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***  HYDROLASE 06-MAY-09 2WHP  ***

elNémo ID: 21072721440329528

Job options:

ID        	=	 21072721440329528
JOBID     	=	 HYDROLASE 06-MAY-09 2WHP
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE                               06-MAY-09   2WHP              
TITLE     CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY SARIN AND
TITLE    2 IN COMPLEX WITH HI-6                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-573;                         
COMPND   5 SYNONYM: ACHE;                                                       
COMPND   6 EC: 3.1.1.7;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: CATALYTIC SER203 PHOSPHONYLATED BY SARIN;             
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: ACETYLCHOLINESTERASE;                                      
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 32-573;                         
COMPND  13 SYNONYM: ACHE;                                                       
COMPND  14 EC: 3.1.1.7;                                                         
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 OTHER_DETAILS: CATALYTIC SER203 PHOSPHONYLATED BY SARIN              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: MOUSE;                                              
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   7 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK) 293 CELLS; 
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: HUMAN EMBRYONIC KIDNEY (HEK) 293 CELLS; 
SOURCE  16 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    SERINE ESTERASE, ALTERNATIVE SPLICING, NEUROTRANSMITTER DEGRADATION,  
KEYWDS   2 HI-6, SARIN, SYNAPSE, MEMBRANE, SECRETED, HYDROLASE, CELL MEMBRANE,  
KEYWDS   3 DISULFIDE BOND, CHOLINESTERASE, GPI-ANCHOR, LIPOPROTEIN,             
KEYWDS   4 GLYCOPROTEIN, CELL JUNCTION                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.EKSTROM,A.HORNBERG,E.ARTURSSON,L.G.HAMMARSTROM,G.SCHNEIDER,Y.P.PANG 
REVDAT   3   29-JUL-20 2WHP    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE                                     
REVDAT   2   17-JAN-18 2WHP    1       REMARK                                   
REVDAT   1   30-JUN-09 2WHP    0                                                
JRNL        AUTH   F.EKSTROM,A.HORNBERG,E.ARTURSSON,L.G.HAMMARSTROM,            
JRNL        AUTH 2 G.SCHNEIDER,Y.P.PANG                                         
JRNL        TITL   STRUCTURE OF HI-6SARIN-ACETYLCHOLINESTERASE DETERMINED BY    
JRNL        TITL 2 X-RAY CRYSTALLOGRAPHY AND MOLECULAR DYNAMICS SIMULATION:     
JRNL        TITL 3 REACTIVATOR MECHANISM AND DESIGN.                            
JRNL        REF    PLOS ONE                      V.   4 E5957 2009              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   19536291                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0005957                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.99                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 102274                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.176                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.210                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2048                            
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 28.9907 -  5.4147    0.97     6945   138  0.1864 0.2137        
REMARK   3     2  5.4147 -  4.3023    1.00     6855   134  0.1306 0.1637        
REMARK   3     3  4.3023 -  3.7598    0.99     6758   135  0.1337 0.1594        
REMARK   3     4  3.7598 -  3.4166    0.99     6748   145  0.1463 0.1859        
REMARK   3     5  3.4166 -  3.1720    0.99     6715   117  0.1592 0.2016        
REMARK   3     6  3.1720 -  2.9852    0.99     6681   149  0.1623 0.1776        
REMARK   3     7  2.9852 -  2.8358    0.99     6682   133  0.1582 0.2053        
REMARK   3     8  2.8358 -  2.7125    0.99     6658   134  0.1682 0.2195        
REMARK   3     9  2.7125 -  2.6081    0.99     6615   154  0.1712 0.2331        
REMARK   3    10  2.6081 -  2.5182    0.99     6651   138  0.1785 0.2170        
REMARK   3    11  2.5182 -  2.4395    0.99     6616   117  0.2023 0.2349        
REMARK   3    12  2.4395 -  2.3698    0.99     6589   128  0.2286 0.2741        
REMARK   3    13  2.3698 -  2.3074    0.99     6601   137  0.2403 0.2690        
REMARK   3    14  2.3074 -  2.2512    0.99     6570   127  0.2586 0.2908        
REMARK   3    15  2.2512 -  2.2000    0.99     6542   162  0.2964 0.3149        
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              : 0.35                                          
REMARK   3   B_SOL              : 71.36                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.300            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.210           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 38.88                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.98570                                             
REMARK   3    B22 (A**2) : -0.86950                                             
REMARK   3    B33 (A**2) : 3.85530                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.013           8699                                  
REMARK   3   ANGLE     :  1.425          11877                                  
REMARK   3   CHIRALITY :  0.091           1276                                  
REMARK   3   PLANARITY :  0.007           1559                                  
REMARK   3   DIHEDRAL  : 18.957           3103                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  27.3150  12.4802  16.5628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0942 T22:   0.0867                                     
REMARK   3      T33:   0.1216 T12:  -0.0058                                     
REMARK   3      T13:  -0.0047 T23:   0.0246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4396 L22:   0.4712                                     
REMARK   3      L33:   1.3064 L12:  -0.0938                                     
REMARK   3      L13:   0.1721 L23:  -0.1490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0366 S12:   0.0268 S13:   0.0000                       
REMARK   3      S21:   0.0268 S22:   0.0218 S23:  -0.0174                       
REMARK   3      S31:   0.0992 S32:  -0.0558 S33:   0.0097                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.6118   4.6970 -40.3581              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1620 T22:   0.1676                                     
REMARK   3      T33:   0.1756 T12:  -0.0078                                     
REMARK   3      T13:  -0.0349 T23:  -0.0470                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3902 L22:   0.6654                                     
REMARK   3      L33:   1.7643 L12:  -0.0664                                     
REMARK   3      L13:   0.2802 L23:   0.4484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1063 S12:   0.0459 S13:  -0.0294                       
REMARK   3      S21:   0.0655 S22:  -0.0680 S23:   0.0576                       
REMARK   3      S31:   0.1588 S32:  -0.0106 S33:  -0.0289                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN W                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.0285   9.3524  -6.8962              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0925 T22:   0.0990                                     
REMARK   3      T33:   0.1082 T12:  -0.0022                                     
REMARK   3      T13:   0.0096 T23:  -0.0007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1118 L22:   0.0983                                     
REMARK   3      L33:   0.4020 L12:  -0.0399                                     
REMARK   3      L13:   0.1859 L23:   0.0316                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0027 S12:   0.0121 S13:  -0.0432                       
REMARK   3      S21:   0.0067 S22:  -0.0066 S23:   0.0010                       
REMARK   3      S31:   0.0481 S32:   0.0191 S33:  -0.0075                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: RESIDUES 258-264 ARE DISORDERED           
REMARK   4                                                                      
REMARK   4 2WHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAY-09.                  
REMARK 100 THE DEPOSITION ID IS D_1290039643.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.041                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 102346                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.46000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 5.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1J06                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26-30 % (V/V) PEG750MME 0.1 M HEPES PH   
REMARK 280  7.0                                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       39.63000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      113.47500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.07500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      113.47500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.63000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.07500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
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     PRO A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     GLY A   263                                                      
REMARK 465     GLY A   264                                                      
REMARK 465     ARG A   493                                                      
REMARK 465     ASP A   494                                                      
REMARK 465     SER A   495                                                      
REMARK 465     LYS A   496                                                      
REMARK 465     THR A   543                                                      
REMARK 465     ALA A   544                                                      
REMARK 465     THR A   545                                                      
REMARK 465     GLU A   546                                                      
REMARK 465     ALA A   547                                                      
REMARK 465     PRO A   548                                                      
REMARK 465     GLU B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     ARG B     3                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     GLY B   263                                                      
REMARK 465     GLY B   264                                                      
REMARK 465     SER B   495                                                      
REMARK 465     LYS B   496                                                      
REMARK 465     SER B   497                                                      
REMARK 465     THR B   543                                                      
REMARK 465     ALA B   544                                                      
REMARK 465     THR B   545                                                      
REMARK 465     GLU B   546                                                      
REMARK 465     ALA B   547                                                      
REMARK 465     PRO B   548                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  81    CG   CD   OE1  OE2                                  
REMARK 470     GLU B   4    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 268    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 323    CG   OD1  OD2                                       
REMARK 470     ARG B 493    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG B   296     O    HOH B  2215              2.04            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH1  ARG A    13     O    SER B    57     2555     2.12            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  47       -2.35     74.19                                   
REMARK 500    ALA A  62       50.49   -113.83                                   
REMARK 500    PHE A 158       -6.28   -141.93                                   
REMARK 500    ALA A 167       68.04   -157.30                                   
REMARK 500    SGB A 203     -121.17     58.17                                   
REMARK 500    ASP A 306      -90.86   -122.15                                   
REMARK 500    HIS A 387       62.79   -153.11                                   
REMARK 500    VAL A 407      -61.95   -135.93                                   
REMARK 500    ARG A 525       51.95     37.82                                   
REMARK 500    PHE B  47      -10.69     76.01                                   
REMARK 500    CYS B  96       11.38   -141.17                                   
REMARK 500    SGB B 203     -123.83     55.49                                   
REMARK 500    ASP B 306      -86.93   -128.44                                   
REMARK 500    VAL B 407      -63.52   -126.33                                   
REMARK 500    HIS B 447      130.95    -36.96                                   
REMARK 500    SER B 462       -7.74    -59.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2050        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH A2051        DISTANCE =  7.06 ANGSTROMS                       
REMARK 525    HOH A2065        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH A2067        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A2102        DISTANCE =  7.21 ANGSTROMS                       
REMARK 525    HOH A2103        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH A2132        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH A2172        DISTANCE =  6.85 ANGSTROMS                       
REMARK 525    HOH A2197        DISTANCE =  6.22 ANGSTROMS                       
REMARK 525    HOH A2239        DISTANCE =  7.29 ANGSTROMS                       
REMARK 525    HOH B2001        DISTANCE =  7.33 ANGSTROMS                       
REMARK 525    HOH B2032        DISTANCE =  6.89 ANGSTROMS                       
REMARK 525    HOH B2058        DISTANCE =  7.38 ANGSTROMS                       
REMARK 525    HOH B2078        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH B2114        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH B2167        DISTANCE =  6.07 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     HI6 A 1543                                                       
REMARK 610     HI6 B 1543                                                       
REMARK 610     P6G B 1545                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2WHQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE, PHOSPHONYLATED BY SARIN   
REMARK 900 (AGED) IN COMPLEX WITH HI-6                                          
REMARK 900 RELATED ID: 2JGH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED VX                                                              
REMARK 900 RELATED ID: 1MAH   RELATED DB: PDB                                   
REMARK 900 FASCICULIN2 - MOUSE ACETYLCHOLINESTERASE COMPLEX                     
REMARK 900 RELATED ID: 1MAA   RELATED DB: PDB                                   
REMARK 900 MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATEDPROTEIN     
REMARK 900 RELATED ID: 2HA6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE       
REMARK 900 COMPLEXED WITH SUCCINYLCHOLINE                                       
REMARK 900 RELATED ID: 2JGG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED SARIN                                                           
REMARK 900 RELATED ID: 2C0Q   RELATED DB: PDB                                   
REMARK 900 NON-AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN       
REMARK 900 RELATED ID: 2JGL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 VX AND SARIN                                                         
REMARK 900 RELATED ID: 1Q84   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-TZ2PA6ANTI       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 2JGM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 DIISOPROPYL FLUOROPHOSPHATE (DFP)                                    
REMARK 900 RELATED ID: 2JGE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED METHAMIDOPHOS                                                   
REMARK 900 RELATED ID: 1Q83   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-TZ2PA6SYN        
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1C2B   RELATED DB: PDB                                   
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                        
REMARK 900 RELATED ID: 2HA3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH        
REMARK 900 CHOLINE                                                              
REMARK 900 RELATED ID: 2HA0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH 4-     
REMARK 900 KETOAMYLTRIMETHYLAMMONIUM                                            
REMARK 900 RELATED ID: 2JEY   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH HLO-7              
REMARK 900 RELATED ID: 2JGI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED DIISOPROPYL FLUOROPHOSPHATE (DFP)                               
REMARK 900 RELATED ID: 1N5R   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-PROPIDIUM        
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 2JGJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 METHAMIDOPHOS                                                        
REMARK 900 RELATED ID: 1J06   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE IN THE APOFORM       
REMARK 900 RELATED ID: 2JF0   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN AND ORTHO-7  
REMARK 900 RELATED ID: 2C0P   RELATED DB: PDB                                   
REMARK 900 AGED FORM OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY TABUN           
REMARK 900 RELATED ID: 2H9Y   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH M-(N,  
REMARK 900 N,N-TRIMETHYLAMMONIO) TRIFLUOROACETOPHENONE                          
REMARK 900 RELATED ID: 2WHR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ACETYLCHOLINESTERASE IN COMPLEX WITH K027       
REMARK 900 RELATED ID: 1N5M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-GALLAMINE        
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 2HA5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF ACETYLCHOLINESTERASECOMPLEXED   
REMARK 900 WITH ACETYLTHIOCHOLINE                                               
REMARK 900 RELATED ID: 2HA2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE COMPLEXEDWITH        
REMARK 900 SUCCINYLCHOLINE                                                      
REMARK 900 RELATED ID: 2JEZ   RELATED DB: PDB                                   
REMARK 900 MUS MUSCULUS ACETYLCHOLINESTERASE IN COMPLEX WITH TABUN AND HLO-7    
REMARK 900 RELATED ID: 2JGK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY AGED    
REMARK 900 FENAMIPHOS                                                           
REMARK 900 RELATED ID: 1KU6   RELATED DB: PDB                                   
REMARK 900 FASCICULIN 2-MOUSE ACETYLCHOLINESTERASE COMPLEX                      
REMARK 900 RELATED ID: 2HA4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE       
REMARK 900 COMPLEXED WITH ACETYLCHOLINE                                         
REMARK 900 RELATED ID: 1J07   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MOUSE ACETYLCHOLINESTERASE-DECIDIUM COMPLEX 
REMARK 900 RELATED ID: 2HA7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MUTANT S203A OF MOUSEACETYLCHOLINESTERASE       
REMARK 900 COMPLEXED WITH BUTYRYLTHIOCHOLINE                                    
REMARK 900 RELATED ID: 2JGF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MOUSE ACETYLCHOLINESTERASE INHIBITED BY NON-    
REMARK 900 AGED FENAMIPHOS                                                      
REMARK 900 RELATED ID: 1C2O   RELATED DB: PDB                                   
REMARK 900 ELECTROPHORUS ELECTRICUS ACETYLCHOLINESTERASE                        
DBREF  2WHP A    1   542  UNP    P21836   ACES_MOUSE      32    573             
DBREF  2WHP A  543   548  PDB    2WHP     2WHP           543    548             
DBREF  2WHP B    1   542  UNP    P21836   ACES_MOUSE      32    573             
DBREF  2WHP B  543   548  PDB    2WHP     2WHP           543    548             
SEQADV 2WHP ASP B  499  UNP  P21836    GLN   531 CONFLICT                       
SEQRES   1 A  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 A  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 A  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 A  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 A  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 A  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 A  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 A  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 A  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 A  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 A  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 A  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 A  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 A  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 A  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 A  548  SER VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER          
SEQRES  17 A  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 A  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 A  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 A  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 A  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 A  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 A  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 A  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 A  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 A  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 A  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 A  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 A  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 A  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 A  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 A  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 A  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 A  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 A  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 A  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 A  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 A  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 A  548  SER LYS SER PRO GLN TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 A  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 A  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 A  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 A  548  ALA PRO                                                      
SEQRES   1 B  548  GLU GLY ARG GLU ASP PRO GLN LEU LEU VAL ARG VAL ARG          
SEQRES   2 B  548  GLY GLY GLN LEU ARG GLY ILE ARG LEU LYS ALA PRO GLY          
SEQRES   3 B  548  GLY PRO VAL SER ALA PHE LEU GLY ILE PRO PHE ALA GLU          
SEQRES   4 B  548  PRO PRO VAL GLY SER ARG ARG PHE MET PRO PRO GLU PRO          
SEQRES   5 B  548  LYS ARG PRO TRP SER GLY VAL LEU ASP ALA THR THR PHE          
SEQRES   6 B  548  GLN ASN VAL CYS TYR GLN TYR VAL ASP THR LEU TYR PRO          
SEQRES   7 B  548  GLY PHE GLU GLY THR GLU MET TRP ASN PRO ASN ARG GLU          
SEQRES   8 B  548  LEU SER GLU ASP CYS LEU TYR LEU ASN VAL TRP THR PRO          
SEQRES   9 B  548  TYR PRO ARG PRO ALA SER PRO THR PRO VAL LEU ILE TRP          
SEQRES  10 B  548  ILE TYR GLY GLY GLY PHE TYR SER GLY ALA ALA SER LEU          
SEQRES  11 B  548  ASP VAL TYR ASP GLY ARG PHE LEU ALA GLN VAL GLU GLY          
SEQRES  12 B  548  ALA VAL LEU VAL SER MET ASN TYR ARG VAL GLY THR PHE          
SEQRES  13 B  548  GLY PHE LEU ALA LEU PRO GLY SER ARG GLU ALA PRO GLY          
SEQRES  14 B  548  ASN VAL GLY LEU LEU ASP GLN ARG LEU ALA LEU GLN TRP          
SEQRES  15 B  548  VAL GLN GLU ASN ILE ALA ALA PHE GLY GLY ASP PRO MET          
SEQRES  16 B  548  SER VAL THR LEU PHE GLY GLU SGB ALA GLY ALA ALA SER          
SEQRES  17 B  548  VAL GLY MET HIS ILE LEU SER LEU PRO SER ARG SER LEU          
SEQRES  18 B  548  PHE HIS ARG ALA VAL LEU GLN SER GLY THR PRO ASN GLY          
SEQRES  19 B  548  PRO TRP ALA THR VAL SER ALA GLY GLU ALA ARG ARG ARG          
SEQRES  20 B  548  ALA THR LEU LEU ALA ARG LEU VAL GLY CYS PRO PRO GLY          
SEQRES  21 B  548  GLY ALA GLY GLY ASN ASP THR GLU LEU ILE ALA CYS LEU          
SEQRES  22 B  548  ARG THR ARG PRO ALA GLN ASP LEU VAL ASP HIS GLU TRP          
SEQRES  23 B  548  HIS VAL LEU PRO GLN GLU SER ILE PHE ARG PHE SER PHE          
SEQRES  24 B  548  VAL PRO VAL VAL ASP GLY ASP PHE LEU SER ASP THR PRO          
SEQRES  25 B  548  GLU ALA LEU ILE ASN THR GLY ASP PHE GLN ASP LEU GLN          
SEQRES  26 B  548  VAL LEU VAL GLY VAL VAL LYS ASP GLU GLY SER TYR PHE          
SEQRES  27 B  548  LEU VAL TYR GLY VAL PRO GLY PHE SER LYS ASP ASN GLU          
SEQRES  28 B  548  SER LEU ILE SER ARG ALA GLN PHE LEU ALA GLY VAL ARG          
SEQRES  29 B  548  ILE GLY VAL PRO GLN ALA SER ASP LEU ALA ALA GLU ALA          
SEQRES  30 B  548  VAL VAL LEU HIS TYR THR ASP TRP LEU HIS PRO GLU ASP          
SEQRES  31 B  548  PRO THR HIS LEU ARG ASP ALA MET SER ALA VAL VAL GLY          
SEQRES  32 B  548  ASP HIS ASN VAL VAL CYS PRO VAL ALA GLN LEU ALA GLY          
SEQRES  33 B  548  ARG LEU ALA ALA GLN GLY ALA ARG VAL TYR ALA TYR ILE          
SEQRES  34 B  548  PHE GLU HIS ARG ALA SER THR LEU THR TRP PRO LEU TRP          
SEQRES  35 B  548  MET GLY VAL PRO HIS GLY TYR GLU ILE GLU PHE ILE PHE          
SEQRES  36 B  548  GLY LEU PRO LEU ASP PRO SER LEU ASN TYR THR THR GLU          
SEQRES  37 B  548  GLU ARG ILE PHE ALA GLN ARG LEU MET LYS TYR TRP THR          
SEQRES  38 B  548  ASN PHE ALA ARG THR GLY ASP PRO ASN ASP PRO ARG ASP          
SEQRES  39 B  548  SER LYS SER PRO ASP TRP PRO PRO TYR THR THR ALA ALA          
SEQRES  40 B  548  GLN GLN TYR VAL SER LEU ASN LEU LYS PRO LEU GLU VAL          
SEQRES  41 B  548  ARG ARG GLY LEU ARG ALA GLN THR CYS ALA PHE TRP ASN          
SEQRES  42 B  548  ARG PHE LEU PRO LYS LEU LEU SER ALA THR ALA THR GLU          
SEQRES  43 B  548  ALA PRO                                                      
MODRES 2WHP ASN A  350  ASN  GLYCOSYLATION SITE                                 
MODRES 2WHP ASN A  464  ASN  GLYCOSYLATION SITE                                 
MODRES 2WHP ASN B  350  ASN  GLYCOSYLATION SITE                                 
MODRES 2WHP SGB A  203  SER                                                     
MODRES 2WHP SGB B  203  SER                                                     
HET    SGB  A 203      13                                                       
HET    SGB  B 203      13                                                       
HET    NAG  A 601      14                                                       
HET    NAG  A 701      14                                                       
HET    HI6  A1543      18                                                       
HET    CO3  A1544       4                                                       
HET    NAG  B 601      14                                                       
HET    HI6  B1543      18                                                       
HET    PEG  B1544       7                                                       
HET    P6G  B1545      15                                                       
HETNAM     SGB O-[(S)-METHYL(1-METHYLETHOXY)PHOSPHORYL]-L-SERINE                
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     HI6 4-(AMINOCARBONYL)-1-[({2-[(E)-(HYDROXYIMINO)                     
HETNAM   2 HI6  METHYL]PYRIDINIUM-1-YL}METHOXY)METHYL]PYRIDINIUM                
HETNAM     CO3 CARBONATE ION                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     P6G HEXAETHYLENE GLYCOL                                              
HETSYN     HI6 1-(2-HYDROXY-IMINOMETHYLPYRIDINIUM)-1-(4-CARBOXYAMINO)-          
HETSYN   2 HI6  PYRIDINIUM DIMETHYLETHER                                        
HETSYN     P6G POLYETHYLENE GLYCOL PEG400                                       
FORMUL   1  SGB    2(C7 H16 N O5 P)                                             
FORMUL   3  NAG    3(C8 H15 N O6)                                               
FORMUL   5  HI6    2(C14 H16 N4 O3 2+)                                          
FORMUL   6  CO3    C O3 2-                                                      
FORMUL   9  PEG    C4 H10 O3                                                    
FORMUL  10  P6G    C12 H26 O7                                                   
FORMUL  11  HOH   *793(H2 O)                                                    
HELIX    1   1 ASP A    5  GLN A    7  5                                   3    
HELIX    2   2 VAL A   42  ARG A   46  5                                   5    
HELIX    3   3 PHE A   80  MET A   85  1                                   6    
HELIX    4   4 LEU A  130  ASP A  134  5                                   5    
HELIX    5   5 GLY A  135  GLY A  143  1                                   9    
HELIX    6   6 VAL A  153  LEU A  159  1                                   7    
HELIX    7   7 ASN A  170  ILE A  187  1                                  18    
HELIX    8   8 ALA A  188  PHE A  190  5                                   3    
HELIX    9   9 ALA A  204  LEU A  214  1                                  11    
HELIX   10  10 SER A  215  SER A  220  1                                   6    
HELIX   11  11 SER A  240  VAL A  255  1                                  16    
HELIX   12  12 ASN A  265  ARG A  276  1                                  12    
HELIX   13  13 PRO A  277  TRP A  286  1                                  10    
HELIX   14  14 HIS A  287  LEU A  289  5                                   3    
HELIX   15  15 THR A  311  GLY A  319  1                                   9    
HELIX   16  16 GLY A  335  VAL A  343  1                                   9    
HELIX   17  17 SER A  355  VAL A  367  1                                  13    
HELIX   18  18 SER A  371  THR A  383  1                                  13    
HELIX   19  19 ASP A  390  VAL A  407  1                                  18    
HELIX   20  20 VAL A  407  GLN A  421  1                                  15    
HELIX   21  21 PRO A  440  GLY A  444  5                                   5    
HELIX   22  22 GLU A  450  PHE A  455  1                                   6    
HELIX   23  23 GLY A  456  ASP A  460  5                                   5    
HELIX   24  24 ASP A  460  ASN A  464  5                                   5    
HELIX   25  25 THR A  466  GLY A  487  1                                  22    
HELIX   26  26 ARG A  525  ARG A  534  1                                  10    
HELIX   27  27 ARG A  534  SER A  541  1                                   8    
HELIX   28  28 ASP B    5  GLN B    7  5                                   3    
HELIX   29  29 VAL B   42  ARG B   46  5                                   5    
HELIX   30  30 PHE B   80  MET B   85  1                                   6    
HELIX   31  31 LEU B  130  ASP B  134  5                                   5    
HELIX   32  32 GLY B  135  GLY B  143  1                                   9    
HELIX   33  33 VAL B  153  LEU B  159  1                                   7    
HELIX   34  34 ASN B  170  ILE B  187  1                                  18    
HELIX   35  35 ALA B  188  PHE B  190  5                                   3    
HELIX   36  36 ALA B  204  SER B  215  1                                  12    
HELIX   37  37 SER B  215  SER B  220  1                                   6    
HELIX   38  38 ALA B  241  VAL B  255  1                                  15    
HELIX   39  39 ASN B  265  THR B  275  1                                  11    
HELIX   40  40 PRO B  277  TRP B  286  1                                  10    
HELIX   41  41 HIS B  287  LEU B  289  5                                   3    
HELIX   42  42 THR B  311  GLY B  319  1                                   9    
HELIX   43  43 GLY B  335  VAL B  340  1                                   6    
HELIX   44  44 SER B  355  VAL B  367  1                                  13    
HELIX   45  45 SER B  371  THR B  383  1                                  13    
HELIX   46  46 ASP B  390  VAL B  407  1                                  18    
HELIX   47  47 VAL B  407  GLN B  421  1                                  15    
HELIX   48  48 PRO B  440  GLY B  444  5                                   5    
HELIX   49  49 GLU B  450  PHE B  455  1                                   6    
HELIX   50  50 GLY B  456  ASP B  460  5                                   5    
HELIX   51  51 ASP B  460  ASN B  464  5                                   5    
HELIX   52  52 THR B  466  GLY B  487  1                                  22    
HELIX   53  53 ARG B  525  ARG B  534  1                                  10    
HELIX   54  54 ARG B  534  ALA B  542  1                                   9    
SHEET    1  AA 3 LEU A   9  VAL A  12  0                                        
SHEET    2  AA 3 GLY A  15  ARG A  18 -1  O  GLY A  15   N  VAL A  12           
SHEET    3  AA 3 VAL A  59  ASP A  61  1  O  LEU A  60   N  ARG A  18           
SHEET    1  AB11 ILE A  20  ALA A  24  0                                        
SHEET    2  AB11 GLY A  27  PRO A  36 -1  O  GLY A  27   N  ALA A  24           
SHEET    3  AB11 TYR A  98  PRO A 104 -1  O  LEU A  99   N  ILE A  35           
SHEET    4  AB11 VAL A 145  MET A 149 -1  O  LEU A 146   N  TRP A 102           
SHEET    5  AB11 THR A 112  ILE A 118  1  O  PRO A 113   N  VAL A 145           
SHEET    6  AB11 GLY A 192  GLY A 201  1  N  ASP A 193   O  THR A 112           
SHEET    7  AB11 ARG A 224  GLN A 228  1  O  ARG A 224   N  LEU A 199           
SHEET    8  AB11 GLN A 325  VAL A 331  1  O  GLN A 325   N  ALA A 225           
SHEET    9  AB11 ARG A 424  PHE A 430  1  O  ARG A 424   N  VAL A 326           
SHEET   10  AB11 GLN A 509  LEU A 513  1  O  VAL A 511   N  ILE A 429           
SHEET   11  AB11 GLU A 519  ARG A 522 -1  O  GLU A 519   N  SER A 512           
SHEET    1  AC 2 VAL A  68  CYS A  69  0                                        
SHEET    2  AC 2 LEU A  92  SER A  93  1  N  SER A  93   O  VAL A  68           
SHEET    1  BA 3 LEU B   9  VAL B  12  0                                        
SHEET    2  BA 3 GLY B  15  ARG B  18 -1  O  GLY B  15   N  VAL B  12           
SHEET    3  BA 3 VAL B  59  ASP B  61  1  O  LEU B  60   N  ARG B  18           
SHEET    1  BB11 ILE B  20  ALA B  24  0                                        
SHEET    2  BB11 GLY B  27  PRO B  36 -1  O  GLY B  27   N  ALA B  24           
SHEET    3  BB11 TYR B  98  PRO B 104 -1  O  LEU B  99   N  ILE B  35           
SHEET    4  BB11 VAL B 145  MET B 149 -1  O  LEU B 146   N  TRP B 102           
SHEET    5  BB11 THR B 112  ILE B 118  1  O  PRO B 113   N  VAL B 145           
SHEET    6  BB11 GLY B 192  GLY B 201  1  N  ASP B 193   O  THR B 112           
SHEET    7  BB11 ARG B 224  GLN B 228  1  O  ARG B 224   N  LEU B 199           
SHEET    8  BB11 GLN B 325  VAL B 331  1  O  GLN B 325   N  ALA B 225           
SHEET    9  BB11 ARG B 424  PHE B 430  1  O  ARG B 424   N  VAL B 326           
SHEET   10  BB11 GLN B 509  LEU B 513  1  O  VAL B 511   N  ILE B 429           
SHEET   11  BB11 GLU B 519  ARG B 522 -1  O  GLU B 519   N  SER B 512           
SHEET    1  BC 2 VAL B  68  CYS B  69  0                                        
SHEET    2  BC 2 LEU B  92  SER B  93  1  N  SER B  93   O  VAL B  68           
SHEET    1  BD 2 VAL B 239  SER B 240  0                                        
SHEET    2  BD 2 VAL B 302  VAL B 303  1  N  VAL B 303   O  VAL B 239           
SSBOND   1 CYS A   69    CYS A   96                          1555   1555  2.03  
SSBOND   2 CYS A  257    CYS A  272                          1555   1555  2.11  
SSBOND   3 CYS A  409    CYS A  529                          1555   1555  2.04  
SSBOND   4 CYS B   69    CYS B   96                          1555   1555  2.04  
SSBOND   5 CYS B  257    CYS B  272                          1555   1555  2.06  
SSBOND   6 CYS B  409    CYS B  529                          1555   1555  2.05  
LINK         C   GLU A 202                 N   SGB A 203     1555   1555  1.33  
LINK         C   SGB A 203                 N   ALA A 204     1555   1555  1.32  
LINK         ND2 ASN A 350                 C1  NAG A 601     1555   1555  1.46  
LINK         ND2 ASN A 464                 C1  NAG A 701     1555   1555  1.45  
LINK         C   GLU B 202                 N   SGB B 203     1555   1555  1.33  
LINK         C   SGB B 203                 N   ALA B 204     1555   1555  1.33  
LINK         ND2 ASN B 350                 C1  NAG B 601     1555   1555  1.46  
CISPEP   1 TYR A  105    PRO A  106          0        -0.91                     
CISPEP   2 SER A  541    ALA A  542          0        12.34                     
CISPEP   3 TYR B  105    PRO B  106          0         3.14                     
CRYST1   79.260  112.150  226.950  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012617  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008917  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004406        0.00000                         
ATOM      1  N   GLU A   1      30.662  15.690  54.202  1.00 95.52           N  
ANISOU    1  N   GLU A   1    13166  12057  11071    784   -431     70       N  
ATOM      2  CA  GLU A   1      29.894  14.620  54.844  1.00 88.74           C  
ANISOU    2  CA  GLU A   1    12322  11243  10150    793   -364    121       C  
ATOM      3  C   GLU A   1      29.731  14.857  56.339  1.00 82.95           C  
ANISOU    3  C   GLU A   1    11667  10544   9305    848   -371    106       C  
ATOM      4  O   GLU A   1      30.710  14.905  57.093  1.00 78.53           O  
ANISOU    4  O   GLU A   1    11155   9969   8712    864   -440     92       O  
ATOM      5  CB  GLU A   1      30.502  13.229  54.592  1.00 78.75           C  
ANISOU    5  CB  GLU A   1    11042   9964   8918    757   -367    178       C  
ATOM      6  CG  GLU A   1      29.803  12.138  55.379  1.00 68.40           C  
ANISOU    6  CG  GLU A   1     9764   8691   7535    761   -308    234       C  
ATOM      7  CD  GLU A   1      29.747  10.811  54.659  1.00 66.90           C  
ANISOU    7  CD  GLU A   1     9544   8483   7392    712   -273    294       C  
ATOM      8  OE1 GLU A   1      28.696  10.115  54.772  1.00 59.54           O  
ANISOU    8  OE1 GLU A   1     8612   7584   6427    692   -199    338       O  
ATOM      9  OE2 GLU A   1      30.757  10.472  53.993  1.00 66.94           O  
ANISOU    9  OE2 GLU A   1     9528   8444   7462    694   -321    298       O  
ATOM     10  N   GLY A   2      28.470  14.986  56.740  1.00 75.83           N  
ANISOU   10  N   GLY A   2    10773   9695   8343    878   -297    110       N  
ATOM     11  CA  GLY A   2      28.081  15.300  58.098  1.00 64.33           C  
ANISOU   11  CA  GLY A   2     9387   8282   6773    938   -286     93       C  
ATOM     12  C   GLY A   2      26.808  16.088  57.923  1.00 65.48           C  
ANISOU   12  C   GLY A   2     9513   8469   6896    975   -221     69       C  
ATOM     13  O   GLY A   2      25.713  15.620  58.241  1.00 59.07           O  
ANISOU   13  O   GLY A   2     8687   7726   6032    986   -138    105       O  
ATOM     14  N   ARG A   3      26.977  17.274  57.341  1.00 74.70           N  
ANISOU   14  N   ARG A   3    10677   9597   8108    990   -259     10       N  
ATOM     15  CA  ARG A   3      25.905  18.242  57.114  1.00 73.35           C  
ANISOU   15  CA  ARG A   3    10496   9454   7919   1039   -213    -25       C  
ATOM     16  C   ARG A   3      25.437  18.265  55.668  1.00 67.45           C  
ANISOU   16  C   ARG A   3     9663   8697   7269    997   -181    -11       C  
ATOM     17  O   ARG A   3      24.619  19.079  55.303  1.00 70.57           O  
ANISOU   17  O   ARG A   3    10041   9110   7664   1036   -149    -39       O  
ATOM     18  CB  ARG A   3      26.388  19.639  57.504  1.00 77.85           C  
ANISOU   18  CB  ARG A   3    11141   9976   8463   1090   -284   -104       C  
ATOM     19  CG  ARG A   3      25.880  20.129  58.860  1.00 84.86           C  
ANISOU   19  CG  ARG A   3    12109  10908   9224   1176   -268   -137       C  
ATOM     20  CD  ARG A   3      26.630  19.516  60.036  1.00 84.73           C  
ANISOU   20  CD  ARG A   3    12155  10899   9138   1176   -307   -124       C  
ATOM     21  NE  ARG A   3      25.834  19.458  61.274  1.00 83.24           N  
ANISOU   21  NE  ARG A   3    12019  10785   8823   1247   -253   -123       N  
ATOM     22  CZ  ARG A   3      24.506  19.312  61.336  1.00 74.85           C  
ANISOU   22  CZ  ARG A   3    10920   9804   7716   1284   -154    -99       C  
ATOM     23  NH1 ARG A   3      23.778  19.207  60.225  1.00 75.81           N  
ANISOU   23  NH1 ARG A   3    10953   9943   7911   1256    -98    -74       N  
ATOM     24  NH2 ARG A   3      23.903  19.259  62.518  1.00 60.52           N  
ANISOU   24  NH2 ARG A   3     9154   8061   5780   1348   -109    -98       N  
ATOM     25  N   GLU A   4      25.964  17.356  54.862  1.00 65.47           N  
ANISOU   25  N   GLU A   4     9360   8418   7097    924   -189     32       N  
ATOM     26  CA  GLU A   4      25.767  17.339  53.424  1.00 58.82           C  
ANISOU   26  CA  GLU A   4     8441   7556   6353    877   -173     44       C  
ATOM     27  C   GLU A   4      24.528  16.539  53.119  1.00 53.83           C  
ANISOU   27  C   GLU A   4     7748   6992   5712    858    -81     96       C  
ATOM     28  O   GLU A   4      24.036  15.817  53.969  1.00 56.81           O  
ANISOU   28  O   GLU A   4     8142   7424   6019    864    -35    132       O  
ATOM     29  CB  GLU A   4      26.950  16.623  52.791  1.00 68.90           C  
ANISOU   29  CB  GLU A   4     9696   8777   7706    812   -224     68       C  
ATOM     30  CG  GLU A   4      27.554  17.318  51.614  1.00 82.34           C  
ANISOU   30  CG  GLU A   4    11364  10422   9501    783   -271     39       C  
ATOM     31  CD  GLU A   4      29.059  17.220  51.639  1.00 89.65           C  
ANISOU   31  CD  GLU A   4    12307  11294  10460    755   -355     31       C  
ATOM     32  OE1 GLU A   4      29.572  16.089  51.793  1.00 90.10           O  
ANISOU   32  OE1 GLU A   4    12358  11354  10521    729   -358     73       O  
ATOM     33  OE2 GLU A   4      29.725  18.276  51.526  1.00 91.95           O  
ANISOU   33  OE2 GLU A   4    12621  11544  10772    759   -419    -16       O  
ATOM     34  N   ASP A   5      24.039  16.643  51.892  1.00 48.76           N  
ANISOU   34  N   ASP A   5     7036   6349   5140    827    -55    103       N  
ATOM     35  CA  ASP A   5      22.848  15.916  51.471  1.00 42.74           C  
ANISOU   35  CA  ASP A   5     6207   5654   4377    798     28    152       C  
ATOM     36  C   ASP A   5      23.234  14.463  51.265  1.00 45.06           C  
ANISOU   36  C   ASP A   5     6488   5932   4699    722     34    212       C  
ATOM     37  O   ASP A   5      23.978  14.155  50.366  1.00 43.71           O  
ANISOU   37  O   ASP A   5     6298   5703   4607    675     -2    216       O  
ATOM     38  CB  ASP A   5      22.302  16.527  50.177  1.00 37.14           C  
ANISOU   38  CB  ASP A   5     5432   4944   3737    789     42    138       C  
ATOM     39  CG  ASP A   5      21.138  15.754  49.602  1.00 42.63           C  
ANISOU   39  CG  ASP A   5     6049   5708   4439    746    118    189       C  
ATOM     40  OD1 ASP A   5      20.894  14.634  50.065  1.00 46.80           O  
ANISOU   40  OD1 ASP A   5     6576   6271   4934    705    154    240       O  
ATOM     41  OD2 ASP A   5      20.449  16.266  48.685  1.00 44.57           O  
ANISOU   41  OD2 ASP A   5     6236   5976   4722    750    140    180       O  
ATOM     42  N   PRO A   6      22.715  13.559  52.101  1.00 55.68           N  
ANISOU   42  N   PRO A   6     7850   7331   5977    711     83    259       N  
ATOM     43  CA  PRO A   6      23.115  12.146  52.058  1.00 55.21           C  
ANISOU   43  CA  PRO A   6     7800   7246   5933    644     85    317       C  
ATOM     44  C   PRO A   6      22.770  11.483  50.722  1.00 50.17           C  
ANISOU   44  C   PRO A   6     7096   6594   5373    570    110    348       C  
ATOM     45  O   PRO A   6      23.315  10.432  50.365  1.00 44.82           O  
ANISOU   45  O   PRO A   6     6430   5870   4731    517     96    384       O  
ATOM     46  CB  PRO A   6      22.272  11.533  53.187  1.00 58.90           C  
ANISOU   46  CB  PRO A   6     8291   7789   6301    649    147    361       C  
ATOM     47  CG  PRO A   6      21.044  12.451  53.223  1.00 55.42           C  
ANISOU   47  CG  PRO A   6     7803   7431   5822    695    202    338       C  
ATOM     48  CD  PRO A   6      21.685  13.790  53.132  1.00 55.08           C  
ANISOU   48  CD  PRO A   6     7784   7342   5800    761    141    264       C  
ATOM     49  N   GLN A   7      21.863  12.088  49.969  1.00 49.36           N  
ANISOU   49  N   GLN A   7     6928   6532   5295    571    145    335       N  
ATOM     50  CA  GLN A   7      21.485  11.486  48.699  1.00 46.63           C  
ANISOU   50  CA  GLN A   7     6519   6179   5018    500    167    363       C  
ATOM     51  C   GLN A   7      22.470  11.735  47.574  1.00 46.03           C  
ANISOU   51  C   GLN A   7     6432   6022   5035    484    109    335       C  
ATOM     52  O   GLN A   7      22.291  11.174  46.511  1.00 49.18           O  
ANISOU   52  O   GLN A   7     6789   6406   5490    426    121    356       O  
ATOM     53  CB  GLN A   7      20.094  11.931  48.252  1.00 63.25           C  
ANISOU   53  CB  GLN A   7     8549   8367   7114    501    227    366       C  
ATOM     54  CG  GLN A   7      18.994  10.872  48.450  1.00 77.38           C  
ANISOU   54  CG  GLN A   7    10306  10232   8862    439    298    431       C  
ATOM     55  CD  GLN A   7      18.121  11.127  49.678  1.00 81.73           C  
ANISOU   55  CD  GLN A   7    10860  10880   9311    486    351    443       C  
ATOM     56  OE1 GLN A   7      17.826  10.201  50.446  1.00 81.71           O  
ANISOU   56  OE1 GLN A   7    10882  10912   9252    449    386    494       O  
ATOM     57  NE2 GLN A   7      17.689  12.384  49.855  1.00 74.51           N  
ANISOU   57  NE2 GLN A   7     9927  10013   8372    571    359    396       N  
ATOM     58  N   LEU A   8      23.501  12.557  47.801  1.00 40.82           N  
ANISOU   58  N   LEU A   8     5809   5312   4388    531     46    288       N  
ATOM     59  CA  LEU A   8      24.435  12.960  46.728  1.00 41.47           C  
ANISOU   59  CA  LEU A   8     5874   5329   4555    517     -8    260       C  
ATOM     60  C   LEU A   8      25.871  12.414  46.891  1.00 41.05           C  
ANISOU   60  C   LEU A   8     5862   5211   4525    507    -68    263       C  
ATOM     61  O   LEU A   8      26.797  12.849  46.199  1.00 42.56           O  
ANISOU   61  O   LEU A   8     6041   5356   4776    504   -119    238       O  
ATOM     62  CB  LEU A   8      24.482  14.498  46.608  1.00 40.25           C  
ANISOU   62  CB  LEU A   8     5717   5167   4409    571    -37    202       C  
ATOM     63  CG  LEU A   8      23.146  15.181  46.229  1.00 39.85           C  
ANISOU   63  CG  LEU A   8     5619   5175   4346    594     14    194       C  
ATOM     64  CD1 LEU A   8      23.208  16.692  46.371  1.00 34.81           C  
ANISOU   64  CD1 LEU A   8     5005   4522   3699    661    -17    136       C  
ATOM     65  CD2 LEU A   8      22.700  14.767  44.814  1.00 31.31           C  
ANISOU   65  CD2 LEU A   8     4466   4096   3333    536     39    217       C  
ATOM     66  N   LEU A   9      26.067  11.488  47.818  1.00 36.56           N  
ANISOU   66  N   LEU A   9     5340   4647   3905    506    -63    297       N  
ATOM     67  CA  LEU A   9      27.410  10.962  48.055  1.00 34.53           C  
ANISOU   67  CA  LEU A   9     5122   4338   3662    508   -121    302       C  
ATOM     68  C   LEU A   9      27.409   9.544  47.544  1.00 37.62           C  
ANISOU   68  C   LEU A   9     5511   4705   4076    458    -97    353       C  
ATOM     69  O   LEU A   9      26.573   8.756  47.952  1.00 37.25           O  
ANISOU   69  O   LEU A   9     5482   4687   3986    433    -47    394       O  
ATOM     70  CB  LEU A   9      27.767  10.997  49.545  1.00 35.77           C  
ANISOU   70  CB  LEU A   9     5344   4507   3738    553   -144    299       C  
ATOM     71  CG  LEU A   9      27.602  12.386  50.220  1.00 50.81           C  
ANISOU   71  CG  LEU A   9     7267   6437   5601    608   -162    246       C  
ATOM     72  CD1 LEU A   9      27.646  12.340  51.795  1.00 43.43           C  
ANISOU   72  CD1 LEU A   9     6404   5530   4568    653   -169    248       C  
ATOM     73  CD2 LEU A   9      28.613  13.408  49.678  1.00 37.07           C  
ANISOU   73  CD2 LEU A   9     5516   4652   3918    617   -233    196       C  
ATOM     74  N   VAL A  10      28.339   9.235  46.642  1.00 36.68           N  
ANISOU   74  N   VAL A  10     5377   4537   4024    442   -134    350       N  
ATOM     75  CA  VAL A  10      28.434   7.933  45.999  1.00 35.03           C  
ANISOU   75  CA  VAL A  10     5174   4294   3843    400   -118    391       C  
ATOM     76  C   VAL A  10      29.926   7.532  45.839  1.00 41.60           C  
ANISOU   76  C   VAL A  10     6023   5076   4707    424   -179    388       C  
ATOM     77  O   VAL A  10      30.812   8.391  45.683  1.00 41.98           O  
ANISOU   77  O   VAL A  10     6048   5119   4785    451   -229    351       O  
ATOM     78  CB  VAL A  10      27.725   7.967  44.611  1.00 40.65           C  
ANISOU   78  CB  VAL A  10     5826   5007   4614    352    -83    389       C  
ATOM     79  CG1 VAL A  10      27.894   6.662  43.873  1.00 43.77           C  
ANISOU   79  CG1 VAL A  10     6236   5358   5038    310    -74    424       C  
ATOM     80  CG2 VAL A  10      26.231   8.270  44.779  1.00 41.21           C  
ANISOU   80  CG2 VAL A  10     5870   5139   4649    331    -23    398       C  
ATOM     81  N   ARG A  11      30.195   6.232  45.879  1.00 33.77           N  
ANISOU   81  N   ARG A  11     5074   4050   3706    413   -174    428       N  
ATOM     82  CA  ARG A  11      31.537   5.713  45.728  1.00 33.09           C  
ANISOU   82  CA  ARG A  11     5005   3923   3643    445   -226    431       C  
ATOM     83  C   ARG A  11      31.639   4.913  44.435  1.00 39.00           C  
ANISOU   83  C   ARG A  11     5739   4632   4449    415   -212    444       C  
ATOM     84  O   ARG A  11      30.778   4.091  44.163  1.00 40.01           O  
ANISOU   84  O   ARG A  11     5890   4744   4567    371   -166    475       O  
ATOM     85  CB  ARG A  11      31.920   4.811  46.913  1.00 31.54           C  
ANISOU   85  CB  ARG A  11     4887   3714   3383    475   -240    467       C  
ATOM     86  CG  ARG A  11      33.289   4.114  46.684  1.00 34.18           C  
ANISOU   86  CG  ARG A  11     5238   4009   3741    516   -291    475       C  
ATOM     87  CD  ARG A  11      33.797   3.357  47.876  1.00 35.53           C  
ANISOU   87  CD  ARG A  11     5485   4169   3848    559   -317    508       C  
ATOM     88  NE  ARG A  11      34.130   4.207  49.015  1.00 34.82           N  
ANISOU   88  NE  ARG A  11     5399   4119   3710    595   -354    486       N  
ATOM     89  CZ  ARG A  11      35.344   4.678  49.260  1.00 42.15           C  
ANISOU   89  CZ  ARG A  11     6307   5060   4647    641   -421    462       C  
ATOM     90  NH1 ARG A  11      35.547   5.430  50.334  1.00 44.62           N  
ANISOU   90  NH1 ARG A  11     6635   5409   4910    667   -455    442       N  
ATOM     91  NH2 ARG A  11      36.345   4.435  48.408  1.00 38.51           N  
ANISOU   91  NH2 ARG A  11     5808   4582   4242    659   -454    457       N  
ATOM     92  N   VAL A  12      32.689   5.160  43.650  1.00 34.77           N  
ANISOU   92  N   VAL A  12     5163   4081   3967    437   -251    421       N  
ATOM     93  CA  VAL A  12      32.982   4.370  42.474  1.00 26.94           C  
ANISOU   93  CA  VAL A  12     4164   3050   3022    424   -243    431       C  
ATOM     94  C   VAL A  12      34.374   3.752  42.623  1.00 35.10           C  
ANISOU   94  C   VAL A  12     5220   4060   4057    482   -292    439       C  
ATOM     95  O   VAL A  12      35.061   3.994  43.639  1.00 34.45           O  
ANISOU   95  O   VAL A  12     5153   3995   3941    525   -332    437       O  
ATOM     96  CB  VAL A  12      32.836   5.181  41.169  1.00 29.49           C  
ANISOU   96  CB  VAL A  12     4411   3386   3409    395   -235    399       C  
ATOM     97  CG1 VAL A  12      31.390   5.578  40.986  1.00 30.63           C  
ANISOU   97  CG1 VAL A  12     4537   3554   3547    344   -185    399       C  
ATOM     98  CG2 VAL A  12      33.734   6.442  41.200  1.00 30.98           C  
ANISOU   98  CG2 VAL A  12     4545   3604   3623    424   -283    362       C  
ATOM     99  N   ARG A  13      34.760   2.921  41.651  1.00 32.35           N  
ANISOU   99  N   ARG A  13     4877   3674   3742    487   -287    447       N  
ATOM    100  CA  ARG A  13      36.015   2.161  41.742  1.00 39.97           C  
ANISOU  100  CA  ARG A  13     5867   4616   4703    552   -326    459       C  
ATOM    101  C   ARG A  13      37.193   3.083  42.130  1.00 37.03           C  
ANISOU  101  C   ARG A  13     5437   4292   4340    598   -384    435       C  
ATOM    102  O   ARG A  13      38.024   2.723  42.941  1.00 39.61           O  
ANISOU  102  O   ARG A  13     5792   4624   4635    653   -424    448       O  
ATOM    103  CB  ARG A  13      36.290   1.394  40.436  1.00 33.26           C  
ANISOU  103  CB  ARG A  13     5016   3727   3893    556   -313    460       C  
ATOM    104  CG  ARG A  13      37.617   0.679  40.420  1.00 40.82           C  
ANISOU  104  CG  ARG A  13     5991   4670   4849    636   -352    469       C  
ATOM    105  CD  ARG A  13      37.626  -0.636  41.228  1.00 45.53           C  
ANISOU  105  CD  ARG A  13     6697   5211   5390    672   -353    510       C  
ATOM    106  NE  ARG A  13      38.780  -0.589  42.108  1.00 51.15           N  
ANISOU  106  NE  ARG A  13     7407   5953   6077    749   -407    515       N  
ATOM    107  CZ  ARG A  13      39.987  -1.007  41.785  1.00 49.90           C  
ANISOU  107  CZ  ARG A  13     7232   5798   5928    826   -441    515       C  
ATOM    108  NH1 ARG A  13      40.199  -1.551  40.611  1.00 70.54           N  
ANISOU  108  NH1 ARG A  13     9843   8383   8575    841   -423    508       N  
ATOM    109  NH2 ARG A  13      40.972  -0.882  42.634  1.00 47.85           N  
ANISOU  109  NH2 ARG A  13     6961   5577   5643    891   -492    520       N  
ATOM    110  N   GLY A  14      37.222   4.290  41.594  1.00 35.16           N  
ANISOU  110  N   GLY A  14     5124   4093   4144    571   -391    401       N  
ATOM    111  CA  GLY A  14      38.304   5.198  41.908  1.00 40.47           C  
ANISOU  111  CA  GLY A  14     5742   4809   4826    599   -448    379       C  
ATOM    112  C   GLY A  14      38.164   6.025  43.177  1.00 42.92           C  
ANISOU  112  C   GLY A  14     6068   5146   5093    599   -476    366       C  
ATOM    113  O   GLY A  14      39.087   6.747  43.566  1.00 41.00           O  
ANISOU  113  O   GLY A  14     5790   4938   4851    617   -531    348       O  
ATOM    114  N   GLY A  15      37.008   5.957  43.825  1.00 43.46           N  
ANISOU  114  N   GLY A  15     6187   5204   5120    576   -438    375       N  
ATOM    115  CA  GLY A  15      36.830   6.712  45.044  1.00 41.71           C  
ANISOU  115  CA  GLY A  15     5989   5010   4850    583   -460    362       C  
ATOM    116  C   GLY A  15      35.475   7.340  45.256  1.00 40.42           C  
ANISOU  116  C   GLY A  15     5836   4855   4667    545   -415    351       C  
ATOM    117  O   GLY A  15      34.493   6.974  44.625  1.00 38.97           O  
ANISOU  117  O   GLY A  15     5651   4657   4497    509   -359    363       O  
ATOM    118  N   GLN A  16      35.443   8.298  46.168  1.00 41.85           N  
ANISOU  118  N   GLN A  16     6027   5063   4811    556   -441    325       N  
ATOM    119  CA  GLN A  16      34.202   8.922  46.591  1.00 41.84           C  
ANISOU  119  CA  GLN A  16     6042   5079   4777    539   -400    313       C  
ATOM    120  C   GLN A  16      33.879  10.125  45.755  1.00 40.63           C  
ANISOU  120  C   GLN A  16     5834   4931   4671    513   -396    275       C  
ATOM    121  O   GLN A  16      34.772  10.899  45.405  1.00 44.27           O  
ANISOU  121  O   GLN A  16     6260   5392   5169    513   -447    248       O  
ATOM    122  CB  GLN A  16      34.273   9.328  48.055  1.00 38.44           C  
ANISOU  122  CB  GLN A  16     5662   4670   4272    573   -428    303       C  
ATOM    123  CG  GLN A  16      33.923   8.209  48.979  1.00 44.88           C  
ANISOU  123  CG  GLN A  16     6544   5486   5022    589   -402    347       C  
ATOM    124  CD  GLN A  16      34.049   8.604  50.423  1.00 50.68           C  
ANISOU  124  CD  GLN A  16     7331   6247   5679    626   -432    337       C  
ATOM    125  OE1 GLN A  16      35.130   8.998  50.876  1.00 56.18           O  
ANISOU  125  OE1 GLN A  16     8030   6947   6368    654   -501    317       O  
ATOM    126  NE2 GLN A  16      32.953   8.494  51.162  1.00 44.32           N  
ANISOU  126  NE2 GLN A  16     6566   5463   4810    625   -381    352       N  
ATOM    127  N   LEU A  17      32.591  10.289  45.469  1.00 36.08           N  
ANISOU  127  N   LEU A  17     5252   4365   4090    490   -338    277       N  
ATOM    128  CA  LEU A  17      32.108  11.391  44.657  1.00 37.24           C  
ANISOU  128  CA  LEU A  17     5353   4518   4277    471   -327    245       C  
ATOM    129  C   LEU A  17      31.037  12.159  45.417  1.00 38.27           C  
ANISOU  129  C   LEU A  17     5507   4678   4355    487   -300    227       C  
ATOM    130  O   LEU A  17      30.269  11.576  46.179  1.00 38.15           O  
ANISOU  130  O   LEU A  17     5525   4686   4282    494   -259    251       O  
ATOM    131  CB  LEU A  17      31.471  10.851  43.371  1.00 33.74           C  
ANISOU  131  CB  LEU A  17     4870   4067   3883    431   -279    264       C  
ATOM    132  CG  LEU A  17      32.360  10.179  42.340  1.00 37.34           C  
ANISOU  132  CG  LEU A  17     5297   4494   4396    416   -295    277       C  
ATOM    133  CD1 LEU A  17      31.509   9.622  41.244  1.00 36.46           C  
ANISOU  133  CD1 LEU A  17     5161   4376   4316    377   -243    294       C  
ATOM    134  CD2 LEU A  17      33.375  11.174  41.775  1.00 41.42           C  
ANISOU  134  CD2 LEU A  17     5770   5007   4961    418   -347    245       C  
ATOM    135  N   ARG A  18      30.960  13.464  45.178  1.00 35.13           N  
ANISOU  135  N   ARG A  18     5094   4281   3974    494   -319    186       N  
ATOM    136  CA  ARG A  18      29.849  14.241  45.662  1.00 32.16           C  
ANISOU  136  CA  ARG A  18     4733   3932   3553    518   -287    166       C  
ATOM    137  C   ARG A  18      29.167  14.951  44.474  1.00 36.61           C  
ANISOU  137  C   ARG A  18     5247   4496   4167    500   -261    152       C  
ATOM    138  O   ARG A  18      29.796  15.751  43.761  1.00 36.69           O  
ANISOU  138  O   ARG A  18     5237   4477   4227    490   -302    127       O  
ATOM    139  CB  ARG A  18      30.293  15.273  46.696  1.00 36.22           C  
ANISOU  139  CB  ARG A  18     5297   4443   4021    558   -338    125       C  
ATOM    140  CG  ARG A  18      29.146  16.260  47.081  1.00 37.03           C  
ANISOU  140  CG  ARG A  18     5420   4571   4079    596   -306     96       C  
ATOM    141  CD  ARG A  18      29.527  17.162  48.254  1.00 47.78           C  
ANISOU  141  CD  ARG A  18     6849   5926   5380    641   -355     54       C  
ATOM    142  NE  ARG A  18      30.779  17.818  47.927  1.00 56.34           N  
ANISOU  142  NE  ARG A  18     7935   6963   6509    620   -433     26       N  
ATOM    143  CZ  ARG A  18      31.934  17.649  48.577  1.00 59.73           C  
ANISOU  143  CZ  ARG A  18     8391   7380   6925    617   -496     23       C  
ATOM    144  NH1 ARG A  18      32.016  16.887  49.676  1.00 52.07           N  
