551   6244   8077  -1539    283    580       O  
ATOM   3835  CB  LYS A 500       0.491  -1.021 -10.888  1.00 70.16           C  
ANISOU 3835  CB  LYS A 500     9219   7874   9565  -1472    350    657       C  
ATOM   3836  CG  LYS A 500       0.647  -2.198  -9.937  1.00 69.43           C  
ANISOU 3836  CG  LYS A 500     9125   7752   9502  -1500    365    749       C  
ATOM   3837  CD  LYS A 500       1.123  -1.741  -8.566  1.00 67.73           C  
ANISOU 3837  CD  LYS A 500     8898   7628   9210  -1469    421    799       C  
ATOM   3838  CE  LYS A 500      -0.015  -1.140  -7.755  1.00 61.53           C  
ANISOU 3838  CE  LYS A 500     8040   6937   8403  -1488    467    838       C  
ATOM   3839  NZ  LYS A 500       0.235  -1.228  -6.289  1.00 50.62           N  
ANISOU 3839  NZ  LYS A 500     6639   5630   6965  -1473    519    917       N  
ATOM   3840  N   GLU A 501      -1.468  -2.985 -12.807  1.00 60.39           N  
ANISOU 3840  N   GLU A 501     7953   6454   8537  -1587    235    636       N  
ATOM   3841  CA  GLU A 501      -2.850  -3.387 -13.013  1.00 58.05           C  
ANISOU 3841  CA  GLU A 501     7597   6139   8321  -1651    215    655       C  
ATOM   3842  C   GLU A 501      -3.577  -3.482 -11.678  1.00 51.83           C  
ANISOU 3842  C   GLU A 501     6741   5413   7538  -1693    272    757       C  
ATOM   3843  O   GLU A 501      -2.967  -3.708 -10.629  1.00 58.87           O  
ANISOU 3843  O   GLU A 501     7643   6330   8394  -1682    315    824       O  
ATOM   3844  CB  GLU A 501      -2.918  -4.725 -13.749  1.00 71.16           C  
ANISOU 3844  CB  GLU A 501     9284   7674  10079  -1689    147    645       C  
ATOM   3845  CG  GLU A 501      -1.785  -4.945 -14.737  1.00 79.94           C  
ANISOU 3845  CG  GLU A 501    10478   8723  11174  -1633    100    567       C  
ATOM   3846  CD  GLU A 501      -1.721  -6.373 -15.242  1.00 88.73           C  
ANISOU 3846  CD  GLU A 501    11622   9709  12382  -1663     34    562       C  
ATOM   3847  OE1 GLU A 501      -2.453  -7.229 -14.702  1.00 93.69           O  
ANISOU 3847  OE1 GLU A 501    12211  10293  13093  -1727     31    631       O  
ATOM   3848  OE2 GLU A 501      -0.938  -6.640 -16.178  1.00 89.73           O  
ANISOU 3848  OE2 GLU A 501    11811   9781  12501  -1616    -12    489       O  
ATOM   3849  N   PHE A 502      -4.894  -3.300 -11.725  1.00 58.85           N  
ANISOU 3849  N   PHE A 502     7557   6336   8467  -1738    274    769       N  
ATOM   3850  CA  PHE A 502      -5.698  -3.341 -10.512  1.00 50.92           C  
ANISOU 3850  CA  PHE A 502     6477   5405   7464  -1776    333    867       C  
ATOM   3851  C   PHE A 502      -5.829  -4.771 -10.000  1.00 49.93           C  
ANISOU 3851  C   PHE A 502     6341   5205   7426  -1841    327    964       C  
ATOM   3852  O   PHE A 502      -6.047  -5.707 -10.774  1.00 54.12           O  
ANISOU 3852  O   PHE A 502     6887   5636   8040  -1864    271    932       O  
ATOM   3853  CB  PHE A 502      -7.083  -2.750 -10.774  1.00 63.66           C  
ANISOU 3853  CB  PHE A 502     8010   7079   9101  -1804    334    850       C  
ATOM   3854  CG  PHE A 502      -7.113  -1.248 -10.771  1.00 76.20           C  
ANISOU 3854  CG  PHE A 502     9590   8770  10595  -1740    364    789       C  
ATOM   3855  CD1 PHE A 502      -6.810  -0.540  -9.621  1.00 77.29           C  
ANISOU 3855  CD1 PHE A 502     9714   9007  10644  -1699    430    825       C  
ATOM   3856  CD2 PHE A 502      -7.442  -0.544 -11.917  1.00 80.68           C  
ANISOU 3856  CD2 PHE A 502    10162   9331  11161  -1718    321    695       C  
ATOM   3857  CE1 PHE A 502      -6.833   0.841  -9.612  1.00 77.93           C  
ANISOU 3857  CE1 PHE A 502     9790   9172  10647  -1640    450    765       C  
ATOM   3858  CE2 PHE A 502      -7.469   0.838 -11.914  1.00 82.69           C  
ANISOU 3858  CE2 PHE A 502    10411   9670  11337  -1660    345    644       C  
ATOM   3859  CZ  PHE A 502      -7.164   1.531 -10.760  1.00 80.00           C  
ANISOU 3859  CZ  PHE A 502    10059   9420  10917  -1622    408    677       C  
ATOM   3860  N   ASN A 503      -5.694  -4.936  -8.684  1.00 54.15           N  
ANISOU 3860  N   ASN A 503     6851   5798   7924  -1843    390   1065       N  
ATOM   3861  CA  ASN A 503      -5.834  -6.250  -8.065  1.00 59.35           C  
ANISOU 3861  CA  ASN A 503     7503   6411   8636  -1865    402   1141       C  
ATOM   3862  C   ASN A 503      -6.789  -6.197  -6.877  1.00 67.16           C  
ANISOU 3862  C   ASN A 503     8405   7504   9610  -1893    472   1243       C  
ATOM   3863  O   ASN A 503      -7.414  -5.163  -6.621  1.00 69.53           O  
ANISOU 3863  O   ASN A 503     8644   7910   9865  -1895    507   1247       O  
ATOM   3864  CB  ASN A 503      -4.469  -6.792  -7.630  1.00 52.79           C  
ANISOU 3864  CB  ASN A 503     6750   5535   7773  -1825    405   1167       C  
ATOM   3865  CG  ASN A 503      -3.714  -5.826  -6.739  1.00 60.78           C  
ANISOU 3865  CG  ASN A 503     7770   6648   8674  -1785    458   1200       C  
ATOM   3866  OD1 ASN A 503      -4.054  -5.646  -5.569  1.00 55.89           O  
ANISOU 3866  OD1 ASN A 503     7100   6125   8008  -1788    521   1287       O  
ATOM   3867  ND2 ASN A 503      -2.678  -5.201  -7.288  1.00 63.41           N  
ANISOU 3867  ND2 ASN A 503     8170   6975   8949  -1724    436   1110       N  
ATOM   3868  N   ALA A 504      -6.906  -7.310  -6.147  1.00 69.17           N  
ANISOU 3868  N   ALA A 504     8652   7732   9898  -1914    491   1328       N  
ATOM   3869  CA  ALA A 504      -7.835  -7.362  -5.022  1.00 68.72           C  
ANISOU 3869  CA  ALA A 504     8509   7775   9825  -1940    558   1432       C  
ATOM   3870  C   ALA A 504      -7.344  -6.514  -3.855  1.00 69.46           C  
ANISOU 3870  C   ALA A 504     8592   7999   9802  -1894    630   1490       C  
ATOM   3871  O   ALA A 504      -8.132  -5.800  -3.225  1.00 77.18           O  
ANISOU 3871  O   ALA A 504     9489   9101  10733  -1896    685   1531       O  
ATOM   3872  CB  ALA A 504      -8.047  -8.810  -4.582  1.00 59.21           C  
ANISOU 3872  CB  ALA A 504     7305   6502   8689  -1975    555   1510       C  
ATOM   3873  N   GLU A 505      -6.046  -6.581  -3.549  1.00 61.85           N  
ANISOU 3873  N   GLU A 505     7701   7013   8785  -1848    630   1495       N  
ATOM   3874  CA  GLU A 505      -5.473  -5.741  -2.505  1.00 69.38           C  
ANISOU 3874  CA  GLU A 505     8650   8090   9622  -1802    690   1540       C  
ATOM   3875  C   GLU A 505      -5.462  -4.265  -2.881  1.00 78.26           C  
ANISOU 3875  C   GLU A 505     9768   9293  10673  -1760    692   1441       C  
ATOM   3876  O   GLU A 505      -5.253  -3.421  -2.003  1.00 84.04           O  
ANISOU 3876  O   GLU A 505    10487  10149  11295  -1698    742   1440       O  
ATOM   3877  CB  GLU A 505      -4.050  -6.203  -2.184  1.00 66.72           C  
ANISOU 3877  CB  GLU A 505     8397   7703   9251  -1761    679   1556       C  
ATOM   3878  CG  GLU A 505      -3.560  -5.816  -0.796  1.00 70.92           C  
ANISOU 3878  CG  GLU A 505     8917   8361   9670  -1716    746   1639       C  
ATOM   3879  CD  GLU A 505      -4.041  -6.769   0.280  1.00 74.06           C  
ANISOU 3879  CD  GLU A 505     9276   8791  10072  -1728    792   1761       C  
ATOM   3880  OE1 GLU A 505      -4.785  -7.715  -0.052  1.00 78.14           O  
ANISOU 3880  OE1 GLU A 505     9775   9230  10686  -1777    771   1780       O  
ATOM   3881  OE2 GLU A 505      -3.676  -6.571   1.458  1.00 77.51           O  
ANISOU 3881  OE2 GLU A 505     9700   9334  10414  -1687    847   1837       O  
ATOM   3882  N   THR A 506      -5.689  -3.936  -4.151  1.00 76.47           N  
ANISOU 3882  N   THR A 506     9558   9000  10496  -1771    636   1337       N  
ATOM   3883  CA  THR A 506      -5.652  -2.552  -4.604  1.00 82.15           C  
ANISOU 3883  CA  THR A 506    10285   9784  11146  -1712    632   1222       C  
ATOM   3884  C   THR A 506      -7.022  -1.885  -4.539  1.00 89.12           C  
ANISOU 3884  C   THR A 506    11076  10757  12029  -1729    658   1220       C  
ATOM   3885  O   THR A 506      -7.164  -0.817  -3.936  1.00 87.73           O  
ANISOU 3885  O   THR A 506    10872  10700  11761  -1673    700   1196       O  
ATOM   3886  CB  THR A 506      -5.104  -2.481  -6.033  1.00 77.31           C  
ANISOU 3886  CB  THR A 506     9740   9062  10574  -1704    560   1111       C  
ATOM   3887  OG1 THR A 506      -3.719  -2.848  -6.034  1.00 79.51           O  
ANISOU 3887  OG1 THR A 506    10102   9282  10828  -1668    542   1099       O  
ATOM   3888  CG2 THR A 506      -5.246  -1.074  -6.583  1.00 80.11           C  
ANISOU 3888  CG2 THR A 506    10092   9474  10870  -1654    554   1005       C  
ATOM   3889  N   PHE A 507      -8.041  -2.499  -5.144  1.00 95.61           N  
ANISOU 3889  N   PHE A 507    11848  11525  12955  -1803    631   1242       N  
ATOM   3890  CA  PHE A 507      -9.345  -1.857  -5.319  1.00 97.14           C  
ANISOU 3890  CA  PHE A 507    11955  11794  13159  -1818    643   1224       C  
ATOM   3891  C   PHE A 507     -10.471  -2.730  -4.773  1.00107.92           C  
ANISOU 3891  C   PHE A 507    13225  13179  14599  -1899    673   1345       C  
ATOM   3892  O   PHE A 507     -11.036  -3.562  -5.488  1.00107.87           O  
ANISOU 3892  O   PHE A 507    13201  13078  14706  -1968    626   1351       O  
ATOM   3893  CB  PHE A 507      -9.569  -1.510  -6.784  1.00 87.33           C  
ANISOU 3893  CB  PHE A 507    10735  10478  11967  -1823    573   1110       C  
ATOM   3894  CG  PHE A 507      -9.375  -0.059  -7.082  1.00 76.68           C  
ANISOU 3894  CG  PHE A 507     9407   9196  10531  -1745    575   1006       C  
ATOM   3895  CD1 PHE A 507      -8.434   0.673  -6.379  1.00 76.78           C  
ANISOU 3895  CD1 PHE A 507     9464   9270  10440  -1672    610    988       C  
ATOM   3896  CD2 PHE A 507     -10.138   0.580  -8.042  1.00 58.76           C  
ANISOU 3896  CD2 PHE A 507     7111   6929   8286  -1743    539    928       C  
ATOM   3897  CE1 PHE A 507      -8.248   2.009  -6.632  1.00 63.51           C  
ANISOU 3897  CE1 PHE A 507     7802   7641   8689  -1604    608    896       C  
ATOM   3898  CE2 PHE A 507      -9.956   1.920  -8.300  1.00 58.55           C  
ANISOU 3898  CE2 PHE A 507     7105   6958   8184  -1671    540    840       C  
ATOM   3899  CZ  PHE A 507      -9.011   2.633  -7.589  1.00 58.67           C  
ANISOU 3899  CZ  PHE A 507     7164   7023   8103  -1603    574    825       C  
ATOM   3900  N   THR A 508     -10.793  -2.524  -3.498  1.00120.86           N  
ANISOU 3900  N   THR A 508    14805  14947  16171  -1881    750   1432       N  
ATOM   3901  CA  THR A 508     -12.017  -3.024  -2.890  1.00134.21           C  
ANISOU 3901  CA  THR A 508    16385  16700  17908  -1941    794   1542       C  
ATOM   3902  C   THR A 508     -12.383  -2.068  -1.763  1.00137.68           C  
ANISOU 3902  C   THR A 508    16762  17324  18227  -1878    875   1571       C  
ATOM   3903  O   THR A 508     -11.504  -1.498  -1.111  1.00142.64           O  
ANISOU 3903  O   THR A 508    17442  18012  18744  -1799    903   1548       O  
ATOM   3904  CB  THR A 508     -11.874  -4.459  -2.368  1.00142.00           C  
ANISOU 3904  CB  THR A 508    17394  17617  18942  -1965    799   1621       C  
ATOM   3905  OG1 THR A 508     -11.018  -5.207  -3.241  1.00142.86           O  
ANISOU 3905  OG1 THR A 508    17602  17565  19114  -1974    727   1563       O  
ATOM   3906  CG2 THR A 508     -13.234  -5.135  -2.322  1.00145.32           C  
ANISOU 3906  CG2 THR A 508    17727  18046  19444  -2025    806   1672       C  
ATOM   3907  N   PHE A 509     -13.685  -1.889  -1.541  1.00133.18           N  
ANISOU 3907  N   PHE A 509    16080  16846  17676  -1907    910   1613       N  
ATOM   3908  CA  PHE A 509     -14.134  -0.742  -0.760  1.00126.65           C  
ANISOU 3908  CA  PHE A 509    15196  16193  16731  -1829    971   1594       C  
ATOM   3909  C   PHE A 509     -15.057  -1.108   0.399  1.00120.28           C  
ANISOU 3909  C   PHE A 509    14275  15521  15907  -1853   1055   1735       C  
ATOM   3910  O   PHE A 509     -14.706  -0.883   1.562  1.00123.83           O  
ANISOU 3910  O   PHE A 509    14719  16084  16246  -1792   1118   1788       O  
ATOM   3911  CB  PHE A 509     -14.813   0.259  -1.696  1.00126.84           C  
ANISOU 3911  CB  PHE A 509    15196  16231  16764  -1805    934   1471       C  
ATOM   3912  CG  PHE A 509     -13.882   0.840  -2.724  1.00126.47           C  
ANISOU 3912  CG  PHE A 509    15251  16047  16754  -1796    850   1348       C  
ATOM   3913  CD1 PHE A 509     -13.066   1.914  -2.404  1.00124.63           C  
ANISOU 3913  CD1 PHE A 509    15119  15797  16440  -1720    837   1271       C  
ATOM   3914  CD2 PHE A 509     -13.803   0.301  -3.997  1.00129.21           C  
ANISOU 3914  CD2 PHE A 509    15591  16287  17216  -1863    784   1311       C  
ATOM   3915  CE1 PHE A 509     -12.199   2.447  -3.340  1.00124.16           C  
ANISOU 3915  CE1 PHE A 509    15147  15620  16410  -1711    766   1167       C  
ATOM   3916  CE2 PHE A 509     -12.938   0.831  -4.938  1.00128.36           C  
ANISOU 3916  CE2 PHE A 509    15574  16065  17131  -1847    710   1201       C  
ATOM   3917  CZ  PHE A 509     -12.135   1.906  -4.608  1.00125.64           C  
ANISOU 3917  CZ  PHE A 509    15327  15708  16702  -1772    705   1133       C  
ATOM   3918  N   HIS A 510     -16.240  -1.648   0.093  1.00110.62           N  
ANISOU 3918  N   HIS A 510    12961  14287  14781  -1927   1051   1782       N  
ATOM   3919  CA  HIS A 510     -17.252  -2.002   1.089  1.00100.63           C  
ANISOU 3919  CA  HIS A 510    11595  13140  13499  -1931   1120   1883       C  
ATOM   3920  C   HIS A 510     -17.767  -0.782   1.847  1.00 79.52           C  
ANISOU 3920  C   HIS A 510     8834  10677  10705  -1863   1195   1891       C  
ATOM   3921  O   HIS A 510     -17.311   0.344   1.619  1.00 74.83           O  
ANISOU 3921  O   HIS A 510     8288  10114  10029  -1781   1179   1772       O  
ATOM   3922  CB  HIS A 510     -16.713  -3.041   2.078  1.00106.13           C  
ANISOU 3922  CB  HIS A 510    12333  13818  14174  -1926   1153   1983       C  
ATOM   3923  CG  HIS A 510     -15.865  -4.099   1.444  1.00110.28           C  
ANISOU 3923  CG  HIS A 510    12964  14149  14787  -1968   1083   1965       C  
ATOM   3924  ND1 HIS A 510     -14.506  -4.187   1.653  1.00110.53           N  
ANISOU 3924  ND1 HIS A 510    13100  14131  14767  -1928   1072   1956       N  
ATOM   3925  CD2 HIS A 510     -16.184  -5.115   0.608  1.00112.72           C  
ANISOU 3925  CD2 HIS A 510    13290  14308  15229  -2042   1019   1951       C  
ATOM   3926  CE1 HIS A 510     -14.024  -5.212   0.973  1.00111.20           C  
ANISOU 3926  CE1 HIS A 510    13260  14044  14947  -1972   1007   1937       C  
ATOM   3927  NE2 HIS A 510     -15.022  -5.792   0.330  1.00111.46           N  
ANISOU 3927  NE2 HIS A 510    13244  14014  15092  -2040    973   1932       N  
ATOM   3928  N   ALA A 511     -18.718  -0.999   2.755  1.00 62.14           N  
ANISOU 3928  N   ALA A 511     6535   8600   8476  -1855   1262   1977       N  
ATOM   3929  CA  ALA A 511     -19.404   0.085   3.447  1.00 60.66           C  
ANISOU 3929  CA  ALA A 511     6249   8621   8179  -1786   1333   1980       C  
ATOM   3930  C   ALA A 511     -18.810   0.411   4.811  1.00 57.70           C  
ANISOU 3930  C   ALA A 511     5885   8389   7648  -1694   1408   2031       C  
ATOM   3931  O   ALA A 511     -19.355   1.268   5.514  1.00 60.60           O  
ANISOU 3931  O   ALA A 511     6173   8942   7908  -1620   1471   2030       O  
ATOM   3932  CB  ALA A 511     -20.891  -0.249   3.606  1.00 57.74           C  
ANISOU 3932  CB  ALA A 511     5754   8320   7864  -1823   1362   2036       C  
ATOM   3933  N   ASP A 512     -17.713  -0.239   5.206  1.00 62.74           N  
ANISOU 3933  N   ASP A 512     6620   8952   8268  -1689   1400   2068       N  
ATOM   3934  CA  ASP A 512     -17.038   0.147   6.440  1.00 62.77           C  
ANISOU 3934  CA  ASP A 512     6642   9091   8117  -1595   1462   2102       C  
ATOM   3935  C   ASP A 512     -16.444   1.549   6.365  1.00 64.30           C  
ANISOU 3935  C   ASP A 512     6893   9340   8200  -1484   1442   1948       C  
ATOM   3936  O   ASP A 512     -16.080   2.106   7.407  1.00 72.15           O  
ANISOU 3936  O   ASP A 512     7892  10470   9053  -1383   1489   1942       O  
ATOM   3937  CB  ASP A 512     -15.940  -0.865   6.789  1.00 60.13           C  
ANISOU 3937  CB  ASP A 512     6408   8646   7793  -1608   1443   2158       C  
ATOM   3938  CG  ASP A 512     -14.946  -1.071   5.658  1.00 64.66           C  
ANISOU 3938  CG  ASP A 512     7090   9027   8450  -1654   1359   2084       C  
ATOM   3939  OD1 ASP A 512     -14.156  -0.145   5.378  1.00 67.81           O  
ANISOU 3939  OD1 ASP A 512     7558   9422   8784  -1588   1330   1967       O  
ATOM   3940  OD2 ASP A 512     -14.949  -2.165   5.054  1.00 66.52           O  
ANISOU 3940  OD2 ASP A 512     7363   9100   8813  -1730   1308   2103       O  
ATOM   3941  N   ILE A 513     -16.348   2.129   5.166  1.00 52.47           N  
ANISOU 3941  N   ILE A 513     5447   7728   6762  -1488   1366   1807       N  
ATOM   3942  CA  ILE A 513     -15.784   3.463   5.004  1.00 46.71           C  
ANISOU 3942  CA  ILE A 513     4785   7020   5944  -1381   1332   1645       C  
ATOM   3943  C   ILE A 513     -16.750   4.547   5.464  1.00 52.39           C  
ANISOU 3943  C   ILE A 513     5416   7911   6578  -1299   1374   1596       C  
ATOM   3944  O   ILE A 513     -16.318   5.660   5.791  1.00 59.04           O  
ANISOU 3944  O   ILE A 513     6299   8817   7316  -1190   1367   1486       O  
ATOM   3945  CB  ILE A 513     -15.369   3.678   3.534  1.00 50.72           C  
ANISOU 3945  CB  ILE A 513     5375   7349   6546  -1416   1239   1524       C  
ATOM   3946  CG1 ILE A 513     -14.449   4.893   3.395  1.00 56.53           C  
ANISOU 3946  CG1 ILE A 513     6204   8076   7199  -1316   1200   1374       C  
ATOM   3947  CG2 ILE A 513     -16.596   3.820   2.642  1.00 57.25           C  
ANISOU 3947  CG2 ILE A 513     6126   8163   7466  -1467   1217   1499       C  
ATOM   3948  CD1 ILE A 513     -14.140   5.265   1.959  1.00 58.60           C  
ANISOU 3948  CD1 ILE A 513     6536   8187   7542  -1339   1116   1257       C  
ATOM   3949  N   CYS A 514     -18.051   4.247   5.511  1.00 56.79           N  
ANISOU 3949  N   CYS A 514     5851   8546   7182  -1346   1415   1675       N  
ATOM   3950  CA  CYS A 514     -19.040   5.255   5.877  1.00 63.82           C  
ANISOU 3950  CA  CYS A 514     6650   9601   7999  -1266   1453   1627       C  
ATOM   3951  C   CYS A 514     -19.044   5.534   7.376  1.00 59.98           C  
ANISOU 3951  C   CYS A 514     6117   9313   7358  -1170   1537   1681       C  
ATOM   3952  O   CYS A 514     -19.407   6.640   7.791  1.00 61.69           O  
ANISOU 3952  O   CYS A 514     6303   9662   7475  -1061   1555   1595       O  
ATOM   3953  CB  CYS A 514     -20.434   4.822   5.419  1.00 65.15           C  
ANISOU 3953  CB  CYS A 514     6694   9792   8269  -1350   1469   1694       C  
ATOM   3954  SG  CYS A 514     -20.523   4.183   3.713  1.00 67.62           S  
ANISOU 3954  SG  CYS A 514     7045   9874   8772  -1479   1371   1658       S  
ATOM   3955  N   THR A 515     -18.654   4.558   8.199  1.00 52.85           N  
ANISOU 3955  N   THR A 515     5212   8438   6432  -1202   1586   1822       N  
ATOM   3956  CA  THR A 515     -18.533   4.760   9.637  1.00 60.87           C  
ANISOU 3956  CA  THR A 515     6195   9643   7292  -1106   1664   1878       C  
ATOM   3957  C   THR A 515     -17.269   5.518  10.023  1.00 54.85           C  
ANISOU 3957  C   THR A 515     5549   8876   6417   -998   1631   1761       C  
ATOM   3958  O   THR A 515     -17.084   5.821  11.205  1.00 60.01           O  
ANISOU 3958  O   THR A 515     6185   9689   6928   -901   1684   1781       O  
ATOM   3959  CB  THR A 515     -18.562   3.411  10.356  1.00 61.93           C  
ANISOU 3959  CB  THR A 515     6284   9804   7444  -1181   1727   2081       C  
ATOM   3960  OG1 THR A 515     -17.274   2.790  10.263  1.00 63.96           O  
ANISOU 3960  OG1 THR A 515     6660   9920   7723  -1210   1686   2094       O  
ATOM   3961  CG2 THR A 515     -19.612   2.495   9.743  1.00 66.81           C  
ANISOU 3961  CG2 THR A 515     6829  10339   8218  -1304   1720   2166       C  
ATOM   3962  N   LEU A 516     -16.403   5.827   9.063  1.00 55.55           N  
ANISOU 3962  N   LEU A 516     5750   8791   6566  -1012   1544   1641       N  
ATOM   3963  CA  LEU A 516     -15.176   6.557   9.332  1.00 51.93           C  
ANISOU 3963  CA  LEU A 516     5399   8314   6019   -921   1504   1526       C  
ATOM   3964  C   LEU A 516     -15.470   8.040   9.536  1.00 49.37           C  
ANISOU 3964  C   LEU A 516     5063   8095   5602   -798   1495   1379       C  
ATOM   3965  O   LEU A 516     -16.542   8.544   9.189  1.00 53.27           O  
ANISOU 3965  O   LEU A 516     5482   8639   6119   -790   1502   1346       O  
ATOM   3966  CB  LEU A 516     -14.184   6.376   8.184  1.00 59.16           C  
ANISOU 3966  CB  LEU A 516     6431   9010   7036   -982   1417   1455       C  
ATOM   3967  CG  LEU A 516     -13.794   4.950   7.794  1.00 57.26           C  
ANISOU 3967  CG  LEU A 516     6219   8634   6902  -1101   1408   1575       C  
ATOM   3968  CD1 LEU A 516     -12.770   4.973   6.670  1.00 52.68           C  
ANISOU 3968  CD1 LEU A 516     5755   7857   6401  -1135   1321   1479       C  
ATOM   3969  CD2 LEU A 516     -13.259   4.188   8.994  1.00 64.14           C  
ANISOU 3969  CD2 LEU A 516     7092   9582   7695  -1084   1463   1700       C  
ATOM   3970  N   SER A 517     -14.494   8.743  10.099  1.00 61.22           N  
ANISOU 3970  N   SER A 517     6638   9624   7000   -700   1473   1287       N  
ATOM   3971  CA  SER A 517     -14.609  10.182  10.293  1.00 66.22           C  
ANISOU 3971  CA  SER A 517     7276  10335   7550   -578   1450   1134       C  
ATOM   3972  C   SER A 517     -14.463  10.879   8.941  1.00 72.34           C  
ANISOU 3972  C   SER A 517     8113  10946   8428   -605   1366   1003       C  
ATOM   3973  O   SER A 517     -14.388  10.247   7.883  1.00 54.81           O  
ANISOU 3973  O   SER A 517     5920   8573   6332   -712   1331   1034       O  
ATOM   3974  CB  SER A 517     -13.571  10.669  11.298  1.00 71.94           C  
ANISOU 3974  CB  SER A 517     8062  11130   8144   -472   1444   1075       C  
ATOM   3975  OG  SER A 517     -12.282  10.163  10.996  1.00 70.33           O  
ANISOU 3975  OG  SER A 517     7961  10783   7981   -520   1398   1078       O  
ATOM   3976  N   GLU A 518     -14.420  12.212   8.965  1.00 78.88           N  
ANISOU 3976  N   GLU A 518     8963  11805   9202   -503   1330    855       N  
ATOM   3977  CA  GLU A 518     -14.212  12.951   7.726  1.00 79.53           C  
ANISOU 3977  CA  GLU A 518     9109  11735   9374   -520   1250    735       C  
ATOM   3978  C   GLU A 518     -12.762  12.880   7.270  1.00 75.08           C  
ANISOU 3978  C   GLU A 518     8667  11016   8845   -548   1187    688       C  
ATOM   3979  O   GLU A 518     -12.483  12.998   6.071  1.00 76.25           O  
ANISOU 3979  O   GLU A 518     8870  11010   9094   -605   1128    639       O  
ATOM   3980  CB  GLU A 518     -14.639  14.408   7.902  1.00 86.23           C  
ANISOU 3980  CB  GLU A 518     9944  12660  10161   -401   1228    595       C  
ATOM   3981  CG  GLU A 518     -16.124  14.601   8.154  1.00 90.80           C  
ANISOU 3981  CG  GLU A 518    10401  13382  10717   -368   1281    623       C  
ATOM   3982  CD  GLU A 518     -16.486  16.054   8.400  1.00 89.64           C  
ANISOU 3982  CD  GLU A 518    10245  13312  10503   -238   1257    479       C  
ATOM   3983  OE1 GLU A 518     -17.469  16.307   9.128  1.00 91.50           O  
ANISOU 3983  OE1 GLU A 518    10384  13720  10663   -166   1312    493       O  
ATOM   3984  OE2 GLU A 518     -15.787  16.942   7.868  1.00 83.22           O  
ANISOU 3984  OE2 GLU A 518     9520  12384   9715   -205   1182    353       O  
ATOM   3985  N   LYS A 519     -11.830  12.677   8.203  1.00 69.10           N  
ANISOU 3985  N   LYS A 519     7948  10302   8003   -508   1200    705       N  
ATOM   3986  CA  LYS A 519     -10.414  12.708   7.859  1.00 70.28           C  
ANISOU 3986  CA  LYS A 519     8207  10320   8177   -523   1140    653       C  
ATOM   3987  C   LYS A 519      -9.940  11.381   7.278  1.00 65.58           C  
ANISOU 3987  C   LYS A 519     7644   9604   7671   -640   1139    761       C  
ATOM   3988  O   LYS A 519      -9.219  11.368   6.275  1.00 66.53           O  
ANISOU 3988  O   LYS A 519     7838   9567   7873   -690   1081    716       O  
ATOM   3989  CB  LYS A 519      -9.584  13.080   9.088  1.00 78.20           C  
ANISOU 3989  CB  LYS A 519     9239  11421   9054   -425   1146    616       C  
ATOM   3990  CG  LYS A 519      -8.104  13.266   8.795  1.00 86.34           C  
ANISOU 3990  CG  LYS A 519    10375  12327  10104   -429   1080    547       C  
ATOM   3991  CD  LYS A 519      -7.325  13.592  10.057  1.00 85.94           C  
ANISOU 3991  CD  LYS A 519    10344  12383   9927   -332   1083    511       C  
ATOM   3992  CE  LYS A 519      -5.976  12.891  10.065  1.00 86.68           C  
ANISOU 3992  CE  LYS A 519    10512  12389  10035   -373   1058    546       C  
ATOM   3993  NZ  LYS A 519      -5.040  13.496  11.051  1.00 86.93           N  
ANISOU 3993  NZ  LYS A 519    10579  12490   9960   -275   1032    467       N  
ATOM   3994  N   GLU A 520     -10.323  10.255   7.886  1.00 60.35           N  
ANISOU 3994  N   GLU A 520     6926   9008   6994   -682   1202    905       N  
ATOM   3995  CA  GLU A 520      -9.880   8.967   7.364  1.00 63.91           C  
ANISOU 3995  CA  GLU A 520     7410   9337   7535   -790   1197   1007       C  
ATOM   3996  C   GLU A 520     -10.698   8.507   6.165  1.00 55.34           C  
ANISOU 3996  C   GLU A 520     6295   8150   6581   -890   1181   1036       C  
ATOM   3997  O   GLU A 520     -10.244   7.626   5.428  1.00 51.93           O  
ANISOU 3997  O   GLU A 520     5907   7581   6241   -976   1153   1081       O  
ATOM   3998  CB  GLU A 520      -9.909   7.897   8.458  1.00 72.60           C  
ANISOU 3998  CB  GLU A 520     8470  10535   8581   -802   1265   1158       C  
ATOM   3999  CG  GLU A 520     -11.184   7.845   9.268  1.00 83.64           C  
ANISOU 3999  CG  GLU A 520     9752  12107   9920   -776   1342   1237       C  
ATOM   4000  CD  GLU A 520     -10.950   7.353  10.683  1.00 96.34           C  
ANISOU 4000  CD  GLU A 520    11334  13861  11411   -726   1407   1340       C  
ATOM   4001  OE1 GLU A 520     -11.940   7.147  11.417  1.00 99.92           O  
ANISOU 4001  OE1 GLU A 520    11687  14466  11812   -709   1480   1431       O  
ATOM   4002  OE2 GLU A 520      -9.773   7.173  11.063  1.00100.73           O  
ANISOU 4002  OE2 GLU A 520    11964  14384  11923   -700   1385   1332       O  
ATOM   4003  N   ARG A 521     -11.889   9.073   5.952  1.00 43.35           N  
ANISOU 4003  N   ARG A 521     4701   6697   5072   -875   1196   1009       N  
ATOM   4004  CA  ARG A 521     -12.591   8.839   4.695  1.00 44.87           C  
ANISOU 4004  CA  ARG A 521     4874   6786   5388   -958   1164   1006       C  
ATOM   4005  C   ARG A 521     -11.859   9.502   3.536  1.00 53.26           C  
ANISOU 4005  C   ARG A 521     6029   7700   6505   -959   1084    882       C  
ATOM   4006  O   ARG A 521     -11.784   8.942   2.436  1.00 55.53           O  
ANISOU 4006  O   ARG A 521     6347   7854   6898  -1041   1044    891       O  
ATOM   4007  CB  ARG A 521     -14.028   9.354   4.784  1.00 53.88           C  
ANISOU 4007  CB  ARG A 521     5909   8043   6520   -933   1198   1001       C  
ATOM   4008  CG  ARG A 521     -15.079   8.348   4.339  1.00 67.70           C  
ANISOU 4008  CG  ARG A 521     7576   9777   8368  -1037   1221   1111       C  
ATOM   4009  CD  ARG A 521     -16.414   9.022   4.049  1.00 68.18           C  
ANISOU 4009  CD  ARG A 521     7545   9919   8443  -1015   1231   1073       C  
ATOM   4010  NE  ARG A 521     -16.640  10.192   4.894  1.00 77.07           N  
ANISOU 4010  NE  ARG A 521     8643  11193   9447   -889   1258    999       N  
ATOM   4011  CZ  ARG A 521     -17.047  10.137   6.159  1.00 84.55           C  
ANISOU 4011  CZ  ARG A 521     9517  12316  10293   -833   1333   1065       C  
ATOM   4012  NH1 ARG A 521     -17.275   8.965   6.736  1.00 84.02           N  
ANISOU 4012  NH1 ARG A 521     9394  12295  10234   -898   1392   1219       N  
ATOM   4013  NH2 ARG A 521     -17.225  11.256   6.848  1.00 89.78           N  
ANISOU 4013  NH2 ARG A 521    10161  13106  10845   -709   1347    979       N  
ATOM   4014  N   GLN A 522     -11.313  10.698   3.767  1.00 43.79           N  
ANISOU 4014  N   GLN A 522     4876   6526   5238   -866   1057    766       N  
ATOM   4015  CA  GLN A 522     -10.510  11.355   2.741  1.00 48.30           C  
ANISOU 4015  CA  GLN A 522     5535   6960   5856   -865    984    659       C  
ATOM   4016  C   GLN A 522      -9.212  10.598   2.493  1.00 41.69           C  
ANISOU 4016  C   GLN A 522     4782   6010   5049   -913    958    687       C  
ATOM   4017  O   GLN A 522      -8.759  10.490   1.349  1.00 37.27           O  
ANISOU 4017  O   GLN A 522     4279   5314   4568   -962    908    654       O  
ATOM   4018  CB  GLN A 522     -10.220  12.799   3.149  1.00 42.15           C  
ANISOU 4018  CB  GLN A 522     4780   6233   5001   -757    962    535       C  
ATOM   4019  CG  GLN A 522     -11.421  13.727   3.059  1.00 47.52           C  
ANISOU 4019  CG  GLN A 522     5395   6990   5671   -704    967    478       C  
ATOM   4020  CD  GLN A 522     -11.106  15.129   3.546  1.00 64.28           C  
ANISOU 4020  CD  GLN A 522     7544   9159   7721   -592    941    354       C  
ATOM   4021  OE1 GLN A 522     -10.140  15.341   4.279  1.00 65.01           O  
ANISOU 4021  OE1 GLN A 522     7683   9270   7748   -545    934    324       O  
ATOM   4022  NE2 GLN A 522     -11.923  16.095   3.139  1.00 65.30           N  
ANISOU 4022  NE2 GLN A 522     7644   9305   7863   -547    921    278       N  
ATOM   4023  N   ILE A 523      -8.604  10.062   3.555  1.00 43.23           N  
ANISOU 4023  N   ILE A 523     4984   6265   5176   -894    993    748       N  
ATOM   4024  CA  ILE A 523      -7.365   9.304   3.401  1.00 44.79           C  
ANISOU 4024  CA  ILE A 523     5258   6364   5397   -933    970    779       C  
ATOM   4025  C   ILE A 523      -7.609   8.044   2.579  1.00 44.66           C  
ANISOU 4025  C   ILE A 523     5239   6242   5487  -1039    965    867       C  
ATOM   4026  O   ILE A 523      -6.769   7.646   1.762  1.00 45.59           O  
ANISOU 4026  O   ILE A 523     5426   6230   5665  -1081    921    851       O  
ATOM   4027  CB  ILE A 523      -6.764   8.983   4.782  1.00 45.62           C  
ANISOU 4027  CB  ILE A 523     5364   6569   5401   -884   1009    833       C  
ATOM   4028  CG1 ILE A 523      -6.313  10.272   5.473  1.00 59.04           C  
ANISOU 4028  CG1 ILE A 523     7082   8349   7003   -776    995    722       C  
ATOM   4029  CG2 ILE A 523      -5.598   8.012   4.654  1.00 46.00           C  
ANISOU 4029  CG2 ILE A 523     5480   6520   5479   -929    991    885       C  
ATOM   4030  CD1 ILE A 523      -5.502  10.047   6.734  1.00 65.85           C  
ANISOU 4030  CD1 ILE A 523     7960   9299   7762   -720   1017    752       C  
ATOM   4031  N   LYS A 524      -8.764   7.401   2.772  1.00 42.18           N  
ANISOU 4031  N   LYS A 524     4842   5983   5200  -1084   1008    958       N  
ATOM   4032  CA  LYS A 524      -9.123   6.262   1.931  1.00 40.95           C  
ANISOU 4032  CA  LYS A 524     4678   5722   5159  -1188    995   1031       C  
ATOM   4033  C   LYS A 524      -9.242   6.684   0.472  1.00 37.08           C  
ANISOU 4033  C   LYS A 524     4221   5116   4752  -1216    932    940       C  
ATOM   4034  O   LYS A 524      -8.715   6.017  -0.426  1.00 41.36           O  
ANISOU 4034  O   LYS A 524     4816   5526   5371  -1274    889    942       O  
ATOM   4035  CB  LYS A 524     -10.430   5.635   2.417  1.00 46.00           C  
ANISOU 4035  CB  LYS A 524     5210   6450   5817  -1230   1052   1141       C  
ATOM   4036  CG  LYS A 524     -10.343   4.971   3.781  1.00 62.64           C  
ANISOU 4036  CG  LYS A 524     7283   8664   7854  -1216   1118   1260       C  
ATOM   4037  CD  LYS A 524      -9.480   3.723   3.745  1.00 71.46           C  
ANISOU 4037  CD  LYS A 524     8456   9675   9020  -1277   1106   1344       C  
ATOM   4038  CE  LYS A 524      -9.541   2.979   5.070  1.00 73.75           C  
ANISOU 4038  CE  LYS A 524     8703  10071   9248  -1271   1175   1483       C  
ATOM   4039  NZ  LYS A 524      -8.743   1.724   5.037  1.00 73.82           N  
ANISOU 4039  NZ  LYS A 524     8766   9971   9312  -1329   1162   1571       N  
ATOM   4040  N   LYS A 525      -9.935   7.798   0.219  1.00 41.59           N  
ANISOU 4040  N   LYS A 525     4759   5738   5305  -1171    924    859       N  
ATOM   4041  CA  LYS A 525     -10.055   8.306  -1.144  1.00 43.25           C  
ANISOU 4041  CA  LYS A 525     5000   5849   5583  -1187    865    773       C  
ATOM   4042  C   LYS A 525      -8.696   8.707  -1.702  1.00 44.16           C  
ANISOU 4042  C   LYS A 525     5220   5865   5696  -1164    815    696       C  
ATOM   4043  O   LYS A 525      -8.433   8.542  -2.900  1.00 40.14           O  
ANISOU 4043  O   LYS A 525     4755   5241   5256  -1204    766    663       O  
ATOM   4044  CB  LYS A 525     -11.020   9.491  -1.178  1.00 47.28           C  
ANISOU 4044  CB  LYS A 525     5457   6443   6066  -1129    868    703       C  
ATOM   4045  CG  LYS A 525     -12.464   9.132  -0.871  1.00 44.34           C  
ANISOU 4045  CG  LYS A 525     4973   6163   5711  -1157    912    772       C  
ATOM   4046  CD  LYS A 525     -13.391  10.312  -1.124  1.00 47.86           C  
ANISOU 4046  CD  LYS A 525     5371   6673   6140  -1099    904    691       C  
ATOM   4047  CE  LYS A 525     -13.178  11.412  -0.095  1.00 65.31           C  
ANISOU 4047  CE  LYS A 525     7582   8995   8239   -990    928    633       C  
ATOM   4048  NZ  LYS A 525     -14.164  12.518  -0.246  1.00 69.47           N  
ANISOU 4048  NZ  LYS A 525     8055   9591   8748   -927    923    559       N  
ATOM   4049  N   GLN A 526      -7.819   9.239  -0.849  1.00 40.96           N  
ANISOU 4049  N   GLN A 526     4849   5506   5207  -1100    826    667       N  
ATOM   4050  CA  GLN A 526      -6.481   9.599  -1.302  1.00 49.54           C  
ANISOU 4050  CA  GLN A 526     6027   6504   6293  -1081    782    602       C  
ATOM   4051  C   GLN A 526      -5.631   8.364  -1.565  1.00 43.03           C  
ANISOU 4051  C   GLN A 526     5250   5588   5510  -1140    771    665       C  
ATOM   4052  O   GLN A 526      -4.759   8.387  -2.441  1.00 40.34           O  
ANISOU 4052  O   GLN A 526     4976   5145   5206  -1152    727    620       O  
ATOM   4053  CB  GLN A 526      -5.811  10.511  -0.274  1.00 37.98           C  
ANISOU 4053  CB  GLN A 526     4580   5117   4732   -997    791    550       C  
ATOM   4054  CG  GLN A 526      -6.300  11.948  -0.336  1.00 32.88           C  
ANISOU 4054  CG  GLN A 526     3918   4516   4060   -930    775    452       C  
ATOM   4055  CD  GLN A 526      -5.804  12.790   0.823  1.00 43.44           C  
ANISOU 4055  CD  GLN A 526     5261   5943   5302   -843    784    400       C  
ATOM   4056  OE1 GLN A 526      -5.417  12.266   1.867  1.00 41.22           O  
ANISOU 4056  OE1 GLN A 526     4973   5730   4959   -826    817    452       O  
ATOM   4057  NE2 GLN A 526      -5.820  14.106   0.646  1.00 40.97           N  
ANISOU 4057  NE2 GLN A 526     4960   5628   4976   -784    751    297       N  
ATOM   4058  N   THR A 527      -5.872   7.279  -0.828  1.00 47.24           N  
ANISOU 4058  N   THR A 527     5749   6159   6041  -1174    812    770       N  
ATOM   4059  CA  THR A 527      -5.168   6.031  -1.100  1.00 47.40           C  
ANISOU 4059  CA  THR A 527     5813   6086   6112  -1231    799    834       C  
ATOM   4060  C   THR A 527      -5.535   5.484  -2.474  1.00 41.66           C  
ANISOU 4060  C   THR A 527     5097   5242   5491  -1299    757    826       C  
ATOM   4061  O   THR A 527      -4.679   4.945  -3.186  1.00 33.87           O  
ANISOU 4061  O   THR A 527     4174   4149   4547  -1324    719    815       O  
ATOM   4062  CB  THR A 527      -5.482   5.009  -0.006  1.00 46.77           C  
ANISOU 4062  CB  THR A 527     5688   6071   6013  -1254    852    958       C  
ATOM   4063  OG1 THR A 527      -5.452   5.657   1.272  1.00 38.93           O  
ANISOU 4063  OG1 THR A 527     4666   5214   4910  -1180    895    959       O  
ATOM   4064  CG2 THR A 527      -4.469   3.878  -0.014  1.00 52.67           C  
ANISOU 4064  CG2 THR A 527     6492   6731   6789  -1287    839   1016       C  
ATOM   4065  N   ALA A 528      -6.803   5.622  -2.869  1.00 37.19           N  
ANISOU 4065  N   ALA A 528     4467   4698   4965  -1326    760    827       N  
ATOM   4066  CA  ALA A 528      -7.228   5.133  -4.176  1.00 41.09           C  
ANISOU 4066  CA  ALA A 528     4966   5088   5556  -1387    714    812       C  
ATOM   4067  C   ALA A 528      -6.725   6.026  -5.302  1.00 43.65           C  
ANISOU 4067  C   ALA A 528     5349   5349   5887  -1356    662    703       C  
ATOM   4068  O   ALA A 528      -6.496   5.544  -6.417  1.00 44.49           O  
ANISOU 4068  O   ALA A 528     5495   5352   6058  -1393    616    682       O  
ATOM   4069  CB  ALA A 528      -8.752   5.021  -4.226  1.00 42.63           C  
ANISOU 4069  CB  ALA A 528     5068   5335   5793  -1424    731    847       C  
ATOM   4070  N   LEU A 529      -6.549   7.323  -5.033  1.00 39.58           N  
ANISOU 4070  N   LEU A 529     4840   4892   5305  -1287    667    634       N  
ATOM   4071  CA  LEU A 529      -6.014   8.223  -6.051  1.00 31.87           C  
ANISOU 4071  CA  LEU A 529     3920   3855   4335  -1258    621    541       C  
ATOM   4072  C   LEU A 529      -4.595   7.828  -6.437  1.00 35.96           C  
ANISOU 4072  C   LEU A 529     4519   4287   4858  -1262    595    531       C  
ATOM   4073  O   LEU A 529      -4.231   7.873  -7.618  1.00 36.16           O  
ANISOU 4073  O   LEU A 529     4588   4229   4922  -1272    552    487       O  
ATOM   4074  CB  LEU A 529      -6.061   9.669  -5.551  1.00 28.79           C  
ANISOU 4074  CB  LEU A 529     3520   3540   3879  -1184    631    475       C  
ATOM   4075  CG  LEU A 529      -5.366  10.745  -6.394  1.00 38.22           C  
ANISOU 4075  CG  LEU A 529     4773   4677   5072  -1146    588    386       C  
ATOM   4076  CD1 LEU A 529      -5.865  10.727  -7.832  1.00 36.65           C  
ANISOU 4076  CD1 LEU A 529     4581   4406   4938  -1177    547    360       C  
ATOM   4077  CD2 LEU A 529      -5.565  12.123  -5.782  1.00 43.63           C  
ANISOU 4077  CD2 LEU A 529     5441   5435   5702  -1075    595    326       C  
ATOM   4078  N   VAL A 530      -3.781   7.430  -5.455  1.00 32.63           N  
ANISOU 4078  N   VAL A 530     4115   3890   4392  -1248    620    571       N  
ATOM   4079  CA  VAL A 530      -2.428   6.964  -5.751  1.00 36.83           C  
ANISOU 4079  CA  VAL A 530     4718   4347   4929  -1251    598    567       C  
ATOM   4080  C   VAL A 530      -2.477   5.753  -6.673  1.00 38.57           C  
ANISOU 4080  C   VAL A 530     4957   4470   5227  -1311    570    600       C  
ATOM   4081  O   VAL A 530      -1.750   5.678  -7.671  1.00 33.83           O  
ANISOU 4081  O   VAL A 530     4411   3790   4653  -1312    532    559       O  
ATOM   4082  CB  VAL A 530      -1.670   6.649  -4.449  1.00 40.00           C  
ANISOU 4082  CB  VAL A 530     5127   4802   5271  -1225    630    613       C  
ATOM   4083  CG1 VAL A 530      -0.408   5.858  -4.747  1.00 36.21           C  
ANISOU 4083  CG1 VAL A 530     4710   4241   4806  -1237    609    628       C  
ATOM   4084  CG2 VAL A 530      -1.326   7.925  -3.717  1.00 38.22           C  
ANISOU 4084  CG2 VAL A 530     4899   4653   4968  -1157    640    556       C  
ATOM   4085  N   GLU A 531      -3.344   4.787  -6.354  1.00 43.64           N  
ANISOU 4085  N   GLU A 531     5553   5120   5910  -1360    588    674       N  
ATOM   4086  CA  GLU A 531      -3.479   3.604  -7.198  1.00 49.10           C  
ANISOU 4086  CA  GLU A 531     6259   5713   6684  -1420    555    701       C  
ATOM   4087  C   GLU A 531      -3.969   3.964  -8.595  1.00 36.25           C  
ANISOU 4087  C   GLU A 531     4637   4032   5104  -1430    508    632       C  
ATOM   4088  O   GLU A 531      -3.617   3.288  -9.568  1.00 40.67           O  
ANISOU 4088  O   GLU A 531     5238   4499   5714  -1454    465    614       O  
ATOM   4089  CB  GLU A 531      -4.423   2.597  -6.540  1.00 47.86           C  
ANISOU 4089  CB  GLU A 531     6041   5575   6570  -1475    582    798       C  
ATOM   4090  CG  GLU A 531      -3.921   2.056  -5.209  1.00 43.39           C  
ANISOU 4090  CG  GLU A 531     5472   5055   5958  -1467    627    882       C  
ATOM   4091  CD  GLU A 531      -2.662   1.220  -5.352  1.00 52.24           C  
ANISOU 4091  CD  GLU A 531     6666   6090   7093  -1467    604    896       C  
ATOM   4092  OE1 GLU A 531      -2.480   0.592  -6.415  1.00 61.63           O  
ANISOU 4092  OE1 GLU A 531     7892   7174   8352  -1498    556    872       O  
ATOM   4093  OE2 GLU A 531      -1.854   1.190  -4.400  1.00 51.09           O  
ANISOU 4093  OE2 GLU A 531     6540   5987   6886  -1432    631    929       O  
ATOM   4094  N   LEU A 532      -4.781   5.018  -8.716  1.00 44.40           N  
ANISOU 4094  N   LEU A 532     5629   5124   6117  -1408    514    590       N  
ATOM   4095  CA  LEU A 532      -5.172   5.509 -10.034  1.00 40.43           C  
ANISOU 4095  CA  LEU A 532     5135   4580   5646  -1406    469    521       C  
ATOM   4096  C   LEU A 532      -3.959   5.978 -10.824  1.00 37.34           C  
ANISOU 4096  C   LEU A 532     4821   4134   5233  -1369    439    460       C  
ATOM   4097  O   LEU A 532      -3.762   5.582 -11.979  1.00 37.08           O  
ANISOU 4097  O   LEU A 532     4822   4027   5238  -1382    395    430       O  
ATOM   4098  CB  LEU A 532      -6.180   6.650  -9.898  1.00 40.91           C  
ANISOU 4098  CB  LEU A 532     5141   4721   5683  -1378    483    489       C  
ATOM   4099  CG  LEU A 532      -7.630   6.326 -10.238  1.00 61.15           C  
ANISOU 4099  CG  LEU A 532     7633   7300   8303  -1420    475    506       C  
ATOM   4100  CD1 LEU A 532      -7.767   6.048 -11.725  1.00 68.38           C  
ANISOU 4100  CD1 LEU A 532     8575   8130   9275  -1442    413    459       C  
ATOM   4101  CD2 LEU A 532      -8.105   5.153  -9.427  1.00 66.16           C  
ANISOU 4101  CD2 LEU A 532     8218   7948   8972  -1477    504    598       C  
ATOM   4102  N   VAL A 533      -3.136   6.834 -10.214  1.00 38.91           N  
ANISOU 4102  N   VAL A 533     5043   4372   5368  -1320    460    440       N  
ATOM   4103  CA  VAL A 533      -1.972   7.378 -10.907  1.00 37.39           C  
ANISOU 4103  CA  VAL A 533     4915   4136   5156  -1286    436    388       C  
ATOM   4104  C   VAL A 533      -0.983   6.269 -11.240  1.00 41.92           C  
ANISOU 4104  C   VAL A 533     5539   4639   5751  -1304    419    410       C  
ATOM   4105  O   VAL A 533      -0.358   6.275 -12.307  1.00 37.06           O  
ANISOU 4105  O   VAL A 533     4968   3966   5146  -1294    387    372       O  
ATOM   4106  CB  VAL A 533      -1.320   8.488 -10.062  1.00 36.80           C  
ANISOU 4106  CB  VAL A 533     4847   4117   5018  -1236    459    365       C  
ATOM   4107  CG1 VAL A 533      -0.142   9.101 -10.805  1.00 32.45           C  
ANISOU 4107  CG1 VAL A 533     4354   3521   4456  -1207    435    318       C  
ATOM   4108  CG2 VAL A 533      -2.346   9.556  -9.711  1.00 34.15           C  
ANISOU 4108  CG2 VAL A 533     4462   3850   4663  -1210    473    339       C  
ATOM   4109  N   LYS A 534      -0.828   5.298 -10.336  1.00 35.90           N  
ANISOU 4109  N   LYS A 534     4768   3880   4992  -1327    441    473       N  
ATOM   4110  CA  LYS A 534       0.032   4.156 -10.626  1.00 40.12           C  
ANISOU 4110  CA  LYS A 534     5349   4342   5553  -1342    422    495       C  
ATOM   4111  C   LYS A 534      -0.504   3.341 -11.795  1.00 41.61           C  
ANISOU 4111  C   LYS A 534     5544   4454   5811  -1379    379    482       C  
ATOM   4112  O   LYS A 534       0.274   2.720 -12.528  1.00 38.00           O  
ANISOU 4112  O   LYS A 534     5137   3928   5372  -1374    347    464       O  
ATOM   4113  CB  LYS A 534       0.173   3.271  -9.385  1.00 36.47           C  
ANISOU 4113  CB  LYS A 534     4873   3898   5084  -1360    454    574       C  
ATOM   4114  CG  LYS A 534       1.023   3.873  -8.275  1.00 39.91           C  
ANISOU 4114  CG  LYS A 534     5316   4400   5446  -1315    488    581       C  
ATOM   4115  CD  LYS A 534       1.244   2.877  -7.141  1.00 34.21           C  
ANISOU 4115  CD  LYS A 534     4588   3694   4716  -1328    516    665       C  
ATOM   4116  CE  LYS A 534       2.074   3.489  -6.021  1.00 43.90           C  
ANISOU 4116  CE  LYS A 534     5821   4996   5863  -1278    544    666       C  
ATOM   4117  NZ  LYS A 534       2.418   2.503  -4.956  1.00 33.84           N  
ANISOU 4117  NZ  LYS A 534     4547   3738   4573  -1282    569    750       N  
ATOM   4118  N   HIS A 535      -1.826   3.336 -11.987  1.00 39.25           N  
ANISOU 4118  N   HIS A 535     5194   4169   5551  -1412    373    487       N  
ATOM   4119  CA  HIS A 535      -2.417   2.596 -13.097  1.00 46.78           C  
ANISOU 4119  CA  HIS A 535     6148   5052   6573  -1447    324    467       C  
ATOM   4120  C   HIS A 535      -2.056   3.214 -14.443  1.00 53.17           C  
ANISOU 4120  C   HIS A 535     6999   5835   7370  -1411    285    389       C  
ATOM   4121  O   HIS A 535      -1.990   2.501 -15.451  1.00 53.34           O  
ANISOU 4121  O   HIS A 535     7048   5789   7431  -1421    238    361       O  
ATOM   4122  CB  HIS A 535      -3.935   2.532 -12.928  1.00 54.76           C  
ANISOU 4122  CB  HIS A 535     7084   6096   7627  -1490    328    492       C  
ATOM   4123  CG  HIS A 535      -4.609   1.579 -13.864  1.00 63.71           C  
ANISOU 4123  CG  HIS A 535     8209   7155   8843  -1537    275    481       C  
ATOM   4124  ND1 HIS A 535      -4.162   0.291 -14.065  1.00 65.08           N  
ANISOU 4124  ND1 HIS A 535     8417   7241   9071  -1567    245    502       N  
ATOM   4125  CD2 HIS A 535      -5.699   1.727 -14.654  1.00 67.76           C  
ANISOU 4125  CD2 HIS A 535     8682   7666   9397  -1557    241    446       C  
ATOM   4126  CE1 HIS A 535      -4.948  -0.314 -14.938  1.00 66.95           C  
ANISOU 4126  CE1 HIS A 535     8635   7422   9379  -1605    192    477       C  
ATOM   4127  NE2 HIS A 535      -5.888   0.535 -15.311  1.00 66.21           N  
ANISOU 4127  NE2 HIS A 535     8496   7382   9278  -1600    189    444       N  
ATOM   4128  N   LYS A 536      -1.825   4.526 -14.482  1.00 52.28           N  