ANISOU  144  NH1 ARG A  18     7460   6434   5890    641   -494     42       N  
ATOM    145  NH2 ARG A  18      33.016  18.284  48.124  1.00 61.38           N  
ANISOU  145  NH2 ARG A  18     8587   7555   7181    587   -565      1       N  
ATOM    146  N   GLY A  19      27.879  14.675  44.285  1.00 27.77           N  
ANISOU  146  N   GLY A  19     4107   3414   3030    496   -196    170       N  
ATOM    147  CA  GLY A  19      27.147  15.225  43.166  1.00 28.81           C  
ANISOU  147  CA  GLY A  19     4189   3554   3205    482   -170    162       C  
ATOM    148  C   GLY A  19      26.332  16.448  43.583  1.00 39.84           C  
ANISOU  148  C   GLY A  19     5598   4975   4563    532   -159    128       C  
ATOM    149  O   GLY A  19      26.520  17.017  44.671  1.00 38.29           O  
ANISOU  149  O   GLY A  19     5456   4779   4313    577   -183    102       O  
ATOM    150  N   ILE A  20      25.425  16.858  42.701  1.00 35.75           N  
ANISOU  150  N   ILE A  20     5035   4478   4069    530   -125    127       N  
ATOM    151  CA  ILE A  20      24.624  18.033  42.945  1.00 33.62           C  
ANISOU  151  CA  ILE A  20     4776   4232   3767    586   -113     95       C  
ATOM    152  C   ILE A  20      23.152  17.758  42.629  1.00 36.79           C  
ANISOU  152  C   ILE A  20     5124   4706   4150    591    -42    119       C  
ATOM    153  O   ILE A  20      22.818  16.993  41.709  1.00 36.86           O  
ANISOU  153  O   ILE A  20     5078   4730   4198    537    -14    151       O  
ATOM    154  CB  ILE A  20      25.156  19.239  42.128  1.00 38.85           C  
ANISOU  154  CB  ILE A  20     5442   4839   4480    592   -162     59       C  
ATOM    155  CG1 ILE A  20      24.381  20.508  42.492  1.00 37.41           C  
ANISOU  155  CG1 ILE A  20     5290   4669   4256    664   -157     22       C  
ATOM    156  CG2 ILE A  20      25.057  18.967  40.634  1.00 32.54           C  
ANISOU  156  CG2 ILE A  20     4578   4033   3752    542   -149     80       C  
ATOM    157  CD1 ILE A  20      24.764  21.714  41.662  1.00 36.86           C  
ANISOU  157  CD1 ILE A  20     5233   4539   4232    669   -202     -9       C  
ATOM    158  N   ARG A  21      22.272  18.365  43.409  1.00 35.61           N  
ANISOU  158  N   ARG A  21     4989   4605   3935    655    -13    103       N  
ATOM    159  CA  ARG A  21      20.850  18.266  43.153  1.00 35.18           C  
ANISOU  159  CA  ARG A  21     4876   4635   3858    668     53    123       C  
ATOM    160  C   ARG A  21      20.442  19.360  42.157  1.00 38.84           C  
ANISOU  160  C   ARG A  21     5310   5089   4357    699     45     98       C  
ATOM    161  O   ARG A  21      20.630  20.548  42.429  1.00 41.48           O  
ANISOU  161  O   ARG A  21     5694   5390   4676    763     13     54       O  
ATOM    162  CB  ARG A  21      20.115  18.471  44.472  1.00 37.84           C  
ANISOU  162  CB  ARG A  21     5239   5036   4101    734     90    117       C  
ATOM    163  CG  ARG A  21      18.672  17.982  44.541  1.00 39.97           C  
ANISOU  163  CG  ARG A  21     5441   5416   4328    735    168    154       C  
ATOM    164  CD  ARG A  21      17.978  18.487  45.822  1.00 41.54           C  
ANISOU  164  CD  ARG A  21     5670   5684   4430    822    203    138       C  
ATOM    165  NE  ARG A  21      16.968  19.479  45.471  1.00 58.53           N  
ANISOU  165  NE  ARG A  21     7783   7891   6566    895    230    116       N  
ATOM    166  CZ  ARG A  21      15.683  19.438  45.837  1.00 65.62           C  
ANISOU  166  CZ  ARG A  21     8626   8905   7401    936    298    136       C  
ATOM    167  NH1 ARG A  21      15.227  18.476  46.639  1.00 67.62           N  
ANISOU  167  NH1 ARG A  21     8860   9234   7598    905    349    179       N  
ATOM    168  NH2 ARG A  21      14.849  20.385  45.416  1.00 65.41           N  
ANISOU  168  NH2 ARG A  21     8563   8924   7365   1011    316    114       N  
ATOM    169  N   LEU A  22      19.879  18.978  41.016  1.00 35.39           N  
ANISOU  169  N   LEU A  22     4802   4680   3964    655     71    124       N  
ATOM    170  CA  LEU A  22      19.476  19.951  40.008  1.00 32.38           C  
ANISOU  170  CA  LEU A  22     4393   4293   3618    684     63    106       C  
ATOM    171  C   LEU A  22      17.977  20.018  39.925  1.00 41.50           C  
ANISOU  171  C   LEU A  22     5484   5551   4734    720    123    122       C  
ATOM    172  O   LEU A  22      17.294  19.048  40.234  1.00 45.70           O  
ANISOU  172  O   LEU A  22     5971   6156   5237    686    173    159       O  
ATOM    173  CB  LEU A  22      20.002  19.570  38.626  1.00 37.27           C  
ANISOU  173  CB  LEU A  22     4976   4869   4318    611     41    122       C  
ATOM    174  CG  LEU A  22      21.525  19.475  38.470  1.00 37.91           C  
ANISOU  174  CG  LEU A  22     5101   4857   4444    570    -18    111       C  
ATOM    175  CD1 LEU A  22      21.849  19.038  37.061  1.00 35.92           C  
ANISOU  175  CD1 LEU A  22     4804   4581   4264    505    -26    130       C  
ATOM    176  CD2 LEU A  22      22.191  20.796  38.826  1.00 31.86           C  
ANISOU  176  CD2 LEU A  22     4401   4029   3674    622    -71     65       C  
ATOM    177  N   LYS A  23      17.465  21.151  39.459  1.00 39.07           N  
ANISOU  177  N   LYS A  23     5168   5249   4427    786    118     96       N  
ATOM    178  CA  LYS A  23      16.047  21.309  39.283  1.00 45.15           C  
ANISOU  178  CA  LYS A  23     5868   6125   5163    830    172    111       C  
ATOM    179  C   LYS A  23      15.688  20.976  37.849  1.00 41.91           C  
ANISOU  179  C   LYS A  23     5381   5731   4812    771    177    138       C  
ATOM    180  O   LYS A  23      16.200  21.587  36.929  1.00 43.98           O  
ANISOU  180  O   LYS A  23     5659   5925   5127    768    136    121       O  
ATOM    181  CB  LYS A  23      15.641  22.753  39.597  1.00 55.24           C  
ANISOU  181  CB  LYS A  23     7186   7401   6401    950    163     67       C  
ATOM    182  CG  LYS A  23      14.184  22.897  39.986  1.00 74.60           C  
ANISOU  182  CG  LYS A  23     9576   9982   8786   1024    227     78       C  
ATOM    183  CD  LYS A  23      13.654  24.332  39.803  1.00 85.24           C  
ANISOU  183  CD  LYS A  23    10948  11329  10111   1146    217     40       C  
ATOM    184  CE  LYS A  23      12.126  24.364  39.934  1.00 86.52           C  
ANISOU  184  CE  LYS A  23    11021  11639  10214   1215    285     60       C  
ATOM    185  NZ  LYS A  23      11.477  23.191  39.255  1.00 82.65           N  
ANISOU  185  NZ  LYS A  23    10414  11241   9750   1117    326    118       N  
ATOM    186  N   ALA A  24      14.816  19.997  37.648  1.00 38.29           N  
ANISOU  186  N   ALA A  24     4843   5363   4343    718    226    181       N  
ATOM    187  CA  ALA A  24      14.182  19.846  36.345  1.00 37.08           C  
ANISOU  187  CA  ALA A  24     4611   5249   4229    680    235    203       C  
ATOM    188  C   ALA A  24      12.759  20.358  36.527  1.00 41.11           C  
ANISOU  188  C   ALA A  24     5054   5881   4685    755    282    209       C  
ATOM    189  O   ALA A  24      12.312  20.537  37.652  1.00 43.10           O  
ANISOU  189  O   ALA A  24     5317   6190   4871    817    314    204       O  
ATOM    190  CB  ALA A  24      14.199  18.394  35.884  1.00 33.99           C  
ANISOU  190  CB  ALA A  24     4178   4872   3866    560    251    246       C  
ATOM    191  N   PRO A  25      12.035  20.593  35.430  1.00 45.58           N  
ANISOU  191  N   PRO A  25     5549   6496   5275    755    287    221       N  
ATOM    192  CA  PRO A  25      10.729  21.269  35.584  1.00 41.66           C  
ANISOU  192  CA  PRO A  25     4988   6116   4724    849    325    222       C  
ATOM    193  C   PRO A  25       9.743  20.512  36.465  1.00 44.28           C  
ANISOU  193  C   PRO A  25     5252   6580   4990    837    390    257       C  
ATOM    194  O   PRO A  25       9.002  21.140  37.214  1.00 51.53           O  
ANISOU  194  O   PRO A  25     6156   7580   5843    939    423    246       O  
ATOM    195  CB  PRO A  25      10.208  21.349  34.151  1.00 38.96           C  
ANISOU  195  CB  PRO A  25     4573   5804   4425    822    315    239       C  
ATOM    196  CG  PRO A  25      11.466  21.274  33.274  1.00 42.32           C  
ANISOU  196  CG  PRO A  25     5060   6094   4928    756    259    226       C  
ATOM    197  CD  PRO A  25      12.341  20.281  34.024  1.00 42.84           C  
ANISOU  197  CD  PRO A  25     5175   6105   4997    679    258    234       C  
ATOM    198  N   GLY A  26       9.740  19.187  36.389  1.00 45.29           N  
ANISOU  198  N   GLY A  26     5346   6731   5132    715    407    299       N  
ATOM    199  CA  GLY A  26       8.836  18.370  37.184  1.00 42.32           C  
ANISOU  199  CA  GLY A  26     4907   6478   4695    681    468    340       C  
ATOM    200  C   GLY A  26       9.412  17.874  38.508  1.00 46.84           C  
ANISOU  200  C   GLY A  26     5551   7018   5226    671    481    342       C  
ATOM    201  O   GLY A  26       8.758  17.114  39.215  1.00 40.87           O  
ANISOU  201  O   GLY A  26     4754   6357   4419    632    531    381       O  
ATOM    202  N   GLY A  27      10.630  18.299  38.859  1.00 49.83           N  
ANISOU  202  N   GLY A  27     6038   7269   5626    703    435    302       N  
ATOM    203  CA  GLY A  27      11.233  17.868  40.114  1.00 45.93           C  
ANISOU  203  CA  GLY A  27     5617   6743   5093    698    440    301       C  
ATOM    204  C   GLY A  27      12.744  17.802  40.088  1.00 51.69           C  
ANISOU  204  C   GLY A  27     6445   7322   5872    670    379    275       C  
ATOM    205  O   GLY A  27      13.376  18.134  39.081  1.00 50.47           O  
ANISOU  205  O   GLY A  27     6305   7086   5785    654    333    255       O  
ATOM    206  N   PRO A  28      13.353  17.349  41.198  1.00 48.03           N  
ANISOU  206  N   PRO A  28     6049   6827   5374    662    378    276       N  
ATOM    207  CA  PRO A  28      14.822  17.352  41.244  1.00 35.16           C  
ANISOU  207  CA  PRO A  28     4508   5065   3786    645    317    250       C  
ATOM    208  C   PRO A  28      15.436  16.126  40.572  1.00 40.34           C  
ANISOU  208  C   PRO A  28     5161   5666   4499    530    300    283       C  
ATOM    209  O   PRO A  28      14.764  15.093  40.454  1.00 37.46           O  
ANISOU  209  O   PRO A  28     4747   5362   4125    457    340    330       O  
ATOM    210  CB  PRO A  28      15.130  17.315  42.733  1.00 34.31           C  
ANISOU  210  CB  PRO A  28     4467   4958   3609    687    324    242       C  
ATOM    211  CG  PRO A  28      13.767  16.883  43.432  1.00 42.30           C  
ANISOU  211  CG  PRO A  28     5417   6112   4543    696    401    281       C  
ATOM    212  CD  PRO A  28      12.742  16.710  42.373  1.00 43.26           C  
ANISOU  212  CD  PRO A  28     5435   6311   4691    658    432    309       C  
ATOM    213  N   VAL A  29      16.697  16.245  40.141  1.00 33.36           N  
ANISOU  213  N   VAL A  29     4331   4672   3672    514    242    259       N  
ATOM    214  CA  VAL A  29      17.454  15.111  39.657  1.00 35.76           C  
ANISOU  214  CA  VAL A  29     4649   4916   4023    424    223    284       C  
ATOM    215  C   VAL A  29      18.848  15.145  40.284  1.00 37.91           C  
ANISOU  215  C   VAL A  29     5004   5098   4303    439    174    262       C  
ATOM    216  O   VAL A  29      19.292  16.178  40.771  1.00 39.70           O  
ANISOU  216  O   VAL A  29     5273   5296   4516    507    144    222       O  
ATOM    217  CB  VAL A  29      17.562  15.068  38.086  1.00 40.51           C  
ANISOU  217  CB  VAL A  29     5208   5486   4699    376    204    285       C  
ATOM    218  CG1 VAL A  29      16.193  14.959  37.436  1.00 41.31           C  
ANISOU  218  CG1 VAL A  29     5223   5681   4792    354    247    310       C  
ATOM    219  CG2 VAL A  29      18.273  16.256  37.563  1.00 34.14           C  
ANISOU  219  CG2 VAL A  29     4424   4616   3932    426    156    242       C  
ATOM    220  N   SER A  30      19.530  14.014  40.277  1.00 36.08           N  
ANISOU  220  N   SER A  30     4798   4821   4089    376    163    288       N  
ATOM    221  CA  SER A  30      20.897  13.947  40.789  1.00 38.10           C  
ANISOU  221  CA  SER A  30     5123   4999   4355    387    113    271       C  
ATOM    222  C   SER A  30      21.862  14.107  39.616  1.00 37.29           C  
ANISOU  222  C   SER A  30     5015   4825   4330    363     67    255       C  
ATOM    223  O   SER A  30      21.704  13.456  38.590  1.00 32.60           O  
ANISOU  223  O   SER A  30     4386   4226   3776    307     77    275       O  
ATOM    224  CB  SER A  30      21.152  12.583  41.445  1.00 41.60           C  
ANISOU  224  CB  SER A  30     5601   5433   4771    341    125    311       C  
ATOM    225  OG  SER A  30      20.206  12.281  42.466  1.00 47.90           O  
ANISOU  225  OG  SER A  30     6400   6305   5496    349    175    337       O  
ATOM    226  N   ALA A  31      22.865  14.966  39.749  1.00 39.69           N  
ANISOU  226  N   ALA A  31     5353   5075   4651    401     15    218       N  
ATOM    227  CA  ALA A  31      23.884  15.034  38.718  1.00 36.17           C  
ANISOU  227  CA  ALA A  31     4901   4568   4274    373    -27    209       C  
ATOM    228  C   ALA A  31      25.284  14.811  39.296  1.00 41.39           C  
ANISOU  228  C   ALA A  31     5611   5176   4939    377    -77    201       C  
ATOM    229  O   ALA A  31      25.624  15.339  40.365  1.00 43.28           O  
ANISOU  229  O   ALA A  31     5895   5411   5139    419   -100    180       O  
ATOM    230  CB  ALA A  31      23.808  16.356  37.974  1.00 30.69           C  
ANISOU  230  CB  ALA A  31     4188   3862   3611    401    -48    177       C  
ATOM    231  N   PHE A  32      26.088  14.041  38.571  1.00 36.45           N  
ANISOU  231  N   PHE A  32     4977   4514   4359    337    -93    216       N  
ATOM    232  CA  PHE A  32      27.490  13.825  38.913  1.00 29.04           C  
ANISOU  232  CA  PHE A  32     4069   3532   3433    342   -143    211       C  
ATOM    233  C   PHE A  32      28.279  14.167  37.673  1.00 33.53           C  
ANISOU  233  C   PHE A  32     4604   4068   4067    321   -172    200       C  
ATOM    234  O   PHE A  32      28.334  13.382  36.709  1.00 35.42           O  
ANISOU  234  O   PHE A  32     4817   4300   4341    287   -156    220       O  
ATOM    235  CB  PHE A  32      27.730  12.370  39.345  1.00 31.39           C  
ANISOU  235  CB  PHE A  32     4393   3822   3710    324   -130    245       C  
ATOM    236  CG  PHE A  32      26.969  11.975  40.594  1.00 33.40           C  
ANISOU  236  CG  PHE A  32     4684   4112   3895    338    -98    263       C  
ATOM    237  CD1 PHE A  32      25.677  11.463  40.509  1.00 26.31           C  
ANISOU  237  CD1 PHE A  32     3767   3255   2973    311    -41    289       C  
ATOM    238  CD2 PHE A  32      27.546  12.129  41.851  1.00 33.34           C  
ANISOU  238  CD2 PHE A  32     4726   4100   3842    377   -127    254       C  
ATOM    239  CE1 PHE A  32      24.981  11.123  41.658  1.00 32.54           C  
ANISOU  239  CE1 PHE A  32     4586   4085   3695    321     -8    309       C  
ATOM    240  CE2 PHE A  32      26.859  11.789  42.998  1.00 36.06           C  
ANISOU  240  CE2 PHE A  32     5105   4480   4117    392    -96    271       C  
ATOM    241  CZ  PHE A  32      25.565  11.291  42.908  1.00 32.78           C  
ANISOU  241  CZ  PHE A  32     4668   4108   3677    364    -34    300       C  
ATOM    242  N   LEU A  33      28.859  15.360  37.692  1.00 27.76           N  
ANISOU  242  N   LEU A  33     3878   3320   3351    340   -214    170       N  
ATOM    243  CA  LEU A  33      29.484  15.961  36.519  1.00 31.56           C  
ANISOU  243  CA  LEU A  33     4325   3778   3890    318   -240    160       C  
ATOM    244  C   LEU A  33      31.008  16.045  36.701  1.00 29.51           C  
ANISOU  244  C   LEU A  33     4072   3492   3649    314   -297    154       C  
ATOM    245  O   LEU A  33      31.477  16.352  37.799  1.00 26.91           O  
ANISOU  245  O   LEU A  33     3780   3158   3286    337   -331    140       O  
ATOM    246  CB  LEU A  33      28.946  17.387  36.322  1.00 33.74           C  
ANISOU  246  CB  LEU A  33     4602   4050   4167    336   -249    133       C  
ATOM    247  CG  LEU A  33      27.421  17.519  36.425  1.00 34.04           C  
ANISOU  247  CG  LEU A  33     4634   4127   4173    358   -198    135       C  
ATOM    248  CD1 LEU A  33      27.003  19.000  36.379  1.00 31.17           C  
ANISOU  248  CD1 LEU A  33     4286   3754   3804    394   -213    104       C  
ATOM    249  CD2 LEU A  33      26.731  16.682  35.321  1.00 27.16           C  
ANISOU  249  CD2 LEU A  33     3712   3280   3328    321   -154    163       C  
ATOM    250  N   GLY A  34      31.763  15.774  35.638  1.00 26.49           N  
ANISOU  250  N   GLY A  34     3650   3100   3315    286   -307    164       N  
ATOM    251  CA  GLY A  34      33.206  15.940  35.690  1.00 32.60           C  
ANISOU  251  CA  GLY A  34     4414   3863   4109    280   -360    160       C  
ATOM    252  C   GLY A  34      33.920  14.771  36.365  1.00 29.69           C  
ANISOU  252  C   GLY A  34     4060   3501   3721    297   -369    178       C  
ATOM    253  O   GLY A  34      34.919  14.948  37.029  1.00 32.49           O  
ANISOU  253  O   GLY A  34     4422   3857   4067    308   -416    172       O  
ATOM    254  N   ILE A  35      33.401  13.564  36.202  1.00 33.08           N  
ANISOU  254  N   ILE A  35     4496   3933   4141    300   -326    201       N  
ATOM    255  CA  ILE A  35      34.048  12.416  36.813  1.00 30.40           C  
ANISOU  255  CA  ILE A  35     4180   3591   3780    321   -334    220       C  
ATOM    256  C   ILE A  35      35.160  11.931  35.909  1.00 31.73           C  
ANISOU  256  C   ILE A  35     4309   3758   3988    320   -350    230       C  
ATOM    257  O   ILE A  35      34.917  11.588  34.763  1.00 35.24           O  
ANISOU  257  O   ILE A  35     4728   4198   4463    301   -321    237       O  
ATOM    258  CB  ILE A  35      33.091  11.238  36.949  1.00 29.33           C  
ANISOU  258  CB  ILE A  35     4077   3450   3618    319   -284    245       C  
ATOM    259  CG1 ILE A  35      31.899  11.610  37.822  1.00 25.40           C  
ANISOU  259  CG1 ILE A  35     3609   2968   3075    321   -258    240       C  
ATOM    260  CG2 ILE A  35      33.864  10.044  37.532  1.00 22.82           C  
ANISOU  260  CG2 ILE A  35     3286   2613   2771    346   -297    267       C  
ATOM    261  CD1 ILE A  35      30.762  10.566  37.773  1.00 28.17           C  
ANISOU  261  CD1 ILE A  35     3978   3322   3403    300   -202    268       C  
ATOM    262  N   PRO A  36      36.384  11.885  36.419  1.00 35.25           N  
ANISOU  262  N   PRO A  36     4749   4214   4430    342   -397    231       N  
ATOM    263  CA  PRO A  36      37.478  11.441  35.542  1.00 30.36           C  
ANISOU  263  CA  PRO A  36     4083   3606   3845    349   -409    241       C  
ATOM    264  C   PRO A  36      37.366   9.945  35.313  1.00 34.83           C  
ANISOU  264  C   PRO A  36     4678   4156   4401    374   -377    264       C  
ATOM    265  O   PRO A  36      37.067   9.212  36.266  1.00 34.01           O  
ANISOU  265  O   PRO A  36     4629   4037   4255    397   -371    276       O  
ATOM    266  CB  PRO A  36      38.730  11.742  36.374  1.00 28.84           C  
ANISOU  266  CB  PRO A  36     3879   3439   3642    370   -470    238       C  
ATOM    267  CG  PRO A  36      38.240  11.718  37.826  1.00 32.25           C  
ANISOU  267  CG  PRO A  36     4373   3861   4019    389   -481    234       C  
ATOM    268  CD  PRO A  36      36.820  12.186  37.795  1.00 33.73           C  
ANISOU  268  CD  PRO A  36     4589   4030   4198    366   -440    223       C  
ATOM    269  N   PHE A  37      37.592   9.491  34.089  1.00 33.23           N  
ANISOU  269  N   PHE A  37     4445   3952   4231    371   -355    270       N  
ATOM    270  CA  PHE A  37      37.567   8.058  33.816  1.00 29.72           C  
ANISOU  270  CA  PHE A  37     4038   3482   3774    398   -329    288       C  
ATOM    271  C   PHE A  37      38.899   7.604  33.194  1.00 30.75           C  
ANISOU  271  C   PHE A  37     4129   3631   3922    439   -348    294       C  
ATOM    272  O   PHE A  37      39.103   6.425  32.951  1.00 36.42           O  
ANISOU  272  O   PHE A  37     4881   4328   4630    476   -333    306       O  
ATOM    273  CB  PHE A  37      36.374   7.689  32.929  1.00 25.77           C  
ANISOU  273  CB  PHE A  37     3554   2955   3282    360   -278    289       C  
ATOM    274  CG  PHE A  37      36.426   8.277  31.539  1.00 28.88           C  
ANISOU  274  CG  PHE A  37     3890   3363   3719    334   -267    278       C  
ATOM    275  CD1 PHE A  37      37.076   7.611  30.516  1.00 25.53           C  
ANISOU  275  CD1 PHE A  37     3449   2939   3312    354   -258    281       C  
ATOM    276  CD2 PHE A  37      35.824   9.508  31.259  1.00 30.59           C  
ANISOU  276  CD2 PHE A  37     4073   3595   3954    293   -265    264       C  
ATOM    277  CE1 PHE A  37      37.137   8.158  29.249  1.00 30.39           C  
ANISOU  277  CE1 PHE A  37     4012   3571   3961    329   -246    273       C  
ATOM    278  CE2 PHE A  37      35.851  10.037  29.980  1.00 26.76           C  
ANISOU  278  CE2 PHE A  37     3541   3121   3504    269   -254    257       C  
ATOM    279  CZ  PHE A  37      36.517   9.362  28.972  1.00 28.92           C  
ANISOU  279  CZ  PHE A  37     3795   3398   3794    284   -244    262       C  
ATOM    280  N   ALA A  38      39.796   8.559  32.949  1.00 29.50           N  
ANISOU  280  N   ALA A  38     3902   3518   3790    432   -381    285       N  
ATOM    281  CA  ALA A  38      41.138   8.294  32.417  1.00 27.60           C  
ANISOU  281  CA  ALA A  38     3605   3315   3564    471   -400    292       C  
ATOM    282  C   ALA A  38      42.203   9.181  33.051  1.00 31.95           C  
ANISOU  282  C   ALA A  38     4103   3919   4119    469   -457    290       C  
ATOM    283  O   ALA A  38      41.900  10.286  33.534  1.00 31.40           O  
ANISOU  283  O   ALA A  38     4029   3850   4051    425   -479    277       O  
ATOM    284  CB  ALA A  38      41.160   8.494  30.910  1.00 27.89           C  
ANISOU  284  CB  ALA A  38     3594   3365   3638    448   -371    288       C  
ATOM    285  N   GLU A  39      43.454   8.707  33.039  1.00 30.70           N  
ANISOU  285  N   GLU A  39     3902   3804   3957    520   -482    302       N  
ATOM    286  CA  GLU A  39      44.579   9.586  33.311  1.00 31.66           C  
ANISOU  286  CA  GLU A  39     3950   3991   4090    506   -535    302       C  
ATOM    287  C   GLU A  39      44.610  10.674  32.226  1.00 30.51           C  
ANISOU  287  C   GLU A  39     3740   3867   3986    441   -527    296       C  
ATOM    288  O   GLU A  39      44.450  10.390  31.050  1.00 32.81           O  
ANISOU  288  O   GLU A  39     4012   4157   4297    441   -486    299       O  
ATOM    289  CB  GLU A  39      45.901   8.792  33.324  1.00 36.32           C  
ANISOU  289  CB  GLU A  39     4493   4637   4669    579   -557    320       C  
ATOM    290  CG  GLU A  39      46.074   7.893  34.533  1.00 39.91           C  
ANISOU  290  CG  GLU A  39     5007   5077   5079    644   -580    330       C  
ATOM    291  CD  GLU A  39      46.133   8.685  35.820  1.00 45.73           C  
ANISOU  291  CD  GLU A  39     5755   5824   5795    615   -633    323       C  
ATOM    292  OE1 GLU A  39      47.007   9.552  35.943  1.00 51.61           O  
ANISOU  292  OE1 GLU A  39     6428   6629   6552    586   -681    321       O  
ATOM    293  OE2 GLU A  39      45.315   8.454  36.721  1.00 48.45           O  
ANISOU  293  OE2 GLU A  39     6183   6119   6109    618   -629    319       O  
ATOM    294  N   PRO A  40      44.813  11.929  32.623  1.00 36.85           N  
ANISOU  294  N   PRO A  40     4517   4686   4799    384   -569    287       N  
ATOM    295  CA  PRO A  40      44.910  13.017  31.635  1.00 35.88           C  
ANISOU  295  CA  PRO A  40     4340   4581   4713    317   -567    286       C  
ATOM    296  C   PRO A  40      45.825  12.648  30.468  1.00 35.25           C  
ANISOU  296  C   PRO A  40     4178   4560   4654    334   -548    304       C  
ATOM    297  O   PRO A  40      46.988  12.291  30.670  1.00 37.07           O  
ANISOU  297  O   PRO A  40     4353   4855   4877    369   -576    319       O  
ATOM    298  CB  PRO A  40      45.541  14.161  32.441  1.00 33.90           C  
ANISOU  298  CB  PRO A  40     4066   4355   4461    269   -634    280       C  
ATOM    299  CG  PRO A  40      45.128  13.892  33.862  1.00 36.90           C  
ANISOU  299  CG  PRO A  40     4519   4702   4801    300   -657    267       C  
ATOM    300  CD  PRO A  40      45.195  12.368  33.977  1.00 35.40           C  
ANISOU  300  CD  PRO A  40     4349   4514   4589    381   -628    281       C  
ATOM    301  N   PRO A  41      45.307  12.692  29.241  1.00 33.94           N  
ANISOU  301  N   PRO A  41     4005   4380   4510    314   -501    305       N  
ATOM    302  CA  PRO A  41      46.203  12.235  28.168  1.00 33.84           C  
ANISOU  302  CA  PRO A  41     3919   4429   4509    341   -480    322       C  
ATOM    303  C   PRO A  41      47.105  13.371  27.667  1.00 36.85           C  
ANISOU  303  C   PRO A  41     4210   4875   4915    278   -508    337       C  
ATOM    304  O   PRO A  41      46.977  13.748  26.496  1.00 30.59           O  
ANISOU  304  O   PRO A  41     3387   4092   4143    244   -476    344       O  
ATOM    305  CB  PRO A  41      45.235  11.800  27.072  1.00 36.68           C  
ANISOU  305  CB  PRO A  41     4315   4744   4876    344   -419    316       C  
ATOM    306  CG  PRO A  41      44.040  12.710  27.264  1.00 36.98           C  
ANISOU  306  CG  PRO A  41     4404   4722   4924    281   -419    301       C  
ATOM    307  CD  PRO A  41      43.953  13.012  28.757  1.00 35.32           C  
ANISOU  307  CD  PRO A  41     4233   4491   4695    279   -463    292       C  
ATOM    308  N   VAL A  42      47.971  13.893  28.544  1.00 33.66           N  
ANISOU  308  N   VAL A  42     3768   4516   4506    258   -567    343       N  
ATOM    309  CA  VAL A  42      48.802  15.051  28.240  1.00 40.81           C  
ANISOU  309  CA  VAL A  42     4595   5478   5433    180   -603    358       C  
ATOM    310  C   VAL A  42      50.307  14.676  28.164  1.00 41.63           C  
ANISOU  310  C   VAL A  42     4592   5696   5531    210   -625    384       C  
ATOM    311  O   VAL A  42      50.695  13.579  28.561  1.00 34.57           O  
ANISOU  311  O   VAL A  42     3695   4827   4614    299   -621    386       O  
ATOM    312  CB  VAL A  42      48.604  16.172  29.299  1.00 49.92           C  
ANISOU  312  CB  VAL A  42     5788   6594   6584    112   -663    344       C  
ATOM    313  CG1 VAL A  42      47.103  16.446  29.533  1.00 44.99           C  
ANISOU  313  CG1 VAL A  42     5270   5867   5957    102   -641    317       C  
ATOM    314  CG2 VAL A  42      49.324  15.826  30.630  1.00 33.90           C  
ANISOU  314  CG2 VAL A  42     3754   4599   4527    147   -719    342       C  
ATOM    315  N   GLY A  43      51.143  15.578  27.647  1.00 37.76           N  
ANISOU  315  N   GLY A  43     4013   5274   5060    138   -647    406       N  
ATOM    316  CA  GLY A  43      52.579  15.339  27.649  1.00 36.42           C  
ANISOU  316  CA  GLY A  43     3729   5225   4882    158   -672    433       C  
ATOM    317  C   GLY A  43      52.921  14.122  26.822  1.00 38.15           C  
ANISOU  317  C   GLY A  43     3909   5497   5091    259   -615    444       C  
ATOM    318  O   GLY A  43      52.535  14.022  25.660  1.00 45.76           O  
ANISOU  318  O   GLY A  43     4872   6449   6065    259   -558    447       O  
ATOM    319  N   SER A  44      53.631  13.175  27.413  1.00 39.79           N  
ANISOU  319  N   SER A  44     4089   5758   5272    351   -629    449       N  
ATOM    320  CA  SER A  44      54.029  11.973  26.683  1.00 41.73           C  
ANISOU  320  CA  SER A  44     4304   6051   5502    461   -578    457       C  
ATOM    321  C   SER A  44      52.820  11.104  26.306  1.00 38.64           C  
ANISOU  321  C   SER A  44     4028   5549   5103    517   -521    432       C  
ATOM    322  O   SER A  44      52.959  10.168  25.526  1.00 34.62           O  
ANISOU  322  O   SER A  44     3516   5059   4581    599   -473    433       O  
ATOM    323  CB  SER A  44      55.009  11.145  27.499  1.00 41.20           C  
ANISOU  323  CB  SER A  44     4194   6057   5404    557   -612    467       C  
ATOM    324  OG  SER A  44      54.396  10.744  28.711  1.00 50.62           O  
ANISOU  324  OG  SER A  44     5490   7165   6580    587   -641    447       O  
ATOM    325  N   ARG A  45      51.638  11.414  26.845  1.00 36.03           N  
ANISOU  325  N   ARG A  45     3802   5110   4780    472   -527    409       N  
ATOM    326  CA  ARG A  45      50.462  10.574  26.568  1.00 35.01           C  
ANISOU  326  CA  ARG A  45     3779   4881   4642    516   -477    388       C  
ATOM    327  C   ARG A  45      49.619  11.073  25.394  1.00 36.89           C  
ANISOU  327  C   ARG A  45     4034   5079   4902    456   -431    382       C  
ATOM    328  O   ARG A  45      48.678  10.395  24.953  1.00 39.81           O  
ANISOU  328  O   ARG A  45     4481   5380   5267    485   -388    366       O  
ATOM    329  CB  ARG A  45      49.596  10.425  27.806  1.00 37.63           C  
ANISOU  329  CB  ARG A  45     4212   5126   4960    515   -501    370       C  
ATOM    330  CG  ARG A  45      50.238   9.757  28.994  1.00 35.29           C  
ANISOU  330  CG  ARG A  45     3922   4852   4633    585   -542    375       C  
ATOM    331  CD  ARG A  45      49.188   9.770  30.114  1.00 51.44           C  
ANISOU  331  CD  ARG A  45     6075   6805   6664    568   -558    357       C  
ATOM    332  NE  ARG A  45      49.708   9.513  31.452  1.00 67.69           N  
ANISOU  332  NE  ARG A  45     8145   8881   8694    606   -610    361       N  
ATOM    333  CZ  ARG A  45      49.722   8.314  32.028  1.00 76.75           C  
ANISOU  333  CZ  ARG A  45     9350  10005   9807    696   -607    365       C  
ATOM    334  NH1 ARG A  45      49.248   7.252  31.378  1.00 76.06           N  
ANISOU  334  NH1 ARG A  45     9318   9870   9713    753   -554    364       N  
ATOM    335  NH2 ARG A  45      50.214   8.180  33.254  1.00 80.29           N  
ANISOU  335  NH2 ARG A  45     9806  10474  10227    728   -659    371       N  
ATOM    336  N   ARG A  46      49.953  12.247  24.870  1.00 37.38           N  
ANISOU  336  N   ARG A  46     4029   5186   4990    371   -443    396       N  
ATOM    337  CA  ARG A  46      49.261  12.716  23.675  1.00 35.43           C  
ANISOU  337  CA  ARG A  46     3791   4909   4760    321   -400    395       C  
ATOM    338  C   ARG A  46      49.354  11.677  22.560  1.00 32.96           C  
ANISOU  338  C   ARG A  46     3471   4618   4433    396   -341    395       C  
ATOM    339  O   ARG A  46      50.433  11.122  22.331  1.00 30.01           O  
ANISOU  339  O   ARG A  46     3027   4330   4044    458   -336    410       O  
ATOM    340  CB  ARG A  46      49.843  14.027  23.174  1.00 38.20           C  
ANISOU  340  CB  ARG A  46     4062   5318   5134    227   -420    418       C  
ATOM    341  CG  ARG A  46      49.013  14.680  22.049  1.00 32.05           C  
ANISOU  341  CG  ARG A  46     3307   4498   4373    167   -383    418       C  
ATOM    342  CD  ARG A  46      49.799  15.904  21.496  1.00 27.86           C  
ANISOU  342  CD  ARG A  46     2690   4034   3862     75   -403    450       C  
ATOM    343  NE  ARG A  46      49.662  17.073  22.347  1.00 32.11           N  
ANISOU  343  NE  ARG A  46     3252   4532   4414    -10   -461    448       N  
ATOM    344  CZ  ARG A  46      50.264  18.238  22.113  1.00 31.65           C  
ANISOU  344  CZ  ARG A  46     3141   4512   4373   -106   -492    474       C  
ATOM    345  NH1 ARG A  46      51.090  18.369  21.083  1.00 31.43           N  
ANISOU  345  NH1 ARG A  46     3021   4574   4347   -128   -468    508       N  
ATOM    346  NH2 ARG A  46      50.069  19.254  22.922  1.00 31.65           N  
ANISOU  346  NH2 ARG A  46     3181   4461   4382   -178   -547    466       N  
ATOM    347  N   PHE A  47      48.238  11.457  21.854  1.00 25.80           N  
ANISOU  347  N   PHE A  47     2634   3640   3528    389   -299    379       N  
ATOM    348  CA  PHE A  47      48.132  10.483  20.766  1.00 27.09           C  
ANISOU  348  CA  PHE A  47     2812   3806   3674    453   -245    372       C  
ATOM    349  C   PHE A  47      48.082   9.055  21.244  1.00 27.91           C  
ANISOU  349  C   PHE A  47     2981   3874   3749    553   -236    357       C  
ATOM    350  O   PHE A  47      47.962   8.147  20.418  1.00 37.29           O  
ANISOU  350  O   PHE A  47     4199   5051   4917    612   -195    346       O  
ATOM    351  CB  PHE A  47      49.280  10.586  19.743  1.00 30.60           C  
ANISOU  351  CB  PHE A  47     3153   4361   4115    470   -223    395       C  
ATOM    352  CG  PHE A  47      49.519  11.961  19.258  1.00 33.57           C  
ANISOU  352  CG  PHE A  47     3459   4781   4515    369   -234    419       C  
ATOM    353  CD1 PHE A  47      48.481  12.702  18.720  1.00 29.80           C  
ANISOU  353  CD1 PHE A  47     3028   4241   4056    295   -222    413       C  
ATOM    354  CD2 PHE A  47      50.783  12.538  19.369  1.00 27.81           C  
ANISOU  354  CD2 PHE A  47     2619   4158   3791    345   -261    449       C  
ATOM    355  CE1 PHE A  47      48.702  13.995  18.249  1.00 30.35           C  
ANISOU  355  CE1 PHE A  47     3043   4342   4146    202   -234    438       C  
ATOM    356  CE2 PHE A  47      50.992  13.815  18.942  1.00 30.67           C  
ANISOU  356  CE2 PHE A  47     2927   4553   4175    242   -274    474       C  
ATOM    357  CZ  PHE A  47      49.932  14.559  18.375  1.00 26.33           C  
ANISOU  357  CZ  PHE A  47     2434   3927   3642    170   -260    468       C  
ATOM    358  N   MET A  48      48.185   8.829  22.551  1.00 29.97           N  
ANISOU  358  N   MET A  48     3270   4115   4003    575   -275    354       N  
ATOM    359  CA  MET A  48      48.178   7.429  23.057  1.00 32.12           C  
ANISOU  359  CA  MET A  48     3613   4349   4244    673   -269    344       C  
ATOM    360  C   MET A  48      46.814   6.974  23.540  1.00 33.27           C  
ANISOU  360  C   MET A  48     3877   4380   4383    657   -261    325       C  
ATOM    361  O   MET A  48      45.970   7.823  23.874  1.00 28.82           O  
ANISOU  361  O   MET A  48     3334   3778   3838    576   -272    320       O  
ATOM    362  CB  MET A  48      49.180   7.268  24.182  1.00 29.68           C  
ANISOU  362  CB  MET A  48     3265   4090   3921    722   -315    357       C  
ATOM    363  CG  MET A  48      50.576   7.698  23.734  1.00 41.11           C  
ANISOU  363  CG  MET A  48     4580   5665   5373    735   -325    380       C  
ATOM    364  SD  MET A  48      51.846   6.822  24.673  1.00 52.75           S  
ANISOU  364  SD  MET A  48     6017   7210   6815    852   -361    394       S  
ATOM    365  CE  MET A  48      51.719   5.301  23.743  1.00 47.78           C  
ANISOU  365  CE  MET A  48     5456   6545   6154    974   -302    380       C  
ATOM    366  N   PRO A  49      46.585   5.647  23.516  1.00 32.47           N  
ANISOU  366  N   PRO A  49     3856   4228   4253    733   -240    315       N  
ATOM    367  CA  PRO A  49      45.368   5.045  24.072  1.00 31.63           C  
ANISOU  367  CA  PRO A  49     3864   4019   4134    719   -234    302       C  
ATOM    368  C   PRO A  49      45.257   5.558  25.485  1.00 36.23           C  
ANISOU  368  C   PRO A  49     4453   4592   4719    689   -276    309       C  
ATOM    369  O   PRO A  49      46.292   5.810  26.124  1.00 31.14           O  
ANISOU  369  O   PRO A  49     3749   4009   4072    718   -313    322       O  
ATOM    370  CB  PRO A  49      45.661   3.525  24.078  1.00 31.48           C  
ANISOU  370  CB  PRO A  49     3917   3965   4079    822   -221    299       C  
ATOM    371  CG  PRO A  49      46.744   3.340  22.995  1.00 32.60           C  
ANISOU  371  CG  PRO A  49     3987   4184   4215    886   -201    300       C  
ATOM    372  CD  PRO A  49      47.530   4.644  22.961  1.00 31.58           C  
ANISOU  372  CD  PRO A  49     3729   4156   4114    838   -222    317       C  
ATOM    373  N   PRO A  50      44.022   5.758  25.957  1.00 28.05           N  
ANISOU  373  N   PRO A  50     3483   3488   3685    630   -273    301       N  
ATOM    374  CA  PRO A  50      43.823   6.288  27.307  1.00 31.50           C  
ANISOU  374  CA  PRO A  50     3934   3916   4119    602   -310    305       C  
ATOM    375  C   PRO A  50      44.175   5.218  28.332  1.00 33.12           C  
ANISOU  375  C   PRO A  50     4196   4098   4288    676   -328    314       C  
ATOM    376  O   PRO A  50      44.044   4.035  28.067  1.00 37.09           O  
ANISOU  376  O   PRO A  50     4764   4558   4770    729   -306    314       O  
ATOM    377  CB  PRO A  50      42.310   6.560  27.361  1.00 28.33           C  
ANISOU  377  CB  PRO A  50     3593   3450   3722    534   -289    295       C  
ATOM    378  CG  PRO A  50      41.729   5.486  26.389  1.00 26.62           C  
ANISOU  378  CG  PRO A  50     3432   3186   3495    553   -245    288       C  
ATOM    379  CD  PRO A  50      42.748   5.511  25.251  1.00 30.01           C  
ANISOU  379  CD  PRO A  50     3793   3674   3937    587   -234    289       C  
ATOM    380  N   GLU A  51      44.599   5.658  29.498  1.00 33.66           N  
ANISOU  380  N   GLU A  51     4249   4192   4349    677   -372    321       N  
ATOM    381  CA  GLU A  51      44.915   4.784  30.611  1.00 43.08           C  
ANISOU  381  CA  GLU A  51     5497   5366   5505    742   -396    332       C  
ATOM    382  C   GLU A  51      43.831   5.023  31.653  1.00 40.63           C  
ANISOU  382  C   GLU A  51     5256   5001   5181    693   -402    329       C  
ATOM    383  O   GLU A  51      43.445   6.166  31.908  1.00 37.98           O  
ANISOU  383  O   GLU A  51     4892   4679   4861    626   -414    320       O  
ATOM    384  CB  GLU A  51      46.297   5.137  31.164  1.00 54.64           C  
ANISOU  384  CB  GLU A  51     6881   6914   6966    782   -446    343       C  
ATOM    385  CG  GLU A  51      46.615   4.527  32.528  1.00 79.70           C  
ANISOU  385  CG  GLU A  51    10104  10076  10100    839   -483    355       C  
ATOM    386  CD  GLU A  51      48.077   4.721  32.961  1.00 92.61           C  
ANISOU  386  CD  GLU A  51    11653  11805  11728    890   -535    368       C  
ATOM    387  OE1 GLU A  51      48.962   4.792  32.071  1.00101.52           O  
ANISOU  387  OE1 GLU A  51    12695  13003  12873    917   -529    372       O  
ATOM    388  OE2 GLU A  51      48.334   4.784  34.190  1.00 86.79           O  
ANISOU  388  OE2 GLU A  51    10933  11078  10965    904   -580    376       O  
ATOM    389  N   PRO A  52      43.304   3.943  32.234  1.00 40.68           N  
ANISOU  389  N   PRO A  52     5359   4945   5153    725   -390    338       N  
ATOM    390  CA  PRO A  52      42.300   4.041  33.303  1.00 35.13           C  
ANISOU  390  CA  PRO A  52     4723   4198   4427    686   -391    341       C  
ATOM    391  C   PRO A  52      42.771   4.974  34.413  1.00 35.79           C  
ANISOU  391  C   PRO A  52     4770   4327   4502    676   -440    340       C  
ATOM    392  O   PRO A  52      43.945   4.968  34.785  1.00 38.30           O  
ANISOU  392  O   PRO A  52     5045   4695   4813    726   -481    347       O  
ATOM    393  CB  PRO A  52      42.223   2.606  33.831  1.00 37.18           C  
ANISOU  393  CB  PRO A  52     5080   4401   4645    745   -385    360       C  
ATOM    394  CG  PRO A  52      42.619   1.752  32.620  1.00 42.99           C  
ANISOU  394  CG  PRO A  52     5821   5123   5390    792   -360    357       C  
ATOM    395  CD  PRO A  52      43.720   2.551  31.974  1.00 40.12           C  
ANISOU  395  CD  PRO A  52     5342   4844   5058    808   -378    349       C  
ATOM    396  N   LYS A  53      41.856   5.783  34.918  1.00 31.48           N  
ANISOU  396  N   LYS A  53     4239   3767   3955    614   -438    330       N  
ATOM    397  CA  LYS A  53      42.162   6.755  35.947  1.00 32.14           C  
ANISOU  397  CA  LYS A  53     4301   3884   4028    598   -484    323       C  
ATOM    398  C   LYS A  53      42.523   6.047  37.237  1.00 39.91           C  
ANISOU  398  C   LYS A  53     5339   4862   4962    653   -513    339       C  
ATOM    399  O   LYS A  53      41.886   5.077  37.618  1.00 44.35           O  
ANISOU  399  O   LYS A  53     5981   5375   5494    672   -488    354       O  
ATOM    400  CB  LYS A  53      40.920   7.622  36.185  1.00 31.97           C  
ANISOU  400  CB  LYS A  53     4303   3839   4007    533   -465    307       C  
ATOM    401  CG  LYS A  53      40.981   8.541  37.394  1.00 33.01           C  
ANISOU  401  CG  LYS A  53     4441   3988   4114    519   -507    296       C  
ATOM    402  CD  LYS A  53      42.022   9.648  37.214  1.00 36.09           C  
ANISOU  402  CD  LYS A  53     4753   4429   4531    499   -557    282       C  
ATOM    403  CE  LYS A  53      42.014  10.630  38.382  1.00 37.09           C  
ANISOU  403  CE  LYS A  53     4897   4563   4631    479   -603    265       C  
ATOM    404  NZ  LYS A  53      42.861  11.783  38.057  1.00 40.56           N  
ANISOU  404  NZ  LYS A  53     5269   5042   5102    440   -649    252       N  
ATOM    405  N   ARG A  54      43.519   6.561  37.932  1.00 39.81           N  
ANISOU  405  N   ARG A  54     5285   4902   4941    672   -570    338       N  
ATOM    406  CA  ARG A  54      43.994   5.928  39.131  1.00 43.54           C  
ANISOU  406  CA  ARG A  54     5801   5378   5365    730   -605    354       C  
ATOM    407  C   ARG A  54      43.198   6.511  40.281  1.00 43.19           C  
ANISOU  407  C   ARG A  54     5809   5315   5286    694   -615    345       C  
ATOM    408  O   ARG A  54      42.864   7.692  40.230  1.00 36.31           O  
ANISOU  408  O   ARG A  54     4909   4456   4433    636   -622    322       O  
ATOM    409  CB  ARG A  54      45.482   6.199  39.286  1.00 46.97           C  
ANISOU  409  CB  ARG A  54     6156   5887   5803    767   -665    357       C  
ATOM    410  CG  ARG A  54      46.297   5.629  38.145  1.00 55.61           C  
ANISOU  410  CG  ARG A  54     7192   7012   6926    812   -651    367       C  
ATOM    411  CD  ARG A  54      47.760   5.589  38.504  1.00 67.64           C  
ANISOU  411  CD  ARG A  54     8645   8616   8439    869   -709    379       C  
ATOM    412  NE  ARG A  54      48.334   6.924  38.597  1.00 76.86           N  
ANISOU  412  NE  ARG A  54     9726   9849   9629    806   -755    365       N  
ATOM    413  CZ  ARG A  54      49.077   7.476  37.646  1.00 86.04           C  
ANISOU  413  CZ  ARG A  54    10786  11075  10830    782   -760    364       C  
ATOM    414  NH1 ARG A  54      49.340   6.807  36.528  1.00 81.51           N  
ANISOU  414  NH1 ARG A  54    10181  10512  10276    824   -718    373       N  
ATOM    415  NH2 ARG A  54      49.560   8.697  37.815  1.00 89.10           N  
ANISOU  415  NH2 ARG A  54    11106  11514  11234    715   -806    354       N  
ATOM    416  N   PRO A  55      42.869   5.680  41.302  1.00 37.04           N  
ANISOU  416  N   PRO A  55     5114   4506   4455    731   -614    365       N  
ATOM    417  CA  PRO A  55      42.040   6.120  42.445  1.00 35.20           C  
ANISOU  417  CA  PRO A  55     4938   4258   4177    704   -616    359       C  
ATOM    418  C   PRO A  55      42.578   7.400  43.070  1.00 41.20           C  
ANISOU  418  C   PRO A  55     5656   5066   4934    683   -674    333       C  
ATOM    419  O   PRO A  55      43.798   7.645  43.081  1.00 35.27           O  
ANISOU  419  O   PRO A  55     4846   4363   4194    704   -728    331       O  
ATOM    420  CB  PRO A  55      42.157   4.971  43.460  1.00 36.20           C  
ANISOU  420  CB  PRO A  55     5145   4364   4246    764   -625    390       C  
ATOM    421  CG  PRO A  55      42.497   3.757  42.642  1.00 40.57           C  
ANISOU  421  CG  PRO A  55     5711   4889   4815    809   -602    413       C  
ATOM    422  CD  PRO A  55      43.274   4.267  41.400  1.00 34.13           C  
ANISOU  422  CD  PRO A  55     4794   4113   4060    803   -610    395       C  
ATOM    423  N   TRP A  56      41.657   8.209  43.571  1.00 34.53           N  
ANISOU  423  N   TRP A  56     4842   4208   4072    641   -662    313       N  
ATOM    424  CA  TRP A  56      41.984   9.455  44.226  1.00 39.03           C  
ANISOU  424  CA  TRP A  56     5394   4806   4630    616   -715    284       C  
ATOM    425  C   TRP A  56      41.645   9.301  45.696  1.00 45.78           C  
ANISOU  425  C   TRP A  56     6325   5657   5411    643   -731    287       C  
ATOM    426  O   TRP A  56      41.028   8.306  46.109  1.00 45.58           O  
ANISOU  426  O   TRP A  56     6364   5605   5350    669   -693    314       O  
ATOM    427  CB  TRP A  56      41.179  10.600  43.609  1.00 39.53           C  
ANISOU  427  CB  TRP A  56     5439   4855   4726    556   -691    255       C  
ATOM    428  CG  TRP A  56      39.702  10.330  43.564  1.00 41.41           C  
ANISOU  428  CG  TRP A  56     5729   5056   4950    544   -621    258       C  
ATOM    429  CD1 TRP A  56      38.789  10.604  44.546  1.00 40.54           C  
ANISOU  429  CD1 TRP A  56     5679   4936   4787    544   -606    250       C  
ATOM    430  CD2 TRP A  56      38.959   9.748  42.474  1.00 39.84           C  
ANISOU  430  CD2 TRP A  56     5520   4831   4785    526   -558    272       C  
ATOM    431  NE1 TRP A  56      37.527  10.222  44.136  1.00 42.41           N  
ANISOU  431  NE1 TRP A  56     5938   5151   5025    527   -537    261       N  
ATOM    432  CE2 TRP A  56      37.606   9.692  42.870  1.00 41.57           C  
ANISOU  432  CE2 TRP A  56     5791   5032   4973    512   -508    274       C  
ATOM    433  CE3 TRP A  56      39.310   9.248  41.218  1.00 39.08           C  
ANISOU  433  CE3 TRP A  56     5378   4730   4739    522   -538    283       C  
ATOM    434  CZ2 TRP A  56      36.608   9.154  42.053  1.00 37.22           C  
ANISOU  434  CZ2 TRP A  56     5243   4459   4441    488   -445    288       C  
ATOM    435  CZ3 TRP A  56      38.313   8.704  40.400  1.00 40.29           C  
ANISOU  435  CZ3 TRP A  56     5544   4854   4909    501   -476    293       C  
ATOM    436  CH2 TRP A  56      36.981   8.672  40.816  1.00 36.56           C  
ANISOU  436  CH2 TRP A  56     5119   4365   4407    480   -432    296       C  
ATOM    437  N   SER A  57      42.060  10.264  46.505  1.00 47.56           N  
ANISOU  437  N   SER A  57     6551   5907   5611    633   -789    262       N  
ATOM    438  CA  SER A  57      41.680  10.209  47.908  1.00 52.73           C  
ANISOU  438  CA  SER A  57     7284   6561   6191    658   -803    261       C  
ATOM    439  C   SER A  57      40.741  11.360  48.182  1.00 45.15           C  
ANISOU  439  C   SER A  57     6351   5586   5216    621   -789    224       C  
ATOM    440  O   SER A  57      40.722  12.340  47.446  1.00 47.92           O  
ANISOU  440  O   SER A  57     6660   5933   5613    578   -794    197       O  
ATOM    441  CB  SER A  57      42.902  10.268  48.826  1.00 57.46           C  
ANISOU  441  CB  SER A  57     7877   7202   6754    689   -886    260       C  
ATOM    442  OG  SER A  57      43.563  11.504  48.677  1.00 63.72           O  
ANISOU  442  OG  SER A  57     8618   8020   7572    646   -945    226       O  
ATOM    443  N   GLY A  58      39.950  11.230  49.231  1.00 44.42           N  
ANISOU  443  N   GLY A  58     6334   5488   5057    641   -768    225       N  
ATOM    444  CA  GLY A  58      39.019  12.272  49.591  1.00 41.96           C  
ANISOU  444  CA  GLY A  58     6055   5167   4719    622   -752    190       C  
ATOM    445  C   GLY A  58      37.783  12.171  48.720  1.00 45.16           C  
ANISOU  445  C   GLY A  58     6451   5551   5156    599   -669    197       C  
ATOM    446  O   GLY A  58      37.608  11.221  47.942  1.00 43.50           O  
ANISOU  446  O   GLY A  58     6219   5329   4981    594   -626    229       O  
ATOM    447  N   VAL A  59      36.912  13.155  48.863  1.00 42.01           N  
ANISOU  447  N   VAL A  59     6072   5147   4742    588   -650    165       N  
ATOM    448  CA  VAL A  59      35.696  13.170  48.105  1.00 41.65           C  
ANISOU  448  CA  VAL A  59     6012   5091   4720    569   -576    169       C  
ATOM    449  C   VAL A  59      35.936  14.076  46.905  1.00 39.77           C  
ANISOU  449  C   VAL A  59     5716   4838   4556    532   -590    144       C  
ATOM    450  O   VAL A  59      36.236  15.256  47.067  1.00 47.48           O  
ANISOU  450  O   VAL A  59     6698   5808   5532    523   -636    106       O  
ATOM    451  CB  VAL A  59      34.523  13.708  48.977  1.00 43.93           C  
ANISOU  451  CB  VAL A  59     6355   5393   4943    590   -541    151       C  
ATOM    452  CG1 VAL A  59      33.227  13.739  48.189  1.00 35.32           C  
ANISOU  452  CG1 VAL A  59     5240   4305   3875    572   -466    157       C  
ATOM    453  CG2 VAL A  59      34.382  12.895  50.273  1.00 35.62           C  
ANISOU  453  CG2 VAL A  59     5365   4361   3809    625   -533    176       C  
ATOM    454  N   LEU A  60      35.826  13.520  45.705  1.00 36.58           N  
ANISOU  454  N   LEU A  60     5263   4426   4211    508   -554    166       N  
ATOM    455  CA  LEU A  60      35.971  14.299  44.481  1.00 34.56           C  
ANISOU  455  CA  LEU A  60     4951   4157   4022    472   -559    149       C  
ATOM    456  C   LEU A  60      34.706  15.133  44.256  1.00 39.95           C  
ANISOU  456  C   LEU A  60     5646   4834   4701    466   -517    127       C  
ATOM    457  O   LEU A  60      33.596  14.601  44.304  1.00 42.07           O  
ANISOU  457  O   LEU A  60     5927   5112   4947    474   -455    144       O  
ATOM    458  CB  LEU A  60      36.239  13.364  43.296  1.00 35.58           C  
ANISOU  458  CB  LEU A  60     5030   4284   4207    455   -531    179       C  
ATOM    459  CG  LEU A  60      36.489  13.973  41.908  1.00 40.62           C  
ANISOU  459  CG  LEU A  60     5604   4913   4915    418   -532    170       C  
ATOM    460  CD1 LEU A  60      37.619  13.245  41.203  1.00 36.35           C  
ANISOU  460  CD1 LEU A  60     5015   4383   4414    416   -550    191       C  
ATOM    461  CD2 LEU A  60      35.207  13.917  41.060  1.00 42.55           C  
ANISOU  461  CD2 LEU A  60     5840   5149   5179    400   -465    175       C  
ATOM    462  N   ASP A  61      34.855  16.441  44.056  1.00 36.15           N  
ANISOU  462  N   ASP A  61     5163   4338   4236    452   -551     91       N  
ATOM    463  CA  ASP A  61      33.688  17.265  43.802  1.00 36.69           C  
ANISOU  463  CA  ASP A  61     5244   4399   4299    457   -514     71       C  
ATOM    464  C   ASP A  61      33.202  17.070  42.367  1.00 37.01           C  
ANISOU  464  C   ASP A  61     5226   4435   4400    428   -469     88       C  
ATOM    465  O   ASP A  61      33.908  17.419  41.420  1.00 35.36           O  
ANISOU  465  O   ASP A  61     4977   4212   4248    395   -495     86       O  
ATOM    466  CB  ASP A  61      33.970  18.744  44.063  1.00 43.88           C  
ANISOU  466  CB  ASP A  61     6187   5283   5203    457   -569     26       C  
ATOM    467  CG  ASP A  61      32.770  19.617  43.755  1.00 55.56           C  
ANISOU  467  CG  ASP A  61     7683   6752   6676    475   -532      4       C  
ATOM    468  OD1 ASP A  61      32.512  19.874  42.561  1.00 55.70           O  
ANISOU  468  OD1 ASP A  61     7657   6758   6747    449   -511     10       O  
ATOM    469  OD2 ASP A  61      32.059  20.018  44.703  1.00 62.18           O  
ANISOU  469  OD2 ASP A  61     8577   7598   7451    520   -520    -18       O  
ATOM    470  N   ALA A  62      32.002  16.508  42.219  1.00 31.86           N  
ANISOU  470  N   ALA A  62     4570   3802   3733    437   -402    106       N  
ATOM    471  CA  ALA A  62      31.425  16.261  40.904  1.00 32.45           C  
ANISOU  471  CA  ALA A  62     4594   3879   3857    409   -358    122       C  
ATOM    472  C   ALA A  62      30.185  17.116  40.668  1.00 37.65           C  
ANISOU  472  C   ALA A  62     5253   4548   4506    423   -323    105       C  
ATOM    473  O   ALA A  62      29.143  16.600  40.280  1.00 38.44           O  
ANISOU  473  O   ALA A  62     5329   4674   4603    418   -267    125       O  
ATOM    474  CB  ALA A  62      31.087  14.795  40.754  1.00 33.25           C  
ANISOU  474  CB  ALA A  62     4684   3994   3954    397   -312    162       C  
ATOM    475  N   THR A  63      30.297  18.418  40.906  1.00 33.17           N  
ANISOU  475  N   THR A  63     4712   3959   3930    442   -360     69       N  
ATOM    476  CA  THR A  63      29.141  19.319  40.827  1.00 33.33           C  
ANISOU  476  CA  THR A  63     4744   3989   3932    474   -331     49       C  
ATOM    477  C   THR A  63      29.166  20.234  39.604  1.00 35.21           C  
ANISOU  477  C   THR A  63     4956   4198   4224    454   -345     37       C  
ATOM    478  O   THR A  63      28.202  20.941  39.339  1.00 38.06           O  
ANISOU  478  O   THR A  63     5320   4566   4575    483   -321     25       O  
ATOM    479  CB  THR A  63      29.028  20.209  42.090  1.00 31.87           C  
ANISOU  479  CB  THR A  63     4630   3797   3683    525   -358     11       C  
ATOM    480  OG1 THR A  63      30.149  21.085  42.153  1.00 34.58           O  
ANISOU  480  OG1 THR A  63     5004   4090   4043    509   -432    -17       O  
ATOM    481  CG2 THR A  63      28.993  19.375  43.377  1.00 35.86           C  
ANISOU  481  CG2 THR A  63     5167   4334   4124    548   -345     23       C  
ATOM    482  N   THR A  64      30.269  20.219  38.857  1.00 36.17           N  
ANISOU  482  N   THR A  64     5051   4291   4399    408   -383     45       N  
ATOM    483  CA  THR A  64      30.395  21.008  37.639  1.00 31.34           C  
ANISOU  483  CA  THR A  64     4414   3654   3841    381   -396     41       C  
ATOM    484  C   THR A  64      31.036  20.266  36.455  1.00 35.93           C  
ANISOU  484  C   THR A  64     4932   4239   4480    331   -390     71       C  
ATOM    485  O   THR A  64      31.840  19.343  36.616  1.00 36.09           O  
ANISOU  485  O   THR A  64     4935   4269   4507    315   -399     88       O  
ATOM    486  CB  THR A  64      31.212  22.287  37.891  1.00 37.47           C  
ANISOU  486  CB  THR A  64     5236   4382   4620    373   -465     10       C  
ATOM    487  OG1 THR A  64      32.569  21.934  38.183  1.00 39.00           O  
ANISOU  487  OG1 THR A  64     5420   4570   4827    338   -513     16       O  
ATOM    488  CG2 THR A  64      30.631  23.083  39.069  1.00 35.76           C  
ANISOU  488  CG2 THR A  64     5094   4152   4340    429   -476    -26       C  
ATOM    489  N   PHE A  65      30.666  20.668  35.249  1.00 29.94           N  
ANISOU  489  N   PHE A  65     4142   3474   3759    313   -374     77       N  
ATOM    490  CA  PHE A  65      31.288  20.113  34.073  1.00 31.25           C  
ANISOU  490  CA  PHE A  65     4253   3644   3976    270   -369    101       C  
ATOM    491  C   PHE A  65      32.790  20.367  34.051  1.00 35.87           C  
ANISOU  491  C   PHE A  65     4831   4212   4587    237   -425    100       C  
ATOM    492  O   PHE A  65      33.245  21.395  34.505  1.00 31.71           O  
ANISOU  492  O   PHE A  65     4339   3657   4053    232   -473     79       O  
ATOM    493  CB  PHE A  65      30.655  20.693  32.832  1.00 25.80           C  
ANISOU  493  CB  PHE A  65     3537   2949   3316    258   -349    105       C  
ATOM    494  CG  PHE A  65      29.247  20.219  32.603  1.00 28.66           C  
ANISOU  494  CG  PHE A  65     3883   3345   3661    280   -292    114       C  
ATOM    495  CD1 PHE A  65      28.996  18.885  32.395  1.00 26.49           C  
ANISOU  495  CD1 PHE A  65     3579   3100   3386    265   -254    137       C  
ATOM    496  CD2 PHE A  65      28.169  21.123  32.600  1.00 30.46           C  
ANISOU  496  CD2 PHE A  65     4129   3576   3870    316   -279    100       C  
ATOM    497  CE1 PHE A  65      27.688  18.432  32.168  1.00 31.32           C  
ANISOU  497  CE1 PHE A  65     4171   3748   3981    273   -204    148       C  
ATOM    498  CE2 PHE A  65      26.871  20.682  32.377  1.00 27.23           C  
ANISOU  498  CE2 PHE A  65     3692   3212   3443    333   -227    111       C  
ATOM    499  CZ  PHE A  65      26.634  19.338  32.156  1.00 28.22           C  
ANISOU  499  CZ  PHE A  65     3782   3370   3571    305   -190    136       C  
ATOM    500  N   GLN A  66      33.537  19.411  33.516  1.00 29.27           N  
ANISOU  500  N   GLN A  66     3950   3393   3777    215   -419    123       N  
ATOM    501  CA  GLN A  66      34.973  19.521  33.390  1.00 27.60           C  
ANISOU  501  CA  GLN A  66     3714   3184   3590    185   -466    129       C  
ATOM    502  C   GLN A  66      35.391  20.131  32.050  1.00 29.14           C  
ANISOU  502  C   GLN A  66     3867   3374   3832    143   -472    139       C  
ATOM    503  O   GLN A  66      34.539  20.490  31.217  1.00 30.53           O  
ANISOU  503  O   GLN A  66     4039   3539   4020    140   -442    141       O  
ATOM    504  CB  GLN A  66      35.590  18.130  33.565  1.00 27.19           C  
ANISOU  504  CB  GLN A  66     3637   3160   3536    197   -455    149       C  
ATOM    505  CG  GLN A  66      36.070  17.940  34.970  1.00 32.18           C  
ANISOU  505  CG  GLN A  66     4303   3795   4128    221   -490    140       C  
ATOM    506  CD  GLN A  66      37.337  18.751  35.241  1.00 40.24           C  
ANISOU  506  CD  GLN A  66     5314   4817   5160    194   -558    131       C  
ATOM    507  OE1 GLN A  66      37.774  19.570  34.397  1.00 40.02           O  
ANISOU  507  OE1 GLN A  66     5256   4782   5167    152   -577    132       O  
ATOM    508  NE2 GLN A  66      37.953  18.507  36.400  1.00 38.50           N  
ANISOU  508  NE2 GLN A  66     5115   4608   4907    212   -596    126       N  
ATOM    509  N   ASN A  67      36.703  20.259  31.847  1.00 35.29           N  
ANISOU  509  N   ASN A  67     4611   4165   4633    110   -512    149       N  
ATOM    510  CA  ASN A  67      37.248  20.836  30.617  1.00 31.55           C  
ANISOU  510  CA  ASN A  67     4094   3694   4201     64   -519    164       C  
ATOM    511  C   ASN A  67      36.728  20.133  29.356  1.00 30.26           C  
ANISOU  511  C   ASN A  67     3892   3547   4058     67   -462    183       C  
ATOM    512  O   ASN A  67      36.436  18.937  29.367  1.00 28.33           O  
ANISOU  512  O   ASN A  67     3638   3321   3804     97   -426    189       O  
ATOM    513  CB  ASN A  67      38.763  20.751  30.635  1.00 38.65           C  
ANISOU  513  CB  ASN A  67     4946   4626   5115     33   -560    178       C  
ATOM    514  CG  ASN A  67      39.390  21.549  31.779  1.00 35.21           C  
ANISOU  514  CG  ASN A  67     4543   4174   4659     14   -627    160       C  
ATOM    515  OD1 ASN A  67      38.901  22.598  32.171  1.00 35.23           O  
ANISOU  515  OD1 ASN A  67     4605   4132   4649      5   -651    138       O  
ATOM    516  ND2 ASN A  67      40.487  21.056  32.288  1.00 36.80           N  
ANISOU  516  ND2 ASN A  67     4711   4416   4857     12   -659    168       N  
ATOM    517  N   VAL A  68      36.629  20.908  28.281  1.00 23.02           N  
ANISOU  517  N   VAL A  68     2960   2620   3167     34   -459    191       N  
ATOM    518  CA  VAL A  68      36.306  20.392  26.962  1.00 22.82           C  
ANISOU  518  CA  VAL A  68     2896   2614   3162     30   -414    209       C  
ATOM    519  C   VAL A  68      37.605  20.028  26.250  1.00 33.09           C  
ANISOU  519  C   VAL A  68     4134   3953   4486      4   -421    231       C  
ATOM    520  O   VAL A  68      38.587  20.763  26.333  1.00 29.55           O  
ANISOU  520  O   VAL A  68     3668   3511   4050    -34   -463    238       O  
ATOM    521  CB  VAL A  68      35.561  21.454  26.130  1.00 34.95           C  
ANISOU  521  CB  VAL A  68     4447   4123   4710     11   -408    210       C  
ATOM    522  CG1 VAL A  68      35.362  20.979  24.700  1.00 28.50           C  
ANISOU  522  CG1 VAL A  68     3587   3329   3911      1   -368    230       C  
ATOM    523  CG2 VAL A  68      34.228  21.797  26.776  1.00 26.78           C  
ANISOU  523  CG2 VAL A  68     3466   3062   3649     48   -397    189       C  
ATOM    524  N   CYS A  69      37.613  18.894  25.555  1.00 21.76           N  
ANISOU  524  N   CYS A  69     2668   2546   3055     23   -381    242       N  
ATOM    525  CA  CYS A  69      38.796  18.477  24.805  1.00 28.07           C  
ANISOU  525  CA  CYS A  69     3405   3390   3870     12   -379    263       C  
ATOM    526  C   CYS A  69      39.200  19.541  23.783  1.00 37.54           C  
ANISOU  526  C   CYS A  69     4572   4597   5093    -41   -389    280       C  
ATOM    527  O   CYS A  69      38.349  20.108  23.099  1.00 25.43           O  
ANISOU  527  O   CYS A  69     3058   3038   3565    -55   -373    280       O  
ATOM    528  CB  CYS A  69      38.557  17.129  24.121  1.00 21.84           C  
ANISOU  528  CB  CYS A  69     2603   2618   3075     48   -331    267       C  
ATOM    529  SG  CYS A  69      38.338  15.756  25.270  1.00 35.57           S  
ANISOU  529  SG  CYS A  69     4381   4348   4786    103   -322    256       S  
ATOM    530  N   TYR A  70      40.502  19.808  23.692  1.00 29.58           N  
ANISOU  530  N   TYR A  70     3513   3628   4097    -70   -418    297       N  
ATOM    531  CA  TYR A  70      41.009  20.893  22.852  1.00 33.88           C  
ANISOU  531  CA  TYR A  70     4029   4182   4661   -133   -433    319       C  
ATOM    532  C   TYR A  70      40.506  20.756  21.425  1.00 34.90           C  
ANISOU  532  C   TYR A  70     4143   4320   4799   -135   -386    332       C  
ATOM    533  O   TYR A  70      40.563  19.674  20.840  1.00 29.69           O  
ANISOU  533  O   TYR A  70     3454   3693   4133    -98   -347    336       O  
ATOM    534  CB  TYR A  70      42.537  20.921  22.864  1.00 33.97           C  
ANISOU  534  CB  TYR A  70     3968   4256   4681   -163   -461    341       C  
ATOM    535  CG  TYR A  70      43.119  22.315  22.946  1.00 39.64           C  
ANISOU  535  CG  TYR A  70     4684   4964   5412   -243   -512    355       C  
ATOM    536  CD1 TYR A  70      43.612  22.806  24.146  1.00 42.26           C  
ANISOU  536  CD1 TYR A  70     5036   5285   5738   -266   -571    343       C  
ATOM    537  CD2 TYR A  70      43.169  23.141  21.829  1.00 40.19           C  
ANISOU  537  CD2 TYR A  70     4740   5033   5496   -299   -505    380       C  
ATOM    538  CE1 TYR A  70      44.145  24.075  24.235  1.00 43.63           C  
ANISOU  538  CE1 TYR A  70     5216   5441   5920   -347   -623    354       C  
ATOM    539  CE2 TYR A  70      43.701  24.416  21.908  1.00 45.60           C  
ANISOU  539  CE2 TYR A  70     5433   5701   6192   -379   -554    396       C  
ATOM    540  CZ  TYR A  70      44.187  24.878  23.114  1.00 53.68           C  
ANISOU  540  CZ  TYR A  70     6478   6708   7210   -405   -614    382       C  
ATOM    541  OH  TYR A  70      44.717  26.146  23.194  1.00 76.40           O  
ANISOU  541  OH  TYR A  70     9372   9561  10095   -494   -668    396       O  
ATOM    542  N   GLN A  71      40.011  21.851  20.861  1.00 27.84           N  
ANISOU  542  N   GLN A  71     3274   3391   3913   -174   -393    340       N  
ATOM    543  CA  GLN A  71      39.392  21.759  19.553  1.00 28.86           C  
ANISOU  543  CA  GLN A  71     3396   3525   4045   -173   -351    352       C  
ATOM    544  C   GLN A  71      39.305  23.096  18.880  1.00 29.93           C  
ANISOU  544  C   GLN A  71     3547   3634   4191   -228   -369    372       C  
ATOM    545  O   GLN A  71      39.305  24.132  19.526  1.00 33.94           O  
ANISOU  545  O   GLN A  71     4096   4098   4703   -258   -412    368       O  
ATOM    546  CB  GLN A  71      37.958  21.180  19.655  1.00 26.59           C  
ANISOU  546  CB  GLN A  71     3155   3205   3743   -124   -320    328       C  
ATOM    547  CG  GLN A  71      37.006  22.034  20.480  1.00 22.11           C  
ANISOU  547  CG  GLN A  71     2652   2580   3170   -118   -345    309       C  
ATOM    548  CD  GLN A  71      35.732  21.300  20.878  1.00 30.49           C  
ANISOU  548  CD  GLN A  71     3745   3628   4213    -69   -316    287       C  
ATOM    549  OE1 GLN A  71      34.661  21.570  20.335  1.00 28.69           O  
ANISOU  549  OE1 GLN A  71     3536   3386   3980    -60   -297    285       O  
ATOM    550  NE2 GLN A  71      35.851  20.332  21.803  1.00 31.85           N  
ANISOU  550  NE2 GLN A  71     3920   3810   4372    -37   -312    272       N  
ATOM    551  N   TYR A  72      39.162  23.037  17.564  1.00 36.62           N  
ANISOU  551  N   TYR A  72     4370   4504   5040   -237   -335    393       N  
ATOM    552  CA  TYR A  72      38.794  24.177  16.737  1.00 39.00           C  
ANISOU  552  CA  TYR A  72     4696   4775   5346   -277   -342    413       C  
ATOM    553  C   TYR A  72      37.420  24.758  17.147  1.00 43.86           C  
ANISOU  553  C   TYR A  72     5387   5323   5955   -250   -352    391       C  
ATOM    554  O   TYR A  72      36.465  24.024  17.438  1.00 35.11           O  
ANISOU  554  O   TYR A  72     4295   4210   4834   -196   -328    366       O  
ATOM    555  CB  TYR A  72      38.788  23.712  15.281  1.00 35.97           C  
ANISOU  555  CB  TYR A  72     4273   4437   4958   -276   -297    435       C  
ATOM    556  CG  TYR A  72      38.408  24.772  14.299  1.00 42.49           C  
ANISOU  556  CG  TYR A  72     5122   5238   5784   -313   -299    462       C  
ATOM    557  CD1 TYR A  72      37.082  24.915  13.866  1.00 38.65           C  
ANISOU  557  CD1 TYR A  72     4680   4717   5288   -282   -284    452       C  
ATOM    558  CD2 TYR A  72      39.373  25.650  13.801  1.00 44.82           C  
ANISOU  558  CD2 TYR A  72     5395   5548   6088   -382   -318    500       C  
ATOM    559  CE1 TYR A  72      36.735  25.903  12.971  1.00 45.50           C  
ANISOU  559  CE1 TYR A  72     5574   5562   6153   -310   -290    478       C  
ATOM    560  CE2 TYR A  72      39.042  26.633  12.898  1.00 49.04           C  
ANISOU  560  CE2 TYR A  72     5958   6054   6619   -418   -321    529       C  
ATOM    561  CZ  TYR A  72      37.725  26.761  12.477  1.00 58.12           C  
ANISOU  561  CZ  TYR A  72     7158   7166   7758   -378   -308    517       C  
ATOM    562  OH  TYR A  72      37.415  27.767  11.568  1.00 65.49           O  
ANISOU  562  OH  TYR A  72     8125   8071   8687   -409   -314    549       O  
ATOM    563  N   VAL A  73      37.345  26.079  17.206  1.00 37.81           N  
ANISOU  563  N   VAL A  73     4667   4505   5193   -286   -388    401       N  
ATOM    564  CA  VAL A  73      36.121  26.761  17.582  1.00 38.22           C  
ANISOU  564  CA  VAL A  73     4792   4494   5234   -252   -400    381       C  
ATOM    565  C   VAL A  73      35.523  27.470  16.360  1.00 41.72           C  
ANISOU  565  C   VAL A  73     5255   4921   5676   -262   -389    406       C  
ATOM    566  O   VAL A  73      36.165  28.286  15.766  1.00 41.30           O  
ANISOU  566  O   VAL A  73     5205   4856   5631   -318   -408    437       O  
ATOM    567  CB  VAL A  73      36.377  27.756  18.705  1.00 36.75           C  
ANISOU  567  CB  VAL A  73     4665   4250   5048   -271   -455    367       C  
ATOM    568  CG1 VAL A  73      35.135  28.635  18.936  1.00 40.99           C  
ANISOU  568  CG1 VAL A  73     5284   4721   5570   -230   -467    349       C  
ATOM    569  CG2 VAL A  73      36.724  26.990  19.959  1.00 32.65           C  
ANISOU  569  CG2 VAL A  73     4133   3749   4523   -247   -463    339       C  
ATOM    570  N  AASP A  74      34.281  27.133  16.026  0.20 46.85           N  
ANISOU  570  N  AASP A  74     5916   5572   6312   -208   -360    393       N  
ATOM    571  N  BASP A  74      34.301  27.113  15.969  0.80 47.67           N  
ANISOU  571  N  BASP A  74     6018   5679   6417   -209   -359    394       N  
ATOM    572  CA AASP A  74      33.605  27.699  14.864  0.20 48.42           C  
ANISOU  572  CA AASP A  74     6130   5762   6505   -207   -350    415       C  
ATOM    573  CA BASP A  74      33.724  27.632  14.725  0.80 48.96           C  
ANISOU  573  CA BASP A  74     6191   5838   6575   -212   -347    419       C  
ATOM    574  C  AASP A  74      33.479  29.209  14.973  0.20 51.08           C  
ANISOU  574  C  AASP A  74     6541   6027   6842   -223   -393    426       C  
ATOM    575  C  BASP A  74      33.404  29.130  14.891  0.80 50.81           C  
ANISOU  575  C  BASP A  74     6503   5997   6806   -220   -388    427       C  
ATOM    576  O  AASP A  74      33.117  29.734  16.025  0.20 51.08           O  
ANISOU  576  O  AASP A  74     6596   5976   6835   -196   -421    401       O  
ATOM    577  O  BASP A  74      32.888  29.562  15.918  0.80 51.18           O  
ANISOU  577  O  BASP A  74     6603   5999   6846   -184   -412    399       O  
ATOM    578  CB AASP A  74      32.211  27.091  14.723  0.20 44.83           C  
ANISOU  578  CB AASP A  74     5676   5325   6033   -143   -319    395       C  
ATOM    579  CB BASP A  74      32.495  26.798  14.252  0.80 47.18           C  
ANISOU  579  CB BASP A  74     5948   5644   6333   -157   -307    405       C  
ATOM    580  CG AASP A  74      31.484  27.583  13.492  0.20 42.63           C  
ANISOU  580  CG AASP A  74     5406   5046   5744   -136   -309    418       C  
ATOM    581  CG BASP A  74      32.893  25.403  13.611  0.80 70.14           C  
ANISOU  581  CG BASP A  74     8790   8619   9240   -162   -265    407       C  
ATOM    582  OD1AASP A  74      32.130  28.181  12.607  0.20 38.57           O  
ANISOU  582  OD1AASP A  74     4893   4527   5236   -182   -316    452       O  
ATOM    583  OD1BASP A  74      33.532  25.373  12.525  0.80 66.75           O  
ANISOU  583  OD1BASP A  74     8330   8220   8812   -196   -252    435       O  
ATOM    584  OD2AASP A  74      30.263  27.363  13.412  0.20 41.55           O  
ANISOU  584  OD2AASP A  74     5274   4920   5592    -86   -294    404       O  
ATOM    585  OD2BASP A  74      32.538  24.331  14.177  0.80 61.22           O  
ANISOU  585  OD2BASP A  74     7646   7511   8105   -130   -246    381       O  
ATOM    586  N   THR A  75      33.764  29.916  13.885  1.00 54.38           N  
ANISOU  586  N   THR A  75     6966   6435   7262   -265   -397    465       N  
ATOM    587  CA  THR A  75      33.617  31.373  13.922  1.00 69.15           C  
ANISOU  587  CA  THR A  75     8920   8226   9129   -282   -441    479       C  
ATOM    588  C   THR A  75      32.927  31.975  12.696  1.00 70.70           C  
ANISOU  588  C   THR A  75     9143   8408   9313   -271   -432    509       C  
ATOM    589  O   THR A  75      33.041  33.177  12.458  1.00 69.85           O  
ANISOU  589  O   THR A  75     9103   8235   9203   -299   -467    533       O  
ATOM    590  CB  THR A  75      34.982  32.098  14.121  1.00 81.78           C  
ANISOU  590  CB  THR A  75    10532   9798  10744   -372   -481    503       C  
ATOM    591  OG1 THR A  75      35.994  31.451  13.333  1.00 80.09           O  
ANISOU  591  OG1 THR A  75    10233   9658  10540   -427   -453    535       O  
ATOM    592  CG2 THR A  75      35.382  32.099  15.593  1.00 77.66           C  
ANISOU  592  CG2 THR A  75    10031   9249  10226   -373   -514    468       C  
ATOM    593  N   LEU A  76      32.198  31.154  11.944  1.00 73.26           N  
ANISOU  593  N   LEU A  76     9420   8790   9626   -230   -390    508       N  
ATOM    594  CA  LEU A  76      31.528  31.625  10.737  1.00 74.01           C  
ANISOU  594  CA  LEU A  76     9532   8882   9705   -216   -382    537       C  
ATOM    595  C   LEU A  76      30.527  32.761  11.007  1.00 75.70           C  
ANISOU  595  C   LEU A  76     9834   9025   9906   -162   -414    532       C  
ATOM    596  O   LEU A  76      30.509  33.767  10.290  1.00 79.83           O  
ANISOU  596  O   LEU A  76    10410   9503  10421   -179   -435    566       O  
ATOM    597  CB  LEU A  76      30.836  30.467  10.022  1.00 80.10           C  
ANISOU  597  CB  LEU A  76    10240   9730  10464   -179   -336    529       C  
ATOM    598  CG  LEU A  76      30.222  30.837   8.666  1.00 85.76           C  
ANISOU  598  CG  LEU A  76    10965  10459  11162   -169   -327    561       C  
ATOM    599  CD1 LEU A  76      31.325  31.189   7.677  1.00 87.24           C  
ANISOU  599  CD1 LEU A  76    11142  10655  11351   -244   -325    608       C  
ATOM    600  CD2 LEU A  76      29.348  29.709   8.130  1.00 86.78           C  
ANISOU  600  CD2 LEU A  76    11040  10658  11274   -128   -290    544       C  
ATOM    601  N   TYR A  77      29.701  32.608  12.038  1.00 71.53           N  
ANISOU  601  N   TYR A  77     9323   8486   9370    -94   -417    490       N  
ATOM    602  CA  TYR A  77      28.680  33.614  12.356  1.00 66.76           C  
ANISOU  602  CA  TYR A  77     8798   7822   8747    -25   -443    480       C  
ATOM    603  C   TYR A  77      28.678  34.016  13.832  1.00 66.36           C  
ANISOU  603  C   TYR A  77     8803   7716   8694      4   -472    441       C  
ATOM    604  O   TYR A  77      27.786  33.630  14.583  1.00 66.20           O  
ANISOU  604  O   TYR A  77     8774   7719   8659     76   -458    406       O  
ATOM    605  CB  TYR A  77      27.291  33.095  11.986  1.00 56.73           C  
ANISOU  605  CB  TYR A  77     7491   6609   7455     55   -413    469       C  
ATOM    606  CG  TYR A  77      27.070  32.860  10.514  1.00 60.53           C  
ANISOU  606  CG  TYR A  77     7934   7136   7928     40   -392    504       C  
ATOM    607  CD1 TYR A  77      27.108  33.909   9.610  1.00 56.32           C  
ANISOU  607  CD1 TYR A  77     7455   6558   7386     29   -415    543       C  
ATOM    608  CD2 TYR A  77      26.780  31.586  10.027  1.00 66.32           C  
ANISOU  608  CD2 TYR A  77     8583   7956   8659     38   -352    497       C  
ATOM    609  CE1 TYR A  77      26.888  33.704   8.266  1.00 57.26           C  
ANISOU  609  CE1 TYR A  77     7542   6723   7492     19   -397    576       C  
ATOM    610  CE2 TYR A  77      26.549  31.366   8.672  1.00 65.39           C  
ANISOU  610  CE2 TYR A  77     8435   7882   8528     27   -335    526       C  
ATOM    611  CZ  TYR A  77      26.608  32.432   7.795  1.00 65.15           C  
ANISOU  611  CZ  TYR A  77     8454   7811   8487     19   -357    566       C  
ATOM    612  OH  TYR A  77      26.377  32.233   6.442  1.00 66.20           O  
ANISOU  612  OH  TYR A  77     8561   7990   8603      9   -341    595       O  
ATOM    613  N   PRO A  78      29.670  34.810  14.241  1.00 76.18           N  
ANISOU  613  N   PRO A  78    10104   8890   9949    -55   -514    449       N  
ATOM    614  CA  PRO A  78      29.949  35.275  15.615  1.00 77.86           C  
ANISOU  614  CA  PRO A  78    10381   9043  10160    -48   -551    414       C  
ATOM    615  C   PRO A  78      28.737  35.739  16.436  1.00 75.92           C  
ANISOU  615  C   PRO A  78    10199   8763   9885     59   -559    375       C  
ATOM    616  O   PRO A  78      28.078  36.700  16.044  1.00 80.18           O  
ANISOU  616  O   PRO A  78    10810   9248  10406    106   -578    385       O  
ATOM    617  CB  PRO A  78      30.880  36.472  15.386  1.00 79.65           C  
ANISOU  617  CB  PRO A  78    10686   9184  10394   -127   -602    443       C  
ATOM    618  CG  PRO A  78      31.607  36.134  14.119  1.00 82.18           C  
ANISOU  618  CG  PRO A  78    10938   9554  10731   -206   -579    493       C  
ATOM    619  CD  PRO A  78      30.638  35.344  13.263  1.00 80.12           C  
ANISOU  619  CD  PRO A  78    10613   9369  10461   -145   -529    498       C  
ATOM    620  N   GLY A  79      28.471  35.090  17.571  1.00 72.98           N  
ANISOU  620  N   GLY A  79     9804   8420   9504    101   -546    334       N  
ATOM    621  CA  GLY A  79      27.414  35.525  18.486  1.00 68.58           C  
ANISOU  621  CA  GLY A  79     9306   7837   8914    203   -552    295       C  
ATOM    622  C   GLY A  79      26.010  35.085  18.092  1.00 65.58           C  
ANISOU  622  C   GLY A  79     8878   7526   8514    293   -510    293       C  
ATOM    623  O   GLY A  79      25.030  35.359  18.792  1.00 60.95           O  
ANISOU  623  O   GLY A  79     8323   6939   7897    387   -506    264       O  
ATOM    624  N   PHE A  80      25.922  34.409  16.949  1.00 62.76           N  
ANISOU  624  N   PHE A  80     8441   7233   8170    262   -478    324       N  
ATOM    625  CA  PHE A  80      24.668  33.882  16.417  1.00 56.35           C  
ANISOU  625  CA  PHE A  80     7570   6498   7342    327   -440    327       C  
ATOM    626  C   PHE A  80      24.390  32.507  17.055  1.00 52.26           C  
ANISOU  626  C   PHE A  80     6968   6065   6824    331   -399    304       C  
ATOM    627  O   PHE A  80      25.244  31.621  17.005  1.00 47.11           O  
ANISOU  627  O   PHE A  80     6267   5439   6195    260   -385    308       O  
ATOM    628  CB  PHE A  80      24.821  33.802  14.897  1.00 50.31           C  
ANISOU  628  CB  PHE A  80     6770   5756   6589    282   -431    370       C  
ATOM    629  CG  PHE A  80      23.832  32.918  14.216  1.00 51.09           C  
ANISOU  629  CG  PHE A  80     6785   5950   6677    313   -391    376       C  
ATOM    630  CD1 PHE A  80      22.494  33.292  14.118  1.00 45.31           C  
ANISOU  630  CD1 PHE A  80     6057   5244   5915    406   -387    372       C  
ATOM    631  CD2 PHE A  80      24.246  31.719  13.634  1.00 48.22           C  
ANISOU  631  CD2 PHE A  80     6340   5651   6330    251   -360    386       C  
ATOM    632  CE1 PHE A  80      21.583  32.488  13.477  1.00 49.79           C  
ANISOU  632  CE1 PHE A  80     6542   5904   6470    425   -355    379       C  
ATOM    633  CE2 PHE A  80      23.337  30.897  12.979  1.00 45.19           C  
ANISOU  633  CE2 PHE A  80     5886   5350   5934    270   -329    390       C  
ATOM    634  CZ  PHE A  80      22.000  31.281  12.901  1.00 50.64           C  
ANISOU  634  CZ  PHE A  80     6575   6070   6596    353   -328    387       C  
ATOM    635  N   GLU A  81      23.219  32.338  17.672  1.00 50.79           N  
ANISOU  635  N   GLU A  81     6768   5921   6608    414   -379    281       N  
ATOM    636  CA  GLU A  81      22.932  31.129  18.464  1.00 57.98           C  
ANISOU  636  CA  GLU A  81     7613   6902   7513    416   -343    259       C  
ATOM    637  C   GLU A  81      23.019  29.846  17.631  1.00 57.09           C  
ANISOU  637  C   GLU A  81     7411   6862   7419    357   -309    278       C  
ATOM    638  O   GLU A  81      23.337  28.766  18.149  1.00 50.90           O  
ANISOU  638  O   GLU A  81     6585   6112   6642    323   -287    267       O  
ATOM    639  CB  GLU A  81      21.552  31.208  19.131  1.00 57.45           C  
ANISOU  639  CB  GLU A  81     7538   6883   7408    515   -323    239       C  
ATOM    640  N   GLY A  82      22.728  29.982  16.341  1.00 53.44           N  
ANISOU  640  N   GLY A  82     6926   6418   6959    348   -306    306       N  
ATOM    641  CA  GLY A  82      22.757  28.856  15.437  1.00 51.48           C  
ANISOU  641  CA  GLY A  82     6604   6233   6722    297   -278    322       C  
ATOM    642  C   GLY A  82      24.104  28.165  15.469  1.00 47.38           C  
ANISOU  642  C   GLY A  82     6073   5698   6231    219   -275    323       C  
ATOM    643  O   GLY A  82      24.165  26.949  15.436  1.00 49.22           O  
ANISOU  643  O   GLY A  82     6253   5979   6468    189   -248    319       O  
ATOM    644  N   THR A  83      25.188  28.931  15.529  1.00 49.76           N  
ANISOU  644  N   THR A  83     6423   5933   6549    185   -305    331       N  
ATOM    645  CA  THR A  83      26.514  28.326  15.634  1.00 51.64           C  
ANISOU  645  CA  THR A  83     6643   6165   6812    116   -305    334       C  
ATOM    646  C   THR A  83      27.027  28.199  17.082  1.00 47.83           C  
ANISOU  646  C   THR A  83     6184   5658   6332    118   -317    307       C  
ATOM    647  O   THR A  83      27.703  27.243  17.416  1.00 48.01           O  
ANISOU  647  O   THR A  83     6170   5704   6365     86   -304    301       O  
ATOM    648  CB  THR A  83      27.536  29.026  14.725  1.00 54.24           C  
ANISOU  648  CB  THR A  83     6992   6458   7159     59   -326    366       C  
ATOM    649  OG1 THR A  83      27.600  30.414  15.063  1.00 61.26           O  
ANISOU  649  OG1 THR A  83     7959   7272   8044     73   -367    368       O  
ATOM    650  CG2 THR A  83      27.129  28.885  13.255  1.00 52.62           C  
ANISOU  650  CG2 THR A  83     6755   6290   6948     52   -308    394       C  
ATOM    651  N   GLU A  84      26.657  29.135  17.943  1.00 46.81           N  
ANISOU  651  N   GLU A  84     6115   5482   6187    164   -343    289       N  
ATOM    652  CA  GLU A  84      27.203  29.178  19.287  1.00 46.94           C  
ANISOU  652  CA  GLU A  84     6165   5468   6202    164   -362    262       C  
ATOM    653  C   GLU A  84      26.794  27.997  20.170  1.00 44.68           C  
ANISOU  653  C   GLU A  84     5838   5236   5903    187   -330    241       C  
ATOM    654  O   GLU A  84      27.585  27.544  21.015  1.00 43.15           O  
ANISOU  654  O   GLU A  84     5645   5036   5714    163   -338    228       O  
ATOM    655  CB  GLU A  84      26.814  30.482  19.970  1.00 51.14           C  
ANISOU  655  CB  GLU A  84     6784   5935   6714    216   -397    245       C  
ATOM    656  CG  GLU A  84      27.347  31.725  19.257  1.00 68.00           C  
ANISOU  656  CG  GLU A  84     8980   7998   8860    185   -437    267       C  
ATOM    657  CD  GLU A  84      28.869  31.843  19.310  1.00 76.41           C  
ANISOU  657  CD  GLU A  84    10051   9029   9951     94   -468    279       C  
ATOM    658  OE1 GLU A  84      29.534  30.892  19.813  1.00 73.33           O  
ANISOU  658  OE1 GLU A  84     9612   8678   9572     62   -456    271       O  
ATOM    659  OE2 GLU A  84      29.397  32.896  18.852  1.00 77.22           O  
ANISOU  659  OE2 GLU A  84    10210   9069  10062     55   -505    299       O  
ATOM    660  N   MET A  85      25.567  27.512  19.991  1.00 36.15           N  
ANISOU  660  N   MET A  85     4723   4210   4804    231   -296    239       N  
ATOM    661  CA  MET A  85      25.088  26.410  20.809  1.00 40.37           C  
ANISOU  661  CA  MET A  85     5222   4795   5322    247   -265    223       C  
ATOM    662  C   MET A  85      26.039  25.192  20.724  1.00 34.83           C  
ANISOU  662  C   MET A  85     4481   4112   4642    186   -252    230       C  
ATOM    663  O   MET A  85      26.125  24.428  21.658  1.00 44.53           O  
ANISOU  663  O   MET A  85     5703   5355   5860    189   -241    217       O  
ATOM    664  CB  MET A  85      23.657  26.018  20.423  1.00 38.59           C  
ANISOU  664  CB  MET A  85     4953   4635   5075    285   -231    228       C  
ATOM    665  CG  MET A  85      23.499  25.551  18.974  1.00 41.90           C  
ANISOU  665  CG  MET A  85     5324   5089   5509    249   -216    253       C  
ATOM    666  SD  MET A  85      21.769  25.131  18.617  1.00 54.25           S  
ANISOU  666  SD  MET A  85     6832   6737   7042    290   -184    258       S  
ATOM    667  CE  MET A  85      21.666  23.553  19.429  1.00 33.95           C  
ANISOU  667  CE  MET A  85     4222   4213   4464    257   -150    248       C  
ATOM    668  N   TRP A  86      26.740  25.034  19.607  1.00 24.74           N  
ANISOU  668  N   TRP A  86     3179   2833   3388    138   -254    251       N  
ATOM    669  CA  TRP A  86      27.642  23.906  19.411  1.00 33.01           C  
ANISOU  669  CA  TRP A  86     4191   3901   4452     93   -240    257       C  
ATOM    670  C   TRP A  86      29.056  24.149  19.948  1.00 34.40           C  
ANISOU  670  C   TRP A  86     4384   4042   4645     61   -270    256       C  
ATOM    671  O   TRP A  86      29.855  23.219  20.051  1.00 30.85           O  
ANISOU  671  O   TRP A  86     3907   3611   4204     37   -262    258       O  
ATOM    672  CB  TRP A  86      27.701  23.508  17.925  1.00 30.32           C  
ANISOU  672  CB  TRP A  86     3811   3587   4121     62   -222    279       C  
ATOM    673  CG  TRP A  86      26.363  23.329  17.333  1.00 29.72           C  
ANISOU  673  CG  TRP A  86     3716   3549   4029     85   -200    282       C  
ATOM    674  CD1 TRP A  86      25.726  24.192  16.485  1.00 33.79           C  
ANISOU  674  CD1 TRP A  86     4236   4063   4538    102   -207    295       C  
ATOM    675  CD2 TRP A  86      25.454  22.236  17.555  1.00 30.22           C  
ANISOU  675  CD2 TRP A  86     3749   3658   4073     94   -170    273       C  
ATOM    676  NE1 TRP A  86      24.488  23.688  16.145  1.00 32.25           N  
ANISOU  676  NE1 TRP A  86     4009   3920   4324    121   -184    295       N  
ATOM    677  CE2 TRP A  86      24.297  22.496  16.795  1.00 29.04           C  
ANISOU  677  CE2 TRP A  86     3582   3543   3910    112   -162    282       C  
ATOM    678  CE3 TRP A  86      25.518  21.053  18.302  1.00 30.61           C  
ANISOU  678  CE3 TRP A  86     3790   3724   4118     84   -152    263       C  
ATOM    679  CZ2 TRP A  86      23.202  21.624  16.778  1.00 35.65           C  
ANISOU  679  CZ2 TRP A  86     4383   4434   4727    114   -136    279       C  
ATOM    680  CZ3 TRP A  86      24.419  20.192  18.279  1.00 29.45           C  
ANISOU  680  CZ3 TRP A  86     3617   3622   3950     84   -125    261       C  
ATOM    681  CH2 TRP A  86      23.288  20.484  17.533  1.00 34.80           C  
ANISOU  681  CH2 TRP A  86     4270   4339   4615     95   -118    269       C  
ATOM    682  N   ASN A  87      29.380  25.393  20.269  1.00 31.16           N  
ANISOU  682  N   ASN A  87     4020   3582   4236     61   -308    253       N  
ATOM    683  CA  ASN A  87      30.745  25.722  20.684  1.00 30.29           C  
ANISOU  683  CA  ASN A  87     3922   3444   4142     19   -342    256       C  
ATOM    684  C   ASN A  87      31.074  25.305  22.116  1.00 33.20           C  
ANISOU  684  C   ASN A  87     4306   3809   4499     34   -355    232       C  
ATOM    685  O   ASN A  87      30.186  25.238  22.956  1.00 33.50           O  
ANISOU  685  O   ASN A  87     4369   3848   4513     82   -346    211       O  
ATOM    686  CB  ASN A  87      30.986  27.240  20.543  1.00 32.77           C  
ANISOU  686  CB  ASN A  87     4291   3698   4460      3   -385    262       C  
ATOM    687  CG  ASN A  87      31.318  27.640  19.115  1.00 42.52           C  
ANISOU  687  CG  ASN A  87     5508   4935   5714    -39   -383    296       C  
ATOM    688  OD1 ASN A  87      31.737  26.809  18.292  1.00 50.55           O  
ANISOU  688  OD1 ASN A  87     6466   5999   6742    -66   -356    314       O  
ATOM    689  ND2 ASN A  87      31.127  28.905  18.811  1.00 44.60           N  
ANISOU  689  ND2 ASN A  87     5827   5145   5975    -41   -411    306       N  
ATOM    690  N   PRO A  88      32.369  25.067  22.418  1.00 36.23           N  
ANISOU  690  N   PRO A  88     4673   4195   4897     -6   -376    236       N  
ATOM    691  CA  PRO A  88      32.794  24.748  23.802  1.00 36.82           C  
ANISOU  691  CA  PRO A  88     4766   4266   4958      7   -396    215       C  
ATOM    692  C   PRO A  88      32.235  25.704  24.847  1.00 36.50           C  
ANISOU  692  C   PRO A  88     4797   4180   4893     41   -424    188       C  
ATOM    693  O   PRO A  88      32.284  26.914  24.663  1.00 30.51           O  
ANISOU  693  O   PRO A  88     4083   3374   4137     28   -457    188       O  
ATOM    694  CB  PRO A  88      34.321  24.933  23.760  1.00 35.33           C  
ANISOU  694  CB  PRO A  88     4555   4079   4791    -50   -432    229       C  
ATOM    695  CG  PRO A  88      34.697  24.612  22.327  1.00 39.26           C  
ANISOU  695  CG  PRO A  88     4996   4609   5311    -82   -406    259       C  
ATOM    696  CD  PRO A  88      33.520  25.219  21.501  1.00 33.36           C  
ANISOU  696  CD  PRO A  88     4274   3842   4560    -64   -388    264       C  
ATOM    697  N   ASN A  89      31.717  25.172  25.945  1.00 35.31           N  
ANISOU  697  N   ASN A  89     4662   4041   4714     85   -413    167       N  
ATOM    698  CA  ASN A  89      31.208  26.025  26.995  1.00 31.44           C  
ANISOU  698  CA  ASN A  89     4241   3512   4192    125   -437    138       C  
ATOM    699  C   ASN A  89      31.979  25.854  28.313  1.00 36.78           C  
ANISOU  699  C   ASN A  89     4942   4181   4852    122   -470    119       C  
ATOM    700  O   ASN A  89      31.490  26.249  29.368  1.00 33.42           O  
ANISOU  700  O   ASN A  89     4572   3735   4390    166   -481     92       O  
ATOM    701  CB  ASN A  89      29.691  25.817  27.173  1.00 30.39           C  
ANISOU  701  CB  ASN A  89     4113   3403   4030    191   -394    128       C  
ATOM    702  CG  ASN A  89      29.342  24.427  27.716  1.00 38.38           C  
ANISOU  702  CG  ASN A  89     5087   4469   5026    206   -354    129       C  
ATOM    703  OD1 ASN A  89      30.129  23.484  27.590  1.00 29.64           O  
ANISOU  703  OD1 ASN A  89     3943   3383   3937    172   -349    142       O  
ATOM    704  ND2 ASN A  89      28.138  24.296  28.309  1.00 35.90           N  
ANISOU  704  ND2 ASN A  89     4784   4180   4676    261   -323    117       N  
ATOM    705  N  AARG A  90      33.164  25.243  28.246  0.50 31.13           N  
ANISOU  705  N  AARG A  90     4185   3486   4157     76   -484    134       N  
ATOM    706  N  BARG A  90      33.168  25.246  28.228  0.50 31.06           N  
ANISOU  706  N  BARG A  90     4175   3477   4148     76   -484    134       N  
ATOM    707  CA AARG A  90      34.105  25.229  29.364  0.50 29.52           C  
ANISOU  707  CA AARG A  90     4000   3276   3940     63   -528    120       C  
ATOM    708  CA BARG A  90      34.109  25.141  29.343  0.50 29.92           C  
ANISOU  708  CA BARG A  90     4047   3331   3992     64   -525    121       C  
ATOM    709  C  AARG A  90      35.474  25.346  28.744  0.50 32.55           C  
ANISOU  709  C  AARG A  90     4341   3669   4359     -5   -559    143       C  
ATOM    710  C  BARG A  90      35.479  25.331  28.738  0.50 32.53           C  
ANISOU  710  C  BARG A  90     4337   3667   4356     -5   -559    143       C  
ATOM    711  O  AARG A  90      35.608  25.286  27.521  0.50 33.21           O  
ANISOU  711  O  AARG A  90     4379   3767   4471    -33   -538    169       O  
ATOM    712  O  BARG A  90      35.621  25.309  27.514  0.50 33.28           O  
ANISOU  712  O  BARG A  90     4388   3775   4480    -34   -539    169       O  
ATOM    713  CB AARG A  90      34.041  23.931  30.188  0.50 31.13           C  
ANISOU  713  CB AARG A  90     4184   3521   4122     96   -502    117       C  
ATOM    714  CB BARG A  90      34.065  23.757  30.014  0.50 30.84           C  
ANISOU  714  CB BARG A  90     4135   3492   4090     94   -495    122       C  
ATOM    715  CG AARG A  90      32.839  23.794  31.108  0.50 35.03           C  
ANISOU  715  CG AARG A  90     4722   4016   4573    158   -476     95       C  
ATOM    716  CG BARG A  90      32.723  23.361  30.578  0.50 31.46           C  
ANISOU  716  CG BARG A  90     4239   3581   4134    153   -453    108       C  
ATOM    717  CD AARG A  90      32.555  25.079  31.899  0.50 37.54           C  
ANISOU  717  CD AARG A  90     5118   4285   4862    182   -515     64       C  
ATOM    718  CD BARG A  90      32.351  24.313  31.683  0.50 36.62           C  
ANISOU  718  CD BARG A  90     4966   4199   4749    187   -483     76       C  
ATOM    719  NE AARG A  90      31.319  24.926  32.660  0.50 41.95           N  
ANISOU  719  NE AARG A  90     5708   4857   5375    249   -480     46       N  
ATOM    720  NE BARG A  90      32.737  23.850  33.008  0.50 32.11           N  
ANISOU  720  NE BARG A  90     4419   3637   4143    204   -501     62       N  
ATOM    721  CZ AARG A  90      30.167  25.531  32.384  0.50 41.23           C  
ANISOU  721  CZ AARG A  90     5638   4759   5270    292   -455     37       C  
ATOM    722  CZ BARG A  90      32.773  24.643  34.081  0.50 38.63           C  
ANISOU  722  CZ BARG A  90     5313   4431   4933    226   -540     32       C  
ATOM    723  NH1AARG A  90      30.080  26.385  31.370  0.50 33.22           N  
ANISOU  723  NH1AARG A  90     4628   3713   4282    276   -466     44       N  
ATOM    724  NH1BARG A  90      32.481  25.945  33.951  0.50 37.28           N  
ANISOU  724  NH1BARG A  90     5196   4210   4758    232   -567     12       N  
ATOM    725  NH2AARG A  90      29.104  25.292  33.148  0.50 40.26           N  
ANISOU  725  NH2AARG A  90     5531   4663   5101    353   -420     24       N  
ATOM    726  NH2BARG A  90      33.112  24.150  35.269  0.50 27.52           N  
ANISOU  726  NH2BARG A  90     3927   3038   3491    243   -555     21       N  
ATOM    727  N   GLU A  91      36.488  25.508  29.584  1.00 31.41           N  
ANISOU  727  N   GLU A  91     4205   3522   4207    -31   -609    135       N  
ATOM    728  CA  GLU A  91      37.845  25.712  29.119  1.00 33.05           C  
ANISOU  728  CA  GLU A  91     4365   3748   4443   -101   -645    158       C  
ATOM    729  C   GLU A  91      38.349  24.547  28.228  1.00 33.53           C  
ANISOU  729  C   GLU A  91     4336   3874   4529   -106   -604    189       C  
ATOM    730  O   GLU A  91      38.148  23.358  28.554  1.00 30.38           O  
ANISOU  730  O   GLU A  91     3916   3509   4118    -60   -571    187       O  
ATOM    731  CB  GLU A  91      38.766  25.881  30.338  1.00 32.61           C  
ANISOU  731  CB  GLU A  91     4328   3692   4369   -119   -705    142       C  
ATOM    732  CG  GLU A  91      40.247  26.034  29.992  1.00 43.01           C  
ANISOU  732  CG  GLU A  91     5584   5044   5711   -194   -747    168       C  
ATOM    733  CD  GLU A  91      41.141  26.066  31.232  1.00 52.54           C  
ANISOU  733  CD  GLU A  91     6801   6264   6897   -210   -808    153       C  
ATOM    734  OE1 GLU A  91      40.629  26.415  32.310  1.00 39.98           O  
ANISOU  734  OE1 GLU A  91     5289   4631   5271   -178   -831    119       O  
ATOM    735  OE2 GLU A  91      42.352  25.728  31.126  1.00 63.51           O  
ANISOU  735  OE2 GLU A  91     8118   7711   8301   -250   -832    176       O  
ATOM    736  N   LEU A  92      39.002  24.887  27.116  1.00 30.22           N  
ANISOU  736  N   LEU A  92     3870   3471   4140   -159   -606    217       N  
ATOM    737  CA  LEU A  92      39.668  23.878  26.284  1.00 34.26           C  
ANISOU  737  CA  LEU A  92     4297   4049   4670   -163   -572    244       C  
ATOM    738  C   LEU A  92      40.921  23.369  26.982  1.00 36.31           C  
ANISOU  738  C   LEU A  92     4513   4357   4927   -173   -605    249       C  
ATOM    739  O   LEU A  92      41.689  24.148  27.486  1.00 34.51           O  
ANISOU  739  O   LEU A  92     4290   4123   4699   -221   -661    249       O  
ATOM    740  CB  LEU A  92      40.077  24.439  24.922  1.00 31.42           C  
ANISOU  740  CB  LEU A  92     3898   3701   4337   -218   -565    276       C  
ATOM    741  CG  LEU A  92      38.993  25.041  24.034  1.00 39.61           C  
ANISOU  741  CG  LEU A  92     4973   4698   5380   -215   -538    279       C  
ATOM    742  CD1 LEU A  92      39.612  25.320  22.652  1.00 35.78           C  
ANISOU  742  CD1 LEU A  92     4434   4242   4918   -268   -526    316       C  
ATOM    743  CD2 LEU A  92      37.822  24.071  23.937  1.00 35.86           C  
ANISOU  743  CD2 LEU A  92     4505   4228   4892   -147   -484    265       C  
ATOM    744  N   SER A  93      41.123  22.052  27.001  1.00 32.79           N  
ANISOU  744  N   SER A  93     4025   3958   4477   -127   -572    255       N  
ATOM    745  CA  SER A  93      42.292  21.514  27.612  1.00 28.18           C  
ANISOU  745  CA  SER A  93     3395   3426   3888   -124   -602    262       C  
ATOM    746  C   SER A  93      42.492  20.099  27.095  1.00 38.14           C  
ANISOU  746  C   SER A  93     4606   4736   5149    -72   -553    275       C  
ATOM    747  O   SER A  93      41.519  19.423  26.780  1.00 32.51           O  
ANISOU  747  O   SER A  93     3920   4002   4430    -31   -505    268       O  
ATOM    748  CB  SER A  93      42.111  21.500  29.133  1.00 32.18           C  
ANISOU  748  CB  SER A  93     3958   3906   4363    -96   -638    234       C  
ATOM    749  OG  SER A  93      43.186  20.834  29.784  1.00 30.23           O  
ANISOU  749  OG  SER A  93     3668   3713   4106    -81   -666    241       O  
ATOM    750  N   GLU A  94      43.741  19.633  27.038  1.00 32.23           N  
ANISOU  750  N   GLU A  94     3787   4054   4404    -72   -568    294       N  
ATOM    751  CA  GLU A  94      43.964  18.241  26.699  1.00 30.49           C  
ANISOU  751  CA  GLU A  94     3533   3874   4177     -8   -527    302       C  
ATOM    752  C   GLU A  94      43.564  17.374  27.886  1.00 31.40           C  
ANISOU  752  C   GLU A  94     3701   3966   4264     53   -530    284       C  
ATOM    753  O   GLU A  94      43.238  16.184  27.757  1.00 32.48           O  
ANISOU  753  O   GLU A  94     3851   4102   4389    110   -490    283       O  
ATOM    754  CB  GLU A  94      45.411  18.012  26.334  1.00 36.11           C  
ANISOU  754  CB  GLU A  94     4153   4671   4897    -14   -541    328       C  
ATOM    755  CG  GLU A  94      45.834  18.689  25.028  1.00 33.94           C  
ANISOU  755  CG  GLU A  94     3818   4430   4646    -71   -527    353       C  
ATOM    756  CD  GLU A  94      47.268  18.286  24.644  1.00 36.65           C  
ANISOU  756  CD  GLU A  94     4058   4876   4991    -64   -532    381       C  
ATOM    757  OE1 GLU A  94      47.477  17.140  24.159  1.00 29.90           O  
ANISOU  757  OE1 GLU A  94     3176   4059   4127      6   -490    386       O  
ATOM    758  OE2 GLU A  94      48.174  19.113  24.844  1.00 34.69           O  
ANISOU  758  OE2 GLU A  94     3759   4670   4751   -128   -578    398       O  
ATOM    759  N   ASP A  95      43.577  17.971  29.075  1.00 30.50           N  
ANISOU  759  N   ASP A  95     3625   3830   4135     38   -578    268       N  
ATOM    760  CA  ASP A  95      43.059  17.291  30.263  1.00 37.74           C  
ANISOU  760  CA  ASP A  95     4601   4719   5018     91   -580    251       C  
ATOM    761  C   ASP A  95      41.542  17.385  30.244  1.00 32.96           C  
ANISOU  761  C   ASP A  95     4065   4053   4405     99   -542    234       C  
ATOM    762  O   ASP A  95      40.965  18.305  30.827  1.00 31.35           O  
ANISOU  762  O   ASP A  95     3910   3811   4191     78   -563    216       O  
ATOM    763  CB  ASP A  95      43.619  17.922  31.542  1.00 32.03           C  
ANISOU  763  CB  ASP A  95     3896   3999   4275     74   -647    240       C  
ATOM    764  CG  ASP A  95      43.116  17.233  32.800  1.00 31.70           C  
ANISOU  764  CG  ASP A  95     3917   3933   4193    129   -649    225       C  
ATOM    765  OD1 ASP A  95      42.335  16.265  32.691  1.00 36.53           O  
ANISOU  765  OD1 ASP A  95     4560   4527   4795    174   -598    226       O  
ATOM    766  OD2 ASP A  95      43.511  17.668  33.903  1.00 40.52           O  
ANISOU  766  OD2 ASP A  95     5057   5052   5287    122   -703    213       O  
ATOM    767  N   CYS A  96      40.888  16.436  29.585  1.00 29.31           N  
ANISOU  767  N   CYS A  96     3609   3584   3944    130   -486    240       N  
ATOM    768  CA  CYS A  96      39.466  16.577  29.288  1.00 32.73           C  
ANISOU  768  CA  CYS A  96     4087   3974   4374    128   -447    229       C  
ATOM    769  C   CYS A  96      38.666  15.279  29.366  1.00 35.40           C  
ANISOU  769  C   CYS A  96     4458   4299   4692    170   -401    231       C  
ATOM    770  O   CYS A  96      37.469  15.273  29.083  1.00 25.07           O  
ANISOU  770  O   CYS A  96     3178   2966   3380    166   -367    225       O  
ATOM    771  CB  CYS A  96      39.284  17.207  27.904  1.00 37.96           C  
ANISOU  771  CB  CYS A  96     4717   4638   5067     90   -427    237       C  
ATOM    772  SG  CYS A  96      39.868  16.173  26.538  1.00 36.14           S  
ANISOU  772  SG  CYS A  96     4429   4449   4854    104   -387    258       S  
ATOM    773  N   LEU A  97      39.307  14.184  29.745  1.00 24.79           N  
ANISOU  773  N   LEU A  97     3112   2972   3334    210   -402    240       N  
ATOM    774  CA  LEU A  97      38.615  12.899  29.790  1.00 32.29           C  
ANISOU  774  CA  LEU A  97     4102   3902   4265    243   -362    244       C  
ATOM    775  C   LEU A  97      37.780  12.713  31.058  1.00 33.04           C  
ANISOU  775  C   LEU A  97     4260   3971   4324    257   -361    237       C  
ATOM    776  O   LEU A  97      38.230  12.117  32.035  1.00 31.00           O  
ANISOU  776  O   LEU A  97     4027   3715   4039    290   -380    242       O  
ATOM    777  CB  LEU A  97      39.613  11.755  29.626  1.00 27.60           C  
ANISOU  777  CB  LEU A  97     3491   3329   3666    288   -361    258       C  
ATOM    778  CG  LEU A  97      40.347  11.777  28.285  1.00 28.87           C  
ANISOU  778  CG  LEU A  97     3589   3524   3855    283   -350    266       C  
ATOM    779  CD1 LEU A  97      41.132  10.497  28.089  1.00 26.26           C  
ANISOU  779  CD1 LEU A  97     3254   3210   3514    343   -340    277       C  
ATOM    780  CD2 LEU A  97      39.360  11.982  27.143  1.00 25.39           C  
ANISOU  780  CD2 LEU A  97     3152   3063   3431    249   -309    262       C  
ATOM    781  N   TYR A  98      36.550  13.227  31.024  1.00 31.18           N  
ANISOU  781  N   TYR A  98     4048   3715   4084    234   -339    228       N  
ATOM    782  CA  TYR A  98      35.655  13.182  32.163  1.00 27.42           C  
ANISOU  782  CA  TYR A  98     3625   3224   3570    246   -332    222       C  
ATOM    783  C   TYR A  98      34.291  12.787  31.645  1.00 29.60           C  
ANISOU  783  C   TYR A  98     3916   3489   3841    231   -281    226       C  
ATOM    784  O   TYR A  98      33.998  12.968  30.458  1.00 30.01           O  
ANISOU  784  O   TYR A  98     3938   3544   3921    208   -261    226       O  
ATOM    785  CB  TYR A  98      35.584  14.571  32.807  1.00 29.92           C  
ANISOU  785  CB  TYR A  98     3950   3539   3881    235   -366    202       C  
ATOM    786  CG  TYR A  98      36.897  15.031  33.372  1.00 29.77           C  
ANISOU  786  CG  TYR A  98     3916   3532   3863    238   -423    197       C  
ATOM    787  CD1 TYR A  98      37.238  14.768  34.710  1.00 33.25           C  
ANISOU  787  CD1 TYR A  98     4392   3975   4265    265   -452    194       C  
ATOM    788  CD2 TYR A  98      37.813  15.721  32.577  1.00 29.44           C  
ANISOU  788  CD2 TYR A  98     3823   3504   3858    208   -451    198       C  
ATOM    789  CE1 TYR A  98      38.480  15.194  35.242  1.00 36.15           C  
ANISOU  789  CE1 TYR A  98     4742   4362   4633    264   -511    190       C  
ATOM    790  CE2 TYR A  98      39.056  16.148  33.098  1.00 28.95           C  
ANISOU  790  CE2 TYR A  98     3740   3463   3797    201   -507    197       C  
ATOM    791  CZ  TYR A  98      39.385  15.864  34.416  1.00 36.21           C  
ANISOU  791  CZ  TYR A  98     4692   4387   4679    229   -539    192       C  
ATOM    792  OH  TYR A  98      40.606  16.266  34.917  1.00 31.18           O  
ANISOU  792  OH  TYR A  98     4030   3777   4041    218   -599    191       O  
ATOM    793  N   LEU A  99      33.447  12.252  32.513  1.00 28.37           N  
ANISOU  793  N   LEU A  99     3803   3327   3648    241   -260    230       N  
ATOM    794  CA  LEU A  99      32.100  11.891  32.083  1.00 30.49           C  
ANISOU  794  CA  LEU A  99     4080   3597   3909    219   -214    237       C  
ATOM    795  C   LEU A  99      31.058  12.362  33.098  1.00 27.75           C  
ANISOU  795  C   LEU A  99     3758   3262   3524    226   -201    232       C  
ATOM    796  O   LEU A  99      31.385  12.750  34.207  1.00 29.13           O  
ANISOU  796  O   LEU A  99     3957   3437   3673    250   -227    223       O  
ATOM    797  CB  LEU A  99      31.993  10.378  31.821  1.00 27.48           C  
ANISOU  797  CB  LEU A  99     3724   3200   3519    215   -187    258       C  
ATOM    798  CG  LEU A  99      32.308   9.418  32.961  1.00 25.94           C  
ANISOU  798  CG  LEU A  99     3580   2990   3286    241   -193    272       C  
ATOM    799  CD1 LEU A  99      31.222   9.412  34.043  1.00 23.42           C  
ANISOU  799  CD1 LEU A  99     3295   2681   2923    234   -173    280       C  
ATOM    800  CD2 LEU A  99      32.491   7.971  32.429  1.00 28.68           C  
ANISOU  800  CD2 LEU A  99     3957   3307   3632    240   -176    291       C  
ATOM    801  N   ASN A 100      29.794  12.279  32.715  1.00 31.27           N  
ANISOU  801  N   ASN A 100     4196   3723   3963    205   -162    237       N  
ATOM    802  CA  ASN A 100      28.724  12.921  33.443  1.00 22.33           C  
ANISOU  802  CA  ASN A 100     3071   2615   2797    215   -145    231       C  
ATOM    803  C   ASN A 100      27.623  11.891  33.649  1.00 29.10           C  
ANISOU  803  C   ASN A 100     3940   3492   3624    193    -99    255       C  
ATOM    804  O   ASN A 100      27.308  11.145  32.728  1.00 27.33           O  
ANISOU  804  O   ASN A 100     3702   3265   3418    158    -78    268       O  
ATOM    805  CB  ASN A 100      28.198  14.041  32.568  1.00 19.64           C  
ANISOU  805  CB  ASN A 100     2694   2287   2483    211   -143    216       C  
ATOM    806  CG  ASN A 100      29.299  15.078  32.194  1.00 29.67           C  
ANISOU  806  CG  ASN A 100     3954   3533   3786    218   -189    197       C  
ATOM    807  OD1 ASN A 100      29.960  15.631  33.081  1.00 29.47           O  
ANISOU  807  OD1 ASN A 100     3954   3496   3748    240   -224    183       O  
ATOM    808  ND2 ASN A 100      29.452  15.370  30.876  1.00 23.49           N  
ANISOU  808  ND2 ASN A 100     3135   2746   3044    195   -189    198       N  
ATOM    809  N   VAL A 101      27.019  11.869  34.833  1.00 28.98           N  
ANISOU  809  N   VAL A 101     3951   3500   3560    209    -85    260       N  
ATOM    810  CA  VAL A 101      25.914  10.981  35.085  1.00 30.66           C  
ANISOU  810  CA  VAL A 101     4169   3740   3739    179    -40    287       C  
ATOM    811  C   VAL A 101      24.716  11.778  35.628  1.00 29.29           C  
ANISOU  811  C   VAL A 101     3975   3623   3530    197    -12    282       C  
ATOM    812  O   VAL A 101      24.856  12.493  36.592  1.00 34.37           O  
ANISOU  812  O   VAL A 101     4640   4275   4145    242    -25    265       O  
ATOM    813  CB  VAL A 101      26.304   9.904  36.145  1.00 30.52           C  
ANISOU  813  CB  VAL A 101     4208   3703   3684    181    -40    310       C  
ATOM    814  CG1 VAL A 101      25.081   9.109  36.570  1.00 27.33           C  
ANISOU  814  CG1 VAL A 101     3813   3334   3238    144      7    342       C  
ATOM    815  CG2 VAL A 101      27.430   8.964  35.626  1.00 24.07           C  
ANISOU  815  CG2 VAL A 101     3415   2833   2896    174    -64    318       C  
ATOM    816  N   TRP A 102      23.542  11.623  35.034  1.00 29.69           N  
ANISOU  816  N   TRP A 102     3985   3716   3579    165     25    296       N  
ATOM    817  CA  TRP A 102      22.293  12.102  35.657  1.00 29.10           C  
ANISOU  817  CA  TRP A 102     3887   3711   3458    183     61    300       C  
ATOM    818  C   TRP A 102      21.413  10.910  36.009  1.00 33.46           C  
ANISOU  818  C   TRP A 102     4439   4300   3974    131    104    340       C  
ATOM    819  O   TRP A 102      21.354   9.925  35.267  1.00 30.74           O  
ANISOU  819  O   TRP A 102     4093   3937   3651     70    111    361       O  
ATOM    820  CB  TRP A 102      21.480  12.969  34.712  1.00 30.15           C  
ANISOU  820  CB  TRP A 102     3961   3882   3612    189     72    288       C  
ATOM    821  CG  TRP A 102      22.073  14.312  34.295  1.00 31.28           C  
ANISOU  821  CG  TRP A 102     4103   3995   3786    238     34    251       C  
ATOM    822  CD1 TRP A 102      21.743  15.549  34.785  1.00 30.49           C  
ANISOU  822  CD1 TRP A 102     4006   3914   3664    300     29    226       C  
ATOM    823  CD2 TRP A 102      23.015  14.535  33.242  1.00 26.25           C  
ANISOU  823  CD2 TRP A 102     3463   3305   3206    223     -1    239       C  
ATOM    824  NE1 TRP A 102      22.432  16.535  34.100  1.00 31.59           N  
ANISOU  824  NE1 TRP A 102     4151   4007   3844    319    -10    200       N  
ATOM    825  CE2 TRP A 102      23.214  15.934  33.145  1.00 34.84           C  
ANISOU  825  CE2 TRP A 102     4553   4379   4304    270    -27    210       C  
ATOM    826  CE3 TRP A 102      23.676  13.694  32.354  1.00 30.28           C  
ANISOU  826  CE3 TRP A 102     3972   3779   3755    177    -10    250       C  
ATOM    827  CZ2 TRP A 102      24.095  16.503  32.216  1.00 32.35           C  
ANISOU  827  CZ2 TRP A 102     4235   4017   4038    263    -63    197       C  
ATOM    828  CZ3 TRP A 102      24.533  14.256  31.427  1.00 38.57           C  
ANISOU  828  CZ3 TRP A 102     5013   4792   4851    179    -42    235       C  
ATOM    829  CH2 TRP A 102      24.732  15.662  31.361  1.00 31.61           C  
ANISOU  829  CH2 TRP A 102     4130   3900   3981    217    -68    210       C  
ATOM    830  N   THR A 103      20.724  11.012  37.141  1.00 35.96           N  
ANISOU  830  N   THR A 103     4761   4671   4233    152    133    351       N  
ATOM    831  CA  THR A 103      19.821   9.972  37.601  1.00 32.69           C  
ANISOU  831  CA  THR A 103     4343   4302   3775     98    177    394       C  
ATOM    832  C   THR A 103      18.697  10.678  38.322  1.00 35.26           C  
ANISOU  832  C   THR A 103     4629   4720   4046    136    215    396       C  
ATOM    833  O   THR A 103      18.867  11.829  38.747  1.00 37.95           O  
ANISOU  833  O   THR A 103     4974   5069   4377    212    202    361       O  
ATOM    834  CB  THR A 103      20.519   8.986  38.622  1.00 39.57           C  
ANISOU  834  CB  THR A 103     5291   5129   4615     88    170    417       C  
ATOM    835  OG1 THR A 103      20.783   9.655  39.862  1.00 39.34           O  
ANISOU  835  OG1 THR A 103     5292   5115   4542    156    163    401       O  
ATOM    836  CG2 THR A 103      21.828   8.487  38.095  1.00 37.01           C  
ANISOU  836  CG2 THR A 103     5011   4715   4338     82    125    408       C  
ATOM    837  N   PRO A 104      17.551   9.995  38.475  1.00 40.13           N  
ANISOU  837  N   PRO A 104     5210   5411   4628     82    263    436       N  
ATOM    838  CA  PRO A 104      16.457  10.447  39.334  1.00 39.27           C  
ANISOU  838  CA  PRO A 104     5062   5405   4454    115    309    447       C  
ATOM    839  C   PRO A 104      16.950  10.784  40.729  1.00 39.90           C  
ANISOU  839  C   PRO A 104     5201   5476   4483    182    305    435       C  
ATOM    840  O   PRO A 104      18.021  10.356  41.129  1.00 45.46           O  
ANISOU  840  O   PRO A 104     5976   6102   5194    182    273    432       O  
ATOM    841  CB  PRO A 104      15.547   9.221  39.397  1.00 38.13           C  
ANISOU  841  CB  PRO A 104     4894   5315   4281     19    352    504       C  
ATOM    842  CG  PRO A 104      15.802   8.522  38.089  1.00 34.42           C  
ANISOU  842  CG  PRO A 104     4420   4786   3872    -57    329    510       C  
ATOM    843  CD  PRO A 104      17.245   8.696  37.836  1.00 38.33           C  
ANISOU  843  CD  PRO A 104     4979   5171   4414    -19    276    475       C  
ATOM    844  N   TYR A 105      16.164  11.563  41.454  1.00 38.29           N  
ANISOU  844  N   TYR A 105     4968   5356   4223    245    338    427       N  
ATOM    845  CA  TYR A 105      16.479  11.936  42.821  1.00 41.83           C  
ANISOU  845  CA  TYR A 105     5474   5810   4611    313    339    413       C  
ATOM    846  C   TYR A 105      15.251  11.676  43.648  1.00 46.11           C  
ANISOU  846  C   TYR A 105     5976   6469   5075    310    405    450       C  
ATOM    847  O   TYR A 105      14.199  12.251  43.367  1.00 51.69           O  
ANISOU  847  O   TYR A 105     6607   7267   5765    336    440    449       O  
ATOM    848  CB  TYR A 105      16.797  13.422  42.889  1.00 30.14           C  
ANISOU  848  CB  TYR A 105     4005   4312   3134    414    309    354       C  
ATOM    849  CG  TYR A 105      17.140  13.957  44.264  1.00 36.07           C  
ANISOU  849  CG  TYR A 105     4821   5064   3820    492    302    330       C  
ATOM    850  CD1 TYR A 105      18.468  14.202  44.619  1.00 38.07           C  
ANISOU  850  CD1 TYR A 105     5151   5223   4090    516    242    298       C  
ATOM    851  CD2 TYR A 105      16.144  14.263  45.198  1.00 32.26           C  
ANISOU  851  CD2 TYR A 105     4320   4682   3256    544    355    337       C  
ATOM    852  CE1 TYR A 105      18.799  14.709  45.879  1.00 35.99           C  
ANISOU  852  CE1 TYR A 105     4952   4959   3764    584    230    273       C  
ATOM    853  CE2 TYR A 105      16.468  14.763  46.462  1.00 30.44           C  
ANISOU  853  CE2 TYR A 105     4156   4450   2958    619    347    311       C  
ATOM    854  CZ  TYR A 105      17.797  14.994  46.781  1.00 40.39           C  
ANISOU  854  CZ  TYR A 105     5498   5609   4238    637    282    278       C  
ATOM    855  OH  TYR A 105      18.151  15.508  48.009  1.00 44.30           O  
ANISOU  855  OH  TYR A 105     6064   6101   4667    708    268    250       O  
ATOM    856  N   PRO A 106      15.360  10.809  44.659  1.00 46.60           N  
ANISOU  856  N   PRO A 106     6085   6535   5084    280    424    487       N  
ATOM    857  CA  PRO A 106      16.566  10.064  45.035  1.00 42.29           C  
ANISOU  857  CA  PRO A 106     5630   5889   4552    254    383    493       C  
ATOM    858  C   PRO A 106      16.841   9.001  43.998  1.00 43.43           C  
ANISOU  858  C   PRO A 106     5772   5970   4757    157    367    521       C  
ATOM    859  O   PRO A 106      15.992   8.791  43.131  1.00 42.59           O  
ANISOU  859  O   PRO A 106     5598   5910   4674    102    392    540       O  
ATOM    860  CB  PRO A 106      16.179   9.395  46.360  1.00 48.36           C  
ANISOU  860  CB  PRO A 106     6432   6710   5234    243    425    537       C  
ATOM    861  CG  PRO A 106      14.814   9.901  46.709  1.00 51.93           C  
ANISOU  861  CG  PRO A 106     6808   7296   5625    270    488    549       C  
ATOM    862  CD  PRO A 106      14.187  10.390  45.446  1.00 49.46           C  
ANISOU  862  CD  PRO A 106     6409   7017   5369    259    493    534       C  
ATOM    863  N   ARG A 107      17.995   8.341  44.071  1.00 43.20           N  
ANISOU  863  N   ARG A 107     5818   5843   4753    141    325    523       N  
ATOM    864  CA  ARG A 107      18.367   7.389  43.035  1.00 40.27           C  
ANISOU  864  CA  ARG A 107     5457   5402   4441     64    305    541       C  
ATOM    865  C   ARG A 107      17.364   6.231  42.976  1.00 42.25           C  
ANISOU  865  C   ARG A 107     5692   5697   4665    -37    352    602       C  
ATOM    866  O   ARG A 107      16.723   5.904  43.965  1.00 42.64           O  
ANISOU  866  O   ARG A 107     5748   5808   4645    -51    393    640       O  
ATOM    867  CB  ARG A 107      19.816   6.918  43.235  1.00 41.68           C  
ANISOU  867  CB  ARG A 107     5720   5475   4642     81    252    532       C  
ATOM    868  CG  ARG A 107      20.821   8.090  43.166  1.00 44.07           C  
ANISOU  868  CG  ARG A 107     6029   5740   4978    165    201    473       C  
ATOM    869  CD  ARG A 107      22.283   7.690  43.198  1.00 35.98           C  
ANISOU  869  CD  ARG A 107     5067   4623   3982    181    145    463       C  
ATOM    870  NE  ARG A 107      22.625   6.889  44.370  1.00 26.00           N  
ANISOU  870  NE  ARG A 107     3874   3342   2661    185    144    495       N  
ATOM    871  CZ  ARG A 107      23.004   7.383  45.542  1.00 25.05           C  
ANISOU  871  CZ  ARG A 107     3792   3236   2491    246    129    481       C  
ATOM    872  NH1 ARG A 107      23.095   8.690  45.717  1.00 27.24           N  
ANISOU  872  NH1 ARG A 107     4046   3537   2767    307    112    433       N  
ATOM    873  NH2 ARG A 107      23.297   6.565  46.549  1.00 25.52           N  
ANISOU  873  NH2 ARG A 107     3918   3280   2497    245    129    515       N  
ATOM    874  N   PRO A 108      17.223   5.622  41.796  1.00 47.39           N  
ANISOU  874  N   PRO A 108     6323   6315   5366   -110    344    613       N  
ATOM    875  CA  PRO A 108      16.303   4.498  41.645  1.00 53.31           C  
ANISOU  875  CA  PRO A 108     7064   7096   6094   -220    381    670       C  
ATOM    876  C   PRO A 108      16.686   3.393  42.637  1.00 55.87           C  
ANISOU  876  C   PRO A 108     7483   7373   6372   -253    384    715       C  
ATOM    877  O   PRO A 108      17.875   3.136  42.827  1.00 59.02           O  
ANISOU  877  O   PRO A 108     7960   7677   6787   -214    342    700       O  
ATOM    878  CB  PRO A 108      16.577   4.020  40.216  1.00 50.16           C  
ANISOU  878  CB  PRO A 108     6664   6630   5765   -276    351    660       C  
ATOM    879  CG  PRO A 108      17.298   5.143  39.546  1.00 51.25           C  
ANISOU  879  CG  PRO A 108     6776   6740   5958   -194    313    599       C  
ATOM    880  CD  PRO A 108      18.067   5.818  40.606  1.00 50.57           C  
ANISOU  880  CD  PRO A 108     6728   6639   5846   -100    297    575       C  
ATOM    881  N   ALA A 109      15.710   2.741  43.248  1.00 53.76           N  
ANISOU  881  N   ALA A 109     7208   7172   6045   -323    432    771       N  
ATOM    882  CA  ALA A 109      16.025   1.689  44.201  1.00 65.23           C  
ANISOU  882  CA  ALA A 109     8756   8578   7448   -358    436    819       C  
ATOM    883  C   ALA A 109      16.266   0.348  43.498  1.00 65.27           C  
ANISOU  883  C   ALA A 109     8831   8486   7484   -455    415    851       C  
ATOM    884  O   ALA A 109      16.905  -0.543  44.054  1.00 67.33           O  
ANISOU  884  O   ALA A 109     9195   8665   7722   -466    398    879       O  
ATOM    885  CB  ALA A 109      14.934   1.560  45.231  1.00 69.89           C  
ANISOU  885  CB  ALA A 109     9318   9281   7956   -392    497    871       C  
ATOM    886  N   SER A 110      15.764   0.210  42.279  1.00 58.18           N  
ANISOU  886  N   SER A 110     7882   7591   6632   -520    413    845       N  
ATOM    887  CA  SER A 110      16.072  -0.976  41.498  1.00 57.69           C  
ANISOU  887  CA  SER A 110     7893   7425   6600   -602    386    863       C  
ATOM    888  C   SER A 110      16.739  -0.601  40.164  1.00 54.66           C  
ANISOU  888  C   SER A 110     7492   6980   6296   -567    343    806       C  
ATOM    889  O   SER A 110      16.561   0.511  39.654  1.00 46.84           O  
ANISOU  889  O   SER A 110     6412   6049   5336   -517    343    764       O  
ATOM    890  CB  SER A 110      14.830  -1.844  41.306  1.00 52.71           C  
ANISOU  890  CB  SER A 110     7244   6842   5941   -743    421    921       C  
ATOM    891  OG  SER A 110      13.855  -1.178  40.547  1.00 57.42           O  
ANISOU  891  OG  SER A 110     7719   7542   6557   -772    442    908       O  
ATOM    892  N   PRO A 111      17.515  -1.538  39.605  1.00 47.13           N  
ANISOU  892  N   PRO A 111     6630   5907   5371   -591    306    805       N  
ATOM    893  CA  PRO A 111      18.387  -1.263  38.465  1.00 44.16           C  
ANISOU  893  CA  PRO A 111     6254   5464   5063   -543    264    752       C  
ATOM    894  C   PRO A 111      17.644  -0.656  37.265  1.00 47.22           C  
ANISOU  894  C   PRO A 111     6540   5911   5489   -577    271    727       C  
ATOM    895  O   PRO A 111      16.699  -1.249  36.761  1.00 46.90           O  
ANISOU  895  O   PRO A 111     6483   5897   5441   -681    287    755       O  
ATOM    896  CB  PRO A 111      18.992  -2.650  38.132  1.00 39.92           C  
ANISOU  896  CB  PRO A 111     5837   4800   4529   -587    236    771       C  
ATOM    897  CG  PRO A 111      18.831  -3.461  39.432  1.00 42.08           C  
ANISOU  897  CG  PRO A 111     6191   5060   4737   -618    255    829       C  
ATOM    898  CD  PRO A 111      17.515  -2.966  39.980  1.00 45.24           C  
ANISOU  898  CD  PRO A 111     6501   5592   5097   -670    306    858       C  
ATOM    899  N   THR A 112      18.088   0.517  36.819  1.00 42.05           N  
ANISOU  899  N   THR A 112     5823   5280   4875   -492    255    675       N  