ANISOU 4128  N   LYS A 536     6888   5773   7201  -1367    301    353       N  
ATOM   4129  CA  LYS A 536      -1.380   5.196 -15.698  1.00 47.91           C  
ANISOU 4129  CA  LYS A 536     6375   5201   6630  -1329    271    292       C  
ATOM   4130  C   LYS A 536      -0.756   6.541 -15.345  1.00 38.07           C  
ANISOU 4130  C   LYS A 536     5139   4004   5324  -1284    299    274       C  
ATOM   4131  O   LYS A 536      -1.453   7.563 -15.313  1.00 40.35           O  
ANISOU 4131  O   LYS A 536     5396   4335   5598  -1270    306    255       O  
ATOM   4132  CB  LYS A 536      -2.538   5.381 -16.681  1.00 54.51           C  
ANISOU 4132  CB  LYS A 536     7182   6032   7497  -1339    235    256       C  
ATOM   4133  CG  LYS A 536      -2.089   5.698 -18.102  1.00 60.20           C  
ANISOU 4133  CG  LYS A 536     7947   6722   8203  -1303    196    200       C  
ATOM   4134  CD  LYS A 536      -3.216   6.297 -18.926  1.00 64.51           C  
ANISOU 4134  CD  LYS A 536     8463   7288   8761  -1298    168    164       C  
ATOM   4135  CE  LYS A 536      -2.726   6.741 -20.296  1.00 60.39           C  
ANISOU 4135  CE  LYS A 536     7985   6749   8211  -1253    135    116       C  
ATOM   4136  NZ  LYS A 536      -3.752   7.550 -21.009  1.00 58.43           N  
ANISOU 4136  NZ  LYS A 536     7709   6531   7963  -1237    112     85       N  
ATOM   4137  N   PRO A 537       0.553   6.581 -15.077  1.00 35.79           N  
ANISOU 4137  N   PRO A 537     4891   3706   5003  -1261    312    278       N  
ATOM   4138  CA  PRO A 537       1.186   7.847 -14.671  1.00 41.48           C  
ANISOU 4138  CA  PRO A 537     5618   4468   5677  -1223    334    261       C  
ATOM   4139  C   PRO A 537       1.221   8.903 -15.764  1.00 52.49           C  
ANISOU 4139  C   PRO A 537     7027   5857   7061  -1194    314    216       C  
ATOM   4140  O   PRO A 537       1.571  10.050 -15.470  1.00 47.98           O  
ANISOU 4140  O   PRO A 537     6455   5312   6463  -1167    327    201       O  
ATOM   4141  CB  PRO A 537       2.604   7.419 -14.269  1.00 49.39           C  
ANISOU 4141  CB  PRO A 537     6657   5453   6656  -1211    345    277       C  
ATOM   4142  CG  PRO A 537       2.835   6.130 -14.985  1.00 49.88           C  
ANISOU 4142  CG  PRO A 537     6748   5456   6750  -1227    319    284       C  
ATOM   4143  CD  PRO A 537       1.501   5.454 -15.079  1.00 33.68           C  
ANISOU 4143  CD  PRO A 537     4662   3391   4745  -1267    305    298       C  
ATOM   4144  N   LYS A 538       0.876   8.569 -17.005  1.00 56.42           N  
ANISOU 4144  N   LYS A 538     7537   6319   7579  -1196    280    195       N  
ATOM   4145  CA  LYS A 538       0.861   9.558 -18.075  1.00 54.74           C  
ANISOU 4145  CA  LYS A 538     7338   6107   7353  -1165    262    161       C  
ATOM   4146  C   LYS A 538      -0.502  10.210 -18.270  1.00 57.31           C  
ANISOU 4146  C   LYS A 538     7623   6459   7693  -1166    252    145       C  
ATOM   4147  O   LYS A 538      -0.588  11.221 -18.975  1.00 51.16           O  
ANISOU 4147  O   LYS A 538     6851   5686   6900  -1136    240    122       O  
ATOM   4148  CB  LYS A 538       1.305   8.919 -19.396  1.00 48.50           C  
ANISOU 4148  CB  LYS A 538     6586   5277   6566  -1154    230    143       C  
ATOM   4149  CG  LYS A 538       2.681   8.277 -19.354  1.00 49.90           C  
ANISOU 4149  CG  LYS A 538     6802   5430   6727  -1145    237    154       C  
ATOM   4150  CD  LYS A 538       3.695   9.093 -20.140  1.00 57.19           C  
ANISOU 4150  CD  LYS A 538     7755   6358   7615  -1106    240    143       C  
ATOM   4151  CE  LYS A 538       3.296   9.214 -21.604  1.00 52.10           C  
ANISOU 4151  CE  LYS A 538     7124   5707   6965  -1082    208    115       C  
ATOM   4152  NZ  LYS A 538       3.873  10.434 -22.238  1.00 33.03           N  
ANISOU 4152  NZ  LYS A 538     4721   3311   4519  -1048    217    117       N  
ATOM   4153  N   ALA A 539      -1.556   9.665 -17.656  1.00 62.24           N  
ANISOU 4153  N   ALA A 539     8203   7101   8344  -1198    256    160       N  
ATOM   4154  CA  ALA A 539      -2.914  10.134 -17.926  1.00 70.21           C  
ANISOU 4154  CA  ALA A 539     9168   8138   9370  -1199    242    144       C  
ATOM   4155  C   ALA A 539      -3.070  11.613 -17.595  1.00 84.02           C  
ANISOU 4155  C   ALA A 539    10905   9927  11093  -1161    258    127       C  
ATOM   4156  O   ALA A 539      -3.418  12.420 -18.465  1.00 90.99           O  
ANISOU 4156  O   ALA A 539    11791  10809  11972  -1133    235    101       O  
ATOM   4157  CB  ALA A 539      -3.920   9.301 -17.132  1.00 62.08           C  
ANISOU 4157  CB  ALA A 539     8084   7129   8375  -1243    253    173       C  
ATOM   4158  N   THR A 540      -2.807  11.977 -16.337  1.00 91.24           N  
ANISOU 4158  N   THR A 540    11805  10876  11987  -1156    293    142       N  
ATOM   4159  CA  THR A 540      -2.961  13.316 -15.771  1.00 98.28           C  
ANISOU 4159  CA  THR A 540    12681  11804  12856  -1119    307    122       C  
ATOM   4160  C   THR A 540      -3.993  14.177 -16.491  1.00 97.38           C  
ANISOU 4160  C   THR A 540    12545  11703  12753  -1095    284     93       C  
ATOM   4161  O   THR A 540      -5.189  13.869 -16.457  1.00 91.55           O  
ANISOU 4161  O   THR A 540    11758  10994  12033  -1108    280     95       O  
ATOM   4162  CB  THR A 540      -1.613  14.039 -15.741  1.00104.31           C  
ANISOU 4162  CB  THR A 540    13492  12544  13596  -1094    311    112       C  
ATOM   4163  OG1 THR A 540      -0.602  13.123 -15.311  1.00106.55           O  
ANISOU 4163  OG1 THR A 540    13799  12812  13872  -1114    325    138       O  
ATOM   4164  CG2 THR A 540      -1.655  15.210 -14.751  1.00103.84           C  
ANISOU 4164  CG2 THR A 540    13416  12522  13518  -1061    326     92       C  
ATOM   4165  N   LYS A 541      -3.532  15.227 -17.180  1.00106.70           N  
ANISOU 4165  N   LYS A 541    13758  12858  13924  -1059    267     71       N  
ATOM   4166  CA  LYS A 541      -4.384  16.363 -17.509  1.00113.19           C  
ANISOU 4166  CA  LYS A 541    14560  13696  14749  -1023    251     44       C  
ATOM   4167  C   LYS A 541      -5.224  16.702 -16.287  1.00114.66           C  
ANISOU 4167  C   LYS A 541    14693  13942  14929  -1012    274     36       C  
ATOM   4168  O   LYS A 541      -4.716  16.751 -15.162  1.00114.19           O  
ANISOU 4168  O   LYS A 541    14632  13904  14851  -1010    301     41       O  
ATOM   4169  CB  LYS A 541      -5.289  16.069 -18.710  1.00112.19           C  
ANISOU 4169  CB  LYS A 541    14422  13564  14641  -1025    218     36       C  
ATOM   4170  CG  LYS A 541      -4.690  15.156 -19.762  1.00105.32           C  
ANISOU 4170  CG  LYS A 541    13590  12653  13774  -1045    198     46       C  
ATOM   4171  CD  LYS A 541      -5.132  15.578 -21.154  1.00100.09           C  
ANISOU 4171  CD  LYS A 541    12940  11979  13112  -1017    159     28       C  
ATOM   4172  CE  LYS A 541      -6.632  15.402 -21.336  1.00 90.82           C  
ANISOU 4172  CE  LYS A 541    11710  10837  11959  -1021    137     12       C  
ATOM   4173  NZ  LYS A 541      -6.985  14.033 -21.804  1.00 83.88           N  
ANISOU 4173  NZ  LYS A 541    10820   9948  11103  -1061    114     11       N  
ATOM   4174  N   GLU A 542      -6.512  16.936 -16.508  1.00112.62           N  
ANISOU 4174  N   GLU A 542    14389  13717  14684   -999    262     22       N  
ATOM   4175  CA  GLU A 542      -7.521  16.840 -15.467  1.00104.74           C  
ANISOU 4175  CA  GLU A 542    13326  12789  13682   -998    287     24       C  
ATOM   4176  C   GLU A 542      -8.457  15.674 -15.745  1.00 95.91           C  
ANISOU 4176  C   GLU A 542    12161  11689  12592  -1045    283     49       C  
ATOM   4177  O   GLU A 542      -9.542  15.591 -15.160  1.00 97.77           O  
ANISOU 4177  O   GLU A 542    12329  11986  12831  -1047    298     54       O  
ATOM   4178  CB  GLU A 542      -8.286  18.160 -15.332  1.00109.00           C  
ANISOU 4178  CB  GLU A 542    13839  13360  14214   -941    278    -14       C  
ATOM   4179  CG  GLU A 542      -7.409  19.355 -14.929  1.00108.97           C  
ANISOU 4179  CG  GLU A 542    13877  13332  14192   -896    277    -42       C  
ATOM   4180  CD  GLU A 542      -6.420  19.767 -16.010  1.00108.10           C  
ANISOU 4180  CD  GLU A 542    13834  13145  14095   -894    249    -42       C  
ATOM   4181  OE1 GLU A 542      -5.415  20.431 -15.681  1.00103.96           O  
ANISOU 4181  OE1 GLU A 542    13347  12590  13565   -879    250    -51       O  
ATOM   4182  OE2 GLU A 542      -6.645  19.419 -17.189  1.00106.76           O  
ANISOU 4182  OE2 GLU A 542    13674  12949  13940   -907    226    -31       O  
ATOM   4183  N   GLN A 543      -8.063  14.794 -16.669  1.00 88.21           N  
ANISOU 4183  N   GLN A 543    11218  10660  11637  -1080    259     61       N  
ATOM   4184  CA  GLN A 543      -8.661  13.471 -16.787  1.00 76.05           C  
ANISOU 4184  CA  GLN A 543     9643   9121  10132  -1135    254     87       C  
ATOM   4185  C   GLN A 543      -8.673  12.757 -15.444  1.00 71.47           C  
ANISOU 4185  C   GLN A 543     9028   8578   9549  -1168    298    130       C  
ATOM   4186  O   GLN A 543      -9.593  11.982 -15.154  1.00 58.71           O  
ANISOU 4186  O   GLN A 543     7353   6991   7963  -1208    305    159       O  
ATOM   4187  CB  GLN A 543      -7.872  12.662 -17.819  1.00 78.95           C  
ANISOU 4187  CB  GLN A 543    10066   9417  10513  -1159    223     87       C  
ATOM   4188  CG  GLN A 543      -8.673  11.692 -18.653  1.00 88.03           C  
ANISOU 4188  CG  GLN A 543    11191  10548  11707  -1196    185     84       C  
ATOM   4189  CD  GLN A 543      -7.783  10.911 -19.601  1.00 91.15           C  
ANISOU 4189  CD  GLN A 543    11648  10877  12109  -1207    154     76       C  
ATOM   4190  OE1 GLN A 543      -8.252  10.063 -20.358  1.00 99.87           O  
ANISOU 4190  OE1 GLN A 543    12743  11956  13248  -1233    114     64       O  
ATOM   4191  NE2 GLN A 543      -6.486  11.199 -19.563  1.00 82.91           N  
ANISOU 4191  NE2 GLN A 543    10663   9808  11030  -1185    170     79       N  
ATOM   4192  N   LEU A 544      -7.653  13.000 -14.617  1.00 64.13           N  
ANISOU 4192  N   LEU A 544     8132   7650   8583  -1152    328    140       N  
ATOM   4193  CA  LEU A 544      -7.647  12.477 -13.257  1.00 56.53           C  
ANISOU 4193  CA  LEU A 544     7138   6737   7605  -1170    372    182       C  
ATOM   4194  C   LEU A 544      -8.633  13.222 -12.364  1.00 63.70           C  
ANISOU 4194  C   LEU A 544     7980   7733   8489  -1137    400    175       C  
ATOM   4195  O   LEU A 544      -9.144  12.647 -11.396  1.00 60.67           O  
ANISOU 4195  O   LEU A 544     7543   7409   8100  -1158    436    218       O  
ATOM   4196  CB  LEU A 544      -6.237  12.563 -12.675  1.00 41.09           C  
ANISOU 4196  CB  LEU A 544     5237   4760   5613  -1156    389    187       C  
ATOM   4197  CG  LEU A 544      -5.281  11.419 -13.019  1.00 42.82           C  
ANISOU 4197  CG  LEU A 544     5503   4915   5850  -1195    381    216       C  
ATOM   4198  CD1 LEU A 544      -3.885  11.705 -12.485  1.00 39.62           C  
ANISOU 4198  CD1 LEU A 544     5149   4498   5407  -1171    395    213       C  
ATOM   4199  CD2 LEU A 544      -5.803  10.093 -12.483  1.00 42.46           C  
ANISOU 4199  CD2 LEU A 544     5419   4880   5832  -1248    398    273       C  
ATOM   4200  N   LYS A 545      -8.905  14.496 -12.663  1.00 67.02           N  
ANISOU 4200  N   LYS A 545     8404   8167   8896  -1083    384    124       N  
ATOM   4201  CA  LYS A 545      -9.914  15.231 -11.906  1.00 73.22           C  
ANISOU 4201  CA  LYS A 545     9124   9037   9658  -1042    405    108       C  
ATOM   4202  C   LYS A 545     -11.288  14.590 -12.047  1.00 72.59           C  
ANISOU 4202  C   LYS A 545     8965   9003   9613  -1076    408    135       C  
ATOM   4203  O   LYS A 545     -12.040  14.502 -11.070  1.00 79.85           O  
ANISOU 4203  O   LYS A 545     9816  10009  10514  -1070    446    159       O  
ATOM   4204  CB  LYS A 545      -9.948  16.694 -12.358  1.00 81.02           C  
ANISOU 4204  CB  LYS A 545    10135  10013  10635   -977    377     46       C  
ATOM   4205  CG  LYS A 545     -11.113  17.505 -11.813  1.00 82.45           C  
ANISOU 4205  CG  LYS A 545    10251  10277  10800   -925    388     20       C  
ATOM   4206  CD  LYS A 545     -11.581  18.501 -12.867  1.00 79.23           C  
ANISOU 4206  CD  LYS A 545     9854   9837  10412   -885    344    -27       C  
ATOM   4207  CE  LYS A 545     -12.857  19.216 -12.447  1.00 77.10           C  
ANISOU 4207  CE  LYS A 545     9513   9649  10132   -832    350    -54       C  
ATOM   4208  NZ  LYS A 545     -14.021  18.293 -12.328  1.00 76.95           N  
ANISOU 4208  NZ  LYS A 545     9408   9697  10131   -872    369    -16       N  
ATOM   4209  N   ALA A 546     -11.639  14.143 -13.255  1.00 72.51           N  
ANISOU 4209  N   ALA A 546     8959   8941   9650  -1109    368    131       N  
ATOM   4210  CA  ALA A 546     -12.943  13.519 -13.450  1.00 75.96           C  
ANISOU 4210  CA  ALA A 546     9316   9416  10128  -1146    363    153       C  
ATOM   4211  C   ALA A 546     -13.040  12.195 -12.701  1.00 71.14           C  
ANISOU 4211  C   ALA A 546     8669   8822   9541  -1213    396    223       C  
ATOM   4212  O   ALA A 546     -14.080  11.881 -12.110  1.00 67.51           O  
ANISOU 4212  O   ALA A 546     8123   8434   9095  -1233    423    259       O  
ATOM   4213  CB  ALA A 546     -13.217  13.313 -14.940  1.00 80.55           C  
ANISOU 4213  CB  ALA A 546     9916   9935  10754  -1163    304    126       C  
ATOM   4214  N   VAL A 547     -11.962  11.408 -12.710  1.00 69.97           N  
ANISOU 4214  N   VAL A 547     8580   8607   9397  -1247    396    249       N  
ATOM   4215  CA  VAL A 547     -11.987  10.107 -12.049  1.00 67.01           C  
ANISOU 4215  CA  VAL A 547     8176   8233   9049  -1311    423    321       C  
ATOM   4216  C   VAL A 547     -12.049  10.272 -10.536  1.00 60.01           C  
ANISOU 4216  C   VAL A 547     7249   7439   8112  -1291    486    363       C  
ATOM   4217  O   VAL A 547     -12.794   9.560  -9.852  1.00 68.03           O  
ANISOU 4217  O   VAL A 547     8193   8508   9147  -1331    519    427       O  
ATOM   4218  CB  VAL A 547     -10.767   9.270 -12.473  1.00 59.41           C  
ANISOU 4218  CB  VAL A 547     7295   7176   8104  -1342    402    332       C  
ATOM   4219  CG1 VAL A 547     -10.724   7.970 -11.689  1.00 54.58           C  
ANISOU 4219  CG1 VAL A 547     6659   6560   7520  -1402    430    411       C  
ATOM   4220  CG2 VAL A 547     -10.803   8.996 -13.966  1.00 61.61           C  
ANISOU 4220  CG2 VAL A 547     7606   7374   8429  -1359    339    291       C  
ATOM   4221  N   MET A 548     -11.268  11.208  -9.990  1.00 59.97           N  
ANISOU 4221  N   MET A 548     7287   7457   8042  -1228    503    330       N  
ATOM   4222  CA  MET A 548     -11.260  11.417  -8.546  1.00 64.55           C  
ANISOU 4222  CA  MET A 548     7833   8131   8562  -1197    558    360       C  
ATOM   4223  C   MET A 548     -12.637  11.811  -8.030  1.00 68.63           C  
ANISOU 4223  C   MET A 548     8254   8756   9068  -1177    587    367       C  
ATOM   4224  O   MET A 548     -13.019  11.426  -6.918  1.00 73.33           O  
ANISOU 4224  O   MET A 548     8791   9438   9634  -1181    639    426       O  
ATOM   4225  CB  MET A 548     -10.224  12.480  -8.175  1.00 63.71           C  
ANISOU 4225  CB  MET A 548     7789   8023   8393  -1129    557    304       C  
ATOM   4226  CG  MET A 548     -10.136  12.774  -6.686  1.00 73.27           C  
ANISOU 4226  CG  MET A 548     8972   9334   9533  -1084    608    321       C  
ATOM   4227  SD  MET A 548      -9.931  11.285  -5.686  1.00 82.07           S  
ANISOU 4227  SD  MET A 548    10062  10480  10641  -1141    657    429       S  
ATOM   4228  CE  MET A 548     -10.555  11.849  -4.105  1.00 82.51           C  
ANISOU 4228  CE  MET A 548    10046  10697  10609  -1075    718    443       C  
ATOM   4229  N   ASP A 549     -13.400  12.564  -8.822  1.00 65.91           N  
ANISOU 4229  N   ASP A 549     7887   8412   8743  -1151    555    313       N  
ATOM   4230  CA  ASP A 549     -14.764  12.908  -8.445  1.00 72.31           C  
ANISOU 4230  CA  ASP A 549     8600   9327   9549  -1130    578    318       C  
ATOM   4231  C   ASP A 549     -15.759  11.811  -8.796  1.00 70.40           C  
ANISOU 4231  C   ASP A 549     8282   9088   9378  -1209    577    378       C  
ATOM   4232  O   ASP A 549     -16.837  11.756  -8.193  1.00 74.83           O  
ANISOU 4232  O   ASP A 549     8746   9749   9936  -1210    613    412       O  
ATOM   4233  CB  ASP A 549     -15.176  14.224  -9.106  1.00 77.49           C  
ANISOU 4233  CB  ASP A 549     9262   9985  10196  -1062    542    234       C  
ATOM   4234  CG  ASP A 549     -14.129  15.309  -8.939  1.00 86.79           C  
ANISOU 4234  CG  ASP A 549    10520  11132  11323   -993    530    172       C  
ATOM   4235  OD1 ASP A 549     -13.194  15.111  -8.134  1.00 91.31           O  
ANISOU 4235  OD1 ASP A 549    11130  11706  11857   -990    556    190       O  
ATOM   4236  OD2 ASP A 549     -14.242  16.358  -9.607  1.00 89.69           O  
ANISOU 4236  OD2 ASP A 549    10913  11474  11694   -942    493    107       O  
ATOM   4237  N   ASP A 550     -15.428  10.942  -9.755  1.00 69.21           N  
ANISOU 4237  N   ASP A 550     8171   8832   9292  -1275    534    389       N  
ATOM   4238  CA  ASP A 550     -16.241   9.752  -9.978  1.00 66.44           C  
ANISOU 4238  CA  ASP A 550     7754   8473   9018  -1360    530    450       C  
ATOM   4239  C   ASP A 550     -16.177   8.820  -8.776  1.00 59.42           C  
ANISOU 4239  C   ASP A 550     6826   7629   8123  -1403    589    547       C  
ATOM   4240  O   ASP A 550     -17.178   8.193  -8.412  1.00 53.60           O  
ANISOU 4240  O   ASP A 550     5993   6946   7426  -1453    614    612       O  
ATOM   4241  CB  ASP A 550     -15.781   9.025 -11.242  1.00 68.08           C  
ANISOU 4241  CB  ASP A 550     8023   8553   9292  -1411    465    430       C  
ATOM   4242  CG  ASP A 550     -16.165   9.758 -12.511  1.00 75.46           C  
ANISOU 4242  CG  ASP A 550     8972   9457  10243  -1379    406    350       C  
ATOM   4243  OD1 ASP A 550     -16.760  10.852 -12.413  1.00 78.18           O  
ANISOU 4243  OD1 ASP A 550     9282   9871  10550  -1318    413    311       O  
ATOM   4244  OD2 ASP A 550     -15.868   9.241 -13.609  1.00 76.64           O  
ANISOU 4244  OD2 ASP A 550     9168   9514  10438  -1411    350    326       O  
ATOM   4245  N   PHE A 551     -15.004   8.719  -8.147  1.00 59.95           N  
ANISOU 4245  N   PHE A 551     6962   7676   8142  -1386    612    563       N  
ATOM   4246  CA  PHE A 551     -14.873   7.908  -6.942  1.00 61.39           C  
ANISOU 4246  CA  PHE A 551     7112   7907   8305  -1415    670    659       C  
ATOM   4247  C   PHE A 551     -15.537   8.583  -5.749  1.00 55.55           C  
ANISOU 4247  C   PHE A 551     6295   7319   7491  -1359    734    679       C  
ATOM   4248  O   PHE A 551     -16.122   7.909  -4.893  1.00 51.92           O  
ANISOU 4248  O   PHE A 551     5759   6934   7034  -1393    786    771       O  
ATOM   4249  CB  PHE A 551     -13.396   7.635  -6.656  1.00 59.44           C  
ANISOU 4249  CB  PHE A 551     6963   7597   8025  -1405    671    664       C  
ATOM   4250  CG  PHE A 551     -13.164   6.673  -5.528  1.00 74.74           C  
ANISOU 4250  CG  PHE A 551     8878   9570   9949  -1439    723    768       C  
ATOM   4251  CD1 PHE A 551     -13.588   5.358  -5.623  1.00 78.18           C  
ANISOU 4251  CD1 PHE A 551     9277   9961  10468  -1528    722    854       C  
ATOM   4252  CD2 PHE A 551     -12.522   7.083  -4.371  1.00 75.56           C  
ANISOU 4252  CD2 PHE A 551     9000   9750   9960  -1380    769    781       C  
ATOM   4253  CE1 PHE A 551     -13.376   4.470  -4.586  1.00 73.48           C  
ANISOU 4253  CE1 PHE A 551     8662   9394   9862  -1559    771    960       C  
ATOM   4254  CE2 PHE A 551     -12.307   6.199  -3.330  1.00 77.40           C  
ANISOU 4254  CE2 PHE A 551     9213  10020  10174  -1405    818    882       C  
ATOM   4255  CZ  PHE A 551     -12.734   4.891  -3.438  1.00 74.35           C  
ANISOU 4255  CZ  PHE A 551     8791   9588   9872  -1496    821    977       C  
ATOM   4256  N   ALA A 552     -15.457   9.915  -5.677  1.00 51.78           N  
ANISOU 4256  N   ALA A 552     5837   6888   6949  -1269    730    595       N  
ATOM   4257  CA  ALA A 552     -16.069  10.640  -4.569  1.00 57.36           C  
ANISOU 4257  CA  ALA A 552     6476   7742   7578  -1201    785    597       C  
ATOM   4258  C   ALA A 552     -17.583  10.466  -4.568  1.00 61.77           C  
ANISOU 4258  C   ALA A 552     6913   8385   8173  -1225    806    635       C  
ATOM   4259  O   ALA A 552     -18.182  10.151  -3.534  1.00 56.07           O  
ANISOU 4259  O   ALA A 552     6107   7779   7419  -1226    869    710       O  
ATOM   4260  CB  ALA A 552     -15.695  12.121  -4.641  1.00 49.54           C  
ANISOU 4260  CB  ALA A 552     5534   6762   6526  -1101    762    488       C  
ATOM   4261  N   ALA A 553     -18.219  10.668  -5.725  1.00 63.58           N  
ANISOU 4261  N   ALA A 553     7127   8563   8467  -1245    754    588       N  
ATOM   4262  CA  ALA A 553     -19.662  10.470  -5.815  1.00 59.23           C  
ANISOU 4262  CA  ALA A 553     6457   8088   7961  -1274    766    621       C  
ATOM   4263  C   ALA A 553     -20.039   9.012  -5.594  1.00 56.56           C  
ANISOU 4263  C   ALA A 553     6057   7739   7693  -1381    790    737       C  
ATOM   4264  O   ALA A 553     -21.133   8.722  -5.095  1.00 57.14           O  
ANISOU 4264  O   ALA A 553     6014   7914   7782  -1405    832    801       O  
ATOM   4265  CB  ALA A 553     -20.177  10.954  -7.171  1.00 63.73           C  
ANISOU 4265  CB  ALA A 553     7031   8596   8586  -1271    697    543       C  
ATOM   4266  N   PHE A 554     -19.151   8.084  -5.958  1.00 54.81           N  
ANISOU 4266  N   PHE A 554     5910   7395   7519  -1446    763    766       N  
ATOM   4267  CA  PHE A 554     -19.413   6.669  -5.722  1.00 57.89           C  
ANISOU 4267  CA  PHE A 554     6252   7759   7985  -1549    780    878       C  
ATOM   4268  C   PHE A 554     -19.473   6.349  -4.233  1.00 65.76           C  
ANISOU 4268  C   PHE A 554     7193   8871   8921  -1542    866    981       C  
ATOM   4269  O   PHE A 554     -20.254   5.486  -3.817  1.00 69.17           O  
ANISOU 4269  O   PHE A 554     7531   9347   9405  -1612    902   1086       O  
ATOM   4270  CB  PHE A 554     -18.341   5.824  -6.414  1.00 56.06           C  
ANISOU 4270  CB  PHE A 554     6123   7368   7808  -1603    729    876       C  
ATOM   4271  CG  PHE A 554     -18.224   4.426  -5.878  1.00 61.49           C  
ANISOU 4271  CG  PHE A 554     6790   8021   8552  -1691    754    995       C  
ATOM   4272  CD1 PHE A 554     -19.188   3.475  -6.168  1.00 70.31           C  
ANISOU 4272  CD1 PHE A 554     7822   9116   9777  -1785    741   1061       C  
ATOM   4273  CD2 PHE A 554     -17.144   4.060  -5.091  1.00 53.69           C  
ANISOU 4273  CD2 PHE A 554     5866   7019   7514  -1678    786   1042       C  
ATOM   4274  CE1 PHE A 554     -19.080   2.188  -5.679  1.00 75.11           C  
ANISOU 4274  CE1 PHE A 554     8412   9680  10446  -1869    761   1176       C  
ATOM   4275  CE2 PHE A 554     -17.031   2.773  -4.599  1.00 67.20           C  
ANISOU 4275  CE2 PHE A 554     7562   8693   9279  -1756    808   1157       C  
ATOM   4276  CZ  PHE A 554     -18.000   1.836  -4.895  1.00 74.52           C  
ANISOU 4276  CZ  PHE A 554     8406   9591  10319  -1852    795   1226       C  
ATOM   4277  N   VAL A 555     -18.671   7.036  -3.419  1.00 60.99           N  
ANISOU 4277  N   VAL A 555     6642   8322   8208  -1457    900    956       N  
ATOM   4278  CA  VAL A 555     -18.692   6.795  -1.980  1.00 61.73           C  
ANISOU 4278  CA  VAL A 555     6687   8540   8229  -1437    982   1048       C  
ATOM   4279  C   VAL A 555     -19.900   7.465  -1.338  1.00 60.32           C  
ANISOU 4279  C   VAL A 555     6390   8531   7999  -1384   1035   1057       C  
ATOM   4280  O   VAL A 555     -20.556   6.880  -0.470  1.00 58.46           O  
ANISOU 4280  O   VAL A 555     6058   8399   7755  -1413   1101   1168       O  
ATOM   4281  CB  VAL A 555     -17.373   7.269  -1.342  1.00 60.90           C  
ANISOU 4281  CB  VAL A 555     6682   8434   8025  -1362    992   1011       C  
ATOM   4282  CG1 VAL A 555     -17.426   7.111   0.171  1.00 56.72           C  
ANISOU 4282  CG1 VAL A 555     6100   8048   7403  -1325   1076   1099       C  
ATOM   4283  CG2 VAL A 555     -16.198   6.498  -1.921  1.00 57.23           C  
ANISOU 4283  CG2 VAL A 555     6323   7811   7611  -1416    946   1015       C  
ATOM   4284  N   GLU A 556     -20.217   8.695  -1.753  1.00 60.95           N  
ANISOU 4284  N   GLU A 556     6473   8642   8043  -1305   1008    944       N  
ATOM   4285  CA  GLU A 556     -21.365   9.395  -1.184  1.00 61.77           C  
ANISOU 4285  CA  GLU A 556     6466   8908   8096  -1243   1054    940       C  
ATOM   4286  C   GLU A 556     -22.669   8.680  -1.515  1.00 68.52           C  
ANISOU 4286  C   GLU A 556     7196   9794   9043  -1328   1064   1015       C  
ATOM   4287  O   GLU A 556     -23.594   8.649  -0.695  1.00 59.97           O  
ANISOU 4287  O   GLU A 556     5995   8862   7928  -1315   1131   1083       O  
ATOM   4288  CB  GLU A 556     -21.409  10.837  -1.691  1.00 64.14           C  
ANISOU 4288  CB  GLU A 556     6803   9212   8354  -1143   1011    798       C  
ATOM   4289  CG  GLU A 556     -20.131  11.625  -1.472  1.00 75.47           C  
ANISOU 4289  CG  GLU A 556     8359  10602   9712  -1065    991    715       C  
ATOM   4290  CD  GLU A 556     -19.504  11.356  -0.120  1.00 88.78           C  
ANISOU 4290  CD  GLU A 556    10053  12370  11308  -1033   1053    775       C  
ATOM   4291  OE1 GLU A 556     -18.439  10.705  -0.077  1.00 91.46           O  
ANISOU 4291  OE1 GLU A 556    10472  12622  11657  -1075   1044    807       O  
ATOM   4292  OE2 GLU A 556     -20.076  11.796   0.899  1.00 91.66           O  
ANISOU 4292  OE2 GLU A 556    10344  12894  11588   -962   1111    788       O  
ATOM   4293  N   LYS A 557     -22.760   8.099  -2.712  1.00 67.21           N  
ANISOU 4293  N   LYS A 557     7051   9492   8993  -1414    997   1003       N  
ATOM   4294  CA  LYS A 557     -23.996   7.443  -3.128  1.00 64.66           C  
ANISOU 4294  CA  LYS A 557     6610   9187   8771  -1499    993   1062       C  
ATOM   4295  C   LYS A 557     -24.258   6.186  -2.309  1.00 54.46           C  
ANISOU 4295  C   LYS A 557     5243   7933   7518  -1589   1053   1219       C  
ATOM   4296  O   LYS A 557     -25.332   6.032  -1.715  1.00 49.68           O  
ANISOU 4296  O   LYS A 557     4503   7458   6915  -1604   1110   1297       O  
ATOM   4297  CB  LYS A 557     -23.932   7.110  -4.620  1.00 66.16           C  
ANISOU 4297  CB  LYS A 557     6851   9216   9071  -1564    898   1003       C  
ATOM   4298  CG  LYS A 557     -25.077   6.240  -5.117  1.00 67.64           C  
ANISOU 4298  CG  LYS A 557     6926   9394   9380  -1669    880   1064       C  
ATOM   4299  CD  LYS A 557     -24.610   5.255  -6.182  1.00 72.68           C  
ANISOU 4299  CD  LYS A 557     7632   9852  10133  -1765    801   1058       C  
ATOM   4300  CE  LYS A 557     -23.652   5.904  -7.170  1.00 71.77           C  
ANISOU 4300  CE  LYS A 557     7655   9624   9992  -1709    730    932       C  
ATOM   4301  NZ  LYS A 557     -22.855   4.894  -7.921  1.00 71.35           N  
ANISOU 4301  NZ  LYS A 557     7689   9403  10018  -1786    670    936       N  
ATOM   4302  N   CYS A 558     -23.285   5.273  -2.263  1.00 62.31           N  
ANISOU 4302  N   CYS A 558     6318   8814   8543  -1648   1043   1271       N  
ATOM   4303  CA  CYS A 558     -23.492   4.000  -1.583  1.00 78.42           C  
ANISOU 4303  CA  CYS A 558     8295  10865  10636  -1741   1091   1427       C  
ATOM   4304  C   CYS A 558     -23.512   4.143  -0.067  1.00 69.21           C  
ANISOU 4304  C   CYS A 558     7076   9866   9354  -1684   1193   1515       C  
ATOM   4305  O   CYS A 558     -24.055   3.269   0.617  1.00 58.12           O  
ANISOU 4305  O   CYS A 558     5577   8522   7982  -1750   1251   1658       O  
ATOM   4306  CB  CYS A 558     -22.413   3.002  -2.006  1.00 85.65           C  
ANISOU 4306  CB  CYS A 558     9319  11604  11619  -1812   1044   1451       C  
ATOM   4307  SG  CYS A 558     -22.411   2.624  -3.777  1.00 89.10           S  
ANISOU 4307  SG  CYS A 558     9811  11847  12195  -1885    925   1359       S  
ATOM   4308  N   CYS A 559     -22.935   5.217   0.472  1.00 58.61           N  
ANISOU 4308  N   CYS A 559     5790   8600   7878  -1561   1214   1436       N  
ATOM   4309  CA  CYS A 559     -22.975   5.413   1.916  1.00 64.41           C  
ANISOU 4309  CA  CYS A 559     6474   9507   8491  -1493   1306   1508       C  
ATOM   4310  C   CYS A 559     -24.370   5.823   2.374  1.00 65.77           C  
ANISOU 4310  C   CYS A 559     6494   9858   8636  -1463   1364   1541       C  
ATOM   4311  O   CYS A 559     -24.840   5.377   3.428  1.00 60.82           O  
ANISOU 4311  O   CYS A 559     5772   9368   7967  -1470   1449   1667       O  
ATOM   4312  CB  CYS A 559     -21.942   6.458   2.338  1.00 54.76           C  
ANISOU 4312  CB  CYS A 559     5359   8310   7139  -1368   1302   1401       C  
ATOM   4313  SG  CYS A 559     -20.255   5.826   2.556  1.00 53.22           S  
ANISOU 4313  SG  CYS A 559     5309   7987   6926  -1384   1282   1421       S  
ATOM   4314  N   LYS A 560     -25.047   6.672   1.599  1.00 63.81           N  
ANISOU 4314  N   LYS A 560     6219   9619   8409  -1427   1322   1433       N  
ATOM   4315  CA  LYS A 560     -26.408   7.099   1.892  1.00 67.09           C  
ANISOU 4315  CA  LYS A 560     6486  10197   8807  -1397   1368   1451       C  
ATOM   4316  C   LYS A 560     -27.457   6.182   1.276  1.00 78.58           C  
ANISOU 4316  C   LYS A 560     7830  11619  10407  -1525   1355   1535       C  
ATOM   4317  O   LYS A 560     -28.638   6.535   1.269  1.00 89.53           O  
ANISOU 4317  O   LYS A 560     9092  13123  11802  -1510   1377   1537       O  
ATOM   4318  CB  LYS A 560     -26.620   8.534   1.402  1.00 65.30           C  
ANISOU 4318  CB  LYS A 560     6284  10000   8527  -1283   1326   1289       C  
ATOM   4319  CG  LYS A 560     -25.618   9.537   1.941  1.00 62.50           C  
ANISOU 4319  CG  LYS A 560     6037   9667   8041  -1156   1327   1191       C  
ATOM   4320  CD  LYS A 560     -25.980  10.956   1.543  1.00 52.53           C  
ANISOU 4320  CD  LYS A 560     4782   8444   6733  -1043   1290   1044       C  
ATOM   4321  CE  LYS A 560     -25.576  11.249   0.107  1.00 66.41           C  
ANISOU 4321  CE  LYS A 560     6637  10018   8576  -1072   1189    939       C  
ATOM   4322  NZ  LYS A 560     -25.965  12.626  -0.310  1.00 73.67           N  
ANISOU 4322  NZ  LYS A 560     7563  10969   9459   -963   1151    805       N  
ATOM   4323  N   ALA A 561     -27.058   5.013   0.778  1.00 74.36           N  
ANISOU 4323  N   ALA A 561     7336  10931   9988  -1648   1317   1602       N  
ATOM   4324  CA  ALA A 561     -27.971   4.108   0.098  1.00 70.02           C  
ANISOU 4324  CA  ALA A 561     6691  10322   9591  -1777   1289   1669       C  
ATOM   4325  C   ALA A 561     -28.833   3.349   1.106  1.00 87.07           C  
ANISOU 4325  C   ALA A 561     8700  12616  11764  -1835   1381   1841       C  
ATOM   4326  O   ALA A 561     -28.727   3.527   2.323  1.00 88.93           O  
ANISOU 4326  O   ALA A 561     8920  12988  11881  -1761   1464   1897       O  
ATOM   4327  CB  ALA A 561     -27.191   3.145  -0.792  1.00 56.92           C  
ANISOU 4327  CB  ALA A 561     5134   8442   8049  -1880   1209   1668       C  
ATOM   4328  N   ASP A 562     -29.699   2.483   0.581  1.00 99.60           N  
ANISOU 4328  N   ASP A 562    10233  14124  13487  -1929   1342   1873       N  
ATOM   4329  CA  ASP A 562     -30.630   1.714   1.397  1.00108.72           C  
ANISOU 4329  CA  ASP A 562    11297  15349  14662  -1958   1397   1981       C  
ATOM   4330  C   ASP A 562     -30.363   0.222   1.262  1.00116.11           C  
ANISOU 4330  C   ASP A 562    12296  16106  15714  -2064   1359   2049       C  
ATOM   4331  O   ASP A 562     -31.286  -0.555   0.998  1.00120.17           O  
ANISOU 4331  O   ASP A 562    12739  16580  16339  -2145   1338   2089       O  
ATOM   4332  CB  ASP A 562     -32.078   2.025   0.997  1.00109.63           C  
ANISOU 4332  CB  ASP A 562    11266  15554  14833  -1972   1393   1964       C  
ATOM   4333  CG  ASP A 562     -32.326   1.867  -0.503  1.00109.38           C  
ANISOU 4333  CG  ASP A 562    11241  15375  14943  -2053   1286   1881       C  
ATOM   4334  OD1 ASP A 562     -31.498   1.245  -1.203  1.00110.28           O  
ANISOU 4334  OD1 ASP A 562    11469  15302  15131  -2114   1214   1853       O  
ATOM   4335  OD2 ASP A 562     -33.371   2.360  -0.981  1.00106.83           O  
ANISOU 4335  OD2 ASP A 562    10807  15129  14655  -2050   1270   1842       O  
ATOM   4336  N   ASP A 563     -29.114  -0.195   1.444  1.00116.89           N  
ANISOU 4336  N   ASP A 563    12525  16100  15788  -2063   1347   2059       N  
ATOM   4337  CA  ASP A 563     -28.712  -1.537   1.052  1.00119.73           C  
ANISOU 4337  CA  ASP A 563    12963  16265  16265  -2158   1290   2092       C  
ATOM   4338  C   ASP A 563     -27.838  -2.147   2.142  1.00127.90           C  
ANISOU 4338  C   ASP A 563    14072  17295  17230  -2134   1341   2181       C  
ATOM   4339  O   ASP A 563     -27.729  -1.625   3.257  1.00129.07           O  
ANISOU 4339  O   ASP A 563    14195  17601  17245  -2052   1423   2229       O  
ATOM   4340  CB  ASP A 563     -27.992  -1.497  -0.301  1.00115.48           C  
ANISOU 4340  CB  ASP A 563    12525  15550  15801  -2193   1187   1979       C  
ATOM   4341  CG  ASP A 563     -26.600  -0.910  -0.198  1.00115.62           C  
ANISOU 4341  CG  ASP A 563    12662  15544  15722  -2126   1188   1933       C  
ATOM   4342  OD1 ASP A 563     -26.429   0.106   0.509  1.00117.32           O  
ANISOU 4342  OD1 ASP A 563    12855  15915  15806  -2036   1253   1930       O  
ATOM   4343  OD2 ASP A 563     -25.674  -1.469  -0.819  1.00113.74           O  
ANISOU 4343  OD2 ASP A 563    12542  15137  15538  -2161   1123   1896       O  
ATOM   4344  N   LYS A 564     -27.223  -3.278   1.800  1.00132.07           N  
ANISOU 4344  N   LYS A 564    14692  17643  17847  -2203   1287   2200       N  
ATOM   4345  CA  LYS A 564     -26.357  -4.057   2.683  1.00132.68           C  
ANISOU 4345  CA  LYS A 564    14847  17682  17883  -2194   1318   2285       C  
ATOM   4346  C   LYS A 564     -25.012  -4.189   1.977  1.00135.13           C  
ANISOU 4346  C   LYS A 564    15304  17829  18209  -2195   1249   2208       C  
ATOM   4347  O   LYS A 564     -24.692  -5.243   1.420  1.00140.16           O  
ANISOU 4347  O   LYS A 564    16007  18295  18952  -2263   1186   2208       O  
ATOM   4348  CB  LYS A 564     -26.969  -5.451   3.007  1.00131.64           C  
ANISOU 4348  CB  LYS A 564    14676  17488  17852  -2280   1320   2396       C  
ATOM   4349  CG  LYS A 564     -28.049  -5.469   4.091  1.00133.62           C  
ANISOU 4349  CG  LYS A 564    14796  17914  18059  -2268   1409   2508       C  
ATOM   4350  CD  LYS A 564     -29.284  -4.671   3.699  1.00131.96           C  
ANISOU 4350  CD  LYS A 564    14458  17817  17862  -2265   1418   2464       C  
ATOM   4351  CE  LYS A 564     -30.312  -4.632   4.814  1.00131.64           C  
ANISOU 4351  CE  LYS A 564    14289  17963  17766  -2241   1510   2574       C  
ATOM   4352  NZ  LYS A 564     -31.071  -5.909   4.909  1.00132.56           N  
ANISOU 4352  NZ  LYS A 564    14349  18013  18006  -2344   1503   2676       N  
ATOM   4353  N   GLU A 565     -24.237  -3.100   1.992  1.00129.54           N  
ANISOU 4353  N   GLU A 565    14646  17178  17396  -2115   1261   2140       N  
ATOM   4354  CA  GLU A 565     -22.938  -2.957   1.330  1.00121.50           C  
ANISOU 4354  CA  GLU A 565    13761  16032  16373  -2101   1202   2058       C  
ATOM   4355  C   GLU A 565     -22.860  -3.641  -0.033  1.00111.63           C  
ANISOU 4355  C   GLU A 565    12566  14583  15266  -2180   1098   1986       C  
ATOM   4356  O   GLU A 565     -21.763  -3.898  -0.540  1.00109.93           O  
ANISOU 4356  O   GLU A 565    12469  14236  15065  -2179   1046   1936       O  
ATOM   4357  CB  GLU A 565     -21.802  -3.466   2.232  1.00126.09           C  
ANISOU 4357  CB  GLU A 565    14432  16592  16884  -2066   1233   2121       C  
ATOM   4358  CG  GLU A 565     -21.842  -4.943   2.604  1.00129.00           C  
ANISOU 4358  CG  GLU A 565    14819  16867  17330  -2129   1228   2218       C  
ATOM   4359  CD  GLU A 565     -22.396  -5.197   3.998  1.00129.66           C  
ANISOU 4359  CD  GLU A 565    14823  17099  17345  -2105   1319   2348       C  
ATOM   4360  OE1 GLU A 565     -23.451  -4.628   4.346  1.00130.72           O  
ANISOU 4360  OE1 GLU A 565    14841  17380  17445  -2088   1369   2370       O  
ATOM   4361  OE2 GLU A 565     -21.774  -5.976   4.750  1.00129.62           O  
ANISOU 4361  OE2 GLU A 565    14869  17064  17316  -2100   1340   2430       O  
ATOM   4362  N   THR A 566     -24.013  -3.918  -0.644  1.00106.24           N  
ANISOU 4362  N   THR A 566    11798  13883  14685  -2243   1066   1977       N  
ATOM   4363  CA  THR A 566     -24.058  -4.442  -2.000  1.00102.51           C  
ANISOU 4363  CA  THR A 566    11368  13242  14341  -2309    964   1894       C  
ATOM   4364  C   THR A 566     -23.894  -3.349  -3.044  1.00 96.75           C  
ANISOU 4364  C   THR A 566    10656  12505  13600  -2281    912   1771       C  
ATOM   4365  O   THR A 566     -23.734  -3.662  -4.228  1.00 83.81           O  
ANISOU 4365  O   THR A 566     9069  10726  12048  -2320    822   1687       O  
ATOM   4366  CB  THR A 566     -25.374  -5.194  -2.233  1.00106.47           C  
ANISOU 4366  CB  THR A 566    11767  13730  14957  -2390    946   1932       C  
ATOM   4367  OG1 THR A 566     -25.314  -5.902  -3.477  1.00108.30           O  
ANISOU 4367  OG1 THR A 566    12052  13787  15312  -2453    843   1856       O  
ATOM   4368  CG2 THR A 566     -26.549  -4.228  -2.261  1.00104.31           C  
ANISOU 4368  CG2 THR A 566    11361  13610  14664  -2374    977   1917       C  
ATOM   4369  N   CYS A 567     -23.923  -2.080  -2.629  1.00102.05           N  
ANISOU 4369  N   CYS A 567    11285  13326  14163  -2210    966   1757       N  
ATOM   4370  CA  CYS A 567     -23.690  -0.978  -3.554  1.00 99.26           C  
ANISOU 4370  CA  CYS A 567    10951  12971  13790  -2179    920   1647       C  
ATOM   4371  C   CYS A 567     -22.213  -0.847  -3.901  1.00 94.12           C  
ANISOU 4371  C   CYS A 567    10443  12214  13103  -2150    883   1592       C  
ATOM   4372  O   CYS A 567     -21.865  -0.649  -5.070  1.00 96.35           O  
ANISOU 4372  O   CYS A 567    10791  12389  13430  -2157    801   1490       O  
ATOM   4373  CB  CYS A 567     -24.214   0.328  -2.957  1.00 99.36           C  
ANISOU 4373  CB  CYS A 567    10869  13187  13697  -2110    990   1651       C  
ATOM   4374  SG  CYS A 567     -24.207   1.729  -4.098  1.00 91.92           S  
ANISOU 4374  SG  CYS A 567     9985  12233  12707  -2014    920   1453       S  
ATOM   4375  N   PHE A 568     -21.394  -0.850  -2.865  1.00 88.33           N  
ANISOU 4375  N   PHE A 568     9767  11513  12282  -2107    939   1649       N  
ATOM   4376  CA  PHE A 568     -19.942  -0.687  -3.049  1.00 91.73           C  
ANISOU 4376  CA  PHE A 568    10332  11847  12675  -2076    907   1600       C  
ATOM   4377  C   PHE A 568     -19.421  -1.854  -3.876  1.00102.20           C  
ANISOU 4377  C   PHE A 568    11749  12975  14107  -2131    826   1569       C  
ATOM   4378  O   PHE A 568     -18.368  -1.741  -4.513  1.00103.13           O  
ANISOU 4378  O   PHE A 568    11971  12994  14221  -2114    773   1497       O  
ATOM   4379  CB  PHE A 568     -19.298  -0.628  -1.666  1.00 84.11           C  
ANISOU 4379  CB  PHE A 568     9397  10967  11595  -2019    984   1674       C  
ATOM   4380  CG  PHE A 568     -19.289   0.737  -1.034  1.00 79.57           C  
ANISOU 4380  CG  PHE A 568     8801  10558  10873  -1904   1041   1622       C  
ATOM   4381  CD1 PHE A 568     -18.366   1.689  -1.425  1.00 80.50           C  
ANISOU 4381  CD1 PHE A 568     9019  10662  10906  -1809   1011   1489       C  
ATOM   4382  CD2 PHE A 568     -20.190   1.064  -0.039  1.00 78.36           C  
ANISOU 4382  CD2 PHE A 568     8528  10578  10669  -1888   1123   1707       C  
ATOM   4383  CE1 PHE A 568     -18.348   2.944  -0.844  1.00 77.61           C  
ANISOU 4383  CE1 PHE A 568     8637  10439  10413  -1702   1054   1435       C  
ATOM   4384  CE2 PHE A 568     -20.165   2.317   0.549  1.00 77.36           C  
ANISOU 4384  CE2 PHE A 568     8384  10604  10406  -1773   1170   1650       C  
ATOM   4385  CZ  PHE A 568     -19.252   3.257   0.139  1.00 74.04           C  
ANISOU 4385  CZ  PHE A 568     8067  10156   9908  -1680   1132   1510       C  
ATOM   4386  N   GLU A 570     -21.387  -3.780  -6.301  1.00111.73           N  
ANISOU 4386  N   GLU A 570    12881  13931  15639  -2309    646   1483       N  
ATOM   4387  CA  GLU A 570     -21.893  -3.694  -7.687  1.00101.51           C  
ANISOU 4387  CA  GLU A 570    11572  12573  14426  -2340    558   1384       C  
ATOM   4388  C   GLU A 570     -21.228  -2.514  -8.382  1.00 94.01           C  
ANISOU 4388  C   GLU A 570    10667  11635  13417  -2287    529   1291       C  
ATOM   4389  O   GLU A 570     -20.554  -2.726  -9.402  1.00 83.11           O  
ANISOU 4389  O   GLU A 570     9367  10138  12074  -2287    446   1199       O  
ATOM   4390  CB  GLU A 570     -23.401  -3.443  -7.665  1.00100.08           C  
ANISOU 4390  CB  GLU A 570    11245  12486  14295  -2381    573   1414       C  
ATOM   4391  CG  GLU A 570     -24.203  -4.490  -8.414  1.00101.75           C  
ANISOU 4391  CG  GLU A 570    11428  12599  14635  -2461    515   1418       C  
ATOM   4392  CD  GLU A 570     -25.595  -4.027  -8.809  1.00106.61           C  
ANISOU 4392  CD  GLU A 570    11913  13284  15311  -2498    495   1399       C  
ATOM   4393  OE1 GLU A 570     -26.382  -4.861  -9.298  1.00108.11           O  
ANISOU 4393  OE1 GLU A 570    12065  13405  15607  -2566    447   1400       O  
ATOM   4394  OE2 GLU A 570     -25.887  -2.833  -8.623  1.00107.34           O  
ANISOU 4394  OE2 GLU A 570    11937  13502  15344  -2457    527   1383       O  
ATOM   4395  N   GLU A 571     -21.431  -1.320  -7.839  1.00 95.58           N  
ANISOU 4395  N   GLU A 571    10819  11978  13519  -2237    595   1315       N  
ATOM   4396  CA  GLU A 571     -20.910  -0.104  -8.494  1.00 91.87           C  
ANISOU 4396  CA  GLU A 571    10425  11527  12954  -2133    570   1179       C  
ATOM   4397  C   GLU A 571     -19.386  -0.075  -8.441  1.00 91.87           C  
ANISOU 4397  C   GLU A 571    10567  11459  12881  -2075    566   1138       C  
ATOM   4398  O   GLU A 571     -18.823   0.864  -9.016  1.00 92.79           O  
ANISOU 4398  O   GLU A 571    10755  11578  12924  -1993    543   1032       O  
ATOM   4399  CB  GLU A 571     -21.647   1.138  -7.997  1.00 92.73           C  
ANISOU 4399  CB  GLU A 571    10461  11810  12963  -2056    637   1170       C  
ATOM   4400  CG  GLU A 571     -23.084   0.876  -7.599  1.00 99.45           C  
ANISOU 4400  CG  GLU A 571    11156  12758  13873  -2103    655   1218       C  
ATOM   4401  CD  GLU A 571     -24.092   0.902  -8.730  1.00107.17           C  
ANISOU 4401  CD  GLU A 571    12099  13655  14968  -2163    564   1156       C  
ATOM   4402  OE1 GLU A 571     -24.707   1.964  -8.946  1.00109.65           O  
ANISOU 4402  OE1 GLU A 571    12355  14043  15261  -2120    549   1088       O  
ATOM   4403  OE2 GLU A 571     -24.263  -0.142  -9.385  1.00110.57           O  
ANISOU 4403  OE2 GLU A 571    12550  13952  15510  -2251    505   1176       O  
ATOM   4404  N   GLY A 572     -18.743  -1.058  -7.796  1.00 96.94           N  
ANISOU 4404  N   GLY A 572    11249  12038  13546  -2116    584   1224       N  
ATOM   4405  CA  GLY A 572     -17.290  -1.036  -7.872  1.00 99.91           C  
ANISOU 4405  CA  GLY A 572    11757  12340  13866  -2066    570   1182       C  
ATOM   4406  C   GLY A 572     -16.787  -1.354  -9.268  1.00104.85           C  
ANISOU 4406  C   GLY A 572    12467  12819  14552  -2078    474   1084       C  
ATOM   4407  O   GLY A 572     -15.972  -0.618  -9.832  1.00107.69           O  
ANISOU 4407  O   GLY A 572    12916  13158  14845  -2005    449    987       O  
ATOM   4408  N   LYS A 573     -17.231  -2.472  -9.825  1.00103.03           N  
ANISOU 4408  N   LYS A 573    12208  12488  14452  -2168    417   1108       N  
ATOM   4409  CA  LYS A 573     -16.739  -2.857 -11.162  1.00 98.47           C  
ANISOU 4409  CA  LYS A 573    11702  11778  13933  -2176    319   1007       C  
ATOM   4410  C   LYS A 573     -17.381  -1.895 -12.156  1.00 98.40           C  
ANISOU 4410  C   LYS A 573    11674  11807  13905  -2134    276    895       C  
ATOM   4411  O   LYS A 573     -16.882  -1.778 -13.280  1.00 97.02           O  
ANISOU 4411  O   LYS A 573    11572  11549  13743  -2112    202    796       O  
ATOM   4412  CB  LYS A 573     -17.117  -4.312 -11.439  1.00 95.55           C  
ANISOU 4412  CB  LYS A 573    11328  11307  13669  -2232    273   1013       C  
ATOM   4413  CG  LYS A 573     -17.593  -5.100 -10.228  1.00 93.26           C  
ANISOU 4413  CG  LYS A 573    11071  10983  13379  -2242    316   1099       C  
ATOM   4414  CD  LYS A 573     -18.489  -6.264 -10.582  1.00 91.59           C  
ANISOU 4414  CD  LYS A 573    10817  10709  13275  -2309    286   1130       C  
ATOM   4415  CE  LYS A 573     -19.948  -6.005 -10.276  1.00 92.91           C  
ANISOU 4415  CE  LYS A 573    10859  10989  13451  -2348    355   1230       C  
ATOM   4416  NZ  LYS A 573     -20.564  -5.072 -11.250  1.00 95.34           N  
ANISOU 4416  NZ  LYS A 573    11069  11386  13769  -2358    346   1193       N  
ATOM   4417  N   LYS A 574     -18.420  -1.199 -11.718  1.00 98.71           N  
ANISOU 4417  N   LYS A 574    11618  11974  13912  -2119    320    909       N  
ATOM   4418  CA  LYS A 574     -19.168  -0.345 -12.661  1.00104.36           C  
ANISOU 4418  CA  LYS A 574    12313  12732  14607  -2073    280    807       C  
ATOM   4419  C   LYS A 574     -18.372   0.897 -13.034  1.00114.59           C  
ANISOU 4419  C   LYS A 574    13719  14019  15800  -1974    267    709       C  
ATOM   4420  O   LYS A 574     -17.928   0.982 -14.190  1.00114.99           O  
ANISOU 4420  O   LYS A 574    13822  14004  15865  -1953    194    617       O  
ATOM   4421  CB  LYS A 574     -20.442   0.148 -11.988  1.00101.14           C  
ANISOU 4421  CB  LYS A 574    11786  12474  14169  -2060    340    845       C  
ATOM   4422  CG  LYS A 574     -21.671  -0.723 -12.201  1.00101.69           C  
ANISOU 4422  CG  LYS A 574    11727  12563  14349  -2158    340    925       C  
ATOM   4423  CD  LYS A 574     -22.912   0.098 -12.430  1.00101.47           C  
ANISOU 4423  CD  LYS A 574    11623  12577  14356  -2155    292    855       C  
ATOM   4424  CE  LYS A 574     -22.699   1.563 -12.118  1.00102.09           C  
ANISOU 4424  CE  LYS A 574    11654  12808  14328  -2069    355    841       C  
ATOM   4425  NZ  LYS A 574     -23.985   2.272 -11.923  1.00104.81           N  
ANISOU 4425  NZ  LYS A 574    11864  13237  14722  -2094    347    842       N  
ATOM   4426  N   LEU A 575     -18.218   1.827 -12.094  1.00124.10           N  
ANISOU 4426  N   LEU A 575    14958  15292  16902  -1911    336    730       N  
ATOM   4427  CA  LEU A 575     -17.574   3.125 -12.416  1.00131.01           C  
ANISOU 4427  CA  LEU A 575    15923  16173  17683  -1818    330    643       C  
ATOM   4428  C   LEU A 575     -16.059   2.968 -12.597  1.00137.74           C  
ANISOU 4428  C   LEU A 575    16886  16948  18501  -1799    331    643       C  
ATOM   4429  O   LEU A 575     -15.457   3.880 -13.165  1.00141.21           O  
ANISOU 4429  O   LEU A 575    17400  17387  18865  -1727    329    581       O  
ATOM   4430  CB  LEU A 575     -17.904   4.097 -11.284  1.00129.27           C  
ANISOU 4430  CB  LEU A 575    15661  16085  17369  -1748    394    642       C  
ATOM   4431  CG  LEU A 575     -19.080   5.037 -11.543  1.00125.41           C  
ANISOU 4431  CG  LEU A 575    15055  15699  16897  -1751    407    647       C  
ATOM   4432  CD1 LEU A 575     -18.599   6.467 -11.727  1.00123.58           C  
ANISOU 4432  CD1 LEU A 575    14826  15562  16566  -1652    437    591       C  
ATOM   4433  CD2 LEU A 575     -19.897   4.592 -12.747  1.00123.31           C  
ANISOU 4433  CD2 LEU A 575    14750  15382  16720  -1795    331    601       C  
ATOM   4434  N   VAL A 576     -15.457   1.886 -12.096  1.00139.82           N  
ANISOU 4434  N   VAL A 576    17159  17144  18821  -1862    333    715       N  
ATOM   4435  CA  VAL A 576     -14.009   1.642 -12.341  1.00139.35           C  
ANISOU 4435  CA  VAL A 576    17207  16979  18762  -1853    300    692       C  
ATOM   4436  C   VAL A 576     -13.790   1.547 -13.853  1.00131.60           C  
ANISOU 4436  C   VAL A 576    16271  15913  17817  -1846    215    594       C  
ATOM   4437  O   VAL A 576     -12.826   2.148 -14.348  1.00133.87           O  
ANISOU 4437  O   VAL A 576    16650  16152  18061  -1796    190    533       O  
ATOM   4438  CB  VAL A 576     -13.526   0.371 -11.623  1.00143.72           C  
ANISOU 4438  CB  VAL A 576    17755  17466  19385  -1925    310    788       C  
ATOM   4439  CG1 VAL A 576     -12.496  -0.425 -12.411  1.00144.54           C  
ANISOU 4439  CG1 VAL A 576    17958  17438  19524  -1928    250    749       C  
ATOM   4440  CG2 VAL A 576     -12.986   0.701 -10.244  1.00145.27           C  
ANISOU 4440  CG2 VAL A 576    17942  17742  19512  -1906    395    875       C  
ATOM   4441  N   ALA A 577     -14.674   0.829 -14.556  1.00115.69           N  
ANISOU 4441  N   ALA A 577    14189  13889  15879  -1892    169    576       N  
ATOM   4442  CA  ALA A 577     -14.529   0.687 -16.011  1.00100.34           C  
ANISOU 4442  CA  ALA A 577    12278  11888  13960  -1875     86    477       C  
ATOM   4443  C   ALA A 577     -14.700   2.070 -16.593  1.00 91.38           C  
ANISOU 4443  C   ALA A 577    11151  10829  12741  -1795     91    405       C  
ATOM   4444  O   ALA A 577     -14.057   2.372 -17.596  1.00 87.27           O  
ANISOU 4444  O   ALA A 577    10701  10270  12187  -1745     46    327       O  
ATOM   4445  CB  ALA A 577     -15.608  -0.209 -16.522  1.00100.99           C  
ANISOU 4445  CB  ALA A 577    12281  11934  14158  -1954     29    480       C  
ATOM   4446  N   ALA A 578     -15.583   2.849 -15.983  1.00 90.46           N  
ANISOU 4446  N   ALA A 578    10961  10822  12588  -1778    144    433       N  
ATOM   4447  CA  ALA A 578     -15.853   4.195 -16.516  1.00 91.23           C  
ANISOU 4447  CA  ALA A 578    11058  10985  12620  -1703    141    366       C  
ATOM   4448  C   ALA A 578     -14.607   5.050 -16.330  1.00 92.97           C  
ANISOU 4448  C   ALA A 578    11369  11211  12744  -1626    169    336       C  
ATOM   4449  O   ALA A 578     -14.492   6.081 -17.008  1.00 88.43           O  
ANISOU 4449  O   ALA A 578    10828  10646  12124  -1564    145    270       O  
ATOM   4450  CB  ALA A 578     -17.042   4.793 -15.829  1.00 92.28           C  
ANISOU 4450  CB  ALA A 578    11083  11232  12745  -1703    187    400       C  
ATOM   4451  N   SER A 579     -13.718   4.640 -15.433  1.00 98.15           N  
ANISOU 4451  N   SER A 579    12061  11864  13369  -1627    219    388       N  
ATOM   4452  CA  SER A 579     -12.484   5.413 -15.337  1.00105.38           C  
ANISOU 4452  CA  SER A 579    13060  12776  14202  -1561    240    359       C  
ATOM   4453  C   SER A 579     -11.390   4.852 -16.238  1.00105.27           C  
ANISOU 4453  C   SER A 579    13138  12662  14197  -1557    194    325       C  
ATOM   4454  O   SER A 579     -10.479   5.590 -16.636  1.00105.60           O  
ANISOU 4454  O   SER A 579    13249  12694  14181  -1500    192    282       O  
ATOM   4455  CB  SER A 579     -12.001   5.469 -13.893  1.00107.18           C  
ANISOU 4455  CB  SER A 579    13283  13056  14384  -1554    312    423       C  
ATOM   4456  OG  SER A 579     -13.080   5.699 -13.001  1.00108.13           O  
ANISOU 4456  OG  SER A 579    13309  13272  14504  -1565    356    467       O  
ATOM   4457  N   GLN A 580     -11.456   3.559 -16.569  1.00103.67           N  
ANISOU 4457  N   GLN A 580    12937  12384  14069  -1617    157    342       N  
ATOM   4458  CA  GLN A 580     -10.642   3.036 -17.658  1.00100.10           C  
ANISOU 4458  CA  GLN A 580    12563  11841  13629  -1607     99    292       C  
ATOM   4459  C   GLN A 580     -11.033   3.656 -18.992  1.00103.63           C  
ANISOU 4459  C   GLN A 580    13020  12288  14066  -1569     44    210       C  
ATOM   4460  O   GLN A 580     -10.232   3.630 -19.932  1.00105.53           O  
ANISOU 4460  O   GLN A 580    13333  12481  14284  -1532      7    160       O  
ATOM   4461  CB  GLN A 580     -10.758   1.513 -17.726  1.00 98.19           C  
ANISOU 4461  CB  GLN A 580    12316  11514  13477  -1677     63    321       C  
ATOM   4462  CG  GLN A 580      -9.862   0.777 -16.738  1.00100.68           C  
ANISOU 4462  CG  GLN A 580    12664  11798  13793  -1697    103    390       C  
ATOM   4463  CD  GLN A 580      -9.885  -0.726 -16.932  1.00106.76           C  
ANISOU 4463  CD  GLN A 580    13440  12466  14658  -1761     57    414       C  
ATOM   4464  OE1 GLN A 580     -10.468  -1.230 -17.891  1.00112.90           O  
ANISOU 4464  OE1 GLN A 580    14206  13190  15502  -1787    -11    367       O  
ATOM   4465  NE2 GLN A 580      -9.251  -1.452 -16.016  1.00104.27           N  
ANISOU 4465  NE2 GLN A 580    13144  12121  14353  -1784     91    485       N  
ATOM   4466  N   ALA A 581     -12.246   4.207 -19.093  1.00103.36           N  
ANISOU 4466  N   ALA A 581    12913  12313  14045  -1572     38    199       N  
ATOM   4467  CA  ALA A 581     -12.624   4.993 -20.260  1.00101.48           C  
ANISOU 4467  CA  ALA A 581    12683  12091  13784  -1524     -8    128       C  
ATOM   4468  C   ALA A 581     -11.939   6.354 -20.279  1.00 98.22           C  
ANISOU 4468  C   ALA A 581    12318  11720  13283  -1446     24    106       C  
ATOM   4469  O   ALA A 581     -11.890   6.997 -21.333  1.00 98.95           O  
ANISOU 4469  O   ALA A 581    12441  11811  13344  -1397    -12     52       O  
ATOM   4470  CB  ALA A 581     -14.142   5.170 -20.305  1.00100.43           C  
ANISOU 4470  CB  ALA A 581    12452  12013  13695  -1548    -25    125       C  
ATOM   4471  N   ALA A 582     -11.415   6.804 -19.143  1.00 97.01           N  
ANISOU 4471  N   ALA A 582    12170  11602  13088  -1434     89    148       N  
ATOM   4472  CA  ALA A 582     -10.697   8.071 -19.073  1.00 96.02           C  
ANISOU 4472  CA  ALA A 582    12090  11506  12889  -1366    117    129       C  
ATOM   4473  C   ALA A 582      -9.297   7.868 -18.503  1.00 93.22           C  
ANISOU 4473  C   ALA A 582    11798  11120  12500  -1359    150    154       C  
ATOM   4474  O   ALA A 582      -8.520   7.060 -19.013  1.00 91.90           O  
ANISOU 4474  O   ALA A 582    11684  10889  12346  -1372    126    148       O  
ATOM   4475  CB  ALA A 582     -11.471   9.078 -18.235  1.00 93.31           C  
ANISOU 4475  CB  ALA A 582    11685  11247  12521  -1342    157    140       C  
TER    4476      ALA A 582                                                      
ATOM   4477  N   LYS B   4      28.131  -7.566 -71.778  1.00 96.24           N  
ANISOU 4477  N   LYS B   4    12870  16008   7689   4523   -115  -1674       N  
ATOM   4478  CA  LYS B   4      27.712  -6.628 -70.743  1.00 99.88           C  
ANISOU 4478  CA  LYS B   4    13346  16362   8241   4328    -45  -1549       C  
ATOM   4479  C   LYS B   4      28.752  -5.528 -70.542  1.00104.96           C  
ANISOU 4479  C   LYS B   4    13896  17141   8843   4271    133  -1312       C  
ATOM   4480  O   LYS B   4      29.939  -5.730 -70.792  1.00104.67           O  
ANISOU 4480  O   LYS B   4    13792  17228   8750   4357    196  -1267       O  
ATOM   4481  CB  LYS B   4      27.460  -7.365 -69.423  1.00 96.44           C  
ANISOU 4481  CB  LYS B   4    12985  15691   7965   4217   -113  -1664       C  
ATOM   4482  CG  LYS B   4      26.567  -6.612 -68.447  1.00 94.13           C  
ANISOU 4482  CG  LYS B   4    12738  15254   7776   4028    -96  -1600       C  
ATOM   4483  CD  LYS B   4      25.095  -6.841 -68.752  1.00 94.10           C  
ANISOU 4483  CD  LYS B   4    12807  15143   7805   4014   -231  -1730       C  
ATOM   4484  CE  LYS B   4      24.236  -6.639 -67.513  1.00 94.45           C  
ANISOU 4484  CE  LYS B   4    12917  14978   7991   3833   -261  -1742       C  
ATOM   4485  NZ  LYS B   4      24.670  -7.509 -66.384  1.00 91.35           N  
ANISOU 4485  NZ  LYS B   4    12562  14424   7723   3780   -291  -1830       N  
ATOM   4486  N   SER B   5      28.289  -4.362 -70.093  1.00109.15           N  
ANISOU 4486  N   SER B   5    14419  17643   9408   4126    208  -1159       N  
ATOM   4487  CA  SER B   5      29.154  -3.228 -69.789  1.00106.46           C  
ANISOU 4487  CA  SER B   5    13993  17401   9057   4041    372   -923       C  
ATOM   4488  C   SER B   5      28.391  -2.217 -68.939  1.00102.44           C  
ANISOU 4488  C   SER B   5    13511  16776   8634   3854    413   -811       C  
ATOM   4489  O   SER B   5      28.978  -1.272 -68.402  1.00 97.59           O  
ANISOU 4489  O   SER B   5    12837  16190   8051   3746    538   -621       O  
ATOM   4490  CB  SER B   5      29.667  -2.591 -71.080  1.00 99.56           C  
ANISOU 4490  CB  SER B   5    13030  16757   8040   4153    447   -794       C  
ATOM   4491  OG  SER B   5      29.840  -1.196 -70.928  1.00 88.22           O  
ANISOU 4491  OG  SER B   5    11533  15378   6609   4037    577   -560       O  
ATOM   4492  N   GLU B   6      27.069  -2.398 -68.863  1.00 94.62           N  
ANISOU 4492  N   GLU B   6    12607  15660   7684   3819    303   -927       N  
ATOM   4493  CA  GLU B   6      26.169  -1.695 -67.948  1.00 87.68           C  
ANISOU 4493  CA  GLU B   6    11776  14639   6901   3648    307   -872       C  
ATOM   4494  C   GLU B   6      25.888  -0.251 -68.357  1.00 74.05           C  
ANISOU 4494  C   GLU B   6    10002  13006   5126   3587    399   -665       C  
ATOM   4495  O   GLU B   6      24.726   0.109 -68.569  1.00 75.45           O  
ANISOU 4495  O   GLU B   6    10227  13136   5304   3555    340   -686       O  
ATOM   4496  CB  GLU B   6      26.706  -1.748 -66.513  1.00 88.61           C  
ANISOU 4496  CB  GLU B   6    11900  14633   7136   3519    359   -838       C  
ATOM   4497  CG  GLU B   6      26.280  -2.999 -65.763  1.00 95.06           C  
ANISOU 4497  CG  GLU B   6    12806  15263   8051   3511    233  -1055       C  
ATOM   4498  CD  GLU B   6      24.814  -2.971 -65.373  1.00106.85           C  
ANISOU 4498  CD  GLU B   6    14386  16595   9616   3423    131  -1144       C  
ATOM   4499  OE1 GLU B   6      24.172  -4.044 -65.381  1.00111.92           O  
ANISOU 4499  OE1 GLU B   6    15099  17119  10308   3464     -9  -1347       O  
ATOM   4500  OE2 GLU B   6      24.303  -1.877 -65.053  1.00108.90           O  
ANISOU 4500  OE2 GLU B   6    14642  16844   9891   3309    188  -1008       O  
ATOM   4501  N   VAL B   7      26.926   0.582 -68.480  1.00 64.68           N  
ANISOU 4501  N   VAL B   7     8722  11947   3906   3568    539   -464       N  
ATOM   4502  CA  VAL B   7      26.699   1.990 -68.806  1.00 66.20           C  
ANISOU 4502  CA  VAL B   7     8868  12211   4073   3497    628   -255       C  
ATOM   4503  C   VAL B   7      26.028   2.138 -70.168  1.00 64.61           C  
ANISOU 4503  C   VAL B   7     8670  12124   3756   3618    578   -279       C  
ATOM   4504  O   VAL B   7      25.176   3.017 -70.356  1.00 64.21           O  
ANISOU 4504  O   VAL B   7     8633  12061   3703   3559    581   -195       O  
ATOM   4505  CB  VAL B   7      28.021   2.783 -68.726  1.00 85.40           C  
ANISOU 4505  CB  VAL B   7    11190  14754   6502   3456    781    -39       C  
ATOM   4506  CG1 VAL B   7      29.108   2.112 -69.546  1.00 98.43           C  
ANISOU 4506  CG1 VAL B   7    12778  16563   8059   3616    799    -76       C  
ATOM   4507  CG2 VAL B   7      27.813   4.233 -69.160  1.00 85.94           C  
ANISOU 4507  CG2 VAL B   7    11208  14893   6552   3389    868    180       C  
ATOM   4508  N   ALA B   8      26.381   1.288 -71.135  1.00 66.28           N  
ANISOU 4508  N   ALA B   8     8867  12446   3870   3792    528   -395       N  
ATOM   4509  CA  ALA B   8      25.633   1.251 -72.387  1.00 70.27           C  
ANISOU 4509  CA  ALA B   8     9385  13044   4269   3917    458   -456       C  
ATOM   4510  C   ALA B   8      24.382   0.387 -72.282  1.00 78.67           C  
ANISOU 4510  C   ALA B   8    10552  13968   5372   3933    296   -681       C  
ATOM   4511  O   ALA B   8      23.452   0.571 -73.075  1.00 81.14           O  
ANISOU 4511  O   ALA B   8    10888  14315   5628   3988    233   -719       O  
ATOM   4512  CB  ALA B   8      26.523   0.745 -73.528  1.00 69.98           C  
ANISOU 4512  CB  ALA B   8     9286  13198   4106   4105    471   -480       C  
ATOM   4513  N   HIS B   9      24.333  -0.542 -71.320  1.00 83.33           N  
ANISOU 4513  N   HIS B   9    11200  14397   6064   3885    227   -829       N  
ATOM   4514  CA  HIS B   9      23.127  -1.345 -71.123  1.00 96.57           C  
ANISOU 4514  CA  HIS B   9    12971  15918   7802   3879     70  -1037       C  
ATOM   4515  C   HIS B   9      22.007  -0.525 -70.494  1.00 90.67           C  
ANISOU 4515  C   HIS B   9    12269  15053   7127   3728     59   -979       C  
ATOM   4516  O   HIS B   9      20.827  -0.811 -70.726  1.00 95.31           O  
ANISOU 4516  O   HIS B   9    12916  15566   7732   3736    -59  -1106       O  
ATOM   4517  CB  HIS B   9      23.434  -2.571 -70.256  1.00105.10           C  
ANISOU 4517  CB  HIS B   9    14099  16852   8981   3867      0  -1203       C  
ATOM   4518  CG  HIS B   9      22.243  -3.445 -69.990  1.00108.25           C  
ANISOU 4518  CG  HIS B   9    14590  17074   9466   3848   -164  -1415       C  
ATOM   4519  ND1 HIS B   9      22.025  -4.059 -68.774  1.00107.52           N  
ANISOU 4519  ND1 HIS B   9    14557  16780   9514   3741   -219  -1512       N  
ATOM   4520  CD2 HIS B   9      21.210  -3.812 -70.785  1.00110.58           C  
ANISOU 4520  CD2 HIS B   9    14922  17360   9733   3919   -287  -1545       C  
ATOM   4521  CE1 HIS B   9      20.908  -4.762 -68.831  1.00106.75           C  
ANISOU 4521  CE1 HIS B   9    14528  16553   9479   3741   -369  -1690       C  
ATOM   4522  NE2 HIS B   9      20.393  -4.629 -70.040  1.00109.37           N  
ANISOU 4522  NE2 HIS B   9    14846  16997   9711   3848   -414  -1714       N  
ATOM   4523  N   ARG B  10      22.351   0.491 -69.698  1.00 84.65           N  
ANISOU 4523  N   ARG B  10    11477  14273   6413   3590    178   -791       N  
ATOM   4524  CA  ARG B  10      21.328   1.345 -69.102  1.00 80.53           C  
ANISOU 4524  CA  ARG B  10    10994  13648   5955   3450    174   -721       C  
ATOM   4525  C   ARG B  10      20.876   2.432 -70.069  1.00 74.14           C  
ANISOU 4525  C   ARG B  10    10149  12963   5056   3478    214   -582       C  
ATOM   4526  O   ARG B  10      19.685   2.760 -70.121  1.00 67.71           O  
ANISOU 4526  O   ARG B  10     9382  12088   4258   3438    145   -611       O  
ATOM   4527  CB  ARG B  10      21.844   1.969 -67.805  1.00 74.57           C  
ANISOU 4527  CB  ARG B  10    10225  12811   5298   3289    276   -581       C  
ATOM   4528  CG  ARG B  10      22.314   0.967 -66.759  1.00 64.16           C  
ANISOU 4528  CG  ARG B  10     8940  11365   4072   3253    246   -704       C  
ATOM   4529  CD  ARG B  10      21.302  -0.145 -66.531  1.00 66.02           C  
ANISOU 4529  CD  ARG B  10     9268  11448   4370   3268     81   -946       C  
ATOM   4530  NE  ARG B  10      21.800  -1.129 -65.574  1.00 76.58           N  
ANISOU 4530  NE  ARG B  10    10636  12660   5799   3241     50  -1060       N  
ATOM   4531  CZ  ARG B  10      21.161  -2.246 -65.240  1.00 73.05           C  
ANISOU 4531  CZ  ARG B  10    10263  12060   5433   3247    -88  -1271       C  
ATOM   4532  NH1 ARG B  10      19.989  -2.533 -65.788  1.00 75.40           N  
ANISOU 4532  NH1 ARG B  10    10607  12312   5732   3276   -212  -1393       N  
ATOM   4533  NH2 ARG B  10      21.698  -3.078 -64.359  1.00 66.93           N  
ANISOU 4533  NH2 ARG B  10     9501  11156   4771   3206   -107  -1345       N  
ATOM   4534  N   PHE B  11      21.811   3.012 -70.829  1.00 75.17           N  
ANISOU 4534  N   PHE B  11    10196  13268   5098   3544    324   -427       N  
ATOM   4535  CA  PHE B  11      21.433   3.942 -71.890  1.00 74.50           C  
ANISOU 4535  CA  PHE B  11    10076  13312   4919   3594    356   -306       C  
ATOM   4536  C   PHE B  11      20.512   3.268 -72.894  1.00 76.02           C  
ANISOU 4536  C   PHE B  11    10310  13538   5035   3730    224   -483       C  
ATOM   4537  O   PHE B  11      19.571   3.885 -73.406  1.00 78.10           O  
ANISOU 4537  O   PHE B  11    10589  13821   5266   3732    193   -450       O  
ATOM   4538  CB  PHE B  11      22.684   4.480 -72.588  1.00 75.64           C  
ANISOU 4538  CB  PHE B  11    10118  13639   4981   3660    486   -133       C  
ATOM   4539  CG  PHE B  11      22.402   5.542 -73.619  1.00 70.78           C  
ANISOU 4539  CG  PHE B  11     9460  13156   4279   3700    536     20       C  
ATOM   4540  CD1 PHE B  11      22.128   5.203 -74.936  1.00 78.31           C  
ANISOU 4540  CD1 PHE B  11    10407  14243   5105   3870    480    -58       C  
ATOM   4541  CD2 PHE B  11      22.427   6.882 -73.271  1.00 69.31           C  
ANISOU 4541  CD2 PHE B  11     9240  12955   4141   3570    637    244       C  
ATOM   4542  CE1 PHE B  11      21.873   6.182 -75.882  1.00 75.18           C  
ANISOU 4542  CE1 PHE B  11     9970  13969   4627   3910    527     86       C  
ATOM   4543  CE2 PHE B  11      22.175   7.863 -74.211  1.00 77.92           C  
ANISOU 4543  CE2 PHE B  11    10290  14157   5157   3606    681    388       C  
ATOM   4544  CZ  PHE B  11      21.898   7.514 -75.518  1.00 78.99           C  
ANISOU 4544  CZ  PHE B  11    10420  14431   5161   3778    628    310       C  
ATOM   4545  N   LYS B  12      20.769   1.994 -73.178  1.00 78.27           N  
ANISOU 4545  N   LYS B  12    10613  13826   5298   3845    140   -674       N  
ATOM   4546  CA  LYS B  12      19.955   1.250 -74.129  1.00 79.92           C  
ANISOU 4546  CA  LYS B  12    10858  14061   5445   3978      6   -857       C  
ATOM   4547  C   LYS B  12      18.572   0.955 -73.563  1.00 72.26           C  
ANISOU 4547  C   LYS B  12     9973  12911   4571   3894   -123   -997       C  
ATOM   4548  O   LYS B  12      17.561   1.094 -74.260  1.00 79.24           O  
ANISOU 4548  O   LYS B  12    10879  13816   5414   3940   -201  -1050       O  
ATOM   4549  CB  LYS B  12      20.669  -0.047 -74.499  1.00 90.20           C  
ANISOU 4549  CB  LYS B  12    12157  15402   6715   4116    -49  -1019       C  
ATOM   4550  CG  LYS B  12      19.793  -1.035 -75.205  1.00 98.65           C  
ANISOU 4550  CG  LYS B  12    13276  16444   7762   4231   -211  -1243       C  
ATOM   4551  CD  LYS B  12      19.530  -0.544 -76.600  1.00107.38           C  
ANISOU 4551  CD  LYS B  12    14342  17732   8725   4363   -205  -1193       C  
ATOM   4552  CE  LYS B  12      18.973  -1.635 -77.468  1.00111.16           C  
ANISOU 4552  CE  LYS B  12    14853  18223   9161   4514   -355  -1415       C  
ATOM   4553  NZ  LYS B  12      17.905  -1.025 -78.284  1.00114.50           N  
ANISOU 4553  NZ  LYS B  12    15281  18704   9520   4549   -397  -1400       N  
ATOM   4554  N   ASP B  13      18.511   0.549 -72.293  1.00 70.02           N  
ANISOU 4554  N   ASP B  13     9735  12451   4417   3770   -148  -1058       N  
ATOM   4555  CA  ASP B  13      17.255   0.063 -71.730  1.00 70.74           C  
ANISOU 4555  CA  ASP B  13     9906  12363   4611   3696   -285  -1217       C  
ATOM   4556  C   ASP B  13      16.291   1.203 -71.421  1.00 63.18           C  
ANISOU 4556  C   ASP B  13     8963  11363   3680   3579   -267  -1101       C  
ATOM   4557  O   ASP B  13      15.094   1.100 -71.710  1.00 65.52           O  
ANISOU 4557  O   ASP B  13     9298  11607   3990   3582   -378  -1201       O  
ATOM   4558  CB  ASP B  13      17.530  -0.767 -70.477  1.00 72.24           C  
ANISOU 4558  CB  ASP B  13    10138  12378   4933   3605   -318  -1319       C  
ATOM   4559  CG  ASP B  13      17.887  -2.209 -70.799  1.00 80.41           C  
ANISOU 4559  CG  ASP B  13    11189  13388   5974   3722   -414  -1520       C  
ATOM   4560  OD1 ASP B  13      17.690  -2.622 -71.962  1.00 68.73           O  
ANISOU 4560  OD1 ASP B  13     9699  12008   4408   3866   -480  -1606       O  
ATOM   4561  OD2 ASP B  13      18.356  -2.931 -69.891  1.00 78.37           O  
ANISOU 4561  OD2 ASP B  13    10956  13011   5811   3672   -427  -1590       O  
ATOM   4562  N   LEU B  14      16.783   2.294 -70.838  1.00 62.14           N  
ANISOU 4562  N   LEU B  14     8799  11251   3562   3474   -133   -890       N  
ATOM   4563  CA  LEU B  14      15.894   3.366 -70.406  1.00 64.75           C  
ANISOU 4563  CA  LEU B  14     9147  11523   3933   3354   -118   -777       C  
ATOM   4564  C   LEU B  14      15.736   4.488 -71.429  1.00 74.19           C  
ANISOU 4564  C   LEU B  14    10295  12871   5024   3405    -53   -612       C  
ATOM   4565  O   LEU B  14      14.809   5.298 -71.305  1.00 83.80           O  
ANISOU 4565  O   LEU B  14    11531  14048   6262   3334    -68   -544       O  
ATOM   4566  CB  LEU B  14      16.380   3.950 -69.085  1.00 68.76           C  
ANISOU 4566  CB  LEU B  14     9651  11938   4535   3195    -20   -643       C  
ATOM   4567  CG  LEU B  14      16.655   2.896 -68.007  1.00 73.96           C  
ANISOU 4567  CG  LEU B  14    10353  12450   5298   3142    -68   -788       C  
ATOM   4568  CD1 LEU B  14      17.630   3.414 -66.959  1.00 69.28           C  
ANISOU 4568  CD1 LEU B  14     9718  11803   4802   3012     60   -626       C  
ATOM   4569  CD2 LEU B  14      15.347   2.440 -67.373  1.00 76.00           C  
ANISOU 4569  CD2 LEU B  14    10673  12504   5699   3045   -207   -936       C  
ATOM   4570  N   GLY B  15      16.602   4.563 -72.434  1.00 76.72           N  
ANISOU 4570  N   GLY B  15    10554  13364   5234   3528     15   -543       N  
ATOM   4571  CA  GLY B  15      16.531   5.623 -73.417  1.00 81.15           C  
ANISOU 4571  CA  GLY B  15    11065  14070   5697   3579     82   -379       C  
ATOM   4572  C   GLY B  15      17.347   6.836 -73.012  1.00 76.97           C  
ANISOU 4572  C   GLY B  15    10477  13577   5191   3478    241   -119       C  
ATOM   4573  O   GLY B  15      17.777   6.991 -71.867  1.00 62.74           O  
ANISOU 4573  O   GLY B  15     8678  11671   3488   3350    296    -60       O  
ATOM   4574  N   GLU B  16      17.562   7.722 -73.987  1.00 67.38           N  
ANISOU 4574  N   GLU B  16     9205  12509   3886   3538    316     40       N  
ATOM   4575  CA  GLU B  16      18.468   8.847 -73.770  1.00 71.88           C  
ANISOU 4575  CA  GLU B  16     9706  13126   4479   3455    469    292       C  
ATOM   4576  C   GLU B  16      17.863   9.897 -72.844  1.00 63.77           C  
ANISOU 4576  C   GLU B  16     8702  11967   3559   3284    499    425       C  
ATOM   4577  O   GLU B  16      18.559  10.433 -71.974  1.00 62.74           O  
ANISOU 4577  O   GLU B  16     8541  11778   3518   3160    593    563       O  
ATOM   4578  CB  GLU B  16      18.852   9.482 -75.106  1.00 67.45           C  
ANISOU 4578  CB  GLU B  16     9076  12755   3796   3570    535    423       C  
ATOM   4579  CG  GLU B  16      19.675  10.750 -74.956  1.00 67.44           C  
ANISOU 4579  CG  GLU B  16     9001  12793   3832   3476    684    693       C  
ATOM   4580  CD  GLU B  16      20.170  11.288 -76.279  1.00 76.52           C  
ANISOU 4580  CD  GLU B  16    10076  14136   4861   3595    752    819       C  
ATOM   4581  OE1 GLU B  16      19.882  10.662 -77.320  1.00 79.20           O  
ANISOU 4581  OE1 GLU B  16    10423  14588   5081   3757    684    695       O  
ATOM   4582  OE2 GLU B  16      20.849  12.337 -76.276  1.00 75.86           O  
ANISOU 4582  OE2 GLU B  16     9926  14091   4807   3525    870   1042       O  
ATOM   4583  N   GLU B  17      16.577  10.218 -73.021  1.00 63.56           N  
ANISOU 4583  N   GLU B  17     8725  11893   3530   3276    417    388       N  
ATOM   4584  CA  GLU B  17      15.983  11.316 -72.262  1.00 62.21           C  
ANISOU 4584  CA  GLU B  17     8572  11613   3453   3126    447    530       C  
ATOM   4585  C   GLU B  17      15.942  11.006 -70.770  1.00 68.04           C  
ANISOU 4585  C   GLU B  17     9353  12178   4321   2986    432    479       C  
ATOM   4586  O   GLU B  17      16.284  11.860 -69.943  1.00 68.65           O  
ANISOU 4586  O   GLU B  17     9410  12184   4491   2852    519    645       O  
ATOM   4587  CB  GLU B  17      14.580  11.628 -72.783  1.00 62.49           C  
ANISOU 4587  CB  GLU B  17     8653  11639   3454   3160    351    482       C  
ATOM   4588  CG  GLU B  17      13.856  12.704 -71.984  1.00 79.91           C  
ANISOU 4588  CG  GLU B  17    10882  13722   5757   3015    366    611       C  
ATOM   4589  CD  GLU B  17      12.704  13.330 -72.746  1.00 91.62           C  
ANISOU 4589  CD  GLU B  17    12384  15239   7189   3062    307    633       C  
ATOM   4590  OE1 GLU B  17      12.958  14.226 -73.580  1.00 99.75           O  
ANISOU 4590  OE1 GLU B  17    13365  16375   8161   3102    381    798       O  
ATOM   4591  OE2 GLU B  17      11.545  12.930 -72.509  1.00 95.05           O  
ANISOU 4591  OE2 GLU B  17    12879  15593   7644   3057    186    484       O  
ATOM   4592  N   ASN B  18      15.526   9.791 -70.406  1.00 59.65           N  
ANISOU 4592  N   ASN B  18     8349  11041   3274   3014    321    250       N  
ATOM   4593  CA  ASN B  18      15.527   9.406 -69.000  1.00 68.80           C  
ANISOU 4593  CA  ASN B  18     9549  12040   4550   2891    305    192       C  
ATOM   4594  C   ASN B  18      16.942   9.191 -68.480  1.00 67.75           C  
ANISOU 4594  C   ASN B  18     9369  11923   4451   2860    408    256       C  
ATOM   4595  O   ASN B  18      17.186   9.339 -67.277  1.00 57.25           O  
ANISOU 4595  O   ASN B  18     8032  10437   3284   2705    440    298       O  
ATOM   4596  CB  ASN B  18      14.685   8.147 -68.798  1.00 70.37           C  
ANISOU 4596  CB  ASN B  18     9818  12139   4779   2923    150    -74       C  
ATOM   4597  CG  ASN B  18      13.208   8.390 -69.034  1.00 68.57           C  
ANISOU 4597  CG  ASN B  18     9631  11850   4575   2909     41   -138       C  
ATOM   4598  OD1 ASN B  18      12.716   9.506 -68.864  1.00 65.21           O  
ANISOU 4598  OD1 ASN B  18     9189  11382   4204   2820     77     12       O  
ATOM   4599  ND2 ASN B  18      12.490   7.344 -69.426  1.00 68.44           N  
ANISOU 4599  ND2 ASN B  18     9662  11823   4519   2998    -98   -363       N  
ATOM   4600  N   PHE B  19      17.880   8.842 -69.364  1.00 59.07           N  
ANISOU 4600  N   PHE B  19     8215  10967   3264   2977    453    260       N  
ATOM   4601  CA  PHE B  19      19.274   8.688 -68.957  1.00 59.02           C  
ANISOU 4601  CA  PHE B  19     8151  10990   3283   2955    554    331       C  
ATOM   4602  C   PHE B  19      19.835  10.004 -68.436  1.00 58.41           C  
ANISOU 4602  C   PHE B  19     8015  10898   3279   2822    686    585       C  
ATOM   4603  O   PHE B  19      20.342  10.079 -67.311  1.00 57.11           O  
ANISOU 4603  O   PHE B  19     7845  10639   3217   2705    737    633       O  
ATOM   4604  CB  PHE B  19      20.108   8.174 -70.133  1.00 65.55           C  
ANISOU 4604  CB  PHE B  19     8923  11990   3993   3117    574    301       C  
ATOM   4605  CG  PHE B  19      21.468   7.669 -69.742  1.00 62.53           C  
ANISOU 4605  CG  PHE B  19     8491  11637   3629   3122    646    312       C  
ATOM   4606  CD1 PHE B  19      22.548   8.532 -69.658  1.00 62.57           C  
ANISOU 4606  CD1 PHE B  19     8410  11708   3657   3064    783    525       C  
ATOM   4607  CD2 PHE B  19      21.666   6.329 -69.462  1.00 60.89           C  
ANISOU 4607  CD2 PHE B  19     8322  11387   3427   3183    570    107       C  
ATOM   4608  CE1 PHE B  19      23.800   8.065 -69.299  1.00 63.43           C  
ANISOU 4608  CE1 PHE B  19     8467  11847   3784   3069    846    533       C  
ATOM   4609  CE2 PHE B  19      22.915   5.856 -69.106  1.00 62.09           C  
ANISOU 4609  CE2 PHE B  19     8428  11568   3596   3193    633    115       C  
ATOM   4610  CZ  PHE B  19      23.983   6.725 -69.024  1.00 65.04           C  
ANISOU 4610  CZ  PHE B  19     8712  12016   3984   3138    772    328       C  
ATOM   4611  N   LYS B  20      19.755  11.061 -69.251  1.00 64.56           N  
ANISOU 4611  N   LYS B  20     8749  11766   4014   2836    740    750       N  
ATOM   4612  CA  LYS B  20      20.251  12.364 -68.823  1.00 63.58           C  
ANISOU 4612  CA  LYS B  20     8568  11616   3975   2706    857    994       C  
ATOM   4613  C   LYS B  20      19.511  12.868 -67.592  1.00 57.52           C  
ANISOU 4613  C   LYS B  20     7851  10670   3334   2548    839   1027       C  
ATOM   4614  O   LYS B  20      20.094  13.578 -66.765  1.00 56.26           O  
ANISOU 4614  O   LYS B  20     7653  10439   3284   2415    925   1178       O  
ATOM   4615  CB  LYS B  20      20.128  13.375 -69.963  1.00 62.13           C  
ANISOU 4615  CB  LYS B  20     8338  11546   3723   2756    901   1148       C  
ATOM   4616  CG  LYS B  20      20.926  13.016 -71.206  1.00 62.52           C  
ANISOU 4616  CG  LYS B  20     8326  11784   3643   2912    933   1145       C  
ATOM   4617  CD  LYS B  20      20.545  13.903 -72.383  1.00 68.12           C  
ANISOU 4617  CD  LYS B  20     9008  12604   4272   2978    952   1266       C  
ATOM   4618  CE  LYS B  20      20.955  15.349 -72.146  1.00 70.31           C  
ANISOU 4618  CE  LYS B  20     9225  12850   4638   2850   1062   1524       C  
ATOM   4619  NZ  LYS B  20      22.431  15.495 -72.002  1.00 65.54           N  
ANISOU 4619  NZ  LYS B  20     8532  12303   4070   2817   1173   1642       N  
ATOM   4620  N   ALA B  21      18.234  12.507 -67.451  1.00 56.45           N  
ANISOU 4620  N   ALA B  21     7798  10459   3190   2560    725    887       N  
ATOM   4621  CA  ALA B  21      17.454  12.964 -66.306  1.00 59.92           C  
ANISOU 4621  CA  ALA B  21     8261  10664   3842   2376    683    891       C  
ATOM   4622  C   ALA B  21      17.896  12.267 -65.025  1.00 56.13           C  
ANISOU 4622  C   ALA B  21     7781  10014   3534   2257    670    798       C  
ATOM   4623  O   ALA B  21      18.136  12.921 -64.003  1.00 61.34           O  
ANISOU 4623  O   ALA B  21     8413  10534   4360   2096    719    902       O  
ATOM   4624  CB  ALA B  21      15.965  12.731 -66.564  1.00 56.97           C  
ANISOU 4624  CB  ALA B  21     7953  10226   3468   2403    551    752       C  
ATOM   4625  N   LEU B  22      18.013  10.938 -65.061  1.00 53.42           N  
ANISOU 4625  N   LEU B  22     7467   9678   3151   2339    601    600       N  
ATOM   4626  CA  LEU B  22      18.422  10.199 -63.870  1.00 63.79           C  
ANISOU 4626  CA  LEU B  22     8783  10832   4620   2236    583    507       C  
ATOM   4627  C   LEU B  22      19.874  10.485 -63.509  1.00 66.82           C  
ANISOU 4627  C   LEU B  22     9099  11272   5020   2201    709    644       C  
ATOM   4628  O   LEU B  22      20.222  10.551 -62.324  1.00 62.79           O  
ANISOU 4628  O   LEU B  22     8570  10609   4677   2057    731    668       O  
ATOM   4629  CB  LEU B  22      18.206   8.702 -64.081  1.00 57.06           C  
ANISOU 4629  CB  LEU B  22     7982   9979   3718   2343    476    266       C  
ATOM   4630  CG  LEU B  22      16.749   8.258 -64.211  1.00 52.26           C  
ANISOU 4630  CG  LEU B  22     7441   9278   3137   2352    335    104       C  
ATOM   4631  CD1 LEU B  22      16.673   6.873 -64.825  1.00 53.20           C  
ANISOU 4631  CD1 LEU B  22     7603   9457   3153   2504    238   -116       C  
ATOM   4632  CD2 LEU B  22      16.054   8.291 -62.858  1.00 66.75           C  
ANISOU 4632  CD2 LEU B  22     9296  10865   5202   2164    286     69       C  
ATOM   4633  N   VAL B  23      20.738  10.651 -64.514  1.00 57.17           N  
ANISOU 4633  N   VAL B  23     7831  10270   3620   2333    793    736       N  
ATOM   4634  CA  VAL B  23      22.126  11.012 -64.241  1.00 62.24           C  
ANISOU 4634  CA  VAL B  23     8396  10980   4273   2299    918    884       C  
ATOM   4635  C   VAL B  23      22.193  12.386 -63.587  1.00 59.71           C  
ANISOU 4635  C   VAL B  23     8033  10564   4092   2130    994   1093       C  
ATOM   4636  O   VAL B  23      23.004  12.624 -62.683  1.00 60.95           O  
ANISOU 4636  O   VAL B  23     8142  10643   4373   2014   1056   1169       O  
ATOM   4637  CB  VAL B  23      22.962  10.953 -65.535  1.00 58.13           C  
ANISOU 4637  CB  VAL B  23     7826  10716   3544   2473    989    945       C  
ATOM   4638  CG1 VAL B  23      24.300  11.648 -65.342  1.00 58.18           C  
ANISOU 4638  CG1 VAL B  23     7730  10768   3609   2403   1118   1136       C  
ATOM   4639  CG2 VAL B  23      23.173   9.509 -65.964  1.00 56.53           C  
ANISOU 4639  CG2 VAL B  23     7652  10574   3251   2620    916    728       C  
ATOM   4640  N   LEU B  24      21.329  13.306 -64.019  1.00 53.31           N  
ANISOU 4640  N   LEU B  24     7238   9750   3266   2114    984   1183       N  
ATOM   4641  CA  LEU B  24      21.281  14.623 -63.393  1.00 52.60           C  
ANISOU 4641  CA  LEU B  24     7116   9552   3319   1954   1041   1369       C  
ATOM   4642  C   LEU B  24      20.799  14.532 -61.949  1.00 53.72           C  
ANISOU 4642  C   LEU B  24     7286   9442   3684   1783    982   1290       C  
ATOM   4643  O   LEU B  24      21.288  15.264 -61.081  1.00 56.18           O  
ANISOU 4643  O   LEU B  24     7554   9652   4138   1641   1041   1410       O  
ATOM   4644  CB  LEU B  24      20.381  15.556 -64.203  1.00 53.30           C  
ANISOU 4644  CB  LEU B  24     7223   9690   3338   1988   1032   1468       C  
ATOM   4645  CG  LEU B  24      20.230  16.979 -63.664  1.00 62.09           C  
ANISOU 4645  CG  LEU B  24     8309  10689   4593   1836   1083   1661       C  
ATOM   4646  CD1 LEU B  24      21.593  17.628 -63.465  1.00 65.39           C  
ANISOU 4646  CD1 LEU B  24     8640  11161   5043   1777   1212   1853       C  
ATOM   4647  CD2 LEU B  24      19.359  17.816 -64.590  1.00 57.21           C  
ANISOU 4647  CD2 LEU B  24     7713  10139   3886   1895   1070   1754       C  
ATOM   4648  N   ILE B  25      19.846  13.638 -61.672  1.00 49.98           N  
ANISOU 4648  N   ILE B  25     6881   8866   3244   1793    864   1089       N  
ATOM   4649  CA  ILE B  25      19.345  13.488 -60.308  1.00 55.79           C  
ANISOU 4649  CA  ILE B  25     7642   9371   4183   1638    807   1011       C  
ATOM   4650  C   ILE B  25      20.439  12.955 -59.392  1.00 49.94           C  
ANISOU 4650  C   ILE B  25     6868   8579   3529   1576    848    991       C  
ATOM   4651  O   ILE B  25      20.594  13.417 -58.255  1.00 63.87           O  
ANISOU 4651  O   ILE B  25     8613  10196   5460   1425    869   1045       O  
ATOM   4652  CB  ILE B  25      18.100  12.582 -60.288  1.00 47.81           C  
ANISOU 4652  CB  ILE B  25     6707   8277   3183   1670    673    803       C  
ATOM   4653  CG1 ILE B  25      16.952  13.226 -61.063  1.00 48.33           C  
ANISOU 4653  CG1 ILE B  25     6802   8376   3186   1712    629    830       C  
ATOM   4654  CG2 ILE B  25      17.660  12.306 -58.856  1.00 53.05           C  
ANISOU 4654  CG2 ILE B  25     7391   8715   4049   1516    620    721       C  
ATOM   4655  CD1 ILE B  25      15.815  12.272 -61.366  1.00 48.36           C  
ANISOU 4655  CD1 ILE B  25     6869   8349   3156   1781    498    625       C  
ATOM   4656  N   ALA B  26      21.217  11.981 -59.873  1.00 57.91           N  
ANISOU 4656  N   ALA B  26     7867   9711   4423   1697    859    911       N  
ATOM   4657  CA  ALA B  26      22.296  11.417 -59.066  1.00 59.79           C  
ANISOU 4657  CA  ALA B  26     8071   9914   4731   1655    896    889       C  
ATOM   4658  C   ALA B  26      23.309  12.486 -58.678  1.00 62.87           C  
ANISOU 4658  C   ALA B  26     8381  10323   5184   1559   1014   1095       C  
ATOM   4659  O   ALA B  26      23.654  12.633 -57.500  1.00 61.16           O  
ANISOU 4659  O   ALA B  26     8144   9967   5125   1424   1027   1115       O  
ATOM   4660  CB  ALA B  26      22.977  10.280 -59.826  1.00 49.05           C  
ANISOU 4660  CB  ALA B  26     6711   8710   3216   1823    892    780       C  
ATOM   4661  N   PHE B  27      23.798  13.243 -59.664  1.00 54.60           N  
ANISOU 4661  N   PHE B  27     7284   9448   4014   1628   1100   1253       N  
ATOM   4662  CA  PHE B  27      24.744  14.318 -59.378  1.00 56.23           C  
ANISOU 4662  CA  PHE B  27     7408   9675   4283   1535   1211   1462       C  
ATOM   4663  C   PHE B  27      24.142  15.344 -58.427  1.00 53.76           C  
ANISOU 4663  C   PHE B  27     7102   9168   4156   1359   1198   1541       C  
ATOM   4664  O   PHE B  27      24.835  15.871 -57.548  1.00 64.64           O  
ANISOU 4664  O   PHE B  27     8429  10466   5665   1234   1249   1633       O  
ATOM   4665  CB  PHE B  27      25.181  14.992 -60.679  1.00 57.16           C  
ANISOU 4665  CB  PHE B  27     7476  10008   4233   1642   1298   1625       C  
ATOM   4666  CG  PHE B  27      26.246  14.243 -61.425  1.00 73.92           C  
ANISOU 4666  CG  PHE B  27     9555  12338   6194   1790   1354   1607       C  
ATOM   4667  CD1 PHE B  27      27.560  14.266 -60.993  1.00 79.09           C  
ANISOU 4667  CD1 PHE B  27    10129  13034   6889   1750   1441   1689       C  
ATOM   4668  CD2 PHE B  27      25.936  13.523 -62.566  1.00 83.06           C  
ANISOU 4668  CD2 PHE B  27    10749  13654   7157   1974   1319   1506       C  
ATOM   4669  CE1 PHE B  27      28.544  13.581 -61.680  1.00 82.44           C  
ANISOU 4669  CE1 PHE B  27    10503  13632   7188   1881   1481   1661       C  
ATOM   4670  CE2 PHE B  27      26.914  12.836 -63.258  1.00 81.86           C  
ANISOU 4670  CE2 PHE B  27    10548  13660   6894   2101   1352   1468       C  
ATOM   4671  CZ  PHE B  27      28.220  12.865 -62.814  1.00 86.60           C  
ANISOU 4671  CZ  PHE B  27    11063  14283   7557   2052   1431   1544       C  
ATOM   4672  N   ALA B  28      22.850  15.639 -58.585  1.00 53.74           N  
ANISOU 4672  N   ALA B  28     7161   9092   4167   1349   1127   1502       N  
ATOM   4673  CA  ALA B  28      22.201  16.603 -57.703  1.00 57.05           C  
ANISOU 4673  CA  ALA B  28     7590   9329   4757   1193   1108   1566       C  
ATOM   4674  C   ALA B  28      22.038  16.045 -56.295  1.00 50.47           C  
ANISOU 4674  C   ALA B  28     6781   8306   4089   1078   1051   1440       C  
ATOM   4675  O   ALA B  28      22.158  16.785 -55.312  1.00 57.87           O  
ANISOU 4675  O   ALA B  28     7696   9111   5182    937   1070   1514       O  
ATOM   4676  CB  ALA B  28      20.848  17.016 -58.281  1.00 58.29           C  
ANISOU 4676  CB  ALA B  28     7803   9468   4875   1226   1044   1551       C  
ATOM   4677  N   GLN B  29      21.770  14.743 -56.175  1.00 44.78           N  
ANISOU 4677  N   GLN B  29     6107   7569   3338   1139    978   1251       N  
ATOM   4678  CA  GLN B  29      21.635  14.131 -54.858  1.00 65.14           C  
ANISOU 4678  CA  GLN B  29     8709   9976   6065   1038    926   1135       C  
ATOM   4679  C   GLN B  29      22.994  13.829 -54.237  1.00 70.11           C  
ANISOU 4679  C   GLN B  29     9283  10620   6737   1005    988   1164       C  
ATOM   4680  O   GLN B  29      23.159  13.941 -53.018  1.00 67.88           O  
ANISOU 4680  O   GLN B  29     8991  10197   6605    880    984   1159       O  
ATOM   4681  CB  GLN B  29      20.799  12.854 -54.953  1.00 43.10           C  
ANISOU 4681  CB  GLN B  29     5988   7150   3238   1109    820    927       C  
ATOM   4682  CG  GLN B  29      19.349  13.096 -55.336  1.00 43.01           C  
ANISOU 4682  CG  GLN B  29     6031   7094   3217   1119    743    879       C  
ATOM   4683  CD  GLN B  29      18.555  11.814 -55.469  1.00 42.89           C  
ANISOU 4683  CD  GLN B  29     6079   7047   3172   1188    635    674       C  
ATOM   4684  OE1 GLN B  29      19.120  10.732 -55.629  1.00 47.13           O  
ANISOU 4684  OE1 GLN B  29     6623   7635   3651   1267    621    572       O  
ATOM   4685  NE2 GLN B  29      17.234  11.929 -55.407  1.00 44.31           N  
ANISOU 4685  NE2 GLN B  29     6303   7139   3395   1158    556    613       N  
ATOM   4686  N   TYR B  30      23.976  13.446 -55.056  1.00 70.69           N  
ANISOU 4686  N   TYR B  30     9316  10867   6675   1120   1046   1191       N  
ATOM   4687  CA  TYR B  30      25.301  13.138 -54.530  1.00 67.56           C  
ANISOU 4687  CA  TYR B  30     8859  10500   6309   1099   1107   1219       C  
ATOM   4688  C   TYR B  30      26.098  14.394 -54.206  1.00 63.31           C  
ANISOU 4688  C   TYR B  30     8241   9964   5850    994   1201   1419       C  
ATOM   4689  O   TYR B  30      26.911  14.380 -53.275  1.00 67.49           O  
ANISOU 4689  O   TYR B  30     8727  10434   6482    909   1230   1439       O  
ATOM   4690  CB  TYR B  30      26.074  12.268 -55.523  1.00 76.50           C  
ANISOU 4690  CB  TYR B  30     9973  11825   7268   1266   1135   1174       C  
ATOM   4691  CG  TYR B  30      25.841  10.785 -55.345  1.00 85.74           C  
ANISOU 4691  CG  TYR B  30    11203  12959   8416   1341   1049    963       C  
ATOM   4692  CD1 TYR B  30      24.992  10.309 -54.355  1.00 91.22           C  
ANISOU 4692  CD1 TYR B  30    11958  13460   9240   1254    959    838       C  
ATOM   4693  CD2 TYR B  30      26.475   9.860 -56.165  1.00 94.65           C  
ANISOU 4693  CD2 TYR B  30    12324  14244   9393   1501   1058    890       C  
ATOM   4694  CE1 TYR B  30      24.780   8.954 -54.187  1.00 96.76           C  
ANISOU 4694  CE1 TYR B  30    12713  14118   9932   1317    878    653       C  
ATOM   4695  CE2 TYR B  30      26.269   8.504 -56.005  1.00 97.92           C  
ANISOU 4695  CE2 TYR B  30    12796  14614   9796   1570    974    694       C  
ATOM   4696  CZ  TYR B  30      25.421   8.057 -55.015  1.00102.45           C  
ANISOU 4696  CZ  TYR B  30    13431  14987  10510   1474    883    580       C  
ATOM   4697  OH  TYR B  30      25.218   6.707 -54.854  1.00108.86           O  
ANISOU 4697  OH  TYR B  30    14298  15745  11320   1537    798    394       O  
ATOM   4698  N   LEU B  31      25.887  15.482 -54.956  1.00 64.15           N  
ANISOU 4698  N   LEU B  31     8326  10137   5912    997   1246   1567       N  
ATOM   4699  CA  LEU B  31      26.549  16.768 -54.717  1.00 69.34           C  
ANISOU 4699  CA  LEU B  31     8908  10785   6652    892   1330   1767       C  
ATOM   4700  C   LEU B  31      25.487  17.865 -54.781  1.00 63.71           C  
ANISOU 4700  C   LEU B  31     8229   9980   5999    825   1305   1844       C  
ATOM   4701  O   LEU B  31      25.308  18.518 -55.811  1.00 67.47           O  
ANISOU 4701  O   LEU B  31     8694  10562   6378    886   1341   1958       O  
ATOM   4702  CB  LEU B  31      27.685  17.010 -55.722  1.00 79.81           C  
ANISOU 4702  CB  LEU B  31    10153  12323   7849    980   1435   1909       C  
ATOM   4703  CG  LEU B  31      28.841  17.860 -55.185  1.00 85.48           C  
ANISOU 4703  CG  LEU B  31    10773  13033   8672    868   1523   2076       C  
ATOM   4704  CD1 LEU B  31      29.234  17.407 -53.788  1.00 85.50           C  
ANISOU 4704  CD1 LEU B  31    10771  12891   8825    764   1491   1983       C  
ATOM   4705  CD2 LEU B  31      30.044  17.836 -56.129  1.00 91.55           C  
ANISOU 4705  CD2 LEU B  31    11455  14025   9305    966   1627   2192       C  
ATOM   4706  N   GLN B  32      24.783  18.065 -53.667  1.00 47.87           N  
ANISOU 4706  N   GLN B  32     6262   7779   4150    705   1242   1782       N  
ATOM   4707  CA  GLN B  32      23.806  19.142 -53.550  1.00 47.30           C  
ANISOU 4707  CA  GLN B  32     6217   7600   4156    630   1215   1850       C  
ATOM   4708  C   GLN B  32      24.456  20.513 -53.416  1.00 48.21           C  
ANISOU 4708  C   GLN B  32     6264   7697   4358    533   1291   2055       C  
ATOM   4709  O   GLN B  32      23.737  21.516 -53.332  1.00 44.05           O  
ANISOU 4709  O   GLN B  32     5755   7079   3903    471   1274   2128       O  
ATOM   4710  CB  GLN B  32      22.888  18.881 -52.350  1.00 58.21           C  
ANISOU 4710  CB  GLN B  32     7657   8785   5675    536   1127   1715       C  
ATOM   4711  CG  GLN B  32      22.487  17.418 -52.185  1.00 42.61           C  
ANISOU 4711  CG  GLN B  32     5736   6800   3654    603   1054   1512       C  
ATOM   4712  CD  GLN B  32      22.330  17.004 -50.729  1.00 60.86           C  
ANISOU 4712  CD  GLN B  32     8067   8942   6116    494   1005   1408       C  
ATOM   4713  OE1 GLN B  32      22.561  15.847 -50.374  1.00 50.13           O  
ANISOU 4713  OE1 GLN B  32     6725   7578   4746    525    974   1280       O  
ATOM   4714  NE2 GLN B  32      21.929  17.946 -49.883  1.00 58.12           N  
ANISOU 4714  NE2 GLN B  32     7718   8457   5909    370    996   1462       N  
ATOM   4715  N   GLN B  33      25.790  20.578 -53.410  1.00 56.37           N  
ANISOU 4715  N   GLN B  33     7217   8813   5389    522   1372   2148       N  
ATOM   4716  CA  GLN B  33      26.501  21.829 -53.169  1.00 62.16           C  
ANISOU 4716  CA  GLN B  33     7876   9515   6226    415   1440   2338       C  