ATOM    900  CA  THR A 112      17.445   1.244  35.727  1.00 37.94           C  
ANISOU  900  CA  THR A 112     5207   4819   4390   -506    259    650       C  
ATOM    901  C   THR A 112      18.292   1.212  34.453  1.00 36.15           C  
ANISOU  901  C   THR A 112     4999   4514   4223   -487    219    610       C  
ATOM    902  O   THR A 112      19.520   1.326  34.524  1.00 40.50           O  
ANISOU  902  O   THR A 112     5598   4996   4797   -413    189    585       O  
ATOM    903  CB  THR A 112      17.290   2.726  36.123  1.00 42.22           C  
ANISOU  903  CB  THR A 112     5667   5446   4931   -418    270    621       C  
ATOM    904  OG1 THR A 112      16.758   2.802  37.440  1.00 45.20           O  
ANISOU  904  OG1 THR A 112     6040   5887   5247   -410    305    651       O  
ATOM    905  CG2 THR A 112      16.389   3.468  35.160  1.00 41.27           C  
ANISOU  905  CG2 THR A 112     5444   5404   4833   -434    281    605       C  
ATOM    906  N   PRO A 113      17.638   1.072  33.289  1.00 37.75           N  
ANISOU  906  N   PRO A 113     5159   4735   4448   -552    219    606       N  
ATOM    907  CA  PRO A 113      18.273   1.105  31.964  1.00 34.64           C  
ANISOU  907  CA  PRO A 113     4772   4283   4105   -538    186    569       C  
ATOM    908  C   PRO A 113      19.080   2.376  31.798  1.00 38.01           C  
ANISOU  908  C   PRO A 113     5156   4718   4569   -432    169    525       C  
ATOM    909  O   PRO A 113      18.632   3.435  32.214  1.00 34.19           O  
ANISOU  909  O   PRO A 113     4602   4312   4077   -392    185    518       O  
ATOM    910  CB  PRO A 113      17.083   1.133  31.010  1.00 34.26           C  
ANISOU  910  CB  PRO A 113     4653   4302   4062   -619    198    575       C  
ATOM    911  CG  PRO A 113      16.027   0.306  31.765  1.00 39.02           C  
ANISOU  911  CG  PRO A 113     5265   4946   4613   -717    228    629       C  
ATOM    912  CD  PRO A 113      16.197   0.775  33.197  1.00 40.54           C  
ANISOU  912  CD  PRO A 113     5458   5173   4773   -651    250    643       C  
ATOM    913  N   VAL A 114      20.244   2.251  31.177  1.00 38.21           N  
ANISOU  913  N   VAL A 114     5224   4665   4630   -389    137    497       N  
ATOM    914  CA  VAL A 114      21.204   3.332  31.067  1.00 36.56           C  
ANISOU  914  CA  VAL A 114     4987   4451   4454   -296    116    460       C  
ATOM    915  C   VAL A 114      21.245   3.763  29.612  1.00 33.45           C  
ANISOU  915  C   VAL A 114     4549   4059   4103   -300    103    432       C  
ATOM    916  O   VAL A 114      21.226   2.924  28.720  1.00 32.52           O  
ANISOU  916  O   VAL A 114     4463   3901   3994   -349     96    433       O  
ATOM    917  CB  VAL A 114      22.615   2.828  31.524  1.00 28.80           C  
ANISOU  917  CB  VAL A 114     4083   3385   3475   -241     89    454       C  
ATOM    918  CG1 VAL A 114      23.671   3.928  31.373  1.00 34.52           C  
ANISOU  918  CG1 VAL A 114     4774   4108   4235   -156     63    418       C  
ATOM    919  CG2 VAL A 114      22.549   2.343  32.963  1.00 21.78           C  
ANISOU  919  CG2 VAL A 114     3244   2492   2538   -239    101    485       C  
ATOM    920  N   LEU A 115      21.261   5.069  29.384  1.00 31.85           N  
ANISOU  920  N   LEU A 115     4278   3903   3922   -250     99    408       N  
ATOM    921  CA  LEU A 115      21.517   5.640  28.068  1.00 30.20           C  
ANISOU  921  CA  LEU A 115     4031   3692   3753   -238     83    381       C  
ATOM    922  C   LEU A 115      22.870   6.304  28.107  1.00 32.23           C  
ANISOU  922  C   LEU A 115     4297   3911   4038   -162     56    356       C  
ATOM    923  O   LEU A 115      23.152   7.055  29.041  1.00 34.24           O  
ANISOU  923  O   LEU A 115     4544   4180   4285   -113     52    351       O  
ATOM    924  CB  LEU A 115      20.487   6.711  27.746  1.00 29.72           C  
ANISOU  924  CB  LEU A 115     3886   3714   3694   -238     96    377       C  
ATOM    925  CG  LEU A 115      19.119   6.142  27.365  1.00 41.88           C  
ANISOU  925  CG  LEU A 115     5393   5307   5211   -320    118    401       C  
ATOM    926  CD1 LEU A 115      18.079   7.212  27.078  1.00 34.43           C  
ANISOU  926  CD1 LEU A 115     4360   4455   4265   -309    131    399       C  
ATOM    927  CD2 LEU A 115      19.332   5.324  26.136  1.00 50.99           C  
ANISOU  927  CD2 LEU A 115     6576   6413   6383   -370    102    395       C  
ATOM    928  N   ILE A 116      23.703   6.034  27.100  1.00 32.58           N  
ANISOU  928  N   ILE A 116     4358   3910   4112   -155     38    340       N  
ATOM    929  CA  ILE A 116      25.004   6.669  27.015  1.00 28.01           C  
ANISOU  929  CA  ILE A 116     3776   3306   3561    -91     13    319       C  
ATOM    930  C   ILE A 116      25.076   7.495  25.745  1.00 29.19           C  
ANISOU  930  C   ILE A 116     3874   3473   3744    -86      5    300       C  
ATOM    931  O   ILE A 116      24.935   6.951  24.654  1.00 27.56           O  
ANISOU  931  O   ILE A 116     3672   3255   3546   -119      8    298       O  
ATOM    932  CB  ILE A 116      26.140   5.639  26.995  1.00 36.02           C  
ANISOU  932  CB  ILE A 116     4854   4255   4577    -71     -2    319       C  
ATOM    933  CG1 ILE A 116      26.087   4.742  28.217  1.00 33.54           C  
ANISOU  933  CG1 ILE A 116     4601   3915   4226    -75      4    342       C  
ATOM    934  CG2 ILE A 116      27.524   6.318  26.929  1.00 27.02           C  
ANISOU  934  CG2 ILE A 116     3697   3104   3464     -7    -28    301       C  
ATOM    935  CD1 ILE A 116      27.254   3.886  28.270  1.00 27.43           C  
ANISOU  935  CD1 ILE A 116     3887   3081   3453    -38    -14    341       C  
ATOM    936  N   TRP A 117      25.289   8.803  25.898  1.00 25.78           N  
ANISOU  936  N   TRP A 117     3401   3068   3328    -47     -6    288       N  
ATOM    937  CA  TRP A 117      25.345   9.734  24.782  1.00 27.83           C  
ANISOU  937  CA  TRP A 117     3614   3345   3616    -41    -14    275       C  
ATOM    938  C   TRP A 117      26.744   9.959  24.253  1.00 31.74           C  
ANISOU  938  C   TRP A 117     4111   3808   4139    -11    -37    263       C  
ATOM    939  O   TRP A 117      27.663  10.292  25.012  1.00 30.22           O  
ANISOU  939  O   TRP A 117     3930   3601   3952     26    -55    259       O  
ATOM    940  CB  TRP A 117      24.799  11.097  25.200  1.00 25.72           C  
ANISOU  940  CB  TRP A 117     3308   3116   3348    -15    -17    269       C  
ATOM    941  CG  TRP A 117      24.890  12.135  24.091  1.00 25.88           C  
ANISOU  941  CG  TRP A 117     3290   3148   3396     -6    -28    259       C  
ATOM    942  CD1 TRP A 117      25.719  13.225  24.054  1.00 31.77           C  
ANISOU  942  CD1 TRP A 117     4028   3879   4163     28    -53    248       C  
ATOM    943  CD2 TRP A 117      24.105  12.196  22.887  1.00 27.82           C  
ANISOU  943  CD2 TRP A 117     3503   3421   3647    -35    -19    262       C  
ATOM    944  NE1 TRP A 117      25.502  13.950  22.912  1.00 29.77           N  
ANISOU  944  NE1 TRP A 117     3744   3640   3929     22    -57    246       N  
ATOM    945  CE2 TRP A 117      24.518  13.341  22.180  1.00 24.04           C  
ANISOU  945  CE2 TRP A 117     3001   2942   3193    -12    -36    254       C  
ATOM    946  CE3 TRP A 117      23.071  11.415  22.360  1.00 29.01           C  
ANISOU  946  CE3 TRP A 117     3642   3599   3781    -83      0    272       C  
ATOM    947  CZ2 TRP A 117      23.950  13.712  20.956  1.00 26.31           C  
ANISOU  947  CZ2 TRP A 117     3255   3254   3487    -28    -34    256       C  
ATOM    948  CZ3 TRP A 117      22.512  11.782  21.131  1.00 27.79           C  
ANISOU  948  CZ3 TRP A 117     3451   3473   3635   -100     -1    271       C  
ATOM    949  CH2 TRP A 117      22.956  12.925  20.446  1.00 26.59           C  
ANISOU  949  CH2 TRP A 117     3278   3320   3506    -69    -17    263       C  
ATOM    950  N   ILE A 118      26.905   9.825  22.944  1.00 29.01           N  
ANISOU  950  N   ILE A 118     3752   3460   3811    -26    -36    258       N  
ATOM    951  CA  ILE A 118      28.163  10.218  22.306  1.00 22.33           C  
ANISOU  951  CA  ILE A 118     2893   2602   2991      2    -53    250       C  
ATOM    952  C   ILE A 118      27.954  11.381  21.354  1.00 25.55           C  
ANISOU  952  C   ILE A 118     3255   3036   3419     -3    -57    246       C  
ATOM    953  O   ILE A 118      27.326  11.223  20.315  1.00 30.91           O  
ANISOU  953  O   ILE A 118     3921   3728   4096    -30    -46    246       O  
ATOM    954  CB  ILE A 118      28.798   9.032  21.567  1.00 22.10           C  
ANISOU  954  CB  ILE A 118     2894   2543   2959      1    -47    247       C  
ATOM    955  CG1 ILE A 118      28.953   7.854  22.552  1.00 21.96           C  
ANISOU  955  CG1 ILE A 118     2935   2492   2919      8    -45    254       C  
ATOM    956  CG2 ILE A 118      30.198   9.393  21.014  1.00 26.20           C  
ANISOU  956  CG2 ILE A 118     3392   3063   3501     36    -61    242       C  
ATOM    957  CD1 ILE A 118      29.255   6.559  21.829  1.00 24.75           C  
ANISOU  957  CD1 ILE A 118     3335   2809   3261      5    -37    250       C  
ATOM    958  N   TYR A 119      28.517  12.547  21.671  1.00 30.75           N  
ANISOU  958  N   TYR A 119     3893   3698   4093     20    -77    243       N  
ATOM    959  CA  TYR A 119      28.260  13.740  20.833  1.00 24.74           C  
ANISOU  959  CA  TYR A 119     3098   2954   3347     16    -84    243       C  
ATOM    960  C   TYR A 119      28.933  13.654  19.457  1.00 25.93           C  
ANISOU  960  C   TYR A 119     3232   3107   3515      6    -83    246       C  
ATOM    961  O   TYR A 119      29.929  12.922  19.273  1.00 25.12           O  
ANISOU  961  O   TYR A 119     3137   2993   3415     15    -82    245       O  
ATOM    962  CB  TYR A 119      28.693  15.022  21.559  1.00 24.53           C  
ANISOU  962  CB  TYR A 119     3068   2920   3331     39   -109    240       C  
ATOM    963  CG  TYR A 119      30.166  15.016  21.960  1.00 21.93           C  
ANISOU  963  CG  TYR A 119     2742   2573   3015     51   -132    239       C  
ATOM    964  CD1 TYR A 119      31.181  15.212  21.002  1.00 23.75           C  
ANISOU  964  CD1 TYR A 119     2949   2808   3267     43   -139    245       C  
ATOM    965  CD2 TYR A 119      30.532  14.832  23.287  1.00 24.08           C  
ANISOU  965  CD2 TYR A 119     3039   2834   3276     71   -145    234       C  
ATOM    966  CE1 TYR A 119      32.525  15.223  21.379  1.00 27.63           C  
ANISOU  966  CE1 TYR A 119     3432   3298   3769     54   -160    247       C  
ATOM    967  CE2 TYR A 119      31.844  14.813  23.673  1.00 27.32           C  
ANISOU  967  CE2 TYR A 119     3447   3237   3696     83   -169    235       C  
ATOM    968  CZ  TYR A 119      32.857  15.011  22.724  1.00 31.68           C  
ANISOU  968  CZ  TYR A 119     3967   3799   4271     74   -177    242       C  
ATOM    969  OH  TYR A 119      34.183  14.949  23.139  1.00 27.65           O  
ANISOU  969  OH  TYR A 119     3444   3294   3767     85   -201    245       O  
ATOM    970  N   GLY A 120      28.364  14.368  18.486  1.00 18.21           N  
ANISOU  970  N   GLY A 120     2230   2148   2542     -7    -81    249       N  
ATOM    971  CA  GLY A 120      28.984  14.563  17.184  1.00 21.00           C  
ANISOU  971  CA  GLY A 120     2564   2508   2907    -16    -81    255       C  
ATOM    972  C   GLY A 120      29.795  15.883  17.163  1.00 24.49           C  
ANISOU  972  C   GLY A 120     2989   2946   3370     -8   -103    263       C  
ATOM    973  O   GLY A 120      30.090  16.461  18.215  1.00 23.15           O  
ANISOU  973  O   GLY A 120     2828   2761   3206      4   -122    260       O  
ATOM    974  N   GLY A 121      30.104  16.355  15.955  1.00 25.58           N  
ANISOU  974  N   GLY A 121     3106   3097   3516    -21   -102    273       N  
ATOM    975  CA  GLY A 121      30.997  17.464  15.679  1.00 22.37           C  
ANISOU  975  CA  GLY A 121     2684   2688   3128    -28   -121    287       C  
ATOM    976  C   GLY A 121      32.178  17.087  14.790  1.00 28.68           C  
ANISOU  976  C   GLY A 121     3458   3506   3931    -35   -112    297       C  
ATOM    977  O   GLY A 121      33.295  17.638  14.942  1.00 28.39           O  
ANISOU  977  O   GLY A 121     3404   3475   3910    -42   -127    309       O  
ATOM    978  N   GLY A 122      31.945  16.170  13.855  1.00 24.71           N  
ANISOU  978  N   GLY A 122     2955   3020   3413    -35    -87    293       N  
ATOM    979  CA  GLY A 122      32.923  15.867  12.812  1.00 24.24           C  
ANISOU  979  CA  GLY A 122     2873   2987   3350    -34    -73    302       C  
ATOM    980  C   GLY A 122      34.212  15.205  13.283  1.00 33.27           C  
ANISOU  980  C   GLY A 122     4004   4141   4497    -11    -71    300       C  
ATOM    981  O   GLY A 122      35.222  15.209  12.561  1.00 32.13           O  
ANISOU  981  O   GLY A 122     3828   4029   4351     -8    -61    312       O  
ATOM    982  N   PHE A 123      34.199  14.657  14.498  1.00 32.04           N  
ANISOU  982  N   PHE A 123     3869   3962   4341      7    -80    287       N  
ATOM    983  CA  PHE A 123      35.413  14.100  15.109  1.00 26.81           C  
ANISOU  983  CA  PHE A 123     3196   3310   3682     36    -84    287       C  
ATOM    984  C   PHE A 123      36.472  15.176  15.333  1.00 28.70           C  
ANISOU  984  C   PHE A 123     3391   3573   3941     20   -108    306       C  
ATOM    985  O   PHE A 123      37.609  14.863  15.679  1.00 30.24           O  
ANISOU  985  O   PHE A 123     3559   3792   4138     41   -114    311       O  
ATOM    986  CB  PHE A 123      36.000  12.973  14.250  1.00 27.25           C  
ANISOU  986  CB  PHE A 123     3250   3386   3718     67    -57    281       C  
ATOM    987  CG  PHE A 123      35.152  11.739  14.209  1.00 25.83           C  
ANISOU  987  CG  PHE A 123     3124   3173   3515     81    -41    261       C  
ATOM    988  CD1 PHE A 123      35.006  10.949  15.357  1.00 27.06           C  
ANISOU  988  CD1 PHE A 123     3319   3297   3666    101    -48    250       C  
ATOM    989  CD2 PHE A 123      34.460  11.390  13.041  1.00 26.13           C  
ANISOU  989  CD2 PHE A 123     3180   3213   3536     68    -21    253       C  
ATOM    990  CE1 PHE A 123      34.215   9.808  15.353  1.00 26.80           C  
ANISOU  990  CE1 PHE A 123     3343   3229   3611    103    -35    235       C  
ATOM    991  CE2 PHE A 123      33.658  10.234  13.002  1.00 24.79           C  
ANISOU  991  CE2 PHE A 123     3065   3010   3343     69    -11    234       C  
ATOM    992  CZ  PHE A 123      33.540   9.436  14.167  1.00 28.93           C  
ANISOU  992  CZ  PHE A 123     3630   3498   3864     84    -18    226       C  
ATOM    993  N   TYR A 124      36.104  16.450  15.146  1.00 23.79           N  
ANISOU  993  N   TYR A 124     2763   2943   3332    -17   -124    318       N  
ATOM    994  CA  TYR A 124      37.021  17.560  15.426  1.00 32.75           C  
ANISOU  994  CA  TYR A 124     3868   4090   4486    -45   -152    337       C  
ATOM    995  C   TYR A 124      36.464  18.547  16.468  1.00 31.51           C  
ANISOU  995  C   TYR A 124     3743   3889   4339    -62   -187    331       C  
ATOM    996  O   TYR A 124      37.102  19.526  16.804  1.00 30.48           O  
ANISOU  996  O   TYR A 124     3603   3756   4222    -92   -217    344       O  
ATOM    997  CB  TYR A 124      37.396  18.310  14.136  1.00 35.67           C  
ANISOU  997  CB  TYR A 124     4205   4488   4859    -79   -144    364       C  
ATOM    998  CG  TYR A 124      36.282  19.176  13.640  1.00 34.98           C  
ANISOU  998  CG  TYR A 124     4148   4370   4772   -102   -147    368       C  
ATOM    999  CD1 TYR A 124      36.069  20.445  14.190  1.00 36.16           C  
ANISOU  999  CD1 TYR A 124     4320   4485   4936   -129   -181    375       C  
ATOM   1000  CD2 TYR A 124      35.423  18.732  12.630  1.00 33.57           C  
ANISOU 1000  CD2 TYR A 124     3981   4198   4578    -92   -119    364       C  
ATOM   1001  CE1 TYR A 124      35.020  21.248  13.747  1.00 32.21           C  
ANISOU 1001  CE1 TYR A 124     3850   3955   4432   -137   -185    379       C  
ATOM   1002  CE2 TYR A 124      34.353  19.540  12.181  1.00 33.60           C  
ANISOU 1002  CE2 TYR A 124     4008   4179   4578   -106   -125    369       C  
ATOM   1003  CZ  TYR A 124      34.187  20.800  12.735  1.00 34.62           C  
ANISOU 1003  CZ  TYR A 124     4157   4275   4722   -125   -157    378       C  
ATOM   1004  OH  TYR A 124      33.153  21.609  12.329  1.00 37.82           O  
ANISOU 1004  OH  TYR A 124     4589   4658   5122   -127   -164    384       O  
ATOM   1005  N   SER A 125      35.278  18.282  16.991  1.00 28.56           N  
ANISOU 1005  N   SER A 125     3411   3486   3956    -43   -181    312       N  
ATOM   1006  CA  SER A 125      34.708  19.169  17.985  1.00 24.20           C  
ANISOU 1006  CA  SER A 125     2892   2897   3406    -46   -209    303       C  
ATOM   1007  C   SER A 125      33.633  18.469  18.774  1.00 27.32           C  
ANISOU 1007  C   SER A 125     3321   3277   3785    -16   -196    282       C  
ATOM   1008  O   SER A 125      33.286  17.304  18.481  1.00 24.71           O  
ANISOU 1008  O   SER A 125     2990   2957   3441     -2   -168    277       O  
ATOM   1009  CB  SER A 125      34.115  20.409  17.324  1.00 27.82           C  
ANISOU 1009  CB  SER A 125     3362   3337   3869    -68   -218    314       C  
ATOM   1010  OG  SER A 125      33.104  20.041  16.396  1.00 29.20           O  
ANISOU 1010  OG  SER A 125     3538   3522   4033    -60   -189    314       O  
ATOM   1011  N   GLY A 126      33.078  19.207  19.738  1.00 31.34           N  
ANISOU 1011  N   GLY A 126     3860   3758   4289     -8   -217    272       N  
ATOM   1012  CA  GLY A 126      31.975  18.711  20.555  1.00 26.35           C  
ANISOU 1012  CA  GLY A 126     3256   3119   3636     18   -204    256       C  
ATOM   1013  C   GLY A 126      32.355  18.545  22.021  1.00 29.56           C  
ANISOU 1013  C   GLY A 126     3686   3513   4033     36   -223    243       C  
ATOM   1014  O   GLY A 126      33.546  18.512  22.423  1.00 26.68           O  
ANISOU 1014  O   GLY A 126     3311   3150   3677     31   -246    246       O  
ATOM   1015  N   ALA A 127      31.335  18.410  22.843  1.00 22.06           N  
ANISOU 1015  N   ALA A 127     2762   2557   3061     58   -214    231       N  
ATOM   1016  CA  ALA A 127      31.527  18.322  24.288  1.00 25.68           C  
ANISOU 1016  CA  ALA A 127     3250   3004   3502     79   -231    219       C  
ATOM   1017  C   ALA A 127      30.259  17.776  24.886  1.00 29.37           C  
ANISOU 1017  C   ALA A 127     3736   3481   3941    100   -203    213       C  
ATOM   1018  O   ALA A 127      29.173  18.053  24.370  1.00 23.01           O  
ANISOU 1018  O   ALA A 127     2924   2689   3131    101   -183    214       O  
ATOM   1019  CB  ALA A 127      31.801  19.690  24.871  1.00 24.52           C  
ANISOU 1019  CB  ALA A 127     3128   2832   3357     81   -270    209       C  
ATOM   1020  N   ALA A 128      30.389  17.029  25.980  1.00 29.41           N  
ANISOU 1020  N   ALA A 128     3763   3486   3925    115   -201    209       N  
ATOM   1021  CA  ALA A 128      29.218  16.465  26.608  1.00 30.96           C  
ANISOU 1021  CA  ALA A 128     3975   3697   4090    128   -172    209       C  
ATOM   1022  C   ALA A 128      28.525  17.491  27.500  1.00 31.86           C  
ANISOU 1022  C   ALA A 128     4112   3812   4182    157   -181    194       C  
ATOM   1023  O   ALA A 128      27.481  17.223  28.064  1.00 31.70           O  
ANISOU 1023  O   ALA A 128     4098   3815   4131    171   -155    195       O  
ATOM   1024  CB  ALA A 128      29.572  15.226  27.384  1.00 26.55           C  
ANISOU 1024  CB  ALA A 128     3437   3137   3514    132   -165    215       C  
ATOM   1025  N   SER A 129      29.121  18.664  27.659  1.00 31.37           N  
ANISOU 1025  N   SER A 129     4064   3725   4130    165   -218    182       N  
ATOM   1026  CA  SER A 129      28.548  19.641  28.588  1.00 30.99           C  
ANISOU 1026  CA  SER A 129     4051   3669   4054    201   -230    164       C  
ATOM   1027  C   SER A 129      27.599  20.645  27.914  1.00 28.65           C  
ANISOU 1027  C   SER A 129     3751   3376   3759    217   -223    160       C  
ATOM   1028  O   SER A 129      27.111  21.563  28.571  1.00 33.17           O  
ANISOU 1028  O   SER A 129     4358   3938   4308    257   -234    142       O  
ATOM   1029  CB  SER A 129      29.661  20.404  29.313  1.00 33.01           C  
ANISOU 1029  CB  SER A 129     4341   3889   4312    202   -281    148       C  
ATOM   1030  OG  SER A 129      30.581  20.981  28.377  1.00 34.05           O  
ANISOU 1030  OG  SER A 129     4456   4000   4482    167   -309    156       O  
ATOM   1031  N   LEU A 130      27.374  20.525  26.605  1.00 23.73           N  
ANISOU 1031  N   LEU A 130     3091   2763   3161    193   -208    175       N  
ATOM   1032  CA  LEU A 130      26.535  21.530  25.940  1.00 27.34           C  
ANISOU 1032  CA  LEU A 130     3547   3223   3619    214   -206    174       C  
ATOM   1033  C   LEU A 130      25.113  21.437  26.473  1.00 27.62           C  
ANISOU 1033  C   LEU A 130     3577   3302   3617    256   -174    170       C  
ATOM   1034  O   LEU A 130      24.639  20.351  26.848  1.00 27.81           O  
ANISOU 1034  O   LEU A 130     3580   3364   3623    247   -142    178       O  
ATOM   1035  CB  LEU A 130      26.534  21.343  24.424  1.00 28.58           C  
ANISOU 1035  CB  LEU A 130     3664   3390   3804    180   -195    193       C  
ATOM   1036  CG  LEU A 130      27.871  21.238  23.698  1.00 34.46           C  
ANISOU 1036  CG  LEU A 130     4398   4112   4583    136   -215    204       C  
ATOM   1037  CD1 LEU A 130      27.613  21.215  22.220  1.00 26.25           C  
ANISOU 1037  CD1 LEU A 130     3326   3088   3560    114   -201    221       C  
ATOM   1038  CD2 LEU A 130      28.802  22.421  24.087  1.00 36.15           C  
ANISOU 1038  CD2 LEU A 130     4649   4278   4807    133   -262    196       C  
ATOM   1039  N   ASP A 131      24.421  22.561  26.473  1.00 35.23           N  
ANISOU 1039  N   ASP A 131     4558   4261   4566    301   -181    159       N  
ATOM   1040  CA  ASP A 131      23.038  22.589  26.915  1.00 32.66           C  
ANISOU 1040  CA  ASP A 131     4218   3989   4201    350   -149    157       C  
ATOM   1041  C   ASP A 131      22.164  21.585  26.194  1.00 32.38           C  
ANISOU 1041  C   ASP A 131     4118   4018   4166    322   -109    179       C  
ATOM   1042  O   ASP A 131      21.330  20.975  26.840  1.00 40.34           O  
ANISOU 1042  O   ASP A 131     5105   5079   5142    333    -77    183       O  
ATOM   1043  CB  ASP A 131      22.459  23.996  26.807  1.00 37.33           C  
ANISOU 1043  CB  ASP A 131     4839   4566   4780    412   -165    143       C  
ATOM   1044  CG  ASP A 131      23.065  24.938  27.829  1.00 42.31           C  
ANISOU 1044  CG  ASP A 131     5545   5137   5395    447   -201    116       C  
ATOM   1045  OD1 ASP A 131      23.799  24.474  28.726  1.00 42.88           O  
ANISOU 1045  OD1 ASP A 131     5638   5193   5461    428   -211    107       O  
ATOM   1046  OD2 ASP A 131      22.814  26.146  27.737  1.00 52.78           O  
ANISOU 1046  OD2 ASP A 131     6913   6429   6711    495   -224    102       O  
ATOM   1047  N   VAL A 132      22.349  21.383  24.886  1.00 28.91           N  
ANISOU 1047  N   VAL A 132     3650   3576   3758    281   -112    194       N  
ATOM   1048  CA  VAL A 132      21.470  20.465  24.164  1.00 33.89           C  
ANISOU 1048  CA  VAL A 132     4225   4266   4385    251    -80    213       C  
ATOM   1049  C   VAL A 132      21.622  19.001  24.561  1.00 35.09           C  
ANISOU 1049  C   VAL A 132     4368   4433   4531    203    -58    222       C  
ATOM   1050  O   VAL A 132      20.814  18.167  24.133  1.00 36.05           O  
ANISOU 1050  O   VAL A 132     4451   4604   4644    171    -32    237       O  
ATOM   1051  CB  VAL A 132      21.629  20.507  22.633  1.00 37.40           C  
ANISOU 1051  CB  VAL A 132     4646   4706   4859    217    -88    226       C  
ATOM   1052  CG1 VAL A 132      20.693  21.492  22.049  1.00 45.55           C  
ANISOU 1052  CG1 VAL A 132     5661   5765   5881    260    -91    229       C  
ATOM   1053  CG2 VAL A 132      23.058  20.759  22.247  1.00 34.13           C  
ANISOU 1053  CG2 VAL A 132     4261   4228   4478    192   -117    223       C  
ATOM   1054  N   TYR A 133      22.649  18.684  25.338  1.00 29.91           N  
ANISOU 1054  N   TYR A 133     3750   3735   3881    196    -71    214       N  
ATOM   1055  CA  TYR A 133      22.871  17.288  25.762  1.00 32.92           C  
ANISOU 1055  CA  TYR A 133     4133   4120   4254    157    -53    224       C  
ATOM   1056  C   TYR A 133      22.578  17.128  27.243  1.00 32.79           C  
ANISOU 1056  C   TYR A 133     4141   4119   4200    184    -41    220       C  
ATOM   1057  O   TYR A 133      23.008  16.167  27.853  1.00 26.86           O  
ANISOU 1057  O   TYR A 133     3410   3355   3440    162    -36    227       O  
ATOM   1058  CB  TYR A 133      24.319  16.815  25.485  1.00 20.65           C  
ANISOU 1058  CB  TYR A 133     2602   2514   2730    131    -75    223       C  
ATOM   1059  CG  TYR A 133      24.832  17.066  24.071  1.00 24.43           C  
ANISOU 1059  CG  TYR A 133     3062   2977   3244    109    -88    226       C  
ATOM   1060  CD1 TYR A 133      23.989  16.930  22.978  1.00 27.04           C  
ANISOU 1060  CD1 TYR A 133     3358   3339   3576     89    -72    236       C  
ATOM   1061  CD2 TYR A 133      26.189  17.390  23.822  1.00 23.21           C  
ANISOU 1061  CD2 TYR A 133     2920   2781   3116    104   -116    222       C  
ATOM   1062  CE1 TYR A 133      24.433  17.154  21.687  1.00 27.80           C  
ANISOU 1062  CE1 TYR A 133     3440   3424   3697     71    -82    240       C  
ATOM   1063  CE2 TYR A 133      26.647  17.590  22.522  1.00 21.23           C  
ANISOU 1063  CE2 TYR A 133     2650   2524   2892     83   -123    229       C  
ATOM   1064  CZ  TYR A 133      25.770  17.472  21.456  1.00 25.73           C  
ANISOU 1064  CZ  TYR A 133     3193   3123   3461     68   -105    238       C  
ATOM   1065  OH  TYR A 133      26.152  17.672  20.142  1.00 25.04           O  
ANISOU 1065  OH  TYR A 133     3088   3033   3393     49   -109    245       O  
ATOM   1066  N   ASP A 134      21.872  18.099  27.815  1.00 29.96           N  
ANISOU 1066  N   ASP A 134     3783   3784   3815    236    -39    209       N  
ATOM   1067  CA  ASP A 134      21.468  18.073  29.212  1.00 31.16           C  
ANISOU 1067  CA  ASP A 134     3956   3961   3923    271    -23    204       C  
ATOM   1068  C   ASP A 134      20.524  16.872  29.540  1.00 33.40           C  
ANISOU 1068  C   ASP A 134     4208   4305   4176    237     20    229       C  
ATOM   1069  O   ASP A 134      19.384  16.808  29.075  1.00 33.20           O  
ANISOU 1069  O   ASP A 134     4133   4344   4139    230     46    242       O  
ATOM   1070  CB  ASP A 134      20.800  19.423  29.536  1.00 30.48           C  
ANISOU 1070  CB  ASP A 134     3875   3892   3813    343    -27    185       C  
ATOM   1071  CG  ASP A 134      20.514  19.613  31.028  1.00 39.88           C  
ANISOU 1071  CG  ASP A 134     5098   5103   4953    393    -16    173       C  
ATOM   1072  OD1 ASP A 134      20.626  18.652  31.813  1.00 42.52           O  
ANISOU 1072  OD1 ASP A 134     5441   5450   5266    369      1    185       O  
ATOM   1073  OD2 ASP A 134      20.160  20.737  31.420  1.00 45.41           O  
ANISOU 1073  OD2 ASP A 134     5821   5804   5630    461    -24    152       O  
ATOM   1074  N   GLY A 135      21.004  15.952  30.376  1.00 31.90           N  
ANISOU 1074  N   GLY A 135     4050   4099   3971    214     25    237       N  
ATOM   1075  CA  GLY A 135      20.265  14.752  30.744  1.00 29.30           C  
ANISOU 1075  CA  GLY A 135     3706   3815   3613    171     62    265       C  
ATOM   1076  C   GLY A 135      19.194  14.897  31.818  1.00 31.75           C  
ANISOU 1076  C   GLY A 135     4001   4195   3867    201     97    273       C  
ATOM   1077  O   GLY A 135      18.497  13.928  32.125  1.00 30.30           O  
ANISOU 1077  O   GLY A 135     3800   4057   3656    157    130    301       O  
ATOM   1078  N   ARG A 136      19.027  16.094  32.382  1.00 32.13           N  
ANISOU 1078  N   ARG A 136     4057   4255   3894    276     90    249       N  
ATOM   1079  CA  ARG A 136      18.064  16.240  33.486  1.00 39.67           C  
ANISOU 1079  CA  ARG A 136     5002   5283   4788    316    126    255       C  
ATOM   1080  C   ARG A 136      16.606  15.829  33.140  1.00 42.41           C  
ANISOU 1080  C   ARG A 136     5272   5732   5111    290    172    284       C  
ATOM   1081  O   ARG A 136      15.881  15.310  33.992  1.00 38.91           O  
ANISOU 1081  O   ARG A 136     4811   5354   4617    282    211    306       O  
ATOM   1082  CB  ARG A 136      18.127  17.646  34.133  1.00 32.80           C  
ANISOU 1082  CB  ARG A 136     4164   4405   3895    411    110    219       C  
ATOM   1083  CG  ARG A 136      17.407  18.736  33.377  1.00 30.52           C  
ANISOU 1083  CG  ARG A 136     3839   4145   3612    461    109    206       C  
ATOM   1084  CD  ARG A 136      17.542  20.117  34.090  1.00 34.52           C  
ANISOU 1084  CD  ARG A 136     4399   4626   4091    559     88    167       C  
ATOM   1085  NE  ARG A 136      18.933  20.578  34.038  1.00 43.04           N  
ANISOU 1085  NE  ARG A 136     5545   5600   5206    552     33    143       N  
ATOM   1086  CZ  ARG A 136      19.472  21.517  34.821  1.00 42.76           C  
ANISOU 1086  CZ  ARG A 136     5580   5516   5152    610      1    108       C  
ATOM   1087  NH1 ARG A 136      20.741  21.847  34.648  1.00 40.59           N  
ANISOU 1087  NH1 ARG A 136     5353   5154   4914    586    -51     92       N  
ATOM   1088  NH2 ARG A 136      18.753  22.142  35.761  1.00 36.10           N  
ANISOU 1088  NH2 ARG A 136     4757   4712   4247    690     20     90       N  
ATOM   1089  N   PHE A 137      16.189  16.039  31.891  1.00 35.61           N  
ANISOU 1089  N   PHE A 137     4361   4887   4281    271    167    287       N  
ATOM   1090  CA  PHE A 137      14.800  15.816  31.512  1.00 34.52           C  
ANISOU 1090  CA  PHE A 137     4142   4854   4121    252    204    313       C  
ATOM   1091  C   PHE A 137      14.486  14.323  31.361  1.00 35.81           C  
ANISOU 1091  C   PHE A 137     4285   5041   4281    146    226    350       C  
ATOM   1092  O   PHE A 137      13.454  13.840  31.837  1.00 40.21           O  
ANISOU 1092  O   PHE A 137     4794   5688   4794    120    265    379       O  
ATOM   1093  CB  PHE A 137      14.482  16.597  30.228  1.00 32.54           C  
ANISOU 1093  CB  PHE A 137     3849   4613   3901    272    186    303       C  
ATOM   1094  CG  PHE A 137      14.859  18.054  30.318  1.00 34.76           C  
ANISOU 1094  CG  PHE A 137     4165   4854   4187    370    159    267       C  
ATOM   1095  CD1 PHE A 137      14.107  18.930  31.085  1.00 40.35           C  
ANISOU 1095  CD1 PHE A 137     4863   5621   4848    460    179    256       C  
ATOM   1096  CD2 PHE A 137      15.970  18.543  29.666  1.00 33.58           C  
ANISOU 1096  CD2 PHE A 137     4064   4608   4086    371    115    247       C  
ATOM   1097  CE1 PHE A 137      14.452  20.287  31.186  1.00 41.61           C  
ANISOU 1097  CE1 PHE A 137     5070   5731   5008    551    150    221       C  
ATOM   1098  CE2 PHE A 137      16.331  19.890  29.777  1.00 34.30           C  
ANISOU 1098  CE2 PHE A 137     4198   4654   4180    450     87    216       C  
ATOM   1099  CZ  PHE A 137      15.575  20.758  30.529  1.00 35.17           C  
ANISOU 1099  CZ  PHE A 137     4309   4812   4244    540    102    203       C  
ATOM   1100  N   LEU A 138      15.359  13.616  30.659  1.00 28.71           N  
ANISOU 1100  N   LEU A 138     3422   4062   3425     86    199    350       N  
ATOM   1101  CA  LEU A 138      15.237  12.183  30.486  1.00 35.39           C  
ANISOU 1101  CA  LEU A 138     4273   4904   4269    -12    211    381       C  
ATOM   1102  C   LEU A 138      15.283  11.481  31.850  1.00 38.33           C  
ANISOU 1102  C   LEU A 138     4685   5280   4598    -25    235    401       C  
ATOM   1103  O   LEU A 138      14.478  10.564  32.117  1.00 35.79           O  
ANISOU 1103  O   LEU A 138     4341   5012   4245    -94    265    437       O  
ATOM   1104  CB  LEU A 138      16.359  11.676  29.559  1.00 32.68           C  
ANISOU 1104  CB  LEU A 138     3978   4462   3978    -50    175    369       C  
ATOM   1105  CG  LEU A 138      16.124  11.975  28.068  1.00 32.71           C  
ANISOU 1105  CG  LEU A 138     3939   4473   4017    -68    159    362       C  
ATOM   1106  CD1 LEU A 138      17.377  11.872  27.222  1.00 29.01           C  
ANISOU 1106  CD1 LEU A 138     3516   3911   3595    -74    124    342       C  
ATOM   1107  CD2 LEU A 138      15.055  11.019  27.538  1.00 32.07           C  
ANISOU 1107  CD2 LEU A 138     3812   4453   3919   -156    179    392       C  
ATOM   1108  N   ALA A 139      16.238  11.883  32.691  1.00 32.50           N  
ANISOU 1108  N   ALA A 139     4008   4484   3857     33    218    380       N  
ATOM   1109  CA  ALA A 139      16.330  11.375  34.065  1.00 36.46           C  
ANISOU 1109  CA  ALA A 139     4553   4990   4312     36    237    396       C  
ATOM   1110  C   ALA A 139      15.049  11.678  34.877  1.00 38.81           C  
ANISOU 1110  C   ALA A 139     4797   5402   4548     60    284    414       C  
ATOM   1111  O   ALA A 139      14.460  10.780  35.480  1.00 37.58           O  
ANISOU 1111  O   ALA A 139     4635   5292   4352      5    318    453       O  
ATOM   1112  CB  ALA A 139      17.533  11.955  34.781  1.00 32.67           C  
ANISOU 1112  CB  ALA A 139     4139   4438   3837    104    205    365       C  
ATOM   1113  N   GLN A 140      14.617  12.938  34.884  1.00 36.88           N  
ANISOU 1113  N   GLN A 140     4515   5204   4294    143    287    389       N  
ATOM   1114  CA  GLN A 140      13.445  13.320  35.691  1.00 37.91           C  
ANISOU 1114  CA  GLN A 140     4593   5450   4360    185    334    402       C  
ATOM   1115  C   GLN A 140      12.153  12.707  35.153  1.00 40.67           C  
ANISOU 1115  C   GLN A 140     4852   5905   4695    114    371    443       C  
ATOM   1116  O   GLN A 140      11.408  12.120  35.911  1.00 42.09           O  
ANISOU 1116  O   GLN A 140     5005   6164   4823     81    413    479       O  
ATOM   1117  CB  GLN A 140      13.306  14.841  35.834  1.00 28.85           C  
ANISOU 1117  CB  GLN A 140     3439   4322   3202    304    326    362       C  
ATOM   1118  CG  GLN A 140      12.589  15.253  37.104  1.00 31.71           C  
ANISOU 1118  CG  GLN A 140     3790   4771   3489    374    367    364       C  
ATOM   1119  CD  GLN A 140      11.068  15.021  37.000  1.00 41.48           C  
ANISOU 1119  CD  GLN A 140     4922   6154   4685    356    422    401       C  
ATOM   1120  OE1 GLN A 140      10.501  15.124  35.908  1.00 43.26           O  
ANISOU 1120  OE1 GLN A 140     5080   6417   4940    333    418    408       O  
ATOM   1121  NE2 GLN A 140      10.421  14.674  38.127  1.00 40.02           N  
ANISOU 1121  NE2 GLN A 140     4720   6057   4430    362    471    428       N  
ATOM   1122  N   VAL A 141      11.892  12.829  33.855  1.00 41.38           N  
ANISOU 1122  N   VAL A 141     4895   6000   4828     86    353    440       N  
ATOM   1123  CA  VAL A 141      10.584  12.425  33.321  1.00 38.90           C  
ANISOU 1123  CA  VAL A 141     4483   5800   4496     26    384    475       C  
ATOM   1124  C   VAL A 141      10.516  10.925  33.033  1.00 40.59           C  
ANISOU 1124  C   VAL A 141     4707   5997   4718   -110    387    514       C  
ATOM   1125  O   VAL A 141       9.519  10.294  33.330  1.00 41.30           O  
ANISOU 1125  O   VAL A 141     4741   6183   4767   -174    424    556       O  
ATOM   1126  CB  VAL A 141      10.242  13.213  32.052  1.00 38.94           C  
ANISOU 1126  CB  VAL A 141     4432   5826   4537     56    361    456       C  
ATOM   1127  CG1 VAL A 141       8.922  12.743  31.446  1.00 37.61           C  
ANISOU 1127  CG1 VAL A 141     4158   5780   4351    -13    386    494       C  
ATOM   1128  CG2 VAL A 141      10.209  14.714  32.357  1.00 35.52           C  
ANISOU 1128  CG2 VAL A 141     3996   5408   4090    193    358    420       C  
ATOM   1129  N   GLU A 142      11.583  10.348  32.474  1.00 37.91           N  
ANISOU 1129  N   GLU A 142     4441   5536   4426   -154    349    502       N  
ATOM   1130  CA  GLU A 142      11.574   8.918  32.114  1.00 32.69           C  
ANISOU 1130  CA  GLU A 142     3807   4843   3773   -278    347    534       C  
ATOM   1131  C   GLU A 142      12.246   8.015  33.131  1.00 34.37           C  
ANISOU 1131  C   GLU A 142     4108   4988   3965   -308    352    552       C  
ATOM   1132  O   GLU A 142      12.249   6.780  32.987  1.00 40.77           O  
ANISOU 1132  O   GLU A 142     4956   5761   4773   -408    351    582       O  
ATOM   1133  CB  GLU A 142      12.188   8.685  30.737  1.00 28.15           C  
ANISOU 1133  CB  GLU A 142     3255   4185   3256   -314    305    514       C  
ATOM   1134  CG  GLU A 142      11.375   9.264  29.604  1.00 35.85           C  
ANISOU 1134  CG  GLU A 142     4142   5231   4246   -315    299    508       C  
ATOM   1135  CD  GLU A 142       9.966   8.681  29.587  1.00 47.48           C  
ANISOU 1135  CD  GLU A 142     5533   6826   5681   -399    330    551       C  
ATOM   1136  OE1 GLU A 142       9.793   7.511  29.984  1.00 50.60           O  
ANISOU 1136  OE1 GLU A 142     5958   7213   6054   -496    343    586       O  
ATOM   1137  OE2 GLU A 142       9.031   9.400  29.207  1.00 51.92           O  
ANISOU 1137  OE2 GLU A 142     6001   7494   6231   -369    341    553       O  
ATOM   1138  N   GLY A 143      12.798   8.612  34.177  1.00 36.90           N  
ANISOU 1138  N   GLY A 143     4466   5289   4264   -221    356    535       N  
ATOM   1139  CA  GLY A 143      13.514   7.834  35.181  1.00 37.20           C  
ANISOU 1139  CA  GLY A 143     4592   5263   4281   -237    356    550       C  
ATOM   1140  C   GLY A 143      14.812   7.215  34.683  1.00 41.45           C  
ANISOU 1140  C   GLY A 143     5216   5666   4865   -256    312    534       C  
ATOM   1141  O   GLY A 143      15.328   6.291  35.309  1.00 46.27           O  
ANISOU 1141  O   GLY A 143     5901   6220   5460   -288    310    555       O  
ATOM   1142  N   ALA A 144      15.351   7.705  33.567  1.00 40.95           N  
ANISOU 1142  N   ALA A 144     5144   5556   4857   -233    278    500       N  
ATOM   1143  CA  ALA A 144      16.588   7.125  32.981  1.00 40.34           C  
ANISOU 1143  CA  ALA A 144     5139   5362   4824   -246    239    484       C  
ATOM   1144  C   ALA A 144      17.863   7.404  33.785  1.00 39.59           C  
ANISOU 1144  C   ALA A 144     5112   5197   4732   -173    214    463       C  
ATOM   1145  O   ALA A 144      17.983   8.430  34.442  1.00 36.77           O  
ANISOU 1145  O   ALA A 144     4742   4865   4362    -98    214    442       O  
ATOM   1146  CB  ALA A 144      16.798   7.656  31.579  1.00 37.77           C  
ANISOU 1146  CB  ALA A 144     4781   5019   4551   -237    212    455       C  
ATOM   1147  N   VAL A 145      18.836   6.506  33.725  1.00 37.85           N  
ANISOU 1147  N   VAL A 145     4965   4888   4528   -193    191    466       N  
ATOM   1148  CA  VAL A 145      20.174   6.917  34.126  1.00 34.10           C  
ANISOU 1148  CA  VAL A 145     4537   4349   4070   -121    157    439       C  
ATOM   1149  C   VAL A 145      20.874   7.359  32.844  1.00 36.85           C  
ANISOU 1149  C   VAL A 145     4867   4656   4476   -105    126    407       C  
ATOM   1150  O   VAL A 145      20.944   6.599  31.881  1.00 38.27           O  
ANISOU 1150  O   VAL A 145     5058   4802   4679   -154    120    413       O  
ATOM   1151  CB  VAL A 145      20.949   5.773  34.824  1.00 33.25           C  
ANISOU 1151  CB  VAL A 145     4516   4173   3944   -133    147    460       C  
ATOM   1152  CG1 VAL A 145      22.465   6.180  35.051  1.00 25.01           C  
ANISOU 1152  CG1 VAL A 145     3510   3067   2924    -59    104    431       C  
ATOM   1153  CG2 VAL A 145      20.269   5.449  36.160  1.00 27.16           C  
ANISOU 1153  CG2 VAL A 145     3762   3447   3109   -145    179    494       C  
ATOM   1154  N   LEU A 146      21.371   8.590  32.801  1.00 36.34           N  
ANISOU 1154  N   LEU A 146     4780   4595   4434    -39    105    375       N  
ATOM   1155  CA  LEU A 146      21.991   9.042  31.571  1.00 30.16           C  
ANISOU 1155  CA  LEU A 146     3977   3780   3702    -29     79    351       C  
ATOM   1156  C   LEU A 146      23.494   9.310  31.738  1.00 34.33           C  
ANISOU 1156  C   LEU A 146     4542   4248   4255     19     40    330       C  
ATOM   1157  O   LEU A 146      23.933   9.993  32.675  1.00 30.15           O  
ANISOU 1157  O   LEU A 146     4027   3719   3711     68     25    317       O  
ATOM   1158  CB  LEU A 146      21.234  10.251  30.990  1.00 27.97           C  
ANISOU 1158  CB  LEU A 146     3633   3557   3435     -9     84    335       C  
ATOM   1159  CG  LEU A 146      21.421  10.430  29.482  1.00 39.43           C  
ANISOU 1159  CG  LEU A 146     5057   4993   4933    -28     69    323       C  
ATOM   1160  CD1 LEU A 146      20.129  10.708  28.811  1.00 45.81           C  
ANISOU 1160  CD1 LEU A 146     5804   5868   5735    -54     91    331       C  
ATOM   1161  CD2 LEU A 146      22.428  11.542  29.177  1.00 43.69           C  
ANISOU 1161  CD2 LEU A 146     5596   5499   5506     26     36    294       C  
ATOM   1162  N   VAL A 147      24.282   8.786  30.810  1.00 32.61           N  
ANISOU 1162  N   VAL A 147     4337   3982   4071      5     22    325       N  
ATOM   1163  CA  VAL A 147      25.710   9.032  30.875  1.00 34.03           C  
ANISOU 1163  CA  VAL A 147     4538   4118   4275     48    -13    308       C  
ATOM   1164  C   VAL A 147      26.226   9.697  29.596  1.00 31.74           C  
ANISOU 1164  C   VAL A 147     4209   3820   4030     53    -31    289       C  
ATOM   1165  O   VAL A 147      25.817   9.322  28.507  1.00 28.28           O  
ANISOU 1165  O   VAL A 147     3755   3384   3607     18    -18    292       O  
ATOM   1166  CB  VAL A 147      26.469   7.709  31.107  1.00 39.12           C  
ANISOU 1166  CB  VAL A 147     5241   4712   4910     43    -20    323       C  
ATOM   1167  CG1 VAL A 147      28.012   7.981  31.217  1.00 25.35           C  
ANISOU 1167  CG1 VAL A 147     3507   2937   3189     95    -59    308       C  
ATOM   1168  CG2 VAL A 147      25.898   6.972  32.362  1.00 23.22           C  
ANISOU 1168  CG2 VAL A 147     3273   2704   2847     30     -1    350       C  
ATOM   1169  N   SER A 148      27.122  10.672  29.721  1.00 22.17           N  
ANISOU 1169  N   SER A 148     2986   2600   2837     92    -61    270       N  
ATOM   1170  CA  SER A 148      27.801  11.187  28.533  1.00 26.60           C  
ANISOU 1170  CA  SER A 148     3516   3151   3440     93    -78    258       C  
ATOM   1171  C   SER A 148      29.306  11.382  28.835  1.00 28.39           C  
ANISOU 1171  C   SER A 148     3752   3353   3683    125   -114    250       C  
ATOM   1172  O   SER A 148      29.675  11.734  29.968  1.00 30.12           O  
ANISOU 1172  O   SER A 148     3990   3570   3883    151   -134    245       O  
ATOM   1173  CB  SER A 148      27.154  12.512  28.124  1.00 28.85           C  
ANISOU 1173  CB  SER A 148     3763   3464   3736     97    -79    246       C  
ATOM   1174  OG  SER A 148      27.334  13.443  29.170  1.00 29.74           O  
ANISOU 1174  OG  SER A 148     3887   3578   3834    132    -98    234       O  
ATOM   1175  N   MET A 149      30.190  11.104  27.873  1.00 26.01           N  
ANISOU 1175  N   MET A 149     3436   3038   3408    124   -123    249       N  
ATOM   1176  CA  MET A 149      31.643  11.265  28.150  1.00 22.85           C  
ANISOU 1176  CA  MET A 149     3032   2629   3021    153   -157    245       C  
ATOM   1177  C   MET A 149      32.281  12.197  27.159  1.00 24.33           C  
ANISOU 1177  C   MET A 149     3173   2827   3244    146   -174    238       C  
ATOM   1178  O   MET A 149      31.834  12.250  25.999  1.00 28.11           O  
ANISOU 1178  O   MET A 149     3630   3312   3738    124   -154    239       O  
ATOM   1179  CB  MET A 149      32.383   9.926  28.032  1.00 23.00           C  
ANISOU 1179  CB  MET A 149     3077   2628   3035    170   -155    255       C  
ATOM   1180  CG  MET A 149      32.723   9.629  26.527  1.00 23.19           C  
ANISOU 1180  CG  MET A 149     3074   2652   3084    160   -143    254       C  
ATOM   1181  SD  MET A 149      31.302   9.127  25.479  1.00 30.86           S  
ANISOU 1181  SD  MET A 149     4055   3619   4051    114   -104    255       S  
ATOM   1182  CE  MET A 149      30.990   7.472  26.034  1.00 26.05           C  
ANISOU 1182  CE  MET A 149     3517   2971   3408    112    -89    268       C  
ATOM   1183  N   ASN A 150      33.320  12.934  27.589  1.00 25.57           N  
ANISOU 1183  N   ASN A 150     3315   2988   3411    160   -210    233       N  
ATOM   1184  CA  ASN A 150      34.166  13.640  26.622  1.00 26.54           C  
ANISOU 1184  CA  ASN A 150     3393   3125   3567    147   -226    233       C  
ATOM   1185  C   ASN A 150      35.083  12.585  26.008  1.00 29.71           C  
ANISOU 1185  C   ASN A 150     3781   3534   3975    164   -219    242       C  
ATOM   1186  O   ASN A 150      35.369  11.593  26.665  1.00 26.08           O  
ANISOU 1186  O   ASN A 150     3349   3065   3495    192   -218    246       O  
ATOM   1187  CB  ASN A 150      35.027  14.744  27.260  1.00 26.03           C  
ANISOU 1187  CB  ASN A 150     3316   3065   3510    146   -271    227       C  
ATOM   1188  CG  ASN A 150      34.231  15.977  27.653  1.00 37.59           C  
ANISOU 1188  CG  ASN A 150     4798   4515   4969    134   -283    214       C  
ATOM   1189  OD1 ASN A 150      33.036  16.140  27.306  1.00 25.54           O  
ANISOU 1189  OD1 ASN A 150     3281   2985   3438    129   -255    212       O  
ATOM   1190  ND2 ASN A 150      34.903  16.877  28.373  1.00 38.42           N  
ANISOU 1190  ND2 ASN A 150     4910   4615   5075    131   -326    206       N  
ATOM   1191  N   TYR A 151      35.509  12.794  24.762  1.00 29.07           N  
ANISOU 1191  N   TYR A 151     3660   3470   3916    151   -211    246       N  
ATOM   1192  CA  TYR A 151      36.544  11.972  24.124  1.00 25.72           C  
ANISOU 1192  CA  TYR A 151     3214   3063   3496    176   -205    254       C  
ATOM   1193  C   TYR A 151      37.402  12.881  23.277  1.00 28.75           C  
ANISOU 1193  C   TYR A 151     3538   3481   3905    157   -218    261       C  
ATOM   1194  O   TYR A 151      36.913  13.923  22.767  1.00 22.80           O  
ANISOU 1194  O   TYR A 151     2770   2726   3166    120   -219    261       O  
ATOM   1195  CB  TYR A 151      35.961  10.842  23.239  1.00 29.11           C  
ANISOU 1195  CB  TYR A 151     3670   3476   3915    181   -167    252       C  
ATOM   1196  CG  TYR A 151      35.013  11.304  22.111  1.00 28.91           C  
ANISOU 1196  CG  TYR A 151     3633   3451   3899    143   -145    250       C  
ATOM   1197  CD1 TYR A 151      33.647  11.511  22.349  1.00 28.43           C  
ANISOU 1197  CD1 TYR A 151     3596   3375   3829    116   -134    246       C  
ATOM   1198  CD2 TYR A 151      35.487  11.518  20.822  1.00 23.47           C  
ANISOU 1198  CD2 TYR A 151     2906   2786   3223    137   -135    253       C  
ATOM   1199  CE1 TYR A 151      32.777  11.946  21.315  1.00 24.64           C  
ANISOU 1199  CE1 TYR A 151     3102   2903   3356     85   -117    245       C  
ATOM   1200  CE2 TYR A 151      34.637  11.925  19.780  1.00 20.81           C  
ANISOU 1200  CE2 TYR A 151     2563   2453   2892    104   -117    252       C  
ATOM   1201  CZ  TYR A 151      33.299  12.148  20.031  1.00 25.56           C  
ANISOU 1201  CZ  TYR A 151     3187   3039   3487     79   -111    248       C  
ATOM   1202  OH  TYR A 151      32.512  12.560  18.982  1.00 23.97           O  
ANISOU 1202  OH  TYR A 151     2972   2846   3288     52    -97    248       O  
ATOM   1203  N   ARG A 152      38.683  12.516  23.116  1.00 27.42           N  
ANISOU 1203  N   ARG A 152     3333   3346   3740    183   -227    269       N  
ATOM   1204  CA  ARG A 152      39.593  13.375  22.328  1.00 27.20           C  
ANISOU 1204  CA  ARG A 152     3239   3362   3733    159   -238    282       C  
ATOM   1205  C   ARG A 152      39.158  13.522  20.857  1.00 29.03           C  
ANISOU 1205  C   ARG A 152     3456   3600   3972    137   -205    286       C  
ATOM   1206  O   ARG A 152      38.828  12.538  20.184  1.00 29.00           O  
ANISOU 1206  O   ARG A 152     3473   3590   3956    162   -172    280       O  
ATOM   1207  CB  ARG A 152      41.057  12.897  22.430  1.00 23.81           C  
ANISOU 1207  CB  ARG A 152     2762   2984   3301    196   -252    293       C  
ATOM   1208  CG  ARG A 152      41.686  13.157  23.824  1.00 17.53           C  
ANISOU 1208  CG  ARG A 152     1963   2196   2500    204   -298    294       C  
ATOM   1209  CD  ARG A 152      43.024  12.402  23.915  1.00 26.52           C  
ANISOU 1209  CD  ARG A 152     3056   3391   3631    256   -307    305       C  
ATOM   1210  NE  ARG A 152      42.720  10.987  24.133  1.00 27.09           N  
ANISOU 1210  NE  ARG A 152     3183   3432   3677    321   -283    297       N  
ATOM   1211  CZ  ARG A 152      43.639  10.032  24.170  1.00 29.43           C  
ANISOU 1211  CZ  ARG A 152     3463   3760   3958    388   -282    304       C  
ATOM   1212  NH1 ARG A 152      44.918  10.354  23.972  1.00 22.27           N  
ANISOU 1212  NH1 ARG A 152     2474   2930   3059    399   -300    319       N  
ATOM   1213  NH2 ARG A 152      43.280   8.753  24.406  1.00 25.20           N  
ANISOU 1213  NH2 ARG A 152     2996   3181   3397    445   -263    297       N  
ATOM   1214  N   VAL A 153      39.149  14.759  20.364  1.00 23.89           N  
ANISOU 1214  N   VAL A 153     2777   2959   3341     89   -216    295       N  
ATOM   1215  CA  VAL A 153      38.811  14.991  18.978  1.00 26.85           C  
ANISOU 1215  CA  VAL A 153     3136   3344   3720     68   -188    303       C  
ATOM   1216  C   VAL A 153      39.997  15.562  18.208  1.00 30.74           C  
ANISOU 1216  C   VAL A 153     3564   3892   4225     47   -193    325       C  
ATOM   1217  O   VAL A 153      41.056  15.835  18.801  1.00 30.21           O  
ANISOU 1217  O   VAL A 153     3458   3856   4164     44   -221    336       O  
ATOM   1218  CB  VAL A 153      37.634  15.958  18.859  1.00 28.58           C  
ANISOU 1218  CB  VAL A 153     3385   3529   3947     31   -192    299       C  
ATOM   1219  CG1 VAL A 153      36.380  15.310  19.347  1.00 28.99           C  
ANISOU 1219  CG1 VAL A 153     3489   3543   3982     48   -177    281       C  
ATOM   1220  CG2 VAL A 153      37.908  17.277  19.646  1.00 22.05           C  
ANISOU 1220  CG2 VAL A 153     2555   2688   3133     -3   -235    304       C  
ATOM   1221  N   GLY A 154      39.819  15.748  16.895  1.00 28.05           N  
ANISOU 1221  N   GLY A 154     3205   3567   3884     30   -166    336       N  
ATOM   1222  CA  GLY A 154      40.875  16.309  16.062  1.00 25.79           C  
ANISOU 1222  CA  GLY A 154     2855   3340   3605      5   -164    362       C  
ATOM   1223  C   GLY A 154      42.148  15.468  16.064  1.00 23.31           C  
ANISOU 1223  C   GLY A 154     2490   3087   3280     50   -155    369       C  
ATOM   1224  O   GLY A 154      42.098  14.239  16.220  1.00 31.73           O  
ANISOU 1224  O   GLY A 154     3580   4147   4329    111   -136    351       O  
ATOM   1225  N   THR A 155      43.294  16.122  15.944  1.00 23.08           N  
ANISOU 1225  N   THR A 155     2391   3118   3260     20   -171    396       N  
ATOM   1226  CA  THR A 155      44.565  15.411  15.967  1.00 26.53           C  
ANISOU 1226  CA  THR A 155     2766   3629   3686     66   -164    405       C  
ATOM   1227  C   THR A 155      44.695  14.637  17.280  1.00 29.58           C  
ANISOU 1227  C   THR A 155     3178   3994   4066    118   -187    386       C  
ATOM   1228  O   THR A 155      45.061  13.465  17.285  1.00 33.63           O  
ANISOU 1228  O   THR A 155     3692   4526   4559    192   -168    376       O  
ATOM   1229  CB  THR A 155      45.797  16.341  15.763  1.00 26.70           C  
ANISOU 1229  CB  THR A 155     2698   3729   3719     13   -183    442       C  
ATOM   1230  OG1 THR A 155      45.818  17.352  16.778  1.00 24.28           O  
ANISOU 1230  OG1 THR A 155     2401   3392   3433    -47   -237    446       O  
ATOM   1231  CG2 THR A 155      45.780  16.988  14.396  1.00 23.50           C  
ANISOU 1231  CG2 THR A 155     2265   3352   3312    -33   -155    467       C  
ATOM   1232  N   PHE A 156      44.360  15.271  18.392  1.00 26.51           N  
ANISOU 1232  N   PHE A 156     2819   3562   3690     84   -229    379       N  
ATOM   1233  CA  PHE A 156      44.524  14.619  19.701  1.00 28.07           C  
ANISOU 1233  CA  PHE A 156     3043   3744   3879    129   -254    364       C  
ATOM   1234  C   PHE A 156      43.836  13.269  19.789  1.00 32.68           C  
ANISOU 1234  C   PHE A 156     3690   4284   4442    197   -224    341       C  
ATOM   1235  O   PHE A 156      44.330  12.363  20.480  1.00 23.97           O  
ANISOU 1235  O   PHE A 156     2593   3190   3323    258   -232    336       O  
ATOM   1236  CB  PHE A 156      44.019  15.554  20.808  1.00 28.53           C  
ANISOU 1236  CB  PHE A 156     3140   3751   3949     80   -299    356       C  
ATOM   1237  CG  PHE A 156      44.548  16.940  20.662  1.00 30.53           C  
ANISOU 1237  CG  PHE A 156     3351   4027   4222      3   -332    376       C  
ATOM   1238  CD1 PHE A 156      45.804  17.262  21.143  1.00 29.06           C  
ANISOU 1238  CD1 PHE A 156     3100   3903   4040    -17   -370    394       C  
ATOM   1239  CD2 PHE A 156      43.827  17.897  19.963  1.00 30.33           C  
ANISOU 1239  CD2 PHE A 156     3348   3966   4210    -53   -325    381       C  
ATOM   1240  CE1 PHE A 156      46.327  18.524  20.950  1.00 32.41           C  
ANISOU 1240  CE1 PHE A 156     3487   4347   4481   -100   -402    416       C  
ATOM   1241  CE2 PHE A 156      44.332  19.177  19.787  1.00 27.80           C  
ANISOU 1241  CE2 PHE A 156     2998   3658   3905   -129   -356    403       C  
ATOM   1242  CZ  PHE A 156      45.590  19.481  20.286  1.00 34.00           C  
ANISOU 1242  CZ  PHE A 156     3723   4502   4695   -157   -395    421       C  
ATOM   1243  N   GLY A 157      42.688  13.148  19.107  1.00 30.22           N  
ANISOU 1243  N   GLY A 157     3429   3924   4128    185   -194    329       N  
ATOM   1244  CA  GLY A 157      41.913  11.923  19.145  1.00 27.77           C  
ANISOU 1244  CA  GLY A 157     3187   3567   3798    233   -168    309       C  
ATOM   1245  C   GLY A 157      42.144  10.970  17.979  1.00 31.95           C  
ANISOU 1245  C   GLY A 157     3715   4117   4309    278   -127    306       C  
ATOM   1246  O   GLY A 157      41.853   9.784  18.109  1.00 29.18           O  
ANISOU 1246  O   GLY A 157     3420   3731   3936    328   -112    290       O  
ATOM   1247  N   PHE A 158      42.672  11.476  16.856  1.00 26.84           N  
ANISOU 1247  N   PHE A 158     3009   3524   3666    261   -110    320       N  
ATOM   1248  CA  PHE A 158      42.586  10.742  15.604  1.00 25.24           C  
ANISOU 1248  CA  PHE A 158     2817   3331   3441    294    -68    313       C  
ATOM   1249  C   PHE A 158      43.780  10.793  14.683  1.00 26.98           C  
ANISOU 1249  C   PHE A 158     2961   3638   3651    319    -48    331       C  
ATOM   1250  O   PHE A 158      43.808  10.094  13.673  1.00 30.40           O  
ANISOU 1250  O   PHE A 158     3407   4084   4060    360    -12    322       O  
ATOM   1251  CB  PHE A 158      41.247  11.063  14.875  1.00 23.82           C  
ANISOU 1251  CB  PHE A 158     2682   3104   3263    244    -53    303       C  
ATOM   1252  CG  PHE A 158      40.027  10.590  15.663  1.00 28.53           C  
ANISOU 1252  CG  PHE A 158     3358   3625   3858    237    -61    283       C  
ATOM   1253  CD1 PHE A 158      39.704   9.238  15.717  1.00 23.41           C  
ANISOU 1253  CD1 PHE A 158     2773   2937   3184    283    -46    263       C  
ATOM   1254  CD2 PHE A 158      39.277  11.480  16.415  1.00 28.68           C  
ANISOU 1254  CD2 PHE A 158     3387   3614   3896    187    -86    285       C  
ATOM   1255  CE1 PHE A 158      38.603   8.786  16.470  1.00 26.13           C  
ANISOU 1255  CE1 PHE A 158     3186   3218   3524    268    -53    251       C  
ATOM   1256  CE2 PHE A 158      38.165  11.054  17.181  1.00 29.62           C  
ANISOU 1256  CE2 PHE A 158     3569   3676   4009    181    -90    270       C  
ATOM   1257  CZ  PHE A 158      37.831   9.705  17.215  1.00 28.96           C  
ANISOU 1257  CZ  PHE A 158     3544   3559   3902    216    -73    255       C  
ATOM   1258  N   LEU A 159      44.774  11.601  15.012  1.00 33.35           N  
ANISOU 1258  N   LEU A 159     3688   4508   4474    295    -71    357       N  
ATOM   1259  CA  LEU A 159      45.989  11.586  14.210  1.00 33.54           C  
ANISOU 1259  CA  LEU A 159     3628   4630   4485    322    -49    378       C  
ATOM   1260  C   LEU A 159      46.585  10.210  14.364  1.00 34.64           C  
ANISOU 1260  C   LEU A 159     3779   4787   4594    429    -33    363       C  
ATOM   1261  O   LEU A 159      46.707   9.707  15.474  1.00 38.05           O  
ANISOU 1261  O   LEU A 159     4237   5193   5027    466    -59    354       O  
ATOM   1262  CB  LEU A 159      46.981  12.635  14.669  1.00 33.39           C  
ANISOU 1262  CB  LEU A 159     3519   4679   4487    271    -82    411       C  
ATOM   1263  CG  LEU A 159      48.263  12.705  13.843  1.00 40.64           C  
ANISOU 1263  CG  LEU A 159     4334   5715   5391    289    -58    440       C  
ATOM   1264  CD1 LEU A 159      48.614  14.188  13.517  1.00 33.38           C  
ANISOU 1264  CD1 LEU A 159     3348   4839   4495    181    -76    478       C  
ATOM   1265  CD2 LEU A 159      49.440  11.947  14.556  1.00 33.07           C  
ANISOU 1265  CD2 LEU A 159     3321   4825   4418    369    -70    444       C  
ATOM   1266  N   ALA A 160      46.957   9.609  13.247  1.00 34.84           N  
ANISOU 1266  N   ALA A 160     3791   4856   4591    483     10    360       N  
ATOM   1267  CA  ALA A 160      47.504   8.266  13.254  1.00 35.08           C  
ANISOU 1267  CA  ALA A 160     3844   4899   4587    597     28    342       C  
ATOM   1268  C   ALA A 160      48.700   8.085  12.305  1.00 36.30           C  
ANISOU 1268  C   ALA A 160     3912   5167   4712    657     64    358       C  
ATOM   1269  O   ALA A 160      48.720   8.582  11.180  1.00 32.23           O  
ANISOU 1269  O   ALA A 160     3361   4696   4189    624     94    370       O  
ATOM   1270  CB  ALA A 160      46.409   7.266  12.917  1.00 27.62           C  
ANISOU 1270  CB  ALA A 160     3019   3856   3620    627     48    306       C  
ATOM   1271  N   LEU A 161      49.707   7.375  12.787  1.00 35.21           N  
ANISOU 1271  N   LEU A 161     3740   5083   4556    749     60    361       N  
ATOM   1272  CA  LEU A 161      50.726   6.816  11.916  1.00 36.47           C  
ANISOU 1272  CA  LEU A 161     3840   5341   4675    842    101    366       C  
ATOM   1273  C   LEU A 161      50.504   5.316  12.033  1.00 31.62           C  
ANISOU 1273  C   LEU A 161     3333   4656   4024    960    113    327       C  
ATOM   1274  O   LEU A 161      51.001   4.676  12.953  1.00 34.90           O  
ANISOU 1274  O   LEU A 161     3757   5070   4432   1033     90    325       O  
ATOM   1275  CB  LEU A 161      52.108   7.278  12.382  1.00 41.62           C  
ANISOU 1275  CB  LEU A 161     4357   6122   5333    855     84    403       C  
ATOM   1276  CG  LEU A 161      52.077   8.779  12.056  1.00 46.62           C  
ANISOU 1276  CG  LEU A 161     4915   6798   6000    719     74    438       C  
ATOM   1277  CD1 LEU A 161      52.744   9.638  13.096  1.00 52.25           C  