ATOM   4717  C   GLN B  33      26.672  22.644 -54.447  1.00 70.96           C  
ANISOU 4717  C   GLN B  33     8954  10772   7235    478   1511   2521       C  
ATOM   4718  O   GLN B  33      26.422  23.854 -54.459  1.00 71.86           O  
ANISOU 4718  O   GLN B  33     9056  10817   7432    403   1526   2660       O  
ATOM   4719  CB  GLN B  33      27.870  21.535 -52.549  1.00 47.40           C  
ANISOU 4719  CB  GLN B  33     5929   7670   4410    368   1493   2358       C  
ATOM   4720  CG  GLN B  33      27.968  21.818 -51.059  1.00 73.69           C  
ANISOU 4720  CG  GLN B  33     9253  10811   7936    218   1457   2319       C  
ATOM   4721  CD  GLN B  33      27.043  20.944 -50.236  1.00 84.67           C  
ANISOU 4721  CD  GLN B  33    10729  12078   9365    211   1360   2116       C  
ATOM   4722  OE1 GLN B  33      26.847  19.767 -50.539  1.00 88.38           O  
ANISOU 4722  OE1 GLN B  33    11238  12612   9729    312   1330   1982       O  
ATOM   4723  NE2 GLN B  33      26.473  21.517 -49.182  1.00 89.83           N  
ANISOU 4723  NE2 GLN B  33    11408  12552  10173     92   1311   2093       N  
ATOM   4724  N   CYS B  34      27.098  21.996 -55.530  1.00 75.11           N  
ANISOU 4724  N   CYS B  34     9461  11497   7578    621   1554   2524       N  
ATOM   4725  CA  CYS B  34      27.569  22.696 -56.714  1.00 78.44           C  
ANISOU 4725  CA  CYS B  34     9827  12067   7910    679   1627   2692       C  
ATOM   4726  C   CYS B  34      26.409  23.264 -57.536  1.00 77.32           C  
ANISOU 4726  C   CYS B  34     9745  11929   7706    731   1592   2727       C  
ATOM   4727  O   CYS B  34      25.300  22.723 -57.518  1.00 72.06           O  
ANISOU 4727  O   CYS B  34     9165  11232   6984    784   1522   2603       O  
ATOM   4728  CB  CYS B  34      28.408  21.759 -57.574  1.00 88.92           C  
ANISOU 4728  CB  CYS B  34    11115  13592   9078    818   1665   2645       C  
ATOM   4729  SG  CYS B  34      30.000  21.336 -56.827  1.00 96.52           S  
ANISOU 4729  SG  CYS B  34    11982  14575  10118    761   1720   2645       S  
ATOM   4730  N   PRO B  35      26.649  24.353 -58.266  1.00 70.92           N  
ANISOU 4730  N   PRO B  35     8887  11138   6922    714   1622   2870       N  
ATOM   4731  CA  PRO B  35      25.563  25.019 -58.996  1.00 70.97           C  
ANISOU 4731  CA  PRO B  35     8944  11135   6885    754   1589   2917       C  
ATOM   4732  C   PRO B  35      25.031  24.173 -60.146  1.00 57.59           C  
ANISOU 4732  C   PRO B  35     7295   9612   4974    933   1569   2832       C  
ATOM   4733  O   PRO B  35      25.559  23.115 -60.495  1.00 53.69           O  
ANISOU 4733  O   PRO B  35     6789   9251   4360   1035   1583   2742       O  
ATOM   4734  CB  PRO B  35      26.215  26.306 -59.515  1.00 85.45           C  
ANISOU 4734  CB  PRO B  35    10702  12966   8798    696   1637   3095       C  
ATOM   4735  CG  PRO B  35      27.423  26.505 -58.656  1.00 82.65           C  
ANISOU 4735  CG  PRO B  35    10270  12548   8586    579   1677   3134       C  
ATOM   4736  CD  PRO B  35      27.899  25.131 -58.309  1.00 73.27           C  
ANISOU 4736  CD  PRO B  35     9082  11441   7318    638   1684   3001       C  
ATOM   4737  N   PHE B  36      23.956  24.688 -60.749  1.00 59.03           N  
ANISOU 4737  N   PHE B  36     7531   9786   5112    975   1530   2859       N  
ATOM   4738  CA  PHE B  36      23.262  23.974 -61.818  1.00 64.02           C  
ANISOU 4738  CA  PHE B  36     8214  10564   5547   1142   1493   2769       C  
ATOM   4739  C   PHE B  36      24.108  23.896 -63.083  1.00 70.03           C  
ANISOU 4739  C   PHE B  36     8909  11515   6185   1253   1548   2824       C  
ATOM   4740  O   PHE B  36      24.143  22.853 -63.748  1.00 75.14           O  
ANISOU 4740  O   PHE B  36     9571  12307   6671   1395   1533   2709       O  
ATOM   4741  CB  PHE B  36      21.924  24.661 -62.099  1.00 64.69           C  
ANISOU 4741  CB  PHE B  36     8365  10586   5630   1149   1437   2797       C  
ATOM   4742  CG  PHE B  36      21.196  24.129 -63.303  1.00 60.76           C  
ANISOU 4742  CG  PHE B  36     7912  10236   4937   1318   1396   2721       C  
ATOM   4743  CD1 PHE B  36      20.491  22.939 -63.235  1.00 60.03           C  
ANISOU 4743  CD1 PHE B  36     7892  10181   4734   1410   1327   2536       C  
ATOM   4744  CD2 PHE B  36      21.193  24.836 -64.495  1.00 68.64           C  
ANISOU 4744  CD2 PHE B  36     8881  11332   5867   1385   1420   2830       C  
ATOM   4745  CE1 PHE B  36      19.810  22.456 -64.338  1.00 60.98           C  
ANISOU 4745  CE1 PHE B  36     8054  10433   4683   1564   1278   2452       C  
ATOM   4746  CE2 PHE B  36      20.515  24.358 -65.602  1.00 64.35           C  
ANISOU 4746  CE2 PHE B  36     8377  10926   5148   1542   1377   2756       C  
ATOM   4747  CZ  PHE B  36      19.820  23.169 -65.522  1.00 65.63           C  
ANISOU 4747  CZ  PHE B  36     8609  11122   5205   1631   1303   2562       C  
ATOM   4748  N   GLU B  37      24.793  24.988 -63.435  1.00 67.24           N  
ANISOU 4748  N   GLU B  37     8480  11163   5906   1194   1607   2996       N  
ATOM   4749  CA  GLU B  37      25.594  24.996 -64.656  1.00 71.33           C  
ANISOU 4749  CA  GLU B  37     8930  11864   6310   1298   1663   3066       C  
ATOM   4750  C   GLU B  37      26.743  23.999 -64.584  1.00 70.61           C  
ANISOU 4750  C   GLU B  37     8783  11880   6165   1346   1703   2997       C  
ATOM   4751  O   GLU B  37      27.175  23.476 -65.617  1.00 68.12           O  
ANISOU 4751  O   GLU B  37     8437  11745   5702   1483   1727   2978       O  
ATOM   4752  CB  GLU B  37      26.127  26.404 -64.926  1.00 76.43           C  
ANISOU 4752  CB  GLU B  37     9504  12473   7064   1210   1719   3270       C  
ATOM   4753  CG  GLU B  37      26.280  26.733 -66.403  1.00 96.08           C  
ANISOU 4753  CG  GLU B  37    11955  15132   9420   1330   1754   3363       C  
ATOM   4754  CD  GLU B  37      27.338  27.788 -66.659  1.00107.44           C  
ANISOU 4754  CD  GLU B  37    13293  16579  10950   1256   1830   3554       C  
ATOM   4755  OE1 GLU B  37      28.417  27.435 -67.179  1.00110.64           O  
ANISOU 4755  OE1 GLU B  37    13620  17129  11290   1315   1888   3584       O  
ATOM   4756  OE2 GLU B  37      27.090  28.971 -66.341  1.00110.46           O  
ANISOU 4756  OE2 GLU B  37    13675  16824  11472   1141   1828   3672       O  
ATOM   4757  N   ASP B  38      27.250  23.725 -63.380  1.00 60.07           N  
ANISOU 4757  N   ASP B  38     7434  10439   4949   1239   1709   2958       N  
ATOM   4758  CA  ASP B  38      28.303  22.725 -63.239  1.00 70.47           C  
ANISOU 4758  CA  ASP B  38     8705  11853   6219   1286   1741   2883       C  
ATOM   4759  C   ASP B  38      27.755  21.312 -63.385  1.00 73.67           C  
ANISOU 4759  C   ASP B  38     9184  12332   6475   1421   1685   2683       C  
ATOM   4760  O   ASP B  38      28.468  20.418 -63.856  1.00 75.38           O  
ANISOU 4760  O   ASP B  38     9368  12689   6582   1530   1704   2612       O  
ATOM   4761  CB  ASP B  38      29.003  22.883 -61.888  1.00 73.54           C  
ANISOU 4761  CB  ASP B  38     9056  12104   6783   1131   1761   2901       C  
ATOM   4762  CG  ASP B  38      29.749  24.196 -61.768  1.00 80.47           C  
ANISOU 4762  CG  ASP B  38     9849  12917   7809   1005   1814   3085       C  
ATOM   4763  OD1 ASP B  38      29.571  25.067 -62.645  1.00 83.89           O  
ANISOU 4763  OD1 ASP B  38    10264  13389   8221   1025   1831   3204       O  
ATOM   4764  OD2 ASP B  38      30.515  24.357 -60.794  1.00 80.67           O  
ANISOU 4764  OD2 ASP B  38     9826  12852   7972    887   1835   3107       O  
ATOM   4765  N   HIS B  39      26.498  21.091 -62.995  1.00 65.53           N  
ANISOU 4765  N   HIS B  39     8251  11208   5440   1417   1612   2586       N  
ATOM   4766  CA  HIS B  39      25.921  19.753 -63.072  1.00 62.13           C  
ANISOU 4766  CA  HIS B  39     7897  10832   4880   1537   1547   2386       C  
ATOM   4767  C   HIS B  39      25.618  19.365 -64.515  1.00 58.92           C  
ANISOU 4767  C   HIS B  39     7503  10597   4287   1714   1525   2337       C  
ATOM   4768  O   HIS B  39      26.001  18.281 -64.969  1.00 57.22           O  
ANISOU 4768  O   HIS B  39     7287  10502   3951   1841   1513   2213       O  
ATOM   4769  CB  HIS B  39      24.658  19.679 -62.213  1.00 70.01           C  
ANISOU 4769  CB  HIS B  39     8991  11676   5932   1476   1472   2303       C  
ATOM   4770  CG  HIS B  39      24.927  19.426 -60.761  1.00 70.58           C  
ANISOU 4770  CG  HIS B  39     9067  11604   6144   1349   1473   2263       C  
ATOM   4771  ND1 HIS B  39      24.745  20.388 -59.791  1.00 72.25           N  
ANISOU 4771  ND1 HIS B  39     9270  11630   6553   1179   1471   2348       N  
ATOM   4772  CD2 HIS B  39      25.364  18.320 -60.115  1.00 75.53           C  
ANISOU 4772  CD2 HIS B  39     9700  12199   6800   1352   1443   2106       C  
ATOM   4773  CE1 HIS B  39      25.057  19.885 -58.610  1.00 70.94           C  
ANISOU 4773  CE1 HIS B  39     9103  11332   6521   1085   1444   2245       C  
ATOM   4774  NE2 HIS B  39      25.436  18.631 -58.779  1.00 68.78           N  
ANISOU 4774  NE2 HIS B  39     8838  11146   6149   1186   1427   2102       N  
ATOM   4775  N   VAL B  40      24.927  20.240 -65.252  1.00 62.29           N  
ANISOU 4775  N   VAL B  40     7941  11036   4690   1729   1516   2429       N  
ATOM   4776  CA  VAL B  40      24.591  19.941 -66.643  1.00 65.20           C  
ANISOU 4776  CA  VAL B  40     8320  11569   4885   1898   1493   2388       C  
ATOM   4777  C   VAL B  40      25.855  19.732 -67.465  1.00 60.68           C  
ANISOU 4777  C   VAL B  40     7655  11165   4234   1984   1564   2440       C  
ATOM   4778  O   VAL B  40      25.898  18.880 -68.361  1.00 61.70           O  
ANISOU 4778  O   VAL B  40     7791  11443   4209   2144   1540   2333       O  
ATOM   4779  CB  VAL B  40      23.711  21.058 -67.233  1.00 59.59           C  
ANISOU 4779  CB  VAL B  40     7629  10835   4179   1886   1481   2504       C  
ATOM   4780  CG1 VAL B  40      23.367  20.762 -68.686  1.00 61.26           C  
ANISOU 4780  CG1 VAL B  40     7847  11221   4208   2063   1457   2464       C  
ATOM   4781  CG2 VAL B  40      22.451  21.211 -66.414  1.00 62.54           C  
ANISOU 4781  CG2 VAL B  40     8092  11047   4625   1810   1407   2446       C  
ATOM   4782  N   LYS B  41      26.906  20.498 -67.166  1.00 61.06           N  
ANISOU 4782  N   LYS B  41     7615  11193   4392   1880   1647   2600       N  
ATOM   4783  CA  LYS B  41      28.177  20.320 -67.860  1.00 70.32           C  
ANISOU 4783  CA  LYS B  41     8692  12525   5501   1953   1718   2658       C  
ATOM   4784  C   LYS B  41      28.704  18.900 -67.694  1.00 62.39           C  
ANISOU 4784  C   LYS B  41     7693  11595   4417   2046   1699   2486       C  
ATOM   4785  O   LYS B  41      29.182  18.290 -68.658  1.00 63.83           O  
ANISOU 4785  O   LYS B  41     7843  11949   4461   2195   1711   2442       O  
ATOM   4786  CB  LYS B  41      29.198  21.335 -67.349  1.00 79.17           C  
ANISOU 4786  CB  LYS B  41     9721  13584   6777   1805   1799   2843       C  
ATOM   4787  CG  LYS B  41      30.593  21.136 -67.910  1.00 81.44           C  
ANISOU 4787  CG  LYS B  41     9902  14028   7014   1865   1873   2905       C  
ATOM   4788  CD  LYS B  41      31.637  21.828 -67.053  1.00 77.97           C  
ANISOU 4788  CD  LYS B  41     9380  13500   6747   1706   1935   3033       C  
ATOM   4789  CE  LYS B  41      32.776  22.358 -67.908  1.00 77.19           C  
ANISOU 4789  CE  LYS B  41     9165  13545   6620   1738   2017   3189       C  
ATOM   4790  NZ  LYS B  41      34.103  21.865 -67.450  1.00 79.78           N  
ANISOU 4790  NZ  LYS B  41     9411  13919   6982   1719   2065   3183       N  
ATOM   4791  N   LEU B  42      28.616  18.351 -66.481  1.00 73.62           N  
ANISOU 4791  N   LEU B  42     9157  12889   5925   1965   1669   2384       N  
ATOM   4792  CA  LEU B  42      29.105  16.998 -66.245  1.00 72.09           C  
ANISOU 4792  CA  LEU B  42     8974  12751   5667   2049   1647   2217       C  
ATOM   4793  C   LEU B  42      28.149  15.938 -66.777  1.00 60.28           C  
ANISOU 4793  C   LEU B  42     7571  11304   4029   2198   1554   2017       C  
ATOM   4794  O   LEU B  42      28.601  14.889 -67.249  1.00 64.47           O  
ANISOU 4794  O   LEU B  42     8096  11950   4451   2332   1537   1893       O  
ATOM   4795  CB  LEU B  42      29.356  16.783 -64.751  1.00 67.77           C  
ANISOU 4795  CB  LEU B  42     8438  12050   5262   1912   1648   2182       C  
ATOM   4796  CG  LEU B  42      30.380  17.727 -64.114  1.00 64.39           C  
ANISOU 4796  CG  LEU B  42     7914  11562   4988   1761   1730   2357       C  
ATOM   4797  CD1 LEU B  42      30.132  17.869 -62.621  1.00 72.14           C  
ANISOU 4797  CD1 LEU B  42     8929  12350   6130   1601   1713   2341       C  
ATOM   4798  CD2 LEU B  42      31.798  17.245 -64.384  1.00 59.57           C  
ANISOU 4798  CD2 LEU B  42     7211  11085   4339   1821   1790   2371       C  
ATOM   4799  N   VAL B  43      26.839  16.186 -66.713  1.00 61.62           N  
ANISOU 4799  N   VAL B  43     7825  11388   4201   2179   1487   1977       N  
ATOM   4800  CA  VAL B  43      25.874  15.218 -67.227  1.00 64.45           C  
ANISOU 4800  CA  VAL B  43     8270  11785   4433   2314   1387   1782       C  
ATOM   4801  C   VAL B  43      26.013  15.074 -68.738  1.00 63.17           C  
ANISOU 4801  C   VAL B  43     8077  11812   4114   2483   1389   1779       C  
ATOM   4802  O   VAL B  43      25.912  13.968 -69.282  1.00 62.22           O  
ANISOU 4802  O   VAL B  43     7988  11777   3876   2629   1329   1607       O  
ATOM   4803  CB  VAL B  43      24.444  15.621 -66.822  1.00 69.01           C  
ANISOU 4803  CB  VAL B  43     8936  12230   5054   2249   1317   1756       C  
ATOM   4804  CG1 VAL B  43      23.423  14.686 -67.455  1.00 70.46           C  
ANISOU 4804  CG1 VAL B  43     9203  12459   5109   2391   1206   1556       C  
ATOM   4805  CG2 VAL B  43      24.300  15.620 -65.308  1.00 60.73           C  
ANISOU 4805  CG2 VAL B  43     7922  11002   4151   2097   1310   1739       C  
ATOM   4806  N   ASN B  44      26.250  16.186 -69.439  1.00 64.72           N  
ANISOU 4806  N   ASN B  44     8210  12073   4308   2469   1455   1968       N  
ATOM   4807  CA  ASN B  44      26.447  16.118 -70.883  1.00 67.37           C  
ANISOU 4807  CA  ASN B  44     8506  12598   4493   2629   1466   1985       C  
ATOM   4808  C   ASN B  44      27.676  15.287 -71.231  1.00 66.02           C  
ANISOU 4808  C   ASN B  44     8270  12564   4252   2730   1505   1937       C  
ATOM   4809  O   ASN B  44      27.635  14.457 -72.147  1.00 72.17           O  
ANISOU 4809  O   ASN B  44     9058  13474   4888   2899   1463   1815       O  
ATOM   4810  CB  ASN B  44      26.566  17.528 -71.464  1.00 68.92           C  
ANISOU 4810  CB  ASN B  44     8642  12828   4717   2580   1538   2213       C  
ATOM   4811  CG  ASN B  44      25.246  18.275 -71.458  1.00 74.36           C  
ANISOU 4811  CG  ASN B  44     9399  13418   5435   2529   1488   2245       C  
ATOM   4812  OD1 ASN B  44      24.175  17.671 -71.535  1.00 64.93           O  
ANISOU 4812  OD1 ASN B  44     8291  12199   4180   2593   1394   2088       O  
ATOM   4813  ND2 ASN B  44      25.316  19.599 -71.366  1.00 78.20           N  
ANISOU 4813  ND2 ASN B  44     9846  13846   6020   2415   1546   2447       N  
ATOM   4814  N   GLU B  45      28.778  15.492 -70.504  1.00 71.54           N  
ANISOU 4814  N   GLU B  45     8900  13231   5052   2630   1580   2029       N  
ATOM   4815  CA  GLU B  45      29.985  14.708 -70.747  1.00 72.75           C  
ANISOU 4815  CA  GLU B  45     8987  13510   5146   2720   1617   1987       C  
ATOM   4816  C   GLU B  45      29.758  13.228 -70.471  1.00 78.47           C  
ANISOU 4816  C   GLU B  45     9782  14222   5812   2815   1531   1742       C  
ATOM   4817  O   GLU B  45      30.361  12.375 -71.133  1.00 81.65           O  
ANISOU 4817  O   GLU B  45    10156  14761   6106   2962   1525   1654       O  
ATOM   4818  CB  GLU B  45      31.137  15.226 -69.883  1.00 72.07           C  
ANISOU 4818  CB  GLU B  45     8816  13371   5196   2579   1705   2125       C  
ATOM   4819  CG  GLU B  45      31.528  16.672 -70.129  1.00 73.61           C  
ANISOU 4819  CG  GLU B  45     8931  13572   5465   2480   1789   2368       C  
ATOM   4820  CD  GLU B  45      32.259  17.282 -68.944  1.00 77.91           C  
ANISOU 4820  CD  GLU B  45     9424  13988   6189   2294   1846   2480       C  
ATOM   4821  OE1 GLU B  45      32.858  18.367 -69.103  1.00 66.80           O  
ANISOU 4821  OE1 GLU B  45     7935  12591   4854   2213   1918   2674       O  
ATOM   4822  OE2 GLU B  45      32.232  16.675 -67.852  1.00 78.73           O  
ANISOU 4822  OE2 GLU B  45     9568  13978   6366   2230   1815   2372       O  
ATOM   4823  N   VAL B  46      28.900  12.913 -69.514  1.00 76.89           N  
ANISOU 4823  N   VAL B  46     9673  13858   5685   2736   1463   1630       N  
ATOM   4824  CA  VAL B  46      28.746  11.476 -69.179  1.00 66.80           C  
ANISOU 4824  CA  VAL B  46     8463  12543   4377   2807   1380   1399       C  
ATOM   4825  C   VAL B  46      28.083  10.807 -70.372  1.00 67.63           C  
ANISOU 4825  C   VAL B  46     8613  12757   4327   2996   1295   1239       C  
ATOM   4826  O   VAL B  46      28.564   9.760 -70.792  1.00 68.72           O  
ANISOU 4826  O   VAL B  46     8736  12992   4382   3128   1274   1122       O  
ATOM   4827  CB  VAL B  46      27.887  11.290 -67.910  1.00 68.86           C  
ANISOU 4827  CB  VAL B  46     8812  12604   4749   2678   1323   1325       C  
ATOM   4828  CG1 VAL B  46      27.265   9.906 -67.809  1.00 65.99           C  
ANISOU 4828  CG1 VAL B  46     8541  12201   4330   2774   1208   1069       C  
ATOM   4829  CG2 VAL B  46      28.622  11.635 -66.631  1.00 65.45           C  
ANISOU 4829  CG2 VAL B  46     8335  12070   4461   2522   1393   1420       C  
ATOM   4830  N   THR B  47      27.025  11.413 -70.897  1.00 67.65           N  
ANISOU 4830  N   THR B  47     8670  12743   4291   3014   1240   1230       N  
ATOM   4831  CA  THR B  47      26.218  10.727 -71.940  1.00 71.50           C  
ANISOU 4831  CA  THR B  47     9211  13310   4647   3182   1142   1057       C  
ATOM   4832  C   THR B  47      26.893  10.855 -73.307  1.00 74.94           C  
ANISOU 4832  C   THR B  47     9575  13950   4949   3328   1183   1130       C  
ATOM   4833  O   THR B  47      26.663   9.982 -74.131  1.00 69.13           O  
ANISOU 4833  O   THR B  47     8872  13298   4096   3482   1105    990       O  
ATOM   4834  CB  THR B  47      24.748  11.156 -71.853  1.00 82.05           C  
ANISOU 4834  CB  THR B  47    10636  14544   5997   3146   1055   1000       C  
ATOM   4835  OG1 THR B  47      23.969  10.253 -72.636  1.00 89.57           O  
ANISOU 4835  OG1 THR B  47    11621  15595   6817   3312    969    865       O  
ATOM   4836  CG2 THR B  47      24.527  12.578 -72.313  1.00 85.44           C  
ANISOU 4836  CG2 THR B  47    11037  14941   6486   3028   1124   1221       C  
ATOM   4837  N   GLU B  48      27.708  11.890 -73.510  1.00 81.18           N  
ANISOU 4837  N   GLU B  48    10267  14821   5755   3284   1300   1345       N  
ATOM   4838  CA  GLU B  48      28.503  11.995 -74.766  1.00 80.09           C  
ANISOU 4838  CA  GLU B  48    10052  14891   5488   3432   1346   1406       C  
ATOM   4839  C   GLU B  48      29.477  10.832 -74.734  1.00 85.43           C  
ANISOU 4839  C   GLU B  48    10689  15654   6116   3533   1351   1302       C  
ATOM   4840  O   GLU B  48      29.626  10.175 -75.759  1.00 91.03           O  
ANISOU 4840  O   GLU B  48    11377  16520   6690   3709   1327   1228       O  
ATOM   4841  CB  GLU B  48      29.359  13.258 -74.777  1.00 78.11           C  
ANISOU 4841  CB  GLU B  48     9708  14694   5278   3348   1465   1672       C  
ATOM   4842  CG  GLU B  48      29.407  13.942 -76.122  1.00 96.07           C  
ANISOU 4842  CG  GLU B  48    11976  17063   7462   3418   1467   1763       C  
ATOM   4843  CD  GLU B  48      28.360  15.027 -76.268  1.00105.21           C  
ANISOU 4843  CD  GLU B  48    13077  18187   8710   3281   1560   2017       C  
ATOM   4844  OE1 GLU B  48      27.301  14.748 -76.858  1.00108.32           O  
ANISOU 4844  OE1 GLU B  48    13501  18570   9088   3274   1542   2082       O  
ATOM   4845  OE2 GLU B  48      28.607  16.142 -75.782  1.00108.75           O  
ANISOU 4845  OE2 GLU B  48    13451  18620   9250   3180   1646   2148       O  
ATOM   4846  N   PHE B  49      30.065  10.572 -73.564  1.00 86.26           N  
ANISOU 4846  N   PHE B  49    10783  15660   6331   3426   1380   1298       N  
ATOM   4847  CA  PHE B  49      31.001   9.428 -73.398  1.00 84.17           C  
ANISOU 4847  CA  PHE B  49    10507  15438   6035   3516   1360   1159       C  
ATOM   4848  C   PHE B  49      30.273   8.079 -73.422  1.00 77.14           C  
ANISOU 4848  C   PHE B  49     9717  14505   5086   3629   1225    898       C  
ATOM   4849  O   PHE B  49      30.912   7.060 -73.641  1.00 82.80           O  
ANISOU 4849  O   PHE B  49    10426  15332   5703   3792   1184    771       O  
ATOM   4850  CB  PHE B  49      31.811   9.593 -72.113  1.00 89.11           C  
ANISOU 4850  CB  PHE B  49    11110  15943   6805   3362   1412   1206       C  
ATOM   4851  N   ALA B  50      28.979   8.074 -73.161  1.00 77.38           N  
ANISOU 4851  N   ALA B  50     9844  14377   5181   3547   1148    815       N  
ATOM   4852  CA  ALA B  50      28.223   6.803 -73.122  1.00 79.75           C  
ANISOU 4852  CA  ALA B  50    10241  14627   5435   3646   1010    571       C  
ATOM   4853  C   ALA B  50      27.792   6.465 -74.545  1.00 73.44           C  
ANISOU 4853  C   ALA B  50     9435  13984   4486   3825    965    520       C  
ATOM   4854  O   ALA B  50      27.678   5.298 -74.870  1.00 71.77           O  
ANISOU 4854  O   ALA B  50     9256  13811   4202   3969    875    327       O  
ATOM   4855  CB  ALA B  50      27.032   6.958 -72.215  1.00 78.30           C  
ANISOU 4855  CB  ALA B  50    10151  14256   5345   3520    942    518       C  
ATOM   4856  N   LYS B  51      27.554   7.504 -75.332  1.00 79.50           N  
ANISOU 4856  N   LYS B  51    10159  14840   5207   3821   1025    692       N  
ATOM   4857  CA  LYS B  51      27.181   7.300 -76.747  1.00 83.39           C  
ANISOU 4857  CA  LYS B  51    10638  15495   5552   3993    992    662       C  
ATOM   4858  C   LYS B  51      28.327   6.527 -77.395  1.00 81.24           C  
ANISOU 4858  C   LYS B  51    10303  15391   5173   4160   1007    608       C  
ATOM   4859  O   LYS B  51      28.048   5.561 -78.109  1.00 85.13           O  
ANISOU 4859  O   LYS B  51    10819  15971   5555   4329    923    457       O  
ATOM   4860  CB  LYS B  51      26.973   8.674 -77.387  1.00 88.17           C  
ANISOU 4860  CB  LYS B  51    11191  16176   6134   3952   1076    890       C  
ATOM   4861  CG  LYS B  51      25.585   9.278 -77.226  1.00 82.85           C  
ANISOU 4861  CG  LYS B  51    10590  15390   5500   3872   1021    894       C  
ATOM   4862  CD  LYS B  51      25.597  10.789 -77.287  1.00 82.40           C  
ANISOU 4862  CD  LYS B  51    10481  15334   5494   3753   1126   1152       C  
ATOM   4863  CE  LYS B  51      24.282  11.411 -76.877  1.00 80.77           C  
ANISOU 4863  CE  LYS B  51    10346  15021   5321   3685   1068   1157       C  
ATOM   4864  NZ  LYS B  51      24.078  12.727 -77.526  1.00 73.69           N  
ANISOU 4864  NZ  LYS B  51     9398  14199   4402   3665   1145   1376       N  
ATOM   4865  N   THR B  52      29.561   6.926 -77.098  1.00 75.80           N  
ANISOU 4865  N   THR B  52     9533  14749   4518   4118   1108    727       N  
ATOM   4866  CA  THR B  52      30.752   6.225 -77.634  1.00 83.95           C  
ANISOU 4866  CA  THR B  52    10499  15950   5448   4278   1128    688       C  
ATOM   4867  C   THR B  52      30.759   4.727 -77.292  1.00 77.18           C  
ANISOU 4867  C   THR B  52     9697  15025   4603   4346   1033    451       C  
ATOM   4868  O   THR B  52      31.365   3.982 -78.050  1.00 78.82           O  
ANISOU 4868  O   THR B  52     9876  15363   4709   4514   1006    357       O  
ATOM   4869  CB  THR B  52      32.024   6.956 -77.203  1.00 87.13           C  
ANISOU 4869  CB  THR B  52    10788  16436   5882   4213   1269    904       C  
ATOM   4870  OG1 THR B  52      32.335   6.597 -75.859  1.00 84.23           O  
ANISOU 4870  OG1 THR B  52    10430  15911   5664   4046   1299    925       O  
ATOM   4871  CG2 THR B  52      31.916   8.458 -77.338  1.00 85.08           C  
ANISOU 4871  CG2 THR B  52    10468  16247   5612   4153   1361   1143       C  
ATOM   4872  N   CYS B  53      30.114   4.298 -76.207  1.00 79.02           N  
ANISOU 4872  N   CYS B  53    10008  15056   4959   4222    979    354       N  
ATOM   4873  CA  CYS B  53      30.117   2.893 -75.806  1.00 74.71           C  
ANISOU 4873  CA  CYS B  53     9525  14431   4432   4288    876    121       C  
ATOM   4874  C   CYS B  53      28.938   2.137 -76.399  1.00 80.09           C  
ANISOU 4874  C   CYS B  53    10294  15077   5059   4395    730    -88       C  
ATOM   4875  O   CYS B  53      29.038   0.927 -76.631  1.00 82.45           O  
ANISOU 4875  O   CYS B  53    10624  15378   5323   4519    638   -282       O  
ATOM   4876  CB  CYS B  53      30.067   2.753 -74.291  1.00 84.64           C  
ANISOU 4876  CB  CYS B  53    10829  15486   5844   4119    873     93       C  
ATOM   4877  SG  CYS B  53      31.622   2.991 -73.401  1.00 87.07           S  
ANISOU 4877  SG  CYS B  53    11045  15809   6227   4026   1002    238       S  
ATOM   4878  N   VAL B  54      27.800   2.804 -76.603  1.00 78.02           N  
ANISOU 4878  N   VAL B  54    10074  14770   4800   4344    700    -58       N  
ATOM   4879  CA  VAL B  54      26.748   2.152 -77.368  1.00 83.47           C  
ANISOU 4879  CA  VAL B  54    10831  15460   5423   4464    566   -242       C  
ATOM   4880  C   VAL B  54      27.228   1.900 -78.789  1.00 79.34           C  
ANISOU 4880  C   VAL B  54    10249  15156   4741   4670    569   -252       C  
ATOM   4881  O   VAL B  54      26.768   0.963 -79.449  1.00 87.55           O  
ANISOU 4881  O   VAL B  54    11329  16218   5716   4812    452   -444       O  
ATOM   4882  CB  VAL B  54      25.451   2.977 -77.336  1.00 85.91           C  
ANISOU 4882  CB  VAL B  54    11190  15689   5762   4372    538   -196       C  
ATOM   4883  CG1 VAL B  54      24.289   2.127 -77.821  1.00 90.32           C  
ANISOU 4883  CG1 VAL B  54    11830  16197   6291   4467    378   -423       C  
ATOM   4884  CG2 VAL B  54      25.160   3.470 -75.925  1.00 81.39           C  
ANISOU 4884  CG2 VAL B  54    10656  14927   5342   4161    566   -133       C  
ATOM   4885  N   ALA B  55      28.182   2.702 -79.269  1.00 88.96           N  
ANISOU 4885  N   ALA B  55    11366  16537   5896   4689    699    -48       N  
ATOM   4886  CA  ALA B  55      28.810   2.484 -80.566  1.00 88.25           C  
ANISOU 4886  CA  ALA B  55    11208  16670   5652   4885    718    -40       C  
ATOM   4887  C   ALA B  55      29.707   1.251 -80.526  1.00 93.54           C  
ANISOU 4887  C   ALA B  55    11866  17376   6299   4998    680   -184       C  
ATOM   4888  O   ALA B  55      29.379   0.224 -81.130  1.00 99.41           O  
ANISOU 4888  O   ALA B  55    12650  18145   6976   5150    565   -383       O  
ATOM   4889  CB  ALA B  55      29.606   3.719 -80.987  1.00 83.36           C  
ANISOU 4889  CB  ALA B  55    10482  16203   4990   4857    871    230       C  
ATOM   4890  N   ASP B  56      30.841   1.335 -79.825  1.00 95.96           N  
ANISOU 4890  N   ASP B  56    12116  17683   6662   4928    772    -87       N  
ATOM   4891  CA  ASP B  56      31.703   0.179 -79.586  1.00 99.62           C  
ANISOU 4891  CA  ASP B  56    12572  18153   7124   5013    738   -220       C  
ATOM   4892  C   ASP B  56      31.796  -0.055 -78.083  1.00 99.08           C  
ANISOU 4892  C   ASP B  56    12550  17880   7217   4844    737   -252       C  
ATOM   4893  O   ASP B  56      32.377   0.759 -77.357  1.00 96.01           O  
ANISOU 4893  O   ASP B  56    12111  17466   6903   4701    850    -74       O  
ATOM   4894  CB  ASP B  56      33.090   0.357 -80.202  1.00106.63           C  
ANISOU 4894  CB  ASP B  56    13343  19254   7917   5112    844    -89       C  
ATOM   4895  CG  ASP B  56      33.986  -0.844 -79.953  1.00110.43           C  
ANISOU 4895  CG  ASP B  56    13817  19745   8395   5205    806   -228       C  
ATOM   4896  OD1 ASP B  56      33.516  -1.983 -80.150  1.00112.13           O  
ANISOU 4896  OD1 ASP B  56    14105  19909   8592   5314    673   -454       O  
ATOM   4897  OD2 ASP B  56      35.145  -0.663 -79.537  1.00112.34           O  
ANISOU 4897  OD2 ASP B  56    13984  20040   8662   5166    902   -113       O  
ATOM   4898  N   GLU B  57      31.221  -1.171 -77.622  1.00 99.78           N  
ANISOU 4898  N   GLU B  57    12732  17819   7361   4862    607   -478       N  
ATOM   4899  CA  GLU B  57      31.195  -1.496 -76.200  1.00105.51           C  
ANISOU 4899  CA  GLU B  57    13512  18340   8238   4712    592   -530       C  
ATOM   4900  C   GLU B  57      32.508  -2.084 -75.703  1.00110.98           C  
ANISOU 4900  C   GLU B  57    14155  19059   8953   4735    637   -534       C  
ATOM   4901  O   GLU B  57      32.729  -2.125 -74.489  1.00111.15           O  
ANISOU 4901  O   GLU B  57    14197  18939   9097   4600    661   -523       O  
ATOM   4902  CB  GLU B  57      30.057  -2.476 -75.896  1.00105.93           C  
ANISOU 4902  CB  GLU B  57    13682  18215   8351   4718    430   -769       C  
ATOM   4903  CG  GLU B  57      28.922  -1.884 -75.073  1.00103.80           C  
ANISOU 4903  CG  GLU B  57    13481  17766   8191   4541    409   -748       C  
ATOM   4904  CD  GLU B  57      27.978  -2.941 -74.528  1.00105.98           C  
ANISOU 4904  CD  GLU B  57    13867  17844   8556   4524    256   -981       C  
ATOM   4905  OE1 GLU B  57      28.095  -4.115 -74.938  1.00107.33           O  
ANISOU 4905  OE1 GLU B  57    14063  18019   8697   4660    155  -1164       O  
ATOM   4906  OE2 GLU B  57      27.119  -2.595 -73.688  1.00106.28           O  
ANISOU 4906  OE2 GLU B  57    13965  17720   8698   4374    233   -980       O  
ATOM   4907  N   SER B  58      33.384  -2.466 -76.637  1.00115.18           N  
ANISOU 4907  N   SER B  58    14624  19769   9369   4907    648   -552       N  
ATOM   4908  CA  SER B  58      34.704  -3.037 -76.264  1.00118.55           C  
ANISOU 4908  CA  SER B  58    14994  20246   9805   4942    697   -543       C  
ATOM   4909  C   SER B  58      35.703  -1.914 -75.973  1.00119.03           C  
ANISOU 4909  C   SER B  58    14926  20484   9814   4924    854   -299       C  
ATOM   4910  O   SER B  58      35.410  -0.762 -76.364  1.00121.63           O  
ANISOU 4910  O   SER B  58    15180  20988  10047   5060    888   -278       O  
ATOM   4911  CB  SER B  58      35.212  -3.954 -77.344  1.00126.15           C  
ANISOU 4911  CB  SER B  58    15975  21274  10684   5147    591   -744       C  
ATOM   4912  OG  SER B  58      34.198  -4.205 -78.305  1.00129.03           O  
ANISOU 4912  OG  SER B  58    16449  21498  11077   5180    439   -956       O  
ATOM   4913  N   ASN B  61      36.354   2.697 -71.635  1.00131.00           N  
ANISOU 4913  N   ASN B  61    16311  21519  11943   3913   1312    527       N  
ATOM   4914  CA  ASN B  61      36.093   2.444 -70.193  1.00119.40           C  
ANISOU 4914  CA  ASN B  61    14922  19846  10599   3800   1263    420       C  
ATOM   4915  C   ASN B  61      34.655   1.939 -70.107  1.00113.82           C  
ANISOU 4915  C   ASN B  61    14343  19005   9898   3807   1140    250       C  
ATOM   4916  O   ASN B  61      33.988   2.222 -69.092  1.00116.35           O  
ANISOU 4916  O   ASN B  61    14728  19153  10328   3666   1119    235       O  
ATOM   4917  CB  ASN B  61      36.277   3.708 -69.352  1.00114.37           C  
ANISOU 4917  CB  ASN B  61    14242  19119  10095   3591   1359    607       C  
ATOM   4918  CG  ASN B  61      37.725   4.127 -69.220  1.00109.54           C  
ANISOU 4918  CG  ASN B  61    13494  18647   9481   3568   1483    810       C  
ATOM   4919  OD1 ASN B  61      38.039   5.314 -69.259  1.00107.78           O  
ANISOU 4919  OD1 ASN B  61    13207  18566   9177   3620   1532    933       O  
ATOM   4920  ND2 ASN B  61      38.615   3.160 -69.065  1.00103.61           N  
ANISOU 4920  ND2 ASN B  61    12694  17855   8818   3491   1532    845       N  
ATOM   4921  N   CYS B  62      34.201   1.231 -71.144  1.00103.67           N  
ANISOU 4921  N   CYS B  62    13093  17799   8498   3970   1056    123       N  
ATOM   4922  CA  CYS B  62      32.810   0.791 -71.193  1.00 93.14           C  
ANISOU 4922  CA  CYS B  62    11874  16346   7170   3983    933    -42       C  
ATOM   4923  C   CYS B  62      32.534  -0.268 -70.140  1.00 92.09           C  
ANISOU 4923  C   CYS B  62    11828  16029   7132   3947    842   -230       C  
ATOM   4924  O   CYS B  62      31.473  -0.261 -69.509  1.00103.30           O  
ANISOU 4924  O   CYS B  62    13334  17286   8629   3851    778   -298       O  
ATOM   4925  CB  CYS B  62      32.470   0.224 -72.569  1.00 89.88           C  
ANISOU 4925  CB  CYS B  62    11474  16059   6618   4177    854   -156       C  
ATOM   4926  SG  CYS B  62      32.662   1.347 -73.958  1.00 89.33           S  
ANISOU 4926  SG  CYS B  62    11311  16212   6417   4249    943     41       S  
ATOM   4927  N   ASP B  63      33.451  -1.220 -69.978  1.00 88.92           N  
ANISOU 4927  N   ASP B  63    11408  15652   6726   4030    829   -321       N  
ATOM   4928  CA  ASP B  63      33.250  -2.363 -69.098  1.00 86.72           C  
ANISOU 4928  CA  ASP B  63    11212  15205   6531   4022    733   -514       C  
ATOM   4929  C   ASP B  63      33.406  -2.015 -67.623  1.00 82.55           C  
ANISOU 4929  C   ASP B  63    10693  14531   6142   3841    787   -446       C  
ATOM   4930  O   ASP B  63      33.396  -2.921 -66.786  1.00 76.08           O  
ANISOU 4930  O   ASP B  63     9933  13574   5401   3827    723   -587       O  
ATOM   4931  CB  ASP B  63      34.222  -3.482 -69.482  1.00 91.90           C  
ANISOU 4931  CB  ASP B  63    11841  15946   7131   4183    700   -628       C  
ATOM   4932  CG  ASP B  63      35.660  -3.156 -69.123  1.00 96.90           C  
ANISOU 4932  CG  ASP B  63    12368  16677   7772   4159    825   -482       C  
ATOM   4933  OD1 ASP B  63      36.055  -1.973 -69.200  1.00 99.72           O  
ANISOU 4933  OD1 ASP B  63    12643  17124   8123   4078    944   -269       O  
ATOM   4934  OD2 ASP B  63      36.400  -4.096 -68.764  1.00 98.22           O  
ANISOU 4934  OD2 ASP B  63    12534  16828   7958   4222    798   -580       O  
ATOM   4935  N   LYS B  64      33.549  -0.736 -67.289  1.00 83.28           N  
ANISOU 4935  N   LYS B  64    10728  14644   6272   3705    900   -235       N  
ATOM   4936  CA  LYS B  64      33.690  -0.325 -65.903  1.00 83.35           C  
ANISOU 4936  CA  LYS B  64    10738  14519   6410   3531    954   -160       C  
ATOM   4937  C   LYS B  64      32.333  -0.315 -65.205  1.00 78.46           C  
ANISOU 4937  C   LYS B  64    10229  13712   5871   3428    875   -244       C  
ATOM   4938  O   LYS B  64      31.275  -0.442 -65.830  1.00 76.01           O  
ANISOU 4938  O   LYS B  64     9983  13382   5517   3476    789   -333       O  
ATOM   4939  CB  LYS B  64      34.332   1.058 -65.818  1.00 80.48           C  
ANISOU 4939  CB  LYS B  64    10270  14239   6069   3419   1097     99       C  
ATOM   4940  CG  LYS B  64      35.828   1.073 -66.069  1.00 72.11           C  
ANISOU 4940  CG  LYS B  64     9095  13329   4976   3474   1187    196       C  
ATOM   4941  CD  LYS B  64      36.430   2.409 -65.669  1.00 70.25           C  
ANISOU 4941  CD  LYS B  64     8761  13122   4807   3324   1317    443       C  
ATOM   4942  CE  LYS B  64      37.946   2.345 -65.632  1.00 76.06           C  
ANISOU 4942  CE  LYS B  64     9384  13976   5540   3353   1400    527       C  
ATOM   4943  NZ  LYS B  64      38.545   3.668 -65.305  1.00 77.96           N  
ANISOU 4943  NZ  LYS B  64     9523  14241   5855   3204   1520    768       N  
ATOM   4944  N   SER B  65      32.374  -0.164 -63.887  1.00 75.86           N  
ANISOU 4944  N   SER B  65     9917  13246   5659   3287    903   -215       N  
ATOM   4945  CA  SER B  65      31.167  -0.019 -63.091  1.00 74.87           C  
ANISOU 4945  CA  SER B  65     9886  12945   5617   3171    844   -268       C  
ATOM   4946  C   SER B  65      30.780   1.451 -62.996  1.00 76.91           C  
ANISOU 4946  C   SER B  65    10110  13214   5900   3036    927    -62       C  
ATOM   4947  O   SER B  65      31.625   2.344 -63.100  1.00 82.20           O  
ANISOU 4947  O   SER B  65    10680  13982   6570   2989   1043    131       O  
ATOM   4948  CB  SER B  65      31.365  -0.602 -61.690  1.00 67.57           C  
ANISOU 4948  CB  SER B  65     9002  11863   4811   3088    828   -341       C  
ATOM   4949  OG  SER B  65      32.288   0.169 -60.940  1.00 67.41           O  
ANISOU 4949  OG  SER B  65     8891  11845   4876   2963    944   -159       O  
ATOM   4950  N   LEU B  66      29.483   1.694 -62.798  1.00 72.65           N  
ANISOU 4950  N   LEU B  66     9652  12564   5389   2973    861   -105       N  
ATOM   4951  CA  LEU B  66      28.998   3.068 -62.711  1.00 69.11           C  
ANISOU 4951  CA  LEU B  66     9177  12098   4985   2840    922     81       C  
ATOM   4952  C   LEU B  66      29.473   3.756 -61.440  1.00 71.92           C  
ANISOU 4952  C   LEU B  66     9481  12315   5529   2638    989    222       C  
ATOM   4953  O   LEU B  66      29.720   4.968 -61.452  1.00 72.17           O  
ANISOU 4953  O   LEU B  66     9449  12398   5576   2553   1086    423       O  
ATOM   4954  CB  LEU B  66      27.473   3.094 -62.785  1.00 65.69           C  
ANISOU 4954  CB  LEU B  66     8830  11532   4597   2797    809     -9       C  
ATOM   4955  CG  LEU B  66      26.861   2.211 -63.869  1.00 67.36           C  
ANISOU 4955  CG  LEU B  66     9108  11832   4653   2985    708   -195       C  
ATOM   4956  CD1 LEU B  66      25.351   2.158 -63.729  1.00 71.21           C  
ANISOU 4956  CD1 LEU B  66     9677  12156   5224   2917    586   -295       C  
ATOM   4957  CD2 LEU B  66      27.255   2.731 -65.234  1.00 73.25           C  
ANISOU 4957  CD2 LEU B  66     9779  12769   5282   3088    759    -91       C  
ATOM   4958  N   HIS B  67      29.600   3.010 -60.341  1.00 68.48           N  
ANISOU 4958  N   HIS B  67     9073  11706   5242   2562    935    120       N  
ATOM   4959  CA  HIS B  67      30.084   3.596 -59.095  1.00 88.08           C  
ANISOU 4959  CA  HIS B  67    11506  14061   7900   2378    991    239       C  
ATOM   4960  C   HIS B  67      31.463   4.213 -59.282  1.00 92.23           C  
ANISOU 4960  C   HIS B  67    11919  14757   8366   2395   1130    411       C  
ATOM   4961  O   HIS B  67      31.713   5.348 -58.860  1.00 95.94           O  
ANISOU 4961  O   HIS B  67    12328  15207   8917   2260   1210    592       O  
ATOM   4962  CB  HIS B  67      30.115   2.535 -57.996  1.00 96.12           C  
ANISOU 4962  CB  HIS B  67    12570  14894   9056   2328    912     92       C  
ATOM   4963  CG  HIS B  67      28.789   2.303 -57.343  1.00 99.91           C  
ANISOU 4963  CG  HIS B  67    13137  15153   9670   2223    799    -10       C  
ATOM   4964  ND1 HIS B  67      28.630   1.463 -56.263  1.00101.78           N  
ANISOU 4964  ND1 HIS B  67    13419  15201  10052   2151    725   -124       N  
ATOM   4965  CD2 HIS B  67      27.560   2.800 -57.618  1.00101.41           C  
ANISOU 4965  CD2 HIS B  67    13374  15286   9872   2178    749    -10       C  
ATOM   4966  CE1 HIS B  67      27.360   1.450 -55.901  1.00101.25           C  
ANISOU 4966  CE1 HIS B  67    13420  14972  10079   2065    637   -188       C  
ATOM   4967  NE2 HIS B  67      26.689   2.255 -56.706  1.00 99.59           N  
ANISOU 4967  NE2 HIS B  67    13210  14837   9792   2080    649   -124       N  
ATOM   4968  N   THR B  68      32.375   3.478 -59.918  1.00 92.84           N  
ANISOU 4968  N   THR B  68    11964  15005   8304   2562   1159    356       N  
ATOM   4969  CA  THR B  68      33.708   4.002 -60.172  1.00 91.81           C  
ANISOU 4969  CA  THR B  68    11720  15059   8106   2591   1293    517       C  
ATOM   4970  C   THR B  68      33.784   4.859 -61.428  1.00 89.33           C  
ANISOU 4970  C   THR B  68    11345  14907   7690   2644   1348    654       C  
ATOM   4971  O   THR B  68      34.822   5.482 -61.665  1.00 94.35           O  
ANISOU 4971  O   THR B  68    11870  15644   8333   2622   1441    811       O  
ATOM   4972  CB  THR B  68      34.727   2.865 -60.273  1.00 96.21           C  
ANISOU 4972  CB  THR B  68    12252  15704   8598   2730   1290    404       C  
ATOM   4973  OG1 THR B  68      34.219   1.839 -61.134  1.00100.64           O  
ANISOU 4973  OG1 THR B  68    12885  16295   9058   2893   1186    215       O  
ATOM   4974  CG2 THR B  68      35.011   2.280 -58.896  1.00 88.98           C  
ANISOU 4974  CG2 THR B  68    11354  14601   7853   2625   1250    332       C  
ATOM   4975  N   LEU B  69      32.729   4.907 -62.239  1.00 79.40           N  
ANISOU 4975  N   LEU B  69    10151  13660   6359   2704   1284    599       N  
ATOM   4976  CA  LEU B  69      32.730   5.831 -63.367  1.00 85.26           C  
ANISOU 4976  CA  LEU B  69    10834  14528   7032   2732   1331    743       C  
ATOM   4977  C   LEU B  69      32.105   7.170 -63.000  1.00 88.71           C  
ANISOU 4977  C   LEU B  69    11268  14884   7553   2572   1373    911       C  
ATOM   4978  O   LEU B  69      32.621   8.223 -63.391  1.00 87.80           O  
ANISOU 4978  O   LEU B  69    11066  14842   7454   2521   1458   1103       O  
ATOM   4979  CB  LEU B  69      31.998   5.222 -64.565  1.00 86.66           C  
ANISOU 4979  CB  LEU B  69    11069  14779   7078   2894   1242    605       C  
ATOM   4980  CG  LEU B  69      31.968   6.086 -65.830  1.00 85.80           C  
ANISOU 4980  CG  LEU B  69    10904  14814   6881   2947   1285    740       C  
ATOM   4981  CD1 LEU B  69      33.364   6.579 -66.196  1.00 88.31           C  
ANISOU 4981  CD1 LEU B  69    11092  15273   7187   2957   1396    905       C  
ATOM   4982  CD2 LEU B  69      31.349   5.324 -66.991  1.00 81.87           C  
ANISOU 4982  CD2 LEU B  69    10458  14397   6251   3124   1191    584       C  
ATOM   4983  N   PHE B  70      31.002   7.148 -62.247  1.00 92.19           N  
ANISOU 4983  N   PHE B  70    11803  15173   8054   2492   1312    842       N  
ATOM   4984  CA  PHE B  70      30.361   8.392 -61.838  1.00 89.13           C  
ANISOU 4984  CA  PHE B  70    11417  14696   7751   2341   1345    995       C  
ATOM   4985  C   PHE B  70      31.209   9.158 -60.832  1.00 84.49           C  
ANISOU 4985  C   PHE B  70    10750  14043   7310   2179   1434   1155       C  
ATOM   4986  O   PHE B  70      31.137  10.391 -60.777  1.00 76.84           O  
ANISOU 4986  O   PHE B  70     9739  13052   6405   2068   1492   1336       O  
ATOM   4987  CB  PHE B  70      28.978   8.104 -61.254  1.00 88.91           C  
ANISOU 4987  CB  PHE B  70    11495  14459   7830   2266   1220    855       C  
ATOM   4988  CG  PHE B  70      27.958   7.695 -62.280  1.00 84.98           C  
ANISOU 4988  CG  PHE B  70    11071  14025   7194   2401   1138    737       C  
ATOM   4989  CD1 PHE B  70      28.149   7.984 -63.622  1.00 82.89           C  
ANISOU 4989  CD1 PHE B  70    10769  13957   6768   2533   1175    800       C  
ATOM   4990  CD2 PHE B  70      26.808   7.022 -61.902  1.00 79.38           C  
ANISOU 4990  CD2 PHE B  70    10454  13146   6560   2376   1006    557       C  
ATOM   4991  CE1 PHE B  70      27.213   7.609 -64.567  1.00 77.94           C  
ANISOU 4991  CE1 PHE B  70    10203  13372   6040   2649   1086    683       C  
ATOM   4992  CE2 PHE B  70      25.867   6.645 -62.842  1.00 80.25           C  
ANISOU 4992  CE2 PHE B  70    10629  13314   6549   2498    923    442       C  
ATOM   4993  CZ  PHE B  70      26.070   6.939 -64.177  1.00 82.21           C  
ANISOU 4993  CZ  PHE B  70    10851  13795   6591   2653    972    506       C  
ATOM   4994  N   GLY B  71      32.013   8.454 -60.032  1.00 86.45           N  
ANISOU 4994  N   GLY B  71    10975  14241   7632   2156   1435   1087       N  
ATOM   4995  CA  GLY B  71      32.860   9.131 -59.066  1.00 86.96           C  
ANISOU 4995  CA  GLY B  71    10958  14238   7843   2003   1508   1225       C  
ATOM   4996  C   GLY B  71      33.971   9.939 -59.703  1.00 91.48           C  
ANISOU 4996  C   GLY B  71    11410  14978   8369   2015   1625   1419       C  
ATOM   4997  O   GLY B  71      34.369  10.978 -59.167  1.00 94.45           O  
ANISOU 4997  O   GLY B  71    11720  15299   8868   1868   1687   1584       O  
ATOM   4998  N   ASP B  72      34.494   9.478 -60.842  1.00 91.76           N  
ANISOU 4998  N   ASP B  72    11411  15177   8278   2169   1629   1385       N  
ATOM   4999  CA  ASP B  72      35.477  10.272 -61.573  1.00 92.82           C  
ANISOU 4999  CA  ASP B  72    11426  15438   8402   2169   1713   1558       C  
ATOM   5000  C   ASP B  72      34.871  11.580 -62.056  1.00 88.53           C  
ANISOU 5000  C   ASP B  72    10873  14876   7888   2092   1737   1716       C  
ATOM   5001  O   ASP B  72      35.490  12.643 -61.936  1.00 91.60           O  
ANISOU 5001  O   ASP B  72    11175  15260   8368   1982   1808   1898       O  
ATOM   5002  CB  ASP B  72      36.030   9.470 -62.750  1.00103.62           C  
ANISOU 5002  CB  ASP B  72    12766  16988   9615   2364   1705   1481       C  
ATOM   5003  CG  ASP B  72      36.908   8.325 -62.307  1.00108.15           C  
ANISOU 5003  CG  ASP B  72    13324  17592  10175   2436   1697   1359       C  
ATOM   5004  OD1 ASP B  72      36.452   7.515 -61.477  1.00107.55           O  
ANISOU 5004  OD1 ASP B  72    13330  17405  10130   2428   1637   1209       O  
ATOM   5005  OD2 ASP B  72      38.050   8.223 -62.798  1.00110.47           O  
ANISOU 5005  OD2 ASP B  72    13523  18023  10426   2503   1750   1412       O  
ATOM   5006  N   LYS B  73      33.654  11.521 -62.603  1.00 83.97           N  
ANISOU 5006  N   LYS B  73    10385  14283   7237   2149   1672   1646       N  
ATOM   5007  CA  LYS B  73      33.002  12.730 -63.091  1.00 76.67           C  
ANISOU 5007  CA  LYS B  73     9458  13340   6334   2087   1688   1788       C  
ATOM   5008  C   LYS B  73      32.694  13.697 -61.958  1.00 80.62           C  
ANISOU 5008  C   LYS B  73     9961  13664   7006   1887   1707   1898       C  
ATOM   5009  O   LYS B  73      32.741  14.917 -62.154  1.00 83.86           O  
ANISOU 5009  O   LYS B  73    10322  14055   7485   1798   1751   2071       O  
ATOM   5010  CB  LYS B  73      31.722  12.364 -63.841  1.00 64.63           C  
ANISOU 5010  CB  LYS B  73     8032  11831   4695   2194   1604   1671       C  
ATOM   5011  CG  LYS B  73      31.965  11.801 -65.228  1.00 73.68           C  
ANISOU 5011  CG  LYS B  73     9159  13163   5675   2385   1592   1613       C  
ATOM   5012  CD  LYS B  73      32.285  12.905 -66.220  1.00 75.19           C  
ANISOU 5012  CD  LYS B  73     9270  13462   5837   2390   1660   1804       C  
ATOM   5013  CE  LYS B  73      32.020  12.454 -67.647  1.00 83.35           C  
ANISOU 5013  CE  LYS B  73    10315  14657   6696   2580   1626   1735       C  
ATOM   5014  NZ  LYS B  73      33.196  12.675 -68.529  1.00 83.36           N  
ANISOU 5014  NZ  LYS B  73    10204  14835   6632   2657   1704   1848       N  
ATOM   5015  N   LEU B  74      32.382  13.179 -60.769  1.00 77.16           N  
ANISOU 5015  N   LEU B  74     9581  13094   6644   1818   1670   1799       N  
ATOM   5016  CA  LEU B  74      32.054  14.055 -59.651  1.00 82.56           C  
ANISOU 5016  CA  LEU B  74    10269  13607   7493   1633   1682   1894       C  
ATOM   5017  C   LEU B  74      33.303  14.694 -59.056  1.00 88.11           C  
ANISOU 5017  C   LEU B  74    10860  14291   8325   1515   1759   2033       C  
ATOM   5018  O   LEU B  74      33.272  15.864 -58.659  1.00 87.55           O  
ANISOU 5018  O   LEU B  74    10755  14124   8386   1371   1786   2177       O  
ATOM   5019  CB  LEU B  74      31.285  13.283 -58.580  1.00 89.21           C  
ANISOU 5019  CB  LEU B  74    11205  14281   8410   1586   1594   1723       C  
ATOM   5020  CG  LEU B  74      30.432  14.152 -57.655  1.00 98.06           C  
ANISOU 5020  CG  LEU B  74    12362  15180   9717   1408   1551   1762       C  
ATOM   5021  CD1 LEU B  74      29.721  15.223 -58.464  1.00 99.84           C  
ANISOU 5021  CD1 LEU B  74    12595  15445   9893   1409   1571   1896       C  
ATOM   5022  CD2 LEU B  74      29.430  13.310 -56.884  1.00 97.63           C  
ANISOU 5022  CD2 LEU B  74    12407  14944   9745   1378   1428   1556       C  
ATOM   5023  N   CYS B  75      34.408  13.953 -58.996  1.00 92.76           N  
ANISOU 5023  N   CYS B  75    11391  14970   8884   1574   1789   1988       N  
ATOM   5024  CA  CYS B  75      35.660  14.490 -58.478  1.00 96.44           C  
ANISOU 5024  CA  CYS B  75    11745  15433   9465   1473   1857   2111       C  
ATOM   5025  C   CYS B  75      36.411  15.334 -59.500  1.00 98.42           C  
ANISOU 5025  C   CYS B  75    11898  15805   9694   1490   1920   2271       C  
ATOM   5026  O   CYS B  75      37.445  15.916 -59.156  1.00 97.66           O  
ANISOU 5026  O   CYS B  75    11702  15707   9698   1400   1975   2387       O  
ATOM   5027  CB  CYS B  75      36.559  13.352 -57.988  1.00 98.60           C  
ANISOU 5027  CB  CYS B  75    11993  15757   9714   1533   1863   2001       C  
ATOM   5028  SG  CYS B  75      36.158  12.755 -56.331  1.00101.36           S  
ANISOU 5028  SG  CYS B  75    12410  15931  10172   1436   1821   1887       S  
ATOM   5029  N   THR B  76      35.837  15.487 -60.695  1.00106.04           N  
ANISOU 5029  N   THR B  76    12886  16876  10530   1605   1910   2277       N  
ATOM   5030  CA  THR B  76      36.444  16.429 -61.671  1.00112.01           C  
ANISOU 5030  CA  THR B  76    13551  17742  11265   1618   1970   2441       C  
ATOM   5031  C   THR B  76      36.260  17.832 -61.083  1.00119.44           C  
ANISOU 5031  C   THR B  76    14459  18555  12368   1442   1996   2613       C  
ATOM   5032  O   THR B  76      37.165  18.672 -61.258  1.00120.76           O  
ANISOU 5032  O   THR B  76    14528  18773  12582   1399   2055   2766       O  
ATOM   5033  CB  THR B  76      35.771  16.310 -63.044  1.00110.19           C  
ANISOU 5033  CB  THR B  76    13361  17640  10865   1776   1947   2407       C  
ATOM   5034  OG1 THR B  76      35.774  14.936 -63.430  1.00109.69           O  
ANISOU 5034  OG1 THR B  76    13355  17654  10667   1932   1897   2213       O  
ATOM   5035  CG2 THR B  76      36.449  17.130 -64.120  1.00106.95           C  
ANISOU 5035  CG2 THR B  76    12847  17388  10401   1830   2015   2556       C  
ATOM   5036  N   GLU B  86      34.819  19.538 -47.865  1.00108.80           N  
ANISOU 5036  N   GLU B  86    13298  15422  12618     50   1646   2301       N  
ATOM   5037  CA  GLU B  86      33.597  18.879 -47.325  1.00 90.83           C  
ANISOU 5037  CA  GLU B  86    11116  13044  10350     71   1558   2104       C  
ATOM   5038  C   GLU B  86      33.407  17.554 -48.085  1.00 98.61           C  
ANISOU 5038  C   GLU B  86    12159  14144  11165    232   1544   1991       C  
ATOM   5039  O   GLU B  86      33.234  16.527 -47.402  1.00 96.03           O  
ANISOU 5039  O   GLU B  86    11889  13767  10832    268   1484   1831       O  
ATOM   5040  CB  GLU B  86      32.401  19.849 -47.373  1.00 67.59           C  
ANISOU 5040  CB  GLU B  86     8253   9920   7507    -14   1486   2066       C  
ATOM   5041  CG  GLU B  86      31.346  19.594 -46.329  1.00 42.44           C  
ANISOU 5041  CG  GLU B  86     5089   6756   4280      0   1503   2173       C  
ATOM   5042  CD  GLU B  86      29.988  20.167 -46.688  1.00 62.39           C  
ANISOU 5042  CD  GLU B  86     7703   9115   6889    -62   1425   2111       C  
ATOM   5043  OE1 GLU B  86      28.977  19.501 -46.395  1.00 73.09           O  
ANISOU 5043  OE1 GLU B  86     9108  10350   8313   -102   1358   1974       O  
ATOM   5044  OE2 GLU B  86      29.946  21.274 -47.262  1.00 65.68           O  
ANISOU 5044  OE2 GLU B  86     8136   9523   7296    -68   1432   2202       O  
ATOM   5045  N   MET B  87      33.467  17.564 -49.432  1.00103.23           N  
ANISOU 5045  N   MET B  87    12732  14878  11613    331   1593   2070       N  
ATOM   5046  CA  MET B  87      33.202  16.348 -50.267  1.00102.24           C  
ANISOU 5046  CA  MET B  87    12649  14884  11313    496   1585   1968       C  
ATOM   5047  C   MET B  87      34.297  16.149 -51.302  1.00 99.71           C  
ANISOU 5047  C   MET B  87    12235  14778  10872    594   1677   2054       C  
ATOM   5048  O   MET B  87      33.992  15.716 -52.393  1.00 86.85           O  
ANISOU 5048  O   MET B  87    10630  13291   9079    745   1685   1998       O  
ATOM   5049  CB  MET B  87      31.868  16.440 -51.014  1.00104.66           C  
ANISOU 5049  CB  MET B  87    13034  15197  11537    555   1552   1958       C  
ATOM   5050  CG  MET B  87      30.693  16.829 -50.149  1.00104.96           C  
ANISOU 5050  CG  MET B  87    13157  15268  11454    688   1486   1779       C  
ATOM   5051  SD  MET B  87      29.224  15.883 -50.593  1.00108.38           S  
ANISOU 5051  SD  MET B  87    13706  15548  11926    656   1387   1690       S  
ATOM   5052  CE  MET B  87      29.980  14.404 -51.263  1.00104.30           C  
ANISOU 5052  CE  MET B  87    13273  15051  11305    791   1305   1462       C  
ATOM   5053  N   ALA B  88      35.521  16.511 -50.953  1.00115.43           N  
ANISOU 5053  N   ALA B  88    14119  16798  12941    513   1746   2187       N  
ATOM   5054  CA  ALA B  88      36.681  16.263 -51.833  1.00124.12           C  
ANISOU 5054  CA  ALA B  88    15116  18094  13948    591   1836   2265       C  
ATOM   5055  C   ALA B  88      37.662  15.446 -50.999  1.00125.39           C  
ANISOU 5055  C   ALA B  88    15269  18273  14103    640   1814   2127       C  
ATOM   5056  O   ALA B  88      38.851  15.398 -51.361  1.00130.62           O  
ANISOU 5056  O   ALA B  88    15857  19110  14663    738   1878   2155       O  
ATOM   5057  CB  ALA B  88      37.273  17.557 -52.298  1.00127.73           C  
ANISOU 5057  CB  ALA B  88    15459  18556  14518    470   1904   2458       C  
ATOM   5058  N   ASP B  89      37.185  14.910 -49.869  1.00115.71           N  
ANISOU 5058  N   ASP B  89    14112  16870  12981    578   1726   1985       N  
ATOM   5059  CA  ASP B  89      38.006  13.978 -49.063  1.00108.31           C  
ANISOU 5059  CA  ASP B  89    13174  15933  12045    623   1698   1853       C  
ATOM   5060  C   ASP B  89      37.654  12.625 -49.652  1.00 99.68           C  
ANISOU 5060  C   ASP B  89    12142  14944  10786    802   1672   1716       C  
ATOM   5061  O   ASP B  89      38.458  11.693 -49.563  1.00 99.32           O  
ANISOU 5061  O   ASP B  89    12053  15017  10666    899   1700   1675       O  
ATOM   5062  CB  ASP B  89      37.637  14.045 -47.581  1.00107.87           C  
ANISOU 5062  CB  ASP B  89    13180  15661  12144    508   1612   1748       C  
ATOM   5063  CG  ASP B  89      36.297  14.703 -47.302  1.00108.24           C  
ANISOU 5063  CG  ASP B  89    13205  15577  12345    341   1613   1858       C  
ATOM   5064  OD1 ASP B  89      35.260  14.100 -47.646  1.00106.25           O  
ANISOU 5064  OD1 ASP B  89    13034  15202  12135    294   1558   1828       O  
ATOM   5065  OD2 ASP B  89      36.299  15.805 -46.728  1.00109.84           O  
ANISOU 5065  OD2 ASP B  89    13306  15799  12628    259   1665   1973       O  
ATOM   5066  N   CYS B  90      36.485  12.566 -50.276  1.00 93.45           N  
ANISOU 5066  N   CYS B  90    11454  14111   9941    849   1614   1640       N  
ATOM   5067  CA  CYS B  90      36.085  11.324 -50.956  1.00 94.96           C  
ANISOU 5067  CA  CYS B  90    11708  14394   9979   1019   1579   1502       C  
ATOM   5068  C   CYS B  90      36.731  11.400 -52.332  1.00103.67           C  
ANISOU 5068  C   CYS B  90    12750  15734  10904   1159   1662   1586       C  
ATOM   5069  O   CYS B  90      36.517  10.485 -53.141  1.00104.99           O  
ANISOU 5069  O   CYS B  90    12970  15993  10930   1311   1633   1476       O  
ATOM   5070  CB  CYS B  90      34.570  11.237 -51.039  1.00 96.96           C  
ANISOU 5070  CB  CYS B  90    12080  14533  10226   1026   1490   1397       C  
ATOM   5071  SG  CYS B  90      33.705  11.636 -49.497  1.00 99.71           S  
ANISOU 5071  SG  CYS B  90    12482  14619  10783    835   1419   1374       S  
ATOM   5072  N   ALA B  92      40.116  11.996 -52.378  1.00117.38           N  
ANISOU 5072  N   ALA B  92    14180  17818  12602   1186   1890   1854       N  
ATOM   5073  CA  ALA B  92      41.465  11.440 -52.127  1.00114.62           C  
ANISOU 5073  CA  ALA B  92    13738  17574  12237   1232   1937   1852       C  
ATOM   5074  C   ALA B  92      41.308   9.936 -51.881  1.00114.07           C  
ANISOU 5074  C   ALA B  92    13738  17506  12100   1364   1868   1644       C  
ATOM   5075  O   ALA B  92      42.035   9.424 -51.019  1.00120.86           O  
ANISOU 5075  O   ALA B  92    14532  18445  12945   1417   1895   1618       O  
ATOM   5076  CB  ALA B  92      42.110  12.106 -50.937  1.00107.81           C  
ANISOU 5076  CB  ALA B  92    12807  16589  11567   1057   1944   1921       C  
ATOM   5077  N   LYS B  93      40.385   9.264 -52.576  1.00103.87           N  
ANISOU 5077  N   LYS B  93    12574  16124  10770   1419   1779   1498       N  
ATOM   5078  CA  LYS B  93      40.154   7.832 -52.269  1.00 98.74           C  
ANISOU 5078  CA  LYS B  93    12001  15450  10064   1540   1701   1295       C  
ATOM   5079  C   LYS B  93      39.473   7.158 -53.445  1.00110.47           C  
ANISOU 5079  C   LYS B  93    13567  17017  11390   1690   1666   1208       C  
ATOM   5080  O   LYS B  93      39.042   7.873 -54.360  1.00112.99           O  
ANISOU 5080  O   LYS B  93    13890  17390  11652   1688   1695   1301       O  
ATOM   5081  CB  LYS B  93      39.134   7.722 -51.136  1.00 83.70           C  
ANISOU 5081  CB  LYS B  93    10183  13301   8319   1429   1600   1176       C  
ATOM   5082  CG  LYS B  93      39.432   6.709 -50.044  1.00 73.75           C  
ANISOU 5082  CG  LYS B  93     8975  11874   7172   1278   1564   1224       C  
ATOM   5083  CD  LYS B  93      38.450   6.833 -48.904  1.00 64.29           C  
ANISOU 5083  CD  LYS B  93     7839  10452   6137   1159   1480   1130       C  
ATOM   5084  CE  LYS B  93      37.823   8.208 -48.823  1.00 68.07           C  
ANISOU 5084  CE  LYS B  93     8254  10838   6772    978   1513   1261       C  
ATOM   5085  NZ  LYS B  93      38.421   9.020 -47.738  1.00 78.03           N  
ANISOU 5085  NZ  LYS B  93     9589  11878   8180    859   1429   1179       N  
ATOM   5086  N   GLN B  94      39.355   5.833 -53.391  1.00118.35           N  
ANISOU 5086  N   GLN B  94    14630  18021  12317   1825   1600   1026       N  
ATOM   5087  CA  GLN B  94      38.600   5.100 -54.437  1.00124.75           C  
ANISOU 5087  CA  GLN B  94    15532  18873  12995   1962   1540    907       C  
ATOM   5088  C   GLN B  94      37.951   3.891 -53.778  1.00130.59           C  
ANISOU 5088  C   GLN B  94    16382  19447  13790   1988   1416    694       C  
ATOM   5089  O   GLN B  94      37.219   4.131 -52.809  1.00133.60           O  
ANISOU 5089  O   GLN B  94    16832  19623  14306   1861   1346    654       O  
ATOM   5090  CB  GLN B  94      39.523   4.613 -55.550  1.00125.28           C  
ANISOU 5090  CB  GLN B  94    15543  19204  12853   2157   1608    924       C  
ATOM   5091  CG  GLN B  94      38.963   4.840 -56.946  1.00126.59           C  
ANISOU 5091  CG  GLN B  94    15802  19430  12866   2326   1538    776       C  
ATOM   5092  CD  GLN B  94      39.338   3.719 -57.883  1.00126.48           C  
ANISOU 5092  CD  GLN B  94    15728  19656  12672   2515   1587    777       C  
ATOM   5093  OE1 GLN B  94      40.316   3.010 -57.666  1.00126.45           O  
ANISOU 5093  OE1 GLN B  94    15637  19736  12673   2548   1633    808       O  
ATOM   5094  NE2 GLN B  94      38.560   3.552 -58.938  1.00125.36           N  
ANISOU 5094  NE2 GLN B  94    15631  19579  12421   2619   1542    729       N  
ATOM   5095  N   GLU B  95      38.276   2.675 -54.223  1.00132.85           N  
ANISOU 5095  N   GLU B  95    16682  19815  13978   2152   1389    560       N  
ATOM   5096  CA  GLU B  95      37.726   1.409 -53.748  1.00134.01           C  
ANISOU 5096  CA  GLU B  95    16934  19812  14171   2193   1269    357       C  
ATOM   5097  C   GLU B  95      36.245   1.336 -54.121  1.00135.02           C  
ANISOU 5097  C   GLU B  95    17170  19838  14292   2188   1180    269       C  
ATOM   5098  O   GLU B  95      35.767   2.167 -54.906  1.00135.06           O  
ANISOU 5098  O   GLU B  95    17166  19925  14225   2189   1215    357       O  
ATOM   5099  CB  GLU B  95      37.932   1.295 -52.234  1.00132.33           C  
ANISOU 5099  CB  GLU B  95    16723  19411  14147   2044   1241    351       C  
ATOM   5100  CG  GLU B  95      38.644   0.043 -51.765  1.00131.17           C  
ANISOU 5100  CG  GLU B  95    16587  19243  14010   2131   1200    224       C  
ATOM   5101  CD  GLU B  95      38.904   0.070 -50.275  1.00128.86           C  
ANISOU 5101  CD  GLU B  95    16284  18782  13896   1980   1184    244       C  
ATOM   5102  OE1 GLU B  95      39.462  -0.913 -49.743  1.00128.34           O  
ANISOU 5102  OE1 GLU B  95    16229  18678  13858   2033   1147    149       O  
ATOM   5103  OE2 GLU B  95      38.552   1.083 -49.636  1.00127.99           O  
ANISOU 5103  OE2 GLU B  95    16155  18580  13896   1812   1206    354       O  
ATOM   5104  N   PRO B  96      35.490   0.346 -53.637  1.00134.01           N  
ANISOU 5104  N   PRO B  96    17143  19541  14232   2191   1063     99       N  
ATOM   5105  CA  PRO B  96      34.039   0.532 -53.514  1.00130.78           C  
ANISOU 5105  CA  PRO B  96    16822  18978  13889   2107    981     52       C  
ATOM   5106  C   PRO B  96      33.648   1.440 -52.359  1.00129.94           C  
ANISOU 5106  C   PRO B  96    16706  18707  13958   1894    993    157       C  
ATOM   5107  O   PRO B  96      32.459   1.736 -52.196  1.00129.18           O  
ANISOU 5107  O   PRO B  96    16671  18486  13923   1813    936    137       O  
ATOM   5108  CB  PRO B  96      33.510  -0.895 -53.297  1.00128.31           C  
ANISOU 5108  CB  PRO B  96    16609  18539  13605   2177    856   -159       C  
ATOM   5109  CG  PRO B  96      34.581  -1.796 -53.774  1.00130.74           C  
ANISOU 5109  CG  PRO B  96    16889  18984  13803   2348    872   -233       C  
ATOM   5110  CD  PRO B  96      35.875  -1.076 -53.594  1.00133.54           C  
ANISOU 5110  CD  PRO B  96    17125  19470  14144   2321    997    -71       C  
ATOM   5111  N   GLU B  97      34.621   1.878 -51.556  1.00129.62           N  
ANISOU 5111  N   GLU B  97    16588  18666  13997   1808   1063    263       N  
ATOM   5112  CA  GLU B  97      34.377   2.831 -50.482  1.00127.93           C  
ANISOU 5112  CA  GLU B  97    16353  18314  13940   1613   1081    370       C  
ATOM   5113  C   GLU B  97      34.172   4.245 -51.001  1.00124.25           C  
ANISOU 5113  C   GLU B  97    15837  17920  13451   1548   1154    536       C  
ATOM   5114  O   GLU B  97      33.673   5.098 -50.259  1.00125.86           O  
ANISOU 5114  O   GLU B  97    16042  17998  13779   1393   1153    611       O  
ATOM   5115  CB  GLU B  97      35.544   2.803 -49.491  1.00131.82           C  
ANISOU 5115  CB  GLU B  97    16775  18792  14520   1552   1126    421       C  
ATOM   5116  CG  GLU B  97      35.508   1.662 -48.471  1.00136.65           C  
ANISOU 5116  CG  GLU B  97    17444  19252  15224   1542   1043    284       C  
ATOM   5117  CD  GLU B  97      35.572   0.268 -49.090  1.00141.28           C  
ANISOU 5117  CD  GLU B  97    18086  19881  15711   1717    982    120       C  
ATOM   5118  OE1 GLU B  97      35.761   0.141 -50.318  1.00143.60           O  
ANISOU 5118  OE1 GLU B  97    18368  20342  15853   1860   1008    106       O  
ATOM   5119  OE2 GLU B  97      35.441  -0.715 -48.332  1.00141.08           O  
ANISOU 5119  OE2 GLU B  97    18118  19723  15762   1715    907      4       O  
ATOM   5120  N   ARG B  98      34.563   4.510 -52.250  1.00117.49           N  
ANISOU 5120  N   ARG B  98    14937  17265  12439   1667   1217    596       N  
ATOM   5121  CA  ARG B  98      34.253   5.784 -52.887  1.00110.82           C  
ANISOU 5121  CA  ARG B  98    14056  16492  11558   1622   1278    750       C  
ATOM   5122  C   ARG B  98      32.762   6.082 -52.812  1.00112.52           C  
ANISOU 5122  C   ARG B  98    14360  16564  11827   1553   1202    708       C  
ATOM   5123  O   ARG B  98      32.352   7.178 -52.416  1.00115.34           O  
ANISOU 5123  O   ARG B  98    14703  16844  12278   1417   1223    822       O  
ATOM   5124  CB  ARG B  98      34.720   5.754 -54.344  1.00103.39           C  
ANISOU 5124  CB  ARG B  98    13075  15792  10416   1793   1339    787       C  
ATOM   5125  CG  ARG B  98      34.772   7.099 -55.043  1.00 96.20           C  
ANISOU 5125  CG  ARG B  98    12100  14995   9457   1758   1429    982       C  
ATOM   5126  CD  ARG B  98      35.524   6.967 -56.357  1.00 89.94           C  
ANISOU 5126  CD  ARG B  98    11248  14462   8463   1933   1505   1027       C  
ATOM   5127  NE  ARG B  98      36.483   8.046 -56.572  1.00 87.40           N  
ANISOU 5127  NE  ARG B  98    10805  14269   8132   1885   1630   1243       N  
ATOM   5128  CZ  ARG B  98      37.036   8.331 -57.747  1.00 86.65           C  
ANISOU 5128  CZ  ARG B  98    10645  14397   7880   2001   1711   1341       C  
ATOM   5129  NH1 ARG B  98      36.736   7.612 -58.819  1.00 94.69           N  
ANISOU 5129  NH1 ARG B  98    11708  15516   8755   2169   1663   1226       N  
ATOM   5130  NH2 ARG B  98      37.898   9.333 -57.851  1.00 82.78           N  
ANISOU 5130  NH2 ARG B  98    10041  13956   7456   1917   1790   1525       N  
ATOM   5131  N   ASN B  99      31.931   5.101 -53.164  1.00108.61           N  
ANISOU 5131  N   ASN B  99    13956  16029  11282   1643   1107    540       N  
ATOM   5132  CA  ASN B  99      30.502   5.363 -53.292  1.00102.61           C  
ANISOU 5132  CA  ASN B  99    13273  15164  10551   1598   1035    499       C  
ATOM   5133  C   ASN B  99      29.787   5.516 -51.953  1.00 97.59           C  
ANISOU 5133  C   ASN B  99    12677  14299  10104   1428    979    476       C  
ATOM   5134  O   ASN B  99      28.686   6.072 -51.924  1.00 97.61           O  
ANISOU 5134  O   ASN B  99    12721  14215  10151   1358    942    488       O  
ATOM   5135  CB  ASN B  99      29.831   4.258 -54.107  1.00 98.40           C  
ANISOU 5135  CB  ASN B  99    12819  14660   9909   1747    946    322       C  
ATOM   5136  CG  ASN B  99      28.546   4.726 -54.762  1.00 97.99           C  
ANISOU 5136  CG  ASN B  99    12819  14593   9819   1748    899    315       C  
ATOM   5137  OD1 ASN B  99      27.486   4.135 -54.564  1.00 97.92           O  
ANISOU 5137  OD1 ASN B  99    12890  14456   9858   1736    796    183       O  
ATOM   5138  ND2 ASN B  99      28.632   5.802 -55.535  1.00101.15           N  
ANISOU 5138  ND2 ASN B  99    13172  15123  10138   1759    975    464       N  
ATOM   5139  N   GLU B 100      30.367   5.038 -50.855  1.00 94.99           N  
ANISOU 5139  N   GLU B 100    12336  13876   9880   1367    971    443       N  
ATOM   5140  CA  GLU B 100      29.743   5.163 -49.546  1.00 99.27           C  
ANISOU 5140  CA  GLU B 100    12912  14212  10593   1212    922    424       C  
ATOM   5141  C   GLU B 100      30.415   6.208 -48.661  1.00 92.64           C  
ANISOU 5141  C   GLU B 100    11999  13339   9862   1073    994    571       C  
ATOM   5142  O   GLU B 100      30.024   6.362 -47.498  1.00 92.33           O  
ANISOU 5142  O   GLU B 100    11979  13140   9963    946    961    562       O  
ATOM   5143  CB  GLU B 100      29.683   3.802 -48.849  1.00106.15           C  
ANISOU 5143  CB  GLU B 100    13840  14973  11519   1235    841    265       C  
ATOM   5144  CG  GLU B 100      28.643   2.902 -49.514  1.00113.72           C  
ANISOU 5144  CG  GLU B 100    14887  15902  12418   1328    745    113       C  
ATOM   5145  CD  GLU B 100      28.266   1.671 -48.724  1.00119.38           C  
ANISOU 5145  CD  GLU B 100    15671  16466  13222   1319    650    -37       C  
ATOM   5146  OE1 GLU B 100      29.098   0.749 -48.611  1.00122.88           O  
ANISOU 5146  OE1 GLU B 100    16109  16935  13644   1397    644   -103       O  
ATOM   5147  OE2 GLU B 100      27.120   1.621 -48.234  1.00120.05           O  
ANISOU 5147  OE2 GLU B 100    15812  16404  13397   1235    581    -86       O  
ATOM   5148  N   CYS B 101      31.433   6.904 -49.177  1.00 88.06           N  
ANISOU 5148  N   CYS B 101    11330  12909   9220   1097   1091    704       N  
ATOM   5149  CA  CYS B 101      31.790   8.227 -48.674  1.00 88.74           C  
ANISOU 5149  CA  CYS B 101    11347  12973   9398    963   1158    868       C  
ATOM   5150  C   CYS B 101      30.846   9.280 -49.243  1.00 89.79           C  
ANISOU 5150  C   CYS B 101    11498  13099   9519    923   1164    950       C  
ATOM   5151  O   CYS B 101      30.297  10.104 -48.506  1.00 77.30           O  
ANISOU 5151  O   CYS B 101     9924  11388   8059    789   1151   1003       O  
ATOM   5152  CB  CYS B 101      33.219   8.573 -49.059  1.00 92.44           C  
ANISOU 5152  CB  CYS B 101    11708  13605   9808   1002   1259    986       C  
ATOM   5153  SG  CYS B 101      33.873  10.030 -48.233  1.00 98.70           S  
ANISOU 5153  SG  CYS B 101    12408  14353  10742    828   1332   1171       S  
ATOM   5154  N   PHE B 102      30.649   9.258 -50.565  1.00 92.00           N  
ANISOU 5154  N   PHE B 102    11785  13521   9650   1045   1180    960       N  
ATOM   5155  CA  PHE B 102      29.708  10.167 -51.211  1.00 87.27           C  
ANISOU 5155  CA  PHE B 102    11209  12926   9024   1027   1179   1031       C  
ATOM   5156  C   PHE B 102      28.286   9.947 -50.701  1.00 84.88           C  
ANISOU 5156  C   PHE B 102    10999  12452   8801    970   1079    920       C  
ATOM   5157  O   PHE B 102      27.524  10.906 -50.532  1.00 77.69           O  
ANISOU 5157  O   PHE B 102    10100  11463   7956    879   1072    989       O  
ATOM   5158  CB  PHE B 102      29.774   9.971 -52.726  1.00 88.25           C  
ANISOU 5158  CB  PHE B 102    11330  13245   8956   1191   1206   1038       C  
ATOM   5159  CG  PHE B 102      30.964  10.628 -53.385  1.00 90.65           C  
ANISOU 5159  CG  PHE B 102    11533  13730   9180   1230   1322   1202       C  
ATOM   5160  CD1 PHE B 102      30.952  11.984 -53.645  1.00 90.38           C  
ANISOU 5160  CD1 PHE B 102    11450  13720   9169   1156   1386   1383       C  
ATOM   5161  CD2 PHE B 102      32.079   9.891 -53.765  1.00 92.23           C  
ANISOU 5161  CD2 PHE B 102    11683  14077   9282   1343   1366   1178       C  
ATOM   5162  CE1 PHE B 102      32.025  12.605 -54.256  1.00 89.47           C  
ANISOU 5162  CE1 PHE B 102    11236  13770   8987   1184   1494   1545       C  
ATOM   5163  CE2 PHE B 102      33.162  10.509 -54.385  1.00 95.49           C  
ANISOU 5163  CE2 PHE B 102    11995  14667   9621   1377   1477   1338       C  
ATOM   5164  CZ  PHE B 102      33.129  11.871 -54.629  1.00 92.53           C  
ANISOU 5164  CZ  PHE B 102    11570  14312   9275   1294   1542   1525       C  
ATOM   5165  N   LEU B 103      27.914   8.690 -50.440  1.00 87.28           N  
ANISOU 5165  N   LEU B 103    11367  12693   9104   1020    998    749       N  
ATOM   5166  CA  LEU B 103      26.581   8.399 -49.917  1.00 90.99           C  
ANISOU 5166  CA  LEU B 103    11917  13001   9655    963    902    643       C  
ATOM   5167  C   LEU B 103      26.421   8.945 -48.503  1.00 90.92           C  
ANISOU 5167  C   LEU B 103    11901  12825   9820    796    897    682       C  
ATOM   5168  O   LEU B 103      25.444   9.640 -48.201  1.00 91.98           O  
ANISOU 5168  O   LEU B 103    12061  12861  10025    710    869    706       O  
ATOM   5169  CB  LEU B 103      26.322   6.891 -49.947  1.00 97.22           C  
ANISOU 5169  CB  LEU B 103    12769  13759  10411   1053    819    458       C  
ATOM   5170  CG  LEU B 103      24.899   6.347 -49.736  1.00103.12           C  
ANISOU 5170  CG  LEU B 103    13602  14372  11209   1031    712    328       C  
ATOM   5171  CD1 LEU B 103      24.476   6.304 -48.263  1.00103.02           C  
ANISOU 5171  CD1 LEU B 103    13608  14167  11368    886    673    303       C  
ATOM   5172  CD2 LEU B 103      23.897   7.144 -50.556  1.00105.01           C  
ANISOU 5172  CD2 LEU B 103    13859  14644  11396   1041    701    371       C  
ATOM   5173  N   GLN B 104      27.380   8.653 -47.626  1.00 88.91           N  
ANISOU 5173  N   GLN B 104    11608  12541   9632    753    922    687       N  
ATOM   5174  CA  GLN B 104      27.331   9.088 -46.231  1.00 80.29           C  
ANISOU 5174  CA  GLN B 104    10507  11301   8699    605    915    714       C  
ATOM   5175  C   GLN B 104      27.490  10.599 -46.065  1.00 78.30           C  
ANISOU 5175  C   GLN B 104    10200  11044   8508    502    976    874       C  
ATOM   5176  O   GLN B 104      27.709  11.060 -44.936  1.00 92.02           O  
ANISOU 5176  O   GLN B 104    11914  12681  10370    385    982    910       O  
ATOM   5177  CB  GLN B 104      28.401   8.359 -45.416  1.00 81.15           C  
ANISOU 5177  CB  GLN B 104    10586  11398   8849    600    926    679       C  
ATOM   5178  CG  GLN B 104      27.900   7.096 -44.731  1.00 85.31           C  
ANISOU 5178  CG  GLN B 104    11182  11811   9421    610    841    525       C  
ATOM   5179  CD  GLN B 104      26.876   7.385 -43.651  1.00 88.23           C  
ANISOU 5179  CD  GLN B 104    11593  12007   9922    483    789    502       C  
ATOM   5180  OE1 GLN B 104      27.014   8.341 -42.888  1.00 91.15           O  
ANISOU 5180  OE1 GLN B 104    11926  12323  10382    371    820    591       O  
ATOM   5181  NE2 GLN B 104      25.837   6.559 -43.583  1.00 86.29           N  
ANISOU 5181  NE2 GLN B 104    11422  11678   9689    501    708    382       N  
ATOM   5182  N   HIS B 105      27.389  11.374 -47.145  1.00 69.80           N  
ANISOU 5182  N   HIS B 105     9102  10072   7348    544   1019    969       N  
ATOM   5183  CA  HIS B 105      27.433  12.829 -47.078  1.00 64.71           C  
ANISOU 5183  CA  HIS B 105     8410   9412   6763    450   1070   1124       C  
ATOM   5184  C   HIS B 105      26.170  13.469 -47.640  1.00 43.26           C  
ANISOU 5184  C   HIS B 105     5741   6666   4030    447   1038   1141       C  
ATOM   5185  O   HIS B 105      26.114  14.698 -47.767  1.00 47.14           O  
ANISOU 5185  O   HIS B 105     6201   7151   4559    384   1077   1272       O  
ATOM   5186  CB  HIS B 105      28.668  13.358 -47.811  1.00 87.91           C  
ANISOU 5186  CB  HIS B 105    11261  12511   9631    491   1168   1263       C  
ATOM   5187  CG  HIS B 105      29.953  13.092 -47.092  1.00108.59           C  
ANISOU 5187  CG  HIS B 105    13814  15145  12301    459   1207   1281       C  
ATOM   5188  ND1 HIS B 105      30.546  11.849 -47.061  1.00113.23           N  
ANISOU 5188  ND1 HIS B 105    14406  15786  12831    547   1195   1176       N  
ATOM   5189  CD2 HIS B 105      30.757  13.910 -46.372  1.00114.06           C  
ANISOU 5189  CD2 HIS B 105    14434  15806  13099    352   1255   1388       C  
ATOM   5190  CE1 HIS B 105      31.660  11.912 -46.354  1.00114.71           C  
ANISOU 5190  CE1 HIS B 105    14524  15978  13082    497   1236   1220       C  
ATOM   5191  NE2 HIS B 105      31.812  13.152 -45.926  1.00114.02           N  
ANISOU 5191  NE2 HIS B 105    14387  15840  13093    377   1271   1347       N  
ATOM   5192  N   LYS B 106      25.163  12.669 -47.986  1.00 54.98           N  
ANISOU 5192  N   LYS B 106     7299   8128   5461    513    965   1012       N  
ATOM   5193  CA  LYS B 106      23.875  13.210 -48.400  1.00 55.15           C  
ANISOU 5193  CA  LYS B 106     7368   8109   5478    505    923   1013       C  
ATOM   5194  C   LYS B 106      23.279  14.045 -47.276  1.00 58.64           C  
ANISOU 5194  C   LYS B 106     7817   8389   6076    360    902   1045       C  
ATOM   5195  O   LYS B 106      23.065  13.547 -46.167  1.00 54.58           O  
ANISOU 5195  O   LYS B 106     7325   7755   5659    294    858    960       O  
ATOM   5196  CB  LYS B 106      22.927  12.074 -48.781  1.00 56.11           C  
ANISOU 5196  CB  LYS B 106     7564   8218   5538    589    838    851       C  
ATOM   5197  CG  LYS B 106      23.146  11.505 -50.171  1.00 55.57           C  
ANISOU 5197  CG  LYS B 106     7501   8317   5297    748    846    821       C  
ATOM   5198  CD  LYS B 106      22.063  10.494 -50.512  1.00 56.60           C  
ANISOU 5198  CD  LYS B 106     7707   8415   5385    818    747    657       C  
ATOM   5199  CE  LYS B 106      22.132  10.062 -51.967  1.00 52.26           C  
ANISOU 5199  CE  LYS B 106     7167   8034   4656    981    746    625       C  
ATOM   5200  NZ  LYS B 106      21.142   8.988 -52.256  1.00 46.03           N  
ANISOU 5200  NZ  LYS B 106     6449   7205   3835   1049    641    450       N  
ATOM   5201  N   ASP B 107      23.017  15.317 -47.562  1.00 55.31           N  
ANISOU 5201  N   ASP B 107     7374   7965   5676    315    933   1170       N  
ATOM   5202  CA  ASP B 107      22.481  16.244 -46.572  1.00 47.21           C  
ANISOU 5202  CA  ASP B 107     6352   6793   4794    186    916   1208       C  
ATOM   5203  C   ASP B 107      20.959  16.163 -46.597  1.00 51.54           C  
ANISOU 5203  C   ASP B 107     6967   7263   5352    187    839   1123       C  
ATOM   5204  O   ASP B 107      20.323  16.581 -47.569  1.00 36.64           O  
ANISOU 5204  O   ASP B 107     5098   5432   3391    244    833   1159       O  
ATOM   5205  CB  ASP B 107      22.964  17.666 -46.849  1.00 53.10           C  
ANISOU 5205  CB  ASP B 107     7041   7564   5569    136    983   1385       C  
ATOM   5206  CG  ASP B 107      22.850  18.569 -45.636  1.00 53.56           C  
ANISOU 5206  CG  ASP B 107     7086   7474   5790     -3    974   1425       C  
ATOM   5207  OD1 ASP B 107      21.993  18.300 -44.768  1.00 49.51           O  
ANISOU 5207  OD1 ASP B 107     6619   6840   5352    -52    910   1324       O  
ATOM   5208  OD2 ASP B 107      23.619  19.551 -45.551  1.00 48.70           O  
ANISOU 5208  OD2 ASP B 107     6412   6863   5229    -61   1030   1557       O  
ATOM   5209  N   ASP B 108      20.376  15.621 -45.524  1.00 46.26           N  
ANISOU 5209  N   ASP B 108     6333   6469   4774    127    780   1014       N  
ATOM   5210  CA  ASP B 108      18.924  15.551 -45.417  1.00 39.98           C  
ANISOU 5210  CA  ASP B 108     5594   5593   4005    116    707    935       C  
ATOM   5211  C   ASP B 108      18.301  16.910 -45.130  1.00 38.85           C  
ANISOU 5211  C   ASP B 108     5444   5374   3941     37    710   1023       C  
ATOM   5212  O   ASP B 108      17.105  17.095 -45.379  1.00 39.24           O  
ANISOU 5212  O   ASP B 108     5531   5390   3987     47    661    988       O  
ATOM   5213  CB  ASP B 108      18.525  14.558 -44.324  1.00 43.59           C  
ANISOU 5213  CB  ASP B 108     6083   5944   4536     72    649    803       C  
ATOM   5214  CG  ASP B 108      18.661  13.113 -44.767  1.00 42.12           C  
ANISOU 5214  CG  ASP B 108     5924   5811   4267    165    616    687       C  
ATOM   5215  OD1 ASP B 108      17.882  12.682 -45.642  1.00 44.54           O  
ANISOU 5215  OD1 ASP B 108     6268   6161   4496    243    571    623       O  
ATOM   5216  OD2 ASP B 108      19.537  12.404 -44.230  1.00 37.67           O  
ANISOU 5216  OD2 ASP B 108     5346   5245   3720    162    630    654       O  
ATOM   5217  N   ASN B 109      19.080  17.857 -44.615  1.00 39.03           N  
ANISOU 5217  N   ASN B 109     5420   5368   4040    -39    762   1132       N  
ATOM   5218  CA  ASN B 109      18.605  19.203 -44.293  1.00 34.07           C  
ANISOU 5218  CA  ASN B 109     4785   4660   3501   -116    765   1219       C  
ATOM   5219  C   ASN B 109      19.594  20.213 -44.862  1.00 44.70           C  
ANISOU 5219  C   ASN B 109     6075   6073   4836   -122    840   1381       C  
ATOM   5220  O   ASN B 109      20.275  20.926 -44.116  1.00 47.19           O  
ANISOU 5220  O   ASN B 109     6348   6329   5252   -210    870   1451       O  
ATOM   5221  CB  ASN B 109      18.445  19.371 -42.781  1.00 40.65           C  
ANISOU 5221  CB  ASN B 109     5618   5352   4474   -225    738   1174       C  
ATOM   5222  CG  ASN B 109      17.674  20.621 -42.407  1.00 50.92           C  
ANISOU 5222  CG  ASN B 109     6924   6557   5865   -292    720   1227       C  
ATOM   5223  OD1 ASN B 109      17.040  21.252 -43.253  1.00 60.22           O  
ANISOU 5223  OD1 ASN B 109     8116   7761   7003   -255    716   1281       O  
ATOM   5224  ND2 ASN B 109      17.723  20.985 -41.130  1.00 48.52           N  
ANISOU 5224  ND2 ASN B 109     6611   6144   5682   -385    707   1210       N  
ATOM   5225  N   PRO B 110      19.695  20.301 -46.188  1.00 44.72           N  
ANISOU 5225  N   PRO B 110     6072   6201   4717    -31    871   1446       N  
ATOM   5226  CA  PRO B 110      20.742  21.133 -46.788  1.00 52.56           C  
ANISOU 5226  CA  PRO B 110     7004   7276   5689    -31    950   1609       C  
ATOM   5227  C   PRO B 110      20.462  22.616 -46.622  1.00 56.67           C  
ANISOU 5227  C   PRO B 110     7511   7714   6308   -109    960   1732       C  
ATOM   5228  O   PRO B 110      19.314  23.068 -46.646  1.00 50.97           O  
ANISOU 5228  O   PRO B 110     6832   6924   5609   -115    913   1713       O  
ATOM   5229  CB  PRO B 110      20.714  20.727 -48.265  1.00 39.68           C  
ANISOU 5229  CB  PRO B 110     5381   5807   3888    102    971   1629       C  
ATOM   5230  CG  PRO B 110      19.316  20.277 -48.498  1.00 46.59           C  
ANISOU 5230  CG  PRO B 110     6327   6651   4725    150    893   1513       C  
ATOM   5231  CD  PRO B 110      18.838  19.667 -47.207  1.00 47.35           C  
ANISOU 5231  CD  PRO B 110     6452   6612   4927     78    832   1377       C  
ATOM   5232  N   ASN B 111      21.543  23.378 -46.450  1.00 63.65           N  
ANISOU 5232  N   ASN B 111     8330   8600   7252   -170   1021   1859       N  
ATOM   5233  CA  ASN B 111      21.470  24.836 -46.375  1.00 61.53           C  
ANISOU 5233  CA  ASN B 111     8041   8256   7082   -245   1036   1995       C  
ATOM   5234  C   ASN B 111      21.097  25.361 -47.758  1.00 62.79           C  
ANISOU 5234  C   ASN B 111     8208   8513   7137   -164   1062   2103       C  
ATOM   5235  O   ASN B 111      21.942  25.738 -48.575  1.00 69.39           O  
ANISOU 5235  O   ASN B 111     8993   9456   7917   -136   1132   2241       O  
ATOM   5236  CB  ASN B 111      22.792  25.414 -45.885  1.00 67.48           C  
ANISOU 5236  CB  ASN B 111     8717   8994   7927   -329   1092   2100       C  
ATOM   5237  CG  ASN B 111      22.872  26.916 -46.059  1.00 64.86           C  
ANISOU 5237  CG  ASN B 111     8356   8604   7685   -394   1116   2263       C  
ATOM   5238  OD1 ASN B 111      21.927  27.640 -45.746  1.00 64.55           O  
ANISOU 5238  OD1 ASN B 111     8357   8450   7721   -432   1067   2256       O  
ATOM   5239  ND2 ASN B 111      24.000  27.392 -46.571  1.00 74.28           N  
ANISOU 5239  ND2 ASN B 111     9475   9875   8872   -406   1190   2412       N  
ATOM   5240  N   LEU B 112      19.796  25.367 -48.030  1.00 44.77           N  
ANISOU 5240  N   LEU B 112     5989   6199   4824   -123   1003   2041       N  
ATOM   5241  CA  LEU B 112      19.270  25.791 -49.318  1.00 47.39           C  
ANISOU 5241  CA  LEU B 112     6337   6621   5048    -36   1014   2125       C  
ATOM   5242  C   LEU B 112      17.921  26.447 -49.089  1.00 51.85           C  
ANISOU 5242  C   LEU B 112     6955   7071   5676    -59    948   2097       C  
ATOM   5243  O   LEU B 112      17.218  26.096 -48.133  1.00 47.01           O  
ANISOU 5243  O   LEU B 112     6376   6350   5137   -103    886   1966       O  
ATOM   5244  CB  LEU B 112      19.125  24.609 -50.290  1.00 46.01           C  
ANISOU 5244  CB  LEU B 112     6187   6599   4696     97   1010   2042       C  
ATOM   5245  CG  LEU B 112      20.406  23.998 -50.864  1.00 48.84           C  
ANISOU 5245  CG  LEU B 112     6494   7110   4953    155   1081   2084       C  
ATOM   5246  CD1 LEU B 112      20.090  22.757 -51.686  1.00 46.48           C  
ANISOU 5246  CD1 LEU B 112     6232   6939   4491    290   1056   1965       C  
ATOM   5247  CD2 LEU B 112      21.170  25.018 -51.699  1.00 47.99           C  
ANISOU 5247  CD2 LEU B 112     6328   7090   4815    162   1164   2293       C  
ATOM   5248  N   PRO B 113      17.535  27.401 -49.928  1.00 51.85           N  
ANISOU 5248  N   PRO B 113     6959   7094   5647    -28    961   2222       N  
ATOM   5249  CA  PRO B 113      16.211  28.010 -49.797  1.00 55.16           C  
ANISOU 5249  CA  PRO B 113     7429   7415   6116    -36    896   2194       C  
ATOM   5250  C   PRO B 113      15.140  27.167 -50.469  1.00 58.35           C  
ANISOU 5250  C   PRO B 113     7884   7892   6392     71    842   2077       C  
ATOM   5251  O   PRO B 113      15.416  26.304 -51.304  1.00 60.69           O  
ANISOU 5251  O   PRO B 113     8181   8331   6547    165    859   2047       O  
ATOM   5252  CB  PRO B 113      16.374  29.350 -50.517  1.00 49.98           C  
ANISOU 5252  CB  PRO B 113     6751   6765   5474    -39    937   2391       C  
ATOM   5253  CG  PRO B 113      17.379  29.054 -51.583  1.00 55.53           C  
ANISOU 5253  CG  PRO B 113     7411   7642   6045     33   1015   2494       C  
ATOM   5254  CD  PRO B 113      18.329  28.032 -50.999  1.00 53.12           C  
ANISOU 5254  CD  PRO B 113     7075   7370   5738     11   1038   2407       C  
ATOM   5255  N   ARG B 114      13.896  27.430 -50.083  1.00 64.93           N  
ANISOU 5255  N   ARG B 114     8761   8628   7281     56    772   2005       N  
ATOM   5256  CA  ARG B 114      12.776  26.919 -50.857  1.00 78.62           C  
ANISOU 5256  CA  ARG B 114    10539  10428   8903    156    717   1923       C  
ATOM   5257  C   ARG B 114      12.720  27.656 -52.187  1.00 77.63           C  
ANISOU 5257  C   ARG B 114    10413  10407   8677    239    748   2069       C  
ATOM   5258  O   ARG B 114      12.969  28.863 -52.253  1.00 73.03           O  
ANISOU 5258  O   ARG B 114     9811   9777   8160    197    782   2221       O  
ATOM   5259  CB  ARG B 114      11.460  27.087 -50.094  1.00 81.42           C  
ANISOU 5259  CB  ARG B 114    10932  10655   9349    117    637   1819       C  
ATOM   5260  CG  ARG B 114      11.174  28.506 -49.631  1.00 88.55           C  
ANISOU 5260  CG  ARG B 114    11832  11434  10380     46    635   1920       C  
ATOM   5261  CD  ARG B 114      10.071  28.540 -48.588  1.00 94.63           C  
ANISOU 5261  CD  ARG B 114    12629  12073  11253     -5    563   1799       C  
ATOM   5262  NE  ARG B 114       8.859  29.180 -49.092  1.00 99.01           N  
ANISOU 5262  NE  ARG B 114    13214  12613  11793     43    515   1814       N  
ATOM   5263  CZ  ARG B 114       7.993  29.839 -48.327  1.00104.22           C  
ANISOU 5263  CZ  ARG B 114    13888  13149  12562     -4    467   1781       C  
ATOM   5264  NH1 ARG B 114       6.913  30.391 -48.863  1.00107.43           N  
ANISOU 5264  NH1 ARG B 114    14319  13553  12946     51    424   1797       N  
ATOM   5265  NH2 ARG B 114       8.210  29.946 -47.024  1.00102.17           N  
ANISOU 5265  NH2 ARG B 114    13616  12772  12431   -100    462   1732       N  
ATOM   5266  N   LEU B 115      12.424  26.922 -53.257  1.00 81.32           N  
ANISOU 5266  N   LEU B 115    10898  11016   8982    358    735   2024       N  
ATOM   5267  CA  LEU B 115      12.367  27.548 -54.570  1.00 82.21           C  
ANISOU 5267  CA  LEU B 115    11011  11247   8980    450    765   2161       C  
ATOM   5268  C   LEU B 115      11.256  28.589 -54.593  1.00 83.22           C  
ANISOU 5268  C   LEU B 115    11168  11286   9167    440    718   2208       C  
ATOM   5269  O   LEU B 115      10.083  28.269 -54.375  1.00 86.80           O  
ANISOU 5269  O   LEU B 115    11659  11692   9629    457    639   2080       O  
ATOM   5270  CB  LEU B 115      12.169  26.497 -55.665  1.00 91.63           C  
ANISOU 5270  CB  LEU B 115    12223  12610   9983    589    747   2080       C  
ATOM   5271  CG  LEU B 115      11.083  25.420 -55.588  1.00 97.88           C  
ANISOU 5271  CG  LEU B 115    13059  13397  10733    638    654   1874       C  
ATOM   5272  CD1 LEU B 115       9.822  25.859 -56.315  1.00 97.77           C  
ANISOU 5272  CD1 LEU B 115    13081  13405  10662    710    594   1875       C  
ATOM   5273  CD2 LEU B 115      11.604  24.118 -56.175  1.00100.13           C  
ANISOU 5273  CD2 LEU B 115    13343  13821  10880    730    659   1778       C  
ATOM   5274  N   VAL B 116      11.637  29.844 -54.816  1.00 83.95           N  
ANISOU 5274  N   VAL B 116    11238  11349   9310    408    766   2393       N  
ATOM   5275  CA  VAL B 116      10.675  30.938 -54.800  1.00 90.37           C  
ANISOU 5275  CA  VAL B 116    12077  12065  10193    395    725   2452       C  
ATOM   5276  C   VAL B 116       9.820  30.859 -56.056  1.00 93.51           C  
ANISOU 5276  C   VAL B 116    12507  12588  10436    528    694   2460       C  
ATOM   5277  O   VAL B 116      10.337  30.897 -57.178  1.00 96.26           O  
ANISOU 5277  O   VAL B 116    12840  13085  10649    613    746   2570       O  
ATOM   5278  CB  VAL B 116      11.385  32.294 -54.700  1.00 94.72           C  
ANISOU 5278  CB  VAL B 116    12596  12543  10850    321    783   2654       C  
ATOM   5279  CG1 VAL B 116      10.394  33.428 -54.918  1.00 91.27           C  
ANISOU 5279  CG1 VAL B 116    12191  12026  10463    333    742   2729       C  
ATOM   5280  CG2 VAL B 116      12.073  32.433 -53.358  1.00 97.24           C  
ANISOU 5280  CG2 VAL B 116    12887  12721  11337    186    797   2627       C  
ATOM   5281  N   ARG B 117       8.516  30.739 -55.872  1.00 93.43           N  
ANISOU 5281  N   ARG B 117    12536  12524  10439    551    609   2341       N  
ATOM   5282  CA  ARG B 117       7.595  30.783 -56.996  1.00 92.39           C  
ANISOU 5282  CA  ARG B 117    12433  12495  10175    673    568   2347       C  
ATOM   5283  C   ARG B 117       7.528  32.201 -57.540  1.00 94.45           C  
ANISOU 5283  C   ARG B 117    12693  12736  10456    684    595   2547       C  
ATOM   5284  O   ARG B 117       7.051  33.099 -56.833  1.00100.05           O  
ANISOU 5284  O   ARG B 117    13413  13293  11310    612    568   2575       O  
ATOM   5285  CB  ARG B 117       6.205  30.315 -56.570  1.00 85.76           C  
ANISOU 5285  CB  ARG B 117    11629  11595   9363    683    467   2168       C  
ATOM   5286  CG  ARG B 117       5.856  28.912 -57.025  1.00 82.86           C  
ANISOU 5286  CG  ARG B 117    11276  11342   8867    766    421   2001       C  
ATOM   5287  CD  ARG B 117       6.568  27.874 -56.179  1.00 88.13           C  
ANISOU 5287  CD  ARG B 117    11927  11979   9579    700    437   1886       C  
ATOM   5288  NE  ARG B 117       6.331  26.517 -56.661  1.00 90.13           N  
ANISOU 5288  NE  ARG B 117    12195  12339   9712    782    394   1732       N  
ATOM   5289  CZ  ARG B 117       6.445  25.429 -55.906  1.00 80.13           C  
ANISOU 5289  CZ  ARG B 117    10928  11031   8487    737    369   1582       C  
ATOM   5290  NH1 ARG B 117       6.213  24.231 -56.425  1.00 73.55           N  
ANISOU 5290  NH1 ARG B 117    10109  10290   7546    817    324   1446       N  
ATOM   5291  NH2 ARG B 117       6.796  25.540 -54.632  1.00 76.60           N  
ANISOU 5291  NH2 ARG B 117    10465  10447   8190    615    387   1566       N  
ATOM   5292  N   PRO B 118       7.992  32.460 -58.761  1.00 88.23           N  
ANISOU 5292  N   PRO B 118    11896  12096   9532    775    648   2690       N  
ATOM   5293  CA  PRO B 118       7.805  33.792 -59.342  1.00 92.25           C  
ANISOU 5293  CA  PRO B 118    12409  12587  10056    794    666   2884       C  
ATOM   5294  C   PRO B 118       6.387  33.944 -59.866  1.00 95.50           C  
ANISOU 5294  C   PRO B 118    12864  13015  10406    885    583   2829       C  
ATOM   5295  O   PRO B 118       5.516  33.129 -59.544  1.00 99.21           O  
ANISOU 5295  O   PRO B 118    13358  13475  10864    904    507   2637       O  
ATOM   5296  CB  PRO B 118       8.853  33.846 -60.465  1.00 85.65           C  
ANISOU 5296  CB  PRO B 118    11541  11923   9078    865    758   3050       C  
ATOM   5297  CG  PRO B 118       9.486  32.462 -60.526  1.00 84.28           C  
ANISOU 5297  CG  PRO B 118    11351  11870   8801    898    777   2920       C  
ATOM   5298  CD  PRO B 118       8.642  31.540 -59.705  1.00 84.77           C  
ANISOU 5298  CD  PRO B 118    11444  11854   8912    874    688   2681       C  
ATOM   5299  N   GLU B 119       6.131  34.976 -60.661  1.00 97.98           N  
ANISOU 5299  N   GLU B 119    13188  13355  10686    940    594   2997       N  
ATOM   5300  CA  GLU B 119       4.783  35.170 -61.168  1.00 99.25           C  
ANISOU 5300  CA  GLU B 119    13388  13534  10790   1031    513   2950       C  
ATOM   5301  C   GLU B 119       4.452  34.109 -62.216  1.00 94.75           C  
ANISOU 5301  C   GLU B 119    12830  13164  10007   1171    485   2852       C  
ATOM   5302  O   GLU B 119       5.327  33.412 -62.738  1.00 84.58           O  
ANISOU 5302  O   GLU B 119    11521  12013   8601   1214    540   2861       O  
ATOM   5303  CB  GLU B 119       4.625  36.581 -61.736  1.00 98.05           C  
ANISOU 5303  CB  GLU B 119    13245  13351  10660   1055    532   3164       C  
ATOM   5304  CG  GLU B 119       4.140  37.579 -60.692  1.00 94.60           C  
ANISOU 5304  CG  GLU B 119    12819  12692  10431    951    495   3178       C  