ANISOU 1277  CD1 LEU A 161     5545   7563   6746    656     23    469       C  
ATOM   1278  CD2 LEU A 161      52.651   9.040  10.668  1.00 46.33           C  
ANISOU 1278  CD2 LEU A 161     4801   6865   5937    723    126    460       C  
ATOM   1279  N   PRO A 162      49.638   4.780  11.171  1.00 37.19           N  
ANISOU 1279  N   PRO A 162     4133   5290   4707    968    142    297       N  
ATOM   1280  CA  PRO A 162      49.150   3.406  11.364  1.00 37.58           C  
ANISOU 1280  CA  PRO A 162     4313   5239   4726   1052    145    258       C  
ATOM   1281  C   PRO A 162      50.305   2.446  11.487  1.00 41.28           C  
ANISOU 1281  C   PRO A 162     4765   5765   5156   1196    156    255       C  
ATOM   1282  O   PRO A 162      51.234   2.471  10.676  1.00 41.65           O  
ANISOU 1282  O   PRO A 162     4730   5921   5174   1256    191    265       O  
ATOM   1283  CB  PRO A 162      48.347   3.150  10.098  1.00 34.35           C  
ANISOU 1283  CB  PRO A 162     3975   4785   4292   1036    180    232       C  
ATOM   1284  CG  PRO A 162      47.823   4.531   9.753  1.00 34.46           C  
ANISOU 1284  CG  PRO A 162     3929   4821   4343    904    176    256       C  
ATOM   1285  CD  PRO A 162      48.913   5.480  10.093  1.00 29.48           C  
ANISOU 1285  CD  PRO A 162     3161   4306   3736    883    166    298       C  
ATOM   1286  N   GLY A 163      50.275   1.624  12.527  1.00 48.18           N  
ANISOU 1286  N   GLY A 163     5710   6571   6024   1255    128    243       N  
ATOM   1287  CA  GLY A 163      51.343   0.665  12.734  1.00 46.34           C  
ANISOU 1287  CA  GLY A 163     5470   6384   5752   1404    134    240       C  
ATOM   1288  C   GLY A 163      52.367   1.097  13.766  1.00 49.54           C  
ANISOU 1288  C   GLY A 163     5763   6883   6177   1422    100    275       C  
ATOM   1289  O   GLY A 163      53.046   0.240  14.342  1.00 50.46           O  
ANISOU 1289  O   GLY A 163     5896   7010   6266   1541     88    272       O  
ATOM   1290  N   SER A 164      52.491   2.404  14.004  1.00 40.60           N  
ANISOU 1290  N   SER A 164     4522   5816   5087   1308     81    306       N  
ATOM   1291  CA  SER A 164      53.376   2.900  15.061  1.00 42.29           C  
ANISOU 1291  CA  SER A 164     4634   6112   5322   1305     39    338       C  
ATOM   1292  C   SER A 164      52.827   2.514  16.434  1.00 46.40           C  
ANISOU 1292  C   SER A 164     5246   6528   5856   1300     -8    329       C  
ATOM   1293  O   SER A 164      51.668   2.097  16.576  1.00 49.32           O  
ANISOU 1293  O   SER A 164     5745   6766   6229   1269     -9    304       O  
ATOM   1294  CB  SER A 164      53.511   4.428  14.995  1.00 47.06           C  
ANISOU 1294  CB  SER A 164     5122   6790   5969   1167     25    372       C  
ATOM   1295  OG  SER A 164      52.274   5.077  15.334  1.00 45.92           O  
ANISOU 1295  OG  SER A 164     5048   6537   5862   1044      4    363       O  
ATOM   1296  N   ARG A 165      53.641   2.691  17.458  1.00 48.75           N  
ANISOU 1296  N   ARG A 165     5474   6889   6161   1323    -49    352       N  
ATOM   1297  CA  ARG A 165      53.204   2.372  18.805  1.00 55.44           C  
ANISOU 1297  CA  ARG A 165     6400   7648   7016   1320    -95    348       C  
ATOM   1298  C   ARG A 165      52.686   3.647  19.467  1.00 49.29           C  
ANISOU 1298  C   ARG A 165     5589   6855   6285   1173   -132    361       C  
ATOM   1299  O   ARG A 165      51.800   3.624  20.334  1.00 45.58           O  
ANISOU 1299  O   ARG A 165     5207   6283   5827   1126   -159    351       O  
ATOM   1300  CB  ARG A 165      54.390   1.829  19.603  1.00 65.82           C  
ANISOU 1300  CB  ARG A 165     7662   9041   8307   1434   -124    364       C  
ATOM   1301  CG  ARG A 165      54.001   0.960  20.770  1.00 83.28           C  
ANISOU 1301  CG  ARG A 165     9992  11149  10504   1487   -158    354       C  
ATOM   1302  CD  ARG A 165      54.953   1.188  21.925  1.00 98.33           C  
ANISOU 1302  CD  ARG A 165    11813  13137  12409   1517   -211    381       C  
ATOM   1303  NE  ARG A 165      54.594   2.398  22.668  1.00107.75           N  
ANISOU 1303  NE  ARG A 165    12966  14330  13644   1376   -252    394       N  
ATOM   1304  CZ  ARG A 165      55.451   3.114  23.391  1.00107.97           C  
ANISOU 1304  CZ  ARG A 165    12881  14458  13683   1349   -299    419       C  
ATOM   1305  NH1 ARG A 165      56.727   2.747  23.459  1.00111.61           N  
ANISOU 1305  NH1 ARG A 165    13246  15041  14118   1453   -309    439       N  
ATOM   1306  NH2 ARG A 165      55.036   4.196  24.038  1.00 97.49           N  
ANISOU 1306  NH2 ARG A 165    11538  13114  12390   1221   -336    425       N  
ATOM   1307  N   GLU A 166      53.259   4.764  19.042  1.00 40.25           N  
ANISOU 1307  N   GLU A 166     4317   5814   5161   1101   -133    386       N  
ATOM   1308  CA  GLU A 166      53.049   6.019  19.721  1.00 39.64           C  
ANISOU 1308  CA  GLU A 166     4198   5739   5124    974   -176    402       C  
ATOM   1309  C   GLU A 166      51.812   6.804  19.234  1.00 41.34           C  
ANISOU 1309  C   GLU A 166     4467   5872   5369    856   -162    390       C  
ATOM   1310  O   GLU A 166      51.383   7.743  19.910  1.00 43.93           O  
ANISOU 1310  O   GLU A 166     4796   6169   5726    759   -198    396       O  
ATOM   1311  CB  GLU A 166      54.320   6.857  19.619  1.00 41.24           C  
ANISOU 1311  CB  GLU A 166     4242   6092   5335    947   -193    437       C  
ATOM   1312  CG  GLU A 166      55.606   6.133  20.158  1.00 52.01           C  
ANISOU 1312  CG  GLU A 166     5535   7559   6669   1067   -212    452       C  
ATOM   1313  CD  GLU A 166      56.383   5.345  19.070  1.00 63.14           C  
ANISOU 1313  CD  GLU A 166     6894   9057   8040   1187   -158    455       C  
ATOM   1314  OE1 GLU A 166      55.805   4.963  18.013  1.00 55.80           O  
ANISOU 1314  OE1 GLU A 166     6025   8078   7098   1206   -105    435       O  
ATOM   1315  OE2 GLU A 166      57.598   5.117  19.274  1.00 66.28           O  
ANISOU 1315  OE2 GLU A 166     7186   9580   8417   1264   -170    477       O  
ATOM   1316  N   ALA A 167      51.245   6.409  18.087  1.00 38.80           N  
ANISOU 1316  N   ALA A 167     4193   5515   5035    871   -112    374       N  
ATOM   1317  CA  ALA A 167      50.116   7.115  17.463  1.00 36.75           C  
ANISOU 1317  CA  ALA A 167     3976   5191   4798    769    -95    365       C  
ATOM   1318  C   ALA A 167      49.376   6.166  16.554  1.00 39.81           C  
ANISOU 1318  C   ALA A 167     4456   5511   5159    817    -50    337       C  
ATOM   1319  O   ALA A 167      49.393   6.334  15.314  1.00 36.04           O  
ANISOU 1319  O   ALA A 167     3953   5068   4672    809    -12    338       O  
ATOM   1320  CB  ALA A 167      50.597   8.320  16.663  1.00 36.53           C  
ANISOU 1320  CB  ALA A 167     3840   5251   4788    690    -87    393       C  
ATOM   1321  N   PRO A 168      48.716   5.163  17.163  1.00 35.16           N  
ANISOU 1321  N   PRO A 168     3981   4824   4555    863    -57    313       N  
ATOM   1322  CA  PRO A 168      48.162   4.006  16.446  1.00 37.29           C  
ANISOU 1322  CA  PRO A 168     4353   5025   4793    924    -22    285       C  
ATOM   1323  C   PRO A 168      46.818   4.336  15.797  1.00 42.63           C  
ANISOU 1323  C   PRO A 168     5090   5627   5481    835     -5    269       C  
ATOM   1324  O   PRO A 168      46.288   3.508  15.022  1.00 41.46           O  
ANISOU 1324  O   PRO A 168     5023   5426   5306    866     23    245       O  
ATOM   1325  CB  PRO A 168      47.950   2.965  17.548  1.00 31.64           C  
ANISOU 1325  CB  PRO A 168     3733   4228   4060    985    -45    273       C  
ATOM   1326  CG  PRO A 168      48.156   3.690  18.870  1.00 33.03           C  
ANISOU 1326  CG  PRO A 168     3863   4422   4263    939    -93    294       C  
ATOM   1327  CD  PRO A 168      48.490   5.106  18.617  1.00 30.37           C  
ANISOU 1327  CD  PRO A 168     3413   4166   3959    853   -101    315       C  
ATOM   1328  N   GLY A 169      46.260   5.506  16.123  1.00 33.94           N  
ANISOU 1328  N   GLY A 169     3958   4520   4417    729    -26    282       N  
ATOM   1329  CA  GLY A 169      44.964   5.878  15.571  1.00 32.53           C  
ANISOU 1329  CA  GLY A 169     3831   4279   4250    649    -13    270       C  
ATOM   1330  C   GLY A 169      43.786   5.501  16.460  1.00 33.57           C  
ANISOU 1330  C   GLY A 169     4059   4309   4386    617    -32    255       C  
ATOM   1331  O   GLY A 169      43.921   4.694  17.395  1.00 32.40           O  
ANISOU 1331  O   GLY A 169     3961   4124   4225    668    -48    251       O  
ATOM   1332  N   ASN A 170      42.632   6.122  16.204  1.00 30.14           N  
ANISOU 1332  N   ASN A 170     3647   3836   3969    533    -30    251       N  
ATOM   1333  CA  ASN A 170      41.407   5.750  16.885  1.00 28.28           C  
ANISOU 1333  CA  ASN A 170     3497   3515   3733    498    -40    239       C  
ATOM   1334  C   ASN A 170      41.373   5.964  18.410  1.00 30.07           C  
ANISOU 1334  C   ASN A 170     3731   3723   3973    489    -74    248       C  
ATOM   1335  O   ASN A 170      40.465   5.463  19.084  1.00 30.90           O  
ANISOU 1335  O   ASN A 170     3910   3760   4069    472    -79    241       O  
ATOM   1336  CB  ASN A 170      41.066   4.282  16.547  1.00 24.93           C  
ANISOU 1336  CB  ASN A 170     3170   3028   3273    549    -21    217       C  
ATOM   1337  CG  ASN A 170      40.803   4.081  15.065  1.00 35.47           C  
ANISOU 1337  CG  ASN A 170     4517   4368   4591    546     10    202       C  
ATOM   1338  OD1 ASN A 170      40.193   4.942  14.419  1.00 37.03           O  
ANISOU 1338  OD1 ASN A 170     4683   4583   4805    479     17    205       O  
ATOM   1339  ND2 ASN A 170      41.276   2.942  14.504  1.00 37.19           N  
ANISOU 1339  ND2 ASN A 170     4786   4572   4773    625     28    185       N  
ATOM   1340  N   VAL A 171      42.337   6.675  18.983  1.00 29.03           N  
ANISOU 1340  N   VAL A 171     3526   3649   3856    496    -98    265       N  
ATOM   1341  CA  VAL A 171      42.329   6.776  20.439  1.00 26.78           C  
ANISOU 1341  CA  VAL A 171     3256   3343   3574    493   -133    271       C  
ATOM   1342  C   VAL A 171      41.106   7.541  21.000  1.00 31.03           C  
ANISOU 1342  C   VAL A 171     3823   3838   4129    416   -144    268       C  
ATOM   1343  O   VAL A 171      40.718   7.342  22.154  1.00 32.60           O  
ANISOU 1343  O   VAL A 171     4066   4001   4320    415   -162    268       O  
ATOM   1344  CB  VAL A 171      43.646   7.285  21.007  1.00 32.05           C  
ANISOU 1344  CB  VAL A 171     3844   4084   4251    518   -163    288       C  
ATOM   1345  CG1 VAL A 171      44.814   6.483  20.424  1.00 31.11           C  
ANISOU 1345  CG1 VAL A 171     3691   4018   4111    605   -148    292       C  
ATOM   1346  CG2 VAL A 171      43.812   8.802  20.752  1.00 29.77           C  
ANISOU 1346  CG2 VAL A 171     3476   3842   3992    442   -178    301       C  
ATOM   1347  N   GLY A 172      40.471   8.381  20.188  1.00 29.59           N  
ANISOU 1347  N   GLY A 172     3618   3661   3964    356   -131    267       N  
ATOM   1348  CA  GLY A 172      39.206   8.987  20.620  1.00 29.52           C  
ANISOU 1348  CA  GLY A 172     3641   3612   3964    296   -136    262       C  
ATOM   1349  C   GLY A 172      38.119   7.919  20.806  1.00 29.21           C  
ANISOU 1349  C   GLY A 172     3685   3511   3903    299   -118    251       C  
ATOM   1350  O   GLY A 172      37.260   8.007  21.691  1.00 32.64           O  
ANISOU 1350  O   GLY A 172     4156   3914   4334    273   -125    250       O  
ATOM   1351  N   LEU A 173      38.135   6.915  19.941  1.00 24.08           N  
ANISOU 1351  N   LEU A 173     3068   2846   3235    326    -93    243       N  
ATOM   1352  CA  LEU A 173      37.216   5.767  20.067  1.00 28.11           C  
ANISOU 1352  CA  LEU A 173     3665   3293   3721    324    -80    233       C  
ATOM   1353  C   LEU A 173      37.521   4.901  21.298  1.00 28.63           C  
ANISOU 1353  C   LEU A 173     3785   3325   3768    367    -95    239       C  
ATOM   1354  O   LEU A 173      36.628   4.374  21.940  1.00 28.11           O  
ANISOU 1354  O   LEU A 173     3782   3211   3687    343    -93    240       O  
ATOM   1355  CB  LEU A 173      37.280   4.920  18.816  1.00 25.60           C  
ANISOU 1355  CB  LEU A 173     3377   2963   3385    346    -55    220       C  
ATOM   1356  CG  LEU A 173      36.636   5.555  17.589  1.00 30.53           C  
ANISOU 1356  CG  LEU A 173     3972   3607   4019    296    -39    214       C  
ATOM   1357  CD1 LEU A 173      36.959   4.749  16.360  1.00 31.75           C  
ANISOU 1357  CD1 LEU A 173     4153   3758   4151    330    -17    199       C  
ATOM   1358  CD2 LEU A 173      35.130   5.610  17.787  1.00 32.18           C  
ANISOU 1358  CD2 LEU A 173     4218   3782   4227    229    -37    212       C  
ATOM   1359  N   LEU A 174      38.793   4.825  21.660  1.00 31.64           N  
ANISOU 1359  N   LEU A 174     4135   3738   4148    429   -111    245       N  
ATOM   1360  CA  LEU A 174      39.200   4.099  22.834  1.00 28.25           C  
ANISOU 1360  CA  LEU A 174     3751   3285   3699    477   -130    253       C  
ATOM   1361  C   LEU A 174      38.843   4.914  24.065  1.00 30.30           C  
ANISOU 1361  C   LEU A 174     3996   3549   3967    439   -154    262       C  
ATOM   1362  O   LEU A 174      38.597   4.328  25.106  1.00 30.46           O  
ANISOU 1362  O   LEU A 174     4074   3533   3967    452   -164    269       O  
ATOM   1363  CB  LEU A 174      40.710   3.778  22.793  1.00 30.71           C  
ANISOU 1363  CB  LEU A 174     4024   3640   4004    562   -141    258       C  
ATOM   1364  CG  LEU A 174      41.188   2.844  21.668  1.00 36.85           C  
ANISOU 1364  CG  LEU A 174     4824   4413   4763    622   -116    247       C  
ATOM   1365  CD1 LEU A 174      42.709   2.811  21.626  1.00 37.55           C  
ANISOU 1365  CD1 LEU A 174     4847   4573   4848    705   -126    254       C  
ATOM   1366  CD2 LEU A 174      40.639   1.416  21.832  1.00 37.14           C  
ANISOU 1366  CD2 LEU A 174     4984   4363   4766    651   -107    239       C  
ATOM   1367  N   ASP A 175      38.848   6.258  23.974  1.00 28.11           N  
ANISOU 1367  N   ASP A 175     3648   3316   3718    395   -164    263       N  
ATOM   1368  CA  ASP A 175      38.317   7.070  25.086  1.00 30.23           C  
ANISOU 1368  CA  ASP A 175     3916   3581   3990    358   -185    266       C  
ATOM   1369  C   ASP A 175      36.861   6.679  25.337  1.00 28.76           C  
ANISOU 1369  C   ASP A 175     3793   3346   3788    318   -164    263       C  
ATOM   1370  O   ASP A 175      36.448   6.448  26.481  1.00 29.84           O  
ANISOU 1370  O   ASP A 175     3972   3461   3905    318   -172    270       O  
ATOM   1371  CB  ASP A 175      38.392   8.575  24.816  1.00 22.65           C  
ANISOU 1371  CB  ASP A 175     2887   2660   3058    314   -199    264       C  
ATOM   1372  CG  ASP A 175      39.828   9.073  24.666  1.00 30.99           C  
ANISOU 1372  CG  ASP A 175     3873   3773   4129    336   -224    271       C  
ATOM   1373  OD1 ASP A 175      40.774   8.345  25.061  1.00 30.22           O  
ANISOU 1373  OD1 ASP A 175     3773   3691   4017    394   -236    277       O  
ATOM   1374  OD2 ASP A 175      40.011  10.192  24.150  1.00 36.97           O  
ANISOU 1374  OD2 ASP A 175     4576   4561   4911    297   -231    273       O  
ATOM   1375  N   GLN A 176      36.089   6.587  24.260  1.00 25.84           N  
ANISOU 1375  N   GLN A 176     3428   2966   3424    284   -137    257       N  
ATOM   1376  CA  GLN A 176      34.679   6.221  24.402  1.00 29.40           C  
ANISOU 1376  CA  GLN A 176     3927   3382   3860    238   -117    257       C  
ATOM   1377  C   GLN A 176      34.569   4.821  25.019  1.00 28.76           C  
ANISOU 1377  C   GLN A 176     3929   3252   3747    259   -112    265       C  
ATOM   1378  O   GLN A 176      33.773   4.592  25.920  1.00 31.53           O  
ANISOU 1378  O   GLN A 176     4319   3583   4079    234   -110    275       O  
ATOM   1379  CB  GLN A 176      33.938   6.296  23.059  1.00 25.06           C  
ANISOU 1379  CB  GLN A 176     3367   2836   3320    198    -93    249       C  
ATOM   1380  CG  GLN A 176      33.932   7.690  22.440  1.00 28.59           C  
ANISOU 1380  CG  GLN A 176     3743   3326   3795    174    -98    245       C  
ATOM   1381  CD  GLN A 176      33.494   7.642  20.985  1.00 31.91           C  
ANISOU 1381  CD  GLN A 176     4151   3753   4221    148    -77    238       C  
ATOM   1382  OE1 GLN A 176      33.026   6.606  20.517  1.00 34.32           O  
ANISOU 1382  OE1 GLN A 176     4504   4028   4507    140    -61    233       O  
ATOM   1383  NE2 GLN A 176      33.625   8.770  20.268  1.00 28.84           N  
ANISOU 1383  NE2 GLN A 176     3705   3399   3854    133    -80    238       N  
ATOM   1384  N   ARG A 177      35.380   3.893  24.528  1.00 30.82           N  
ANISOU 1384  N   ARG A 177     4218   3493   3999    308   -111    262       N  
ATOM   1385  CA  ARG A 177      35.335   2.523  25.015  1.00 36.41           C  
ANISOU 1385  CA  ARG A 177     5017   4142   4674    334   -109    270       C  
ATOM   1386  C   ARG A 177      35.645   2.450  26.526  1.00 36.44           C  
ANISOU 1386  C   ARG A 177     5044   4142   4662    361   -131    286       C  
ATOM   1387  O   ARG A 177      34.975   1.716  27.266  1.00 34.11           O  
ANISOU 1387  O   ARG A 177     4820   3801   4338    343   -126    300       O  
ATOM   1388  CB  ARG A 177      36.302   1.631  24.220  1.00 33.29           C  
ANISOU 1388  CB  ARG A 177     4649   3729   4270    400   -107    261       C  
ATOM   1389  CG  ARG A 177      36.398   0.188  24.798  1.00 40.57           C  
ANISOU 1389  CG  ARG A 177     5679   4580   5155    441   -111    270       C  
ATOM   1390  CD  ARG A 177      37.345  -0.676  23.953  1.00 33.57           C  
ANISOU 1390  CD  ARG A 177     4824   3675   4255    519   -107    257       C  
ATOM   1391  NE  ARG A 177      36.651  -1.005  22.714  1.00 39.21           N  
ANISOU 1391  NE  ARG A 177     5568   4363   4967    478    -85    239       N  
ATOM   1392  CZ  ARG A 177      37.252  -1.413  21.605  1.00 38.72           C  
ANISOU 1392  CZ  ARG A 177     5512   4301   4898    528    -74    220       C  
ATOM   1393  NH1 ARG A 177      38.581  -1.534  21.571  1.00 35.48           N  
ANISOU 1393  NH1 ARG A 177     5073   3924   4484    625    -81    219       N  
ATOM   1394  NH2 ARG A 177      36.518  -1.713  20.543  1.00 35.62           N  
ANISOU 1394  NH2 ARG A 177     5155   3881   4500    482    -57    203       N  
ATOM   1395  N   LEU A 178      36.632   3.231  26.981  1.00 28.94           N  
ANISOU 1395  N   LEU A 178     4031   3239   3725    399   -156    287       N  
ATOM   1396  CA  LEU A 178      36.980   3.270  28.402  1.00 25.36           C  
ANISOU 1396  CA  LEU A 178     3594   2789   3253    426   -182    300       C  
ATOM   1397  C   LEU A 178      35.806   3.783  29.252  1.00 35.09           C  
ANISOU 1397  C   LEU A 178     4840   4018   4476    367   -176    306       C  
ATOM   1398  O   LEU A 178      35.496   3.197  30.307  1.00 31.50           O  
ANISOU 1398  O   LEU A 178     4445   3535   3988    372   -179    322       O  
ATOM   1399  CB  LEU A 178      38.224   4.112  28.641  1.00 25.01           C  
ANISOU 1399  CB  LEU A 178     3472   2803   3226    465   -215    297       C  
ATOM   1400  CG  LEU A 178      38.833   4.147  30.038  1.00 35.67           C  
ANISOU 1400  CG  LEU A 178     4833   4165   4555    503   -250    309       C  
ATOM   1401  CD1 LEU A 178      38.997   2.723  30.632  1.00 30.70           C  
ANISOU 1401  CD1 LEU A 178     4293   3485   3887    557   -251    325       C  
ATOM   1402  CD2 LEU A 178      40.192   4.880  29.936  1.00 35.42           C  
ANISOU 1402  CD2 LEU A 178     4714   4199   4543    537   -283    305       C  
ATOM   1403  N   ALA A 179      35.140   4.843  28.780  1.00 29.36           N  
ANISOU 1403  N   ALA A 179     4060   3321   3773    316   -166    295       N  
ATOM   1404  CA  ALA A 179      33.912   5.299  29.441  1.00 36.75           C  
ANISOU 1404  CA  ALA A 179     5007   4260   4697    267   -153    299       C  
ATOM   1405  C   ALA A 179      32.865   4.211  29.515  1.00 27.63           C  
ANISOU 1405  C   ALA A 179     3921   3064   3514    232   -125    313       C  
ATOM   1406  O   ALA A 179      32.182   4.134  30.517  1.00 36.51           O  
ANISOU 1406  O   ALA A 179     5074   4186   4611    213   -119    327       O  
ATOM   1407  CB  ALA A 179      33.300   6.603  28.791  1.00 19.52           C  
ANISOU 1407  CB  ALA A 179     2760   2114   2542    225   -146    284       C  
ATOM   1408  N   LEU A 180      32.718   3.399  28.467  1.00 30.13           N  
ANISOU 1408  N   LEU A 180     4264   3351   3835    219   -109    311       N  
ATOM   1409  CA  LEU A 180      31.742   2.284  28.486  1.00 34.07           C  
ANISOU 1409  CA  LEU A 180     4836   3803   4306    174    -87    326       C  
ATOM   1410  C   LEU A 180      32.166   1.231  29.512  1.00 38.21           C  
ANISOU 1410  C   LEU A 180     5443   4281   4795    209    -98    346       C  
ATOM   1411  O   LEU A 180      31.318   0.637  30.151  1.00 39.66           O  
ANISOU 1411  O   LEU A 180     5681   4439   4948    167    -84    368       O  
ATOM   1412  CB  LEU A 180      31.507   1.610  27.100  1.00 17.52           C  
ANISOU 1412  CB  LEU A 180     2762   1677   2217    150    -73    315       C  
ATOM   1413  CG  LEU A 180      31.171   2.443  25.848  1.00 29.65           C  
ANISOU 1413  CG  LEU A 180     4228   3253   3785    120    -63    295       C  
ATOM   1414  CD1 LEU A 180      30.698   1.582  24.672  1.00 28.98           C  
ANISOU 1414  CD1 LEU A 180     4185   3132   3693     84    -49    287       C  
ATOM   1415  CD2 LEU A 180      30.164   3.589  26.126  1.00 27.61           C  
ANISOU 1415  CD2 LEU A 180     3908   3047   3536     73    -54    297       C  
ATOM   1416  N   GLN A 181      33.471   0.988  29.657  1.00 34.65           N  
ANISOU 1416  N   GLN A 181     4999   3821   4345    286   -122    343       N  
ATOM   1417  CA  GLN A 181      33.944   0.020  30.661  1.00 36.83           C  
ANISOU 1417  CA  GLN A 181     5355   4054   4585    331   -136    364       C  
ATOM   1418  C   GLN A 181      33.681   0.573  32.053  1.00 39.40           C  
ANISOU 1418  C   GLN A 181     5672   4408   4891    323   -145    380       C  
ATOM   1419  O   GLN A 181      33.279  -0.159  32.949  1.00 34.65           O  
ANISOU 1419  O   GLN A 181     5143   3772   4251    313   -141    405       O  
ATOM   1420  CB  GLN A 181      35.424  -0.303  30.457  1.00 31.26           C  
ANISOU 1420  CB  GLN A 181     4646   3346   3884    423   -162    357       C  
ATOM   1421  CG  GLN A 181      35.627  -0.981  29.109  1.00 44.07           C  
ANISOU 1421  CG  GLN A 181     6292   4936   5516    438   -148    342       C  
ATOM   1422  CD  GLN A 181      37.082  -1.211  28.729  1.00 46.69           C  
ANISOU 1422  CD  GLN A 181     6604   5282   5853    535   -167    332       C  
ATOM   1423  OE1 GLN A 181      37.965  -0.432  29.081  1.00 48.43           O  
ANISOU 1423  OE1 GLN A 181     6749   5564   6089    575   -189    330       O  
ATOM   1424  NE2 GLN A 181      37.326  -2.271  27.973  1.00 42.79           N  
ANISOU 1424  NE2 GLN A 181     6178   4736   5345    573   -159    325       N  
ATOM   1425  N   TRP A 182      33.876   1.887  32.214  1.00 31.63           N  
ANISOU 1425  N   TRP A 182     4604   3484   3929    326   -157    364       N  
ATOM   1426  CA  TRP A 182      33.531   2.545  33.443  1.00 30.52           C  
ANISOU 1426  CA  TRP A 182     4455   3374   3767    317   -164    371       C  
ATOM   1427  C   TRP A 182      32.038   2.356  33.775  1.00 35.84           C  
ANISOU 1427  C   TRP A 182     5158   4043   4416    248   -129    388       C  
ATOM   1428  O   TRP A 182      31.675   2.185  34.936  1.00 36.44           O  
ANISOU 1428  O   TRP A 182     5272   4120   4453    245   -127    408       O  
ATOM   1429  CB  TRP A 182      33.852   4.032  33.352  1.00 34.29           C  
ANISOU 1429  CB  TRP A 182     4846   3908   4275    321   -182    347       C  
ATOM   1430  CG  TRP A 182      33.716   4.754  34.661  1.00 37.44           C  
ANISOU 1430  CG  TRP A 182     5243   4335   4648    327   -197    349       C  
ATOM   1431  CD1 TRP A 182      34.727   5.029  35.554  1.00 29.41           C  
ANISOU 1431  CD1 TRP A 182     4223   3333   3617    377   -238    347       C  
ATOM   1432  CD2 TRP A 182      32.513   5.322  35.225  1.00 30.79           C  
ANISOU 1432  CD2 TRP A 182     4399   3514   3785    287   -174    350       C  
ATOM   1433  NE1 TRP A 182      34.220   5.732  36.630  1.00 37.50           N  
ANISOU 1433  NE1 TRP A 182     5254   4382   4614    368   -242    345       N  
ATOM   1434  CE2 TRP A 182      32.877   5.935  36.452  1.00 37.37           C  
ANISOU 1434  CE2 TRP A 182     5237   4370   4592    317   -202    346       C  
ATOM   1435  CE3 TRP A 182      31.191   5.395  34.807  1.00 26.39           C  
ANISOU 1435  CE3 TRP A 182     3833   2966   3227    231   -135    353       C  
ATOM   1436  CZ2 TRP A 182      31.942   6.587  37.277  1.00 36.57           C  
ANISOU 1436  CZ2 TRP A 182     5138   4296   4460    300   -187    344       C  
ATOM   1437  CZ3 TRP A 182      30.267   6.055  35.612  1.00 24.25           C  
ANISOU 1437  CZ3 TRP A 182     3555   2730   2929    215   -119    354       C  
ATOM   1438  CH2 TRP A 182      30.638   6.622  36.843  1.00 30.80           C  
ANISOU 1438  CH2 TRP A 182     4395   3578   3728    252   -143    349       C  
ATOM   1439  N   VAL A 183      31.165   2.383  32.771  1.00 30.83           N  
ANISOU 1439  N   VAL A 183     4503   3410   3800    192   -102    381       N  
ATOM   1440  CA  VAL A 183      29.770   2.279  33.104  1.00 31.51           C  
ANISOU 1440  CA  VAL A 183     4602   3510   3862    125    -70    399       C  
ATOM   1441  C   VAL A 183      29.511   0.864  33.616  1.00 34.59           C  
ANISOU 1441  C   VAL A 183     5088   3843   4211    105    -61    432       C  
ATOM   1442  O   VAL A 183      28.810   0.664  34.610  1.00 39.64           O  
ANISOU 1442  O   VAL A 183     5757   4492   4812     77    -45    458       O  
ATOM   1443  CB  VAL A 183      28.855   2.701  31.931  1.00 36.66           C  
ANISOU 1443  CB  VAL A 183     5201   4187   4541     68    -47    386       C  
ATOM   1444  CG1 VAL A 183      27.442   2.246  32.144  1.00 26.31           C  
ANISOU 1444  CG1 VAL A 183     3908   2886   3201     -6    -14    410       C  
ATOM   1445  CG2 VAL A 183      28.883   4.245  31.762  1.00 39.35           C  
ANISOU 1445  CG2 VAL A 183     5455   4586   4910     85    -54    360       C  
ATOM   1446  N   GLN A 184      30.140  -0.117  32.986  1.00 35.45           N  
ANISOU 1446  N   GLN A 184     5252   3891   4325    125    -71    432       N  
ATOM   1447  CA  GLN A 184      29.925  -1.502  33.377  1.00 36.50           C  
ANISOU 1447  CA  GLN A 184     5492   3956   4421    106    -66    463       C  
ATOM   1448  C   GLN A 184      30.329  -1.706  34.823  1.00 37.80           C  
ANISOU 1448  C   GLN A 184     5702   4116   4546    147    -80    488       C  
ATOM   1449  O   GLN A 184      29.637  -2.392  35.578  1.00 33.67           O  
ANISOU 1449  O   GLN A 184     5244   3569   3981    104    -65    524       O  
ATOM   1450  CB  GLN A 184      30.725  -2.447  32.487  1.00 31.23           C  
ANISOU 1450  CB  GLN A 184     4884   3221   3763    144    -81    453       C  
ATOM   1451  CG  GLN A 184      30.137  -2.539  31.141  1.00 31.70           C  
ANISOU 1451  CG  GLN A 184     4927   3272   3846     90    -65    435       C  
ATOM   1452  CD  GLN A 184      28.774  -3.163  31.193  1.00 38.93           C  
ANISOU 1452  CD  GLN A 184     5887   4167   4735    -13    -41    460       C  
ATOM   1453  OE1 GLN A 184      28.616  -4.332  31.618  1.00 41.43           O  
ANISOU 1453  OE1 GLN A 184     6310   4415   5017    -35    -42    488       O  
ATOM   1454  NE2 GLN A 184      27.773  -2.411  30.758  1.00 35.69           N  
ANISOU 1454  NE2 GLN A 184     5401   3819   4342    -79    -20    453       N  
ATOM   1455  N   GLU A 185      31.458  -1.122  35.203  1.00 31.17           N  
ANISOU 1455  N   GLU A 185     4828   3299   3716    227   -110    473       N  
ATOM   1456  CA  GLU A 185      31.958  -1.338  36.536  1.00 33.70           C  
ANISOU 1456  CA  GLU A 185     5192   3615   3997    274   -130    495       C  
ATOM   1457  C   GLU A 185      31.200  -0.557  37.610  1.00 40.43           C  
ANISOU 1457  C   GLU A 185     6016   4523   4822    245   -117    504       C  
ATOM   1458  O   GLU A 185      31.015  -1.093  38.707  1.00 37.36           O  
ANISOU 1458  O   GLU A 185     5692   4121   4384    245   -115    537       O  
ATOM   1459  CB  GLU A 185      33.458  -1.057  36.668  1.00 34.62           C  
ANISOU 1459  CB  GLU A 185     5284   3743   4127    370   -173    478       C  
ATOM   1460  CG  GLU A 185      33.911  -1.334  38.087  1.00 42.56           C  
ANISOU 1460  CG  GLU A 185     6340   4745   5085    416   -196    503       C  
ATOM   1461  CD  GLU A 185      35.396  -1.592  38.267  1.00 54.67           C  
ANISOU 1461  CD  GLU A 185     7880   6273   6619    514   -241    499       C  
ATOM   1462  OE1 GLU A 185      35.761  -2.192  39.322  1.00 54.73           O  
ANISOU 1462  OE1 GLU A 185     7955   6259   6581    557   -261    526       O  
ATOM   1463  OE2 GLU A 185      36.191  -1.196  37.378  1.00 57.47           O  
ANISOU 1463  OE2 GLU A 185     8170   6651   7016    549   -255    471       O  
ATOM   1464  N   ASN A 186      30.747   0.671  37.296  1.00 32.24           N  
ANISOU 1464  N   ASN A 186     4890   3549   3812    222   -107    478       N  
ATOM   1465  CA  ASN A 186      30.374   1.624  38.337  1.00 27.32           C  
ANISOU 1465  CA  ASN A 186     4234   2982   3164    225   -104    476       C  
ATOM   1466  C   ASN A 186      28.918   2.076  38.359  1.00 33.34           C  
ANISOU 1466  C   ASN A 186     4963   3790   3914    159    -61    481       C  
ATOM   1467  O   ASN A 186      28.470   2.591  39.361  1.00 36.55           O  
ANISOU 1467  O   ASN A 186     5363   4239   4284    162    -52    487       O  
ATOM   1468  CB  ASN A 186      31.247   2.878  38.233  1.00 27.22           C  
ANISOU 1468  CB  ASN A 186     4150   3008   3184    275   -139    437       C  
ATOM   1469  CG  ASN A 186      32.710   2.594  38.482  1.00 34.29           C  
ANISOU 1469  CG  ASN A 186     5063   3883   4082    345   -185    434       C  
ATOM   1470  OD1 ASN A 186      33.112   2.274  39.603  1.00 38.71           O  
ANISOU 1470  OD1 ASN A 186     5670   4438   4601    382   -204    452       O  
ATOM   1471  ND2 ASN A 186      33.526   2.712  37.433  1.00 37.54           N  
ANISOU 1471  ND2 ASN A 186     5434   4290   4540    368   -202    414       N  
ATOM   1472  N   ILE A 187      28.190   1.908  37.259  1.00 31.74           N  
ANISOU 1472  N   ILE A 187     4735   3585   3738    102    -37    479       N  
ATOM   1473  CA  ILE A 187      26.862   2.495  37.139  1.00 33.38           C  
ANISOU 1473  CA  ILE A 187     4890   3852   3941     47      0    480       C  
ATOM   1474  C   ILE A 187      25.848   1.881  38.133  1.00 38.07           C  
ANISOU 1474  C   ILE A 187     5525   4464   4475     -1     35    522       C  
ATOM   1475  O   ILE A 187      24.893   2.550  38.542  1.00 33.11           O  
ANISOU 1475  O   ILE A 187     4850   3904   3825    -20     63    525       O  
ATOM   1476  CB  ILE A 187      26.332   2.429  35.668  1.00 29.46           C  
ANISOU 1476  CB  ILE A 187     4355   3353   3486     -5     15    468       C  
ATOM   1477  CG1 ILE A 187      25.353   3.588  35.385  1.00 33.13           C  
ANISOU 1477  CG1 ILE A 187     4734   3894   3962    -25     37    452       C  
ATOM   1478  CG2 ILE A 187      25.719   1.082  35.362  1.00 29.31           C  
ANISOU 1478  CG2 ILE A 187     4397   3291   3448    -75     34    501       C  
ATOM   1479  CD1 ILE A 187      26.039   4.964  35.538  1.00 29.79           C  
ANISOU 1479  CD1 ILE A 187     4261   3497   3560     42     11    416       C  
ATOM   1480  N   ALA A 188      26.041   0.618  38.526  1.00 31.28           N  
ANISOU 1480  N   ALA A 188     4752   3546   3585    -17     33    557       N  
ATOM   1481  CA  ALA A 188      25.174   0.046  39.561  1.00 27.53           C  
ANISOU 1481  CA  ALA A 188     4321   3089   3050    -64     64    603       C  
ATOM   1482  C   ALA A 188      25.215   0.906  40.828  1.00 36.40           C  
ANISOU 1482  C   ALA A 188     5425   4271   4134    -12     66    600       C  
ATOM   1483  O   ALA A 188      24.261   0.913  41.615  1.00 36.88           O  
ANISOU 1483  O   ALA A 188     5483   4385   4145    -46    102    628       O  
ATOM   1484  CB  ALA A 188      25.542  -1.419  39.874  1.00 30.05           C  
ANISOU 1484  CB  ALA A 188     4753   3323   3339    -80     55    643       C  
ATOM   1485  N   ALA A 189      26.301   1.650  41.034  1.00 35.01           N  
ANISOU 1485  N   ALA A 189     5234   4092   3977     69     26    564       N  
ATOM   1486  CA  ALA A 189      26.396   2.479  42.241  1.00 32.04           C  
ANISOU 1486  CA  ALA A 189     4850   3765   3560    119     20    556       C  
ATOM   1487  C   ALA A 189      25.395   3.609  42.207  1.00 34.76           C  
ANISOU 1487  C   ALA A 189     5118   4189   3902    108     51    536       C  
ATOM   1488  O   ALA A 189      25.108   4.195  43.237  1.00 43.07           O  
ANISOU 1488  O   ALA A 189     6168   5289   4907    137     60    534       O  
ATOM   1489  CB  ALA A 189      27.791   3.053  42.430  1.00 30.42           C  
ANISOU 1489  CB  ALA A 189     4644   3539   3376    198    -35    522       C  
ATOM   1490  N   PHE A 190      24.904   3.960  41.025  1.00 33.91           N  
ANISOU 1490  N   PHE A 190     4949   4095   3842     74     64    518       N  
ATOM   1491  CA  PHE A 190      24.020   5.118  40.893  1.00 34.68           C  
ANISOU 1491  CA  PHE A 190     4971   4266   3941     77     88    496       C  
ATOM   1492  C   PHE A 190      22.597   4.638  40.655  1.00 33.77           C  
ANISOU 1492  C   PHE A 190     4828   4200   3805      1    141    530       C  
ATOM   1493  O   PHE A 190      21.722   5.442  40.428  1.00 41.03           O  
ANISOU 1493  O   PHE A 190     5679   5187   4723     -1    166    518       O  
ATOM   1494  CB  PHE A 190      24.424   6.034  39.715  1.00 33.59           C  
ANISOU 1494  CB  PHE A 190     4774   4120   3869     97     63    452       C  
ATOM   1495  CG  PHE A 190      25.806   6.596  39.810  1.00 31.39           C  
ANISOU 1495  CG  PHE A 190     4507   3802   3616    159     10    419       C  
ATOM   1496  CD1 PHE A 190      26.906   5.834  39.463  1.00 34.26           C  
ANISOU 1496  CD1 PHE A 190     4908   4104   4005    168    -22    423       C  
ATOM   1497  CD2 PHE A 190      26.014   7.900  40.232  1.00 33.24           C  
ANISOU 1497  CD2 PHE A 190     4718   4066   3848    210    -10    384       C  
ATOM   1498  CE1 PHE A 190      28.197   6.382  39.538  1.00 27.16           C  
ANISOU 1498  CE1 PHE A 190     4007   3183   3129    222    -72    395       C  
ATOM   1499  CE2 PHE A 190      27.279   8.441  40.317  1.00 26.12           C  
ANISOU 1499  CE2 PHE A 190     3824   3133   2969    255    -62    356       C  
ATOM   1500  CZ  PHE A 190      28.372   7.689  39.968  1.00 26.05           C  
ANISOU 1500  CZ  PHE A 190     3838   3074   2987    259    -93    363       C  
ATOM   1501  N   GLY A 191      22.373   3.328  40.683  1.00 33.79           N  
ANISOU 1501  N   GLY A 191     4882   4168   3788    -62    155    573       N  
ATOM   1502  CA  GLY A 191      21.059   2.767  40.405  1.00 27.00           C  
ANISOU 1502  CA  GLY A 191     3997   3352   2909   -150    201    610       C  
ATOM   1503  C   GLY A 191      20.900   2.331  38.961  1.00 36.11           C  
ANISOU 1503  C   GLY A 191     5132   4473   4116   -209    194    604       C  
ATOM   1504  O   GLY A 191      19.816   1.883  38.561  1.00 36.88           O  
ANISOU 1504  O   GLY A 191     5202   4608   4203   -292    225    632       O  
ATOM   1505  N   GLY A 192      21.971   2.455  38.164  1.00 31.99           N  
ANISOU 1505  N   GLY A 192     4622   3885   3647   -168    153    569       N  
ATOM   1506  CA  GLY A 192      21.923   2.008  36.782  1.00 35.16           C  
ANISOU 1506  CA  GLY A 192     5016   4251   4094   -216    145    561       C  
ATOM   1507  C   GLY A 192      22.145   0.504  36.598  1.00 38.83           C  
ANISOU 1507  C   GLY A 192     5572   4631   4549   -270    138    592       C  
ATOM   1508  O   GLY A 192      22.833  -0.123  37.388  1.00 41.18           O  
ANISOU 1508  O   GLY A 192     5949   4876   4821   -242    124    609       O  
ATOM   1509  N   ASP A 193      21.581  -0.059  35.533  1.00 36.52           N  
ANISOU 1509  N   ASP A 193     5277   4324   4276   -344    144    596       N  
ATOM   1510  CA  ASP A 193      21.658  -1.489  35.220  1.00 33.18           C  
ANISOU 1510  CA  ASP A 193     4949   3815   3843   -405    136    622       C  
ATOM   1511  C   ASP A 193      22.714  -1.760  34.148  1.00 34.20           C  
ANISOU 1511  C   ASP A 193     5113   3864   4016   -364    101    587       C  
ATOM   1512  O   ASP A 193      22.469  -1.541  32.971  1.00 32.34           O  
ANISOU 1512  O   ASP A 193     4834   3638   3815   -389     98    563       O  
ATOM   1513  CB  ASP A 193      20.291  -1.921  34.680  1.00 39.73           C  
ANISOU 1513  CB  ASP A 193     5751   4684   4660   -523    163    648       C  
ATOM   1514  CG  ASP A 193      20.172  -3.423  34.456  1.00 44.68           C  
ANISOU 1514  CG  ASP A 193     6487   5223   5268   -605    156    680       C  
ATOM   1515  OD1 ASP A 193      21.192  -4.148  34.545  1.00 42.97           O  
ANISOU 1515  OD1 ASP A 193     6370   4906   5051   -562    129    678       O  
ATOM   1516  OD2 ASP A 193      19.026  -3.872  34.200  1.00 47.46           O  
ANISOU 1516  OD2 ASP A 193     6824   5608   5601   -716    176    710       O  
ATOM   1517  N   PRO A 194      23.902  -2.241  34.548  1.00 36.73           N  
ANISOU 1517  N   PRO A 194     5510   4112   4334   -295     74    585       N  
ATOM   1518  CA  PRO A 194      24.948  -2.424  33.534  1.00 36.45           C  
ANISOU 1518  CA  PRO A 194     5496   4015   4338   -243     44    550       C  
ATOM   1519  C   PRO A 194      24.539  -3.477  32.484  1.00 43.79           C  
ANISOU 1519  C   PRO A 194     6484   4882   5270   -316     44    554       C  
ATOM   1520  O   PRO A 194      25.220  -3.607  31.447  1.00 35.83           O  
ANISOU 1520  O   PRO A 194     5488   3833   4293   -281     25    522       O  
ATOM   1521  CB  PRO A 194      26.136  -2.933  34.353  1.00 36.85           C  
ANISOU 1521  CB  PRO A 194     5625   4006   4371   -163     19    558       C  
ATOM   1522  CG  PRO A 194      25.478  -3.640  35.553  1.00 32.92           C  
ANISOU 1522  CG  PRO A 194     5194   3500   3816   -212     37    609       C  
ATOM   1523  CD  PRO A 194      24.340  -2.690  35.888  1.00 34.45           C  
ANISOU 1523  CD  PRO A 194     5291   3796   4001   -260     70    615       C  
ATOM   1524  N   MET A 195      23.475  -4.240  32.770  1.00 39.41           N  
ANISOU 1524  N   MET A 195     5973   4321   4681   -416     63    593       N  
ATOM   1525  CA  MET A 195      23.003  -5.258  31.821  1.00 42.15           C  
ANISOU 1525  CA  MET A 195     6383   4606   5025   -499     59    598       C  
ATOM   1526  C   MET A 195      21.949  -4.707  30.847  1.00 42.92           C  
ANISOU 1526  C   MET A 195     6388   4777   5144   -575     73    584       C  
ATOM   1527  O   MET A 195      21.484  -5.418  29.959  1.00 44.50           O  
ANISOU 1527  O   MET A 195     6627   4937   5342   -651     66    583       O  
ATOM   1528  CB  MET A 195      22.529  -6.551  32.539  1.00 42.00           C  
ANISOU 1528  CB  MET A 195     6481   4522   4955   -577     64    650       C  
ATOM   1529  CG  MET A 195      23.670  -7.293  33.295  1.00 39.34           C  
ANISOU 1529  CG  MET A 195     6259   4091   4596   -495     42    662       C  
ATOM   1530  SD  MET A 195      23.260  -8.978  33.795  1.00 64.99           S  
ANISOU 1530  SD  MET A 195     9677   7228   7788   -585     38    718       S  
ATOM   1531  CE  MET A 195      21.547  -8.715  34.245  1.00 49.80           C  
ANISOU 1531  CE  MET A 195     7675   5408   5837   -731     79    764       C  
ATOM   1532  N   SER A 196      21.603  -3.428  30.998  1.00 36.86           N  
ANISOU 1532  N   SER A 196     5500   4112   4393   -549     89    572       N  
ATOM   1533  CA  SER A 196      20.798  -2.745  29.994  1.00 33.42           C  
ANISOU 1533  CA  SER A 196     4969   3748   3982   -593     97    553       C  
ATOM   1534  C   SER A 196      21.384  -1.371  29.620  1.00 35.12           C  
ANISOU 1534  C   SER A 196     5093   4014   4238   -500     91    512       C  
ATOM   1535  O   SER A 196      21.039  -0.346  30.203  1.00 37.83           O  
ANISOU 1535  O   SER A 196     5357   4437   4580   -472    107    512       O  
ATOM   1536  CB  SER A 196      19.324  -2.647  30.437  1.00 33.96           C  
ANISOU 1536  CB  SER A 196     4978   3906   4020   -688    129    590       C  
ATOM   1537  OG  SER A 196      18.543  -1.949  29.465  1.00 36.37           O  
ANISOU 1537  OG  SER A 196     5184   4288   4347   -721    134    572       O  
ATOM   1538  N   VAL A 197      22.284  -1.367  28.644  1.00 38.79           N  
ANISOU 1538  N   VAL A 197     5573   4429   4735   -452     67    476       N  
ATOM   1539  CA  VAL A 197      22.983  -0.161  28.242  1.00 36.22           C  
ANISOU 1539  CA  VAL A 197     5174   4139   4449   -370     58    441       C  
ATOM   1540  C   VAL A 197      22.735   0.084  26.764  1.00 37.74           C  
ANISOU 1540  C   VAL A 197     5325   4344   4668   -395     52    415       C  
ATOM   1541  O   VAL A 197      23.053  -0.763  25.926  1.00 34.88           O  
ANISOU 1541  O   VAL A 197     5025   3919   4309   -411     39    404       O  
ATOM   1542  CB  VAL A 197      24.513  -0.268  28.471  1.00 44.47           C  
ANISOU 1542  CB  VAL A 197     6266   5125   5507   -275     35    425       C  
ATOM   1543  CG1 VAL A 197      25.258   0.948  27.815  1.00 38.79           C  
ANISOU 1543  CG1 VAL A 197     5468   4440   4829   -207     22    389       C  
ATOM   1544  CG2 VAL A 197      24.839  -0.387  29.982  1.00 32.52           C  
ANISOU 1544  CG2 VAL A 197     4789   3604   3964   -240     36    449       C  
ATOM   1545  N   THR A 198      22.148   1.238  26.450  1.00 33.04           N  
ANISOU 1545  N   THR A 198     4632   3831   4091   -394     61    405       N  
ATOM   1546  CA  THR A 198      21.852   1.607  25.070  1.00 30.82           C  
ANISOU 1546  CA  THR A 198     4304   3573   3832   -414     55    383       C  
ATOM   1547  C   THR A 198      22.766   2.786  24.721  1.00 30.53           C  
ANISOU 1547  C   THR A 198     4216   3553   3832   -329     44    355       C  
ATOM   1548  O   THR A 198      22.745   3.801  25.421  1.00 29.76           O  
ANISOU 1548  O   THR A 198     4066   3501   3739   -288     48    356       O  
ATOM   1549  CB  THR A 198      20.379   2.046  24.933  1.00 35.14           C  
ANISOU 1549  CB  THR A 198     4776   4209   4369   -481     72    399       C  
ATOM   1550  OG1 THR A 198      19.521   0.934  25.217  1.00 42.08           O  
ANISOU 1550  OG1 THR A 198     5697   5077   5212   -575     82    429       O  
ATOM   1551  CG2 THR A 198      20.079   2.574  23.533  1.00 31.40           C  
ANISOU 1551  CG2 THR A 198     4247   3767   3918   -493     63    376       C  
ATOM   1552  N   LEU A 199      23.562   2.656  23.662  1.00 29.73           N  
ANISOU 1552  N   LEU A 199     4130   3413   3751   -303     28    331       N  
ATOM   1553  CA  LEU A 199      24.339   3.781  23.148  1.00 33.47           C  
ANISOU 1553  CA  LEU A 199     4548   3909   4258   -239     19    309       C  
ATOM   1554  C   LEU A 199      23.465   4.685  22.249  1.00 39.09           C  
ANISOU 1554  C   LEU A 199     5185   4685   4983   -266     23    302       C  
ATOM   1555  O   LEU A 199      22.621   4.193  21.501  1.00 34.71           O  
ANISOU 1555  O   LEU A 199     4630   4140   4417   -328     26    305       O  
ATOM   1556  CB  LEU A 199      25.512   3.272  22.342  1.00 30.99           C  
ANISOU 1556  CB  LEU A 199     4276   3540   3957   -199      5    289       C  
ATOM   1557  CG  LEU A 199      26.472   2.269  23.007  1.00 33.32           C  
ANISOU 1557  CG  LEU A 199     4653   3769   4238   -160     -2    294       C  
ATOM   1558  CD1 LEU A 199      27.632   2.004  22.055  1.00 27.91           C  
ANISOU 1558  CD1 LEU A 199     3988   3052   3566   -107    -13    271       C  
ATOM   1559  CD2 LEU A 199      27.000   2.807  24.353  1.00 30.57           C  
ANISOU 1559  CD2 LEU A 199     4291   3434   3891   -111     -7    304       C  
ATOM   1560  N   PHE A 200      23.649   6.001  22.322  1.00 31.83           N  
ANISOU 1560  N   PHE A 200     4203   3806   4084   -221     19    295       N  
ATOM   1561  CA  PHE A 200      23.051   6.842  21.292  1.00 30.35           C  
ANISOU 1561  CA  PHE A 200     3955   3668   3911   -232     19    287       C  
ATOM   1562  C   PHE A 200      23.928   8.019  20.999  1.00 28.80           C  
ANISOU 1562  C   PHE A 200     3724   3476   3744   -173      6    273       C  
ATOM   1563  O   PHE A 200      24.629   8.481  21.882  1.00 29.43           O  
ANISOU 1563  O   PHE A 200     3809   3544   3830   -128     -1    272       O  
ATOM   1564  CB  PHE A 200      21.584   7.215  21.573  1.00 21.61           C  
ANISOU 1564  CB  PHE A 200     2797   2629   2785   -271     33    302       C  
ATOM   1565  CG  PHE A 200      21.338   8.196  22.726  1.00 30.97           C  
ANISOU 1565  CG  PHE A 200     3948   3853   3966   -228     40    309       C  
ATOM   1566  CD1 PHE A 200      21.895   8.010  23.983  1.00 31.44           C  
ANISOU 1566  CD1 PHE A 200     4044   3885   4015   -199     42    313       C  
ATOM   1567  CD2 PHE A 200      20.396   9.232  22.568  1.00 25.97           C  
ANISOU 1567  CD2 PHE A 200     3248   3289   3331   -218     46    311       C  
ATOM   1568  CE1 PHE A 200      21.590   8.894  25.048  1.00 29.15           C  
ANISOU 1568  CE1 PHE A 200     3729   3633   3713   -160     49    316       C  
ATOM   1569  CE2 PHE A 200      20.081  10.092  23.617  1.00 25.37           C  
ANISOU 1569  CE2 PHE A 200     3149   3249   3243   -174     55    313       C  
ATOM   1570  CZ  PHE A 200      20.701   9.937  24.867  1.00 21.55           C  
ANISOU 1570  CZ  PHE A 200     2706   2734   2749   -146     56    315       C  
ATOM   1571  N   GLY A 201      23.930   8.472  19.749  1.00 27.39           N  
ANISOU 1571  N   GLY A 201     3516   3311   3579   -176      0    264       N  
ATOM   1572  CA  GLY A 201      24.771   9.597  19.387  1.00 28.68           C  
ANISOU 1572  CA  GLY A 201     3649   3478   3769   -129    -12    255       C  
ATOM   1573  C   GLY A 201      24.290  10.155  18.076  1.00 31.82           C  
ANISOU 1573  C   GLY A 201     4009   3907   4173   -144    -15    252       C  
ATOM   1574  O   GLY A 201      23.506   9.541  17.359  1.00 28.86           O  
ANISOU 1574  O   GLY A 201     3637   3547   3783   -188     -9    253       O  
ATOM   1575  N   GLU A 202      24.777  11.334  17.755  1.00 26.36           N  
ANISOU 1575  N   GLU A 202     3288   3224   3502   -111    -25    251       N  
ATOM   1576  CA  GLU A 202      24.346  11.977  16.559  1.00 30.61           C  
ANISOU 1576  CA  GLU A 202     3794   3793   4044   -120    -29    252       C  
ATOM   1577  C   GLU A 202      25.528  12.375  15.697  1.00 26.74           C  
ANISOU 1577  C   GLU A 202     3302   3285   3573   -100    -37    249       C  
ATOM   1578  O   GLU A 202      26.583  12.735  16.196  1.00 31.90           O  
ANISOU 1578  O   GLU A 202     3960   3916   4242    -71    -45    248       O  
ATOM   1579  CB  GLU A 202      23.426  13.156  16.904  1.00 28.24           C  
ANISOU 1579  CB  GLU A 202     3455   3532   3744   -104    -33    259       C  
ATOM   1580  CG  GLU A 202      22.810  13.820  15.701  1.00 30.81           C  
ANISOU 1580  CG  GLU A 202     3747   3892   4069   -110    -38    264       C  
ATOM   1581  CD  GLU A 202      23.684  14.963  15.193  1.00 34.17           C  
ANISOU 1581  CD  GLU A 202     4167   4300   4516    -78    -53    266       C  
ATOM   1582  OE1 GLU A 202      24.663  15.310  15.884  1.00 30.69           O  
ANISOU 1582  OE1 GLU A 202     3744   3826   4091    -55    -60    264       O  
ATOM   1583  OE2 GLU A 202      23.341  15.550  14.152  1.00 31.70           O  
ANISOU 1583  OE2 GLU A 202     3835   4010   4202    -79    -59    273       O  
HETATM 1584  N   SGB A 203      25.331  12.280  14.388  1.00 27.26           N  
ANISOU 1584  N   SGB A 203     3359   3366   3633   -118    -35    248       N  
HETATM 1585  CA  SGB A 203      26.324  12.647  13.406  1.00 25.03           C  
ANISOU 1585  CA  SGB A 203     3071   3079   3361   -104    -38    248       C  
HETATM 1586  C   SGB A 203      27.577  11.812  13.659  1.00 30.53           C  
ANISOU 1586  C   SGB A 203     3796   3743   4060    -85    -33    240       C  
HETATM 1587  O   SGB A 203      27.511  10.583  13.664  1.00 32.38           O  
ANISOU 1587  O   SGB A 203     4068   3958   4278    -95    -24    229       O  
HETATM 1588  CB  SGB A 203      26.576  14.147  13.512  1.00 26.12           C  
ANISOU 1588  CB  SGB A 203     3180   3226   3519    -81    -51    260       C  
HETATM 1589  OG  SGB A 203      27.269  14.468  12.322  1.00 32.87           O  
ANISOU 1589  OG  SGB A 203     4025   4088   4378    -81    -51    266       O  
HETATM 1590  O1  SGB A 203      29.508  15.103  13.432  1.00 40.38           O  
ANISOU 1590  O1  SGB A 203     4971   5008   5364    -47    -65    274       O  
HETATM 1591  P1  SGB A 203      28.619  15.379  12.271  1.00 50.31           P  
ANISOU 1591  P1  SGB A 203     6220   6288   6609    -64    -60    279       P  
HETATM 1592  C1  SGB A 203      29.372  15.097  10.999  1.00 46.95           C  
ANISOU 1592  C1  SGB A 203     5786   5877   6175    -68    -48    283       C  
HETATM 1593  O2  SGB A 203      28.069  16.938  12.459  1.00 58.93           O  
ANISOU 1593  O2  SGB A 203     7299   7381   7712    -60    -80    293       O  
HETATM 1594  C2  SGB A 203      28.842  18.131  12.625  1.00 53.72           C  
ANISOU 1594  C2  SGB A 203     6634   6706   7072    -55    -98    308       C  
HETATM 1595  C4  SGB A 203      27.881  19.294  12.531  1.00 51.12           C  
ANISOU 1595  C4  SGB A 203     6308   6375   6740    -47   -113    317       C  
HETATM 1596  C3  SGB A 203      29.895  18.321  11.531  1.00 53.42           C  
ANISOU 1596  C3  SGB A 203     6581   6680   7038    -70    -93    324       C  
ATOM   1597  N   ALA A 204      28.707  12.454  13.911  1.00 18.31           N  
ANISOU 1597  N   ALA A 204     2233   2190   2532    -57    -39    246       N  
ATOM   1598  CA  ALA A 204      29.912  11.673  14.299  1.00 29.78           C  
ANISOU 1598  CA  ALA A 204     3706   3622   3986    -30    -36    240       C  
ATOM   1599  C   ALA A 204      29.757  10.812  15.564  1.00 29.97           C  
ANISOU 1599  C   ALA A 204     3767   3618   4003    -23    -36    234       C  
ATOM   1600  O   ALA A 204      30.420   9.768  15.701  1.00 30.22           O  
ANISOU 1600  O   ALA A 204     3831   3626   4023     -3    -31    227       O  
ATOM   1601  CB  ALA A 204      31.147  12.551  14.410  1.00 23.07           C  
ANISOU 1601  CB  ALA A 204     2825   2784   3159     -9    -47    251       C  
ATOM   1602  N   GLY A 205      28.909  11.245  16.495  1.00 24.50           N  
ANISOU 1602  N   GLY A 205     3071   2927   3311    -35    -42    238       N  
ATOM   1603  CA  GLY A 205      28.601  10.417  17.655  1.00 22.65           C  
ANISOU 1603  CA  GLY A 205     2873   2671   3063    -35    -40    237       C  
ATOM   1604  C   GLY A 205      27.895   9.137  17.178  1.00 30.75           C  
ANISOU 1604  C   GLY A 205     3938   3682   4064    -67    -26    231       C  
ATOM   1605  O   GLY A 205      28.225   8.025  17.641  1.00 33.84           O  
ANISOU 1605  O   GLY A 205     4379   4038   4442    -61    -23    228       O  
ATOM   1606  N   ALA A 206      26.942   9.284  16.244  1.00 22.38           N  
ANISOU 1606  N   ALA A 206     2860   2646   2996   -103    -21    231       N  
ATOM   1607  CA  ALA A 206      26.330   8.127  15.581  1.00 23.76           C  
ANISOU 1607  CA  ALA A 206     3072   2807   3147   -142    -14    223       C  
ATOM   1608  C   ALA A 206      27.373   7.234  14.843  1.00 29.99           C  
ANISOU 1608  C   ALA A 206     3906   3562   3929   -118    -11    209       C  
ATOM   1609  O   ALA A 206      27.329   6.011  14.990  1.00 31.93           O  
ANISOU 1609  O   ALA A 206     4212   3766   4153   -130     -8    202       O  
ATOM   1610  CB  ALA A 206      25.273   8.566  14.602  1.00 22.08           C  
ANISOU 1610  CB  ALA A 206     2826   2636   2928   -180    -15    225       C  
ATOM   1611  N   ALA A 207      28.242   7.813  14.005  1.00 20.78           N  
ANISOU 1611  N   ALA A 207     2711   2412   2774    -87    -11    206       N  
ATOM   1612  CA  ALA A 207      29.300   7.007  13.386  1.00 28.09           C  
ANISOU 1612  CA  ALA A 207     3672   3314   3687    -51     -4    192       C  
ATOM   1613  C   ALA A 207      30.035   6.229  14.485  1.00 34.69           C  
ANISOU 1613  C   ALA A 207     4549   4110   4522    -14     -5    192       C  
ATOM   1614  O   ALA A 207      30.363   5.035  14.320  1.00 33.54           O  
ANISOU 1614  O   ALA A 207     4467   3924   4354      3     -1    179       O  
ATOM   1615  CB  ALA A 207      30.311   7.866  12.618  1.00 22.63           C  
ANISOU 1615  CB  ALA A 207     2932   2657   3010    -17      0    196       C  
ATOM   1616  N   SER A 208      30.307   6.916  15.598  1.00 25.99           N  
ANISOU 1616  N   SER A 208     3417   3019   3440      1    -14    205       N  
ATOM   1617  CA  SER A 208      31.012   6.290  16.732  1.00 30.36           C  
ANISOU 1617  CA  SER A 208     4004   3541   3991     38    -19    208       C  
ATOM   1618  C   SER A 208      30.242   5.074  17.269  1.00 30.24           C  
ANISOU 1618  C   SER A 208     4062   3478   3950     11    -16    206       C  
ATOM   1619  O   SER A 208      30.820   4.026  17.508  1.00 30.72           O  
ANISOU 1619  O   SER A 208     4183   3497   3994     43    -16    202       O  
ATOM   1620  CB  SER A 208      31.275   7.296  17.866  1.00 21.33           C  
ANISOU 1620  CB  SER A 208     2818   2418   2868     50    -33    221       C  
ATOM   1621  OG  SER A 208      32.194   8.307  17.462  1.00 26.99           O  
ANISOU 1621  OG  SER A 208     3478   3171   3607     73    -40    224       O  
ATOM   1622  N   VAL A 209      28.942   5.233  17.455  1.00 29.12           N  
ANISOU 1622  N   VAL A 209     3916   3347   3803    -48    -14    213       N  
ATOM   1623  CA  VAL A 209      28.117   4.178  17.988  1.00 27.30           C  
ANISOU 1623  CA  VAL A 209     3747   3079   3547    -90    -11    218       C  
ATOM   1624  C   VAL A 209      28.252   3.035  17.014  1.00 32.60           C  
ANISOU 1624  C   VAL A 209     4484   3707   4196    -96    -10    202       C  
ATOM   1625  O   VAL A 209      28.436   1.878  17.420  1.00 32.68           O  
ANISOU 1625  O   VAL A 209     4574   3658   4184    -90    -12    201       O  
ATOM   1626  CB  VAL A 209      26.640   4.600  18.049  1.00 28.83           C  
ANISOU 1626  CB  VAL A 209     3907   3310   3736   -157     -7    229       C  
ATOM   1627  CG1 VAL A 209      25.737   3.380  18.172  1.00 23.77           C  
ANISOU 1627  CG1 VAL A 209     3330   2636   3066   -220     -4    234       C  
ATOM   1628  CG2 VAL A 209      26.414   5.544  19.214  1.00 25.27           C  
ANISOU 1628  CG2 VAL A 209     3411   2893   3298   -145     -7    243       C  
ATOM   1629  N   GLY A 210      28.209   3.379  15.726  1.00 28.30           N  
ANISOU 1629  N   GLY A 210     3912   3187   3653   -102     -7    188       N  
ATOM   1630  CA  GLY A 210      28.374   2.418  14.654  1.00 26.95           C  
ANISOU 1630  CA  GLY A 210     3803   2980   3457   -102     -6    167       C  
ATOM   1631  C   GLY A 210      29.655   1.633  14.759  1.00 32.13           C  
ANISOU 1631  C   GLY A 210     4514   3591   4103    -27     -4    156       C  
ATOM   1632  O   GLY A 210      29.685   0.422  14.509  1.00 33.61           O  
ANISOU 1632  O   GLY A 210     4792   3717   4260    -25     -6    142       O  
ATOM   1633  N   MET A 211      30.733   2.306  15.145  1.00 27.63           N  
ANISOU 1633  N   MET A 211     3893   3051   3556     37     -2    163       N  
ATOM   1634  CA  MET A 211      32.012   1.622  15.197  1.00 28.48           C  
ANISOU 1634  CA  MET A 211     4038   3132   3652    118     -1    154       C  
ATOM   1635  C   MET A 211      32.145   0.698  16.381  1.00 27.52           C  
ANISOU 1635  C   MET A 211     3988   2953   3517    137     -9    163       C  
ATOM   1636  O   MET A 211      32.863  -0.278  16.307  1.00 27.26           O  
ANISOU 1636  O   MET A 211     4022   2875   3461    196     -9    152       O  
ATOM   1637  CB  MET A 211      33.169   2.631  15.143  1.00 28.84           C  
ANISOU 1637  CB  MET A 211     3996   3238   3722    174      2    161       C  
ATOM   1638  CG  MET A 211      33.446   2.931  13.654  1.00 35.84           C  
ANISOU 1638  CG  MET A 211     4853   4161   4602    184     16    148       C  
ATOM   1639  SD  MET A 211      34.231   4.461  13.507  1.00 45.47           S  
ANISOU 1639  SD  MET A 211     5959   5461   5857    199     17    166       S  
ATOM   1640  CE  MET A 211      33.596   4.961  11.906  1.00 40.93           C  
ANISOU 1640  CE  MET A 211     5360   4918   5273    156     30    158       C  
ATOM   1641  N   HIS A 212      31.439   1.016  17.464  1.00 26.75           N  
ANISOU 1641  N   HIS A 212     3877   2857   3428     93    -15    183       N  
ATOM   1642  CA  HIS A 212      31.363   0.132  18.600  1.00 28.38           C  
ANISOU 1642  CA  HIS A 212     4157   3009   3618     96    -23    196       C  
ATOM   1643  C   HIS A 212      30.593  -1.132  18.266  1.00 33.38           C  
ANISOU 1643  C   HIS A 212     4893   3571   4217     48    -23    189       C  
ATOM   1644  O   HIS A 212      30.986  -2.218  18.705  1.00 31.79           O  
ANISOU 1644  O   HIS A 212     4785   3302   3992     81    -29    190       O  
ATOM   1645  CB  HIS A 212      30.775   0.831  19.816  1.00 27.75           C  
ANISOU 1645  CB  HIS A 212     4036   2957   3551     60    -26    219       C  
ATOM   1646  CG  HIS A 212      31.674   1.889  20.361  1.00 29.14           C  
ANISOU 1646  CG  HIS A 212     4135   3184   3754    113    -34    224       C  
ATOM   1647  ND1 HIS A 212      32.914   1.601  20.890  1.00 28.04           N  
ANISOU 1647  ND1 HIS A 212     4008   3035   3612    190    -44    226       N  
ATOM   1648  CD2 HIS A 212      31.536   3.234  20.431  1.00 27.18           C  
ANISOU 1648  CD2 HIS A 212     3801   2995   3532     98    -35    228       C  
ATOM   1649  CE1 HIS A 212      33.501   2.725  21.266  1.00 33.30           C  
ANISOU 1649  CE1 HIS A 212     4594   3755   4303    212    -53    231       C  
ATOM   1650  NE2 HIS A 212      32.685   3.731  20.998  1.00 30.63           N  
ANISOU 1650  NE2 HIS A 212     4201   3454   3982    157    -48    232       N  
ATOM   1651  N   ILE A 213      29.521  -0.993  17.485  1.00 32.49           N  
ANISOU 1651  N   ILE A 213     4769   3473   4102    -30    -20    183       N  
ATOM   1652  CA  ILE A 213      28.813  -2.160  16.962  1.00 32.74           C  
ANISOU 1652  CA  ILE A 213     4899   3441   4101    -86    -25    173       C  
ATOM   1653  C   ILE A 213      29.776  -3.064  16.176  1.00 41.35           C  
ANISOU 1653  C   ILE A 213     6070   4473   5167    -15    -27    145       C  
ATOM   1654  O   ILE A 213      29.667  -4.268  16.236  1.00 41.67           O  
ANISOU 1654  O   ILE A 213     6225   4432   5176    -23    -36    139       O  