ATOM   5305  CD  GLU B 119       3.860  38.956 -61.259  1.00100.53           C  
ANISOU 5305  CD  GLU B 119    13585  13402  11210    983    499   3378       C  
ATOM   5306  OE1 GLU B 119       2.684  39.240 -61.570  1.00103.10           O  
ANISOU 5306  OE1 GLU B 119    13944  13723  11508   1057    427   3342       O  
ATOM   5307  OE2 GLU B 119       4.807  39.762 -61.373  1.00103.09           O  
ANISOU 5307  OE2 GLU B 119    13885  13692  11591    932    573   3573       O  
ATOM   5308  N   VAL B 120       3.155  33.970 -62.500  1.00 93.31           N  
ANISOU 5308  N   VAL B 120    12679  12996   9778   1244    394   2748       N  
ATOM   5309  CA  VAL B 120       2.713  32.883 -63.368  1.00 84.32           C  
ANISOU 5309  CA  VAL B 120    11553  12028   8456   1371    347   2617       C  
ATOM   5310  C   VAL B 120       3.230  33.081 -64.786  1.00 84.46           C  
ANISOU 5310  C   VAL B 120    11567  12241   8282   1499    402   2771       C  
ATOM   5311  O   VAL B 120       3.517  32.106 -65.493  1.00 80.44           O  
ANISOU 5311  O   VAL B 120    11054  11897   7611   1592    405   2696       O  
ATOM   5312  CB  VAL B 120       1.175  32.758 -63.319  1.00 83.23           C  
ANISOU 5312  CB  VAL B 120    11444  11855   8325   1414    233   2475       C  
ATOM   5313  CG1 VAL B 120       0.674  31.736 -64.328  1.00 84.69           C  
ANISOU 5313  CG1 VAL B 120    11641  12220   8317   1553    176   2350       C  
ATOM   5314  CG2 VAL B 120       0.723  32.382 -61.917  1.00 85.24           C  
ANISOU 5314  CG2 VAL B 120    11695  11939   8752   1293    185   2312       C  
ATOM   5315  N   ASP B 121       3.388  34.334 -65.216  1.00 89.48           N  
ANISOU 5315  N   ASP B 121    12201  12864   8932   1508    448   2990       N  
ATOM   5316  CA  ASP B 121       3.840  34.587 -66.580  1.00 95.53           C  
ANISOU 5316  CA  ASP B 121    12961  13822   9512   1633    503   3153       C  
ATOM   5317  C   ASP B 121       5.330  34.305 -66.735  1.00 91.53           C  
ANISOU 5317  C   ASP B 121    12414  13403   8960   1610    614   3250       C  
ATOM   5318  O   ASP B 121       5.739  33.598 -67.663  1.00 85.13           O  
ANISOU 5318  O   ASP B 121    11585  12770   7989   1706    634   3205       O  
ATOM   5319  CB  ASP B 121       3.514  36.021 -66.994  1.00103.39           C  
ANISOU 5319  CB  ASP B 121    13969  14772  10543   1650    516   3365       C  
ATOM   5320  CG  ASP B 121       2.976  36.105 -68.413  1.00114.42           C  
ANISOU 5320  CG  ASP B 121    15372  16331  11772   1796    486   3377       C  
ATOM   5321  OD1 ASP B 121       3.742  35.835 -69.362  1.00118.34           O  
ANISOU 5321  OD1 ASP B 121    15833  16977  12153   1852    544   3407       O  
ATOM   5322  OD2 ASP B 121       1.781  36.429 -68.578  1.00117.02           O  
ANISOU 5322  OD2 ASP B 121    15738  16641  12083   1859    405   3352       O  
ATOM   5323  N   VAL B 122       6.163  34.839 -65.834  1.00 94.86           N  
ANISOU 5323  N   VAL B 122    12806  13682   9553   1467    676   3338       N  
ATOM   5324  CA  VAL B 122       7.603  34.613 -65.936  1.00 94.54           C  
ANISOU 5324  CA  VAL B 122    12707  13696   9517   1417    770   3386       C  
ATOM   5325  C   VAL B 122       7.940  33.124 -65.923  1.00 94.38           C  
ANISOU 5325  C   VAL B 122    12688  13802   9370   1473    769   3228       C  
ATOM   5326  O   VAL B 122       8.964  32.713 -66.479  1.00 96.50           O  
ANISOU 5326  O   VAL B 122    12911  14192   9564   1498    834   3242       O  
ATOM   5327  CB  VAL B 122       8.342  35.393 -64.816  1.00 92.64           C  
ANISOU 5327  CB  VAL B 122    12436  13262   9499   1245    819   3479       C  
ATOM   5328  CG1 VAL B 122       7.728  35.111 -63.460  1.00 87.01           C  
ANISOU 5328  CG1 VAL B 122    11755  12380   8926   1156    757   3344       C  
ATOM   5329  CG2 VAL B 122       9.849  35.098 -64.833  1.00 93.11           C  
ANISOU 5329  CG2 VAL B 122    12431  13377   9570   1190    911   3516       C  
ATOM   5330  N   MET B 123       7.075  32.296 -65.339  1.00 94.40           N  
ANISOU 5330  N   MET B 123    12725  13748   9396   1469    677   3009       N  
ATOM   5331  CA  MET B 123       7.324  30.860 -65.320  1.00 91.52           C  
ANISOU 5331  CA  MET B 123    12358  13472   8943   1509    657   2818       C  
ATOM   5332  C   MET B 123       7.002  30.195 -66.654  1.00 85.74           C  
ANISOU 5332  C   MET B 123    11643  12961   7974   1689    629   2768       C  
ATOM   5333  O   MET B 123       7.664  29.219 -67.027  1.00 88.80           O  
ANISOU 5333  O   MET B 123    12017  13481   8243   1752    654   2694       O  
ATOM   5334  CB  MET B 123       6.515  30.202 -64.204  1.00 91.14           C  
ANISOU 5334  CB  MET B 123    12333  13270   9025   1429    566   2594       C  
ATOM   5335  CG  MET B 123       6.989  30.584 -62.813  1.00 91.63           C  
ANISOU 5335  CG  MET B 123    12376  13135   9305   1258    595   2608       C  
ATOM   5336  SD  MET B 123       5.773  30.237 -61.528  1.00 86.09           S  
ANISOU 5336  SD  MET B 123    11703  12240   8768   1167    486   2396       S  
ATOM   5337  CE  MET B 123       5.444  28.508 -61.838  1.00 78.26           C  
ANISOU 5337  CE  MET B 123    10727  11364   7644   1253    420   2155       C  
ATOM   5338  N   CYS B 124       6.001  30.701 -67.385  1.00 81.25           N  
ANISOU 5338  N   CYS B 124    11104  12437   7330   1780    575   2801       N  
ATOM   5339  CA  CYS B 124       5.621  30.071 -68.648  1.00 74.93           C  
ANISOU 5339  CA  CYS B 124    10322  11848   6301   1958    536   2741       C  
ATOM   5340  C   CYS B 124       6.499  30.549 -69.803  1.00 64.19           C  
ANISOU 5340  C   CYS B 124     8911  10619   4859   2013    622   2882       C  
ATOM   5341  O   CYS B 124       6.820  29.762 -70.700  1.00 73.21           O  
ANISOU 5341  O   CYS B 124    10038  11929   5849   2123    626   2802       O  
ATOM   5342  CB  CYS B 124       4.142  30.326 -68.963  1.00 72.42           C  
ANISOU 5342  CB  CYS B 124    10043  11511   5962   2021    428   2671       C  
ATOM   5343  SG  CYS B 124       2.950  29.627 -67.770  1.00 76.47           S  
ANISOU 5343  SG  CYS B 124    10581  11837   6638   1928    301   2404       S  
ATOM   5344  N   THR B 125       6.876  31.834 -69.820  1.00 64.65           N  
ANISOU 5344  N   THR B 125     8940  10595   5028   1937    686   3078       N  
ATOM   5345  CA  THR B 125       7.850  32.297 -70.806  1.00 76.36           C  
ANISOU 5345  CA  THR B 125    10365  12188   6462   1967    776   3213       C  
ATOM   5346  C   THR B 125       9.163  31.540 -70.669  1.00 72.83           C  
ANISOU 5346  C   THR B 125     9869  11807   5997   1942    850   3185       C  
ATOM   5347  O   THR B 125       9.774  31.160 -71.673  1.00 66.68           O  
ANISOU 5347  O   THR B 125     9052  11195   5087   2037    892   3188       O  
ATOM   5348  CB  THR B 125       8.089  33.804 -70.668  1.00 83.92           C  
ANISOU 5348  CB  THR B 125    11299  13019   7569   1867    827   3423       C  
ATOM   5349  OG1 THR B 125       9.036  34.053 -69.622  1.00 96.19           O  
ANISOU 5349  OG1 THR B 125    12820  14439   9287   1716    889   3483       O  
ATOM   5350  CG2 THR B 125       6.792  34.546 -70.383  1.00 79.91           C  
ANISOU 5350  CG2 THR B 125    10844  12391   7127   1860    748   3439       C  
ATOM   5351  N   ALA B 126       9.618  31.320 -69.432  1.00 70.71           N  
ANISOU 5351  N   ALA B 126     9598  11409   5859   1818    869   3159       N  
ATOM   5352  CA  ALA B 126      10.794  30.484 -69.216  1.00 74.03           C  
ANISOU 5352  CA  ALA B 126     9977  11891   6261   1798    929   3110       C  
ATOM   5353  C   ALA B 126      10.524  29.044 -69.635  1.00 74.70           C  
ANISOU 5353  C   ALA B 126    10089  12118   6174   1927    874   2908       C  
ATOM   5354  O   ALA B 126      11.381  28.393 -70.243  1.00 70.95           O  
ANISOU 5354  O   ALA B 126     9575  11783   5600   1994    919   2876       O  
ATOM   5355  CB  ALA B 126      11.221  30.551 -67.750  1.00 76.69           C  
ANISOU 5355  CB  ALA B 126    10310  12051   6776   1640    951   3115       C  
ATOM   5356  N   PHE B 127       9.330  28.532 -69.323  1.00 76.18           N  
ANISOU 5356  N   PHE B 127    10343  12272   6329   1966    771   2765       N  
ATOM   5357  CA  PHE B 127       8.969  27.188 -69.760  1.00 72.07           C  
ANISOU 5357  CA  PHE B 127     9853  11878   5653   2090    701   2558       C  
ATOM   5358  C   PHE B 127       8.799  27.117 -71.272  1.00 67.28           C  
ANISOU 5358  C   PHE B 127     9233  11453   4879   2245    689   2551       C  
ATOM   5359  O   PHE B 127       9.083  26.078 -71.877  1.00 69.69           O  
ANISOU 5359  O   PHE B 127     9532  11895   5054   2350    673   2420       O  
ATOM   5360  CB  PHE B 127       7.687  26.732 -69.060  1.00 61.97           C  
ANISOU 5360  CB  PHE B 127     8643  10511   4393   2087    586   2408       C  
ATOM   5361  CG  PHE B 127       7.137  25.435 -69.584  1.00 67.84           C  
ANISOU 5361  CG  PHE B 127     9416  11361   4999   2208    491   2177       C  
ATOM   5362  CD1 PHE B 127       7.760  24.233 -69.290  1.00 67.06           C  
ANISOU 5362  CD1 PHE B 127     9310  11285   4884   2210    489   2024       C  
ATOM   5363  CD2 PHE B 127       5.997  25.417 -70.372  1.00 67.47           C  
ANISOU 5363  CD2 PHE B 127     9403  11388   4843   2323    399   2110       C  
ATOM   5364  CE1 PHE B 127       7.257  23.038 -69.770  1.00 61.86           C  
ANISOU 5364  CE1 PHE B 127     8681  10714   4110   2321    395   1808       C  
ATOM   5365  CE2 PHE B 127       5.490  24.225 -70.856  1.00 60.67           C  
ANISOU 5365  CE2 PHE B 127     8568  10621   3864   2433    304   1892       C  
ATOM   5366  CZ  PHE B 127       6.121  23.035 -70.553  1.00 58.21           C  
ANISOU 5366  CZ  PHE B 127     8251  10323   3544   2431    301   1740       C  
ATOM   5367  N   HIS B 128       8.342  28.204 -71.898  1.00 71.39           N  
ANISOU 5367  N   HIS B 128     9748  11976   5403   2264    695   2687       N  
ATOM   5368  CA  HIS B 128       8.158  28.205 -73.345  1.00 70.58           C  
ANISOU 5368  CA  HIS B 128     9631  12047   5141   2413    686   2691       C  
ATOM   5369  C   HIS B 128       9.475  28.420 -74.082  1.00 70.02           C  
ANISOU 5369  C   HIS B 128     9487  12090   5027   2435    799   2816       C  
ATOM   5370  O   HIS B 128       9.717  27.788 -75.116  1.00 66.71           O  
ANISOU 5370  O   HIS B 128     9047  11844   4454   2569    800   2751       O  
ATOM   5371  CB  HIS B 128       7.149  29.280 -73.748  1.00 80.48           C  
ANISOU 5371  CB  HIS B 128    10907  13262   6410   2430    648   2790       C  
ATOM   5372  CG  HIS B 128       5.721  28.847 -73.631  1.00 78.10           C  
ANISOU 5372  CG  HIS B 128    10669  12938   6067   2487    519   2631       C  
ATOM   5373  ND1 HIS B 128       4.706  29.718 -73.299  1.00 74.61           N  
ANISOU 5373  ND1 HIS B 128    10260  12383   5706   2449    467   2690       N  
ATOM   5374  CD2 HIS B 128       5.137  27.638 -73.806  1.00 76.13           C  
ANISOU 5374  CD2 HIS B 128    10452  12764   5712   2579    425   2411       C  
ATOM   5375  CE1 HIS B 128       3.559  29.064 -73.270  1.00 75.97           C  
ANISOU 5375  CE1 HIS B 128    10479  12567   5820   2515    349   2516       C  
ATOM   5376  NE2 HIS B 128       3.792  27.800 -73.576  1.00 77.23           N  
ANISOU 5376  NE2 HIS B 128    10639  12837   5869   2591    319   2342       N  
ATOM   5377  N   ASP B 129      10.328  29.311 -73.569  1.00 74.75           N  
ANISOU 5377  N   ASP B 129    10044  12595   5765   2308    890   2993       N  
ATOM   5378  CA  ASP B 129      11.597  29.607 -74.230  1.00 82.32           C  
ANISOU 5378  CA  ASP B 129    10926  13657   6697   2320    998   3125       C  
ATOM   5379  C   ASP B 129      12.444  28.348 -74.373  1.00 74.14           C  
ANISOU 5379  C   ASP B 129     9862  12742   5567   2383   1019   2997       C  
ATOM   5380  O   ASP B 129      12.778  27.928 -75.487  1.00 70.85           O  
ANISOU 5380  O   ASP B 129     9414  12504   5000   2516   1037   2975       O  
ATOM   5381  CB  ASP B 129      12.353  30.685 -73.450  1.00 88.94           C  
ANISOU 5381  CB  ASP B 129    11724  14346   7724   2153   1077   3310       C  
ATOM   5382  CG  ASP B 129      13.366  31.424 -74.304  1.00 98.59           C  
ANISOU 5382  CG  ASP B 129    12870  15661   8931   2165   1177   3493       C  
ATOM   5383  OD1 ASP B 129      14.104  30.763 -75.065  1.00100.55           O  
ANISOU 5383  OD1 ASP B 129    13073  16079   9053   2262   1218   3463       O  
ATOM   5384  OD2 ASP B 129      13.424  32.668 -74.214  1.00103.97           O  
ANISOU 5384  OD2 ASP B 129    13534  16243   9727   2079   1211   3667       O  
ATOM   5385  N   ASN B 130      12.802  27.732 -73.250  1.00 76.28           N  
ANISOU 5385  N   ASN B 130    10142  12916   5923   2293   1017   2912       N  
ATOM   5386  CA  ASN B 130      13.525  26.462 -73.241  1.00 72.56           C  
ANISOU 5386  CA  ASN B 130     9655  12540   5375   2348   1025   2770       C  
ATOM   5387  C   ASN B 130      12.746  25.507 -72.343  1.00 78.65           C  
ANISOU 5387  C   ASN B 130    10497  13224   6161   2332    930   2570       C  
ATOM   5388  O   ASN B 130      12.836  25.587 -71.114  1.00 61.44           O  
ANISOU 5388  O   ASN B 130     8332  10892   4120   2200    935   2574       O  
ATOM   5389  CB  ASN B 130      14.962  26.639 -72.762  1.00 68.83           C  
ANISOU 5389  CB  ASN B 130     9112  12046   4996   2251   1131   2877       C  
ATOM   5390  CG  ASN B 130      15.861  25.490 -73.181  1.00 71.23           C  
ANISOU 5390  CG  ASN B 130     9379  12498   5187   2346   1156   2770       C  
ATOM   5391  OD1 ASN B 130      17.077  25.538 -72.992  1.00 80.52           O  
ANISOU 5391  OD1 ASN B 130    10489  13694   6410   2296   1241   2849       O  
ATOM   5392  ND2 ASN B 130      15.267  24.449 -73.752  1.00 70.06           N  
ANISOU 5392  ND2 ASN B 130     9273  12454   4894   2486   1078   2586       N  
ATOM   5393  N   GLU B 131      11.980  24.607 -72.964  1.00 82.87           N  
ANISOU 5393  N   GLU B 131    11074  13855   6557   2466    839   2392       N  
ATOM   5394  CA  GLU B 131      11.163  23.673 -72.197  1.00 74.53           C  
ANISOU 5394  CA  GLU B 131    10086  12722   5509   2460    737   2192       C  
ATOM   5395  C   GLU B 131      12.016  22.731 -71.360  1.00 67.35           C  
ANISOU 5395  C   GLU B 131     9169  11781   4640   2409    761   2098       C  
ATOM   5396  O   GLU B 131      11.596  22.313 -70.274  1.00 67.05           O  
ANISOU 5396  O   GLU B 131     9177  11619   4679   2333    710   2003       O  
ATOM   5397  CB  GLU B 131      10.259  22.874 -73.138  1.00 78.54           C  
ANISOU 5397  CB  GLU B 131    10632  13347   5862   2619    631   2014       C  
ATOM   5398  CG  GLU B 131       9.351  21.876 -72.434  1.00 77.52           C  
ANISOU 5398  CG  GLU B 131    10571  13141   5740   2618    511   1794       C  
ATOM   5399  CD  GLU B 131       8.120  21.527 -73.246  1.00 86.24           C  
ANISOU 5399  CD  GLU B 131    11716  14314   6738   2740    392   1655       C  
ATOM   5400  OE1 GLU B 131       7.403  22.456 -73.673  1.00 89.26           O  
ANISOU 5400  OE1 GLU B 131    12103  14694   7118   2752    379   1755       O  
ATOM   5401  OE2 GLU B 131       7.869  20.321 -73.455  1.00 91.32           O  
ANISOU 5401  OE2 GLU B 131    12384  15006   7305   2824    308   1443       O  
ATOM   5402  N   GLU B 132      13.217  22.396 -71.832  1.00 61.66           N  
ANISOU 5402  N   GLU B 132     8389  11171   3868   2452    837   2126       N  
ATOM   5403  CA  GLU B 132      14.026  21.375 -71.183  1.00 75.30           C  
ANISOU 5403  CA  GLU B 132    10109  12890   5611   2431    853   2017       C  
ATOM   5404  C   GLU B 132      15.061  21.932 -70.215  1.00 71.63           C  
ANISOU 5404  C   GLU B 132     9596  12326   5295   2279    952   2161       C  
ATOM   5405  O   GLU B 132      15.502  21.199 -69.324  1.00 79.33           O  
ANISOU 5405  O   GLU B 132    10579  13242   6320   2226    953   2072       O  
ATOM   5406  CB  GLU B 132      14.714  20.503 -72.238  1.00 82.16           C  
ANISOU 5406  CB  GLU B 132    10943  13943   6332   2581    865   1932       C  
ATOM   5407  CG  GLU B 132      13.771  19.484 -72.863  1.00 87.23           C  
ANISOU 5407  CG  GLU B 132    11642  14655   6847   2722    743   1711       C  
ATOM   5408  CD  GLU B 132      14.437  18.150 -73.128  1.00 91.77           C  
ANISOU 5408  CD  GLU B 132    12207  15323   7338   2821    726   1543       C  
ATOM   5409  OE1 GLU B 132      13.776  17.108 -72.935  1.00 91.15           O  
ANISOU 5409  OE1 GLU B 132    12188  15216   7230   2868    618   1329       O  
ATOM   5410  OE2 GLU B 132      15.619  18.143 -73.532  1.00 95.19           O  
ANISOU 5410  OE2 GLU B 132    12574  15855   7740   2853    816   1623       O  
ATOM   5411  N   THR B 133      15.464  23.197 -70.359  1.00 60.67           N  
ANISOU 5411  N   THR B 133     8156  10911   3982   2207   1032   2375       N  
ATOM   5412  CA  THR B 133      16.203  23.838 -69.275  1.00 70.59           C  
ANISOU 5412  CA  THR B 133     9378  12032   5413   2040   1104   2501       C  
ATOM   5413  C   THR B 133      15.292  24.095 -68.082  1.00 63.23           C  
ANISOU 5413  C   THR B 133     8507  10912   4606   1926   1047   2473       C  
ATOM   5414  O   THR B 133      15.728  23.996 -66.929  1.00 63.24           O  
ANISOU 5414  O   THR B 133     8504  10797   4730   1808   1071   2472       O  
ATOM   5415  CB  THR B 133      16.835  25.146 -69.761  1.00 67.92           C  
ANISOU 5415  CB  THR B 133     8969  11704   5133   1991   1192   2729       C  
ATOM   5416  OG1 THR B 133      17.744  24.870 -70.833  1.00 80.62           O  
ANISOU 5416  OG1 THR B 133    10515  13495   6624   2098   1249   2758       O  
ATOM   5417  CG2 THR B 133      17.594  25.834 -68.632  1.00 61.87           C  
ANISOU 5417  CG2 THR B 133     8163  10786   4560   1813   1256   2849       C  
ATOM   5418  N   PHE B 134      14.020  24.401 -68.346  1.00 66.77           N  
ANISOU 5418  N   PHE B 134     9012  11335   5024   1964    970   2446       N  
ATOM   5419  CA  PHE B 134      13.054  24.627 -67.277  1.00 61.88           C  
ANISOU 5419  CA  PHE B 134     8452  10547   4512   1873    908   2414       C  
ATOM   5420  C   PHE B 134      12.832  23.361 -66.457  1.00 66.38           C  
ANISOU 5420  C   PHE B 134     9056  11043   5122   1849    836   2183       C  
ATOM   5421  O   PHE B 134      12.830  23.398 -65.221  1.00 56.39           O  
ANISOU 5421  O   PHE B 134     7789   9588   4050   1701    823   2138       O  
ATOM   5422  CB  PHE B 134      11.739  25.120 -67.881  1.00 66.44           C  
ANISOU 5422  CB  PHE B 134     9076  11132   5037   1939    832   2413       C  
ATOM   5423  CG  PHE B 134      10.760  25.641 -66.874  1.00 55.38           C  
ANISOU 5423  CG  PHE B 134     7711   9524   3806   1821    769   2389       C  
ATOM   5424  CD1 PHE B 134      10.800  26.965 -66.471  1.00 58.49           C  
ANISOU 5424  CD1 PHE B 134     8089   9803   4333   1716    816   2578       C  
ATOM   5425  CD2 PHE B 134       9.788  24.812 -66.341  1.00 60.95           C  
ANISOU 5425  CD2 PHE B 134     8459  10132   4567   1805    655   2161       C  
ATOM   5426  CE1 PHE B 134       9.896  27.450 -65.547  1.00 60.19           C  
ANISOU 5426  CE1 PHE B 134     8329   9814   4725   1605    751   2533       C  
ATOM   5427  CE2 PHE B 134       8.880  25.291 -65.417  1.00 65.11           C  
ANISOU 5427  CE2 PHE B 134     9006  10461   5270   1690    595   2124       C  
ATOM   5428  CZ  PHE B 134       8.934  26.612 -65.020  1.00 65.86           C  
ANISOU 5428  CZ  PHE B 134     9086  10449   5488   1594    643   2306       C  
ATOM   5429  N   LEU B 135      12.648  22.225 -67.133  1.00 65.43           N  
ANISOU 5429  N   LEU B 135     8960  11053   4846   1986    780   2017       N  
ATOM   5430  CA  LEU B 135      12.338  20.984 -66.432  1.00 62.64           C  
ANISOU 5430  CA  LEU B 135     8637  10607   4557   1959    694   1775       C  
ATOM   5431  C   LEU B 135      13.574  20.345 -65.812  1.00 62.95           C  
ANISOU 5431  C   LEU B 135     8640  10635   4641   1909    756   1750       C  
ATOM   5432  O   LEU B 135      13.467  19.698 -64.763  1.00 65.34           O  
ANISOU 5432  O   LEU B 135     8957  10787   5082   1814    709   1612       O  
ATOM   5433  CB  LEU B 135      11.656  20.002 -67.384  1.00 70.56           C  
ANISOU 5433  CB  LEU B 135     9681  11740   5386   2124    600   1598       C  
ATOM   5434  CG  LEU B 135      10.131  20.112 -67.408  1.00 78.19           C  
ANISOU 5434  CG  LEU B 135    10696  12625   6388   2125    483   1499       C  
ATOM   5435  CD1 LEU B 135       9.541  19.173 -68.442  1.00 84.79           C  
ANISOU 5435  CD1 LEU B 135    11567  13607   7043   2295    391   1332       C  
ATOM   5436  CD2 LEU B 135       9.558  19.827 -66.031  1.00 69.49           C  
ANISOU 5436  CD2 LEU B 135     9611  11290   5504   1968    420   1377       C  
ATOM   5437  N   LYS B 136      14.744  20.503 -66.437  1.00 62.81           N  
ANISOU 5437  N   LYS B 136     8574  10779   4510   1975    861   1884       N  
ATOM   5438  CA  LYS B 136      15.973  20.034 -65.808  1.00 54.27           C  
ANISOU 5438  CA  LYS B 136     7449   9687   3484   1919    929   1884       C  
ATOM   5439  C   LYS B 136      16.258  20.801 -64.524  1.00 55.68           C  
ANISOU 5439  C   LYS B 136     7601   9666   3890   1723    968   1979       C  
ATOM   5440  O   LYS B 136      16.780  20.229 -63.559  1.00 57.62           O  
ANISOU 5440  O   LYS B 136     7835   9812   4246   1638    969   1897       O  
ATOM   5441  CB  LYS B 136      17.149  20.161 -66.778  1.00 63.23           C  
ANISOU 5441  CB  LYS B 136     8516  11012   4495   2009   1028   2004       C  
ATOM   5442  CG  LYS B 136      17.406  18.915 -67.612  1.00 62.61           C  
ANISOU 5442  CG  LYS B 136     8443  11087   4260   2169    992   1837       C  
ATOM   5443  CD  LYS B 136      18.121  19.258 -68.912  1.00 75.22           C  
ANISOU 5443  CD  LYS B 136     9969  12850   5761   2267   1055   1937       C  
ATOM   5444  CE  LYS B 136      17.954  18.155 -69.944  1.00 74.20           C  
ANISOU 5444  CE  LYS B 136     9859  12871   5462   2448    993   1763       C  
ATOM   5445  NZ  LYS B 136      16.939  18.506 -70.973  1.00 82.93           N  
ANISOU 5445  NZ  LYS B 136    10993  14044   6474   2544    935   1757       N  
ATOM   5446  N   LYS B 137      15.919  22.092 -64.493  1.00 53.10           N  
ANISOU 5446  N   LYS B 137     7266   9277   3635   1654    996   2148       N  
ATOM   5447  CA  LYS B 137      16.058  22.861 -63.262  1.00 55.32           C  
ANISOU 5447  CA  LYS B 137     7527   9356   4137   1472   1017   2223       C  
ATOM   5448  C   LYS B 137      15.124  22.335 -62.180  1.00 54.78           C  
ANISOU 5448  C   LYS B 137     7508   9094   4212   1385    913   2032       C  
ATOM   5449  O   LYS B 137      15.479  22.329 -60.997  1.00 48.98           O  
ANISOU 5449  O   LYS B 137     6759   8212   3641   1253    921   2009       O  
ATOM   5450  CB  LYS B 137      15.790  24.341 -63.535  1.00 63.73           C  
ANISOU 5450  CB  LYS B 137     8579  10391   5243   1430   1056   2434       C  
ATOM   5451  CG  LYS B 137      17.008  25.110 -64.019  1.00 73.74           C  
ANISOU 5451  CG  LYS B 137     9774  11758   6486   1424   1177   2654       C  
ATOM   5452  CD  LYS B 137      16.689  26.580 -64.227  1.00 82.88           C  
ANISOU 5452  CD  LYS B 137    10916  12834   7740   1359   1192   2827       C  
ATOM   5453  CE  LYS B 137      17.852  27.307 -64.884  1.00 92.54           C  
ANISOU 5453  CE  LYS B 137    12051  14124   8984   1342   1281   2984       C  
ATOM   5454  NZ  LYS B 137      17.496  28.703 -65.258  1.00 97.28           N  
ANISOU 5454  NZ  LYS B 137    12643  14661   9659   1300   1289   3146       N  
ATOM   5455  N   TYR B 138      13.928  21.884 -62.566  1.00 51.57           N  
ANISOU 5455  N   TYR B 138     7156   8692   3745   1457    814   1894       N  
ATOM   5456  CA  TYR B 138      13.015  21.285 -61.597  1.00 51.51           C  
ANISOU 5456  CA  TYR B 138     7190   8517   3864   1382    715   1709       C  
ATOM   5457  C   TYR B 138      13.619  20.025 -60.991  1.00 56.35           C  
ANISOU 5457  C   TYR B 138     7800   9108   4501   1368    702   1557       C  
ATOM   5458  O   TYR B 138      13.603  19.840 -59.769  1.00 55.53           O  
ANISOU 5458  O   TYR B 138     7698   8842   4559   1243    683   1493       O  
ATOM   5459  CB  TYR B 138      11.672  20.976 -62.259  1.00 52.77           C  
ANISOU 5459  CB  TYR B 138     7400   8708   3940   1475    611   1592       C  
ATOM   5460  CG  TYR B 138      10.755  20.118 -61.413  1.00 66.19           C  
ANISOU 5460  CG  TYR B 138     9138  10267   5745   1419    505   1383       C  
ATOM   5461  CD1 TYR B 138      10.025  20.669 -60.367  1.00 67.27           C  
ANISOU 5461  CD1 TYR B 138     9283  10218   6057   1287    471   1378       C  
ATOM   5462  CD2 TYR B 138      10.620  18.757 -61.660  1.00 67.63           C  
ANISOU 5462  CD2 TYR B 138     9345  10500   5851   1498    439   1193       C  
ATOM   5463  CE1 TYR B 138       9.187  19.889 -59.592  1.00 69.36           C  
ANISOU 5463  CE1 TYR B 138     9576  10362   6417   1235    380   1199       C  
ATOM   5464  CE2 TYR B 138       9.785  17.969 -60.889  1.00 62.56           C  
ANISOU 5464  CE2 TYR B 138     8732   9725   5312   1441    344   1012       C  
ATOM   5465  CZ  TYR B 138       9.071  18.540 -59.857  1.00 68.40           C  
ANISOU 5465  CZ  TYR B 138     9476  10290   6223   1308    318   1021       C  
ATOM   5466  OH  TYR B 138       8.238  17.761 -59.087  1.00 64.65           O  
ANISOU 5466  OH  TYR B 138     9024   9691   5848   1250    228    852       O  
ATOM   5467  N   LEU B 139      14.157  19.142 -61.838  1.00 48.87           N  
ANISOU 5467  N   LEU B 139     6851   8326   3391   1500    711   1495       N  
ATOM   5468  CA  LEU B 139      14.838  17.951 -61.342  1.00 50.66           C  
ANISOU 5468  CA  LEU B 139     7074   8543   3632   1500    705   1361       C  
ATOM   5469  C   LEU B 139      15.989  18.322 -60.420  1.00 55.95           C  
ANISOU 5469  C   LEU B 139     7692   9144   4423   1380    794   1467       C  
ATOM   5470  O   LEU B 139      16.156  17.728 -59.348  1.00 64.78           O  
ANISOU 5470  O   LEU B 139     8815  10136   5664   1292    769   1367       O  
ATOM   5471  CB  LEU B 139      15.353  17.117 -62.516  1.00 56.34           C  
ANISOU 5471  CB  LEU B 139     7793   9471   4144   1675    714   1306       C  
ATOM   5472  CG  LEU B 139      14.330  16.442 -63.428  1.00 58.63           C  
ANISOU 5472  CG  LEU B 139     8135   9840   4302   1810    611   1156       C  
ATOM   5473  CD1 LEU B 139      15.029  15.450 -64.337  1.00 59.44           C  
ANISOU 5473  CD1 LEU B 139     8235  10128   4222   1972    619   1075       C  
ATOM   5474  CD2 LEU B 139      13.244  15.755 -62.618  1.00 54.36           C  
ANISOU 5474  CD2 LEU B 139     7642   9126   3887   1740    493    967       C  
ATOM   5475  N   TYR B 140      16.790  19.311 -60.822  1.00 59.38           N  
ANISOU 5475  N   TYR B 140     8074   9660   4826   1376    895   1672       N  
ATOM   5476  CA  TYR B 140      17.974  19.684 -60.056  1.00 58.64           C  
ANISOU 5476  CA  TYR B 140     7922   9521   4837   1271    982   1781       C  
ATOM   5477  C   TYR B 140      17.596  20.231 -58.684  1.00 59.62           C  
ANISOU 5477  C   TYR B 140     8052   9421   5179   1098    957   1781       C  
ATOM   5478  O   TYR B 140      18.159  19.821 -57.662  1.00 52.58           O  
ANISOU 5478  O   TYR B 140     7144   8436   4397   1011    964   1728       O  
ATOM   5479  CB  TYR B 140      18.792  20.701 -60.853  1.00 63.65           C  
ANISOU 5479  CB  TYR B 140     8497  10290   5396   1300   1092   2011       C  
ATOM   5480  CG  TYR B 140      19.787  21.508 -60.052  1.00 59.94           C  
ANISOU 5480  CG  TYR B 140     7963   9742   5069   1163   1176   2164       C  
ATOM   5481  CD1 TYR B 140      21.037  20.992 -59.737  1.00 59.76           C  
ANISOU 5481  CD1 TYR B 140     7886   9770   5049   1152   1237   2167       C  
ATOM   5482  CD2 TYR B 140      19.487  22.798 -59.634  1.00 49.63           C  
ANISOU 5482  CD2 TYR B 140     6648   8315   3895   1050   1191   2304       C  
ATOM   5483  CE1 TYR B 140      21.954  21.732 -59.014  1.00 49.13           C  
ANISOU 5483  CE1 TYR B 140     6477   8355   3835   1027   1309   2303       C  
ATOM   5484  CE2 TYR B 140      20.396  23.544 -58.912  1.00 52.94           C  
ANISOU 5484  CE2 TYR B 140     7006   8658   4449    924   1260   2438       C  
ATOM   5485  CZ  TYR B 140      21.628  23.007 -58.606  1.00 51.85           C  
ANISOU 5485  CZ  TYR B 140     6814   8574   4314    911   1318   2437       C  
ATOM   5486  OH  TYR B 140      22.537  23.747 -57.886  1.00 56.32           O  
ANISOU 5486  OH  TYR B 140     7315   9067   5019    785   1382   2566       O  
ATOM   5487  N   GLU B 141      16.632  21.153 -58.640  1.00 56.20           N  
ANISOU 5487  N   GLU B 141     7644   8903   4807   1052    924   1837       N  
ATOM   5488  CA  GLU B 141      16.260  21.764 -57.369  1.00 56.54           C  
ANISOU 5488  CA  GLU B 141     7691   8741   5050    897    901   1843       C  
ATOM   5489  C   GLU B 141      15.526  20.785 -56.460  1.00 54.94           C  
ANISOU 5489  C   GLU B 141     7532   8414   4928    855    809   1635       C  
ATOM   5490  O   GLU B 141      15.600  20.912 -55.233  1.00 50.79           O  
ANISOU 5490  O   GLU B 141     7001   7738   4560    731    802   1612       O  
ATOM   5491  CB  GLU B 141      15.407  23.010 -57.613  1.00 49.82           C  
ANISOU 5491  CB  GLU B 141     6855   7837   4238    871    889   1956       C  
ATOM   5492  CG  GLU B 141      16.065  24.063 -58.499  1.00 59.94           C  
ANISOU 5492  CG  GLU B 141     8094   9229   5453    904    978   2179       C  
ATOM   5493  CD  GLU B 141      17.113  24.891 -57.775  1.00 62.57           C  
ANISOU 5493  CD  GLU B 141     8368   9486   5921    780   1057   2327       C  
ATOM   5494  OE1 GLU B 141      17.664  25.823 -58.398  1.00 62.66           O  
ANISOU 5494  OE1 GLU B 141     8338   9567   5904    787   1132   2522       O  
ATOM   5495  OE2 GLU B 141      17.389  24.618 -56.588  1.00 58.56           O  
ANISOU 5495  OE2 GLU B 141     7852   8850   5549    674   1044   2251       O  
ATOM   5496  N   ILE B 142      14.822  19.809 -57.033  1.00 53.05           N  
ANISOU 5496  N   ILE B 142     7337   8236   4585    958    737   1486       N  
ATOM   5497  CA  ILE B 142      14.107  18.830 -56.220  1.00 47.85           C  
ANISOU 5497  CA  ILE B 142     6716   7461   4002    919    649   1294       C  
ATOM   5498  C   ILE B 142      15.070  17.795 -55.651  1.00 53.70           C  
ANISOU 5498  C   ILE B 142     7443   8200   4762    906    667   1211       C  
ATOM   5499  O   ILE B 142      15.028  17.474 -54.458  1.00 52.69           O  
ANISOU 5499  O   ILE B 142     7319   7931   4769    803    643   1140       O  
ATOM   5500  CB  ILE B 142      12.990  18.160 -57.042  1.00 49.02           C  
ANISOU 5500  CB  ILE B 142     6913   7668   4044   1029    557   1161       C  
ATOM   5501  CG1 ILE B 142      11.824  19.126 -57.256  1.00 54.56           C  
ANISOU 5501  CG1 ILE B 142     7634   8324   4771   1014    519   1214       C  
ATOM   5502  CG2 ILE B 142      12.506  16.896 -56.350  1.00 49.50           C  
ANISOU 5502  CG2 ILE B 142     7007   7638   4163   1006    473    960       C  
ATOM   5503  CD1 ILE B 142      11.105  19.505 -55.985  1.00 65.71           C  
ANISOU 5503  CD1 ILE B 142     9056   9545   6367    876    481   1182       C  
ATOM   5504  N   ALA B 143      15.954  17.263 -56.498  1.00 44.87           N  
ANISOU 5504  N   ALA B 143     6305   7240   3503   1015    710   1221       N  
ATOM   5505  CA  ALA B 143      16.812  16.157 -56.083  1.00 43.16           C  
ANISOU 5505  CA  ALA B 143     6078   7033   3286   1027    718   1125       C  
ATOM   5506  C   ALA B 143      17.812  16.586 -55.017  1.00 47.25           C  
ANISOU 5506  C   ALA B 143     6548   7470   3934    904    787   1214       C  
ATOM   5507  O   ALA B 143      18.082  15.832 -54.074  1.00 50.00           O  
ANISOU 5507  O   ALA B 143     6902   7730   4367    849    765   1116       O  
ATOM   5508  CB  ALA B 143      17.537  15.576 -57.295  1.00 56.46           C  
ANISOU 5508  CB  ALA B 143     7750   8920   4783   1183    752   1122       C  
ATOM   5509  N   ARG B 144      18.376  17.789 -55.145  1.00 47.07           N  
ANISOU 5509  N   ARG B 144     6478   7475   3931    860    868   1400       N  
ATOM   5510  CA  ARG B 144      19.382  18.231 -54.188  1.00 50.39           C  
ANISOU 5510  CA  ARG B 144     6846   7826   4474    745    932   1487       C  
ATOM   5511  C   ARG B 144      18.773  18.655 -52.858  1.00 48.82           C  
ANISOU 5511  C   ARG B 144     6664   7426   4458    601    889   1458       C  
ATOM   5512  O   ARG B 144      19.504  18.783 -51.871  1.00 44.78           O  
ANISOU 5512  O   ARG B 144     6118   6837   4058    504    920   1483       O  
ATOM   5513  CB  ARG B 144      20.210  19.373 -54.778  1.00 47.24           C  
ANISOU 5513  CB  ARG B 144     6385   7520   4043    742   1030   1699       C  
ATOM   5514  CG  ARG B 144      19.496  20.710 -54.846  1.00 44.42           C  
ANISOU 5514  CG  ARG B 144     6035   7094   3751    682   1030   1822       C  
ATOM   5515  CD  ARG B 144      20.148  21.604 -55.888  1.00 45.08           C  
ANISOU 5515  CD  ARG B 144     6068   7316   3744    731   1118   2021       C  
ATOM   5516  NE  ARG B 144      19.783  23.008 -55.723  1.00 60.71           N  
ANISOU 5516  NE  ARG B 144     8039   9204   5825    645   1132   2167       N  
ATOM   5517  CZ  ARG B 144      20.600  23.939 -55.242  1.00 63.79           C  
ANISOU 5517  CZ  ARG B 144     8371   9540   6327    541   1197   2316       C  
ATOM   5518  NH1 ARG B 144      20.185  25.192 -55.125  1.00 65.67           N  
ANISOU 5518  NH1 ARG B 144     8608   9684   6658    469   1199   2439       N  
ATOM   5519  NH2 ARG B 144      21.832  23.616 -54.875  1.00 64.84           N  
ANISOU 5519  NH2 ARG B 144     8445   9709   6481    510   1255   2340       N  
ATOM   5520  N   ARG B 145      17.459  18.877 -52.810  1.00 45.09           N  
ANISOU 5520  N   ARG B 145     6240   6874   4017    588    819   1404       N  
ATOM   5521  CA  ARG B 145      16.763  19.141 -51.560  1.00 43.72           C  
ANISOU 5521  CA  ARG B 145     6087   6520   4006    466    771   1353       C  
ATOM   5522  C   ARG B 145      16.146  17.887 -50.955  1.00 49.46           C  
ANISOU 5522  C   ARG B 145     6856   7176   4758    466    691   1162       C  
ATOM   5523  O   ARG B 145      15.738  17.914 -49.789  1.00 50.52           O  
ANISOU 5523  O   ARG B 145     7001   7170   5025    365    658   1112       O  
ATOM   5524  CB  ARG B 145      15.677  20.202 -51.771  1.00 45.35           C  
ANISOU 5524  CB  ARG B 145     6315   6673   4244    445    742   1414       C  
ATOM   5525  CG  ARG B 145      16.210  21.626 -51.745  1.00 48.33           C  
ANISOU 5525  CG  ARG B 145     6650   7031   4683    381    811   1602       C  
ATOM   5526  CD  ARG B 145      15.100  22.643 -51.939  1.00 39.95           C  
ANISOU 5526  CD  ARG B 145     5614   5908   3656    366    776   1655       C  
ATOM   5527  NE  ARG B 145      15.111  23.219 -53.279  1.00 77.77           N  
ANISOU 5527  NE  ARG B 145    10398  10829   8322    460    811   1777       N  
ATOM   5528  CZ  ARG B 145      15.863  24.253 -53.639  1.00 70.95           C  
ANISOU 5528  CZ  ARG B 145     9492  10002   7466    440    886   1961       C  
ATOM   5529  NH1 ARG B 145      16.671  24.829 -52.759  1.00 78.22           N  
ANISOU 5529  NH1 ARG B 145    10370  10833   8517    327    930   2037       N  
ATOM   5530  NH2 ARG B 145      15.806  24.714 -54.878  1.00 68.87           N  
ANISOU 5530  NH2 ARG B 145     9225   9864   7080    532    915   2071       N  
ATOM   5531  N   HIS B 146      16.073  16.798 -51.717  1.00 45.06           N  
ANISOU 5531  N   HIS B 146     6324   6716   4081    578    658   1058       N  
ATOM   5532  CA  HIS B 146      15.598  15.507 -51.222  1.00 38.24           C  
ANISOU 5532  CA  HIS B 146     5499   5790   3241    584    583    880       C  
ATOM   5533  C   HIS B 146      16.530  14.435 -51.763  1.00 38.89           C  
ANISOU 5533  C   HIS B 146     5574   5986   3216    683    600    822       C  
ATOM   5534  O   HIS B 146      16.216  13.748 -52.743  1.00 45.20           O  
ANISOU 5534  O   HIS B 146     6401   6881   3893    801    560    742       O  
ATOM   5535  CB  HIS B 146      14.147  15.253 -51.639  1.00 40.51           C  
ANISOU 5535  CB  HIS B 146     5834   6055   3502    623    493    781       C  
ATOM   5536  CG  HIS B 146      13.189  16.296 -51.153  1.00 44.66           C  
ANISOU 5536  CG  HIS B 146     6365   6478   4127    538    474    833       C  
ATOM   5537  ND1 HIS B 146      12.578  16.229 -49.919  1.00 51.58           N  
ANISOU 5537  ND1 HIS B 146     7251   7203   5144    431    434    772       N  
ATOM   5538  CD2 HIS B 146      12.738  17.433 -51.734  1.00 44.95           C  
ANISOU 5538  CD2 HIS B 146     6396   6542   4139    550    489    942       C  
ATOM   5539  CE1 HIS B 146      11.791  17.278 -49.762  1.00 45.31           C  
ANISOU 5539  CE1 HIS B 146     6459   6351   4407    383    425    834       C  
ATOM   5540  NE2 HIS B 146      11.871  18.025 -50.848  1.00 50.40           N  
ANISOU 5540  NE2 HIS B 146     7095   7097   4957    452    456    937       N  
ATOM   5541  N   PRO B 147      17.699  14.258 -51.137  1.00 38.64           N  
ANISOU 5541  N   PRO B 147     5505   5948   3227    642    656    855       N  
ATOM   5542  CA  PRO B 147      18.723  13.369 -51.714  1.00 40.99           C  
ANISOU 5542  CA  PRO B 147     5788   6371   3415    744    685    820       C  
ATOM   5543  C   PRO B 147      18.327  11.903 -51.764  1.00 45.36           C  
ANISOU 5543  C   PRO B 147     6390   6908   3935    813    603    634       C  
ATOM   5544  O   PRO B 147      19.066  11.108 -52.359  1.00 48.91           O  
ANISOU 5544  O   PRO B 147     6835   7467   4282    917    615    588       O  
ATOM   5545  CB  PRO B 147      19.933  13.582 -50.793  1.00 38.95           C  
ANISOU 5545  CB  PRO B 147     5478   6078   3244    661    754    894       C  
ATOM   5546  CG  PRO B 147      19.352  14.075 -49.508  1.00 43.67           C  
ANISOU 5546  CG  PRO B 147     6085   6501   4008    518    726    894       C  
ATOM   5547  CD  PRO B 147      18.144  14.882 -49.880  1.00 44.82           C  
ANISOU 5547  CD  PRO B 147     6257   6615   4158    505    692    923       C  
ATOM   5548  N   TYR B 148      17.199  11.517 -51.168  1.00 43.23           N  
ANISOU 5548  N   TYR B 148     6166   6509   3751    759    519    527       N  
ATOM   5549  CA  TYR B 148      16.721  10.142 -51.214  1.00 38.51           C  
ANISOU 5549  CA  TYR B 148     5614   5880   3136    814    432    352       C  
ATOM   5550  C   TYR B 148      15.401  10.016 -51.965  1.00 38.90           C  
ANISOU 5550  C   TYR B 148     5706   5938   3135    869    350    274       C  
ATOM   5551  O   TYR B 148      14.718   8.995 -51.840  1.00 40.23           O  
ANISOU 5551  O   TYR B 148     5914   6043   3327    885    262    127       O  
ATOM   5552  CB  TYR B 148      16.577   9.579 -49.800  1.00 45.18           C  
ANISOU 5552  CB  TYR B 148     6471   6562   4131    704    397    283       C  
ATOM   5553  CG  TYR B 148      17.875   9.499 -49.028  1.00 48.10           C  
ANISOU 5553  CG  TYR B 148     6803   6923   4548    660    464    335       C  
ATOM   5554  CD1 TYR B 148      18.688   8.376 -49.112  1.00 52.49           C  
ANISOU 5554  CD1 TYR B 148     7364   7520   5060    731    459    256       C  
ATOM   5555  CD2 TYR B 148      18.285  10.545 -48.212  1.00 47.13           C  
ANISOU 5555  CD2 TYR B 148     6640   6750   4518    549    527    458       C  
ATOM   5556  CE1 TYR B 148      19.874   8.298 -48.405  1.00 57.50           C  
ANISOU 5556  CE1 TYR B 148     7960   8150   5736    695    518    303       C  
ATOM   5557  CE2 TYR B 148      19.468  10.475 -47.500  1.00 36.39           C  
ANISOU 5557  CE2 TYR B 148     5240   5382   3202    509    582    502       C  
ATOM   5558  CZ  TYR B 148      20.259   9.350 -47.599  1.00 46.23           C  
ANISOU 5558  CZ  TYR B 148     6490   6677   4401    582    579    426       C  
ATOM   5559  OH  TYR B 148      21.439   9.279 -46.894  1.00 52.48           O  
ANISOU 5559  OH  TYR B 148     7239   7466   5235    545    632    469       O  
ATOM   5560  N   PHE B 149      15.025  11.036 -52.735  1.00 39.76           N  
ANISOU 5560  N   PHE B 149     5805   6121   3180    897    374    370       N  
ATOM   5561  CA  PHE B 149      13.791  10.978 -53.507  1.00 44.45           C  
ANISOU 5561  CA  PHE B 149     6435   6737   3717    957    296    301       C  
ATOM   5562  C   PHE B 149      13.810   9.785 -54.455  1.00 50.85           C  
ANISOU 5562  C   PHE B 149     7275   7642   4402   1098    237    163       C  
ATOM   5563  O   PHE B 149      14.818   9.506 -55.109  1.00 57.42           O  
ANISOU 5563  O   PHE B 149     8092   8603   5121   1195    285    183       O  
ATOM   5564  CB  PHE B 149      13.596  12.275 -54.295  1.00 41.79           C  
ANISOU 5564  CB  PHE B 149     6079   6488   3311    983    342    444       C  
ATOM   5565  CG  PHE B 149      12.168  12.539 -54.695  1.00 40.63           C  
ANISOU 5565  CG  PHE B 149     5963   6317   3159    996    265    398       C  
ATOM   5566  CD1 PHE B 149      11.562  11.794 -55.694  1.00 41.52           C  
ANISOU 5566  CD1 PHE B 149     6108   6511   3158   1116    188    280       C  
ATOM   5567  CD2 PHE B 149      11.436  13.539 -54.076  1.00 39.91           C  
ANISOU 5567  CD2 PHE B 149     5865   6124   3174    892    266    470       C  
ATOM   5568  CE1 PHE B 149      10.252  12.034 -56.063  1.00 41.67           C  
ANISOU 5568  CE1 PHE B 149     6149   6511   3172   1129    114    237       C  
ATOM   5569  CE2 PHE B 149      10.124  13.784 -54.441  1.00 40.04           C  
ANISOU 5569  CE2 PHE B 149     5905   6123   3186    908    194    429       C  
ATOM   5570  CZ  PHE B 149       9.532  13.031 -55.435  1.00 45.52           C  
ANISOU 5570  CZ  PHE B 149     6628   6901   3768   1024    119    313       C  
ATOM   5571  N   TYR B 150      12.686   9.069 -54.507  1.00 40.84           N  
ANISOU 5571  N   TYR B 150     6048   6310   3158   1109    131     20       N  
ATOM   5572  CA  TYR B 150      12.507   7.968 -55.445  1.00 53.05           C  
ANISOU 5572  CA  TYR B 150     7628   7935   4592   1244     55   -126       C  
ATOM   5573  C   TYR B 150      12.732   8.464 -56.868  1.00 45.39           C  
ANISOU 5573  C   TYR B 150     6650   7157   3438   1383     87    -66       C  
ATOM   5574  O   TYR B 150      11.887   9.170 -57.426  1.00 49.97           O  
ANISOU 5574  O   TYR B 150     7235   7771   3979   1401     65    -28       O  
ATOM   5575  CB  TYR B 150      11.110   7.361 -55.297  1.00 55.10           C  
ANISOU 5575  CB  TYR B 150     7925   8089   4920   1218    -67   -269       C  
ATOM   5576  CG  TYR B 150      11.003   5.918 -55.737  1.00 58.45           C  
ANISOU 5576  CG  TYR B 150     8387   8521   5302   1311   -160   -452       C  
ATOM   5577  CD1 TYR B 150      12.134   5.123 -55.872  1.00 49.13           C  
ANISOU 5577  CD1 TYR B 150     7209   7394   4065   1385   -135   -493       C  
ATOM   5578  CD2 TYR B 150       9.766   5.349 -56.012  1.00 61.78           C  
ANISOU 5578  CD2 TYR B 150     8839   8892   5744   1327   -278   -587       C  
ATOM   5579  CE1 TYR B 150      12.035   3.802 -56.272  1.00 54.79           C  
ANISOU 5579  CE1 TYR B 150     7962   8107   4747   1474   -227   -667       C  
ATOM   5580  CE2 TYR B 150       9.657   4.031 -56.411  1.00 61.77           C  
ANISOU 5580  CE2 TYR B 150     8872   8884   5713   1409   -372   -760       C  
ATOM   5581  CZ  TYR B 150      10.794   3.262 -56.540  1.00 61.75           C  
ANISOU 5581  CZ  TYR B 150     8877   8931   5656   1484   -348   -801       C  
ATOM   5582  OH  TYR B 150      10.688   1.949 -56.937  1.00 63.43           O  
ANISOU 5582  OH  TYR B 150     9127   9129   5844   1570   -447   -978       O  
ATOM   5583  N   ALA B 151      13.875   8.103 -57.452  1.00 44.08           N  
ANISOU 5583  N   ALA B 151     6470   7121   3157   1487    139    -53       N  
ATOM   5584  CA  ALA B 151      14.260   8.653 -58.750  1.00 55.22           C  
ANISOU 5584  CA  ALA B 151     7864   8731   4387   1618    190     31       C  
ATOM   5585  C   ALA B 151      13.243   8.382 -59.852  1.00 52.85           C  
ANISOU 5585  C   ALA B 151     7601   8509   3972   1735     98    -70       C  
ATOM   5586  O   ALA B 151      12.886   9.330 -60.573  1.00 60.52           O  
ANISOU 5586  O   ALA B 151     8562   9572   4862   1772    124     33       O  
ATOM   5587  CB  ALA B 151      15.647   8.130 -59.135  1.00 50.61           C  
ANISOU 5587  CB  ALA B 151     7256   8274   3698   1715    255     40       C  
ATOM   5588  N   PRO B 152      12.744   7.155 -60.054  1.00 47.07           N  
ANISOU 5588  N   PRO B 152     6911   7747   3227   1798    -12   -266       N  
ATOM   5589  CA  PRO B 152      11.814   6.952 -61.178  1.00 59.83           C  
ANISOU 5589  CA  PRO B 152     8557   9451   4724   1918   -102   -361       C  
ATOM   5590  C   PRO B 152      10.488   7.671 -61.005  1.00 58.98           C  
ANISOU 5590  C   PRO B 152     8458   9262   4692   1838   -152   -338       C  
ATOM   5591  O   PRO B 152       9.927   8.155 -61.996  1.00 52.53           O  
ANISOU 5591  O   PRO B 152     7645   8556   3757   1927   -174   -317       O  
ATOM   5592  CB  PRO B 152      11.639   5.426 -61.217  1.00 58.59           C  
ANISOU 5592  CB  PRO B 152     8442   9246   4575   1979   -214   -582       C  
ATOM   5593  CG  PRO B 152      12.813   4.883 -60.467  1.00 48.85           C  
ANISOU 5593  CG  PRO B 152     7195   7968   3399   1944   -155   -576       C  
ATOM   5594  CD  PRO B 152      13.061   5.879 -59.389  1.00 52.00           C  
ANISOU 5594  CD  PRO B 152     7557   8270   3931   1781    -63   -410       C  
ATOM   5595  N   GLU B 153       9.962   7.760 -59.780  1.00 57.40           N  
ANISOU 5595  N   GLU B 153     8256   8874   4680   1677   -171   -340       N  
ATOM   5596  CA  GLU B 153       8.729   8.519 -59.590  1.00 55.24           C  
ANISOU 5596  CA  GLU B 153     7983   8529   4478   1603   -210   -308       C  
ATOM   5597  C   GLU B 153       8.971  10.016 -59.726  1.00 48.15           C  
ANISOU 5597  C   GLU B 153     7053   7690   3553   1574   -108   -100       C  
ATOM   5598  O   GLU B 153       8.047  10.761 -60.071  1.00 55.80           O  
ANISOU 5598  O   GLU B 153     8023   8669   4510   1574   -135    -59       O  
ATOM   5599  CB  GLU B 153       8.095   8.205 -58.235  1.00 64.73           C  
ANISOU 5599  CB  GLU B 153     9188   9524   5882   1445   -254   -365       C  
ATOM   5600  CG  GLU B 153       6.596   8.484 -58.206  1.00 76.55           C  
ANISOU 5600  CG  GLU B 153    10693  10953   7440   1401   -340   -411       C  
ATOM   5601  CD  GLU B 153       5.984   8.308 -56.833  1.00 91.25           C  
ANISOU 5601  CD  GLU B 153    12549  12623   9499   1242   -369   -443       C  
ATOM   5602  OE1 GLU B 153       5.861   9.313 -56.101  1.00 95.95           O  
ANISOU 5602  OE1 GLU B 153    13120  13154  10181   1137   -310   -321       O  
ATOM   5603  OE2 GLU B 153       5.616   7.165 -56.488  1.00 97.60           O  
ANISOU 5603  OE2 GLU B 153    13371  13341  10370   1223   -452   -590       O  
ATOM   5604  N   LEU B 154      10.197  10.474 -59.461  1.00 45.24           N  
ANISOU 5604  N   LEU B 154     6653   7358   3178   1550      6     32       N  
ATOM   5605  CA  LEU B 154      10.535  11.866 -59.737  1.00 47.90           C  
ANISOU 5605  CA  LEU B 154     6957   7763   3478   1537    103    235       C  
ATOM   5606  C   LEU B 154      10.436  12.176 -61.225  1.00 55.52           C  
ANISOU 5606  C   LEU B 154     7927   8922   4246   1695    104    272       C  
ATOM   5607  O   LEU B 154      10.076  13.297 -61.604  1.00 51.93           O  
ANISOU 5607  O   LEU B 154     7461   8507   3764   1693    136    404       O  
ATOM   5608  CB  LEU B 154      11.940  12.180 -59.221  1.00 45.68           C  
ANISOU 5608  CB  LEU B 154     6637   7493   3226   1486    219    359       C  
ATOM   5609  CG  LEU B 154      12.388  13.635 -59.371  1.00 45.34           C  
ANISOU 5609  CG  LEU B 154     6554   7499   3173   1451    324    579       C  
ATOM   5610  CD1 LEU B 154      11.314  14.574 -58.846  1.00 47.89           C  
ANISOU 5610  CD1 LEU B 154     6884   7699   3613   1348    296    631       C  
ATOM   5611  CD2 LEU B 154      13.714  13.875 -58.668  1.00 44.88           C  
ANISOU 5611  CD2 LEU B 154     6453   7422   3178   1378    426    685       C  
ATOM   5612  N   LEU B 155      10.748  11.201 -62.081  1.00 55.37           N  
ANISOU 5612  N   LEU B 155     7926   9027   4087   1838     67    157       N  
ATOM   5613  CA  LEU B 155      10.591  11.406 -63.517  1.00 49.70           C  
ANISOU 5613  CA  LEU B 155     7214   8502   3168   2001     58    174       C  
ATOM   5614  C   LEU B 155       9.126  11.608 -63.880  1.00 54.23           C  
ANISOU 5614  C   LEU B 155     7816   9047   3742   2015    -44    108       C  
ATOM   5615  O   LEU B 155       8.799  12.423 -64.751  1.00 61.98           O  
ANISOU 5615  O   LEU B 155     8794  10144   4614   2088    -28    205       O  
ATOM   5616  CB  LEU B 155      11.177  10.220 -64.283  1.00 50.82           C  
ANISOU 5616  CB  LEU B 155     7371   8772   3166   2154     27     38       C  
ATOM   5617  CG  LEU B 155      12.690  10.031 -64.172  1.00 57.28           C  
ANISOU 5617  CG  LEU B 155     8155   9664   3944   2176    133    108       C  
ATOM   5618  CD1 LEU B 155      13.180   9.014 -65.190  1.00 60.20           C  
ANISOU 5618  CD1 LEU B 155     8541  10199   4133   2362    102    -17       C  
ATOM   5619  CD2 LEU B 155      13.411  11.359 -64.343  1.00 57.38           C  
ANISOU 5619  CD2 LEU B 155     8119   9763   3922   2150    268    352       C  
ATOM   5620  N   PHE B 156       8.228  10.879 -63.217  1.00 56.45           N  
ANISOU 5620  N   PHE B 156     8122   9178   4147   1945   -149    -50       N  
ATOM   5621  CA  PHE B 156       6.806  11.056 -63.482  1.00 58.73           C  
ANISOU 5621  CA  PHE B 156     8430   9433   4452   1948   -249   -116       C  
ATOM   5622  C   PHE B 156       6.296  12.383 -62.934  1.00 60.66           C  
ANISOU 5622  C   PHE B 156     8654   9595   4798   1833   -204     40       C  
ATOM   5623  O   PHE B 156       5.405  12.996 -63.534  1.00 51.40           O  
ANISOU 5623  O   PHE B 156     7487   8469   3575   1876   -243     67       O  
ATOM   5624  CB  PHE B 156       6.013   9.889 -62.896  1.00 65.21           C  
ANISOU 5624  CB  PHE B 156     9275  10114   5387   1898   -371   -322       C  
ATOM   5625  CG  PHE B 156       4.534  10.025 -63.071  1.00 75.02           C  
ANISOU 5625  CG  PHE B 156    10529  11312   6663   1888   -477   -396       C  
ATOM   5626  CD1 PHE B 156       3.984  10.096 -64.339  1.00 79.75           C  
ANISOU 5626  CD1 PHE B 156    11141  12057   7102   2032   -537   -436       C  
ATOM   5627  CD2 PHE B 156       3.691  10.080 -61.975  1.00 75.03           C  
ANISOU 5627  CD2 PHE B 156    10523  11133   6852   1739   -517   -424       C  
ATOM   5628  CE1 PHE B 156       2.623  10.222 -64.511  1.00 80.70           C  
ANISOU 5628  CE1 PHE B 156    11267  12143   7254   2025   -638   -505       C  
ATOM   5629  CE2 PHE B 156       2.327  10.202 -62.142  1.00 82.25           C  
ANISOU 5629  CE2 PHE B 156    11440  12014   7798   1731   -614   -491       C  
ATOM   5630  CZ  PHE B 156       1.792  10.275 -63.411  1.00 83.22           C  
ANISOU 5630  CZ  PHE B 156    11576  12280   7765   1873   -676   -532       C  
ATOM   5631  N   PHE B 157       6.842  12.843 -61.805  1.00 58.39           N  
ANISOU 5631  N   PHE B 157     8344   9188   4653   1693   -126    139       N  
ATOM   5632  CA  PHE B 157       6.496  14.171 -61.309  1.00 58.14           C  
ANISOU 5632  CA  PHE B 157     8292   9084   4713   1593    -75    295       C  
ATOM   5633  C   PHE B 157       6.862  15.243 -62.327  1.00 48.86           C  
ANISOU 5633  C   PHE B 157     7104   8062   3399   1681     -2    469       C  
ATOM   5634  O   PHE B 157       6.106  16.200 -62.535  1.00 52.42           O  
ANISOU 5634  O   PHE B 157     7554   8506   3858   1672    -11    552       O  
ATOM   5635  CB  PHE B 157       7.198  14.439 -59.978  1.00 53.40           C  
ANISOU 5635  CB  PHE B 157     7669   8345   4274   1441     -1    369       C  
ATOM   5636  CG  PHE B 157       6.415  13.993 -58.776  1.00 43.83           C  
ANISOU 5636  CG  PHE B 157     6465   6949   3238   1315    -67    260       C  
ATOM   5637  CD1 PHE B 157       5.395  14.779 -58.265  1.00 56.73           C  
ANISOU 5637  CD1 PHE B 157     8095   8483   4975   1231    -93    296       C  
ATOM   5638  CD2 PHE B 157       6.704  12.792 -58.152  1.00 43.28           C  
ANISOU 5638  CD2 PHE B 157     6406   6809   3231   1283   -100    128       C  
ATOM   5639  CE1 PHE B 157       4.675  14.370 -57.154  1.00 59.52           C  
ANISOU 5639  CE1 PHE B 157     8450   8679   5485   1118   -148    202       C  
ATOM   5640  CE2 PHE B 157       5.990  12.377 -57.043  1.00 46.09           C  
ANISOU 5640  CE2 PHE B 157     6765   7000   3745   1166   -156     39       C  
ATOM   5641  CZ  PHE B 157       4.974  13.167 -56.544  1.00 53.25           C  
ANISOU 5641  CZ  PHE B 157     7664   7819   4749   1084   -178     77       C  
ATOM   5642  N   ALA B 158       8.021  15.095 -62.973  1.00 49.04           N  
ANISOU 5642  N   ALA B 158     7112   8226   3292   1770     72    529       N  
ATOM   5643  CA  ALA B 158       8.399  16.017 -64.038  1.00 58.79           C  
ANISOU 5643  CA  ALA B 158     8332   9627   4379   1867    143    696       C  
ATOM   5644  C   ALA B 158       7.429  15.942 -65.208  1.00 62.05           C  
ANISOU 5644  C   ALA B 158     8772  10159   4646   2006     59    630       C  
ATOM   5645  O   ALA B 158       7.163  16.958 -65.861  1.00 60.79           O  
ANISOU 5645  O   ALA B 158     8606  10076   4414   2050     89    769       O  
ATOM   5646  CB  ALA B 158       9.825  15.721 -64.506  1.00 57.32           C  
ANISOU 5646  CB  ALA B 158     8120   9582   4076   1944    235    756       C  
ATOM   5647  N   LYS B 159       6.887  14.754 -65.487  1.00 63.84           N  
ANISOU 5647  N   LYS B 159     9029  10399   4830   2076    -50    421       N  
ATOM   5648  CA  LYS B 159       5.907  14.623 -66.560  1.00 67.62           C  
ANISOU 5648  CA  LYS B 159     9532  10985   5176   2206   -144    339       C  
ATOM   5649  C   LYS B 159       4.602  15.323 -66.201  1.00 69.50           C  
ANISOU 5649  C   LYS B 159     9776  11111   5521   2128   -205    351       C  
ATOM   5650  O   LYS B 159       3.986  15.973 -67.053  1.00 70.16           O  
ANISOU 5650  O   LYS B 159     9864  11291   5503   2212   -226    409       O  
ATOM   5651  CB  LYS B 159       5.664  13.147 -66.873  1.00 71.24           C  
ANISOU 5651  CB  LYS B 159    10019  11468   5582   2291   -254    101       C  
ATOM   5652  CG  LYS B 159       4.657  12.907 -67.984  1.00 81.40           C  
ANISOU 5652  CG  LYS B 159    11330  12865   6732   2430   -364     -8       C  
ATOM   5653  CD  LYS B 159       4.616  11.442 -68.385  1.00 85.51           C  
ANISOU 5653  CD  LYS B 159    11878  13425   7188   2528   -467   -238       C  
ATOM   5654  CE  LYS B 159       3.571  11.197 -69.460  1.00 91.34           C  
ANISOU 5654  CE  LYS B 159    12639  14268   7798   2663   -588   -358       C  
ATOM   5655  NZ  LYS B 159       3.467   9.756 -69.815  1.00 95.54           N  
ANISOU 5655  NZ  LYS B 159    13198  14819   8283   2753   -703   -597       N  
ATOM   5656  N   ARG B 160       4.162  15.199 -64.945  1.00 65.98           N  
ANISOU 5656  N   ARG B 160     9326  10466   5275   1973   -232    298       N  
ATOM   5657  CA  ARG B 160       3.001  15.959 -64.494  1.00 63.49           C  
ANISOU 5657  CA  ARG B 160     9009  10042   5072   1891   -275    326       C  
ATOM   5658  C   ARG B 160       3.311  17.448 -64.448  1.00 57.62           C  
ANISOU 5658  C   ARG B 160     8247   9303   4345   1850   -174    556       C  
ATOM   5659  O   ARG B 160       2.456  18.279 -64.780  1.00 59.44           O  
ANISOU 5659  O   ARG B 160     8480   9541   4565   1868   -201    618       O  
ATOM   5660  CB  ARG B 160       2.547  15.475 -63.117  1.00 69.75           C  
ANISOU 5660  CB  ARG B 160     9799  10632   6072   1736   -318    224       C  
ATOM   5661  CG  ARG B 160       2.288  13.987 -63.018  1.00 75.17           C  
ANISOU 5661  CG  ARG B 160    10502  11286   6772   1754   -415      6       C  
ATOM   5662  CD  ARG B 160       2.290  13.549 -61.565  1.00 74.17           C  
ANISOU 5662  CD  ARG B 160    10368  10969   6845   1594   -416    -47       C  
ATOM   5663  NE  ARG B 160       1.015  13.824 -60.909  1.00 84.69           N  
ANISOU 5663  NE  ARG B 160    11691  12176   8309   1501   -482    -86       N  
ATOM   5664  CZ  ARG B 160       0.799  13.681 -59.605  1.00 79.88           C  
ANISOU 5664  CZ  ARG B 160    11069  11402   7878   1356   -481   -111       C  
ATOM   5665  NH1 ARG B 160       1.776  13.263 -58.811  1.00 79.27           N  
ANISOU 5665  NH1 ARG B 160    10990  11261   7869   1287   -421   -101       N  
ATOM   5666  NH2 ARG B 160      -0.393  13.956 -59.094  1.00 78.22           N  
ANISOU 5666  NH2 ARG B 160    10847  11098   7774   1285   -540   -143       N  
ATOM   5667  N   TYR B 161       4.524  17.802 -64.017  1.00 50.27           N  
ANISOU 5667  N   TYR B 161     7294   8359   3446   1793    -61    684       N  
ATOM   5668  CA  TYR B 161       4.966  19.191 -64.080  1.00 62.22           C  
ANISOU 5668  CA  TYR B 161     8787   9887   4967   1763     39    911       C  
ATOM   5669  C   TYR B 161       4.934  19.706 -65.514  1.00 63.51           C  
ANISOU 5669  C   TYR B 161     8954  10243   4933   1917     54   1009       C  
ATOM   5670  O   TYR B 161       4.621  20.878 -65.756  1.00 60.37           O  
ANISOU 5670  O   TYR B 161     8551   9848   4537   1913     83   1162       O  
ATOM   5671  CB  TYR B 161       6.372  19.308 -63.491  1.00 68.51           C  
ANISOU 5671  CB  TYR B 161     9554  10659   5816   1690    152   1015       C  
ATOM   5672  CG  TYR B 161       6.732  20.678 -62.963  1.00 71.50           C  
ANISOU 5672  CG  TYR B 161     9909  10959   6300   1586    240   1220       C  
ATOM   5673  CD1 TYR B 161       6.208  21.144 -61.765  1.00 69.79           C  
ANISOU 5673  CD1 TYR B 161     9690  10552   6275   1442    223   1217       C  
ATOM   5674  CD2 TYR B 161       7.612  21.499 -63.656  1.00 76.51           C  
ANISOU 5674  CD2 TYR B 161    10518  11710   6843   1634    340   1416       C  
ATOM   5675  CE1 TYR B 161       6.544  22.395 -61.277  1.00 74.71           C  
ANISOU 5675  CE1 TYR B 161    10292  11095   6998   1350    295   1395       C  
ATOM   5676  CE2 TYR B 161       7.953  22.748 -63.178  1.00 78.97           C  
ANISOU 5676  CE2 TYR B 161    10806  11938   7261   1536    415   1603       C  
ATOM   5677  CZ  TYR B 161       7.417  23.192 -61.989  1.00 83.56           C  
ANISOU 5677  CZ  TYR B 161    11391  12324   8036   1396    389   1587       C  
ATOM   5678  OH  TYR B 161       7.757  24.437 -61.513  1.00 92.35           O  
ANISOU 5678  OH  TYR B 161    12481  13347   9259   1301    455   1763       O  
ATOM   5679  N   LYS B 162       5.245  18.839 -66.479  1.00 52.36           N  
ANISOU 5679  N   LYS B 162     7553   8994   3347   2060     31    921       N  
ATOM   5680  CA  LYS B 162       5.198  19.227 -67.885  1.00 58.01           C  
ANISOU 5680  CA  LYS B 162     8273   9911   3856   2223     40   1000       C  
ATOM   5681  C   LYS B 162       3.765  19.311 -68.394  1.00 69.48           C  
ANISOU 5681  C   LYS B 162     9752  11376   5272   2285    -76    914       C  
ATOM   5682  O   LYS B 162       3.425  20.228 -69.149  1.00 66.52           O  
ANISOU 5682  O   LYS B 162     9378  11089   4807   2355    -61   1044       O  
ATOM   5683  CB  LYS B 162       6.006  18.236 -68.726  1.00 55.62           C  
ANISOU 5683  CB  LYS B 162     7972   9785   3375   2364     50    921       C  
ATOM   5684  CG  LYS B 162       5.828  18.390 -70.230  1.00 67.60           C  
ANISOU 5684  CG  LYS B 162     9500  11528   4658   2555     36    956       C  
ATOM   5685  CD  LYS B 162       7.150  18.219 -70.961  1.00 75.09           C  
ANISOU 5685  CD  LYS B 162    10426  12665   5441   2662    137   1042       C  
ATOM   5686  CE  LYS B 162       7.689  16.806 -70.803  1.00 82.44           C  
ANISOU 5686  CE  LYS B 162    11365  13610   6350   2698    102    848       C  
ATOM   5687  NZ  LYS B 162       9.118  16.703 -71.210  1.00 88.67           N  
ANISOU 5687  NZ  LYS B 162    12112  14527   7051   2752    218    941       N  
ATOM   5688  N   ALA B 163       2.910  18.368 -67.987  1.00 79.12           N  
ANISOU 5688  N   ALA B 163    10991  12507   6562   2259   -192    701       N  
ATOM   5689  CA  ALA B 163       1.541  18.339 -68.493  1.00 88.56           C  
ANISOU 5689  CA  ALA B 163    12205  13722   7722   2322   -311    602       C  
ATOM   5690  C   ALA B 163       0.741  19.545 -68.014  1.00 91.94           C  
ANISOU 5690  C   ALA B 163    12626  14040   8269   2233   -307    720       C  
ATOM   5691  O   ALA B 163       0.004  20.156 -68.797  1.00 98.96           O  
ANISOU 5691  O   ALA B 163    13522  15009   9068   2319   -345    768       O  
ATOM   5692  CB  ALA B 163       0.855  17.039 -68.073  1.00 88.57           C  
ANISOU 5692  CB  ALA B 163    12221  13639   7795   2297   -433    352       C  
ATOM   5693  N   ALA B 164       0.870  19.901 -66.734  1.00 84.61           N  
ANISOU 5693  N   ALA B 164    11682  12928   7537   2066   -265    764       N  
ATOM   5694  CA  ALA B 164       0.118  21.033 -66.205  1.00 77.99           C  
ANISOU 5694  CA  ALA B 164    10837  11975   6821   1982   -264    865       C  
ATOM   5695  C   ALA B 164       0.593  22.354 -66.797  1.00 70.90           C  
ANISOU 5695  C   ALA B 164     9934  11154   5852   2023   -171   1103       C  
ATOM   5696  O   ALA B 164      -0.200  23.293 -66.927  1.00 68.87           O  
ANISOU 5696  O   ALA B 164     9679  10870   5619   2026   -193   1184       O  
ATOM   5697  CB  ALA B 164       0.220  21.069 -64.681  1.00 74.38           C  
ANISOU 5697  CB  ALA B 164    10366  11311   6583   1801   -239    851       C  
ATOM   5698  N   PHE B 165       1.873  22.446 -67.161  1.00 67.92           N  
ANISOU 5698  N   PHE B 165     9545  10871   5391   2056    -68   1221       N  
ATOM   5699  CA  PHE B 165       2.396  23.679 -67.737  1.00 66.74           C  
ANISOU 5699  CA  PHE B 165     9384  10796   5178   2090     26   1460       C  
ATOM   5700  C   PHE B 165       1.982  23.855 -69.192  1.00 66.79           C  
ANISOU 5700  C   PHE B 165     9406  11001   4972   2269     -5   1497       C  
ATOM   5701  O   PHE B 165       1.760  24.986 -69.636  1.00 64.56           O  
ANISOU 5701  O   PHE B 165     9122  10745   4661   2297     26   1668       O  
ATOM   5702  CB  PHE B 165       3.920  23.710 -67.618  1.00 63.33           C  
ANISOU 5702  CB  PHE B 165     8926  10404   4732   2060    150   1580       C  
ATOM   5703  CG  PHE B 165       4.422  24.524 -66.459  1.00 63.75           C  
ANISOU 5703  CG  PHE B 165     8957  10283   4982   1893    225   1703       C  
ATOM   5704  CD1 PHE B 165       4.678  25.877 -66.604  1.00 68.01           C  
ANISOU 5704  CD1 PHE B 165     9483  10809   5549   1867    298   1930       C  
ATOM   5705  CD2 PHE B 165       4.639  23.935 -65.225  1.00 61.61           C  
ANISOU 5705  CD2 PHE B 165     8680   9861   4870   1763    217   1593       C  
ATOM   5706  CE1 PHE B 165       5.139  26.628 -65.540  1.00 63.32           C  
ANISOU 5706  CE1 PHE B 165     8869  10050   5139   1714    358   2034       C  
ATOM   5707  CE2 PHE B 165       5.101  24.680 -64.157  1.00 54.30           C  
ANISOU 5707  CE2 PHE B 165     7733   8779   4118   1615    280   1698       C  
ATOM   5708  CZ  PHE B 165       5.351  26.027 -64.315  1.00 58.56           C  
ANISOU 5708  CZ  PHE B 165     8259   9304   4687   1591    348   1914       C  
ATOM   5709  N   THR B 166       1.871  22.761 -69.948  1.00 72.29           N  
ANISOU 5709  N   THR B 166    10116  11834   5518   2394    -69   1337       N  
ATOM   5710  CA  THR B 166       1.512  22.881 -71.357  1.00 79.38           C  
ANISOU 5710  CA  THR B 166    11028  12935   6199   2575   -102   1363       C  
ATOM   5711  C   THR B 166       0.038  23.215 -71.541  1.00 83.12           C  
ANISOU 5711  C   THR B 166    11519  13373   6689   2602   -213   1302       C  
ATOM   5712  O   THR B 166      -0.334  23.835 -72.544  1.00 84.23           O  
ANISOU 5712  O   THR B 166    11668  13645   6690   2723   -222   1397       O  
ATOM   5713  CB  THR B 166       1.853  21.591 -72.103  1.00 82.75           C  
ANISOU 5713  CB  THR B 166    11464  13519   6457   2708   -143   1198       C  
ATOM   5714  OG1 THR B 166       1.256  20.476 -71.431  1.00 87.57           O  
ANISOU 5714  OG1 THR B 166    12087  14015   7171   2650   -250    956       O  
ATOM   5715  CG2 THR B 166       3.360  21.396 -72.168  1.00 73.37           C  
ANISOU 5715  CG2 THR B 166    10255  12412   5212   2716    -23   1289       C  
ATOM   5716  N   GLU B 167      -0.813  22.820 -70.596  1.00 76.13           N  
ANISOU 5716  N   GLU B 167    10636  12319   5970   2495   -298   1149       N  
ATOM   5717  CA  GLU B 167      -2.245  23.061 -70.731  1.00 84.00           C  
ANISOU 5717  CA  GLU B 167    11642  13284   6990   2519   -408   1077       C  
ATOM   5718  C   GLU B 167      -2.671  24.414 -70.172  1.00 79.07           C  
ANISOU 5718  C   GLU B 167    11011  12533   6499   2427   -374   1240       C  
ATOM   5719  O   GLU B 167      -3.561  25.063 -70.735  1.00 82.68           O  
ANISOU 5719  O   GLU B 167    11476  13033   6906   2498   -424   1283       O  
ATOM   5720  CB  GLU B 167      -3.037  21.949 -70.039  1.00 85.11           C  
ANISOU 5720  CB  GLU B 167    11783  13315   7241   2455   -522    830       C  
ATOM   5721  CG  GLU B 167      -4.546  22.098 -70.177  1.00 87.63           C  
ANISOU 5721  CG  GLU B 167    12102  13607   7585   2479   -644    738       C  
ATOM   5722  CD  GLU B 167      -5.311  20.910 -69.632  1.00 84.62           C  
ANISOU 5722  CD  GLU B 167    11715  13139   7298   2427   -760    493       C  
ATOM   5723  OE1 GLU B 167      -5.050  20.507 -68.479  1.00 76.68           O  
ANISOU 5723  OE1 GLU B 167    10699  11979   6457   2285   -737    442       O  
ATOM   5724  OE2 GLU B 167      -6.178  20.382 -70.359  1.00 85.06           O  
ANISOU 5724  OE2 GLU B 167    11775  13281   7262   2528   -875    355       O  
ATOM   5725  N   CYS B 168      -2.056  24.857 -69.078  1.00 74.04           N  
ANISOU 5725  N   CYS B 168    10361  11741   6032   2277   -292   1328       N  
ATOM   5726  CA  CYS B 168      -2.507  26.075 -68.419  1.00 75.94           C  
ANISOU 5726  CA  CYS B 168    10595  11839   6419   2182   -271   1456       C  
ATOM   5727  C   CYS B 168      -1.832  27.330 -68.956  1.00 77.74           C  
ANISOU 5727  C   CYS B 168    10823  12123   6593   2215   -169   1715       C  
ATOM   5728  O   CYS B 168      -2.439  28.406 -68.919  1.00 84.73           O  
ANISOU 5728  O   CYS B 168    11713  12947   7534   2203   -176   1827       O  
ATOM   5729  CB  CYS B 168      -2.279  25.977 -66.910  1.00 72.80           C  
ANISOU 5729  CB  CYS B 168    10183  11236   6241   2001   -245   1414       C  
ATOM   5730  SG  CYS B 168      -3.337  24.762 -66.075  1.00 83.94           S  
ANISOU 5730  SG  CYS B 168    11590  12539   7763   1935   -369   1138       S  
ATOM   5731  N   CYS B 169      -0.596  27.226 -69.460  1.00 75.63           N  
ANISOU 5731  N   CYS B 169    10548  11970   6220   2257    -74   1818       N  
ATOM   5732  CA  CYS B 169       0.094  28.399 -69.986  1.00 82.15           C  
ANISOU 5732  CA  CYS B 169    11366  12852   6996   2283     28   2077       C  
ATOM   5733  C   CYS B 169      -0.454  28.844 -71.336  1.00 88.26           C  
ANISOU 5733  C   CYS B 169    12156  13799   7580   2451     -2   2157       C  
ATOM   5734  O   CYS B 169      -0.023  29.887 -71.839  1.00 96.59           O  
ANISOU 5734  O   CYS B 169    13207  14901   8592   2480     76   2383       O  
ATOM   5735  CB  CYS B 169       1.599  28.135 -70.102  1.00 81.30           C  
ANISOU 5735  CB  CYS B 169    11236  12822   6833   2275    143   2166       C  
ATOM   5736  SG  CYS B 169       2.437  27.807 -68.511  1.00 80.44           S  
ANISOU 5736  SG  CYS B 169    11103  12513   6949   2075    197   2118       S  
ATOM   5737  N   GLN B 170      -1.360  28.072 -71.945  1.00 84.63           N  
ANISOU 5737  N   GLN B 170    11713  13436   7006   2562   -113   1980       N  
ATOM   5738  CA  GLN B 170      -2.100  28.500 -73.125  1.00 89.64           C  
ANISOU 5738  CA  GLN B 170    12363  14216   7479   2716   -163   2029       C  
ATOM   5739  C   GLN B 170      -3.558  28.799 -72.802  1.00 88.62           C  
ANISOU 5739  C   GLN B 170    12247  13985   7440   2700   -277   1941       C  
ATOM   5740  O   GLN B 170      -4.404  28.780 -73.700  1.00 91.49           O  
ANISOU 5740  O   GLN B 170    12623  14468   7670   2833   -358   1899       O  
ATOM   5741  CB  GLN B 170      -2.002  27.446 -74.229  1.00 86.99           C  
ANISOU 5741  CB  GLN B 170    12017  14058   6977   2846   -201   1874       C  
ATOM   5742  CG  GLN B 170      -2.531  26.070 -73.846  1.00 92.35           C  
ANISOU 5742  CG  GLN B 170    12717  14741   7629   2866   -316   1614       C  
ATOM   5743  CD  GLN B 170      -2.312  25.035 -74.936  1.00 98.53           C  
ANISOU 5743  CD  GLN B 170    13488  15688   8262   2991   -347   1464       C  
ATOM   5744  OE1 GLN B 170      -1.840  25.358 -76.026  1.00105.61           O  
ANISOU 5744  OE1 GLN B 170    14359  16707   9062   3075   -285   1554       O  
ATOM   5745  NE2 GLN B 170      -2.652  23.783 -74.645  1.00 99.89           N  
ANISOU 5745  NE2 GLN B 170    13676  15858   8420   3005   -445   1233       N  
ATOM   5746  N   ALA B 171      -3.865  29.076 -71.539  1.00 84.97           N  
ANISOU 5746  N   ALA B 171    11776  13308   7202   2541   -284   1911       N  
ATOM   5747  CA  ALA B 171      -5.219  29.367 -71.098  1.00 86.53           C  
ANISOU 5747  CA  ALA B 171    11976  13394   7506   2510   -384   1826       C  
ATOM   5748  C   ALA B 171      -5.393  30.864 -70.870  1.00 94.01           C  
ANISOU 5748  C   ALA B 171    12927  14241   8550   2468   -340   2033       C  
ATOM   5749  O   ALA B 171      -4.436  31.642 -70.887  1.00 96.16           O  
ANISOU 5749  O   ALA B 171    13198  14500   8837   2436   -232   2236       O  
ATOM   5750  CB  ALA B 171      -5.546  28.590 -69.819  1.00 90.52           C  
ANISOU 5750  CB  ALA B 171    12467  13733   8192   2370   -430   1634       C  
ATOM   5751  N   ALA B 172      -6.646  31.264 -70.654  1.00100.89           N  
ANISOU 5751  N   ALA B 172    13802  15040   9492   2469   -429   1979       N  
ATOM   5752  CA  ALA B 172      -6.949  32.665 -70.385  1.00102.78           C  
ANISOU 5752  CA  ALA B 172    14048  15168   9835   2433   -403   2154       C  
ATOM   5753  C   ALA B 172      -6.578  33.038 -68.954  1.00101.49           C  
ANISOU 5753  C   ALA B 172    13872  14785   9903   2252   -352   2174       C  
ATOM   5754  O   ALA B 172      -5.819  33.986 -68.723  1.00101.92           O  
ANISOU 5754  O   ALA B 172    13930  14767  10028   2194   -262   2366       O  
ATOM   5755  CB  ALA B 172      -8.430  32.940 -70.657  1.00106.62           C  
ANISOU 5755  CB  ALA B 172    14538  15659  10312   2505   -519   2081       C  
ATOM   5756  N   ASP B 173      -7.106  32.298 -67.980  1.00103.32           N  
ANISOU 5756  N   ASP B 173    14090  14910  10257   2161   -411   1978       N  
ATOM   5757  CA  ASP B 173      -6.776  32.498 -66.569  1.00107.16           C  
ANISOU 5757  CA  ASP B 173    14563  15199  10953   1993   -369   1969       C  
ATOM   5758  C   ASP B 173      -5.749  31.435 -66.193  1.00105.76           C  
ANISOU 5758  C   ASP B 173    14375  15036  10774   1930   -319   1887       C  
ATOM   5759  O   ASP B 173      -6.090  30.358 -65.700  1.00106.08           O  
ANISOU 5759  O   ASP B 173    14405  15055  10848   1892   -375   1691       O  
ATOM   5760  CB  ASP B 173      -8.024  32.425 -65.697  1.00108.53           C  
ANISOU 5760  CB  ASP B 173    14724  15249  11265   1935   -460   1820       C  
ATOM   5761  CG  ASP B 173      -7.745  32.776 -64.249  1.00109.80           C  
ANISOU 5761  CG  ASP B 173    14873  15210  11637   1773   -418   1823       C  
ATOM   5762  OD1 ASP B 173      -6.756  33.491 -63.988  1.00109.76           O  
ANISOU 5762  OD1 ASP B 173    14874  15143  11688   1715   -326   1982       O  
ATOM   5763  OD2 ASP B 173      -8.526  32.349 -63.373  1.00110.66           O  
ANISOU 5763  OD2 ASP B 173    14963  15227  11855   1706   -479   1670       O  
ATOM   5764  N   LYS B 174      -4.474  31.748 -66.436  1.00101.98           N  
ANISOU 5764  N   LYS B 174    13897  14594  10257   1921   -213   2044       N  
ATOM   5765  CA  LYS B 174      -3.406  30.794 -66.169  1.00 96.81           C  
ANISOU 5765  CA  LYS B 174    13230  13966   9586   1874   -159   1983       C  
ATOM   5766  C   LYS B 174      -3.217  30.575 -64.674  1.00 89.09           C  
ANISOU 5766  C   LYS B 174    12238  12802   8810   1709   -145   1901       C  
ATOM   5767  O   LYS B 174      -2.785  29.495 -64.258  1.00 86.59           O  
ANISOU 5767  O   LYS B 174    11913  12487   8503   1667   -144   1771       O  
ATOM   5768  CB  LYS B 174      -2.102  31.292 -66.790  1.00 94.66           C  
ANISOU 5768  CB  LYS B 174    12955  13781   9229   1903    -44   2188       C  
ATOM   5769  CG  LYS B 174      -2.087  31.363 -68.310  1.00 99.10           C  
ANISOU 5769  CG  LYS B 174    13530  14558   9567   2074    -42   2272       C  
ATOM   5770  CD  LYS B 174      -0.744  31.897 -68.812  1.00101.31           C  
ANISOU 5770  CD  LYS B 174    13797  14916   9780   2087     83   2490       C  
ATOM   5771  CE  LYS B 174      -0.250  33.130 -68.044  1.00104.72           C  
ANISOU 5771  CE  LYS B 174    14219  15180  10389   1960    158   2676       C  
ATOM   5772  NZ  LYS B 174      -1.308  34.118 -67.649  1.00107.63           N  
ANISOU 5772  NZ  LYS B 174    14604  15410  10880   1929    100   2710       N  
ATOM   5773  N   ALA B 175      -3.512  31.590 -63.859  1.00 87.71           N  
ANISOU 5773  N   ALA B 175    12062  12469   8796   1620   -136   1978       N  
ATOM   5774  CA  ALA B 175      -3.312  31.504 -62.417  1.00 85.32           C  
ANISOU 5774  CA  ALA B 175    11745  11991   8683   1468   -120   1915       C  
ATOM   5775  C   ALA B 175      -4.153  30.379 -61.830  1.00 86.27           C  
ANISOU 5775  C   ALA B 175    11857  12081   8843   1439   -206   1682       C  
ATOM   5776  O   ALA B 175      -3.624  29.314 -61.495  1.00 85.08           O  
ANISOU 5776  O   ALA B 175    11697  11942   8687   1401   -196   1573       O  
ATOM   5777  CB  ALA B 175      -3.648  32.834 -61.739  1.00 83.37           C  
ANISOU 5777  CB  ALA B 175    11501  11588   8589   1398   -111   2025       C  
ATOM   5778  N   ALA B 176      -5.470  30.586 -61.744  1.00 89.48           N  
ANISOU 5778  N   ALA B 176    12263  12453   9284   1463   -293   1607       N  
ATOM   5779  CA  ALA B 176      -6.368  29.572 -61.196  1.00 92.62           C  
ANISOU 5779  CA  ALA B 176    12645  12821   9727   1433   -378   1396       C  
ATOM   5780  C   ALA B 176      -6.260  28.228 -61.908  1.00 93.12           C  
ANISOU 5780  C   ALA B 176    12708  13018   9653   1504   -416   1263       C  
ATOM   5781  O   ALA B 176      -6.862  27.252 -61.447  1.00100.79           O  
ANISOU 5781  O   ALA B 176    13665  13962  10667   1471   -484   1085       O  
ATOM   5782  CB  ALA B 176      -7.814  30.064 -61.251  1.00 95.87           C  
ANISOU 5782  CB  ALA B 176    13050  13208  10167   1472   -466   1354       C  
ATOM   5783  N   CYS B 177      -5.513  28.151 -63.010  1.00 86.78           N  
ANISOU 5783  N   CYS B 177    11922  12361   8690   1604   -377   1343       N  
ATOM   5784  CA  CYS B 177      -5.216  26.884 -63.665  1.00 84.82           C  
ANISOU 5784  CA  CYS B 177    11677  12241   8311   1675   -404   1221       C  
ATOM   5785  C   CYS B 177      -3.925  26.262 -63.143  1.00 84.32           C  
ANISOU 5785  C   CYS B 177    11610  12153   8277   1602   -326   1218       C  
ATOM   5786  O   CYS B 177      -3.875  25.052 -62.893  1.00 84.34           O  
ANISOU 5786  O   CYS B 177    11608  12159   8279   1585   -363   1057       O  
ATOM   5787  CB  CYS B 177      -5.118  27.088 -65.181  1.00 86.67           C  
ANISOU 5787  CB  CYS B 177    11928  12664   8338   1837   -406   1301       C  
ATOM   5788  SG  CYS B 177      -5.197  25.572 -66.174  1.00 89.66           S  
ANISOU 5788  SG  CYS B 177    12314  13216   8535   1963   -482   1114       S  
ATOM   5789  N   LEU B 178      -2.874  27.068 -62.981  1.00 87.50           N  
ANISOU 5789  N   LEU B 178    12011  12528   8706   1560   -220   1394       N  
ATOM   5790  CA  LEU B 178      -1.575  26.576 -62.538  1.00 83.02           C  
ANISOU 5790  CA  LEU B 178    11434  11947   8161   1496   -140   1410       C  
ATOM   5791  C   LEU B 178      -1.436  26.520 -61.023  1.00 78.71           C  
ANISOU 5791  C   LEU B 178    10875  11220   7813   1338   -123   1362       C  
ATOM   5792  O   LEU B 178      -0.590  25.771 -60.521  1.00 74.20           O  
ANISOU 5792  O   LEU B 178    10295  10630   7269   1282    -85   1311       O  
ATOM   5793  CB  LEU B 178      -0.456  27.456 -63.107  1.00 79.60           C  
ANISOU 5793  CB  LEU B 178    10999  11581   7664   1524    -32   1628       C  
ATOM   5794  CG  LEU B 178       0.953  26.861 -63.150  1.00 81.64           C  
ANISOU 5794  CG  LEU B 178    11245  11902   7874   1514     51   1654       C  
ATOM   5795  CD1 LEU B 178       1.041  25.765 -64.200  1.00 85.13           C  
ANISOU 5795  CD1 LEU B 178    11696  12523   8126   1648     17   1548       C  
ATOM   5796  CD2 LEU B 178       1.986  27.948 -63.410  1.00 85.63           C  
ANISOU 5796  CD2 LEU B 178    11736  12428   8372   1502    161   1889       C  
ATOM   5797  N   LEU B 179      -2.240  27.290 -60.285  1.00 85.48           N  
ANISOU 5797  N   LEU B 179    11728  11947   8803   1269   -150   1376       N  
ATOM   5798  CA  LEU B 179      -2.070  27.341 -58.833  1.00 91.77           C  
ANISOU 5798  CA  LEU B 179    12511  12577   9781   1124   -129   1344       C  
ATOM   5799  C   LEU B 179      -2.549  26.072 -58.133  1.00 92.00           C  
ANISOU 5799  C   LEU B 179    12530  12563   9861   1076   -191   1141       C  
ATOM   5800  O   LEU B 179      -1.776  25.508 -57.337  1.00 93.15           O  
ANISOU 5800  O   LEU B 179    12668  12650  10073    993   -151   1103       O  
ATOM   5801  CB  LEU B 179      -2.746  28.597 -58.272  1.00 96.44           C  
ANISOU 5801  CB  LEU B 179    13100  13049  10493   1075   -137   1424       C  
ATOM   5802  CG  LEU B 179      -1.990  29.936 -58.298  1.00101.55           C  
ANISOU 5802  CG  LEU B 179    13750  13651  11182   1050    -57   1633       C  
ATOM   5803  CD1 LEU B 179      -0.946  29.975 -57.187  1.00103.11           C  
ANISOU 5803  CD1 LEU B 179    13933  13738  11506    923     13   1661       C  
ATOM   5804  CD2 LEU B 179      -1.349  30.246 -59.651  1.00101.48           C  
ANISOU 5804  CD2 LEU B 179    13751  13792  11013   1158    -10   1775       C  
ATOM   5805  N   PRO B 180      -3.766  25.560 -58.364  1.00 92.63           N  
ANISOU 5805  N   PRO B 180    12610  12667   9920   1120   -288   1008       N  
ATOM   5806  CA  PRO B 180      -4.175  24.333 -57.662  1.00 92.52           C  
ANISOU 5806  CA  PRO B 180    12584  12604   9968   1063   -345    824       C  
ATOM   5807  C   PRO B 180      -3.538  23.066 -58.207  1.00 88.92           C  
ANISOU 5807  C   PRO B 180    12136  12242   9407   1114   -352    732       C  
ATOM   5808  O   PRO B 180      -3.647  22.014 -57.561  1.00 91.41           O  
ANISOU 5808  O   PRO B 180    12444  12505   9784   1057   -386    594       O  
ATOM   5809  CB  PRO B 180      -5.700  24.303 -57.847  1.00 92.10           C  
ANISOU 5809  CB  PRO B 180    12519  12552   9921   1100   -448    728       C  
ATOM   5810  CG  PRO B 180      -5.995  25.181 -59.000  1.00 92.85           C  
ANISOU 5810  CG  PRO B 180    12630  12748   9902   1215   -456    834       C  
ATOM   5811  CD  PRO B 180      -4.782  25.997 -59.338  1.00 92.83           C  
ANISOU 5811  CD  PRO B 180    12642  12775   9855   1228   -354   1018       C  
ATOM   5812  N   LYS B 181      -2.887  23.126 -59.368  1.00 78.95           N  
ANISOU 5812  N   LYS B 181    10889  11118   7989   1222   -321    804       N  
ATOM   5813  CA  LYS B 181      -2.148  21.981 -59.884  1.00 64.51           C  
ANISOU 5813  CA  LYS B 181     9069   9384   6057   1278   -319    724       C  
ATOM   5814  C   LYS B 181      -0.727  21.932 -59.338  1.00 64.22           C  
ANISOU 5814  C   LYS B 181     9029   9317   6057   1212   -217    800       C  
ATOM   5815  O   LYS B 181      -0.201  20.846 -59.074  1.00 68.04           O  
ANISOU 5815  O   LYS B 181     9513   9799   6540   1196   -220    698       O  
ATOM   5816  CB  LYS B 181      -2.124  22.013 -61.414  1.00 55.31           C  
ANISOU 5816  CB  LYS B 181     7921   8401   4694   1438   -335    757       C  
ATOM   5817  CG  LYS B 181      -3.499  21.922 -62.057  1.00 52.39           C  
ANISOU 5817  CG  LYS B 181     7555   8081   4272   1517   -446    664       C  
ATOM   5818  CD  LYS B 181      -3.401  21.617 -63.543  1.00 57.74           C  
ANISOU 5818  CD  LYS B 181     8249   8949   4740   1683   -473    654       C  
ATOM   5819  CE  LYS B 181      -4.779  21.409 -64.151  1.00 63.99           C  
ANISOU 5819  CE  LYS B 181     9041   9789   5482   1761   -595    540       C  
ATOM   5820  NZ  LYS B 181      -4.707  21.072 -65.599  1.00 70.82           N  
ANISOU 5820  NZ  LYS B 181     9924  10847   6136   1930   -630    517       N  
ATOM   5821  N   LEU B 182      -0.096  23.096 -59.160  1.00 58.63           N  
ANISOU 5821  N   LEU B 182     8313   8579   5384   1174   -131    978       N  
ATOM   5822  CA  LEU B 182       1.241  23.132 -58.578  1.00 55.95           C  
ANISOU 5822  CA  LEU B 182     7963   8203   5094   1103    -36   1056       C  
ATOM   5823  C   LEU B 182       1.210  22.845 -57.083  1.00 54.11           C  
ANISOU 5823  C   LEU B 182     7718   7807   5036    961    -38    983       C  
ATOM   5824  O   LEU B 182       2.173  22.291 -56.539  1.00 54.86           O  
ANISOU 5824  O   LEU B 182     7804   7877   5164    909      8    967       O  
ATOM   5825  CB  LEU B 182       1.893  24.490 -58.843  1.00 58.02           C  
ANISOU 5825  CB  LEU B 182     8217   8477   5352   1099     51   1271       C  
ATOM   5826  CG  LEU B 182       3.041  24.531 -59.854  1.00 67.25           C  
ANISOU 5826  CG  LEU B 182     9381   9797   6376   1185    127   1385       C  
ATOM   5827  CD1 LEU B 182       2.563  24.114 -61.235  1.00 55.94           C  
ANISOU 5827  CD1 LEU B 182     7965   8533   4754   1342     77   1342       C  
ATOM   5828  CD2 LEU B 182       3.661  25.919 -59.896  1.00 67.21           C  
ANISOU 5828  CD2 LEU B 182     9361   9769   6407   1151    213   1605       C  
ATOM   5829  N   ASP B 183       0.121  23.218 -56.404  1.00 55.20           N  
ANISOU 5829  N   ASP B 183     7852   7839   5284    903    -91    940       N  
ATOM   5830  CA  ASP B 183       0.007  22.943 -54.975  1.00 58.76           C  
ANISOU 5830  CA  ASP B 183     8289   8143   5893    776    -96    869       C  
ATOM   5831  C   ASP B 183      -0.084  21.449 -54.706  1.00 56.25           C  
ANISOU 5831  C   ASP B 183     7973   7825   5574    767   -145    698       C  
ATOM   5832  O   ASP B 183       0.498  20.950 -53.736  1.00 52.17           O  
ANISOU 5832  O   ASP B 183     7449   7232   5144    680   -116    662       O  
ATOM   5833  CB  ASP B 183      -1.213  23.656 -54.399  1.00 59.62           C  
ANISOU 5833  CB  ASP B 183     8391   8157   6104    732   -144    857       C  
ATOM   5834  CG  ASP B 183      -1.026  25.149 -54.323  1.00 63.29           C  
ANISOU 5834  CG  ASP B 183     8855   8577   6614    713    -92   1023       C  
ATOM   5835  OD1 ASP B 183       0.122  25.612 -54.481  1.00 63.12           O  
ANISOU 5835  OD1 ASP B 183     8834   8575   6575    705    -13   1147       O  
ATOM   5836  OD2 ASP B 183      -2.025  25.862 -54.108  1.00 67.90           O  
ANISOU 5836  OD2 ASP B 183     9437   9106   7256    705   -132   1029       O  
ATOM   5837  N   GLU B 184      -0.819  20.724 -55.548  1.00 67.11           N  
ANISOU 5837  N   GLU B 184     9359   9284   6857    855   -224    591       N  
ATOM   5838  CA  GLU B 184      -0.935  19.283 -55.370  1.00 71.80           C  
ANISOU 5838  CA  GLU B 184     9956   9873   7452    851   -280    426       C  
ATOM   5839  C   GLU B 184       0.399  18.590 -55.618  1.00 69.63           C  
ANISOU 5839  C   GLU B 184     9690   9659   7108    879   -226    429       C  
ATOM   5840  O   GLU B 184       0.759  17.651 -54.900  1.00 67.54           O  
ANISOU 5840  O   GLU B 184     9423   9333   6905    821   -230    341       O  
ATOM   5841  CB  GLU B 184      -2.016  18.732 -56.298  1.00 78.92           C  
ANISOU 5841  CB  GLU B 184    10864  10853   8268    945   -383    312       C  
ATOM   5842  CG  GLU B 184      -2.083  17.219 -56.343  1.00 93.02           C  
ANISOU 5842  CG  GLU B 184    12656  12646  10040    960   -450    141       C  
ATOM   5843  CD  GLU B 184      -3.498  16.706 -56.512  1.00102.07           C  
ANISOU 5843  CD  GLU B 184    13793  13781  11207    975   -565      6       C  
ATOM   5844  OE1 GLU B 184      -3.842  15.693 -55.868  1.00101.51           O  
ANISOU 5844  OE1 GLU B 184    13713  13633  11222    913   -618   -121       O  
ATOM   5845  OE2 GLU B 184      -4.266  17.316 -57.286  1.00105.18           O  
ANISOU 5845  OE2 GLU B 184    14187  14243  11535   1048   -606     29       O  
ATOM   5846  N   LEU B 185       1.155  19.052 -56.617  1.00 65.46           N  
ANISOU 5846  N   LEU B 185     9169   9251   6450    969   -172    536       N  
ATOM   5847  CA  LEU B 185       2.428  18.414 -56.938  1.00 62.99           C  
ANISOU 5847  CA  LEU B 185     8860   9014   6059   1010   -118    543       C  
ATOM   5848  C   LEU B 185       3.456  18.635 -55.836  1.00 54.76           C  
ANISOU 5848  C   LEU B 185     7800   7879   5127    897    -34    615       C  
ATOM   5849  O   LEU B 185       4.226  17.724 -55.507  1.00 45.87           O  
ANISOU 5849  O   LEU B 185     6674   6748   4007    883    -18    553       O  
ATOM   5850  CB  LEU B 185       2.952  18.935 -58.276  1.00 59.95           C  
ANISOU 5850  CB  LEU B 185     8479   8792   5505   1135    -75    654       C  
ATOM   5851  CG  LEU B 185       2.234  18.413 -59.521  1.00 66.43           C  
ANISOU 5851  CG  LEU B 185     9320   9742   6178   1274   -158    561       C  
ATOM   5852  CD1 LEU B 185       2.871  18.967 -60.787  1.00 66.04           C  
ANISOU 5852  CD1 LEU B 185     9272   9863   5956   1399   -101    688       C  
ATOM   5853  CD2 LEU B 185       2.232  16.892 -59.539  1.00 62.07           C  
ANISOU 5853  CD2 LEU B 185     8781   9199   5603   1304   -225    372       C  
ATOM   5854  N   ARG B 186       3.488  19.836 -55.255  1.00 56.96           N  
ANISOU 5854  N   ARG B 186     8064   8081   5496    821     16    743       N  
ATOM   5855  CA  ARG B 186       4.427  20.110 -54.172  1.00 57.58           C  
ANISOU 5855  CA  ARG B 186     8125   8067   5687    712     89    808       C  
ATOM   5856  C   ARG B 186       4.117  19.252 -52.951  1.00 55.95           C  
ANISOU 5856  C   ARG B 186     7916   7739   5602    618     49    677       C  
ATOM   5857  O   ARG B 186       5.020  18.664 -52.344  1.00 50.96           O  
ANISOU 5857  O   ARG B 186     7277   7078   5006    572     86    656       O  
ATOM   5858  CB  ARG B 186       4.391  21.596 -53.810  1.00 63.57           C  
ANISOU 5858  CB  ARG B 186     8870   8760   6524    652    135    958       C  
ATOM   5859  CG  ARG B 186       4.998  21.917 -52.453  1.00 68.51           C  
ANISOU 5859  CG  ARG B 186     9477   9256   7299    523    184    993       C  
ATOM   5860  CD  ARG B 186       4.438  23.212 -51.885  1.00 73.03           C  
ANISOU 5860  CD  ARG B 186    10043   9726   7979    458    187   1078       C  
ATOM   5861  NE  ARG B 186       2.978  23.234 -51.899  1.00 66.22           N  
ANISOU 5861  NE  ARG B 186     9194   8834   7135    475    105    996       N  
ATOM   5862  CZ  ARG B 186       2.246  24.297 -51.583  1.00 62.08           C  
ANISOU 5862  CZ  ARG B 186     8668   8236   6685    444     90   1050       C  
ATOM   5863  NH1 ARG B 186       2.837  25.429 -51.225  1.00 64.02           N  
ANISOU 5863  NH1 ARG B 186     8904   8423   6999    393    148   1184       N  
ATOM   5864  NH2 ARG B 186       0.922  24.229 -51.624  1.00 57.76           N  
ANISOU 5864  NH2 ARG B 186     8127   7673   6148    466     14    968       N  
ATOM   5865  N   ASP B 187       2.838  19.164 -52.580  1.00 46.81           N  
ANISOU 5865  N   ASP B 187     6763   6514   4509    589    -26    591       N  
ATOM   5866  CA  ASP B 187       2.460  18.371 -51.414  1.00 47.88           C  
ANISOU 5866  CA  ASP B 187     6893   6537   4761    499    -63    475       C  
ATOM   5867  C   ASP B 187       2.628  16.881 -51.680  1.00 45.74           C  
ANISOU 5867  C   ASP B 187     6636   6303   4440    540   -107    340       C  
ATOM   5868  O   ASP B 187       3.079  16.136 -50.802  1.00 42.91           O  
ANISOU 5868  O   ASP B 187     6274   5876   4153    474    -98    284       O  
ATOM   5869  CB  ASP B 187       1.023  18.690 -51.007  1.00 53.62           C  
ANISOU 5869  CB  ASP B 187     7614   7194   5565    462   -129    426       C  
ATOM   5870  CG  ASP B 187       0.839  20.144 -50.625  1.00 62.66           C  
ANISOU 5870  CG  ASP B 187     8747   8285   6774    419    -90    549       C  
ATOM   5871  OD1 ASP B 187       1.795  20.742 -50.088  1.00 64.02           O  
ANISOU 5871  OD1 ASP B 187     8913   8419   6994    365    -16    647       O  
ATOM   5872  OD2 ASP B 187      -0.258  20.689 -50.864  1.00 72.31           O  
ANISOU 5872  OD2 ASP B 187     9968   9503   8003    441   -137    546       O  
ATOM   5873  N   GLU B 188       2.268  16.424 -52.883  1.00 51.81           N  
ANISOU 5873  N   GLU B 188     7420   7180   5085    652   -160    282       N  
ATOM   5874  CA  GLU B 188       2.523  15.033 -53.242  1.00 52.40           C  
ANISOU 5874  CA  GLU B 188     7511   7295   5104    705   -204    153       C  
ATOM   5875  C   GLU B 188       4.017  14.735 -53.244  1.00 50.15           C  
ANISOU 5875  C   GLU B 188     7227   7052   4776    720   -127    200       C  
ATOM   5876  O   GLU B 188       4.438  13.632 -52.876  1.00 47.98           O  
ANISOU 5876  O   GLU B 188     6960   6748   4523    708   -144    106       O  
ATOM   5877  CB  GLU B 188       1.912  14.717 -54.608  1.00 57.80           C  
ANISOU 5877  CB  GLU B 188     8212   8098   5653    835   -275     87       C  
ATOM   5878  CG  GLU B 188       0.413  14.468 -54.578  1.00 70.62           C  
ANISOU 5878  CG  GLU B 188     9832   9676   7323    824   -378    -19       C  
ATOM   5879  CD  GLU B 188      -0.070  13.676 -55.777  1.00 89.39           C  
ANISOU 5879  CD  GLU B 188    12227  12156   9580    946   -467   -137       C  
ATOM   5880  OE1 GLU B 188       0.212  12.461 -55.843  1.00 94.07           O  
ANISOU 5880  OE1 GLU B 188    12834  12748  10160    968   -508   -256       O  
ATOM   5881  OE2 GLU B 188      -0.731  14.269 -56.656  1.00 95.33           O  
ANISOU 5881  OE2 GLU B 188    12981  12990  10250   1022   -499   -112       O  
ATOM   5882  N   GLY B 189       4.834  15.712 -53.646  1.00 52.30           N  
ANISOU 5882  N   GLY B 189     7488   7392   4991    745    -43    349       N  
ATOM   5883  CA  GLY B 189       6.273  15.500 -53.667  1.00 42.06           C  
ANISOU 5883  CA  GLY B 189     6183   6145   3653    759     35    404       C  
ATOM   5884  C   GLY B 189       6.861  15.297 -52.283  1.00 38.39           C  
ANISOU 5884  C   GLY B 189     5704   5559   3324    639     72    404       C  
ATOM   5885  O   GLY B 189       7.730  14.444 -52.087  1.00 40.15           O  
ANISOU 5885  O   GLY B 189     5928   5793   3536    646     91    359       O  
ATOM   5886  N   LYS B 190       6.404  16.084 -51.306  1.00 42.58           N  
ANISOU 5886  N   LYS B 190     6222   5976   3981    532     82    453       N  
ATOM   5887  CA  LYS B 190       6.871  15.904 -49.934  1.00 49.05           C  
ANISOU 5887  CA  LYS B 190     7028   6680   4929    419    111    447       C  
ATOM   5888  C   LYS B 190       6.395  14.566 -49.378  1.00 44.69           C  
ANISOU 5888  C   LYS B 190     6491   6063   4427    395     42    291       C  
ATOM   5889  O   LYS B 190       7.199  13.781 -48.861  1.00 44.71           O  
ANISOU 5889  O   LYS B 190     6493   6042   4453    372     61    254       O  
ATOM   5890  CB  LYS B 190       6.413  17.092 -49.069  1.00 54.86           C  
ANISOU 5890  CB  LYS B 190     7747   7316   5779    323    131    528       C  
ATOM   5891  CG  LYS B 190       6.509  17.030 -47.503  1.00 66.49           C  
ANISOU 5891  CG  LYS B 190     9207   8656   7400    199    143    508       C  
ATOM   5892  CD  LYS B 190       7.486  16.019 -46.867  1.00 75.39           C  
ANISOU 5892  CD  LYS B 190    10332   9763   8550    170    165    458       C  