ATOM   1655  CB  ILE A 213      27.644  -1.753  16.044  1.00 28.41           C  
ANISOU 1655  CB  ILE A 213     4309   2932   3552   -173    -25    166       C  
ATOM   1656  CG1 ILE A 213      26.597  -0.943  16.838  1.00 28.82           C  
ANISOU 1656  CG1 ILE A 213     4286   3043   3621   -238    -21    194       C  
ATOM   1657  CG2 ILE A 213      27.026  -3.006  15.324  1.00 30.94           C  
ANISOU 1657  CG2 ILE A 213     4739   3183   3835   -234    -36    150       C  
ATOM   1658  CD1 ILE A 213      25.401  -0.521  16.003  1.00 24.83           C  
ANISOU 1658  CD1 ILE A 213     3732   2588   3115   -319    -23    192       C  
ATOM   1659  N   LEU A 214      30.732  -2.483  15.457  1.00 38.58           N  
ANISOU 1659  N   LEU A 214     5663   4167   4828     59    -18    129       N  
ATOM   1660  CA  LEU A 214      31.551  -3.258  14.528  1.00 35.54           C  
ANISOU 1660  CA  LEU A 214     5344   3744   4416    129    -15    100       C  
ATOM   1661  C   LEU A 214      32.891  -3.668  15.127  1.00 40.48           C  
ANISOU 1661  C   LEU A 214     5994   4350   5036    242    -14    101       C  
ATOM   1662  O   LEU A 214      33.711  -4.302  14.458  1.00 38.20           O  
ANISOU 1662  O   LEU A 214     5755   4037   4722    321     -9     78       O  
ATOM   1663  CB  LEU A 214      31.825  -2.438  13.261  1.00 29.15           C  
ANISOU 1663  CB  LEU A 214     4457   3004   3615    145     -2     83       C  
ATOM   1664  CG  LEU A 214      30.576  -2.022  12.513  1.00 39.38           C  
ANISOU 1664  CG  LEU A 214     5727   4326   4912     46     -6     79       C  
ATOM   1665  CD1 LEU A 214      30.911  -1.081  11.352  1.00 33.91           C  
ANISOU 1665  CD1 LEU A 214     4950   3705   4227     67      7     69       C  
ATOM   1666  CD2 LEU A 214      29.803  -3.291  12.045  1.00 31.66           C  
ANISOU 1666  CD2 LEU A 214     4871   3265   3891    -10    -20     59       C  
ATOM   1667  N   SER A 215      33.136  -3.252  16.358  1.00 40.55           N  
ANISOU 1667  N   SER A 215     5961   4379   5067    254    -19    128       N  
ATOM   1668  CA  SER A 215      34.378  -3.576  17.014  1.00 34.17           C  
ANISOU 1668  CA  SER A 215     5165   3563   4254    359    -23    134       C  
ATOM   1669  C   SER A 215      34.129  -4.482  18.205  1.00 37.00           C  
ANISOU 1669  C   SER A 215     5619   3846   4593    353    -38    153       C  
ATOM   1670  O   SER A 215      33.552  -4.064  19.214  1.00 34.30           O  
ANISOU 1670  O   SER A 215     5249   3516   4266    298    -43    178       O  
ATOM   1671  CB  SER A 215      35.097  -2.305  17.457  1.00 34.32           C  
ANISOU 1671  CB  SER A 215     5054   3674   4310    390    -21    150       C  
ATOM   1672  OG  SER A 215      36.415  -2.647  17.887  1.00 40.14           O  
ANISOU 1672  OG  SER A 215     5794   4417   5038    498    -26    153       O  
ATOM   1673  N   LEU A 216      34.611  -5.718  18.094  1.00 39.51           N  
ANISOU 1673  N   LEU A 216     6054   4085   4875    416    -43    140       N  
ATOM   1674  CA  LEU A 216      34.269  -6.783  19.023  1.00 38.35           C  
ANISOU 1674  CA  LEU A 216     6028   3844   4701    402    -58    157       C  
ATOM   1675  C   LEU A 216      34.435  -6.431  20.480  1.00 37.05           C  
ANISOU 1675  C   LEU A 216     5828   3700   4550    410    -67    192       C  
ATOM   1676  O   LEU A 216      33.556  -6.684  21.279  1.00 39.98           O  
ANISOU 1676  O   LEU A 216     6242   4035   4914    333    -73    216       O  
ATOM   1677  CB  LEU A 216      35.089  -8.052  18.704  1.00 53.34           C  
ANISOU 1677  CB  LEU A 216     8052   5658   6557    505    -65    138       C  
ATOM   1678  CG  LEU A 216      34.693  -8.640  17.346  1.00 68.24           C  
ANISOU 1678  CG  LEU A 216    10013   7498   8418    481    -61    101       C  
ATOM   1679  CD1 LEU A 216      35.441  -9.940  17.001  1.00 66.18           C  
ANISOU 1679  CD1 LEU A 216     9893   7142   8108    587    -68     77       C  
ATOM   1680  CD2 LEU A 216      33.172  -8.855  17.313  1.00 75.30           C  
ANISOU 1680  CD2 LEU A 216    10955   8347   9308    331    -68    109       C  
ATOM   1681  N   PRO A 217      35.594  -5.874  20.854  1.00 38.41           N  
ANISOU 1681  N   PRO A 217     5923   3935   4738    503    -70    196       N  
ATOM   1682  CA  PRO A 217      35.754  -5.618  22.290  1.00 32.33           C  
ANISOU 1682  CA  PRO A 217     5132   3178   3974    511    -83    228       C  
ATOM   1683  C   PRO A 217      34.761  -4.599  22.842  1.00 34.70           C  
ANISOU 1683  C   PRO A 217     5354   3529   4300    409    -79    245       C  
ATOM   1684  O   PRO A 217      34.655  -4.498  24.055  1.00 40.81           O  
ANISOU 1684  O   PRO A 217     6131   4304   5071    401    -88    271       O  
ATOM   1685  CB  PRO A 217      37.175  -5.061  22.383  1.00 32.76           C  
ANISOU 1685  CB  PRO A 217     5099   3307   4043    620    -89    225       C  
ATOM   1686  CG  PRO A 217      37.865  -5.607  21.161  1.00 33.10           C  
ANISOU 1686  CG  PRO A 217     5169   3338   4069    696    -78    196       C  
ATOM   1687  CD  PRO A 217      36.818  -5.572  20.092  1.00 27.10           C  
ANISOU 1687  CD  PRO A 217     4427   2558   3311    605    -63    176       C  
ATOM   1688  N   SER A 218      34.080  -3.833  21.995  1.00 35.38           N  
ANISOU 1688  N   SER A 218     5372   3660   4409    340    -65    232       N  
ATOM   1689  CA  SER A 218      33.053  -2.911  22.512  1.00 37.48           C  
ANISOU 1689  CA  SER A 218     5573   3973   4696    251    -60    248       C  
ATOM   1690  C   SER A 218      31.741  -3.637  22.701  1.00 41.63           C  
ANISOU 1690  C   SER A 218     6176   4443   5198    155    -56    261       C  
ATOM   1691  O   SER A 218      30.897  -3.217  23.486  1.00 39.17           O  
ANISOU 1691  O   SER A 218     5837   4157   4889     91    -52    283       O  
ATOM   1692  CB  SER A 218      32.847  -1.730  21.582  1.00 30.99           C  
ANISOU 1692  CB  SER A 218     4643   3225   3906    221    -50    233       C  
ATOM   1693  OG  SER A 218      34.010  -0.929  21.609  1.00 36.12           O  
ANISOU 1693  OG  SER A 218     5212   3934   4578    293    -55    229       O  
ATOM   1694  N   ARG A 219      31.591  -4.760  22.002  1.00 46.21           N  
ANISOU 1694  N   ARG A 219     6859   4949   5752    146    -57    248       N  
ATOM   1695  CA  ARG A 219      30.289  -5.409  21.917  1.00 50.66           C  
ANISOU 1695  CA  ARG A 219     7490   5465   6294     37    -55    258       C  
ATOM   1696  C   ARG A 219      29.732  -5.878  23.251  1.00 45.36           C  
ANISOU 1696  C   ARG A 219     6872   4760   5602     -9    -58    296       C  
ATOM   1697  O   ARG A 219      28.528  -5.837  23.456  1.00 47.08           O  
ANISOU 1697  O   ARG A 219     7083   4992   5815   -113    -50    314       O  
ATOM   1698  CB  ARG A 219      30.326  -6.534  20.900  1.00 55.16           C  
ANISOU 1698  CB  ARG A 219     8169   5952   6836     38    -62    234       C  
ATOM   1699  CG  ARG A 219      30.486  -5.987  19.487  1.00 56.60           C  
ANISOU 1699  CG  ARG A 219     8291   6181   7034     50    -55    199       C  
ATOM   1700  CD  ARG A 219      29.334  -5.040  19.168  1.00 60.25           C  
ANISOU 1700  CD  ARG A 219     8657   6717   7518    -50    -46    204       C  
ATOM   1701  NE  ARG A 219      28.037  -5.675  19.404  1.00 57.33           N  
ANISOU 1701  NE  ARG A 219     8347   6309   7127   -167    -51    222       N  
ATOM   1702  CZ  ARG A 219      27.349  -6.336  18.485  1.00 63.32           C  
ANISOU 1702  CZ  ARG A 219     9167   7027   7864   -236    -59    206       C  
ATOM   1703  NH1 ARG A 219      27.818  -6.444  17.251  1.00 63.59           N  
ANISOU 1703  NH1 ARG A 219     9218   7052   7893   -195    -61    169       N  
ATOM   1704  NH2 ARG A 219      26.186  -6.890  18.802  1.00 73.83           N  
ANISOU 1704  NH2 ARG A 219    10545   8332   9176   -350    -65    227       N  
ATOM   1705  N   SER A 220      30.610  -6.289  24.156  1.00 38.87           N  
ANISOU 1705  N   SER A 220     6098   3905   4767     71    -68    310       N  
ATOM   1706  CA  SER A 220      30.191  -6.733  25.472  1.00 42.73           C  
ANISOU 1706  CA  SER A 220     6641   4362   5231     37    -71    349       C  
ATOM   1707  C   SER A 220      29.844  -5.596  26.419  1.00 44.01           C  
ANISOU 1707  C   SER A 220     6697   4613   5410     16    -61    368       C  
ATOM   1708  O   SER A 220      29.556  -5.849  27.583  1.00 49.74           O  
ANISOU 1708  O   SER A 220     7459   5328   6114     -4    -61    401       O  
ATOM   1709  CB  SER A 220      31.282  -7.603  26.121  1.00 54.84           C  
ANISOU 1709  CB  SER A 220     8271   5827   6739    138    -89    358       C  
ATOM   1710  OG  SER A 220      32.496  -6.892  26.326  1.00 58.80           O  
ANISOU 1710  OG  SER A 220     8694   6387   7262    247    -96    347       O  
ATOM   1711  N   LEU A 221      29.849  -4.353  25.936  1.00 38.68           N  
ANISOU 1711  N   LEU A 221     5900   4024   4772     19    -54    349       N  
ATOM   1712  CA  LEU A 221      29.715  -3.205  26.833  1.00 32.15           C  
ANISOU 1712  CA  LEU A 221     4979   3275   3960     20    -49    361       C  
ATOM   1713  C   LEU A 221      28.399  -2.482  26.636  1.00 32.64           C  
ANISOU 1713  C   LEU A 221     4972   3398   4032    -72    -31    365       C  
ATOM   1714  O   LEU A 221      28.146  -1.439  27.276  1.00 32.02           O  
ANISOU 1714  O   LEU A 221     4815   3387   3964    -73    -25    371       O  
ATOM   1715  CB  LEU A 221      30.873  -2.203  26.636  1.00 33.27           C  
ANISOU 1715  CB  LEU A 221     5035   3472   4135    107    -60    339       C  
ATOM   1716  CG  LEU A 221      32.319  -2.727  26.697  1.00 42.26           C  
ANISOU 1716  CG  LEU A 221     6211   4578   5268    213    -80    332       C  
ATOM   1717  CD1 LEU A 221      33.336  -1.646  26.262  1.00 38.59           C  
ANISOU 1717  CD1 LEU A 221     5643   4183   4838    275    -88    311       C  
ATOM   1718  CD2 LEU A 221      32.681  -3.325  28.095  1.00 39.58           C  
ANISOU 1718  CD2 LEU A 221     5938   4203   4897    251    -94    360       C  
ATOM   1719  N   PHE A 222      27.581  -2.988  25.720  1.00 30.67           N  
ANISOU 1719  N   PHE A 222     4749   3127   3777   -145    -23    360       N  
ATOM   1720  CA  PHE A 222      26.257  -2.387  25.516  1.00 39.64           C  
ANISOU 1720  CA  PHE A 222     5816   4327   4917   -235     -7    367       C  
ATOM   1721  C   PHE A 222      25.334  -3.389  24.844  1.00 37.15           C  
ANISOU 1721  C   PHE A 222     5566   3968   4580   -329     -5    373       C  
ATOM   1722  O   PHE A 222      25.798  -4.362  24.285  1.00 40.04           O  
ANISOU 1722  O   PHE A 222     6024   4255   4934   -317    -18    361       O  
ATOM   1723  CB  PHE A 222      26.341  -1.085  24.686  1.00 27.74           C  
ANISOU 1723  CB  PHE A 222     4198   2893   3448   -212     -5    341       C  
ATOM   1724  CG  PHE A 222      26.776  -1.301  23.260  1.00 30.33           C  
ANISOU 1724  CG  PHE A 222     4536   3197   3789   -196    -12    311       C  
ATOM   1725  CD1 PHE A 222      28.125  -1.467  22.943  1.00 32.97           C  
ANISOU 1725  CD1 PHE A 222     4895   3501   4133   -107    -23    292       C  
ATOM   1726  CD2 PHE A 222      25.849  -1.340  22.234  1.00 32.05           C  
ANISOU 1726  CD2 PHE A 222     4739   3433   4007   -269     -8    302       C  
ATOM   1727  CE1 PHE A 222      28.538  -1.678  21.614  1.00 35.94           C  
ANISOU 1727  CE1 PHE A 222     5280   3860   4515    -87    -26    264       C  
ATOM   1728  CE2 PHE A 222      26.254  -1.568  20.900  1.00 35.93           C  
ANISOU 1728  CE2 PHE A 222     5247   3902   4504   -252    -15    273       C  
ATOM   1729  CZ  PHE A 222      27.590  -1.732  20.593  1.00 33.51           C  
ANISOU 1729  CZ  PHE A 222     4966   3563   4204   -161    -22    253       C  
ATOM   1730  N   HIS A 223      24.035  -3.129  24.867  1.00 37.39           N  
ANISOU 1730  N   HIS A 223     5549   4054   4604   -421      9    390       N  
ATOM   1731  CA  HIS A 223      23.060  -4.089  24.350  1.00 41.30           C  
ANISOU 1731  CA  HIS A 223     6103   4516   5075   -529      7    401       C  
ATOM   1732  C   HIS A 223      22.255  -3.574  23.169  1.00 43.77           C  
ANISOU 1732  C   HIS A 223     6341   4887   5402   -586      7    383       C  
ATOM   1733  O   HIS A 223      21.752  -4.358  22.385  1.00 51.62           O  
ANISOU 1733  O   HIS A 223     7389   5844   6381   -658     -4    377       O  
ATOM   1734  CB  HIS A 223      22.166  -4.528  25.502  1.00 37.28           C  
ANISOU 1734  CB  HIS A 223     5615   4017   4532   -606     21    447       C  
ATOM   1735  CG  HIS A 223      22.945  -4.707  26.766  1.00 44.73           C  
ANISOU 1735  CG  HIS A 223     6606   4926   5462   -538     22    466       C  
ATOM   1736  ND1 HIS A 223      23.576  -5.895  27.091  1.00 44.86           N  
ANISOU 1736  ND1 HIS A 223     6754   4836   5454   -519      7    477       N  
ATOM   1737  CD2 HIS A 223      23.299  -3.815  27.723  1.00 35.27           C  
ANISOU 1737  CD2 HIS A 223     5346   3783   4272   -472     32    472       C  
ATOM   1738  CE1 HIS A 223      24.242  -5.737  28.221  1.00 41.05           C  
ANISOU 1738  CE1 HIS A 223     6282   4351   4964   -448      9    492       C  
ATOM   1739  NE2 HIS A 223      24.089  -4.486  28.621  1.00 43.51           N  
ANISOU 1739  NE2 HIS A 223     6478   4760   5294   -422     23    489       N  
ATOM   1740  N   ARG A 224      22.165  -2.262  23.020  1.00 41.44           N  
ANISOU 1740  N   ARG A 224     5930   4681   5135   -550     17    372       N  
ATOM   1741  CA  ARG A 224      21.312  -1.675  21.987  1.00 42.33           C  
ANISOU 1741  CA  ARG A 224     5964   4860   5258   -599     17    360       C  
ATOM   1742  C   ARG A 224      21.959  -0.369  21.540  1.00 40.16           C  
ANISOU 1742  C   ARG A 224     5603   4635   5020   -513     17    335       C  
ATOM   1743  O   ARG A 224      22.774   0.174  22.274  1.00 38.37           O  
ANISOU 1743  O   ARG A 224     5362   4409   4807   -436     20    334       O  
ATOM   1744  CB  ARG A 224      19.922  -1.386  22.568  1.00 39.09           C  
ANISOU 1744  CB  ARG A 224     5487   4534   4833   -681     34    393       C  
ATOM   1745  CG  ARG A 224      18.973  -2.535  22.441  1.00 49.03           C  
ANISOU 1745  CG  ARG A 224     6803   5768   6058   -801     30    415       C  
ATOM   1746  CD  ARG A 224      17.701  -2.351  23.267  1.00 47.55           C  
ANISOU 1746  CD  ARG A 224     6550   5669   5848   -878     52    456       C  
ATOM   1747  NE  ARG A 224      18.041  -2.212  24.661  1.00 58.27           N  
ANISOU 1747  NE  ARG A 224     7917   7026   7195   -831     71    480       N  
ATOM   1748  CZ  ARG A 224      18.259  -3.229  25.489  1.00 62.62           C  
ANISOU 1748  CZ  ARG A 224     8568   7506   7719   -857     72    506       C  
ATOM   1749  NH1 ARG A 224      18.158  -4.473  25.058  1.00 60.30           N  
ANISOU 1749  NH1 ARG A 224     8377   7129   7406   -932     54    512       N  
ATOM   1750  NH2 ARG A 224      18.593  -2.991  26.754  1.00 64.99           N  
ANISOU 1750  NH2 ARG A 224     8870   7814   8008   -805     88    526       N  
ATOM   1751  N   ALA A 225      21.564   0.153  20.380  1.00 37.05           N  
ANISOU 1751  N   ALA A 225     5154   4284   4639   -531     13    317       N  
ATOM   1752  CA  ALA A 225      22.197   1.342  19.829  1.00 32.65           C  
ANISOU 1752  CA  ALA A 225     4527   3765   4114   -457     11    295       C  
ATOM   1753  C   ALA A 225      21.248   2.228  19.014  1.00 32.60           C  
ANISOU 1753  C   ALA A 225     4432   3839   4115   -490     12    292       C  
ATOM   1754  O   ALA A 225      20.412   1.733  18.267  1.00 32.57           O  
ANISOU 1754  O   ALA A 225     4434   3847   4095   -563      5    292       O  
ATOM   1755  CB  ALA A 225      23.365   0.925  18.961  1.00 28.44           C  
ANISOU 1755  CB  ALA A 225     4049   3170   3588   -404     -1    267       C  
ATOM   1756  N   VAL A 226      21.416   3.539  19.147  1.00 28.00           N  
ANISOU 1756  N   VAL A 226     3772   3310   3556   -434     16    290       N  
ATOM   1757  CA  VAL A 226      20.661   4.491  18.368  1.00 30.33           C  
ANISOU 1757  CA  VAL A 226     3987   3678   3860   -445     15    287       C  
ATOM   1758  C   VAL A 226      21.603   5.343  17.521  1.00 34.72           C  
ANISOU 1758  C   VAL A 226     4520   4230   4443   -379      6    266       C  
ATOM   1759  O   VAL A 226      22.533   5.979  18.065  1.00 36.65           O  
ANISOU 1759  O   VAL A 226     4757   4461   4707   -313      6    263       O  
ATOM   1760  CB  VAL A 226      19.857   5.406  19.283  1.00 30.64           C  
ANISOU 1760  CB  VAL A 226     3955   3789   3898   -437     28    306       C  
ATOM   1761  CG1 VAL A 226      19.010   6.372  18.414  1.00 35.44           C  
ANISOU 1761  CG1 VAL A 226     4482   4474   4511   -442     24    305       C  
ATOM   1762  CG2 VAL A 226      18.987   4.567  20.228  1.00 27.46           C  
ANISOU 1762  CG2 VAL A 226     3570   3398   3464   -501     42    333       C  
ATOM   1763  N   LEU A 227      21.400   5.356  16.204  1.00 31.96           N  
ANISOU 1763  N   LEU A 227     4160   3893   4092   -400     -3    254       N  
ATOM   1764  CA  LEU A 227      22.280   6.154  15.327  1.00 34.09           C  
ANISOU 1764  CA  LEU A 227     4408   4163   4383   -344     -9    238       C  
ATOM   1765  C   LEU A 227      21.471   7.279  14.719  1.00 33.15           C  
ANISOU 1765  C   LEU A 227     4213   4114   4270   -348    -13    244       C  
ATOM   1766  O   LEU A 227      20.626   7.051  13.849  1.00 28.49           O  
ANISOU 1766  O   LEU A 227     3609   3554   3662   -397    -20    243       O  
ATOM   1767  CB  LEU A 227      22.929   5.319  14.210  1.00 29.69           C  
ANISOU 1767  CB  LEU A 227     3907   3559   3814   -347    -15    217       C  
ATOM   1768  CG  LEU A 227      24.006   4.303  14.676  1.00 34.28           C  
ANISOU 1768  CG  LEU A 227     4568   4066   4392   -315    -13    208       C  
ATOM   1769  CD1 LEU A 227      23.363   3.058  15.310  1.00 25.39           C  
ANISOU 1769  CD1 LEU A 227     3508   2900   3239   -374    -14    216       C  
ATOM   1770  CD2 LEU A 227      24.952   3.900  13.575  1.00 27.90           C  
ANISOU 1770  CD2 LEU A 227     3799   3226   3578   -281    -15    185       C  
ATOM   1771  N   GLN A 228      21.742   8.498  15.165  1.00 28.88           N  
ANISOU 1771  N   GLN A 228     3628   3596   3750   -296    -12    250       N  
ATOM   1772  CA  GLN A 228      21.017   9.676  14.653  1.00 26.82           C  
ANISOU 1772  CA  GLN A 228     3302   3396   3494   -285    -17    257       C  
ATOM   1773  C   GLN A 228      21.835  10.423  13.597  1.00 31.29           C  
ANISOU 1773  C   GLN A 228     3858   3953   4075   -249    -26    250       C  
ATOM   1774  O   GLN A 228      22.940  10.930  13.890  1.00 30.96           O  
ANISOU 1774  O   GLN A 228     3826   3882   4056   -204    -26    247       O  
ATOM   1775  CB  GLN A 228      20.626  10.596  15.802  1.00 21.33           C  
ANISOU 1775  CB  GLN A 228     2569   2730   2804   -251    -11    269       C  
ATOM   1776  CG  GLN A 228      19.819   9.895  16.901  1.00 22.09           C  
ANISOU 1776  CG  GLN A 228     2670   2845   2880   -286      2    280       C  
ATOM   1777  CD  GLN A 228      19.585  10.746  18.144  1.00 29.12           C  
ANISOU 1777  CD  GLN A 228     3534   3760   3770   -241     11    288       C  
ATOM   1778  OE1 GLN A 228      19.420  10.210  19.237  1.00 28.91           O  
ANISOU 1778  OE1 GLN A 228     3526   3730   3729   -252     24    297       O  
ATOM   1779  NE2 GLN A 228      19.627  12.079  17.990  1.00 28.42           N  
ANISOU 1779  NE2 GLN A 228     3412   3692   3695   -187      3    286       N  
ATOM   1780  N   SER A 229      21.331  10.442  12.355  1.00 26.51           N  
ANISOU 1780  N   SER A 229     3238   3377   3458   -274    -34    248       N  
ATOM   1781  CA  SER A 229      22.016  11.143  11.276  1.00 21.54           C  
ANISOU 1781  CA  SER A 229     2600   2747   2838   -246    -40    245       C  
ATOM   1782  C   SER A 229      23.549  10.858  11.196  1.00 23.32           C  
ANISOU 1782  C   SER A 229     2864   2920   3076   -214    -34    235       C  
ATOM   1783  O   SER A 229      24.327  11.785  11.081  1.00 22.10           O  
ANISOU 1783  O   SER A 229     2692   2763   2940   -177    -35    242       O  
ATOM   1784  CB  SER A 229      21.877  12.649  11.459  1.00 22.68           C  
ANISOU 1784  CB  SER A 229     2700   2919   3000   -204    -46    259       C  
ATOM   1785  OG  SER A 229      20.536  13.050  11.613  1.00 30.34           O  
ANISOU 1785  OG  SER A 229     3627   3943   3956   -214    -51    270       O  
ATOM   1786  N   GLY A 230      23.955   9.604  11.191  1.00 24.74           N  
ANISOU 1786  N   GLY A 230     3095   3062   3243   -229    -28    221       N  
ATOM   1787  CA  GLY A 230      25.353   9.252  11.092  1.00 26.93           C  
ANISOU 1787  CA  GLY A 230     3404   3301   3528   -191    -20    211       C  
ATOM   1788  C   GLY A 230      25.512   7.737  11.080  1.00 28.70           C  
ANISOU 1788  C   GLY A 230     3696   3481   3729   -207    -16    194       C  
ATOM   1789  O   GLY A 230      24.675   7.018  11.638  1.00 32.74           O  
ANISOU 1789  O   GLY A 230     4233   3980   4227   -249    -19    194       O  
ATOM   1790  N   THR A 231      26.594   7.267  10.464  1.00 24.64           N  
ANISOU 1790  N   THR A 231     3212   2942   3207   -173     -9    181       N  
ATOM   1791  CA  THR A 231      26.819   5.833  10.237  1.00 34.92           C  
ANISOU 1791  CA  THR A 231     4592   4194   4481   -177     -6    160       C  
ATOM   1792  C   THR A 231      28.311   5.596  10.188  1.00 30.77           C  
ANISOU 1792  C   THR A 231     4083   3648   3958   -108      5    152       C  
ATOM   1793  O   THR A 231      29.037   6.494   9.831  1.00 28.77           O  
ANISOU 1793  O   THR A 231     3780   3430   3722    -74     11    161       O  
ATOM   1794  CB  THR A 231      26.209   5.355   8.869  1.00 30.81           C  
ANISOU 1794  CB  THR A 231     4098   3680   3927   -214    -12    143       C  
ATOM   1795  OG1 THR A 231      26.729   6.164   7.806  1.00 33.25           O  
ANISOU 1795  OG1 THR A 231     4367   4028   4237   -185     -6    144       O  
ATOM   1796  CG2 THR A 231      24.688   5.462   8.880  1.00 26.82           C  
ANISOU 1796  CG2 THR A 231     3572   3204   3415   -287    -26    151       C  
ATOM   1797  N   PRO A 232      28.770   4.384  10.523  1.00 33.17           N  
ANISOU 1797  N   PRO A 232     4460   3897   4245    -86      7    138       N  
ATOM   1798  CA  PRO A 232      30.219   4.179  10.347  1.00 28.92           C  
ANISOU 1798  CA  PRO A 232     3930   3354   3706     -9     19    131       C  
ATOM   1799  C   PRO A 232      30.596   3.986   8.861  1.00 31.63           C  
ANISOU 1799  C   PRO A 232     4285   3713   4021     11     30    112       C  
ATOM   1800  O   PRO A 232      31.725   4.263   8.477  1.00 33.12           O  
ANISOU 1800  O   PRO A 232     4444   3929   4210     70     44    113       O  
ATOM   1801  CB  PRO A 232      30.508   2.916  11.171  1.00 25.50           C  
ANISOU 1801  CB  PRO A 232     3577   2854   3256     14     17    122       C  
ATOM   1802  CG  PRO A 232      29.164   2.186  11.295  1.00 25.46           C  
ANISOU 1802  CG  PRO A 232     3630   2811   3233    -63      5    117       C  
ATOM   1803  CD  PRO A 232      28.059   3.162  10.981  1.00 31.80           C  
ANISOU 1803  CD  PRO A 232     4366   3668   4049   -127     -1    129       C  
ATOM   1804  N   ASN A 233      29.668   3.508   8.031  1.00 31.64           N  
ANISOU 1804  N   ASN A 233     4327   3701   3993    -37     23     96       N  
ATOM   1805  CA  ASN A 233      29.924   3.419   6.584  1.00 29.88           C  
ANISOU 1805  CA  ASN A 233     4116   3499   3740    -21     32     77       C  
ATOM   1806  C   ASN A 233      29.699   4.814   5.977  1.00 30.62           C  
ANISOU 1806  C   ASN A 233     4121   3662   3850    -40     34     99       C  
ATOM   1807  O   ASN A 233      29.277   5.716   6.667  1.00 31.63           O  
ANISOU 1807  O   ASN A 233     4193   3813   4012    -66     26    122       O  
ATOM   1808  CB  ASN A 233      28.962   2.426   5.934  1.00 29.06           C  
ANISOU 1808  CB  ASN A 233     4092   3354   3595    -73     17     51       C  
ATOM   1809  CG  ASN A 233      27.541   2.692   6.343  1.00 35.05           C  
ANISOU 1809  CG  ASN A 233     4829   4122   4366   -161     -3     65       C  
ATOM   1810  OD1 ASN A 233      27.230   2.632   7.521  1.00 37.31           O  
ANISOU 1810  OD1 ASN A 233     5112   4391   4675   -181     -8     81       O  
ATOM   1811  ND2 ASN A 233      26.675   3.024   5.389  1.00 33.37           N  
ANISOU 1811  ND2 ASN A 233     4597   3946   4136   -211    -15     62       N  
ATOM   1812  N   GLY A 234      29.949   4.977   4.685  1.00 28.16           N  
ANISOU 1812  N   GLY A 234     3804   3382   3512    -26     44     90       N  
ATOM   1813  CA  GLY A 234      29.822   6.277   4.057  1.00 27.44           C  
ANISOU 1813  CA  GLY A 234     3639   3354   3434    -41     45    113       C  
ATOM   1814  C   GLY A 234      31.153   6.986   3.865  1.00 32.51           C  
ANISOU 1814  C   GLY A 234     4229   4037   4089     14     67    132       C  
ATOM   1815  O   GLY A 234      32.192   6.476   4.225  1.00 36.66           O  
ANISOU 1815  O   GLY A 234     4766   4551   4613     69     82    125       O  
ATOM   1816  N   PRO A 235      31.120   8.179   3.294  1.00 34.10           N  
ANISOU 1816  N   PRO A 235     4369   4287   4299     -1     69    157       N  
ATOM   1817  CA  PRO A 235      32.340   8.770   2.729  1.00 33.88           C  
ANISOU 1817  CA  PRO A 235     4296   4307   4269     39     92    175       C  
ATOM   1818  C   PRO A 235      33.152   9.650   3.687  1.00 34.95           C  
ANISOU 1818  C   PRO A 235     4372   4459   4450     51     92    205       C  
ATOM   1819  O   PRO A 235      34.262  10.095   3.324  1.00 37.25           O  
ANISOU 1819  O   PRO A 235     4619   4794   4741     79    110    223       O  
ATOM   1820  CB  PRO A 235      31.805   9.644   1.581  1.00 37.96           C  
ANISOU 1820  CB  PRO A 235     4788   4866   4770      7     90    192       C  
ATOM   1821  CG  PRO A 235      30.326   9.879   1.890  1.00 36.84           C  
ANISOU 1821  CG  PRO A 235     4654   4705   4640    -48     60    192       C  
ATOM   1822  CD  PRO A 235      29.894   8.949   2.989  1.00 29.57           C  
ANISOU 1822  CD  PRO A 235     3773   3732   3731    -56     49    170       C  
ATOM   1823  N   TRP A 236      32.633   9.913   4.881  1.00 31.08           N  
ANISOU 1823  N   TRP A 236     3876   3938   3995     28     71    211       N  
ATOM   1824  CA  TRP A 236      33.327  10.857   5.779  1.00 34.48           C  
ANISOU 1824  CA  TRP A 236     4254   4381   4465     31     64    237       C  
ATOM   1825  C   TRP A 236      33.836  10.232   7.100  1.00 34.09           C  
ANISOU 1825  C   TRP A 236     4218   4300   4433     60     58    228       C  
ATOM   1826  O   TRP A 236      34.773  10.732   7.697  1.00 31.99           O  
ANISOU 1826  O   TRP A 236     3911   4053   4190     77     56    245       O  
ATOM   1827  CB  TRP A 236      32.449  12.097   6.049  1.00 27.97           C  
ANISOU 1827  CB  TRP A 236     3404   3558   3667    -14     42    259       C  
ATOM   1828  CG  TRP A 236      31.099  11.742   6.656  1.00 30.24           C  
ANISOU 1828  CG  TRP A 236     3722   3811   3956    -40     25    244       C  
ATOM   1829  CD1 TRP A 236      29.894  11.537   5.972  1.00 27.99           C  
ANISOU 1829  CD1 TRP A 236     3457   3529   3649    -71     19    234       C  
ATOM   1830  CD2 TRP A 236      30.798  11.538   8.052  1.00 26.26           C  
ANISOU 1830  CD2 TRP A 236     3230   3275   3473    -42     13    239       C  
ATOM   1831  NE1 TRP A 236      28.899  11.206   6.864  1.00 27.28           N  
ANISOU 1831  NE1 TRP A 236     3385   3415   3566    -93      6    226       N  
ATOM   1832  CE2 TRP A 236      29.412  11.194   8.137  1.00 26.07           C  
ANISOU 1832  CE2 TRP A 236     3229   3238   3438    -75      3    228       C  
ATOM   1833  CE3 TRP A 236      31.546  11.623   9.232  1.00 24.36           C  
ANISOU 1833  CE3 TRP A 236     2979   3019   3256    -20      8    243       C  
ATOM   1834  CZ2 TRP A 236      28.769  10.950   9.369  1.00 21.66           C  
ANISOU 1834  CZ2 TRP A 236     2683   2656   2891    -87     -6    225       C  
ATOM   1835  CZ3 TRP A 236      30.895  11.356  10.475  1.00 26.62           C  
ANISOU 1835  CZ3 TRP A 236     3286   3275   3553    -29     -4    237       C  
ATOM   1836  CH2 TRP A 236      29.520  11.011  10.522  1.00 18.05           C  
ANISOU 1836  CH2 TRP A 236     2223   2180   2455    -61     -8    229       C  
ATOM   1837  N   ALA A 237      33.233   9.126   7.533  1.00 30.04           N  
ANISOU 1837  N   ALA A 237     3765   3742   3907     63     55    203       N  
ATOM   1838  CA  ALA A 237      33.445   8.638   8.903  1.00 31.34           C  
ANISOU 1838  CA  ALA A 237     3949   3872   4089     80     45    199       C  
ATOM   1839  C   ALA A 237      34.768   7.919   9.114  1.00 27.77           C  
ANISOU 1839  C   ALA A 237     3502   3423   3628    145     57    193       C  
ATOM   1840  O   ALA A 237      35.184   7.782  10.252  1.00 26.99           O  
ANISOU 1840  O   ALA A 237     3402   3309   3545    165     46    197       O  
ATOM   1841  CB  ALA A 237      32.286   7.719   9.379  1.00 19.91           C  
ANISOU 1841  CB  ALA A 237     2565   2372   2628     52     35    181       C  
ATOM   1842  N   THR A 238      35.400   7.433   8.049  1.00 28.12           N  
ANISOU 1842  N   THR A 238     3554   3490   3642    183     79    183       N  
ATOM   1843  CA  THR A 238      36.696   6.744   8.201  1.00 29.57           C  
ANISOU 1843  CA  THR A 238     3736   3687   3811    259     93    177       C  
ATOM   1844  C   THR A 238      37.621   7.143   7.065  1.00 35.33           C  
ANISOU 1844  C   THR A 238     4414   4488   4524    288    118    188       C  
ATOM   1845  O   THR A 238      37.169   7.709   6.057  1.00 31.54           O  
ANISOU 1845  O   THR A 238     3918   4031   4033    251    126    193       O  
ATOM   1846  CB  THR A 238      36.576   5.231   8.179  1.00 30.46           C  
ANISOU 1846  CB  THR A 238     3942   3743   3889    301     98    145       C  
ATOM   1847  OG1 THR A 238      35.973   4.821   6.953  1.00 31.87           O  
ANISOU 1847  OG1 THR A 238     4166   3913   4032    286    109    124       O  
ATOM   1848  CG2 THR A 238      35.737   4.713   9.335  1.00 41.02           C  
ANISOU 1848  CG2 THR A 238     5335   5012   5238    271     75    139       C  
ATOM   1849  N   VAL A 239      38.924   6.908   7.251  1.00 28.35           N  
ANISOU 1849  N   VAL A 239     3493   3643   3634    353    131    194       N  
ATOM   1850  CA  VAL A 239      39.875   7.076   6.178  1.00 27.60           C  
ANISOU 1850  CA  VAL A 239     3350   3624   3514    391    162    203       C  
ATOM   1851  C   VAL A 239      40.740   5.821   6.209  1.00 31.31           C  
ANISOU 1851  C   VAL A 239     3854   4094   3950    490    179    181       C  
ATOM   1852  O   VAL A 239      40.805   5.157   7.232  1.00 35.53           O  
ANISOU 1852  O   VAL A 239     4426   4581   4492    520    162    170       O  
ATOM   1853  CB  VAL A 239      40.820   8.285   6.394  1.00 35.55           C  
ANISOU 1853  CB  VAL A 239     4249   4707   4551    371    160    245       C  
ATOM   1854  CG1 VAL A 239      40.138   9.595   6.057  1.00 27.13           C  
ANISOU 1854  CG1 VAL A 239     3151   3647   3508    285    149    270       C  
ATOM   1855  CG2 VAL A 239      41.447   8.261   7.808  1.00 32.61           C  
ANISOU 1855  CG2 VAL A 239     3851   4331   4208    391    137    254       C  
ATOM   1856  N   SER A 240      41.400   5.512   5.102  1.00 26.66           N  
ANISOU 1856  N   SER A 240     3254   3557   3318    545    213    174       N  
ATOM   1857  CA  SER A 240      42.290   4.347   5.026  1.00 34.90           C  
ANISOU 1857  CA  SER A 240     4329   4609   4322    655    233    151       C  
ATOM   1858  C   SER A 240      43.558   4.605   5.798  1.00 34.17           C  
ANISOU 1858  C   SER A 240     4149   4584   4248    703    233    178       C  
ATOM   1859  O   SER A 240      43.869   5.741   6.150  1.00 32.96           O  
ANISOU 1859  O   SER A 240     3905   4485   4134    647    222    215       O  
ATOM   1860  CB  SER A 240      42.664   4.086   3.560  1.00 29.73           C  
ANISOU 1860  CB  SER A 240     3678   4007   3612    703    273    138       C  
ATOM   1861  OG  SER A 240      43.501   5.145   3.107  1.00 39.81           O  
ANISOU 1861  OG  SER A 240     4836   5393   4897    689    295    178       O  
ATOM   1862  N   ALA A 241      44.338   3.563   6.025  1.00 36.47           N  
ANISOU 1862  N   ALA A 241     4468   4878   4509    809    244    161       N  
ATOM   1863  CA  ALA A 241      45.584   3.748   6.732  1.00 32.49           C  
ANISOU 1863  CA  ALA A 241     3875   4451   4019    862    242    187       C  
ATOM   1864  C   ALA A 241      46.488   4.677   5.926  1.00 40.24           C  
ANISOU 1864  C   ALA A 241     4732   5560   4995    854    271    221       C  
ATOM   1865  O   ALA A 241      47.148   5.555   6.487  1.00 36.07           O  
ANISOU 1865  O   ALA A 241     4103   5101   4502    818    258    259       O  
ATOM   1866  CB  ALA A 241      46.281   2.391   6.988  1.00 38.65           C  
ANISOU 1866  CB  ALA A 241     4711   5216   4759    996    251    161       C  
ATOM   1867  N   GLY A 242      46.502   4.497   4.606  1.00 40.55           N  
ANISOU 1867  N   GLY A 242     4784   5633   4990    880    310    209       N  
ATOM   1868  CA  GLY A 242      47.357   5.298   3.740  1.00 40.71           C  
ANISOU 1868  CA  GLY A 242     4692   5781   4997    873    344    245       C  
ATOM   1869  C   GLY A 242      47.041   6.784   3.835  1.00 41.68           C  
ANISOU 1869  C   GLY A 242     4743   5926   5169    744    325    287       C  
ATOM   1870  O   GLY A 242      47.937   7.629   3.924  1.00 45.41           O  
ANISOU 1870  O   GLY A 242     5101   6494   5657    718    329    331       O  
ATOM   1871  N   GLU A 243      45.759   7.104   3.803  1.00 35.04           N  
ANISOU 1871  N   GLU A 243     3970   4995   4348    663    302    276       N  
ATOM   1872  CA  GLU A 243      45.338   8.488   3.862  1.00 38.21           C  
ANISOU 1872  CA  GLU A 243     4323   5404   4792    549    282    312       C  
ATOM   1873  C   GLU A 243      45.631   9.091   5.253  1.00 37.55           C  
ANISOU 1873  C   GLU A 243     4191   5313   4762    509    241    335       C  
ATOM   1874  O   GLU A 243      46.167  10.208   5.348  1.00 35.89           O  
ANISOU 1874  O   GLU A 243     3895   5163   4577    448    233    377       O  
ATOM   1875  CB  GLU A 243      43.870   8.617   3.410  1.00 35.64           C  
ANISOU 1875  CB  GLU A 243     4082   4993   4468    487    270    293       C  
ATOM   1876  CG  GLU A 243      43.278  10.007   3.500  1.00 38.27           C  
ANISOU 1876  CG  GLU A 243     4382   5317   4842    379    246    326       C  
ATOM   1877  CD  GLU A 243      43.932  11.033   2.560  1.00 42.34           C  
ANISOU 1877  CD  GLU A 243     4815   5925   5347    341    269    371       C  
ATOM   1878  OE1 GLU A 243      43.553  12.222   2.654  1.00 40.17           O  
ANISOU 1878  OE1 GLU A 243     4516   5640   5105    256    247    402       O  
ATOM   1879  OE2 GLU A 243      44.805  10.665   1.733  1.00 41.20           O  
ANISOU 1879  OE2 GLU A 243     4632   5861   5160    397    310    376       O  
ATOM   1880  N   ALA A 244      45.354   8.333   6.318  1.00 32.39           N  
ANISOU 1880  N   ALA A 244     3597   4589   4122    544    216    309       N  
ATOM   1881  CA  ALA A 244      45.672   8.781   7.670  1.00 27.53           C  
ANISOU 1881  CA  ALA A 244     2943   3968   3548    518    176    326       C  
ATOM   1882  C   ALA A 244      47.169   9.108   7.774  1.00 38.08           C  
ANISOU 1882  C   ALA A 244     4164   5421   4883    547    184    360       C  
ATOM   1883  O   ALA A 244      47.566  10.146   8.341  1.00 39.23           O  
ANISOU 1883  O   ALA A 244     4239   5603   5064    480    157    393       O  
ATOM   1884  CB  ALA A 244      45.286   7.749   8.692  1.00 27.50           C  
ANISOU 1884  CB  ALA A 244     3020   3882   3545    567    155    294       C  
ATOM   1885  N   ARG A 245      47.994   8.253   7.191  1.00 28.31           N  
ANISOU 1885  N   ARG A 245     2907   4247   3602    645    220    351       N  
ATOM   1886  CA  ARG A 245      49.435   8.439   7.285  1.00 41.87           C  
ANISOU 1886  CA  ARG A 245     4506   6089   5312    685    230    384       C  
ATOM   1887  C   ARG A 245      49.817   9.710   6.533  1.00 41.47           C  
ANISOU 1887  C   ARG A 245     4361   6125   5271    597    244    430       C  
ATOM   1888  O   ARG A 245      50.615  10.517   7.004  1.00 38.62           O  
ANISOU 1888  O   ARG A 245     3903   5837   4934    548    224    469       O  
ATOM   1889  CB  ARG A 245      50.210   7.214   6.721  1.00 36.03           C  
ANISOU 1889  CB  ARG A 245     3770   5405   4516    824    272    363       C  
ATOM   1890  CG  ARG A 245      51.718   7.448   6.523  1.00 38.47           C  
ANISOU 1890  CG  ARG A 245     3938   5871   4807    869    295    401       C  
ATOM   1891  CD  ARG A 245      52.510   6.097   6.445  1.00 28.13           C  
ANISOU 1891  CD  ARG A 245     2639   4604   3446   1032    323    375       C  
ATOM   1892  NE  ARG A 245      52.384   5.306   7.679  1.00 33.68           N  
ANISOU 1892  NE  ARG A 245     3408   5226   4161   1089    284    351       N  
ATOM   1893  CZ  ARG A 245      53.231   5.387   8.702  1.00 41.54           C  
ANISOU 1893  CZ  ARG A 245     4329   6279   5175   1113    253    373       C  
ATOM   1894  NH1 ARG A 245      54.261   6.226   8.643  1.00 40.07           N  
ANISOU 1894  NH1 ARG A 245     3995   6233   4998   1079    256    419       N  
ATOM   1895  NH2 ARG A 245      53.060   4.632   9.784  1.00 39.39           N  
ANISOU 1895  NH2 ARG A 245     4128   5929   4909   1167    219    351       N  
ATOM   1896  N   ARG A 246      49.228   9.881   5.363  1.00 34.33           N  
ANISOU 1896  N   ARG A 246     3490   5210   4344    571    275    426       N  
ATOM   1897  CA  ARG A 246      49.535  11.030   4.529  1.00 40.54           C  
ANISOU 1897  CA  ARG A 246     4199   6073   5132    490    292    472       C  
ATOM   1898  C   ARG A 246      49.142  12.360   5.225  1.00 42.62           C  
ANISOU 1898  C   ARG A 246     4447   6296   5452    364    243    502       C  
ATOM   1899  O   ARG A 246      49.943  13.298   5.284  1.00 36.05           O  
ANISOU 1899  O   ARG A 246     3520   5541   4634    301    235    549       O  
ATOM   1900  CB  ARG A 246      48.822  10.841   3.208  1.00 38.48           C  
ANISOU 1900  CB  ARG A 246     3998   5790   4831    496    329    456       C  
ATOM   1901  CG  ARG A 246      49.136  11.839   2.160  1.00 39.63           C  
ANISOU 1901  CG  ARG A 246     4077   6018   4964    430    356    502       C  
ATOM   1902  CD  ARG A 246      47.811  12.221   1.511  1.00 47.80           C  
ANISOU 1902  CD  ARG A 246     5198   6966   5999    369    350    490       C  
ATOM   1903  NE  ARG A 246      47.825  13.668   1.471  1.00 55.83           N  
ANISOU 1903  NE  ARG A 246     6164   8000   7048    254    330    543       N  
ATOM   1904  CZ  ARG A 246      46.805  14.460   1.709  1.00 46.56           C  
ANISOU 1904  CZ  ARG A 246     5043   6739   5909    173    294    546       C  
ATOM   1905  NH1 ARG A 246      45.606  13.986   1.981  1.00 36.24           N  
ANISOU 1905  NH1 ARG A 246     3832   5327   4610    186    274    502       N  
ATOM   1906  NH2 ARG A 246      47.015  15.755   1.650  1.00 59.16           N  
ANISOU 1906  NH2 ARG A 246     6591   8357   7528     78    278    596       N  
ATOM   1907  N   ARG A 247      47.925  12.432   5.772  1.00 34.24           N  
ANISOU 1907  N   ARG A 247     3478   5113   4418    327    210    476       N  
ATOM   1908  CA  ARG A 247      47.518  13.602   6.582  1.00 33.34           C  
ANISOU 1908  CA  ARG A 247     3363   4951   4354    225    161    496       C  
ATOM   1909  C   ARG A 247      48.339  13.857   7.848  1.00 30.55           C  
ANISOU 1909  C   ARG A 247     2952   4625   4031    214    122    511       C  
ATOM   1910  O   ARG A 247      48.638  15.002   8.164  1.00 36.82           O  
ANISOU 1910  O   ARG A 247     3699   5437   4853    127     92    546       O  
ATOM   1911  CB  ARG A 247      46.040  13.525   6.973  1.00 26.21           C  
ANISOU 1911  CB  ARG A 247     2568   3923   3470    204    137    462       C  
ATOM   1912  CG  ARG A 247      45.129  13.340   5.786  1.00 30.94           C  
ANISOU 1912  CG  ARG A 247     3224   4491   4040    204    166    447       C  
ATOM   1913  CD  ARG A 247      43.632  13.172   6.242  1.00 25.65           C  
ANISOU 1913  CD  ARG A 247     2653   3707   3387    185    141    414       C  
ATOM   1914  NE  ARG A 247      42.755  12.989   5.092  1.00 26.42           N  
ANISOU 1914  NE  ARG A 247     2800   3782   3455    181    164    400       N  
ATOM   1915  CZ  ARG A 247      41.414  12.962   5.154  1.00 33.89           C  
ANISOU 1915  CZ  ARG A 247     3818   4649   4408    155    147    378       C  
ATOM   1916  NH1 ARG A 247      40.778  13.160   6.313  1.00 29.08           N  
ANISOU 1916  NH1 ARG A 247     3239   3977   3833    130    111    368       N  
ATOM   1917  NH2 ARG A 247      40.706  12.749   4.050  1.00 30.11           N  
ANISOU 1917  NH2 ARG A 247     3379   4163   3898    154    166    366       N  
ATOM   1918  N   ALA A 248      48.675  12.817   8.596  1.00 29.75           N  
ANISOU 1918  N   ALA A 248     2862   4521   3921    300    117    484       N  
ATOM   1919  CA  ALA A 248      49.458  13.003   9.808  1.00 34.00           C  
ANISOU 1919  CA  ALA A 248     3346   5089   4483    295     76    497       C  
ATOM   1920  C   ALA A 248      50.812  13.589   9.428  1.00 32.53           C  
ANISOU 1920  C   ALA A 248     3030   5039   4290    270     86    545       C  
ATOM   1921  O   ALA A 248      51.337  14.477  10.096  1.00 33.48           O  
ANISOU 1921  O   ALA A 248     3092   5189   4438    197     46    575       O  
ATOM   1922  CB  ALA A 248      49.640  11.694  10.569  1.00 33.01           C  
ANISOU 1922  CB  ALA A 248     3256   4944   4343    404     73    464       C  
ATOM   1923  N   THR A 249      51.363  13.141   8.322  1.00 33.53           N  
ANISOU 1923  N   THR A 249     3112   5251   4378    325    139    554       N  
ATOM   1924  CA  THR A 249      52.728  13.572   8.032  1.00 32.47           C  
ANISOU 1924  CA  THR A 249     2842   5263   4232    310    151    602       C  
ATOM   1925  C   THR A 249      52.743  14.948   7.399  1.00 32.75           C  
ANISOU 1925  C   THR A 249     2835   5327   4282    182    150    650       C  
ATOM   1926  O   THR A 249      53.628  15.730   7.706  1.00 34.89           O  
ANISOU 1926  O   THR A 249     3011   5677   4568    112    127    693       O  
ATOM   1927  CB  THR A 249      53.646  12.456   7.367  1.00 48.96           C  
ANISOU 1927  CB  THR A 249     4874   7461   6266    441    206    597       C  
ATOM   1928  OG1 THR A 249      54.311  12.947   6.199  1.00 48.35           O  
ANISOU 1928  OG1 THR A 249     4707   7502   6161    414    252    639       O  
ATOM   1929  CG2 THR A 249      52.875  11.212   7.036  1.00 34.16           C  
ANISOU 1929  CG2 THR A 249     3114   5504   4362    547    234    542       C  
ATOM   1930  N   LEU A 250      51.706  15.277   6.622  1.00 35.12           N  
ANISOU 1930  N   LEU A 250     3212   5551   4580    143    165    641       N  
ATOM   1931  CA  LEU A 250      51.534  16.641   6.128  1.00 36.21           C  
ANISOU 1931  CA  LEU A 250     3336   5687   4735     18    155    685       C  
ATOM   1932  C   LEU A 250      51.379  17.604   7.308  1.00 41.68           C  
ANISOU 1932  C   LEU A 250     4042   6316   5478    -75     87    695       C  
ATOM   1933  O   LEU A 250      52.069  18.637   7.371  1.00 42.18           O  
ANISOU 1933  O   LEU A 250     4037   6434   5557   -171     64    743       O  
ATOM   1934  CB  LEU A 250      50.332  16.773   5.163  1.00 33.34           C  
ANISOU 1934  CB  LEU A 250     3064   5244   4360      4    178    671       C  
ATOM   1935  CG  LEU A 250      50.076  18.182   4.600  1.00 31.64           C  
ANISOU 1935  CG  LEU A 250     2848   5017   4158   -118    167    717       C  
ATOM   1936  CD1 LEU A 250      51.382  18.818   4.044  1.00 34.14           C  
ANISOU 1936  CD1 LEU A 250     3042   5470   4459   -174    187    781       C  
ATOM   1937  CD2 LEU A 250      49.037  18.151   3.516  1.00 31.21           C  
ANISOU 1937  CD2 LEU A 250     2870   4910   4080   -111    196    705       C  
ATOM   1938  N   LEU A 251      50.491  17.269   8.252  1.00 35.83           N  
ANISOU 1938  N   LEU A 251     3391   5463   4760    -50     53    650       N  
ATOM   1939  CA  LEU A 251      50.320  18.107   9.427  1.00 33.58           C  
ANISOU 1939  CA  LEU A 251     3127   5116   4516   -124    -11    653       C  
ATOM   1940  C   LEU A 251      51.638  18.294  10.201  1.00 31.88           C  
ANISOU 1940  C   LEU A 251     2811   4993   4310   -145    -42    680       C  
ATOM   1941  O   LEU A 251      51.978  19.416  10.586  1.00 35.19           O  
ANISOU 1941  O   LEU A 251     3202   5416   4753   -249    -85    712       O  
ATOM   1942  CB  LEU A 251      49.258  17.563  10.380  1.00 41.41           C  
ANISOU 1942  CB  LEU A 251     4222   5991   5523    -79    -36    601       C  
ATOM   1943  CG  LEU A 251      49.295  18.542  11.551  1.00 43.23           C  
ANISOU 1943  CG  LEU A 251     4460   6177   5788   -158   -101    609       C  
ATOM   1944  CD1 LEU A 251      48.191  19.571  11.450  1.00 37.00           C  
ANISOU 1944  CD1 LEU A 251     3752   5288   5019   -231   -122    608       C  
ATOM   1945  CD2 LEU A 251      49.282  17.833  12.864  1.00 47.16           C  
ANISOU 1945  CD2 LEU A 251     4983   6642   6292   -100   -132    574       C  
ATOM   1946  N   ALA A 252      52.357  17.208  10.466  1.00 31.52           N  
ANISOU 1946  N   ALA A 252     2715   5018   4243    -46    -26    666       N  
ATOM   1947  CA  ALA A 252      53.684  17.323  11.083  1.00 36.79           C  
ANISOU 1947  CA  ALA A 252     3269   5796   4912    -58    -52    696       C  
ATOM   1948  C   ALA A 252      54.519  18.370  10.344  1.00 37.84           C  
ANISOU 1948  C   ALA A 252     3303   6031   5044   -161    -45    757       C  
ATOM   1949  O   ALA A 252      55.083  19.255  10.986  1.00 40.06           O  
ANISOU 1949  O   ALA A 252     3536   6338   5348   -257    -97    787       O  
ATOM   1950  CB  ALA A 252      54.406  16.001  11.123  1.00 36.44           C  
ANISOU 1950  CB  ALA A 252     3174   5835   4836     76    -21    680       C  
ATOM   1951  N  AARG A 253      54.589  18.271   9.014  0.70 34.49           N  
ANISOU 1951  N  AARG A 253     2851   5663   4589   -147     16    777       N  
ATOM   1952  N  BARG A 253      54.577  18.278   9.015  0.30 36.53           N  
ANISOU 1952  N  BARG A 253     3111   5920   4848   -148     15    777       N  
ATOM   1953  CA AARG A 253      55.361  19.242   8.224  0.70 41.53           C  
ANISOU 1953  CA AARG A 253     3649   6656   5474   -249     29    842       C  
ATOM   1954  CA BARG A 253      55.354  19.230   8.212  0.30 40.28           C  
ANISOU 1954  CA BARG A 253     3491   6497   5315   -248     30    842       C  
ATOM   1955  C  AARG A 253      54.892  20.681   8.509  0.70 43.46           C  
ANISOU 1955  C  AARG A 253     3944   6812   5755   -397    -25    866       C  
ATOM   1956  C  BARG A 253      54.893  20.682   8.421  0.30 41.76           C  
ANISOU 1956  C  BARG A 253     3728   6600   5539   -397    -21    868       C  
ATOM   1957  O  AARG A 253      55.702  21.568   8.828  0.70 42.80           O  
ANISOU 1957  O  AARG A 253     3789   6786   5686   -503    -62    912       O  
ATOM   1958  O  BARG A 253      55.715  21.587   8.579  0.30 43.13           O  
ANISOU 1958  O  BARG A 253     3826   6839   5724   -505    -51    918       O  
ATOM   1959  CB AARG A 253      55.265  18.932   6.728  0.70 38.74           C  
ANISOU 1959  CB AARG A 253     3287   6354   5079   -209    104    855       C  
ATOM   1960  CB BARG A 253      55.310  18.860   6.723  0.30 41.59           C  
ANISOU 1960  CB BARG A 253     3643   6721   5438   -202    106    854       C  
ATOM   1961  CG AARG A 253      56.447  18.212   6.180  0.70 48.47           C  
ANISOU 1961  CG AARG A 253     4396   7753   6268   -131    156    876       C  
ATOM   1962  CG BARG A 253      56.170  17.667   6.347  0.30 47.46           C  
ANISOU 1962  CG BARG A 253     4304   7591   6136    -71    159    846       C  
ATOM   1963  CD AARG A 253      56.295  17.957   4.687  0.70 56.04           C  
ANISOU 1963  CD AARG A 253     5356   8757   7180    -93    230    886       C  
ATOM   1964  CD BARG A 253      56.433  17.630   4.839  0.30 53.29           C  
ANISOU 1964  CD BARG A 253     4999   8422   6828    -57    232    876       C  
ATOM   1965  NE AARG A 253      55.475  16.769   4.464  0.70 60.54           N  
ANISOU 1965  NE AARG A 253     6025   9249   7728     37    259    822       N  
ATOM   1966  NE BARG A 253      57.693  16.969   4.500  0.30 49.07           N  
ANISOU 1966  NE BARG A 253     4334   8060   6251     26    277    897       N  
ATOM   1967  CZ AARG A 253      54.683  16.586   3.415  0.70 57.28           C  
ANISOU 1967  CZ AARG A 253     5687   8790   7288     60    301    806       C  
ATOM   1968  CZ BARG A 253      57.797  15.717   4.063  0.30 44.48           C  
ANISOU 1968  CZ BARG A 253     3762   7515   5625    178    328    860       C  
ATOM   1969  NH1AARG A 253      53.975  15.468   3.331  0.70 48.28           N  
ANISOU 1969  NH1AARG A 253     4639   7577   6129    171    319    745       N  
ATOM   1970  NH1BARG A 253      58.994  15.217   3.780  0.30 38.45           N  
ANISOU 1970  NH1BARG A 253     2871   6917   4819    254    368    883       N  
ATOM   1971  NH2AARG A 253      54.595  17.522   2.465  0.70 54.72           N  
ANISOU 1971  NH2AARG A 253     5348   8489   6953    -33    320    851       N  
ATOM   1972  NH2BARG A 253      56.712  14.965   3.906  0.30 40.56           N  
ANISOU 1972  NH2BARG A 253     3399   6891   5120    254    339    801       N  
ATOM   1973  N   LEU A 254      53.578  20.892   8.435  1.00 34.39           N  
ANISOU 1973  N   LEU A 254     2923   5522   4621   -403    -32    835       N  
ATOM   1974  CA  LEU A 254      53.001  22.225   8.640  1.00 36.17           C  
ANISOU 1974  CA  LEU A 254     3216   5651   4877   -525    -79    852       C  
ATOM   1975  C   LEU A 254      53.361  22.867   9.969  1.00 36.26           C  
ANISOU 1975  C   LEU A 254     3223   5632   4920   -595   -155    853       C  
ATOM   1976  O   LEU A 254      53.322  24.084  10.083  1.00 39.20           O  
ANISOU 1976  O   LEU A 254     3622   5960   5312   -712   -197    882       O  
ATOM   1977  CB  LEU A 254      51.452  22.192   8.489  1.00 31.14           C  
ANISOU 1977  CB  LEU A 254     2715   4869   4246   -494    -76    810       C  
ATOM   1978  CG  LEU A 254      51.032  21.845   7.055  1.00 36.24           C  
ANISOU 1978  CG  LEU A 254     3374   5537   4859   -455    -10    816       C  
ATOM   1979  CD1 LEU A 254      49.534  21.795   6.860  1.00 34.02           C  
ANISOU 1979  CD1 LEU A 254     3215   5129   4582   -427     -9    778       C  
ATOM   1980  CD2 LEU A 254      51.684  22.830   6.072  1.00 38.78           C  
ANISOU 1980  CD2 LEU A 254     3634   5932   5167   -555      6    885       C  
ATOM   1981  N   VAL A 255      53.670  22.062  10.983  1.00 42.65           N  
ANISOU 1981  N   VAL A 255     4013   6459   5734   -522   -175    820       N  
ATOM   1982  CA  VAL A 255      54.060  22.591  12.290  1.00 41.19           C  
ANISOU 1982  CA  VAL A 255     3823   6254   5574   -581   -249    817       C  
ATOM   1983  C   VAL A 255      55.537  22.346  12.558  1.00 51.15           C  
ANISOU 1983  C   VAL A 255     4942   7668   6825   -586   -259    850       C  
ATOM   1984  O   VAL A 255      55.995  22.434  13.692  1.00 56.54           O  
ANISOU 1984  O   VAL A 255     5604   8359   7520   -604   -316    842       O  
ATOM   1985  CB  VAL A 255      53.233  21.994  13.463  1.00 41.00           C  
ANISOU 1985  CB  VAL A 255     3893   6123   5562   -505   -279    755       C  
ATOM   1986  CG1 VAL A 255      51.737  22.330  13.302  1.00 35.04           C  
ANISOU 1986  CG1 VAL A 255     3272   5222   4818   -507   -276    725       C  
ATOM   1987  CG2 VAL A 255      53.450  20.469  13.618  1.00 35.48           C  
ANISOU 1987  CG2 VAL A 255     3164   5476   4841   -363   -243    724       C  
ATOM   1988  N   GLY A 256      56.291  22.024  11.521  1.00 54.26           N  
ANISOU 1988  N   GLY A 256     5233   8191   7191   -566   -202    887       N  
ATOM   1989  CA  GLY A 256      57.739  21.934  11.683  1.00 53.06           C  
ANISOU 1989  CA  GLY A 256     4930   8204   7027   -583   -210    928       C  
ATOM   1990  C   GLY A 256      58.281  20.670  12.322  1.00 54.11           C  
ANISOU 1990  C   GLY A 256     5008   8409   7143   -447   -204    899       C  
ATOM   1991  O   GLY A 256      59.159  20.727  13.157  1.00 56.29           O  
ANISOU 1991  O   GLY A 256     5204   8760   7424   -468   -250    912       O  
ATOM   1992  N   CYS A 257      57.769  19.518  11.923  1.00 57.82           N  
ANISOU 1992  N   CYS A 257     5524   8855   7592   -309   -149    859       N  
ATOM   1993  CA  CYS A 257      58.269  18.260  12.441  1.00 52.04           C  
ANISOU 1993  CA  CYS A 257     4750   8183   6838   -169   -139    832       C  
ATOM   1994  C   CYS A 257      58.694  17.391  11.282  1.00 56.58           C  
ANISOU 1994  C   CYS A 257     5265   8864   7370    -64    -59    840       C  
ATOM   1995  O   CYS A 257      57.868  17.093  10.429  1.00 65.06           O  
ANISOU 1995  O   CYS A 257     6418   9871   8431    -26    -10    819       O  
ATOM   1996  CB  CYS A 257      57.178  17.566  13.272  1.00 44.06           C  
ANISOU 1996  CB  CYS A 257     3879   7022   5839    -90   -159    768       C  
ATOM   1997  SG  CYS A 257      56.922  18.327  14.894  1.00 46.21           S  
ANISOU 1997  SG  CYS A 257     4206   7200   6150   -176   -255    753       S  
ATOM   1998  N   ASN A 265      61.114   8.007  10.111  1.00 70.16           N  
ANISOU 1998  N   ASN A 265     6987  10883   8786   1146    218    646       N  
ATOM   1999  CA  ASN A 265      60.949   7.365  11.424  1.00 69.68           C  
ANISOU 1999  CA  ASN A 265     6997  10738   8741   1207    163    618       C  
ATOM   2000  C   ASN A 265      59.732   7.920  12.209  1.00 58.77           C  
ANISOU 2000  C   ASN A 265     5737   9180   7414   1083    109    598       C  
ATOM   2001  O   ASN A 265      59.708   9.110  12.561  1.00 53.89           O  
ANISOU 2001  O   ASN A 265     5067   8571   6837    935     70    628       O  
ATOM   2002  CB  ASN A 265      62.261   7.505  12.213  1.00 69.98           C  
ANISOU 2002  CB  ASN A 265     6881  10933   8777   1232    126    657       C  
ATOM   2003  CG  ASN A 265      62.255   6.737  13.525  1.00 71.68           C  
ANISOU 2003  CG  ASN A 265     7159  11082   8996   1319     72    632       C  
ATOM   2004  OD1 ASN A 265      61.764   7.234  14.538  1.00 67.25           O  
ANISOU 2004  OD1 ASN A 265     6645  10431   8477   1225     10    629       O  
ATOM   2005  ND2 ASN A 265      62.849   5.532  13.523  1.00 72.55           N  
ANISOU 2005  ND2 ASN A 265     7268  11242   9057   1504     95    616       N  
ATOM   2006  N   ASP A 266      58.719   7.079  12.463  1.00 46.86           N  
ANISOU 2006  N   ASP A 266     4390   7513   5903   1142    108    548       N  
ATOM   2007  CA  ASP A 266      57.506   7.562  13.133  1.00 47.25           C  
ANISOU 2007  CA  ASP A 266     4552   7405   5998   1032     65    529       C  
ATOM   2008  C   ASP A 266      57.776   8.073  14.542  1.00 51.04           C  
ANISOU 2008  C   ASP A 266     4997   7885   6512    974     -7    544       C  
ATOM   2009  O   ASP A 266      57.204   9.081  14.958  1.00 49.15           O  
ANISOU 2009  O   ASP A 266     4777   7585   6315    840    -44    552       O  
ATOM   2010  CB  ASP A 266      56.403   6.494  13.203  1.00 42.93           C  
ANISOU 2010  CB  ASP A 266     4176   6697   5437   1105     76    476       C  
ATOM   2011  CG  ASP A 266      55.833   6.137  11.848  1.00 40.14           C  
ANISOU 2011  CG  ASP A 266     3885   6310   5055   1129    137    454       C  
ATOM   2012  OD1 ASP A 266      56.019   6.904  10.876  1.00 47.27           O  
ANISOU 2012  OD1 ASP A 266     4715   7287   5957   1064    168    479       O  
ATOM   2013  OD2 ASP A 266      55.183   5.075  11.743  1.00 44.13           O  
ANISOU 2013  OD2 ASP A 266     4519   6713   5537   1211    152    412       O  
ATOM   2014  N   THR A 267      58.633   7.366  15.274  1.00 49.18           N  
ANISOU 2014  N   THR A 267     4718   7714   6256   1081    -28    547       N  
ATOM   2015  CA  THR A 267      58.936   7.679  16.674  1.00 47.16           C  
ANISOU 2015  CA  THR A 267     4436   7460   6023   1047   -100    559       C  
ATOM   2016  C   THR A 267      59.412   9.126  16.825  1.00 45.88           C  
ANISOU 2016  C   THR A 267     4157   7381   5895    892   -136    601       C  
ATOM   2017  O   THR A 267      58.989   9.823  17.743  1.00 49.40           O  
ANISOU 2017  O   THR A 267     4637   7758   6374    794   -193    599       O  
ATOM   2018  CB  THR A 267      60.018   6.699  17.253  1.00 50.91           C  
ANISOU 2018  CB  THR A 267     4854   8030   6461   1200   -113    564       C  
ATOM   2019  OG1 THR A 267      59.558   5.350  17.131  1.00 49.73           O  
ANISOU 2019  OG1 THR A 267     4830   7787   6277   1342    -82    525       O  
ATOM   2020  CG2 THR A 267      60.315   6.996  18.717  1.00 41.15           C  
ANISOU 2020  CG2 THR A 267     3596   6796   5244   1166   -190    575       C  
ATOM   2021  N   GLU A 268      60.289   9.565  15.925  1.00 41.65           N  
ANISOU 2021  N   GLU A 268     3486   6992   5346    872   -104    638       N  
ATOM   2022  CA  GLU A 268      60.794  10.953  15.923  1.00 45.63           C  
ANISOU 2022  CA  GLU A 268     3877   7581   5880    715   -135    684       C  
ATOM   2023  C   GLU A 268      59.735  11.987  15.501  1.00 41.17           C  
ANISOU 2023  C   GLU A 268     3390   6903   5351    568   -134    682       C  
ATOM   2024  O   GLU A 268      59.588  13.007  16.139  1.00 47.02           O  
ANISOU 2024  O   GLU A 268     4130   7609   6126    441   -189    695       O  
ATOM   2025  CB  GLU A 268      61.992  11.098  14.979  1.00 47.05           C  
ANISOU 2025  CB  GLU A 268     3891   7955   6031    731    -93    730       C  
ATOM   2026  CG  GLU A 268      63.084  10.074  15.224  1.00 70.99           C  
ANISOU 2026  CG  GLU A 268     6834  11119   9021    891    -84    736       C  
ATOM   2027  CD  GLU A 268      64.257  10.219  14.249  1.00 91.41           C  
ANISOU 2027  CD  GLU A 268     9247  13911  11574    912    -36    783       C  
ATOM   2028  OE1 GLU A 268      64.373  11.289  13.582  1.00 91.34           O  
ANISOU 2028  OE1 GLU A 268     9168  13956  11580    772    -23    822       O  
ATOM   2029  OE2 GLU A 268      65.062   9.256  14.159  1.00 99.92           O  
ANISOU 2029  OE2 GLU A 268    10259  15098  12606   1071     -9    783       O  
ATOM   2030  N   LEU A 269      59.066  11.744  14.383  1.00 36.08           N  
ANISOU 2030  N   LEU A 269     2808   6209   4693    590    -73    667       N  
ATOM   2031  CA  LEU A 269      57.959  12.585  13.955  1.00 45.79           C  
ANISOU 2031  CA  LEU A 269     4123   7323   5951    473    -70    660       C  
ATOM   2032  C   LEU A 269      56.970  12.805  15.116  1.00 43.71           C  