ATOM   5893  CE  LYS B 190       8.951  16.224 -47.237  1.00 74.10           C  
ANISOU 5893  CE  LYS B 190    10153   9674   8328    199    243    549       C  
ATOM   5894  NZ  LYS B 190       9.786  15.095 -46.726  1.00 73.04           N  
ANISOU 5894  NZ  LYS B 190    10019   9528   8205    188    252    482       N  
ATOM   5895  N   ALA B 191       5.097  14.274 -49.498  1.00 35.39           N  
ANISOU 5895  N   ALA B 191     5323   4857   3266    401    -40    201       N  
ATOM   5896  CA  ALA B 191       4.583  12.983 -49.049  1.00 43.65           C  
ANISOU 5896  CA  ALA B 191     6381   5841   4364    378   -112     57       C  
ATOM   5897  C   ALA B 191       5.395  11.832 -49.636  1.00 35.66           C  
ANISOU 5897  C   ALA B 191     5388   4893   3269    455   -122    -16       C  
ATOM   5898  O   ALA B 191       5.767  10.892 -48.926  1.00 35.21           O  
ANISOU 5898  O   ALA B 191     5336   4772   3272    414   -131    -82       O  
ATOM   5899  CB  ALA B 191       3.105  12.849 -49.421  1.00 45.33           C  
ANISOU 5899  CB  ALA B 191     6597   6044   4581    396   -202    -25       C  
ATOM   5900  N   SER B 192       5.718  11.917 -50.930  1.00 42.06           N  
ANISOU 5900  N   SER B 192     6208   5834   3937    573   -118      0       N  
ATOM   5901  CA  SER B 192       6.447  10.838 -51.591  1.00 37.39           C  
ANISOU 5901  CA  SER B 192     5636   5317   3254    665   -132    -78       C  
ATOM   5902  C   SER B 192       7.883  10.734 -51.085  1.00 37.05           C  
ANISOU 5902  C   SER B 192     5581   5277   3220    642    -48    -16       C  
ATOM   5903  O   SER B 192       8.378   9.628 -50.837  1.00 37.02           O  
ANISOU 5903  O   SER B 192     5589   5250   3226    654    -67   -103       O  
ATOM   5904  CB  SER B 192       6.426  11.048 -53.105  1.00 40.76           C  
ANISOU 5904  CB  SER B 192     6074   5898   3517    805   -143    -68       C  
ATOM   5905  OG  SER B 192       7.388  10.229 -53.747  1.00 48.49           O  
ANISOU 5905  OG  SER B 192     7064   6968   4391    902   -132   -113       O  
ATOM   5906  N   SER B 193       8.571  11.869 -50.935  1.00 36.87           N  
ANISOU 5906  N   SER B 193     5532   5279   3197    611     42    133       N  
ATOM   5907  CA  SER B 193       9.951  11.836 -50.457  1.00 45.67           C  
ANISOU 5907  CA  SER B 193     6627   6401   4324    586    123    197       C  
ATOM   5908  C   SER B 193      10.025  11.360 -49.011  1.00 35.47           C  
ANISOU 5908  C   SER B 193     5332   4970   3176    472    117    155       C  
ATOM   5909  O   SER B 193      10.953  10.633 -48.637  1.00 35.34           O  
ANISOU 5909  O   SER B 193     5313   4947   3166    472    140    128       O  
ATOM   5910  CB  SER B 193      10.592  13.217 -50.598  1.00 50.05           C  
ANISOU 5910  CB  SER B 193     7149   7004   4862    568    214    370       C  
ATOM   5911  OG  SER B 193      11.627  13.403 -49.647  1.00 46.05           O  
ANISOU 5911  OG  SER B 193     6616   6447   4433    489    281    434       O  
ATOM   5912  N   ALA B 194       9.057  11.760 -48.185  1.00 43.71           N  
ANISOU 5912  N   ALA B 194     6373   5905   4329    378     88    150       N  
ATOM   5913  CA  ALA B 194       9.045  11.312 -46.797  1.00 40.02           C  
ANISOU 5913  CA  ALA B 194     5903   5313   3992    273     81    112       C  
ATOM   5914  C   ALA B 194       8.824   9.807 -46.708  1.00 33.79           C  
ANISOU 5914  C   ALA B 194     5138   4487   3213    295     12    -31       C  
ATOM   5915  O   ALA B 194       9.457   9.125 -45.894  1.00 33.33           O  
ANISOU 5915  O   ALA B 194     5080   4372   3211    254     24    -57       O  
ATOM   5916  CB  ALA B 194       7.973  12.069 -46.014  1.00 33.01           C  
ANISOU 5916  CB  ALA B 194     5005   4331   3207    181     63    134       C  
ATOM   5917  N   LYS B 195       7.942   9.266 -47.553  1.00 43.65           N  
ANISOU 5917  N   LYS B 195     6410   5767   4410    362    -67   -124       N  
ATOM   5918  CA  LYS B 195       7.722   7.823 -47.573  1.00 44.94           C  
ANISOU 5918  CA  LYS B 195     6597   5891   4585    388   -142   -264       C  
ATOM   5919  C   LYS B 195       8.979   7.085 -48.018  1.00 37.92           C  
ANISOU 5919  C   LYS B 195     5721   5071   3617    470   -116   -287       C  
ATOM   5920  O   LYS B 195       9.372   6.082 -47.411  1.00 37.52           O  
ANISOU 5920  O   LYS B 195     5682   4955   3619    449   -135   -353       O  
ATOM   5921  CB  LYS B 195       6.546   7.481 -48.490  1.00 39.63           C  
ANISOU 5921  CB  LYS B 195     5942   5247   3868    450   -235   -359       C  
ATOM   5922  CG  LYS B 195       5.193   7.933 -47.968  1.00 44.34           C  
ANISOU 5922  CG  LYS B 195     6525   5765   4556    368   -277   -364       C  
ATOM   5923  CD  LYS B 195       4.082   7.559 -48.936  1.00 53.20           C  
ANISOU 5923  CD  LYS B 195     7659   6923   5630    435   -373   -462       C  
ATOM   5924  CE  LYS B 195       2.721   7.967 -48.399  1.00 61.86           C  
ANISOU 5924  CE  LYS B 195     8734   7946   6822    354   -416   -469       C  
ATOM   5925  NZ  LYS B 195       2.439   7.347 -47.075  1.00 74.71           N  
ANISOU 5925  NZ  LYS B 195    10351   9442   8593    240   -429   -504       N  
ATOM   5926  N   GLN B 196       9.626   7.571 -49.080  1.00 49.68           N  
ANISOU 5926  N   GLN B 196     7205   6694   4975    568    -73   -230       N  
ATOM   5927  CA  GLN B 196      10.841   6.924 -49.565  1.00 46.26           C  
ANISOU 5927  CA  GLN B 196     6778   6345   4456    657    -43   -248       C  
ATOM   5928  C   GLN B 196      11.979   7.037 -48.559  1.00 35.90           C  
ANISOU 5928  C   GLN B 196     5441   4991   3207    588     36   -174       C  
ATOM   5929  O   GLN B 196      12.803   6.121 -48.455  1.00 37.42           O  
ANISOU 5929  O   GLN B 196     5641   5190   3386    626     37   -227       O  
ATOM   5930  CB  GLN B 196      11.255   7.525 -50.909  1.00 39.88           C  
ANISOU 5930  CB  GLN B 196     5961   5701   3490    774     -4   -187       C  
ATOM   5931  CG  GLN B 196      12.433   6.822 -51.570  1.00 38.50           C  
ANISOU 5931  CG  GLN B 196     5789   5635   3204    887     22   -216       C  
ATOM   5932  CD  GLN B 196      12.124   5.388 -51.954  1.00 39.11           C  
ANISOU 5932  CD  GLN B 196     5907   5697   3256    965    -76   -390       C  
ATOM   5933  OE1 GLN B 196      10.974   5.037 -52.218  1.00 43.45           O  
ANISOU 5933  OE1 GLN B 196     6481   6205   3822    971   -167   -485       O  
ATOM   5934  NE2 GLN B 196      13.153   4.550 -51.989  1.00 39.59           N  
ANISOU 5934  NE2 GLN B 196     5973   5790   3280   1026    -61   -435       N  
ATOM   5935  N   ARG B 197      12.042   8.145 -47.816  1.00 35.13           N  
ANISOU 5935  N   ARG B 197     5314   4852   3181    491     96    -57       N  
ATOM   5936  CA  ARG B 197      13.062   8.282 -46.781  1.00 37.41           C  
ANISOU 5936  CA  ARG B 197     5578   5096   3540    418    163      8       C  
ATOM   5937  C   ARG B 197      12.929   7.195 -45.723  1.00 35.43           C  
ANISOU 5937  C   ARG B 197     5345   4726   3392    359    117    -86       C  
ATOM   5938  O   ARG B 197      13.938   6.729 -45.179  1.00 34.86           O  
ANISOU 5938  O   ARG B 197     5263   4642   3339    351    150    -81       O  
ATOM   5939  CB  ARG B 197      12.973   9.666 -46.137  1.00 36.42           C  
ANISOU 5939  CB  ARG B 197     5421   4933   3485    321    219    134       C  
ATOM   5940  CG  ARG B 197      14.204  10.051 -45.337  1.00 39.37           C  
ANISOU 5940  CG  ARG B 197     5759   5295   3904    264    298    222       C  
ATOM   5941  CD  ARG B 197      15.451   9.944 -46.193  1.00 40.01           C  
ANISOU 5941  CD  ARG B 197     5821   5507   3874    357    354    265       C  
ATOM   5942  NE  ARG B 197      16.669  10.252 -45.450  1.00 33.83           N  
ANISOU 5942  NE  ARG B 197     4999   4719   3136    305    425    345       N  
ATOM   5943  CZ  ARG B 197      17.469   9.334 -44.918  1.00 34.58           C  
ANISOU 5943  CZ  ARG B 197     5092   4798   3250    310    428    295       C  
ATOM   5944  NH1 ARG B 197      17.178   8.046 -45.038  1.00 40.47           N  
ANISOU 5944  NH1 ARG B 197     5877   5522   3978    363    364    166       N  
ATOM   5945  NH2 ARG B 197      18.561   9.704 -44.265  1.00 37.73           N  
ANISOU 5945  NH2 ARG B 197     5448   5198   3689    262    493    372       N  
ATOM   5946  N   LEU B 198      11.699   6.774 -45.423  1.00 33.55           N  
ANISOU 5946  N   LEU B 198     5129   4399   3220    318     40   -167       N  
ATOM   5947  CA  LEU B 198      11.500   5.676 -44.483  1.00 37.81           C  
ANISOU 5947  CA  LEU B 198     5686   4825   3856    265     -8   -252       C  
ATOM   5948  C   LEU B 198      11.959   4.350 -45.079  1.00 38.71           C  
ANISOU 5948  C   LEU B 198     5830   4965   3913    361    -54   -360       C  
ATOM   5949  O   LEU B 198      12.607   3.547 -44.396  1.00 35.79           O  
ANISOU 5949  O   LEU B 198     5467   4542   3590    344    -52   -390       O  
ATOM   5950  CB  LEU B 198      10.028   5.606 -44.070  1.00 39.42           C  
ANISOU 5950  CB  LEU B 198     5897   4935   4144    196    -76   -303       C  
ATOM   5951  CG  LEU B 198       9.559   4.409 -43.237  1.00 41.12           C  
ANISOU 5951  CG  LEU B 198     6131   5032   4461    143   -139   -395       C  
ATOM   5952  CD1 LEU B 198      10.429   4.214 -42.006  1.00 31.78           C  
ANISOU 5952  CD1 LEU B 198     4938   3788   3351     76    -89   -352       C  
ATOM   5953  CD2 LEU B 198       8.098   4.575 -42.839  1.00 40.55           C  
ANISOU 5953  CD2 LEU B 198     6053   4885   4471     69   -192   -420       C  
ATOM   5954  N   LYS B 199      11.632   4.103 -46.351  1.00 36.75           N  
ANISOU 5954  N   LYS B 199     5601   4801   3563    467    -99   -422       N  
ATOM   5955  CA  LYS B 199      12.060   2.867 -46.999  1.00 40.22           C  
ANISOU 5955  CA  LYS B 199     6070   5271   3940    571   -150   -535       C  
ATOM   5956  C   LYS B 199      13.577   2.750 -47.012  1.00 35.90           C  
ANISOU 5956  C   LYS B 199     5509   4795   3335    624    -77   -489       C  
ATOM   5957  O   LYS B 199      14.129   1.674 -46.754  1.00 36.09           O  
ANISOU 5957  O   LYS B 199     5552   4782   3378    653   -102   -562       O  
ATOM   5958  CB  LYS B 199      11.512   2.803 -48.426  1.00 43.47           C  
ANISOU 5958  CB  LYS B 199     6501   5783   4235    686   -204   -600       C  
ATOM   5959  CG  LYS B 199       9.999   2.899 -48.525  1.00 41.25           C  
ANISOU 5959  CG  LYS B 199     6228   5443   4002    645   -283   -652       C  
ATOM   5960  CD  LYS B 199       9.531   2.705 -49.961  1.00 45.74           C  
ANISOU 5960  CD  LYS B 199     6817   6115   4447    772   -345   -731       C  
ATOM   5961  CE  LYS B 199       8.045   2.997 -50.107  1.00 45.03           C  
ANISOU 5961  CE  LYS B 199     6727   5984   4399    731   -416   -766       C  
ATOM   5962  NZ  LYS B 199       7.240   2.272 -49.086  1.00 50.72           N  
ANISOU 5962  NZ  LYS B 199     7452   6545   5274    623   -481   -834       N  
ATOM   5963  N   CYS B 200      14.267   3.853 -47.305  1.00 35.89           N  
ANISOU 5963  N   CYS B 200     5473   4895   3270    635     13   -365       N  
ATOM   5964  CA  CYS B 200      15.724   3.827 -47.335  1.00 36.12           C  
ANISOU 5964  CA  CYS B 200     5477   5003   3245    681     88   -311       C  
ATOM   5965  C   CYS B 200      16.294   3.575 -45.943  1.00 35.20           C  
ANISOU 5965  C   CYS B 200     5349   4782   3246    584    115   -287       C  
ATOM   5966  O   CYS B 200      17.182   2.734 -45.773  1.00 39.88           O  
ANISOU 5966  O   CYS B 200     5945   5379   3829    628    119   -328       O  
ATOM   5967  CB  CYS B 200      16.261   5.136 -47.922  1.00 40.19           C  
ANISOU 5967  CB  CYS B 200     5951   5642   3679    700    178   -171       C  
ATOM   5968  SG  CYS B 200      15.996   5.333 -49.711  1.00 44.24           S  
ANISOU 5968  SG  CYS B 200     6473   6322   4014    852    164   -188       S  
ATOM   5969  N   ALA B 201      15.794   4.293 -44.933  1.00 34.21           N  
ANISOU 5969  N   ALA B 201     5207   4563   3227    457    133   -222       N  
ATOM   5970  CA  ALA B 201      16.288   4.101 -43.573  1.00 37.78           C  
ANISOU 5970  CA  ALA B 201     5647   4921   3786    366    157   -197       C  
ATOM   5971  C   ALA B 201      16.080   2.667 -43.108  1.00 36.23           C  
ANISOU 5971  C   ALA B 201     5489   4630   3647    371     84   -316       C  
ATOM   5972  O   ALA B 201      16.946   2.097 -42.436  1.00 33.21           O  
ANISOU 5972  O   ALA B 201     5103   4219   3297    364    102   -319       O  
ATOM   5973  CB  ALA B 201      15.603   5.083 -42.622  1.00 33.21           C  
ANISOU 5973  CB  ALA B 201     5049   4261   3307    239    175   -124       C  
ATOM   5974  N   SER B 202      14.939   2.066 -43.454  1.00 33.66           N  
ANISOU 5974  N   SER B 202     5200   4253   3338    382     -2   -412       N  
ATOM   5975  CA  SER B 202      14.716   0.662 -43.120  1.00 45.69           C  
ANISOU 5975  CA  SER B 202     6760   5680   4918    391    -79   -525       C  
ATOM   5976  C   SER B 202      15.705  -0.240 -43.849  1.00 55.31           C  
ANISOU 5976  C   SER B 202     7996   6967   6050    517    -89   -592       C  
ATOM   5977  O   SER B 202      16.202  -1.220 -43.281  1.00 53.84           O  
ANISOU 5977  O   SER B 202     7829   6716   5913    522   -110   -641       O  
ATOM   5978  CB  SER B 202      13.278   0.266 -43.456  1.00 48.09           C  
ANISOU 5978  CB  SER B 202     7092   5922   5257    379   -172   -613       C  
ATOM   5979  OG  SER B 202      13.107   0.115 -44.856  1.00 55.29           O  
ANISOU 5979  OG  SER B 202     8021   6930   6056    497   -211   -679       O  
ATOM   5980  N   LEU B 203      16.088   0.047 -45.079  1.00 48.53           N  
ANISOU 5980  N   LEU B 203     7133   6245   5060    627    -73   -594       N  
ATOM   5981  CA  LEU B 203      17.081  -0.864 -45.702  1.00 50.55           C  
ANISOU 5981  CA  LEU B 203     7402   6587   5218    761    -77   -657       C  
ATOM   5982  C   LEU B 203      18.484  -0.635 -45.126  1.00 61.63           C  
ANISOU 5982  C   LEU B 203     8765   8056   6597    767     20   -564       C  
ATOM   5983  O   LEU B 203      19.154  -1.617 -44.826  1.00 46.37           O  
ANISOU 5983  O   LEU B 203     6839   6076   4702    776     15   -598       O  
ATOM   5984  CB  LEU B 203      17.063  -0.635 -47.215  1.00 39.92           C  
ANISOU 5984  CB  LEU B 203     6062   5377   3729    883    -92   -691       C  
ATOM   5985  CG  LEU B 203      15.979  -1.378 -47.981  1.00 42.47           C  
ANISOU 5985  CG  LEU B 203     6434   5664   4040    944   -208   -837       C  
ATOM   5986  CD1 LEU B 203      15.632  -0.633 -49.255  1.00 53.21           C  
ANISOU 5986  CD1 LEU B 203     7789   7169   5259   1044   -208   -836       C  
ATOM   5987  CD2 LEU B 203      16.424  -2.794 -48.293  1.00 49.12           C  
ANISOU 5987  CD2 LEU B 203     7312   6473   4878   1031   -270   -964       C  
ATOM   5988  N   GLN B 204      18.889   0.612 -44.931  1.00 80.40           N  
ANISOU 5988  N   GLN B 204    11095  10539   8914    759    106   -442       N  
ATOM   5989  CA  GLN B 204      20.289   0.927 -44.546  1.00 82.69           C  
ANISOU 5989  CA  GLN B 204    11337  10915   9166    777    198   -350       C  
ATOM   5990  C   GLN B 204      20.585   0.714 -43.058  1.00 83.79           C  
ANISOU 5990  C   GLN B 204    11467  10953   9418    691    214   -332       C  
ATOM   5991  O   GLN B 204      21.645   0.170 -42.761  1.00 94.26           O  
ANISOU 5991  O   GLN B 204    12759  12338  10717    724    269   -293       O  
ATOM   5992  CB  GLN B 204      20.616   2.339 -45.018  1.00 81.86           C  
ANISOU 5992  CB  GLN B 204    11183  10897   9025    737    282   -207       C  
ATOM   5993  CG  GLN B 204      20.630   2.475 -46.533  1.00 84.59           C  
ANISOU 5993  CG  GLN B 204    11506  11140   9494    585    310   -118       C  
ATOM   5994  CD  GLN B 204      20.444   3.904 -46.975  1.00 86.67           C  
ANISOU 5994  CD  GLN B 204    11752  11440   9739    548    338    -29       C  
ATOM   5995  OE1 GLN B 204      19.882   4.728 -46.257  1.00 96.00           O  
ANISOU 5995  OE1 GLN B 204    12939  12720  10815    634    333    -32       O  
ATOM   5996  NE2 GLN B 204      20.921   4.207 -48.171  1.00 69.43           N  
ANISOU 5996  NE2 GLN B 204     9547   9177   7656    425    365     50       N  
ATOM   5997  N   LYS B 205      19.709   1.153 -42.164  1.00 83.65           N  
ANISOU 5997  N   LYS B 205    11474  10789   9522    586    166   -357       N  
ATOM   5998  CA  LYS B 205      20.040   1.035 -40.729  1.00 83.23           C  
ANISOU 5998  CA  LYS B 205    11416  10637   9570    514    173   -348       C  
ATOM   5999  C   LYS B 205      19.394  -0.219 -40.146  1.00 86.45           C  
ANISOU 5999  C   LYS B 205    11877  10903  10067    484     81   -452       C  
ATOM   6000  O   LYS B 205      19.930  -0.761 -39.182  1.00 99.08           O  
ANISOU 6000  O   LYS B 205    13503  12473  11670    544     44   -528       O  
ATOM   6001  CB  LYS B 205      19.538   2.275 -39.985  1.00 83.29           C  
ANISOU 6001  CB  LYS B 205    11382  10612   9651    388    235   -229       C  
ATOM   6002  CG  LYS B 205      20.505   2.846 -38.956  1.00 89.41           C  
ANISOU 6002  CG  LYS B 205    12131  11357  10485    344    274   -188       C  
ATOM   6003  CD  LYS B 205      21.803   2.065 -38.822  1.00 94.94           C  
ANISOU 6003  CD  LYS B 205    12817  12150  11105    456    299   -210       C  
ATOM   6004  CE  LYS B 205      23.019   2.783 -39.371  1.00100.84           C  
ANISOU 6004  CE  LYS B 205    13506  13049  11760    500    384   -115       C  
ATOM   6005  NZ  LYS B 205      23.622   2.043 -40.504  1.00103.26           N  
ANISOU 6005  NZ  LYS B 205    13803  13460  11972    631    397   -156       N  
ATOM   6006  N   PHE B 206      18.284  -0.651 -40.715  1.00 62.31           N  
ANISOU 6006  N   PHE B 206     8833   7758   7082    397     43   -456       N  
ATOM   6007  CA  PHE B 206      17.578  -1.788 -40.093  1.00 48.05           C  
ANISOU 6007  CA  PHE B 206     7066   5808   5382    343    -34   -530       C  
ATOM   6008  C   PHE B 206      17.820  -3.103 -40.817  1.00 48.58           C  
ANISOU 6008  C   PHE B 206     7180   5847   5430    440   -116   -659       C  
ATOM   6009  O   PHE B 206      17.855  -4.092 -40.111  1.00 54.15           O  
ANISOU 6009  O   PHE B 206     7917   6428   6229    401   -178   -717       O  
ATOM   6010  CB  PHE B 206      16.119  -1.456 -39.804  1.00 53.41           C  
ANISOU 6010  CB  PHE B 206     7749   6427   6118    259    -69   -527       C  
ATOM   6011  CG  PHE B 206      15.940  -0.376 -38.771  1.00 46.89           C  
ANISOU 6011  CG  PHE B 206     6892   5552   5374    135    -19   -430       C  
ATOM   6012  CD1 PHE B 206      16.153  -0.640 -37.430  1.00 43.12           C  
ANISOU 6012  CD1 PHE B 206     6417   4975   4993     61    -22   -420       C  
ATOM   6013  CD2 PHE B 206      15.581   0.906 -39.142  1.00 45.78           C  
ANISOU 6013  CD2 PHE B 206     6720   5465   5211     96     28   -350       C  
ATOM   6014  CE1 PHE B 206      15.999   0.354 -36.480  1.00 43.13           C  
ANISOU 6014  CE1 PHE B 206     6389   4938   5061    -44     21   -338       C  
ATOM   6015  CE2 PHE B 206      15.427   1.899 -38.190  1.00 47.20           C  
ANISOU 6015  CE2 PHE B 206     6871   5597   5465    -12     68   -271       C  
ATOM   6016  CZ  PHE B 206      15.634   1.621 -36.862  1.00 36.96           C  
ANISOU 6016  CZ  PHE B 206     5577   4208   4258    -80     65   -268       C  
ATOM   6017  N   GLY B 207      17.980  -3.124 -42.142  1.00 42.30           N  
ANISOU 6017  N   GLY B 207     6391   5164   4516    567   -118   -704       N  
ATOM   6018  CA  GLY B 207      18.272  -4.428 -42.696  1.00 40.57           C  
ANISOU 6018  CA  GLY B 207     6214   4933   4268    676   -187   -826       C  
ATOM   6019  C   GLY B 207      17.299  -4.820 -43.798  1.00 44.56           C  
ANISOU 6019  C   GLY B 207     6755   5446   4731    742   -273   -935       C  
ATOM   6020  O   GLY B 207      16.156  -4.360 -43.863  1.00 49.46           O  
ANISOU 6020  O   GLY B 207     7375   6033   5385    678   -302   -931       O  
ATOM   6021  N   GLU B 208      17.780  -5.702 -44.678  1.00 38.97           N  
ANISOU 6021  N   GLU B 208     6075   4786   3945    878   -319  -1039       N  
ATOM   6022  CA  GLU B 208      16.909  -6.296 -45.684  1.00 48.02           C  
ANISOU 6022  CA  GLU B 208     7261   5927   5057    952   -419  -1167       C  
ATOM   6023  C   GLU B 208      15.746  -7.034 -45.039  1.00 45.20           C  
ANISOU 6023  C   GLU B 208     6937   5392   4847    858   -515  -1233       C  
ATOM   6024  O   GLU B 208      14.635  -7.034 -45.578  1.00 44.13           O  
ANISOU 6024  O   GLU B 208     6814   5235   4717    851   -583  -1293       O  
ATOM   6025  CB  GLU B 208      17.717  -7.239 -46.573  1.00 48.97           C  
ANISOU 6025  CB  GLU B 208     7410   6114   5082   1116   -456  -1277       C  
ATOM   6026  CG  GLU B 208      17.137  -7.448 -47.948  1.00 64.07           C  
ANISOU 6026  CG  GLU B 208     9347   8103   6893   1231   -528  -1388       C  
ATOM   6027  CD  GLU B 208      18.099  -8.154 -48.875  1.00 73.08           C  
ANISOU 6027  CD  GLU B 208    10507   9350   7911   1408   -543  -1479       C  
ATOM   6028  OE1 GLU B 208      18.869  -9.010 -48.392  1.00 78.28           O  
ANISOU 6028  OE1 GLU B 208    11182   9951   8610   1438   -553  -1516       O  
ATOM   6029  OE2 GLU B 208      18.088  -7.848 -50.085  1.00 81.40           O  
ANISOU 6029  OE2 GLU B 208    11558  10548   8823   1523   -544  -1513       O  
ATOM   6030  N   ARG B 209      15.976  -7.648 -43.875  1.00 43.50           N  
ANISOU 6030  N   ARG B 209     6730   5050   4748    783   -519  -1217       N  
ATOM   6031  CA  ARG B 209      14.920  -8.402 -43.206  1.00 44.78           C  
ANISOU 6031  CA  ARG B 209     6919   5041   5056    690   -605  -1268       C  
ATOM   6032  C   ARG B 209      13.786  -7.492 -42.748  1.00 42.86           C  
ANISOU 6032  C   ARG B 209     6646   4767   4873    561   -588  -1194       C  
ATOM   6033  O   ARG B 209      12.608  -7.834 -42.905  1.00 45.41           O  
ANISOU 6033  O   ARG B 209     6982   5012   5259    522   -671  -1258       O  
ATOM   6034  CB  ARG B 209      15.500  -9.171 -42.021  1.00 53.22           C  
ANISOU 6034  CB  ARG B 209     7999   5994   6228    640   -600  -1246       C  
ATOM   6035  CG  ARG B 209      14.644 -10.336 -41.564  1.00 57.20           C  
ANISOU 6035  CG  ARG B 209     8541   6321   6870    586   -707  -1325       C  
ATOM   6036  CD  ARG B 209      15.395 -11.219 -40.584  1.00 55.36           C  
ANISOU 6036  CD  ARG B 209     8328   5989   6719    572   -707  -1312       C  
ATOM   6037  NE  ARG B 209      14.509 -12.178 -39.932  1.00 59.78           N  
ANISOU 6037  NE  ARG B 209     8915   6369   7429    489   -794  -1352       N  
ATOM   6038  CZ  ARG B 209      13.849 -11.937 -38.805  1.00 59.84           C  
ANISOU 6038  CZ  ARG B 209     8900   6290   7546    347   -772  -1265       C  
ATOM   6039  NH1 ARG B 209      13.974 -10.764 -38.199  1.00 48.62           N  
ANISOU 6039  NH1 ARG B 209     7433   4941   6100    276   -671  -1143       N  
ATOM   6040  NH2 ARG B 209      13.063 -12.868 -38.283  1.00 63.06           N  
ANISOU 6040  NH2 ARG B 209     9330   6540   8090    278   -852  -1299       N  
ATOM   6041  N   ALA B 210      14.119  -6.333 -42.176  1.00 40.93           N  
ANISOU 6041  N   ALA B 210     6358   4581   4614    495   -486  -1063       N  
ATOM   6042  CA  ALA B 210      13.082  -5.404 -41.739  1.00 40.48           C  
ANISOU 6042  CA  ALA B 210     6271   4501   4608    381   -467   -993       C  
ATOM   6043  C   ALA B 210      12.325  -4.829 -42.926  1.00 44.85           C  
ANISOU 6043  C   ALA B 210     6822   5141   5079    431   -495  -1028       C  
ATOM   6044  O   ALA B 210      11.097  -4.679 -42.875  1.00 53.75           O  
ANISOU 6044  O   ALA B 210     7944   6214   6265    366   -542  -1045       O  
ATOM   6045  CB  ALA B 210      13.698  -4.282 -40.905  1.00 44.27           C  
ANISOU 6045  CB  ALA B 210     6709   5026   5087    311   -355   -853       C  
ATOM   6046  N   PHE B 211      13.039  -4.497 -44.006  1.00 43.87           N  
ANISOU 6046  N   PHE B 211     6697   5157   4816    550   -465  -1036       N  
ATOM   6047  CA  PHE B 211      12.360  -4.013 -45.202  1.00 47.96           C  
ANISOU 6047  CA  PHE B 211     7215   5766   5243    613   -495  -1072       C  
ATOM   6048  C   PHE B 211      11.549  -5.117 -45.859  1.00 38.18           C  
ANISOU 6048  C   PHE B 211     6016   4467   4023    666   -623  -1225       C  
ATOM   6049  O   PHE B 211      10.536  -4.830 -46.504  1.00 62.43           O  
ANISOU 6049  O   PHE B 211     9086   7560   7075    671   -674  -1264       O  
ATOM   6050  CB  PHE B 211      13.351  -3.443 -46.215  1.00 49.66           C  
ANISOU 6050  CB  PHE B 211     7418   6154   5297    735   -431  -1039       C  
ATOM   6051  CG  PHE B 211      12.698  -2.928 -47.479  1.00 46.08           C  
ANISOU 6051  CG  PHE B 211     6965   5807   4737    810   -459  -1069       C  
ATOM   6052  CD1 PHE B 211      12.224  -1.627 -47.546  1.00 44.99           C  
ANISOU 6052  CD1 PHE B 211     6794   5723   4577    758   -405   -965       C  
ATOM   6053  CD2 PHE B 211      12.555  -3.743 -48.596  1.00 52.67           C  
ANISOU 6053  CD2 PHE B 211     7834   6686   5491    938   -543  -1203       C  
ATOM   6054  CE1 PHE B 211      11.632  -1.145 -48.700  1.00 56.37           C  
ANISOU 6054  CE1 PHE B 211     8237   7265   5918    831   -431   -986       C  
ATOM   6055  CE2 PHE B 211      11.958  -3.266 -49.753  1.00 56.41           C  
ANISOU 6055  CE2 PHE B 211     8308   7266   5860   1013   -571  -1230       C  
ATOM   6056  CZ  PHE B 211      11.498  -1.964 -49.804  1.00 54.65           C  
ANISOU 6056  CZ  PHE B 211     8051   7098   5614    958   -513  -1118       C  
ATOM   6057  N   LYS B 212      11.976  -6.384 -45.721  1.00 42.00           N  
ANISOU 6057  N   LYS B 212     6536   4875   4549    708   -681  -1317       N  
ATOM   6058  CA  LYS B 212      11.254  -7.486 -46.364  1.00 44.52           C  
ANISOU 6058  CA  LYS B 212     6895   5128   4894    762   -811  -1472       C  
ATOM   6059  C   LYS B 212      10.022  -7.885 -45.566  1.00 53.23           C  
ANISOU 6059  C   LYS B 212     7997   6070   6159    629   -880  -1490       C  
ATOM   6060  O   LYS B 212       9.037  -8.360 -46.140  1.00 50.58           O  
ANISOU 6060  O   LYS B 212     7675   5691   5850    641   -983  -1594       O  
ATOM   6061  CB  LYS B 212      12.161  -8.697 -46.578  1.00 44.22           C  
ANISOU 6061  CB  LYS B 212     6898   5064   4841    865   -855  -1570       C  
ATOM   6062  CG  LYS B 212      13.040  -8.592 -47.793  1.00 52.11           C  
ANISOU 6062  CG  LYS B 212     7904   6229   5665   1033   -833  -1613       C  
ATOM   6063  CD  LYS B 212      13.917  -9.820 -47.917  1.00 61.78           C  
ANISOU 6063  CD  LYS B 212     9169   7420   6884   1135   -879  -1714       C  
ATOM   6064  CE  LYS B 212      14.656  -9.843 -49.247  1.00 71.31           C  
ANISOU 6064  CE  LYS B 212    10385   8798   7910   1319   -874  -1780       C  
ATOM   6065  NZ  LYS B 212      15.522 -11.048 -49.334  1.00 76.63           N  
ANISOU 6065  NZ  LYS B 212    11097   9437   8581   1424   -920  -1884       N  
ATOM   6066  N   ALA B 213      10.027  -7.633 -44.257  1.00 41.91           N  
ANISOU 6066  N   ALA B 213     6540   4554   4830    501   -822  -1386       N  
ATOM   6067  CA  ALA B 213       8.836  -7.906 -43.460  1.00 46.21           C  
ANISOU 6067  CA  ALA B 213     7074   4961   5524    371   -874  -1385       C  
ATOM   6068  C   ALA B 213       7.725  -6.896 -43.752  1.00 41.75           C  
ANISOU 6068  C   ALA B 213     6474   4446   4945    321   -870  -1351       C  
ATOM   6069  O   ALA B 213       6.541  -7.253 -43.781  1.00 40.71           O  
ANISOU 6069  O   ALA B 213     6337   4237   4895    267   -953  -1408       O  
ATOM   6070  CB  ALA B 213       9.197  -7.912 -41.971  1.00 39.20           C  
ANISOU 6070  CB  ALA B 213     6171   3986   4738    259   -809  -1281       C  
ATOM   6071  N   TRP B 214       8.092  -5.631 -43.989  1.00 37.42           N  
ANISOU 6071  N   TRP B 214     5899   4024   4296    339   -778  -1257       N  
ATOM   6072  CA  TRP B 214       7.099  -4.574 -44.193  1.00 39.61           C  
ANISOU 6072  CA  TRP B 214     6142   4347   4560    292   -766  -1211       C  
ATOM   6073  C   TRP B 214       6.362  -4.751 -45.521  1.00 37.95           C  
ANISOU 6073  C   TRP B 214     5946   4193   4282    380   -856  -1320       C  
ATOM   6074  O   TRP B 214       5.130  -4.658 -45.576  1.00 43.32           O  
ANISOU 6074  O   TRP B 214     6608   4833   5018    325   -915  -1349       O  
ATOM   6075  CB  TRP B 214       7.796  -3.210 -44.136  1.00 36.08           C  
ANISOU 6075  CB  TRP B 214     5667   4016   4026    296   -646  -1081       C  
ATOM   6076  CG  TRP B 214       6.864  -2.023 -44.124  1.00 35.56           C  
ANISOU 6076  CG  TRP B 214     5565   3984   3960    236   -621  -1013       C  
ATOM   6077  CD1 TRP B 214       5.884  -1.745 -45.032  1.00 36.58           C  
ANISOU 6077  CD1 TRP B 214     5692   4159   4049    271   -679  -1063       C  
ATOM   6078  CD2 TRP B 214       6.836  -0.950 -43.168  1.00 43.17           C  
ANISOU 6078  CD2 TRP B 214     6494   4942   4967    139   -535   -886       C  
ATOM   6079  NE1 TRP B 214       5.243  -0.579 -44.700  1.00 44.35           N  
ANISOU 6079  NE1 TRP B 214     6639   5162   5049    202   -634   -973       N  
ATOM   6080  CE2 TRP B 214       5.807  -0.069 -43.561  1.00 42.21           C  
ANISOU 6080  CE2 TRP B 214     6349   4859   4830    121   -546   -866       C  
ATOM   6081  CE3 TRP B 214       7.576  -0.650 -42.019  1.00 42.23           C  
ANISOU 6081  CE3 TRP B 214     6360   4789   4897     70   -454   -793       C  
ATOM   6082  CZ2 TRP B 214       5.500   1.088 -42.850  1.00 50.47           C  
ANISOU 6082  CZ2 TRP B 214     7360   5907   5911     38   -480   -759       C  
ATOM   6083  CZ3 TRP B 214       7.267   0.503 -41.313  1.00 45.69           C  
ANISOU 6083  CZ3 TRP B 214     6762   5230   5367    -14   -391   -690       C  
ATOM   6084  CH2 TRP B 214       6.241   1.358 -41.734  1.00 47.21           C  
ANISOU 6084  CH2 TRP B 214     6935   5458   5546    -27   -404   -675       C  
ATOM   6085  N   ALA B 215       7.111  -4.997 -46.601  1.00 49.93           N  
ANISOU 6085  N   ALA B 215     7491   5809   5671    520   -868  -1383       N  
ATOM   6086  CA  ALA B 215       6.530  -5.242 -47.919  1.00 40.51           C  
ANISOU 6086  CA  ALA B 215     6315   4680   4395    623   -958  -1499       C  
ATOM   6087  C   ALA B 215       5.677  -6.502 -47.939  1.00 40.81           C  
ANISOU 6087  C   ALA B 215     6376   4588   4543    604  -1094  -1638       C  
ATOM   6088  O   ALA B 215       4.663  -6.550 -48.642  1.00 51.65           O  
ANISOU 6088  O   ALA B 215     7746   5972   5909    623  -1179  -1717       O  
ATOM   6089  CB  ALA B 215       7.641  -5.350 -48.964  1.00 40.78           C  
ANISOU 6089  CB  ALA B 215     6375   4849   4270    784   -937  -1536       C  
ATOM   6090  N   VAL B 216       6.083  -7.548 -47.214  1.00 43.89           N  
ANISOU 6090  N   VAL B 216     6788   4855   5033    570  -1120  -1672       N  
ATOM   6091  CA  VAL B 216       5.248  -8.746 -47.159  1.00 48.12           C  
ANISOU 6091  CA  VAL B 216     7342   5249   5692    537  -1250  -1794       C  
ATOM   6092  C   VAL B 216       3.897  -8.411 -46.544  1.00 44.94           C  
ANISOU 6092  C   VAL B 216     6897   4768   5409    398  -1274  -1755       C  
ATOM   6093  O   VAL B 216       2.845  -8.793 -47.070  1.00 50.77           O  
ANISOU 6093  O   VAL B 216     7632   5471   6189    394  -1380  -1852       O  
ATOM   6094  CB  VAL B 216       5.952  -9.881 -46.391  1.00 46.64           C  
ANISOU 6094  CB  VAL B 216     7186   4934   5600    518  -1266  -1818       C  
ATOM   6095  CG1 VAL B 216       4.944 -10.952 -46.008  1.00 48.03           C  
ANISOU 6095  CG1 VAL B 216     7368   4937   5944    436  -1385  -1901       C  
ATOM   6096  CG2 VAL B 216       7.056 -10.494 -47.233  1.00 43.69           C  
ANISOU 6096  CG2 VAL B 216     6859   4626   5116    678  -1286  -1908       C  
ATOM   6097  N   ALA B 217       3.902  -7.665 -45.438  1.00 43.69           N  
ANISOU 6097  N   ALA B 217     6704   4590   5306    285  -1176  -1614       N  
ATOM   6098  CA  ALA B 217       2.646  -7.296 -44.794  1.00 42.35           C  
ANISOU 6098  CA  ALA B 217     6488   4358   5245    155  -1188  -1569       C  
ATOM   6099  C   ALA B 217       1.841  -6.331 -45.655  1.00 43.51           C  
ANISOU 6099  C   ALA B 217     6609   4614   5309    187  -1199  -1573       C  
ATOM   6100  O   ALA B 217       0.618  -6.473 -45.776  1.00 46.89           O  
ANISOU 6100  O   ALA B 217     7011   4998   5807    137  -1277  -1622       O  
ATOM   6101  CB  ALA B 217       2.920  -6.689 -43.418  1.00 44.19           C  
ANISOU 6101  CB  ALA B 217     6692   4558   5541     42  -1078  -1422       C  
ATOM   6102  N   ARG B 218       2.506  -5.346 -46.264  1.00 43.02           N  
ANISOU 6102  N   ARG B 218     6549   4696   5099    270  -1122  -1518       N  
ATOM   6103  CA  ARG B 218       1.788  -4.351 -47.056  1.00 43.99           C  
ANISOU 6103  CA  ARG B 218     6648   4927   5139    303  -1124  -1505       C  
ATOM   6104  C   ARG B 218       1.263  -4.945 -48.358  1.00 52.17           C  
ANISOU 6104  C   ARG B 218     7705   6001   6115    408  -1245  -1654       C  
ATOM   6105  O   ARG B 218       0.124  -4.672 -48.754  1.00 53.48           O  
ANISOU 6105  O   ARG B 218     7846   6179   6296    391  -1305  -1689       O  
ATOM   6106  CB  ARG B 218       2.692  -3.152 -47.341  1.00 41.56           C  
ANISOU 6106  CB  ARG B 218     6338   4757   4696    362  -1008  -1395       C  
ATOM   6107  CG  ARG B 218       1.997  -2.008 -48.070  1.00 43.24           C  
ANISOU 6107  CG  ARG B 218     6526   5078   4825    391   -998  -1359       C  
ATOM   6108  CD  ARG B 218       0.733  -1.569 -47.344  1.00 46.47           C  
ANISOU 6108  CD  ARG B 218     6890   5417   5349    268  -1012  -1320       C  
ATOM   6109  NE  ARG B 218      -0.130  -0.754 -48.194  1.00 53.55           N  
ANISOU 6109  NE  ARG B 218     7768   6404   6176    309  -1040  -1324       N  
ATOM   6110  CZ  ARG B 218      -1.450  -0.669 -48.060  1.00 58.99           C  
ANISOU 6110  CZ  ARG B 218     8421   7050   6942    245  -1101  -1351       C  
ATOM   6111  NH1 ARG B 218      -2.067  -1.351 -47.105  1.00 66.24           N  
ANISOU 6111  NH1 ARG B 218     9317   7838   8012    132  -1138  -1373       N  
ATOM   6112  NH2 ARG B 218      -2.154   0.098 -48.881  1.00 47.42           N  
ANISOU 6112  NH2 ARG B 218     6939   5676   5402    295  -1125  -1353       N  
ATOM   6113  N   LEU B 219       2.076  -5.754 -49.042  1.00 47.67           N  
ANISOU 6113  N   LEU B 219     7182   5455   5476    522  -1283  -1747       N  
ATOM   6114  CA  LEU B 219       1.639  -6.326 -50.313  1.00 58.91           C  
ANISOU 6114  CA  LEU B 219     8628   6923   6832    635  -1402  -1898       C  
ATOM   6115  C   LEU B 219       0.535  -7.356 -50.107  1.00 59.69           C  
ANISOU 6115  C   LEU B 219     8721   6876   7082    564  -1535  -2012       C  
ATOM   6116  O   LEU B 219      -0.373  -7.472 -50.939  1.00 65.51           O  
ANISOU 6116  O   LEU B 219     9451   7639   7800    604  -1635  -2111       O  
ATOM   6117  CB  LEU B 219       2.823  -6.946 -51.052  1.00 52.68           C  
ANISOU 6117  CB  LEU B 219     7889   6199   5929    782  -1409  -1973       C  
ATOM   6118  CG  LEU B 219       3.462  -6.083 -52.142  1.00 50.04           C  
ANISOU 6118  CG  LEU B 219     7561   6062   5391    921  -1348  -1940       C  
ATOM   6119  CD1 LEU B 219       4.245  -4.931 -51.533  1.00 58.05           C  
ANISOU 6119  CD1 LEU B 219     8550   7142   6364    877  -1192  -1759       C  
ATOM   6120  CD2 LEU B 219       4.354  -6.926 -53.039  1.00 56.25           C  
ANISOU 6120  CD2 LEU B 219     8394   6909   6068   1079  -1392  -2057       C  
ATOM   6121  N   SER B 220       0.594  -8.114 -49.010  1.00 56.68           N  
ANISOU 6121  N   SER B 220     8341   6342   6854    459  -1540  -1997       N  
ATOM   6122  CA  SER B 220      -0.489  -9.038 -48.696  1.00 60.82           C  
ANISOU 6122  CA  SER B 220     8850   6718   7541    371  -1657  -2082       C  
ATOM   6123  C   SER B 220      -1.771  -8.308 -48.327  1.00 68.64           C  
ANISOU 6123  C   SER B 220     9778   7702   8600    260  -1656  -2022       C  
ATOM   6124  O   SER B 220      -2.860  -8.867 -48.496  1.00 68.13           O  
ANISOU 6124  O   SER B 220     9691   7564   8632    216  -1768  -2110       O  
ATOM   6125  CB  SER B 220      -0.073  -9.978 -47.565  1.00 54.18           C  
ANISOU 6125  CB  SER B 220     8022   5719   6844    283  -1651  -2060       C  
ATOM   6126  OG  SER B 220       1.268 -10.407 -47.732  1.00 53.98           O  
ANISOU 6126  OG  SER B 220     8049   5717   6744    381  -1619  -2078       O  
ATOM   6127  N   GLN B 221      -1.667  -7.076 -47.825  1.00 68.52           N  
ANISOU 6127  N   GLN B 221     9731   7760   8542    215  -1534  -1877       N  
ATOM   6128  CA  GLN B 221      -2.858  -6.263 -47.610  1.00 63.32           C  
ANISOU 6128  CA  GLN B 221     9015   7118   7925    134  -1531  -1825       C  
ATOM   6129  C   GLN B 221      -3.492  -5.862 -48.935  1.00 55.93           C  
ANISOU 6129  C   GLN B 221     8075   6296   6881    233  -1601  -1906       C  
ATOM   6130  O   GLN B 221      -4.717  -5.921 -49.089  1.00 60.43           O  
ANISOU 6130  O   GLN B 221     8605   6838   7518    187  -1683  -1956       O  
ATOM   6131  CB  GLN B 221      -2.505  -5.020 -46.793  1.00 60.20           C  
ANISOU 6131  CB  GLN B 221     8594   6776   7503     77  -1387  -1657       C  
ATOM   6132  CG  GLN B 221      -2.413  -5.250 -45.297  1.00 60.62           C  
ANISOU 6132  CG  GLN B 221     8627   6713   7693    -57  -1328  -1568       C  
ATOM   6133  CD  GLN B 221      -2.414  -3.951 -44.515  1.00 62.15           C  
ANISOU 6133  CD  GLN B 221     8784   6956   7873   -121  -1208  -1420       C  
ATOM   6134  OE1 GLN B 221      -2.239  -2.872 -45.082  1.00 64.44           O  
ANISOU 6134  OE1 GLN B 221     9072   7364   8046    -60  -1156  -1373       O  
ATOM   6135  NE2 GLN B 221      -2.608  -4.049 -43.206  1.00 63.10           N  
ANISOU 6135  NE2 GLN B 221     8876   6986   8114   -243  -1165  -1344       N  
ATOM   6136  N   ARG B 222      -2.670  -5.457 -49.905  1.00 58.21           N  
ANISOU 6136  N   ARG B 222     8401   6718   6999    372  -1572  -1918       N  
ATOM   6137  CA  ARG B 222      -3.192  -5.005 -51.189  1.00 69.94           C  
ANISOU 6137  CA  ARG B 222     9885   8328   8362    479  -1630  -1984       C  
ATOM   6138  C   ARG B 222      -3.573  -6.174 -52.088  1.00 80.66           C  
ANISOU 6138  C   ARG B 222    11268   9655   9726    555  -1784  -2170       C  
ATOM   6139  O   ARG B 222      -4.576  -6.104 -52.807  1.00 86.91           O  
ANISOU 6139  O   ARG B 222    12037  10482  10502    582  -1876  -2249       O  
ATOM   6140  CB  ARG B 222      -2.164  -4.117 -51.887  1.00 73.90           C  
ANISOU 6140  CB  ARG B 222    10413   8991   8674    600  -1535  -1915       C  
ATOM   6141  CG  ARG B 222      -1.798  -2.860 -51.118  1.00 76.96           C  
ANISOU 6141  CG  ARG B 222    10775   9416   9050    534  -1390  -1735       C  
ATOM   6142  CD  ARG B 222      -1.067  -1.892 -52.021  1.00 84.90           C  
ANISOU 6142  CD  ARG B 222    11797  10591   9871    655  -1317  -1672       C  
ATOM   6143  NE  ARG B 222      -0.485  -0.762 -51.306  1.00 96.57           N  
ANISOU 6143  NE  ARG B 222    13257  12097  11337    599  -1177  -1503       N  
ATOM   6144  CZ  ARG B 222       0.822  -0.544 -51.198  1.00101.71           C  
ANISOU 6144  CZ  ARG B 222    13929  12797  11920    639  -1082  -1429       C  
ATOM   6145  NH1 ARG B 222       1.683  -1.382 -51.758  1.00102.65           N  
ANISOU 6145  NH1 ARG B 222    14086  12945  11969    738  -1106  -1509       N  
ATOM   6146  NH2 ARG B 222       1.267   0.513 -50.532  1.00101.05           N  
ANISOU 6146  NH2 ARG B 222    13824  12732  11839    580   -965  -1280       N  
ATOM   6147  N   PHE B 223      -2.787  -7.252 -52.066  1.00 75.59           N  
ANISOU 6147  N   PHE B 223    10672   8945   9105    595  -1818  -2248       N  
ATOM   6148  CA  PHE B 223      -3.015  -8.426 -52.907  1.00 73.42           C  
ANISOU 6148  CA  PHE B 223    10429   8631   8838    676  -1968  -2435       C  
ATOM   6149  C   PHE B 223      -3.242  -9.649 -52.024  1.00 75.69           C  
ANISOU 6149  C   PHE B 223    10718   8717   9324    566  -2037  -2486       C  
ATOM   6150  O   PHE B 223      -2.376 -10.531 -51.932  1.00 79.91           O  
ANISOU 6150  O   PHE B 223    11300   9190   9873    609  -2052  -2539       O  
ATOM   6151  CB  PHE B 223      -1.843  -8.668 -53.857  1.00 66.54           C  
ANISOU 6151  CB  PHE B 223     9616   7868   7798    851  -1962  -2500       C  
ATOM   6152  CG  PHE B 223      -1.414  -7.450 -54.622  1.00 70.86           C  
ANISOU 6152  CG  PHE B 223    10163   8614   8148    955  -1871  -2420       C  
ATOM   6153  CD1 PHE B 223      -2.350  -6.568 -55.138  1.00 73.31           C  
ANISOU 6153  CD1 PHE B 223    10436   9012   8404    960  -1885  -2398       C  
ATOM   6154  CD2 PHE B 223      -0.069  -7.190 -54.831  1.00 66.60           C  
ANISOU 6154  CD2 PHE B 223     9655   8173   7478   1050  -1771  -2362       C  
ATOM   6155  CE1 PHE B 223      -1.952  -5.448 -55.842  1.00 70.18           C  
ANISOU 6155  CE1 PHE B 223    10040   8794   7831   1056  -1802  -2314       C  
ATOM   6156  CE2 PHE B 223       0.334  -6.072 -55.536  1.00 66.74           C  
ANISOU 6156  CE2 PHE B 223     9667   8371   7318   1142  -1686  -2278       C  
ATOM   6157  CZ  PHE B 223      -0.609  -5.200 -56.042  1.00 66.63           C  
ANISOU 6157  CZ  PHE B 223     9623   8439   7256   1144  -1701  -2251       C  
ATOM   6158  N   PRO B 224      -4.401  -9.741 -51.364  1.00 72.75           N  
ANISOU 6158  N   PRO B 224    10292   8241   9109    426  -2080  -2470       N  
ATOM   6159  CA  PRO B 224      -4.674 -10.928 -50.545  1.00 73.93           C  
ANISOU 6159  CA  PRO B 224    10439   8198   9455    317  -2149  -2511       C  
ATOM   6160  C   PRO B 224      -5.144 -12.123 -51.353  1.00 80.87           C  
ANISOU 6160  C   PRO B 224    11339   9000  10386    371  -2325  -2706       C  
ATOM   6161  O   PRO B 224      -5.096 -13.249 -50.840  1.00 85.87           O  
ANISOU 6161  O   PRO B 224    11989   9473  11166    313  -2389  -2757       O  
ATOM   6162  CB  PRO B 224      -5.763 -10.444 -49.581  1.00 75.03           C  
ANISOU 6162  CB  PRO B 224    10502   8277   9727    151  -2118  -2407       C  
ATOM   6163  CG  PRO B 224      -6.478  -9.374 -50.336  1.00 75.77           C  
ANISOU 6163  CG  PRO B 224    10561   8514   9713    197  -2117  -2400       C  
ATOM   6164  CD  PRO B 224      -5.532  -8.797 -51.361  1.00 74.35           C  
ANISOU 6164  CD  PRO B 224    10432   8499   9320    364  -2072  -2413       C  
ATOM   6165  N   LYS B 225      -5.589 -11.919 -52.594  1.00 82.06           N  
ANISOU 6165  N   LYS B 225    11492   9261  10425    483  -2408  -2817       N  
ATOM   6166  CA  LYS B 225      -5.995 -13.023 -53.452  1.00 89.57           C  
ANISOU 6166  CA  LYS B 225    12453  10167  11414    547  -2554  -2981       C  
ATOM   6167  C   LYS B 225      -4.812 -13.759 -54.065  1.00 89.68           C  
ANISOU 6167  C   LYS B 225    12533  10207  11335    691  -2561  -3054       C  
ATOM   6168  O   LYS B 225      -4.999 -14.854 -54.607  1.00 95.21           O  
ANISOU 6168  O   LYS B 225    13232  10853  12092    732  -2651  -3149       O  
ATOM   6169  CB  LYS B 225      -6.921 -12.516 -54.562  1.00 96.12           C  
ANISOU 6169  CB  LYS B 225    13248  11120  12151    617  -2625  -3050       C  
ATOM   6170  CG  LYS B 225      -8.382 -12.887 -54.358  1.00 99.43           C  
ANISOU 6170  CG  LYS B 225    13588  11450  12741    493  -2704  -3061       C  
ATOM   6171  CD  LYS B 225      -9.207 -12.623 -55.606  1.00102.31           C  
ANISOU 6171  CD  LYS B 225    13925  11933  13014    586  -2791  -3154       C  
ATOM   6172  CE  LYS B 225     -10.309 -11.611 -55.334  1.00100.10           C  
ANISOU 6172  CE  LYS B 225    13580  11696  12758    498  -2784  -3095       C  
ATOM   6173  NZ  LYS B 225     -11.432 -11.738 -56.303  1.00 99.43           N  
ANISOU 6173  NZ  LYS B 225    13445  11663  12669    539  -2892  -3185       N  
ATOM   6174  N   ALA B 226      -3.613 -13.189 -54.000  1.00 78.94           N  
ANISOU 6174  N   ALA B 226    11228   8930   9834    770  -2469  -3014       N  
ATOM   6175  CA  ALA B 226      -2.418 -13.896 -54.432  1.00 79.07           C  
ANISOU 6175  CA  ALA B 226    11302   8968   9773    899  -2462  -3070       C  
ATOM   6176  C   ALA B 226      -1.938 -14.834 -53.335  1.00 76.36           C  
ANISOU 6176  C   ALA B 226    10973   8447   9595    804  -2444  -3029       C  
ATOM   6177  O   ALA B 226      -2.092 -14.562 -52.141  1.00 69.97           O  
ANISOU 6177  O   ALA B 226    10145   7541   8900    659  -2387  -2925       O  
ATOM   6178  CB  ALA B 226      -1.302 -12.916 -54.794  1.00 79.38           C  
ANISOU 6178  CB  ALA B 226    11377   9185   9598   1019  -2345  -3008       C  
ATOM   6179  N   GLU B 227      -1.354 -15.952 -53.752  1.00 74.15           N  
ANISOU 6179  N   GLU B 227    10723   8126   9325    889  -2494  -3111       N  
ATOM   6180  CA  GLU B 227      -0.793 -16.883 -52.790  1.00 78.13           C  
ANISOU 6180  CA  GLU B 227    11245   8472   9969    819  -2478  -3074       C  
ATOM   6181  C   GLU B 227       0.505 -16.321 -52.215  1.00 73.47           C  
ANISOU 6181  C   GLU B 227    10703   7927   9286    853  -2360  -2998       C  
ATOM   6182  O   GLU B 227       1.087 -15.363 -52.733  1.00 68.50           O  
ANISOU 6182  O   GLU B 227    10098   7460   8470    956  -2298  -2991       O  
ATOM   6183  CB  GLU B 227      -0.555 -18.246 -53.440  1.00 78.86           C  
ANISOU 6183  CB  GLU B 227    11358   8509  10098    909  -2573  -3188       C  
ATOM   6184  CG  GLU B 227      -1.779 -18.818 -54.138  1.00 79.58           C  
ANISOU 6184  CG  GLU B 227    11405   8566  10267    895  -2697  -3278       C  
ATOM   6185  CD  GLU B 227      -2.848 -19.283 -53.166  1.00 83.44           C  
ANISOU 6185  CD  GLU B 227    11840   8883  10980    703  -2728  -3218       C  
ATOM   6186  OE1 GLU B 227      -2.538 -19.444 -51.967  1.00 83.35           O  
ANISOU 6186  OE1 GLU B 227    11831   8761  11077    592  -2664  -3115       O  
ATOM   6187  OE2 GLU B 227      -4.