ANISOU 2032  C   LEU A 269     3978   6908   5722    426   -126    628       C  
ATOM   2033  O   LEU A 269      56.655  13.930  15.461  1.00 45.16           O  
ANISOU 2033  O   LEU A 269     4172   7048   5939    298   -167    641       O  
ATOM   2034  CB  LEU A 269      57.264  11.960  12.744  1.00 42.31           C  
ANISOU 2034  CB  LEU A 269     3756   6835   5484    536      0    636       C  
ATOM   2035  CG  LEU A 269      56.149  12.766  12.105  1.00 51.59           C  
ANISOU 2035  CG  LEU A 269     5011   7909   6682    430     11    632       C  
ATOM   2036  CD1 LEU A 269      55.956  12.335  10.679  1.00 56.93           C  
ANISOU 2036  CD1 LEU A 269     5700   8609   7323    480     82    627       C  
ATOM   2037  CD2 LEU A 269      54.866  12.559  12.883  1.00 48.61           C  
ANISOU 2037  CD2 LEU A 269     4778   7363   6328    424    -20    588       C  
ATOM   2038  N   ILE A 270      56.524  11.716  15.737  1.00 45.12           N  
ANISOU 2038  N   ILE A 270     4247   7008   5888    533   -130    588       N  
ATOM   2039  CA  ILE A 270      55.556  11.785  16.825  1.00 39.66           C  
ANISOU 2039  CA  ILE A 270     3670   6179   5221    502   -175    558       C  
ATOM   2040  C   ILE A 270      56.064  12.507  18.066  1.00 37.53           C  
ANISOU 2040  C   ILE A 270     3354   5934   4973    434   -248    574       C  
ATOM   2041  O   ILE A 270      55.326  13.266  18.685  1.00 41.68           O  
ANISOU 2041  O   ILE A 270     3945   6367   5526    344   -287    564       O  
ATOM   2042  CB  ILE A 270      55.015  10.394  17.195  1.00 33.95           C  
ANISOU 2042  CB  ILE A 270     3053   5373   4475    630   -160    517       C  
ATOM   2043  CG1 ILE A 270      54.345   9.768  15.976  1.00 38.07           C  
ANISOU 2043  CG1 ILE A 270     3641   5849   4976    678    -95    496       C  
ATOM   2044  CG2 ILE A 270      54.021  10.504  18.333  1.00 30.71           C  
ANISOU 2044  CG2 ILE A 270     2752   4831   4085    591   -204    491       C  
ATOM   2045  CD1 ILE A 270      54.170   8.274  16.086  1.00 46.50           C  
ANISOU 2045  CD1 ILE A 270     4791   6867   6009    818    -73    462       C  
ATOM   2046  N   ALA A 271      57.319  12.271  18.425  1.00 36.11           N  
ANISOU 2046  N   ALA A 271     3061   5882   4776    479   -268    598       N  
ATOM   2047  CA  ALA A 271      57.916  12.940  19.556  1.00 34.30           C  
ANISOU 2047  CA  ALA A 271     2777   5693   4562    413   -341    615       C  
ATOM   2048  C   ALA A 271      57.927  14.433  19.275  1.00 42.05           C  
ANISOU 2048  C   ALA A 271     3718   6684   5574    249   -365    643       C  
ATOM   2049  O   ALA A 271      57.701  15.253  20.162  1.00 44.82           O  
ANISOU 2049  O   ALA A 271     4101   6981   5948    156   -427    640       O  
ATOM   2050  CB  ALA A 271      59.355  12.432  19.778  1.00 39.76           C  
ANISOU 2050  CB  ALA A 271     3333   6547   5228    492   -353    642       C  
ATOM   2051  N   CYS A 272      58.195  14.796  18.027  1.00 41.79           N  
ANISOU 2051  N   CYS A 272     3621   6719   5539    212   -317    672       N  
ATOM   2052  CA  CYS A 272      58.232  16.197  17.703  1.00 42.87           C  
ANISOU 2052  CA  CYS A 272     3726   6863   5701     55   -339    704       C  
ATOM   2053  C   CYS A 272      56.806  16.766  17.824  1.00 39.18           C  
ANISOU 2053  C   CYS A 272     3405   6224   5260     -9   -349    673       C  
ATOM   2054  O   CYS A 272      56.627  17.796  18.491  1.00 34.63           O  
ANISOU 2054  O   CYS A 272     2856   5595   4707   -118   -407    677       O  
ATOM   2055  CB  CYS A 272      58.870  16.461  16.335  1.00 46.43           C  
ANISOU 2055  CB  CYS A 272     4072   7432   6138     28   -284    747       C  
ATOM   2056  SG  CYS A 272      58.811  18.227  15.831  1.00 50.09           S  
ANISOU 2056  SG  CYS A 272     4517   7885   6631   -175   -308    792       S  
ATOM   2057  N   LEU A 273      55.808  16.065  17.265  1.00 32.98           N  
ANISOU 2057  N   LEU A 273     2715   5351   4466     64   -297    641       N  
ATOM   2058  CA  LEU A 273      54.402  16.495  17.405  1.00 34.39           C  
ANISOU 2058  CA  LEU A 273     3027   5375   4665     18   -303    611       C  
ATOM   2059  C   LEU A 273      54.024  16.693  18.882  1.00 35.73           C  
ANISOU 2059  C   LEU A 273     3264   5464   4849      0   -368    585       C  
ATOM   2060  O   LEU A 273      53.283  17.626  19.208  1.00 39.96           O  
ANISOU 2060  O   LEU A 273     3869   5909   5406    -85   -399    576       O  
ATOM   2061  CB  LEU A 273      53.407  15.529  16.722  1.00 34.16           C  
ANISOU 2061  CB  LEU A 273     3087   5273   4621    107   -244    577       C  
ATOM   2062  CG  LEU A 273      53.328  15.572  15.186  1.00 35.50           C  
ANISOU 2062  CG  LEU A 273     3233   5479   4778    104   -181    594       C  
ATOM   2063  CD1 LEU A 273      52.404  14.516  14.659  1.00 34.44           C  
ANISOU 2063  CD1 LEU A 273     3190   5273   4624    195   -132    556       C  
ATOM   2064  CD2 LEU A 273      52.911  16.932  14.634  1.00 36.61           C  
ANISOU 2064  CD2 LEU A 273     3383   5586   4940    -25   -189    618       C  
ATOM   2065  N   ARG A 274      54.561  15.842  19.765  1.00 30.58           N  
ANISOU 2065  N   ARG A 274     2590   4847   4180     84   -390    574       N  
ATOM   2066  CA  ARG A 274      54.274  15.933  21.194  1.00 32.86           C  
ANISOU 2066  CA  ARG A 274     2941   5070   4475     78   -450    551       C  
ATOM   2067  C   ARG A 274      54.871  17.182  21.849  1.00 38.30           C  
ANISOU 2067  C   ARG A 274     3583   5790   5180    -41   -520    572       C  
ATOM   2068  O   ARG A 274      54.435  17.577  22.925  1.00 38.46           O  
ANISOU 2068  O   ARG A 274     3673   5735   5207    -73   -572    550       O  
ATOM   2069  CB  ARG A 274      54.653  14.650  21.966  1.00 30.15           C  
ANISOU 2069  CB  ARG A 274     2599   4752   4105    204   -455    535       C  
ATOM   2070  CG  ARG A 274      53.708  13.467  21.698  1.00 32.30           C  
ANISOU 2070  CG  ARG A 274     2972   4939   4362    307   -403    502       C  
ATOM   2071  CD  ARG A 274      53.871  12.360  22.753  1.00 39.33           C  
ANISOU 2071  CD  ARG A 274     3899   5817   5229    413   -423    485       C  
ATOM   2072  NE  ARG A 274      55.301  12.110  22.933  1.00 49.64           N  
ANISOU 2072  NE  ARG A 274     5085   7259   6518    459   -444    512       N  
ATOM   2073  CZ  ARG A 274      55.955  11.102  22.355  1.00 50.13           C  
ANISOU 2073  CZ  ARG A 274     5098   7395   6553    571   -405    519       C  
ATOM   2074  NH1 ARG A 274      55.257  10.232  21.605  1.00 38.18           N  
ANISOU 2074  NH1 ARG A 274     3662   5817   5026    643   -346    497       N  
ATOM   2075  NH2 ARG A 274      57.288  10.961  22.532  1.00 40.54           N  
ANISOU 2075  NH2 ARG A 274     3760   6319   5322    613   -426    547       N  
ATOM   2076  N   THR A 275      55.835  17.832  21.202  1.00 33.66           N  
ANISOU 2076  N   THR A 275     2883   5310   4598   -112   -523    614       N  
ATOM   2077  CA  THR A 275      56.378  19.056  21.778  1.00 36.41           C  
ANISOU 2077  CA  THR A 275     3194   5679   4961   -241   -594    635       C  
ATOM   2078  C   THR A 275      55.578  20.299  21.341  1.00 39.47           C  
ANISOU 2078  C   THR A 275     3655   5968   5372   -358   -600    638       C  
ATOM   2079  O   THR A 275      55.778  21.373  21.887  1.00 42.71           O  
ANISOU 2079  O   THR A 275     4075   6358   5795   -467   -663    646       O  
ATOM   2080  CB  THR A 275      57.857  19.284  21.382  1.00 35.85           C  
ANISOU 2080  CB  THR A 275     2961   5778   4884   -283   -604    687       C  
ATOM   2081  OG1 THR A 275      57.919  19.588  19.978  1.00 39.11           O  
ANISOU 2081  OG1 THR A 275     3329   6233   5300   -320   -546    718       O  
ATOM   2082  CG2 THR A 275      58.719  18.041  21.697  1.00 29.61           C  
ANISOU 2082  CG2 THR A 275     2086   5099   4065   -153   -594    688       C  
ATOM   2083  N   ARG A 276      54.696  20.157  20.355  1.00 36.38           N  
ANISOU 2083  N   ARG A 276     3320   5518   4984   -334   -539    630       N  
ATOM   2084  CA  ARG A 276      53.909  21.287  19.845  1.00 36.73           C  
ANISOU 2084  CA  ARG A 276     3435   5472   5048   -431   -541    635       C  
ATOM   2085  C   ARG A 276      52.744  21.726  20.760  1.00 37.92           C  
ANISOU 2085  C   ARG A 276     3722   5477   5208   -443   -577    592       C  
ATOM   2086  O   ARG A 276      52.058  20.902  21.348  1.00 31.56           O  
ANISOU 2086  O   ARG A 276     2981   4617   4394   -353   -566    554       O  
ATOM   2087  CB  ARG A 276      53.382  20.977  18.442  1.00 35.61           C  
ANISOU 2087  CB  ARG A 276     3301   5327   4902   -398   -464    643       C  
ATOM   2088  CG  ARG A 276      54.506  20.821  17.443  1.00 42.64           C  
ANISOU 2088  CG  ARG A 276     4060   6361   5779   -406   -427    689       C  
ATOM   2089  CD  ARG A 276      55.337  22.089  17.381  1.00 47.92           C  
ANISOU 2089  CD  ARG A 276     4663   7085   6461   -548   -472    737       C  
ATOM   2090  NE  ARG A 276      56.464  21.950  16.472  1.00 61.56           N  
ANISOU 2090  NE  ARG A 276     6251   8965   8173   -559   -436    787       N  
ATOM   2091  CZ  ARG A 276      57.739  21.818  16.856  1.00 65.23           C  
ANISOU 2091  CZ  ARG A 276     6591   9565   8629   -570   -462    815       C  
ATOM   2092  NH1 ARG A 276      58.064  21.820  18.151  1.00 61.67           N  
ANISOU 2092  NH1 ARG A 276     6139   9109   8183   -574   -529    798       N  
ATOM   2093  NH2 ARG A 276      58.692  21.694  15.938  1.00 60.73           N  
ANISOU 2093  NH2 ARG A 276     5892   9142   8041   -575   -420    862       N  
ATOM   2094  N   PRO A 277      52.562  23.044  20.907  1.00 38.29           N  
ANISOU 2094  N   PRO A 277     3813   5464   5270   -555   -623    601       N  
ATOM   2095  CA  PRO A 277      51.416  23.602  21.624  1.00 28.37           C  
ANISOU 2095  CA  PRO A 277     2689   4072   4019   -565   -652    562       C  
ATOM   2096  C   PRO A 277      50.132  23.001  21.052  1.00 33.80           C  
ANISOU 2096  C   PRO A 277     3449   4689   4705   -485   -589    537       C  
ATOM   2097  O   PRO A 277      50.015  22.914  19.838  1.00 35.96           O  
ANISOU 2097  O   PRO A 277     3696   4986   4980   -485   -537    558       O  
ATOM   2098  CB  PRO A 277      51.475  25.095  21.261  1.00 36.31           C  
ANISOU 2098  CB  PRO A 277     3720   5037   5040   -695   -689    588       C  
ATOM   2099  CG  PRO A 277      52.980  25.391  21.024  1.00 28.17           C  
ANISOU 2099  CG  PRO A 277     2561   4133   4010   -776   -715    638       C  
ATOM   2100  CD  PRO A 277      53.564  24.066  20.511  1.00 34.86           C  
ANISOU 2100  CD  PRO A 277     3302   5099   4844   -679   -656    649       C  
ATOM   2101  N   ALA A 278      49.209  22.556  21.898  1.00 31.08           N  
ANISOU 2101  N   ALA A 278     3190   4267   4353   -420   -592    494       N  
ATOM   2102  CA  ALA A 278      47.888  22.153  21.406  1.00 35.04           C  
ANISOU 2102  CA  ALA A 278     3766   4696   4852   -363   -540    471       C  
ATOM   2103  C   ALA A 278      47.369  23.091  20.317  1.00 31.88           C  
ANISOU 2103  C   ALA A 278     3391   4257   4464   -425   -522    490       C  
ATOM   2104  O   ALA A 278      46.943  22.642  19.261  1.00 32.54           O  
ANISOU 2104  O   ALA A 278     3466   4351   4545   -392   -466    497       O  
ATOM   2105  CB  ALA A 278      46.871  22.029  22.568  1.00 23.55           C  
ANISOU 2105  CB  ALA A 278     2409   3151   3387   -321   -560    428       C  
ATOM   2106  N   GLN A 279      47.435  24.394  20.543  1.00 35.61           N  
ANISOU 2106  N   GLN A 279     3897   4685   4946   -513   -571    500       N  
ATOM   2107  CA  GLN A 279      46.749  25.317  19.621  1.00 33.15           C  
ANISOU 2107  CA  GLN A 279     3635   4317   4644   -561   -558    515       C  
ATOM   2108  C   GLN A 279      47.384  25.321  18.231  1.00 35.86           C  
ANISOU 2108  C   GLN A 279     3898   4737   4990   -597   -518    561       C  
ATOM   2109  O   GLN A 279      46.679  25.550  17.240  1.00 33.29           O  
ANISOU 2109  O   GLN A 279     3604   4381   4665   -596   -482    571       O  
ATOM   2110  CB  GLN A 279      46.666  26.743  20.196  1.00 29.05           C  
ANISOU 2110  CB  GLN A 279     3188   3720   4132   -646   -624    514       C  
ATOM   2111  CG  GLN A 279      45.821  27.707  19.380  1.00 31.03           C  
ANISOU 2111  CG  GLN A 279     3510   3894   4387   -680   -615    525       C  
ATOM   2112  CD  GLN A 279      44.347  27.346  19.450  1.00 36.26           C  
ANISOU 2112  CD  GLN A 279     4250   4487   5042   -593   -582    488       C  
ATOM   2113  OE1 GLN A 279      43.795  27.154  20.536  1.00 39.44           O  
ANISOU 2113  OE1 GLN A 279     4706   4845   5435   -546   -601    448       O  
ATOM   2114  NE2 GLN A 279      43.722  27.201  18.296  1.00 36.36           N  
ANISOU 2114  NE2 GLN A 279     4262   4500   5054   -572   -532    501       N  
ATOM   2115  N   ASP A 280      48.702  25.075  18.146  1.00 32.73           N  
ANISOU 2115  N   ASP A 280     3397   4447   4593   -624   -524    591       N  
ATOM   2116  CA  ASP A 280      49.365  24.953  16.836  1.00 28.64           C  
ANISOU 2116  CA  ASP A 280     2791   4019   4070   -647   -478    636       C  
ATOM   2117  C   ASP A 280      48.798  23.788  16.021  1.00 32.01           C  
ANISOU 2117  C   ASP A 280     3213   4467   4483   -545   -406    621       C  
ATOM   2118  O   ASP A 280      48.671  23.897  14.814  1.00 39.55           O  
ANISOU 2118  O   ASP A 280     4153   5443   5432   -557   -363    645       O  
ATOM   2119  CB  ASP A 280      50.879  24.714  16.980  1.00 38.42           C  
ANISOU 2119  CB  ASP A 280     3906   5386   5304   -675   -493    668       C  
ATOM   2120  CG  ASP A 280      51.655  25.968  17.369  1.00 55.26           C  
ANISOU 2120  CG  ASP A 280     6020   7526   7449   -806   -560    700       C  
ATOM   2121  OD1 ASP A 280      51.031  27.029  17.596  1.00 61.55           O  
ANISOU 2121  OD1 ASP A 280     6913   8216   8256   -871   -598    694       O  
ATOM   2122  OD2 ASP A 280      52.910  25.888  17.460  1.00 68.35           O  
ANISOU 2122  OD2 ASP A 280     7569   9299   9104   -844   -576    732       O  
ATOM   2123  N   LEU A 281      48.509  22.656  16.679  1.00 33.80           N  
ANISOU 2123  N   LEU A 281     3454   4688   4702   -449   -393    582       N  
ATOM   2124  CA  LEU A 281      47.926  21.501  15.991  1.00 32.80           C  
ANISOU 2124  CA  LEU A 281     3337   4567   4559   -356   -331    563       C  
ATOM   2125  C   LEU A 281      46.553  21.893  15.479  1.00 30.46           C  
ANISOU 2125  C   LEU A 281     3131   4178   4266   -360   -314    549       C  
ATOM   2126  O   LEU A 281      46.226  21.642  14.316  1.00 32.17           O  
ANISOU 2126  O   LEU A 281     3342   4409   4471   -343   -266    558       O  
ATOM   2127  CB  LEU A 281      47.832  20.256  16.906  1.00 30.47           C  
ANISOU 2127  CB  LEU A 281     3056   4268   4253   -260   -328    526       C  
ATOM   2128  CG  LEU A 281      49.216  19.791  17.458  1.00 30.92           C  
ANISOU 2128  CG  LEU A 281     3020   4424   4304   -240   -348    541       C  
ATOM   2129  CD1 LEU A 281      49.123  18.524  18.272  1.00 27.02           C  
ANISOU 2129  CD1 LEU A 281     2547   3923   3795   -139   -343    508       C  
ATOM   2130  CD2 LEU A 281      50.163  19.573  16.318  1.00 29.95           C  
ANISOU 2130  CD2 LEU A 281     2798   4413   4170   -239   -308    577       C  
ATOM   2131  N   VAL A 282      45.763  22.544  16.336  1.00 35.92           N  
ANISOU 2131  N   VAL A 282     3902   4777   4968   -380   -353    526       N  
ATOM   2132  CA  VAL A 282      44.407  22.947  15.953  1.00 33.59           C  
ANISOU 2132  CA  VAL A 282     3690   4399   4673   -376   -340    512       C  
ATOM   2133  C   VAL A 282      44.496  23.908  14.775  1.00 35.64           C  
ANISOU 2133  C   VAL A 282     3940   4665   4936   -444   -332    551       C  
ATOM   2134  O   VAL A 282      43.759  23.751  13.813  1.00 34.63           O  
ANISOU 2134  O   VAL A 282     3834   4525   4799   -422   -293    553       O  
ATOM   2135  CB  VAL A 282      43.606  23.578  17.130  1.00 36.16           C  
ANISOU 2135  CB  VAL A 282     4101   4632   5005   -382   -386    482       C  
ATOM   2136  CG1 VAL A 282      42.366  24.305  16.610  1.00 33.31           C  
ANISOU 2136  CG1 VAL A 282     3814   4198   4646   -390   -378    478       C  
ATOM   2137  CG2 VAL A 282      43.190  22.492  18.141  1.00 31.45           C  
ANISOU 2137  CG2 VAL A 282     3527   4023   4399   -304   -381    443       C  
ATOM   2138  N   ASP A 283      45.434  24.864  14.827  1.00 36.14           N  
ANISOU 2138  N   ASP A 283     3971   4752   5010   -530   -368    586       N  
ATOM   2139  CA  ASP A 283      45.549  25.864  13.762  1.00 37.84           C  
ANISOU 2139  CA  ASP A 283     4185   4967   5226   -605   -364    630       C  
ATOM   2140  C   ASP A 283      45.825  25.283  12.373  1.00 39.23           C  
ANISOU 2140  C   ASP A 283     4298   5223   5384   -586   -302    657       C  
ATOM   2141  O   ASP A 283      45.595  25.951  11.382  1.00 37.71           O  
ANISOU 2141  O   ASP A 283     4121   5021   5187   -628   -288    688       O  
ATOM   2142  CB  ASP A 283      46.633  26.932  14.079  1.00 28.84           C  
ANISOU 2142  CB  ASP A 283     3014   3846   4097   -714   -416    667       C  
ATOM   2143  CG  ASP A 283      46.212  27.901  15.210  1.00 42.08           C  
ANISOU 2143  CG  ASP A 283     4783   5419   5786   -752   -484    645       C  
ATOM   2144  OD1 ASP A 283      45.031  27.897  15.626  1.00 36.68           O  
ANISOU 2144  OD1 ASP A 283     4186   4650   5101   -697   -486    606       O  
ATOM   2145  OD2 ASP A 283      47.088  28.672  15.693  1.00 55.89           O  
ANISOU 2145  OD2 ASP A 283     6516   7176   7543   -840   -536    667       O  
ATOM   2146  N   HIS A 284      46.353  24.067  12.280  1.00 38.37           N  
ANISOU 2146  N   HIS A 284     4121   5193   5263   -520   -266    647       N  
ATOM   2147  CA  HIS A 284      46.716  23.558  10.956  1.00 32.94           C  
ANISOU 2147  CA  HIS A 284     3375   4587   4553   -500   -208    672       C  
ATOM   2148  C   HIS A 284      45.920  22.333  10.515  1.00 32.84           C  
ANISOU 2148  C   HIS A 284     3390   4566   4521   -400   -159    634       C  
ATOM   2149  O   HIS A 284      46.014  21.894   9.353  1.00 32.57           O  
ANISOU 2149  O   HIS A 284     3327   4585   4464   -376   -110    647       O  
ATOM   2150  CB  HIS A 284      48.205  23.246  10.925  1.00 30.27           C  
ANISOU 2150  CB  HIS A 284     2923   4370   4208   -513   -200    702       C  
ATOM   2151  CG  HIS A 284      49.059  24.470  10.913  1.00 36.13           C  
ANISOU 2151  CG  HIS A 284     3624   5143   4962   -630   -237    753       C  
ATOM   2152  ND1 HIS A 284      49.672  24.959  12.044  1.00 44.29           N  
ANISOU 2152  ND1 HIS A 284     4642   6173   6014   -683   -297    754       N  
ATOM   2153  CD2 HIS A 284      49.376  25.320   9.910  1.00 40.00           C  
ANISOU 2153  CD2 HIS A 284     4091   5663   5445   -711   -225    805       C  
ATOM   2154  CE1 HIS A 284      50.358  26.047  11.731  1.00 49.19           C  
ANISOU 2154  CE1 HIS A 284     5230   6820   6640   -797   -321    806       C  
ATOM   2155  NE2 HIS A 284      50.190  26.291  10.444  1.00 47.07           N  
ANISOU 2155  NE2 HIS A 284     4956   6571   6356   -817   -277    839       N  
ATOM   2156  N   GLU A 285      45.121  21.795  11.417  1.00 27.58           N  
ANISOU 2156  N   GLU A 285     2783   3833   3862   -347   -173    589       N  
ATOM   2157  CA  GLU A 285      44.517  20.489  11.145  1.00 35.09           C  
ANISOU 2157  CA  GLU A 285     3756   4781   4794   -257   -132    554       C  
ATOM   2158  C   GLU A 285      43.669  20.488   9.869  1.00 37.72           C  
ANISOU 2158  C   GLU A 285     4123   5099   5110   -251    -95    556       C  
ATOM   2159  O   GLU A 285      43.703  19.540   9.089  1.00 37.23           O  
ANISOU 2159  O   GLU A 285     4046   5077   5021   -198    -52    547       O  
ATOM   2160  CB  GLU A 285      43.746  19.975  12.352  1.00 32.97           C  
ANISOU 2160  CB  GLU A 285     3550   4443   4535   -213   -155    510       C  
ATOM   2161  CG  GLU A 285      42.499  20.781  12.680  1.00 43.22           C  
ANISOU 2161  CG  GLU A 285     4927   5648   5845   -241   -180    497       C  
ATOM   2162  CD  GLU A 285      41.615  20.098  13.744  1.00 47.77           C  
ANISOU 2162  CD  GLU A 285     5561   6167   6423   -189   -189    454       C  
ATOM   2163  OE1 GLU A 285      40.567  20.676  14.120  1.00 44.41           O  
ANISOU 2163  OE1 GLU A 285     5196   5675   6003   -199   -207    441       O  
ATOM   2164  OE2 GLU A 285      41.988  18.988  14.198  1.00 45.76           O  
ANISOU 2164  OE2 GLU A 285     5291   5938   6159   -135   -178    437       O  
ATOM   2165  N   TRP A 286      42.978  21.586   9.617  1.00 34.93           N  
ANISOU 2165  N   TRP A 286     3814   4692   4767   -306   -114    571       N  
ATOM   2166  CA  TRP A 286      42.044  21.662   8.505  1.00 35.61           C  
ANISOU 2166  CA  TRP A 286     3938   4757   4835   -300    -87    573       C  
ATOM   2167  C   TRP A 286      42.760  21.741   7.142  1.00 40.85           C  
ANISOU 2167  C   TRP A 286     4547   5499   5473   -320    -49    612       C  
ATOM   2168  O   TRP A 286      42.178  21.413   6.114  1.00 45.33           O  
ANISOU 2168  O   TRP A 286     5134   6073   6016   -295    -17    609       O  
ATOM   2169  CB  TRP A 286      41.117  22.855   8.726  1.00 33.58           C  
ANISOU 2169  CB  TRP A 286     3747   4420   4594   -343   -123    579       C  
ATOM   2170  CG  TRP A 286      39.796  22.791   8.041  1.00 45.94           C  
ANISOU 2170  CG  TRP A 286     5366   5945   6144   -317   -108    565       C  
ATOM   2171  CD1 TRP A 286      39.375  21.867   7.113  1.00 46.18           C  
ANISOU 2171  CD1 TRP A 286     5393   6005   6147   -273    -67    552       C  
ATOM   2172  CD2 TRP A 286      38.734  23.756   8.154  1.00 53.47           C  
ANISOU 2172  CD2 TRP A 286     6384   6827   7106   -334   -136    566       C  
ATOM   2173  NE1 TRP A 286      38.114  22.190   6.665  1.00 48.36           N  
ANISOU 2173  NE1 TRP A 286     5722   6237   6415   -268    -70    545       N  
ATOM   2174  CE2 TRP A 286      37.697  23.341   7.286  1.00 54.01           C  
ANISOU 2174  CE2 TRP A 286     6477   6893   7153   -300   -110    555       C  
ATOM   2175  CE3 TRP A 286      38.560  24.931   8.908  1.00 53.22           C  
ANISOU 2175  CE3 TRP A 286     6394   6732   7094   -371   -182    573       C  
ATOM   2176  CZ2 TRP A 286      36.490  24.064   7.159  1.00 51.48           C  
ANISOU 2176  CZ2 TRP A 286     6213   6518   6831   -297   -128    553       C  
ATOM   2177  CZ3 TRP A 286      37.370  25.633   8.783  1.00 52.32           C  
ANISOU 2177  CZ3 TRP A 286     6344   6557   6977   -362   -197    570       C  
ATOM   2178  CH2 TRP A 286      36.354  25.200   7.906  1.00 51.70           C  
ANISOU 2178  CH2 TRP A 286     6280   6487   6878   -324   -170    562       C  
ATOM   2179  N   HIS A 287      44.032  22.126   7.148  1.00 35.73           N  
ANISOU 2179  N   HIS A 287     3828   4918   4829   -363    -53    649       N  
ATOM   2180  CA  HIS A 287      44.812  22.290   5.921  1.00 39.87           C  
ANISOU 2180  CA  HIS A 287     4292   5529   5327   -388    -15    692       C  
ATOM   2181  C   HIS A 287      45.227  20.986   5.235  1.00 43.55           C  
ANISOU 2181  C   HIS A 287     4714   6073   5757   -308     40    676       C  
ATOM   2182  O   HIS A 287      45.714  21.001   4.118  1.00 46.06           O  
ANISOU 2182  O   HIS A 287     4991   6465   6046   -314     79    707       O  
ATOM   2183  CB  HIS A 287      46.064  23.135   6.204  1.00 43.43           C  
ANISOU 2183  CB  HIS A 287     4673   6036   5792   -469    -38    740       C  
ATOM   2184  CG  HIS A 287      45.754  24.511   6.706  1.00 56.23           C  
ANISOU 2184  CG  HIS A 287     6346   7579   7442   -556    -93    761       C  
ATOM   2185  ND1 HIS A 287      46.535  25.161   7.638  1.00 62.07           N  
ANISOU 2185  ND1 HIS A 287     7059   8321   8206   -621   -139    778       N  
ATOM   2186  CD2 HIS A 287      44.732  25.354   6.418  1.00 60.51           C  
ANISOU 2186  CD2 HIS A 287     6970   8033   7987   -585   -110    765       C  
ATOM   2187  CE1 HIS A 287      46.014  26.348   7.895  1.00 64.71           C  
ANISOU 2187  CE1 HIS A 287     7464   8565   8557   -687   -184    790       C  
ATOM   2188  NE2 HIS A 287      44.920  26.490   7.165  1.00 63.82           N  
ANISOU 2188  NE2 HIS A 287     7419   8398   8433   -662   -166    784       N  
ATOM   2189  N   VAL A 288      45.011  19.847   5.870  1.00 39.64           N  
ANISOU 2189  N   VAL A 288     4238   5562   5262   -230     44    629       N  
ATOM   2190  CA  VAL A 288      45.482  18.609   5.256  1.00 38.94           C  
ANISOU 2190  CA  VAL A 288     4117   5542   5137   -148     92    612       C  
ATOM   2191  C   VAL A 288      44.480  17.828   4.415  1.00 37.46           C  
ANISOU 2191  C   VAL A 288     3994   5319   4918    -95    123    578       C  
ATOM   2192  O   VAL A 288      44.826  16.742   3.928  1.00 34.27           O  
ANISOU 2192  O   VAL A 288     3580   4961   4480    -21    161    558       O  
ATOM   2193  CB  VAL A 288      46.068  17.640   6.304  1.00 35.47           C  
ANISOU 2193  CB  VAL A 288     3655   5118   4704    -83     84    583       C  
ATOM   2194  CG1 VAL A 288      47.109  18.369   7.146  1.00 35.23           C  
ANISOU 2194  CG1 VAL A 288     3554   5131   4701   -136     49    616       C  
ATOM   2195  CG2 VAL A 288      44.960  17.028   7.168  1.00 26.76           C  
ANISOU 2195  CG2 VAL A 288     2639   3914   3615    -45     62    534       C  
ATOM   2196  N   LEU A 289      43.256  18.344   4.258  1.00 32.51           N  
ANISOU 2196  N   LEU A 289     3436   4615   4301   -127    105    571       N  
ATOM   2197  CA  LEU A 289      42.258  17.711   3.369  1.00 38.02           C  
ANISOU 2197  CA  LEU A 289     4192   5286   4967    -90    130    543       C  
ATOM   2198  C   LEU A 289      42.723  17.702   1.911  1.00 36.90           C  
ANISOU 2198  C   LEU A 289     4020   5221   4781    -86    174    568       C  
ATOM   2199  O   LEU A 289      43.250  18.679   1.440  1.00 46.04           O  
ANISOU 2199  O   LEU A 289     5135   6420   5938   -143    177    617       O  
ATOM   2200  CB  LEU A 289      40.879  18.400   3.465  1.00 29.28           C  
ANISOU 2200  CB  LEU A 289     3152   4095   3877   -129     99    537       C  
ATOM   2201  CG  LEU A 289      40.051  18.150   4.729  1.00 36.41           C  
ANISOU 2201  CG  LEU A 289     4103   4921   4810   -117     65    501       C  
ATOM   2202  CD1 LEU A 289      38.690  18.882   4.687  1.00 33.86           C  
ANISOU 2202  CD1 LEU A 289     3836   4531   4497   -147     40    499       C  
ATOM   2203  CD2 LEU A 289      39.870  16.659   4.966  1.00 30.99           C  
ANISOU 2203  CD2 LEU A 289     3442   4225   4106    -47     82    456       C  
ATOM   2204  N   PRO A 290      42.506  16.596   1.185  1.00 42.10           N  
ANISOU 2204  N   PRO A 290     4704   5894   5397    -20    208    536       N  
ATOM   2205  CA  PRO A 290      43.064  16.487  -0.181  1.00 40.86           C  
ANISOU 2205  CA  PRO A 290     4516   5820   5189     -3    255    556       C  
ATOM   2206  C   PRO A 290      42.331  17.353  -1.220  1.00 45.03           C  
ANISOU 2206  C   PRO A 290     5072   6337   5700    -57    256    583       C  
ATOM   2207  O   PRO A 290      42.932  17.695  -2.234  1.00 42.39           O  
ANISOU 2207  O   PRO A 290     4698   6076   5330    -69    289    620       O  
ATOM   2208  CB  PRO A 290      42.888  15.002  -0.538  1.00 41.91           C  
ANISOU 2208  CB  PRO A 290     4692   5951   5281     88    283    503       C  
ATOM   2209  CG  PRO A 290      42.006  14.408   0.560  1.00 41.81           C  
ANISOU 2209  CG  PRO A 290     4744   5843   5300    103    248    458       C  
ATOM   2210  CD  PRO A 290      41.584  15.500   1.511  1.00 34.73           C  
ANISOU 2210  CD  PRO A 290     3843   4895   4458     32    202    480       C  
ATOM   2211  N   GLN A 291      41.063  17.691  -0.981  1.00 43.43           N  
ANISOU 2211  N   GLN A 291     4933   6049   5517    -83    221    568       N  
ATOM   2212  CA  GLN A 291      40.332  18.594  -1.884  1.00 46.53           C  
ANISOU 2212  CA  GLN A 291     5354   6429   5895   -130    215    597       C  
ATOM   2213  C   GLN A 291      39.469  19.613  -1.115  1.00 44.44           C  
ANISOU 2213  C   GLN A 291     5123   6084   5677   -182    165    607       C  
ATOM   2214  O   GLN A 291      39.208  19.433   0.068  1.00 42.22           O  
ANISOU 2214  O   GLN A 291     4856   5752   5433   -175    137    581       O  
ATOM   2215  CB  GLN A 291      39.435  17.806  -2.856  1.00 44.59           C  
ANISOU 2215  CB  GLN A 291     5163   6176   5602    -90    231    562       C  
ATOM   2216  CG  GLN A 291      40.067  16.601  -3.533  1.00 43.98           C  
ANISOU 2216  CG  GLN A 291     5079   6158   5475    -22    277    535       C  
ATOM   2217  CD  GLN A 291      39.783  15.290  -2.788  1.00 54.96           C  
ANISOU 2217  CD  GLN A 291     6508   7503   6870     37    271    474       C  
ATOM   2218  OE1 GLN A 291      40.386  14.235  -3.084  1.00 58.14           O  
ANISOU 2218  OE1 GLN A 291     6912   7942   7237    103    303    447       O  
ATOM   2219  NE2 GLN A 291      38.862  15.345  -1.821  1.00 46.99           N  
ANISOU 2219  NE2 GLN A 291     5536   6415   5903     16    230    454       N  
ATOM   2220  N   GLU A 292      39.047  20.682  -1.788  1.00 46.21           N  
ANISOU 2220  N   GLU A 292     5365   6298   5894   -230    154    646       N  
ATOM   2221  CA  GLU A 292      38.127  21.651  -1.221  1.00 46.40           C  
ANISOU 2221  CA  GLU A 292     5432   6247   5952   -265    108    654       C  
ATOM   2222  C   GLU A 292      36.861  20.879  -0.980  1.00 39.35           C  
ANISOU 2222  C   GLU A 292     4588   5307   5057   -222     96    602       C  
ATOM   2223  O   GLU A 292      36.351  20.269  -1.907  1.00 43.21           O  
ANISOU 2223  O   GLU A 292     5096   5816   5505   -196    114    586       O  
ATOM   2224  CB  GLU A 292      37.867  22.780  -2.226  1.00 56.04           C  
ANISOU 2224  CB  GLU A 292     6671   7469   7152   -309    104    705       C  
ATOM   2225  CG  GLU A 292      37.154  24.002  -1.648  1.00 66.74           C  
ANISOU 2225  CG  GLU A 292     8070   8746   8541   -346     56    723       C  
ATOM   2226  CD  GLU A 292      36.800  25.045  -2.731  1.00 85.31           C  
ANISOU 2226  CD  GLU A 292    10453  11095  10866   -380     50    773       C  
ATOM   2227  OE1 GLU A 292      37.376  24.970  -3.850  1.00 89.95           O  
ANISOU 2227  OE1 GLU A 292    11015  11748  11412   -391     85    804       O  
ATOM   2228  OE2 GLU A 292      35.952  25.946  -2.469  1.00 89.11           O  
ANISOU 2228  OE2 GLU A 292    10985  11510  11363   -390     11    783       O  
ATOM   2229  N   SER A 293      36.352  20.869   0.248  1.00 37.82           N  
ANISOU 2229  N   SER A 293     4413   5056   4902   -216     65    576       N  
ATOM   2230  CA  SER A 293      35.249  19.954   0.570  1.00 33.21           C  
ANISOU 2230  CA  SER A 293     3866   4439   4314   -178     58    527       C  
ATOM   2231  C   SER A 293      34.232  20.567   1.473  1.00 31.34           C  
ANISOU 2231  C   SER A 293     3659   4140   4108   -187     19    520       C  
ATOM   2232  O   SER A 293      34.489  21.582   2.101  1.00 29.87           O  
ANISOU 2232  O   SER A 293     3472   3926   3951   -214     -4    543       O  
ATOM   2233  CB  SER A 293      35.767  18.731   1.333  1.00 35.82           C  
ANISOU 2233  CB  SER A 293     4185   4774   4652   -141     72    489       C  
ATOM   2234  OG  SER A 293      36.970  18.254   0.812  1.00 42.69           O  
ANISOU 2234  OG  SER A 293     5016   5704   5500   -124    106    498       O  
ATOM   2235  N   ILE A 294      33.069  19.919   1.566  1.00 36.07           N  
ANISOU 2235  N   ILE A 294     4287   4720   4698   -164     13    485       N  
ATOM   2236  CA  ILE A 294      32.247  20.050   2.761  1.00 35.26           C  
ANISOU 2236  CA  ILE A 294     4203   4569   4625   -157    -15    465       C  
ATOM   2237  C   ILE A 294      31.871  18.654   3.237  1.00 33.81           C  
ANISOU 2237  C   ILE A 294     4030   4381   4435   -131     -5    421       C  
ATOM   2238  O   ILE A 294      31.976  17.692   2.483  1.00 33.91           O  
ANISOU 2238  O   ILE A 294     4048   4420   4417   -118     18    404       O  
ATOM   2239  CB  ILE A 294      31.018  20.904   2.551  1.00 37.68           C  
ANISOU 2239  CB  ILE A 294     4534   4855   4929   -161    -40    476       C  
ATOM   2240  CG1 ILE A 294      30.143  20.309   1.464  1.00 35.83           C  
ANISOU 2240  CG1 ILE A 294     4309   4650   4654   -152    -31    465       C  
ATOM   2241  CG2 ILE A 294      31.416  22.363   2.266  1.00 36.93           C  
ANISOU 2241  CG2 ILE A 294     4443   4746   4842   -186    -56    522       C  
ATOM   2242  CD1 ILE A 294      28.911  21.125   1.233  1.00 37.54           C  
ANISOU 2242  CD1 ILE A 294     4542   4858   4865   -148    -57    477       C  
ATOM   2243  N   PHE A 295      31.496  18.541   4.506  1.00 31.66           N  
ANISOU 2243  N   PHE A 295     3767   4074   4189   -124    -21    403       N  
ATOM   2244  CA  PHE A 295      31.181  17.249   5.106  1.00 28.14           C  
ANISOU 2244  CA  PHE A 295     3337   3618   3739   -105    -14    366       C  
ATOM   2245  C   PHE A 295      32.385  16.309   4.940  1.00 31.44           C  
ANISOU 2245  C   PHE A 295     3744   4054   4146    -86     12    356       C  
ATOM   2246  O   PHE A 295      32.220  15.128   4.644  1.00 29.49           O  
ANISOU 2246  O   PHE A 295     3520   3808   3875    -70     26    329       O  
ATOM   2247  CB  PHE A 295      29.895  16.641   4.490  1.00 24.15           C  
ANISOU 2247  CB  PHE A 295     2852   3119   3205   -109    -14    347       C  
ATOM   2248  CG  PHE A 295      28.950  16.003   5.513  1.00 29.57           C  
ANISOU 2248  CG  PHE A 295     3555   3781   3899   -108    -24    322       C  
ATOM   2249  CD1 PHE A 295      29.431  15.069   6.449  1.00 25.65           C  
ANISOU 2249  CD1 PHE A 295     3072   3262   3411    -96    -17    301       C  
ATOM   2250  CD2 PHE A 295      27.574  16.350   5.548  1.00 27.60           C  
ANISOU 2250  CD2 PHE A 295     3307   3537   3645   -118    -41    322       C  
ATOM   2251  CE1 PHE A 295      28.580  14.470   7.384  1.00 30.86           C  
ANISOU 2251  CE1 PHE A 295     3749   3901   4074   -100    -24    283       C  
ATOM   2252  CE2 PHE A 295      26.687  15.749   6.483  1.00 21.50           C  
ANISOU 2252  CE2 PHE A 295     2542   2753   2875   -122    -47    303       C  
ATOM   2253  CZ  PHE A 295      27.176  14.822   7.405  1.00 29.97           C  
ANISOU 2253  CZ  PHE A 295     3631   3800   3955   -117    -37    285       C  
ATOM   2254  N   ARG A 296      33.597  16.855   5.115  1.00 29.11           N  
ANISOU 2254  N   ARG A 296     3418   3775   3867    -89     15    379       N  
ATOM   2255  CA  ARG A 296      34.814  16.033   5.223  1.00 31.13           C  
ANISOU 2255  CA  ARG A 296     3654   4055   4117    -61     36    371       C  
ATOM   2256  C   ARG A 296      35.689  16.543   6.356  1.00 29.40           C  
ANISOU 2256  C   ARG A 296     3407   3831   3933    -66     19    384       C  
ATOM   2257  O   ARG A 296      35.799  17.749   6.585  1.00 29.72           O  
ANISOU 2257  O   ARG A 296     3433   3864   3994   -100     -1    411       O  
ATOM   2258  CB  ARG A 296      35.622  15.966   3.912  1.00 31.23           C  
ANISOU 2258  CB  ARG A 296     3643   4124   4100    -54     66    388       C  
ATOM   2259  CG  ARG A 296      34.901  15.315   2.687  1.00 31.62           C  
ANISOU 2259  CG  ARG A 296     3725   4185   4106    -44     83    370       C  
ATOM   2260  CD  ARG A 296      34.720  13.791   2.759  1.00 31.29           C  
ANISOU 2260  CD  ARG A 296     3724   4125   4040     -5     96    326       C  
ATOM   2261  NE  ARG A 296      34.163  13.290   1.503  1.00 33.36           N  
ANISOU 2261  NE  ARG A 296     4019   4401   4257     -2    109    311       N  
ATOM   2262  CZ  ARG A 296      32.855  13.229   1.243  1.00 33.93           C  
ANISOU 2262  CZ  ARG A 296     4124   4450   4319    -28     90    298       C  
ATOM   2263  NH1 ARG A 296      31.972  13.600   2.164  1.00 29.01           N  
ANISOU 2263  NH1 ARG A 296     3503   3792   3726    -52     63    299       N  
ATOM   2264  NH2 ARG A 296      32.434  12.802   0.068  1.00 32.32           N  
ANISOU 2264  NH2 ARG A 296     3947   4262   4069    -27     99    285       N  
ATOM   2265  N   PHE A 297      36.340  15.636   7.069  1.00 25.55           N  
ANISOU 2265  N   PHE A 297     2915   3344   3447    -32     25    366       N  
ATOM   2266  CA  PHE A 297      37.050  16.042   8.281  1.00 23.04           C  
ANISOU 2266  CA  PHE A 297     2574   3019   3159    -36      3    374       C  
ATOM   2267  C   PHE A 297      38.440  15.406   8.307  1.00 32.75           C  
ANISOU 2267  C   PHE A 297     3764   4298   4382     -2     20    378       C  
ATOM   2268  O   PHE A 297      38.603  14.235   7.926  1.00 32.29           O  
ANISOU 2268  O   PHE A 297     3720   4251   4297     46     45    357       O  
ATOM   2269  CB  PHE A 297      36.213  15.674   9.491  1.00 27.37           C  
ANISOU 2269  CB  PHE A 297     3164   3514   3720    -27    -17    349       C  
ATOM   2270  CG  PHE A 297      34.722  15.982   9.303  1.00 28.80           C  
ANISOU 2270  CG  PHE A 297     3381   3663   3898    -46    -24    341       C  
ATOM   2271  CD1 PHE A 297      34.269  17.299   9.308  1.00 26.27           C  
ANISOU 2271  CD1 PHE A 297     3059   3330   3593    -78    -45    361       C  
ATOM   2272  CD2 PHE A 297      33.807  14.962   9.075  1.00 29.01           C  
ANISOU 2272  CD2 PHE A 297     3445   3675   3904    -33    -12    316       C  
ATOM   2273  CE1 PHE A 297      32.892  17.611   9.089  1.00 30.88           C  
ANISOU 2273  CE1 PHE A 297     3669   3895   4170    -86    -52    355       C  
ATOM   2274  CE2 PHE A 297      32.436  15.249   8.876  1.00 28.37           C  
ANISOU 2274  CE2 PHE A 297     3385   3578   3817    -53    -20    312       C  
ATOM   2275  CZ  PHE A 297      31.977  16.580   8.887  1.00 24.34           C  
ANISOU 2275  CZ  PHE A 297     2864   3063   3321    -75    -39    332       C  
ATOM   2276  N   SER A 298      39.427  16.188   8.741  1.00 26.11           N  
ANISOU 2276  N   SER A 298     2873   3486   3561    -25      4    404       N  
ATOM   2277  CA  SER A 298      40.839  15.826   8.622  1.00 29.89           C  
ANISOU 2277  CA  SER A 298     3293   4032   4031      1     20    418       C  
ATOM   2278  C   SER A 298      41.222  14.573   9.391  1.00 27.78           C  
ANISOU 2278  C   SER A 298     3036   3762   3757     67     23    390       C  
ATOM   2279  O   SER A 298      41.768  13.635   8.825  1.00 35.37           O  
ANISOU 2279  O   SER A 298     3988   4761   4689    122     54    381       O  
ATOM   2280  CB  SER A 298      41.687  16.996   9.087  1.00 29.32           C  
ANISOU 2280  CB  SER A 298     3168   3988   3985    -52     -8    453       C  
ATOM   2281  OG  SER A 298      41.413  18.057   8.211  1.00 39.36           O  
ANISOU 2281  OG  SER A 298     4437   5262   5258   -108     -7    482       O  
ATOM   2282  N   PHE A 299      40.843  14.537  10.662  1.00 25.32           N  
ANISOU 2282  N   PHE A 299     2755   3400   3466     66     -7    376       N  
ATOM   2283  CA  PHE A 299      41.240  13.466  11.538  1.00 29.22           C  
ANISOU 2283  CA  PHE A 299     3263   3887   3954    124    -10    355       C  
ATOM   2284  C   PHE A 299      40.047  12.711  12.119  1.00 33.81           C  
ANISOU 2284  C   PHE A 299     3923   4394   4530    139    -14    324       C  
ATOM   2285  O   PHE A 299      39.353  13.211  13.033  1.00 30.15           O  
ANISOU 2285  O   PHE A 299     3485   3886   4086    108    -41    321       O  
ATOM   2286  CB  PHE A 299      42.190  14.039  12.588  1.00 27.41           C  
ANISOU 2286  CB  PHE A 299     2984   3684   3747    110    -43    373       C  
ATOM   2287  CG  PHE A 299      43.470  14.560  11.980  1.00 25.73           C  
ANISOU 2287  CG  PHE A 299     2685   3558   3533     97    -35    406       C  
ATOM   2288  CD1 PHE A 299      44.536  13.714  11.772  1.00 26.37           C  
ANISOU 2288  CD1 PHE A 299     2720   3706   3593    160    -14    408       C  
ATOM   2289  CD2 PHE A 299      43.580  15.883  11.583  1.00 28.02           C  
ANISOU 2289  CD2 PHE A 299     2941   3865   3839     21    -48    437       C  
ATOM   2290  CE1 PHE A 299      45.722  14.179  11.211  1.00 28.96           C  
ANISOU 2290  CE1 PHE A 299     2959   4129   3917    147     -3    442       C  
ATOM   2291  CE2 PHE A 299      44.773  16.373  11.006  1.00 32.07           C  
ANISOU 2291  CE2 PHE A 299     3370   4465   4349     -3    -40    473       C  
ATOM   2292  CZ  PHE A 299      45.846  15.496  10.818  1.00 28.05           C  
ANISOU 2292  CZ  PHE A 299     2805   4035   3819     60    -15    476       C  
ATOM   2293  N   VAL A 300      39.832  11.505  11.564  1.00 26.46           N  
ANISOU 2293  N   VAL A 300     3032   3451   3570    185     12    302       N  
ATOM   2294  CA  VAL A 300      38.660  10.674  11.873  1.00 23.47           C  
ANISOU 2294  CA  VAL A 300     2732   3006   3181    190     12    275       C  
ATOM   2295  C   VAL A 300      39.159   9.214  12.090  1.00 31.17           C  
ANISOU 2295  C   VAL A 300     3746   3967   4130    261     25    255       C  
ATOM   2296  O   VAL A 300      40.333   8.921  11.913  1.00 29.73           O  
ANISOU 2296  O   VAL A 300     3527   3832   3937    312     35    261       O  
ATOM   2297  CB  VAL A 300      37.631  10.708  10.697  1.00 19.04           C  
ANISOU 2297  CB  VAL A 300     2199   2433   2604    159     30    267       C  
ATOM   2298  CG1 VAL A 300      37.165  12.103  10.404  1.00 20.49           C  
ANISOU 2298  CG1 VAL A 300     2350   2628   2808    101     18    288       C  
ATOM   2299  CG2 VAL A 300      38.256  10.098   9.405  1.00 25.31           C  
ANISOU 2299  CG2 VAL A 300     2987   3265   3364    198     62    262       C  
ATOM   2300  N   PRO A 301      38.268   8.305  12.502  1.00 31.88           N  
ANISOU 2300  N   PRO A 301     3912   3993   4207    266     23    233       N  
ATOM   2301  CA  PRO A 301      38.695   6.898  12.632  1.00 29.90           C  
ANISOU 2301  CA  PRO A 301     3716   3716   3927    334     33    215       C  
ATOM   2302  C   PRO A 301      39.371   6.353  11.376  1.00 31.48           C  
ANISOU 2302  C   PRO A 301     3914   3952   4097    385     62    205       C  
ATOM   2303  O   PRO A 301      38.974   6.621  10.235  1.00 32.41           O  
ANISOU 2303  O   PRO A 301     4028   4085   4203    359     79    201       O  
ATOM   2304  CB  PRO A 301      37.375   6.158  12.909  1.00 27.64           C  
ANISOU 2304  CB  PRO A 301     3516   3354   3630    303     28    196       C  
ATOM   2305  CG  PRO A 301      36.609   7.186  13.766  1.00 26.04           C  
ANISOU 2305  CG  PRO A 301     3289   3146   3459    241      7    211       C  
ATOM   2306  CD  PRO A 301      36.911   8.528  13.035  1.00 30.07           C  
ANISOU 2306  CD  PRO A 301     3722   3714   3988    211      8    228       C  
ATOM   2307  N   VAL A 302      40.421   5.593  11.613  1.00 32.26           N  
ANISOU 2307  N   VAL A 302     4014   4066   4178    465     69    201       N  
ATOM   2308  CA  VAL A 302      41.210   5.041  10.554  1.00 32.23           C  
ANISOU 2308  CA  VAL A 302     4004   4104   4140    532     99    191       C  
ATOM   2309  C   VAL A 302      40.962   3.520  10.509  1.00 33.43           C  
ANISOU 2309  C   VAL A 302     4267   4184   4253    593    105    159       C  
ATOM   2310  O   VAL A 302      40.773   2.881  11.547  1.00 34.28           O  
ANISOU 2310  O   VAL A 302     4429   4232   4362    608     85    154       O  
ATOM   2311  CB  VAL A 302      42.723   5.361  10.788  1.00 31.78           C  
ANISOU 2311  CB  VAL A 302     3854   4135   4087    589    102    214       C  
ATOM   2312  CG1 VAL A 302      43.212   4.873  12.175  1.00 24.79           C  
ANISOU 2312  CG1 VAL A 302     2980   3230   3211    635     76    217       C  
ATOM   2313  CG2 VAL A 302      43.540   4.766   9.711  1.00 28.01           C  
ANISOU 2313  CG2 VAL A 302     3365   3709   3568    668    138    205       C  
ATOM   2314  N   VAL A 303      40.945   2.937   9.313  1.00 32.55           N  
ANISOU 2314  N   VAL A 303     4194   4071   4102    625    131    136       N  
ATOM   2315  CA  VAL A 303      40.811   1.492   9.209  1.00 36.48           C  
ANISOU 2315  CA  VAL A 303     4807   4495   4557    687    135    103       C  
ATOM   2316  C   VAL A 303      42.205   0.887   9.525  1.00 43.03           C  
ANISOU 2316  C   VAL A 303     5620   5363   5368    807    144    104       C  
ATOM   2317  O   VAL A 303      43.070   0.787   8.655  1.00 42.83           O  
ANISOU 2317  O   VAL A 303     5558   5403   5313    877    173    100       O  
ATOM   2318  CB  VAL A 303      40.297   1.109   7.847  1.00 37.26           C  
ANISOU 2318  CB  VAL A 303     4960   4579   4618    680    155     75       C  
ATOM   2319  CG1 VAL A 303      40.081  -0.410   7.748  1.00 34.54           C  
ANISOU 2319  CG1 VAL A 303     4754   4143   4228    736    153     38       C  
ATOM   2320  CG2 VAL A 303      39.015   1.837   7.599  1.00 31.07           C  
ANISOU 2320  CG2 VAL A 303     4172   3777   3856    566    142     81       C  
ATOM   2321  N   ASP A 304      42.417   0.559  10.797  1.00 40.46           N  
ANISOU 2321  N   ASP A 304     5312   5005   5057    830    120    113       N  
ATOM   2322  CA  ASP A 304      43.743   0.218  11.318  1.00 35.76           C  
ANISOU 2322  CA  ASP A 304     4676   4459   4452    936    121    124       C  
ATOM   2323  C   ASP A 304      43.992  -1.289  11.293  1.00 42.79           C  
ANISOU 2323  C   ASP A 304     5684   5281   5293   1043    125     95       C  
ATOM   2324  O   ASP A 304      45.094  -1.737  11.633  1.00 35.46           O  
ANISOU 2324  O   ASP A 304     4734   4391   4346   1151    128    100       O  
ATOM   2325  CB  ASP A 304      43.899   0.699  12.776  1.00 29.23           C  
ANISOU 2325  CB  ASP A 304     3806   3636   3663    910     87    151       C  
ATOM   2326  CG  ASP A 304      42.752   0.207  13.691  1.00 34.93           C  
ANISOU 2326  CG  ASP A 304     4632   4246   4393    856     61    144       C  
ATOM   2327  OD1 ASP A 304      41.768  -0.355  13.168  1.00 37.61           O  
ANISOU 2327  OD1 ASP A 304     5063   4511   4714    820     67    121       O  
ATOM   2328  OD2 ASP A 304      42.804   0.411  14.929  1.00 34.95           O  
ANISOU 2328  OD2 ASP A 304     4622   4240   4418    843     34    162       O  
ATOM   2329  N   GLY A 305      42.967  -2.054  10.918  1.00 39.56           N  
ANISOU 2329  N   GLY A 305     5400   4771   4861   1012    124     66       N  
ATOM   2330  CA  GLY A 305      43.010  -3.499  11.052  1.00 41.79           C  
ANISOU 2330  CA  GLY A 305     5820   4960   5099   1094    119     39       C  
ATOM   2331  C   GLY A 305      43.049  -3.905  12.512  1.00 46.81           C  
ANISOU 2331  C   GLY A 305     6495   5543   5750   1108     88     56       C  
ATOM   2332  O   GLY A 305      43.358  -5.043  12.831  1.00 43.45           O  
ANISOU 2332  O   GLY A 305     6171   5050   5288   1196     81     43       O  
ATOM   2333  N   ASP A 306      42.733  -2.968  13.408  1.00 46.89           N  
ANISOU 2333  N   ASP A 306     6429   5580   5808   1025     69     86       N  
ATOM   2334  CA  ASP A 306      42.761  -3.237  14.841  1.00 44.80           C  
ANISOU 2334  CA  ASP A 306     6193   5273   5554   1032     39    106       C  
ATOM   2335  C   ASP A 306      41.376  -2.967  15.469  1.00 44.99           C  
ANISOU 2335  C   ASP A 306     6257   5231   5604    905     20    114       C  
ATOM   2336  O   ASP A 306      40.516  -3.870  15.527  1.00 40.65           O  
ANISOU 2336  O   ASP A 306     5831   4580   5032    875     14    100       O  
ATOM   2337  CB  ASP A 306      43.871  -2.416  15.511  1.00 41.97           C  
ANISOU 2337  CB  ASP A 306     5703   5020   5222   1071     29    135       C  
ATOM   2338  CG  ASP A 306      44.039  -2.742  17.001  1.00 53.48           C  
ANISOU 2338  CG  ASP A 306     7192   6444   6686   1094     -4    154       C  
ATOM   2339  OD1 ASP A 306      43.435  -3.740  17.480  1.00 47.83           O  
ANISOU 2339  OD1 ASP A 306     6605   5621   5947   1099    -15    147       O  
ATOM   2340  OD2 ASP A 306      44.774  -1.984  17.692  1.00 51.21           O  
ANISOU 2340  OD2 ASP A 306     6800   6236   6422   1103    -20    179       O  
ATOM   2341  N   PHE A 307      41.151  -1.736  15.938  1.00 41.78           N  
ANISOU 2341  N   PHE A 307     5750   4883   5241    829     11    137       N  
ATOM   2342  CA  PHE A 307      39.798  -1.336  16.329  1.00 34.82           C  
ANISOU 2342  CA  PHE A 307     4890   3957   4381    711      1    143       C  
ATOM   2343  C   PHE A 307      38.833  -1.700  15.193  1.00 38.53           C  
ANISOU 2343  C   PHE A 307     5422   4383   4833    658     17    118       C  
ATOM   2344  O   PHE A 307      37.796  -2.316  15.408  1.00 41.86           O  
ANISOU 2344  O   PHE A 307     5934   4727   5243    600      9    113       O  
ATOM   2345  CB  PHE A 307      39.730   0.162  16.683  1.00 33.96           C  
ANISOU 2345  CB  PHE A 307     4662   3925   4317    646     -6    164       C  
ATOM   2346  CG  PHE A 307      38.436   0.574  17.376  1.00 33.07           C  
ANISOU 2346  CG  PHE A 307     4567   3775   4224    545    -19    174       C  
ATOM   2347  CD1 PHE A 307      37.254   0.612  16.677  1.00 28.86           C  
ANISOU 2347  CD1 PHE A 307     4063   3213   3688    468     -8    163       C  
ATOM   2348  CD2 PHE A 307      38.427   0.914  18.732  1.00 33.28           C  
ANISOU 2348  CD2 PHE A 307     4578   3801   4265    533    -40    193       C  
ATOM   2349  CE1 PHE A 307      36.062   0.983  17.317  1.00 36.18           C  
ANISOU 2349  CE1 PHE A 307     4998   4119   4629    382    -17    173       C  
ATOM   2350  CE2 PHE A 307      37.253   1.301  19.377  1.00 38.00           C  
ANISOU 2350  CE2 PHE A 307     5189   4374   4874    449    -47    202       C  
ATOM   2351  CZ  PHE A 307      36.060   1.330  18.673  1.00 35.23           C  
ANISOU 2351  CZ  PHE A 307     4862   4001   4523    375    -34    193       C  
ATOM   2352  N   LEU A 308      39.186  -1.333  13.970  1.00 39.04           N  
ANISOU 2352  N   LEU A 308     5438   4502   4892    674     38    105       N  
ATOM   2353  CA  LEU A 308      38.374  -1.707  12.820  1.00 41.26           C  
ANISOU 2353  CA  LEU A 308     5780   4747   5150    632     50     80       C  
ATOM   2354  C   LEU A 308      39.160  -2.751  12.035  1.00 41.67           C  
ANISOU 2354  C   LEU A 308     5900   4777   5154    737     66     52       C  
ATOM   2355  O   LEU A 308      40.196  -2.436  11.464  1.00 41.08           O  
ANISOU 2355  O   LEU A 308     5756   4780   5073    810     86     52       O  
ATOM   2356  CB  LEU A 308      38.096  -0.478  11.943  1.00 38.62           C  
ANISOU 2356  CB  LEU A 308     5346   4488   4838    572     63     86       C  
ATOM   2357  CG  LEU A 308      37.155   0.587  12.521  1.00 39.96           C  
ANISOU 2357  CG  LEU A 308     5459   4674   5050    469     49    108       C  
ATOM   2358  CD1 LEU A 308      36.998   1.726  11.533  1.00 32.69           C  
ANISOU 2358  CD1 LEU A 308     4453   3823   4145    426     61    113       C  
ATOM   2359  CD2 LEU A 308      35.786  -0.017  12.881  1.00 39.26           C  
ANISOU 2359  CD2 LEU A 308     5458   4507   4953    393     35    101       C  
ATOM   2360  N   SER A 309      38.689  -3.992  12.013  1.00 41.81           N  
ANISOU 2360  N   SER A 309     6056   4693   5135    747     58     30       N  
ATOM   2361  CA  SER A 309      39.468  -5.064  11.398  1.00 40.57           C  
ANISOU 2361  CA  SER A 309     5983   4503   4928    861     69      1       C  
ATOM   2362  C   SER A 309      39.397  -4.975   9.879  1.00 42.04           C  
ANISOU 2362  C   SER A 309     6167   4719   5086    863     93    -28       C  
ATOM   2363  O   SER A 309      40.182  -5.612   9.179  1.00 44.15           O  
ANISOU 2363  O   SER A 309     6475   4990   5310    969    110    -53       O  
ATOM   2364  CB  SER A 309      39.002  -6.438  11.901  1.00 46.66           C  
ANISOU 2364  CB  SER A 309     6920   5143   5666    870     49    -14       C  
ATOM   2365  OG  SER A 309      37.643  -6.663  11.554  1.00 50.89           O  
ANISOU 2365  OG  SER A 309     7528   5613   6197    751     37    -25       O  
ATOM   2366  N   ASP A 310      38.479  -4.152   9.375  1.00 37.80           N  
ANISOU 2366  N   ASP A 310     5579   4210   4571    753     93    -24       N  
ATOM   2367  CA  ASP A 310      38.285  -3.975   7.932  1.00 38.16           C  
ANISOU 2367  CA  ASP A 310     5621   4288   4591    741    111    -48       C  
ATOM   2368  C   ASP A 310      37.405  -2.726   7.744  1.00 32.84           C  
ANISOU 2368  C   ASP A 310     4852   3667   3957    622    107    -26       C  
ATOM   2369  O   ASP A 310      36.971  -2.131   8.740  1.00 33.73           O  
ANISOU 2369  O   ASP A 310     4917   3785   4114    561     91      2       O  
ATOM   2370  CB  ASP A 310      37.604  -5.227   7.341  1.00 40.04           C  
ANISOU 2370  CB  ASP A 310     6019   4419   4777    732    100    -89       C  
ATOM   2371  CG  ASP A 310      37.804  -5.368   5.823  1.00 50.85           C  
ANISOU 2371  CG  ASP A 310     7408   5814   6098    770    122   -123       C  
ATOM   2372  OD1 ASP A 310      38.336  -4.434   5.174  1.00 49.03           O  
ANISOU 2372  OD1 ASP A 310     7064   5690   5876    789    148   -112       O  
ATOM   2373  OD2 ASP A 310      37.425  -6.435   5.271  1.00 57.95           O  
ANISOU 2373  OD2 ASP A 310     8446   6626   6947    779    112   -162       O  
ATOM   2374  N   THR A 311      37.150  -2.307   6.509  1.00 30.66           N  
ANISOU 2374  N   THR A 311     4551   3434   3665    597    122    -39       N  
ATOM   2375  CA  THR A 311      36.310  -1.130   6.295  1.00 39.47           C  
ANISOU 2375  CA  THR A 311     5584   4598   4815    493    116    -17       C  
ATOM   2376  C   THR A 311      34.930  -1.386   6.873  1.00 40.10           C  
ANISOU 2376  C   THR A 311     5720   4609   4908    391     86    -16       C  
ATOM   2377  O   THR A 311      34.475  -2.526   6.895  1.00 39.56           O  
ANISOU 2377  O   THR A 311     5769   4455   4808    383     73    -41       O  
ATOM   2378  CB  THR A 311      36.092  -0.854   4.824  1.00 45.88           C  
ANISOU 2378  CB  THR A 311     6386   5449   5595    479    131    -34       C  
ATOM   2379  OG1 THR A 311      35.248  -1.886   4.286  1.00 46.37           O  
ANISOU 2379  OG1 THR A 311     6572   5431   5615    448    116    -71       O  
ATOM   2380  CG2 THR A 311      37.441  -0.799   4.078  1.00 40.03           C  
ANISOU 2380  CG2 THR A 311     5605   4779   4827    585    166    -39       C  
ATOM   2381  N   PRO A 312      34.262  -0.333   7.357  1.00 40.08           N  
ANISOU 2381  N   PRO A 312     5636   4644   4950    313     76     13       N  
ATOM   2382  CA  PRO A 312      32.881  -0.511   7.820  1.00 41.31           C  
ANISOU 2382  CA  PRO A 312     5830   4752   5114    214     52     16       C  
ATOM   2383  C   PRO A 312      31.974  -1.140   6.769  1.00 39.23           C  
ANISOU 2383  C   PRO A 312     5642   4453   4810    161     43    -13       C  
ATOM   2384  O   PRO A 312      31.087  -1.883   7.145  1.00 50.23           O  
ANISOU 2384  O   PRO A 312     7111   5782   6193    100     22    -19       O  
ATOM   2385  CB  PRO A 312      32.444   0.911   8.171  1.00 36.14           C  
ANISOU 2385  CB  PRO A 312     5062   4165   4505    160     50     48       C  
ATOM   2386  CG  PRO A 312      33.707   1.543   8.596  1.00 39.51           C  
ANISOU 2386  CG  PRO A 312     5416   4641   4956    230     63     67       C  
ATOM   2387  CD  PRO A 312      34.779   1.001   7.685  1.00 36.54           C  
ANISOU 2387  CD  PRO A 312     5062   4276   4544    316     84     46       C  
ATOM   2388  N   GLU A 313      32.197  -0.859   5.494  1.00 42.18           N  
ANISOU 2388  N   GLU A 313     5997   4870   5159    180     56    -28       N  
ATOM   2389  CA  GLU A 313      31.436  -1.474   4.408  1.00 47.45           C  
ANISOU 2389  CA  GLU A 313     6741   5507   5781    137     44    -60       C  
ATOM   2390  C   GLU A 313      31.574  -3.003   4.427  1.00 51.00           C  
ANISOU 2390  C   GLU A 313     7336   5856   6186    168     34    -95       C  
ATOM   2391  O   GLU A 313      30.591  -3.749   4.318  1.00 45.96           O  
ANISOU 2391  O   GLU A 313     6784   5154   5524     93      8   -112       O  
ATOM   2392  CB  GLU A 313      31.918  -0.923   3.055  1.00 59.78           C  
ANISOU 2392  CB  GLU A 313     8260   7136   7318    175     65    -70       C  
ATOM   2393  CG  GLU A 313      31.019  -1.262   1.865  1.00 79.84           C  
ANISOU 2393  CG  GLU A 313    10858   9665   9814    118     49    -98       C  
ATOM   2394  CD  GLU A 313      31.606  -0.827   0.505  1.00 94.94           C  
ANISOU 2394  CD  GLU A 313    12739  11642  11690    167     73   -110       C  
ATOM   2395  OE1 GLU A 313      32.854  -0.744   0.371  1.00 98.72           O  
ANISOU 2395  OE1 GLU A 313    13192  12154  12162    264    105   -108       O  
ATOM   2396  OE2 GLU A 313      30.814  -0.581  -0.438  1.00 98.75           O  
ANISOU 2396  OE2 GLU A 313    13223  12148  12148    110     59   -118       O  
ATOM   2397  N   ALA A 314      32.803  -3.478   4.567  1.00 45.95           N  
ANISOU 2397  N   ALA A 314     6725   5202   5532    279     54   -105       N  
ATOM   2398  CA  ALA A 314      33.031  -4.902   4.536  1.00 42.35           C  
ANISOU 2398  CA  ALA A 314     6414   4647   5028    327     45   -140       C  
ATOM   2399  C   ALA A 314      32.423  -5.517   5.781  1.00 49.51           C  
ANISOU 2399  C   ALA A 314     7384   5473   5953    271     19   -125       C  
ATOM   2400  O   ALA A 314      31.848  -6.600   5.721  1.00 57.79           O  
ANISOU 2400  O   ALA A 314     8564   6427   6968    233     -4   -148       O  
ATOM   2401  CB  ALA A 314      34.517  -5.201   4.453  1.00 44.18           C  
ANISOU 2401  CB  ALA A 314     6651   4895   5241    472     73   -151       C  
ATOM   2402  N   LEU A 315      32.548  -4.828   6.911  1.00 44.86           N  
ANISOU 2402  N   LEU A 315     6709   4922   5416    263     23    -86       N  
ATOM   2403  CA  LEU A 315      32.074  -5.361   8.191  1.00 41.93           C  
ANISOU 2403  CA  LEU A 315     6389   4482   5059    220      3    -66       C  
ATOM   2404  C   LEU A 315      30.561  -5.353   8.347  1.00 43.83           C  
ANISOU 2404  C   LEU A 315     6642   4704   5306     80    -21    -56       C  
ATOM   2405  O   LEU A 315      30.039  -6.233   9.006  1.00 49.67           O  
ANISOU 2405  O   LEU A 315     7475   5363   6034     33    -40    -52       O  
ATOM   2406  CB  LEU A 315      32.686  -4.616   9.374  1.00 43.32           C  
ANISOU 2406  CB  LEU A 315     6470   4708   5283    258     12    -29       C  
ATOM   2407  CG  LEU A 315      34.193  -4.725   9.495  1.00 39.90           C  
ANISOU 2407  CG  LEU A 315     6022   4295   4844    393     31    -33       C  
ATOM   2408  CD1 LEU A 315      34.684  -3.913  10.673  1.00 25.17           C  
ANISOU 2408  CD1 LEU A 315     4057   2482   3025    411     33      4       C  
ATOM   2409  CD2 LEU A 315      34.550  -6.241   9.620  1.00 31.57           C  
ANISOU 2409  CD2 LEU A 315     5122   3131   3741    458     22    -58       C  
ATOM   2410  N   ILE A 316      29.844  -4.373   7.791  1.00 42.12           N  
ANISOU 2410  N   ILE A 316     6331   4563   5108     12    -20    -47       N  
ATOM   2411  CA  ILE A 316      28.380  -4.469   7.845  1.00 47.44           C  
ANISOU 2411  CA  ILE A 316     7017   5226   5781   -118    -44    -39       C  
ATOM   2412  C   ILE A 316      27.893  -5.507   6.821  1.00 61.89           C  
ANISOU 2412  C   ILE A 316     8968   6992   7558   -159    -65    -77       C  
ATOM   2413  O   ILE A 316      26.820  -6.072   6.979  1.00 64.83           O  
ANISOU 2413  O   ILE A 316     9395   7322   7916   -264    -91    -75       O  
ATOM   2414  CB  ILE A 316      27.592  -3.107   7.625  1.00 44.03           C  
ANISOU 2414  CB  ILE A 316     6449   4897   5383   -182    -42    -16       C  
ATOM   2415  CG1 ILE A 316      27.865  -2.492   6.249  1.00 49.32           C  
ANISOU 2415  CG1 ILE A 316     7073   5626   6039   -152    -33    -34       C  
ATOM   2416  CG2 ILE A 316      27.898  -2.084   8.702  1.00 47.27           C  
ANISOU 2416  CG2 ILE A 316     6755   5363   5844   -156    -28     21       C  
ATOM   2417  CD1 ILE A 316      27.124  -1.158   5.992  1.00 45.53           C  
ANISOU 2417  CD1 ILE A 316     6471   5241   5589   -205    -34    -10       C  
ATOM   2418  N   ASN A 317      28.680  -5.754   5.774  1.00 65.50           N  
ANISOU 2418  N   ASN A 317     9464   7442   7980    -80    -54   -113       N  
ATOM   2419  CA  ASN A 317      28.288  -6.708   4.736  1.00 68.83           C  
ANISOU 2419  CA  ASN A 317    10007   7800   8344   -110    -76   -155       C  
ATOM   2420  C   ASN A 317      28.324  -8.155   5.203  1.00 69.34           C  
ANISOU 2420  C   ASN A 317    10237   7736   8375   -109    -96   -173       C  
ATOM   2421  O   ASN A 317      27.518  -8.970   4.767  1.00 70.27           O  
ANISOU 2421  O   ASN A 317    10459   7786   8455   -193   -127   -195       O  
ATOM   2422  CB  ASN A 317      29.164  -6.568   3.488  1.00 66.78           C  
ANISOU 2422  CB  ASN A 317     9749   7575   8051    -14    -55   -189       C  
ATOM   2423  CG  ASN A 317      28.781  -5.373   2.646  1.00 72.99           C  
ANISOU 2423  CG  ASN A 317    10413   8469   8850    -49    -48   -179       C  
ATOM   2424  OD1 ASN A 317      27.766  -4.715   2.906  1.00 78.99           O  
ANISOU 2424  OD1 ASN A 317    11099   9274   9641   -147    -62   -152       O  
ATOM   2425  ND2 ASN A 317      29.602  -5.067   1.634  1.00 70.13           N  
ANISOU 2425  ND2 ASN A 317    10030   8153   8463     35    -23   -199       N  
ATOM   2426  N   THR A 318      29.255  -8.464   6.098  1.00 65.50           N  
ANISOU 2426  N   THR A 318     9774   7213   7900    -18    -81   -162       N  
ATOM   2427  CA  THR A 318      29.537  -9.843   6.454  1.00 64.44           C  
ANISOU 2427  CA  THR A 318     9807   6950   7727     15    -97   -181       C  
ATOM   2428  C   THR A 318      29.161 -10.138   7.886  1.00 64.96           C  
ANISOU 2428  C   THR A 318     9893   6970   7820    -37   -108   -141       C  
ATOM   2429  O   THR A 318      29.211 -11.276   8.327  1.00 67.30           O  
ANISOU 2429  O   THR A 318    10332   7152   8086    -32   -126   -147       O  
ATOM   2430  CB  THR A 318      31.031 -10.129   6.333  1.00 69.26           C  
ANISOU 2430  CB  THR A 318    10447   7548   8318    185    -71   -201       C  
ATOM   2431  OG1 THR A 318      31.743  -9.330   7.292  1.00 70.15           O  
ANISOU 2431  OG1 THR A 318    10440   7733   8482    246    -48   -163       O  
ATOM   2432  CG2 THR A 318      31.520  -9.803   4.936  1.00 71.49           C  
ANISOU 2432  CG2 THR A 318    10703   7889   8571    249    -52   -238       C  
ATOM   2433  N   GLY A 319      28.815  -9.107   8.631  1.00 66.66           N  
ANISOU 2433  N   GLY A 319     9969   7270   8087    -81    -97    -99       N  
ATOM   2434  CA  GLY A 319      28.571  -9.289  10.044  1.00 68.14           C  
ANISOU 2434  CA  GLY A 319    10164   7428   8298   -115   -102    -59       C  
ATOM   2435  C   GLY A 319      27.308 -10.067  10.354  1.00 68.18           C  
ANISOU 2435  C   GLY A 319    10257   7363   8283   -257   -132    -47       C  
ATOM   2436  O   GLY A 319      26.362 -10.123   9.559  1.00 64.02           O  
ANISOU 2436  O   GLY A 319     9739   6845   7739   -358   -150    -61       O  
ATOM   2437  N   ASP A 320      27.306 -10.680  11.529  1.00 67.47           N  
ANISOU 2437  N   ASP A 320    10234   7208   8194   -267   -138    -19       N  
ATOM   2438  CA  ASP A 320      26.123 -11.312  12.062  1.00 69.50           C  
ANISOU 2438  CA  ASP A 320    10556   7413   8438   -409   -162      6       C  
ATOM   2439  C   ASP A 320      25.586 -10.377  13.145  1.00 67.74           C  
ANISOU 2439  C   ASP A 320    10197   7282   8260   -461   -146     57       C  
ATOM   2440  O   ASP A 320      26.281 -10.104  14.134  1.00 68.81           O  
ANISOU 2440  O   ASP A 320    10300   7429   8417   -384   -129     80       O  
ATOM   2441  CB  ASP A 320      26.502 -12.661  12.659  1.00 75.04           C  
ANISOU 2441  CB  ASP A 320    11436   7972   9103   -383   -178      8       C  
ATOM   2442  CG  ASP A 320      25.316 -13.409  13.225  1.00 77.69           C  
ANISOU 2442  CG  ASP A 320    11854   8245   9421   -539   -204     38       C  
ATOM   2443  OD1 ASP A 320      24.185 -13.219  12.728  1.00 83.67           O  
ANISOU 2443  OD1 ASP A 320    12570   9044  10175   -671   -218     40       O  
ATOM   2444  OD2 ASP A 320      25.530 -14.208  14.157  1.00 78.26           O  
ANISOU 2444  OD2 ASP A 320    12032   8226   9477   -529   -211     62       O  
ATOM   2445  N   PHE A 321      24.364  -9.875  12.958  1.00 57.78           N  
ANISOU 2445  N   PHE A 321     8855   6091   7009   -585   -151     72       N  
ATOM   2446  CA  PHE A 321      23.822  -8.885  13.886  1.00 58.19           C  
ANISOU 2446  CA  PHE A 321     8769   6242   7099   -623   -133    115       C  
ATOM   2447  C   PHE A 321      22.547  -9.344  14.583  1.00 61.74           C  
ANISOU 2447  C   PHE A 321     9239   6683   7535   -768   -145    154       C  
ATOM   2448  O   PHE A 321      21.642  -8.548  14.842  1.00 63.90           O  
ANISOU 2448  O   PHE A 321     9393   7057   7830   -838   -136    180       O  
ATOM   2449  CB  PHE A 321      23.629  -7.546  13.168  1.00 55.54           C  
ANISOU 2449  CB  PHE A 321     8281   6029   6794   -612   -120    107       C  
ATOM   2450  CG  PHE A 321      24.904  -6.997  12.587  1.00 49.11           C  
ANISOU 2450  CG  PHE A 321     7431   5234   5993   -476   -104     78       C  
ATOM   2451  CD1 PHE A 321      25.864  -6.436  13.410  1.00 42.91           C  
ANISOU 2451  CD1 PHE A 321     6592   4473   5237   -376    -84     93       C  
ATOM   2452  CD2 PHE A 321      25.161  -7.088  11.229  1.00 51.60           C  
ANISOU 2452  CD2 PHE A 321     7772   5546   6289   -450   -111     38       C  
ATOM   2453  CE1 PHE A 321      27.060  -5.949  12.885  1.00 44.61           C  
ANISOU 2453  CE1 PHE A 321     6770   4715   5463   -259    -70     71       C  
ATOM   2454  CE2 PHE A 321      26.349  -6.593  10.692  1.00 52.64           C  
ANISOU 2454  CE2 PHE A 321     7867   5704   6429   -327    -92     16       C  
ATOM   2455  CZ  PHE A 321      27.293  -6.015  11.526  1.00 45.61           C  
ANISOU 2455  CZ  PHE A 321     6915   4845   5571   -235    -71     35       C  
ATOM   2456  N   GLN A 322      22.526 -10.624  14.938  1.00 61.78           N  
ANISOU 2456  N   GLN A 322     9398   6570   7506   -806   -164    159       N  
ATOM   2457  CA  GLN A 322      21.336 -11.281  15.450  1.00 63.53           C  
ANISOU 2457  CA  GLN A 322     9665   6768   7705   -958   -179    195       C  
ATOM   2458  C   GLN A 322      20.858 -10.810  16.810  1.00 59.57           C  
ANISOU 2458  C   GLN A 322     9079   6332   7223   -995   -157    251       C  
ATOM   2459  O   GLN A 322      19.661 -10.651  17.029  1.00 66.94           O  
ANISOU 2459  O   GLN A 322     9949   7331   8153  -1119   -157    282       O  
ATOM   2460  CB  GLN A 322      21.540 -12.787  15.467  1.00 71.75           C  
ANISOU 2460  CB  GLN A 322    10909   7652   8701   -984   -207    187       C  
ATOM   2461  CG  GLN A 322      21.343 -13.408  14.113  1.00 84.30           C  
ANISOU 2461  CG  GLN A 322    12590   9182  10257  -1025   -239    140       C  
ATOM   2462  CD  GLN A 322      21.335 -14.915  14.174  1.00 94.07           C  
ANISOU 2462  CD  GLN A 322    14039  10257  11446  -1075   -272    135       C  
ATOM   2463  OE1 GLN A 322      22.239 -15.531  14.751  1.00 91.86           O  
ANISOU 2463  OE1 GLN A 322    13869   9880  11154   -979   -269    136       O  
ATOM   2464  NE2 GLN A 322      20.310 -15.525  13.578  1.00 98.64           N  
ANISOU 2464  NE2 GLN A 322    14681  10803  11993  -1226   -307    130       N  
ATOM   2465  N   ASP A 323      21.763 -10.584  17.736  1.00 55.40           N  
ANISOU 2465  N   ASP A 323     8545   5794   6710   -887   -137    264       N  
ATOM   2466  CA  ASP A 323      21.294 -10.177  19.051  1.00 66.29           C  
ANISOU 2466  CA  ASP A 323     9854   7233   8100   -921   -116    315       C  
ATOM   2467  C   ASP A 323      21.276  -8.652  19.212  1.00 58.75           C  
ANISOU 2467  C   ASP A 323     8720   6415   7186   -869    -90    317       C  
ATOM   2468  O   ASP A 323      21.432  -8.140  20.311  1.00 55.70           O  
ANISOU 2468  O   ASP A 323     8279   6071   6814   -831    -70    346       O  
ATOM   2469  CB  ASP A 323      22.166 -10.802  20.138  1.00 81.58           C  
ANISOU 2469  CB  ASP A 323    11890   9083  10024   -846   -113    335       C  
ATOM   2470  CG  ASP A 323      23.627 -10.380  20.023  1.00 97.17           C  
ANISOU 2470  CG  ASP A 323    13851  11050  12021   -677   -106    303       C  
ATOM   2471  OD1 ASP A 323      24.002  -9.768  18.981  1.00 96.46           O  
ANISOU 2471  OD1 ASP A 323    13699  11003  11950   -623   -105    264       O  
ATOM   2472  OD2 ASP A 323      24.395 -10.664  20.977  1.00105.35           O  
ANISOU 2472  OD2 ASP A 323    14937  12041  13051   -600   -102    321       O  
ATOM   2473  N   LEU A 324      21.090  -7.928  18.117  1.00 58.60           N  
ANISOU 2473  N   LEU A 324     8618   6463   7186   -866    -92    287       N  
ATOM   2474  CA  LEU A 324      21.220  -6.472  18.158  1.00 54.81           C  
ANISOU 2474  CA  LEU A 324     7984   6097   6744   -802    -71    285       C  
ATOM   2475  C   LEU A 324      19.917  -5.766  17.788  1.00 46.01           C  
ANISOU 2475  C   LEU A 324     6755   5091   5635   -895    -68    298       C  
ATOM   2476  O   LEU A 324      19.311  -6.087  16.768  1.00 45.12           O  
ANISOU 2476  O   LEU A 324     6658   4980   5508   -968    -88    281       O  
ATOM   2477  CB  LEU A 324      22.331  -6.029  17.207  1.00 48.78           C  
ANISOU 2477  CB  LEU A 324     7208   5326   5998   -689    -72    242       C  
ATOM   2478  CG  LEU A 324      22.612  -4.528  17.201  1.00 48.06           C  
ANISOU 2478  CG  LEU A 324     6975   5339   5947   -621    -54    239       C  
ATOM   2479  CD1 LEU A 324      23.256  -4.139  18.488  1.00 46.01           C  
ANISOU 2479  CD1 LEU A 324     6692   5087   5704   -551    -39    261       C  
ATOM   2480  CD2 LEU A 324      23.506  -4.170  16.055  1.00 52.19           C  
ANISOU 2480  CD2 LEU A 324     7486   5863   6482   -540    -57    200       C  
ATOM   2481  N   GLN A 325      19.487  -4.810  18.613  1.00 43.48           N  
ANISOU 2481  N   GLN A 325     6323   4865   5333   -889    -46    325       N  
ATOM   2482  CA  GLN A 325      18.399  -3.920  18.201  1.00 45.80           C  
ANISOU 2482  CA  GLN A 325     6491   5276   5635   -944    -41    333       C  
ATOM   2483  C   GLN A 325      18.914  -2.509  17.952  1.00 43.28           C  
ANISOU 2483  C   GLN A 325     6066   5027   5352   -841    -29    315       C  
ATOM   2484  O   GLN A 325      19.769  -2.020  18.688  1.00 45.91           O  
ANISOU 2484  O   GLN A 325     6388   5352   5704   -751    -16    316       O  
ATOM   2485  CB  GLN A 325      17.251  -3.902  19.210  1.00 47.46           C  
ANISOU 2485  CB  GLN A 325     6649   5554   5829  -1029    -25    380       C  
ATOM   2486  CG  GLN A 325      16.737  -5.265  19.569  1.00 49.44           C  
ANISOU 2486  CG  GLN A 325     7004   5737   6043  -1141    -36    405       C  
ATOM   2487  CD  GLN A 325      17.323  -5.712  20.862  1.00 59.80           C  
ANISOU 2487  CD  GLN A 325     8386   6989   7346  -1104    -22    430       C  
ATOM   2488  OE1 GLN A 325      17.211  -5.018  21.873  1.00 58.99           O  
ANISOU 2488  OE1 GLN A 325     8211   6953   7250  -1069      4    455       O  
ATOM   2489  NE2 GLN A 325      17.992  -6.854  20.846  1.00 65.72           N  
ANISOU 2489  NE2 GLN A 325     9281   7611   8077  -1101    -39    423       N  
ATOM   2490  N   VAL A 326      18.398  -1.854  16.917  1.00 37.59           N  
ANISOU 2490  N   VAL A 326     5271   4373   4640   -858    -37    300       N  
ATOM   2491  CA  VAL A 326      18.996  -0.596  16.480  1.00 34.62           C  
ANISOU 2491  CA  VAL A 326     4815   4044   4295   -763    -30    282       C  
ATOM   2492  C   VAL A 326      17.909   0.364  16.051  1.00 36.95           C  
ANISOU 2492  C   VAL A 326     4995   4450   4595   -796    -30    291       C  
ATOM   2493  O   VAL A 326      16.980  -0.023  15.348  1.00 36.60           O  
ANISOU 2493  O   VAL A 326     4943   4434   4530   -882    -45    292       O  
ATOM   2494  CB  VAL A 326      19.974  -0.833  15.303  1.00 42.10           C  
ANISOU 2494  CB  VAL A 326     5819   4933   5246   -711    -44    243       C  
ATOM   2495  CG1 VAL A 326      20.476   0.445  14.764  1.00 47.88           C  
ANISOU 2495  CG1 VAL A 326     6468   5719   6007   -633    -38    230       C  
ATOM   2496  CG2 VAL A 326      21.152  -1.681  15.758  1.00 48.00           C  
ANISOU 2496  CG2 VAL A 326     6671   5578   5988   -654    -43    233       C  
ATOM   2497  N   LEU A 327      18.019   1.613  16.495  1.00 34.89           N  
ANISOU 2497  N   LEU A 327     4648   4251   4359   -727    -14    297       N  
ATOM   2498  CA  LEU A 327      17.143   2.674  16.034  1.00 32.28           C  
ANISOU 2498  CA  LEU A 327     4210   4022   4034   -731    -14    303       C  
ATOM   2499  C   LEU A 327      17.989   3.673  15.210  1.00 38.26           C  
ANISOU 2499  C   LEU A 327     4940   4780   4818   -645    -19    279       C  
ATOM   2500  O   LEU A 327      18.995   4.218  15.712  1.00 34.57           O  
ANISOU 2500  O   LEU A 327     4478   4284   4373   -564    -10    273       O  
ATOM   2501  CB  LEU A 327      16.498   3.350  17.239  1.00 32.89           C  
ANISOU 2501  CB  LEU A 327     4216   4169   4110   -720      8    332       C  
ATOM   2502  CG  LEU A 327      15.657   4.617  16.991  1.00 39.14           C  
ANISOU 2502  CG  LEU A 327     4895   5069   4908   -696     11    339       C  
ATOM   2503  CD1 LEU A 327      14.774   4.462  15.819  1.00 43.15           C  
ANISOU 2503  CD1 LEU A 327     5368   5628   5401   -762     -8    337       C  
ATOM   2504  CD2 LEU A 327      14.788   4.848  18.180  1.00 47.99           C  
ANISOU 2504  CD2 LEU A 327     5962   6260   6013   -709     34    369       C  
ATOM   2505  N   VAL A 328      17.628   3.902  13.948  1.00 29.81           N  
ANISOU 2505  N   VAL A 328     3842   3740   3742   -664    -35    266       N  
ATOM   2506  CA  VAL A 328      18.439   4.800  13.124  1.00 33.38           C  
ANISOU 2506  CA  VAL A 328     4275   4192   4216   -589    -39    248       C  
ATOM   2507  C   VAL A 328      17.521   5.747  12.434  1.00 36.13           C  
ANISOU 2507  C   VAL A 328     4537   4629   4563   -596    -47    256       C  
ATOM   2508  O   VAL A 328      16.393   5.381  12.129  1.00 42.78           O  
ANISOU 2508  O   VAL A 328     5353   5520   5381   -670    -58    265       O  
ATOM   2509  CB  VAL A 328      19.201   4.060  11.981  1.00 37.05           C  
ANISOU 2509  CB  VAL A 328     4813   4593   4669   -589    -52    220       C  
ATOM   2510  CG1 VAL A 328      20.362   3.270  12.516  1.00 35.44           C  
ANISOU 2510  CG1 VAL A 328     4694   4301   4469   -552    -44    209       C  
ATOM   2511  CG2 VAL A 328      18.228   3.147  11.184  1.00 37.17           C  
ANISOU 2511  CG2 VAL A 328     4856   4617   4651   -686    -73    214       C  
ATOM   2512  N   GLY A 329      18.007   6.940  12.119  1.00 32.07           N  
ANISOU 2512  N   GLY A 329     3982   4134   4070   -524    -46    253       N  
ATOM   2513  CA  GLY A 329      17.216   7.862  11.317  1.00 29.63           C  
ANISOU 2513  CA  GLY A 329     3600   3900   3756   -520    -57    260       C  
ATOM   2514  C   GLY A 329      17.922   9.125  10.881  1.00 33.86           C  
ANISOU 2514  C   GLY A 329     4111   4439   4316   -441    -57    257       C  
ATOM   2515  O   GLY A 329      19.143   9.270  11.087  1.00 31.97           O  
ANISOU 2515  O   GLY A 329     3908   4142   4097   -393    -49    249       O  
ATOM   2516  N   VAL A 330      17.152  10.056  10.294  1.00 33.34           N  
ANISOU 2516  N   VAL A 330     3982   4441   4245   -429    -68    268       N  
ATOM   2517  CA  VAL A 330      17.722  11.241   9.623  1.00 27.53           C  
ANISOU 2517  CA  VAL A 330     3230   3706   3525   -366    -74    269       C  
ATOM   2518  C   VAL A 330      16.784  12.412   9.866  1.00 32.88           C  
ANISOU 2518  C   VAL A 330     3838   4453   4202   -331    -78    288       C  
ATOM   2519  O   VAL A 330      15.606  12.203  10.226  1.00 29.65           O  
ANISOU 2519  O   VAL A 330     3384   4108   3775   -362    -78    299       O  
ATOM   2520  CB  VAL A 330      17.890  11.000   8.082  1.00 31.83           C  
ANISOU 2520  CB  VAL A 330     3793   4251   4052   -386    -89    258       C  
ATOM   2521  CG1 VAL A 330      18.832   9.810   7.795  1.00 28.35           C  
ANISOU 2521  CG1 VAL A 330     3428   3741   3605   -410    -84    236       C  
ATOM   2522  CG2 VAL A 330      16.525  10.739   7.420  1.00 32.06           C  
ANISOU 2522  CG2 VAL A 330     3781   4352   4049   -442   -109    264       C  
ATOM   2523  N   VAL A 331      17.280  13.641   9.692  1.00 26.00           N  
ANISOU 2523  N   VAL A 331     2958   3573   3349   -266    -81    294       N  
ATOM   2524  CA  VAL A 331      16.369  14.785   9.661  1.00 32.13           C  
ANISOU 2524  CA  VAL A 331     3678   4411   4119   -224    -90    311       C  
ATOM   2525  C   VAL A 331      15.987  15.078   8.211  1.00 34.35           C  
ANISOU 2525  C   VAL A 331     3940   4729   4381   -231   -111    317       C  
ATOM   2526  O   VAL A 331      16.624  14.589   7.273  1.00 35.15           O  
ANISOU 2526  O   VAL A 331     4077   4799   4478   -258   -116    307       O  
ATOM   2527  CB  VAL A 331      16.966  16.053  10.309  1.00 30.94           C  
ANISOU 2527  CB  VAL A 331     3536   4227   3992   -149    -88    316       C  
ATOM   2528  CG1 VAL A 331      17.213  15.830  11.792  1.00 28.34           C  
ANISOU 2528  CG1 VAL A 331     3222   3872   3674   -138    -70    310       C  
ATOM   2529  CG2 VAL A 331      18.246  16.491   9.578  1.00 22.32           C  
ANISOU 2529  CG2 VAL A 331     2487   3075   2920   -132    -94    313       C  
ATOM   2530  N   LYS A 332      14.963  15.892   8.032  1.00 31.23           N  
ANISOU 2530  N   LYS A 332     3490   4403   3973   -200   -123    333       N  
ATOM   2531  CA  LYS A 332      14.445  16.152   6.722  1.00 33.07           C  
ANISOU 2531  CA  LYS A 332     3699   4682   4183   -206   -146    341       C  
ATOM   2532  C   LYS A 332      15.481  16.781   5.803  1.00 38.09           C  
ANISOU 2532  C   LYS A 332     4378   5265   4828   -177   -153    343       C  
ATOM   2533  O   LYS A 332      15.531  16.456   4.624  1.00 40.25           O  
ANISOU 2533  O   LYS A 332     4661   5548   5082   -206   -166    341       O  
ATOM   2534  CB  LYS A 332      13.178  17.003   6.816  1.00 38.80           C  
ANISOU 2534  CB  LYS A 332     4356   5495   4891   -162   -158    361       C  
ATOM   2535  CG  LYS A 332      12.494  17.287   5.470  1.00 40.29           C  
ANISOU 2535  CG  LYS A 332     4511   5745   5050   -165   -187    373       C  
ATOM   2536  CD  LYS A 332      11.176  18.024   5.698  1.00 49.91           C  
ANISOU 2536  CD  LYS A 332     5653   7062   6249   -115   -198    393       C  
ATOM   2537  CE  LYS A 332      11.025  19.289   4.828  1.00 62.07           C  
ANISOU 2537  CE  LYS A 332     7189   8617   7779    -41   -221    412       C  
ATOM   2538  NZ  LYS A 332      11.826  20.506   5.305  1.00 55.75           N  
ANISOU 2538  NZ  LYS A 332     6438   7739   7004     42   -214    417       N  
ATOM   2539  N   ASP A 333      16.325  17.666   6.334  1.00 33.48           N  
ANISOU 2539  N   ASP A 333     3822   4626   4272   -124   -145    347       N  
ATOM   2540  CA  ASP A 333      17.278  18.367   5.486  1.00 27.79           C  
ANISOU 2540  CA  ASP A 333     3137   3863   3560   -102   -151    356       C  
ATOM   2541  C   ASP A 333      18.756  18.223   5.949  1.00 31.57           C  
ANISOU 2541  C   ASP A 333     3664   4262   4067   -104   -134    346       C  
ATOM   2542  O   ASP A 333      19.368  19.171   6.438  1.00 28.07           O  
ANISOU 2542  O   ASP A 333     3239   3780   3647    -65   -134    355       O  
ATOM   2543  CB  ASP A 333      16.865  19.839   5.334  1.00 23.49           C  
ANISOU 2543  CB  ASP A 333     2580   3332   3014    -36   -168    380       C  
ATOM   2544  CG  ASP A 333      15.429  19.993   4.823  1.00 33.58           C  
ANISOU 2544  CG  ASP A 333     3802   4697   4259    -25   -187    391       C  
ATOM   2545  OD1 ASP A 333      14.485  19.945   5.653  1.00 30.22           O  
ANISOU 2545  OD1 ASP A 333     3334   4320   3827    -10   -184    390       O  
ATOM   2546  OD2 ASP A 333      15.244  20.177   3.601  1.00 35.08           O  
ANISOU 2546  OD2 ASP A 333     3990   4913   4427    -30   -205    403       O  
ATOM   2547  N   GLU A 334      19.322  17.027   5.806  1.00 31.16           N  
ANISOU 2547  N   GLU A 334     3636   4190   4014   -148   -121    328       N  
ATOM   2548  CA  GLU A 334      20.648  16.782   6.351  1.00 28.47           C  
ANISOU 2548  CA  GLU A 334     3331   3788   3698   -145   -105    319       C  
ATOM   2549  C   GLU A 334      21.690  17.764   5.755  1.00 32.16           C  
ANISOU 2549  C   GLU A 334     3816   4227   4178   -120   -107    335       C  
ATOM   2550  O   GLU A 334      22.603  18.203   6.442  1.00 31.58           O  
ANISOU 2550  O   GLU A 334     3757   4112   4130   -102   -102    338       O  
ATOM   2551  CB  GLU A 334      21.035  15.324   6.093  1.00 31.48           C  
ANISOU 2551  CB  GLU A 334     3741   4154   4067   -189    -93    296       C  
ATOM   2552  CG  GLU A 334      20.218  14.304   6.875  1.00 24.31           C  
ANISOU 2552  CG  GLU A 334     2829   3258   3151   -224    -90    283       C  
ATOM   2553  CD  GLU A 334      20.619  14.299   8.336  1.00 32.01           C  
ANISOU 2553  CD  GLU A 334     3813   4199   4151   -205    -77    281       C  
ATOM   2554  OE1 GLU A 334      21.662  14.954   8.682  1.00 31.43           O  
ANISOU 2554  OE1 GLU A 334     3753   4089   4102   -169    -74    285       O  
ATOM   2555  OE2 GLU A 334      19.902  13.658   9.137  1.00 29.13           O  
ANISOU 2555  OE2 GLU A 334     3442   3848   3779   -229    -73    277       O  
ATOM   2556  N   GLY A 335      21.536  18.127   4.482  1.00 25.57           N  
ANISOU 2556  N   GLY A 335     2977   3416   3321   -122   -116    349       N  
ATOM   2557  CA  GLY A 335      22.582  18.860   3.815  1.00 27.28           C  
ANISOU 2557  CA  GLY A 335     3211   3610   3544   -111   -114    368       C  
ATOM   2558  C   GLY A 335      22.672  20.367   4.015  1.00 30.87           C  
ANISOU 2558  C   GLY A 335     3669   4044   4014    -77   -129    395       C  
ATOM   2559  O   GLY A 335      23.760  20.919   3.898  1.00 36.00           O  
ANISOU 2559  O   GLY A 335     4337   4662   4679    -77   -125    410       O  
ATOM   2560  N   SER A 336      21.568  21.033   4.344  1.00 24.11           N  
ANISOU 2560  N   SER A 336     2799   3208   3155    -47   -146    402       N  
ATOM   2561  CA  SER A 336      21.495  22.492   4.209  1.00 30.76           C  
ANISOU 2561  CA  SER A 336     3657   4031   4001     -9   -166    430       C  
ATOM   2562  C   SER A 336      22.498  23.211   5.081  1.00 36.24           C  
ANISOU 2562  C   SER A 336     4381   4662   4727      0   -166    435       C  
ATOM   2563  O   SER A 336      23.170  24.116   4.620  1.00 38.79           O  
ANISOU 2563  O   SER A 336     4730   4952   5054     -1   -176    460       O  
ATOM   2564  CB  SER A 336      20.076  23.011   4.512  1.00 32.09           C  
ANISOU 2564  CB  SER A 336     3802   4235   4155     35   -183    433       C  
ATOM   2565  OG  SER A 336      19.665  22.715   5.845  1.00 31.13           O  
ANISOU 2565  OG  SER A 336     3667   4114   4046     50   -176    412       O  
ATOM   2566  N   TYR A 337      22.575  22.798   6.343  1.00 35.67           N  
ANISOU 2566  N   TYR A 337     4307   4573   4674      4   -159    412       N  
ATOM   2567  CA  TYR A 337      23.560  23.297   7.310  1.00 41.32           C  
ANISOU 2567  CA  TYR A 337     5050   5232   5418      6   -162    410       C  
ATOM   2568  C   TYR A 337      24.976  23.421   6.738  1.00 33.63           C  
ANISOU 2568  C   TYR A 337     4090   4233   4457    -29   -157    426       C  
ATOM   2569  O   TYR A 337      25.685  24.387   6.987  1.00 35.31           O  
ANISOU 2569  O   TYR A 337     4329   4402   4685    -31   -172    443       O  
ATOM   2570  CB  TYR A 337      23.590  22.341   8.520  1.00 45.88           C  
ANISOU 2570  CB  TYR A 337     5617   5809   6006      1   -148    381       C  
ATOM   2571  CG  TYR A 337      24.431  22.801   9.657  1.00 42.45           C  
ANISOU 2571  CG  TYR A 337     5209   5325   5597      8   -155    376       C  
ATOM   2572  CD1 TYR A 337      23.976  23.778  10.496  1.00 50.53           C  
ANISOU 2572  CD1 TYR A 337     6254   6322   6622     48   -173    374       C  
ATOM   2573  CD2 TYR A 337      25.683  22.256   9.899  1.00 49.92           C  
ANISOU 2573  CD2 TYR A 337     6157   6250   6559    -22   -146    371       C  
ATOM   2574  CE1 TYR A 337      24.732  24.229  11.564  1.00 57.99           C  
ANISOU 2574  CE1 TYR A 337     7229   7219   7586     52   -185    366       C  
ATOM   2575  CE2 TYR A 337      26.465  22.704  10.974  1.00 57.08           C  
ANISOU 2575  CE2 TYR A 337     7085   7116   7487    -18   -159    366       C  
ATOM   2576  CZ  TYR A 337      25.968  23.706  11.807  1.00 61.06           C  
ANISOU 2576  CZ  TYR A 337     7617   7591   7993     16   -180    363       C  
ATOM   2577  OH  TYR A 337      26.676  24.209  12.888  1.00 61.65           O  
ANISOU 2577  OH  TYR A 337     7720   7622   8083     18   -197    355       O  
ATOM   2578  N   PHE A 338      25.382  22.436   5.963  1.00 33.33           N  
ANISOU 2578  N   PHE A 338     4034   4224   4407    -58   -137    422       N  
ATOM   2579  CA  PHE A 338      26.759  22.379   5.457  1.00 32.18           C  
ANISOU 2579  CA  PHE A 338     3890   4069   4268    -87   -125    436       C  
ATOM   2580  C   PHE A 338      27.041  23.292   4.287  1.00 36.78           C  
ANISOU 2580  C   PHE A 338     4482   4654   4837    -99   -132    472       C  
ATOM   2581  O   PHE A 338      28.194  23.651   4.060  1.00 43.74           O  
ANISOU 2581  O   PHE A 338     5366   5525   5729   -124   -127    493       O  
ATOM   2582  CB  PHE A 338      27.105  20.944   5.091  1.00 29.27           C  
ANISOU 2582  CB  PHE A 338     3505   3730   3887   -103    -99    414       C  
ATOM   2583  CG  PHE A 338      27.111  20.040   6.272  1.00 31.70           C  
ANISOU 2583  CG  PHE A 338     3811   4025   4208    -98    -92    384       C  
ATOM   2584  CD1 PHE A 338      25.941  19.395   6.677  1.00 26.72           C  
ANISOU 2584  CD1 PHE A 338     3177   3408   3567    -91    -93    363       C  
ATOM   2585  CD2 PHE A 338      28.257  19.892   7.033  1.00 28.05           C  
ANISOU 2585  CD2 PHE A 338     3350   3541   3769   -101    -87    381       C  
ATOM   2586  CE1 PHE A 338      25.933  18.563   7.807  1.00 24.81           C  
ANISOU 2586  CE1 PHE A 338     2938   3153   3335    -90    -86    340       C  
ATOM   2587  CE2 PHE A 338      28.258  19.051   8.169  1.00 33.71           C  
ANISOU 2587  CE2 PHE A 338     4069   4243   4494    -93    -83    355       C  
ATOM   2588  CZ  PHE A 338      27.102  18.395   8.554  1.00 31.49           C  
ANISOU 2588  CZ  PHE A 338     3792   3972   4202    -88    -81    336       C  
ATOM   2589  N   LEU A 339      26.003  23.668   3.547  1.00 32.81           N  
ANISOU 2589  N   LEU A 339     3984   4172   4311    -81   -143    483       N  
ATOM   2590  CA  LEU A 339      26.186  24.513   2.374  1.00 37.52           C  
ANISOU 2590  CA  LEU A 339     4595   4772   4889    -90   -150    521       C  
ATOM   2591  C   LEU A 339      26.653  25.928   2.757  1.00 39.97           C  
ANISOU 2591  C   LEU A 339     4942   5027   5220    -91   -173    551       C  
ATOM   2592  O   LEU A 339      27.442  26.531   2.034  1.00 37.04           O  
ANISOU 2592  O   LEU A 339     4583   4646   4843   -120   -172    586       O  
ATOM   2593  CB  LEU A 339      24.892  24.605   1.529  1.00 30.07           C  
ANISOU 2593  CB  LEU A 339     3648   3866   3912    -65   -162    527       C  
ATOM   2594  CG  LEU A 339      24.264  23.255   1.160  1.00 38.25           C  
ANISOU 2594  CG  LEU A 339     4654   4954   4925    -72   -148    496       C  
ATOM   2595  CD1 LEU A 339      23.003  23.418   0.331  1.00 38.15           C  
ANISOU 2595  CD1 LEU A 339     4633   4985   4878    -53   -166    504       C  
ATOM   2596  CD2 LEU A 339      25.245  22.353   0.426  1.00 38.53           C  
ANISOU 2596  CD2 LEU A 339     4686   5008   4948   -105   -121    490       C  
ATOM   2597  N   VAL A 340      26.160  26.455   3.873  1.00 40.77           N  
ANISOU 2597  N   VAL A 340     5063   5090   5339    -60   -193    538       N  
ATOM   2598  CA  VAL A 340      26.456  27.844   4.232  1.00 49.69           C  
ANISOU 2598  CA  VAL A 340     6242   6156   6482    -57   -222    563       C  
ATOM   2599  C   VAL A 340      27.879  28.023   4.703  1.00 55.76           C  
ANISOU 2599  C   VAL A 340     7018   6892   7277   -106   -221    571       C  
ATOM   2600  O   VAL A 340      28.336  29.141   4.835  1.00 66.11           O  
ANISOU 2600  O   VAL A 340     8372   8149   8596   -123   -245    597       O  
ATOM   2601  CB  VAL A 340      25.518  28.433   5.315  1.00 52.16           C  
ANISOU 2601  CB  VAL A 340     6582   6435   6801     -1   -245    544       C  
ATOM   2602  CG1 VAL A 340      24.074  28.440   4.838  1.00 57.77           C  
ANISOU 2602  CG1 VAL A 340     7280   7185   7482     52   -250    542       C  
ATOM   2603  CG2 VAL A 340      25.651  27.668   6.624  1.00 49.37           C  
ANISOU 2603  CG2 VAL A 340     6210   6082   6468      2   -235    504       C  
ATOM   2604  N   TYR A 341      28.591  26.934   4.940  1.00 53.94           N  
ANISOU 2604  N   TYR A 341     6745   6693   7055   -129   -195    552       N  
ATOM   2605  CA  TYR A 341      29.961  27.060   5.387  1.00 61.01           C  
ANISOU 2605  CA  TYR A 341     7635   7571   7974   -174   -196    561       C  
ATOM   2606  C   TYR A 341      30.900  27.201   4.220  1.00 70.26           C  
ANISOU 2606  C   TYR A 341     8791   8772   9134   -220   -180    600       C  
ATOM   2607  O   TYR A 341      31.736  28.106   4.205  1.00 83.12           O  
ANISOU 2607  O   TYR A 341    10436  10371  10773   -263   -196    633       O  
ATOM   2608  CB  TYR A 341      30.377  25.875   6.265  1.00 70.66           C  
ANISOU 2608  CB  TYR A 341     8822   8815   9211   -170   -178    524       C  
ATOM   2609  CG  TYR A 341      29.988  26.065   7.711  1.00 72.43           C  
ANISOU 2609  CG  TYR A 341     9069   8999   9453   -144   -199    496       C  
ATOM   2610  CD1 TYR A 341      28.703  25.768   8.149  1.00 63.39           C  
ANISOU 2610  CD1 TYR A 341     7930   7857   8298    -96   -199    470       C  
ATOM   2611  CD2 TYR A 341      30.901  26.578   8.632  1.00 76.07           C  
ANISOU 2611  CD2 TYR A 341     9544   9421   9936   -168   -220    498       C  
ATOM   2612  CE1 TYR A 341      28.343  25.962   9.452  1.00 65.09           C  
ANISOU 2612  CE1 TYR A 341     8166   8041   8523    -69   -214    446       C  
ATOM   2613  CE2 TYR A 341      30.551  26.769   9.944  1.00 74.47           C  
ANISOU 2613  CE2 TYR A 341     9368   9182   9744   -141   -240    471       C  
ATOM   2614  CZ  TYR A 341      29.268  26.462  10.349  1.00 73.29           C  
ANISOU 2614  CZ  TYR A 341     9226   9038   9582    -89   -235    445       C  
ATOM   2615  OH  TYR A 341      28.915  26.650  11.659  1.00 78.11           O  
ANISOU 2615  OH  TYR A 341     9862   9618  10197    -58   -251    419       O  
ATOM   2616  N   GLY A 342      30.766  26.335   3.221  1.00 62.48           N  
ANISOU 2616  N   GLY A 342     7774   7843   8123   -214   -150    598       N  
ATOM   2617  CA  GLY A 342      31.783  26.315   2.190  1.00 56.91           C  
ANISOU 2617  CA  GLY A 342     7044   7176   7402   -254   -127    631       C  
ATOM   2618  C   GLY A 342      31.373  26.184   0.741  1.00 55.82           C  
ANISOU 2618  C   GLY A 342     6905   7080   7223   -250   -110    650       C  
ATOM   2619  O   GLY A 342      32.209  25.849  -0.097  1.00 63.55           O  
ANISOU 2619  O   GLY A 342     7857   8106   8183   -273    -81    669       O  
ATOM   2620  N   VAL A 343      30.111  26.431   0.419  1.00 45.19           N  
ANISOU 2620  N   VAL A 343     5585   5724   5860   -216   -126    646       N  
ATOM   2621  CA  VAL A 343      29.727  26.375  -0.982  1.00 38.17           C  
ANISOU 2621  CA  VAL A 343     4698   4876   4929   -213   -115    667       C  
ATOM   2622  C   VAL A 343      29.357  27.773  -1.463  1.00 36.69           C  
ANISOU 2622  C   VAL A 343     4557   4652   4732   -216   -144    713       C  
ATOM   2623  O   VAL A 343      28.419  28.363  -0.981  1.00 44.52           O  
ANISOU 2623  O   VAL A 343     5579   5606   5731   -182   -174    707       O  
ATOM   2624  CB  VAL A 343      28.570  25.380  -1.214  1.00 37.75           C  
ANISOU 2624  CB  VAL A 343     4633   4858   4854   -176   -111    627       C  
ATOM   2625  CG1 VAL A 343      28.196  25.303  -2.704  1.00 31.70           C  
ANISOU 2625  CG1 VAL A 343     3869   4136   4037   -175   -103    647       C  
ATOM   2626  CG2 VAL A 343      28.940  24.037  -0.661  1.00 37.83           C  
ANISOU 2626  CG2 VAL A 343     4612   4889   4874   -174    -87    584       C  
ATOM   2627  N   PRO A 344      30.111  28.316  -2.413  1.00 36.41           N  
ANISOU 2627  N   PRO A 344     4529   4630   4676   -255   -134    761       N  
ATOM   2628  CA  PRO A 344      29.811  29.708  -2.759  1.00 39.41           C  
ANISOU 2628  CA  PRO A 344     4966   4961   5048   -261   -165    808       C  
ATOM   2629  C   PRO A 344      28.356  29.868  -3.251  1.00 42.37           C  
ANISOU 2629  C   PRO A 344     5364   5340   5395   -203   -186    803       C  
ATOM   2630  O   PRO A 344      27.841  29.000  -3.969  1.00 41.45           O  
ANISOU 2630  O   PRO A 344     5218   5283   5247   -184   -169    785       O  
ATOM   2631  CB  PRO A 344      30.797  30.004  -3.893  1.00 40.12           C  
ANISOU 2631  CB  PRO A 344     5050   5083   5110   -314   -142    862       C  
ATOM   2632  CG  PRO A 344      31.930  28.971  -3.718  1.00 39.05           C  
ANISOU 2632  CG  PRO A 344     4852   5003   4984   -342   -102    842       C  
ATOM   2633  CD  PRO A 344      31.234  27.747  -3.185  1.00 36.34           C  
ANISOU 2633  CD  PRO A 344     4482   4680   4648   -292    -94    777       C  
ATOM   2634  N   GLY A 345      27.710  30.962  -2.861  1.00 38.34           N  
ANISOU 2634  N   GLY A 345     4908   4768   4893   -175   -224    819       N  
ATOM   2635  CA  GLY A 345      26.345  31.246  -3.269  1.00 34.79           C  
ANISOU 2635  CA  GLY A 345     4478   4325   4416   -113   -248    819       C  
ATOM   2636  C   GLY A 345      25.379  30.962  -2.134  1.00 39.71           C  
ANISOU 2636  C   GLY A 345     5089   4939   5061    -57   -263    770       C  
ATOM   2637  O   GLY A 345      24.205  31.374  -2.162  1.00 43.36           O  
ANISOU 2637  O   GLY A 345     5567   5401   5507      4   -288    769       O  
ATOM   2638  N   PHE A 346      25.859  30.248  -1.121  1.00 37.94           N  
ANISOU 2638  N   PHE A 346     4833   4713   4870    -74   -246    732       N  
ATOM   2639  CA  PHE A 346      25.006  29.929   0.025  1.00 44.95           C  
ANISOU 2639  CA  PHE A 346     5707   5596   5776    -26   -256    687       C  
ATOM   2640  C   PHE A 346      25.262  30.815   1.248  1.00 41.49           C  
ANISOU 2640  C   PHE A 346     5314   5079   5369    -15   -279    683       C  
ATOM   2641  O   PHE A 346      26.384  31.204   1.504  1.00 47.61           O  
ANISOU 2641  O   PHE A 346     6112   5813   6165    -65   -280    700       O  
ATOM   2642  CB  PHE A 346      25.095  28.435   0.373  1.00 37.58           C  
ANISOU 2642  CB  PHE A 346     4713   4715   4850    -42   -225    643       C  
ATOM   2643  CG  PHE A 346      24.494  27.558  -0.674  1.00 33.03           C  
ANISOU 2643  CG  PHE A 346     4102   4210   4238    -40   -212    635       C  
ATOM   2644  CD1 PHE A 346      25.218  27.221  -1.815  1.00 32.24           C  
ANISOU 2644  CD1 PHE A 346     3995   4141   4114    -78   -191    655       C  
ATOM   2645  CD2 PHE A 346      23.180  27.109  -0.553  1.00 31.82           C  
ANISOU 2645  CD2 PHE A 346     3924   4097   4071      0   -221    611       C  
ATOM   2646  CE1 PHE A 346      24.651  26.434  -2.825  1.00 34.06           C  
ANISOU 2646  CE1 PHE A 346     4202   4434   4305    -76   -182    646       C  
ATOM   2647  CE2 PHE A 346      22.626  26.306  -1.514  1.00 25.12           C  
ANISOU 2647  CE2 PHE A 346     3045   3312   3186     -7   -215    603       C  
ATOM   2648  CZ  PHE A 346      23.336  25.969  -2.668  1.00 28.64           C  
ANISOU 2648  CZ  PHE A 346     3494   3782   3607    -43   -197    618       C  
ATOM   2649  N   SER A 347      24.200  31.115   1.991  1.00 41.98           N  
ANISOU 2649  N   SER A 347     5389   5128   5431     50   -298    662       N  
ATOM   2650  CA  SER A 347      24.274  32.010   3.144  1.00 45.92           C  
ANISOU 2650  CA  SER A 347     5944   5552   5953     75   -323    653       C  
ATOM   2651  C   SER A 347      23.073  31.849   4.067  1.00 42.73           C  
ANISOU 2651  C   SER A 347     5525   5165   5545    151   -329    616       C  
ATOM   2652  O   SER A 347      21.969  31.573   3.609  1.00 42.44           O  
ANISOU 2652  O   SER A 347     5456   5187   5483    197   -327    613       O  
ATOM   2653  CB  SER A 347      24.336  33.479   2.682  1.00 48.38           C  
ANISOU 2653  CB  SER A 347     6338   5791   6252     86   -358    698       C  
ATOM   2654  OG  SER A 347      24.303  34.337   3.808  1.00 48.47           O  
ANISOU 2654  OG  SER A 347     6414   5725   6279    118   -386    684       O  
ATOM   2655  N   LYS A 348      23.273  32.048   5.365  1.00 38.63           N  
ANISOU 2655  N   LYS A 348     5030   4601   5048    164   -336    589       N  
ATOM   2656  CA  LYS A 348      22.141  32.041   6.281  1.00 42.07           C  
ANISOU 2656  CA  LYS A 348     5457   5053   5474    242   -340    557       C  
ATOM   2657  C   LYS A 348      21.319  33.312   6.140  1.00 44.59           C  
ANISOU 2657  C   LYS A 348     5838   5333   5770    321   -372    575       C  
ATOM   2658  O   LYS A 348      20.154  33.328   6.540  1.00 45.21           O  
ANISOU 2658  O   LYS A 348     5897   5450   5829    400   -373    557       O  
ATOM   2659  CB  LYS A 348      22.590  31.864   7.745  1.00 45.30           C  
ANISOU 2659  CB  LYS A 348     5877   5428   5907    238   -338    522       C  
ATOM   2660  CG  LYS A 348      23.199  33.102   8.393  1.00 48.95           C  
ANISOU 2660  CG  LYS A 348     6430   5789   6380    242   -372    527       C  
ATOM   2661  CD  LYS A 348      23.628  32.833   9.851  1.00 53.56           C  
ANISOU 2661  CD  LYS A 348     7021   6347   6982    237   -371    488       C  
ATOM   2662  CE  LYS A 348      23.487  34.078  10.729  1.00 56.06           C  
ANISOU 2662  CE  LYS A 348     7432   6578   7292    290   -408    477       C  
ATOM   2663  NZ  LYS A 348      22.057  34.592  10.768  1.00 56.89           N  
ANISOU 2663  NZ  LYS A 348     7552   6699   7364    399   -413    470       N  
ATOM   2664  N   ASP A 349      21.916  34.361   5.559  1.00 41.61           N  
ANISOU 2664  N   ASP A 349     5535   4884   5391    301   -398    612       N  
ATOM   2665  CA  ASP A 349      21.321  35.715   5.575  1.00 44.84           C  
ANISOU 2665  CA  ASP A 349     6030   5228   5780    378   -435    628       C  
ATOM   2666  C   ASP A 349      20.540  36.110   4.324  1.00 48.02           C  
ANISOU 2666  C   ASP A 349     6435   5662   6149    421   -446    665       C  
ATOM   2667  O   ASP A 349      20.139  37.261   4.196  1.00 48.21           O  
ANISOU 2667  O   ASP A 349     6540   5626   6153    484   -479    686       O  
ATOM   2668  CB  ASP A 349      22.377  36.795   5.861  1.00 43.88           C  
ANISOU 2668  CB  ASP A 349     6010   4988   5674    335   -466    647       C  
ATOM   2669  CG  ASP A 349      23.028  36.625   7.228  1.00 50.53           C  
ANISOU 2669  CG  ASP A 349     6865   5792   6544    309   -467    609       C  
ATOM   2670  OD1 ASP A 349      22.315  36.264   8.197  1.00 44.69           O  
ANISOU 2670  OD1 ASP A 349     6099   5080   5799    372   -457    567       O  
ATOM   2671  OD2 ASP A 349      24.269  36.816   7.319  1.00 55.94           O  
ANISOU 2671  OD2 ASP A 349     7578   6425   7252    221   -476    622       O  
ATOM   2672  N   ASN A 350      20.353  35.169   3.403  1.00 44.31           N  
ANISOU 2672  N   ASN A 350     5886   5281   5669    389   -422    674       N  
ATOM   2673  CA  ASN A 350      19.494  35.380   2.248  1.00 44.04           C  
ANISOU 2673  CA  ASN A 350     5840   5296   5598    433   -433    704       C  
ATOM   2674  C   ASN A 350      18.995  34.050   1.770  1.00 42.15           C  
ANISOU 2674  C   ASN A 350     5496   5171   5349    411   -404    687       C  
ATOM   2675  O   ASN A 350      19.328  33.014   2.347  1.00 43.87           O  
ANISOU 2675  O   ASN A 350     5660   5421   5589    365   -376    653       O  
ATOM   2676  CB  ASN A 350      20.189  36.148   1.105  1.00 41.16           C  
ANISOU 2676  CB  ASN A 350     5539   4879   5221    389   -449    759       C  
ATOM   2677  CG  ASN A 350      21.363  35.404   0.513  1.00 46.88           C  
ANISOU 2677  CG  ASN A 350     6229   5623   5961    279   -421    770       C  
ATOM   2678  OD1 ASN A 350      21.332  34.184   0.376  1.00 49.50           O  
ANISOU 2678  OD1 ASN A 350     6478   6034   6295    249   -391    746       O  
ATOM   2679  ND2 ASN A 350      22.417  36.153   0.148  1.00 57.34           N  
ANISOU 2679  ND2 ASN A 350     7620   6875   7292    219   -432    810       N  
ATOM   2680  N   GLU A 351      18.219  34.075   0.701  1.00 38.45           N  
ANISOU 2680  N   GLU A 351     5005   4760   4844    442   -414    710       N  
ATOM   2681  CA  GLU A 351      17.548  32.884   0.223  1.00 40.96           C  
ANISOU 2681  CA  GLU A 351     5229   5189   5146    427   -396    693       C  
ATOM   2682  C   GLU A 351      18.477  31.918  -0.520  1.00 37.69           C  
ANISOU 2682  C   GLU A 351     4785   4797   4737    329   -370    695       C  
ATOM   2683  O   GLU A 351      18.063  30.821  -0.878  1.00 34.39           O  
ANISOU 2683  O   GLU A 351     4300   4460   4307    304   -354    675       O  
ATOM   2684  CB  GLU A 351      16.350  33.274  -0.658  1.00 47.09           C  
ANISOU 2684  CB  GLU A 351     5989   6026   5877    498   -421    717       C  
ATOM   2685  CG  GLU A 351      15.117  33.673   0.136  1.00 62.13           C  
ANISOU 2685  CG  GLU A 351     7874   7963   7770    602   -436    701       C  
ATOM   2686  CD  GLU A 351      14.472  32.470   0.828  1.00 81.25           C  
ANISOU 2686  CD  GLU A 351    10198  10476  10198    590   -411    659       C  
ATOM   2687  OE1 GLU A 351      13.715  31.693   0.167  1.00 87.60           O  
ANISOU 2687  OE1 GLU A 351    10926  11382  10978    577   -410    658       O  
ATOM   2688  OE2 GLU A 351      14.728  32.298   2.039  1.00 81.81           O  
ANISOU 2688  OE2 GLU A 351    10272  10517  10297    588   -394    628       O  
ATOM   2689  N   SER A 352      19.721  32.316  -0.770  1.00 40.37           N  
ANISOU 2689  N   SER A 352     5176   5069   5092    273   -365    718       N  
ATOM   2690  CA  SER A 352      20.676  31.409  -1.408  1.00 34.40           C  
ANISOU 2690  CA  SER A 352     4391   4340   4339    188   -336    718       C  
ATOM   2691  C   SER A 352      20.149  30.840  -2.723  1.00 35.57           C  
ANISOU 2691  C   SER A 352     4502   4567   4445    182   -333    730       C  
ATOM   2692  O   SER A 352      20.356  29.668  -3.014  1.00 34.88           O  
ANISOU 2692  O   SER A 352     4367   4532   4353    137   -309    706       O  
ATOM   2693  CB  SER A 352      20.971  30.238  -0.477  1.00 32.61           C  
ANISOU 2693  CB  SER A 352     4114   4135   4142    155   -307    670       C  
ATOM   2694  OG  SER A 352      21.622  30.670   0.700  1.00 40.32           O  
ANISOU 2694  OG  SER A 352     5123   5041   5155    151   -309    659       O  
ATOM   2695  N   LEU A 353      19.459  31.649  -3.514  1.00 33.18           N  
ANISOU 2695  N   LEU A 353     4227   4273   4108    229   -361    765       N  
ATOM   2696  CA  LEU A 353      19.030  31.210  -4.824  1.00 36.07           C  
ANISOU 2696  CA  LEU A 353     4566   4712   4429    221   -364    779       C  
ATOM   2697  C   LEU A 353      20.256  31.198  -5.735  1.00 45.68           C  
ANISOU 2697  C   LEU A 353     5811   5909   5635    153   -344    809       C  
ATOM   2698  O   LEU A 353      20.768  32.243  -6.092  1.00 62.96           O  
ANISOU 2698  O   LEU A 353     8062   8040   7818    150   -355    855       O  
ATOM   2699  CB  LEU A 353      17.968  32.171  -5.373  1.00 35.99           C  
ANISOU 2699  CB  LEU A 353     4579   4714   4381    299   -403    813       C  
ATOM   2700  CG  LEU A 353      16.685  32.314  -4.547  1.00 41.74           C  
ANISOU 2700  CG  LEU A 353     5274   5474   5111    381   -424    789       C  
ATOM   2701  CD1 LEU A 353      15.774  33.458  -5.078  1.00 44.44           C  
ANISOU 2701  CD1 LEU A 353     5652   5817   5415    472   -465    828       C  
ATOM   2702  CD2 LEU A 353      15.927  31.026  -4.513  1.00 39.05           C  
ANISOU 2702  CD2 LEU A 353     4842   5234   4761    364   -413    750       C  
ATOM   2703  N   ILE A 354      20.728  30.027  -6.118  1.00 37.54           N  
ANISOU 2703  N   ILE A 354     4739   4927   4598     98   -314    785       N  
ATOM   2704  CA  ILE A 354      21.951  29.914  -6.888  1.00 28.73           C  
ANISOU 2704  CA  ILE A 354     3640   3803   3471     38   -287    810       C  
ATOM   2705  C   ILE A 354      21.742  29.654  -8.387  1.00 33.95           C  
ANISOU 2705  C   ILE A 354     4299   4528   4074     30   -287    831       C  
ATOM   2706  O   ILE A 354      20.636  29.328  -8.857  1.00 35.24           O  
ANISOU 2706  O   ILE A 354     4437   4748   4203     62   -308    819       O  
ATOM   2707  CB  ILE A 354      22.870  28.813  -6.287  1.00 35.19           C  
ANISOU 2707  CB  ILE A 354     4423   4627   4321    -12   -249    769       C  
ATOM   2708  CG1 ILE A 354      22.145  27.468  -6.252  1.00 29.26           C  
ANISOU 2708  CG1 ILE A 354     3620   3941   3559    -10   -242    718       C  
ATOM   2709  CG2 ILE A 354      23.231  29.184  -4.896  1.00 36.65           C  
ANISOU 2709  CG2 ILE A 354     4618   4748   4559     -9   -251    756       C  
ATOM   2710  CD1 ILE A 354      23.043  26.234  -6.367  1.00 26.77           C  
ANISOU 2710  CD1 ILE A 354     3281   3647   3244    -57   -203    687       C  
ATOM   2711  N   SER A 355      22.825  29.819  -9.137  1.00 30.62           N  
ANISOU 2711  N   SER A 355     3901   4099   3636    -16   -264    865       N  
ATOM   2712  CA  SER A 355      22.821  29.591 -10.572  1.00 30.22           C  
ANISOU 2712  CA  SER A 355     3854   4105   3523    -28   -257    887       C  
ATOM   2713  C   SER A 355      23.247  28.153 -10.902  1.00 30.34           C  
ANISOU 2713  C   SER A 355     3827   4177   3522    -63   -222    843       C  
ATOM   2714  O   SER A 355      23.729  27.417 -10.044  1.00 28.30           O  
ANISOU 2714  O   SER A 355     3542   3908   3304    -82   -199    803       O  
ATOM   2715  CB  SER A 355      23.829  30.542 -11.203  1.00 35.28           C  
ANISOU 2715  CB  SER A 355     4544   4711   4150    -61   -246    951       C  
ATOM   2716  OG  SER A 355      25.126  30.124 -10.782  1.00 38.02           O  
ANISOU 2716  OG  SER A 355     4872   5046   4527   -115   -205    942       O  
ATOM   2717  N   ARG A 356      23.082  27.766 -12.159  1.00 32.22           N  
ANISOU 2717  N   ARG A 356     4067   4475   3700    -67   -219    850       N  
ATOM   2718  CA  ARG A 356      23.512  26.456 -12.598  1.00 35.49           C  
ANISOU 2718  CA  ARG A 356     4458   4939   4089    -94   -186    809       C  
ATOM   2719  C   ARG A 356      25.019  26.326 -12.400  1.00 35.86           C  
ANISOU 2719  C   ARG A 356     4503   4966   4157   -132   -139    817       C  
ATOM   2720  O   ARG A 356      25.483  25.325 -11.905  1.00 38.44           O  
ANISOU 2720  O   ARG A 356     4804   5298   4502   -145   -113    772       O  
ATOM   2721  CB  ARG A 356      23.130  26.204 -14.065  1.00 36.54           C  
ANISOU 2721  CB  ARG A 356     4604   5136   4144    -91   -193    819       C  
ATOM   2722  CG  ARG A 356      23.493  24.808 -14.553  1.00 44.21           C  
ANISOU 2722  CG  ARG A 356     5562   6155   5082   -112   -164    770       C  
ATOM   2723  CD  ARG A 356      22.438  24.160 -15.458  1.00 43.36           C  
ANISOU 2723  CD  ARG A 356     5455   6107   4912   -102   -194    744       C  
ATOM   2724  NE  ARG A 356      22.738  22.736 -15.661  1.00 47.77           N  
ANISOU 2724  NE  ARG A 356     6010   6692   5447   -122   -170    685       N  
ATOM   2725  CZ  ARG A 356      22.237  21.730 -14.942  1.00 43.27           C  
ANISOU 2725  CZ  ARG A 356     5421   6118   4903   -132   -180    627       C  
ATOM   2726  NH1 ARG A 356      21.363  21.945 -13.965  1.00 40.19           N  
ANISOU 2726  NH1 ARG A 356     5002   5708   4559   -123   -210    619       N  
ATOM   2727  NH2 ARG A 356      22.598  20.492 -15.222  1.00 46.96           N  
ANISOU 2727  NH2 ARG A 356     5901   6600   5343   -148   -159    578       N  
ATOM   2728  N   ALA A 357      25.773  27.346 -12.764  1.00 32.12           N  
ANISOU 2728  N   ALA A 357     4057   4471   3678   -151   -129    877       N  
ATOM   2729  CA  ALA A 357      27.218  27.314 -12.542  1.00 38.07           C  
ANISOU 2729  CA  ALA A 357     4798   5215   4452   -192    -86    892       C  
ATOM   2730  C   ALA A 357      27.585  27.046 -11.082  1.00 34.54           C  
ANISOU 2730  C   ALA A 357     4325   4722   4074   -198    -82    857       C  
ATOM   2731  O   ALA A 357      28.491  26.288 -10.792  1.00 36.97           O  
ANISOU 2731  O   ALA A 357     4604   5048   4396   -216    -46    833       O  
ATOM   2732  CB  ALA A 357      27.893  28.637 -13.055  1.00 33.02           C  
ANISOU 2732  CB  ALA A 357     4195   4553   3800   -222    -84    972       C  
ATOM   2733  N   GLN A 358      26.899  27.678 -10.152  1.00 33.59           N  
ANISOU 2733  N   GLN A 358     4218   4547   3997   -178   -118    855       N  
ATOM   2734  CA  GLN A 358      27.239  27.465  -8.756  1.00 31.27           C  
ANISOU 2734  CA  GLN A 358     3905   4211   3765   -183   -115    823       C  
ATOM   2735  C   GLN A 358      26.780  26.068  -8.293  1.00 32.30           C  
ANISOU 2735  C   GLN A 358     4000   4370   3902   -166   -106    755       C  
ATOM   2736  O   GLN A 358      27.357  25.493  -7.367  1.00 33.11           O  
ANISOU 2736  O   GLN A 358     4081   4458   4043   -176    -89    724       O  
ATOM   2737  CB  GLN A 358      26.638  28.568  -7.866  1.00 35.58           C  
ANISOU 2737  CB  GLN A 358     4482   4688   4348   -162   -156    838       C  
ATOM   2738  CG  GLN A 358      27.131  29.999  -8.137  1.00 29.75           C  
ANISOU 2738  CG  GLN A 358     3794   3899   3609   -184   -170    905       C  
ATOM   2739  CD  GLN A 358      26.236  31.044  -7.470  1.00 38.41           C  
ANISOU 2739  CD  GLN A 358     4936   4930   4728   -142   -216    914       C  
ATOM   2740  OE1 GLN A 358      24.992  31.040  -7.624  1.00 42.92           O  
ANISOU 2740  OE1 GLN A 358     5510   5519   5280    -86   -242    901       O  
ATOM   2741  NE2 GLN A 358      26.851  31.934  -6.715  1.00 38.60           N  
ANISOU 2741  NE2 GLN A 358     4996   4882   4788   -165   -229    936       N  
ATOM   2742  N   PHE A 359      25.762  25.514  -8.948  1.00 28.71           N  
ANISOU 2742  N   PHE A 359     3542   3958   3408   -144   -120    733       N  
ATOM   2743  CA  PHE A 359      25.341  24.139  -8.643  1.00 29.94           C  
ANISOU 2743  CA  PHE A 359     3673   4140   3563   -139   -113    672       C  
ATOM   2744  C   PHE A 359      26.447  23.179  -9.068  1.00 29.78           C  
ANISOU 2744  C   PHE A 359     3645   4147   3523   -159    -70    653       C  
ATOM   2745  O   PHE A 359      26.855  22.336  -8.281  1.00 30.71           O  
ANISOU 2745  O   PHE A 359     3747   4252   3669   -162    -53    615       O  
ATOM   2746  CB  PHE A 359      24.029  23.789  -9.340  1.00 31.51           C  
ANISOU 2746  CB  PHE A 359     3872   4383   3719   -121   -142    656       C  
ATOM   2747  CG  PHE A 359      23.578  22.361  -9.132  1.00 30.52           C  
ANISOU 2747  CG  PHE A 359     3728   4282   3586   -129   -139    596       C  
ATOM   2748  CD1 PHE A 359      23.461  21.503 -10.198  1.00 29.22           C  
ANISOU 2748  CD1 PHE A 359     3574   4164   3364   -140   -134    575       C  
ATOM   2749  CD2 PHE A 359      23.265  21.889  -7.885  1.00 30.02           C  
ANISOU 2749  CD2 PHE A 359     3646   4193   3568   -129   -143    562       C  
ATOM   2750  CE1 PHE A 359      23.030  20.194 -10.027  1.00 27.28           C  
ANISOU 2750  CE1 PHE A 359     3324   3932   3109   -154   -136    520       C  
ATOM   2751  CE2 PHE A 359      22.858  20.562  -7.706  1.00 28.47           C  
ANISOU 2751  CE2 PHE A 359     3441   4014   3362   -144   -141    511       C  
ATOM   2752  CZ  PHE A 359      22.739  19.726  -8.796  1.00 25.27           C  
ANISOU 2752  CZ  PHE A 359     3051   3648   2901   -158   -140    490       C  
ATOM   2753  N   LEU A 360      26.928  23.311 -10.306  1.00 33.01           N  
ANISOU 2753  N   LEU A 360     4066   4594   3880   -167    -52    682       N  
ATOM   2754  CA  LEU A 360      28.010  22.444 -10.784  1.00 40.34           C  
ANISOU 2754  CA  LEU A 360     4987   5557   4782   -176     -6    666       C  
ATOM   2755  C   LEU A 360      29.212  22.574  -9.867  1.00 38.50           C  
ANISOU 2755  C   LEU A 360     4731   5299   4599   -190     21    674       C  
ATOM   2756  O   LEU A 360      29.748  21.577  -9.429  1.00 40.07           O  
ANISOU 2756  O   LEU A 360     4914   5503   4808   -182     44    635       O  
ATOM   2757  CB  LEU A 360      28.370  22.712 -12.257  1.00 42.54           C  
ANISOU 2757  CB  LEU A 360     5283   5888   4994   -180     13    702       C  
ATOM   2758  CG  LEU A 360      27.158  22.642 -13.219  1.00 53.02           C  
ANISOU 2758  CG  LEU A 360     6634   7245   6265   -166    -20    697       C  
ATOM   2759  CD1 LEU A 360      27.515  22.838 -14.703  1.00 56.12           C  
ANISOU 2759  CD1 LEU A 360     7048   7693   6583   -168     -1    731       C  
ATOM   2760  CD2 LEU A 360      26.399  21.360 -13.071  1.00 51.36           C  
ANISOU 2760  CD2 LEU A 360     6425   7046   6045   -156    -33    629       C  
ATOM   2761  N   ALA A 361      29.610  23.799  -9.531  1.00 36.84           N  
ANISOU 2761  N   ALA A 361     4521   5058   4420   -210     12    725       N  
ATOM   2762  CA  ALA A 361      30.736  23.975  -8.605  1.00 36.09           C  
ANISOU 2762  CA  ALA A 361     4400   4940   4372   -231     30    733       C  
ATOM   2763  C   ALA A 361      30.505  23.340  -7.214  1.00 36.77           C  
ANISOU 2763  C   ALA A 361     4473   4987   4511   -216     19    683       C  
ATOM   2764  O   ALA A 361      31.414  22.716  -6.665  1.00 40.82           O  
ANISOU 2764  O   ALA A 361     4960   5507   5043   -218     44    664       O  
ATOM   2765  CB  ALA A 361      31.157  25.458  -8.494  1.00 31.88           C  
ANISOU 2765  CB  ALA A 361     3880   4373   3860   -266     15    798       C  
ATOM   2766  N   GLY A 362      29.307  23.500  -6.655  1.00 32.19           N  
ANISOU 2766  N   GLY A 362     3908   4372   3949   -199    -18    664       N  
ATOM   2767  CA  GLY A 362      28.971  22.925  -5.361  1.00 32.07           C  
ANISOU 2767  CA  GLY A 362     3883   4324   3977   -186    -29    620       C  
ATOM   2768  C   GLY A 362      28.965  21.397  -5.381  1.00 38.70           C  
ANISOU 2768  C   GLY A 362     4713   5189   4800   -173     -8    567       C  
ATOM   2769  O   GLY A 362      29.351  20.739  -4.399  1.00 33.19           O  
ANISOU 2769  O   GLY A 362     4004   4472   4134   -168      1    537       O  
ATOM   2770  N   VAL A 363      28.551  20.815  -6.506  1.00 34.33           N  
ANISOU 2770  N   VAL A 363     4173   4677   4194   -167     -2    555       N  
ATOM   2771  CA  VAL A 363      28.629  19.368  -6.620  1.00 30.67           C  
ANISOU 2771  CA  VAL A 363     3716   4231   3709   -157     16    505       C  
ATOM   2772  C   VAL A 363      30.087  18.874  -6.497  1.00 36.39           C  
ANISOU 2772  C   VAL A 363     4425   4966   4436   -149     58    501       C  
ATOM   2773  O   VAL A 363      30.332  17.869  -5.831  1.00 36.90           O  
ANISOU 2773  O   VAL A 363     4490   5015   4514   -135     68    461       O  
ATOM   2774  CB  VAL A 363      27.938  18.835  -7.881  1.00 28.28           C  
ANISOU 2774  CB  VAL A 363     3437   3967   3343   -154     11    490       C  
ATOM   2775  CG1 VAL A 363      28.388  17.351  -8.169  1.00 25.29           C  
ANISOU 2775  CG1 VAL A 363     3077   3601   2930   -141     38    440       C  
ATOM   2776  CG2 VAL A 363      26.408  18.910  -7.691  1.00 32.70           C  
ANISOU 2776  CG2 VAL A 363     4000   4520   3904   -159    -32    477       C  
ATOM   2777  N   ARG A 364      31.050  19.595  -7.093  1.00 37.34           N  
ANISOU 2777  N   ARG A 364     4528   5115   4543   -159     80    546       N  
ATOM   2778  CA  ARG A 364      32.466  19.214  -6.989  1.00 34.49           C  
ANISOU 2778  CA  ARG A 364     4140   4781   4185   -151    121    548       C  
ATOM   2779  C   ARG A 364      32.973  19.355  -5.547  1.00 36.03           C  
ANISOU 2779  C   ARG A 364     4309   4937   4442   -156    113    545       C  
ATOM   2780  O   ARG A 364      33.813  18.579  -5.120  1.00 34.89           O  
ANISOU 2780  O   ARG A 364     4147   4805   4305   -136    137    524       O  
ATOM   2781  CB  ARG A 364      33.373  20.024  -7.916  1.00 35.59           C  
ANISOU 2781  CB  ARG A 364     4259   4970   4296   -169    147    604       C  
ATOM   2782  CG  ARG A 364      33.176  19.807  -9.401  1.00 40.85           C  
ANISOU 2782  CG  ARG A 364     4946   5687   4889   -159    164    609       C  
ATOM   2783  CD  ARG A 364      32.857  18.368  -9.701  1.00 53.98           C  
ANISOU 2783  CD  ARG A 364     6636   7359   6515   -120    175    546       C  
ATOM   2784  NE  ARG A 364      33.996  17.446  -9.569  1.00 61.05           N  
ANISOU 2784  NE  ARG A 364     7513   8284   7400    -86    217    522       N  
ATOM   2785  CZ  ARG A 364      34.721  17.015 -10.599  1.00 58.84           C  
ANISOU 2785  CZ  ARG A 364     7232   8066   7058    -58    259    523       C  
ATOM   2786  NH1 ARG A 364      34.446  17.462 -11.822  1.00 63.74           N  
ANISOU 2786  NH1 ARG A 364     7869   8725   7624    -69    264    549       N  
ATOM   2787  NH2 ARG A 364      35.717  16.163 -10.413  1.00 51.94           N  
ANISOU 2787  NH2 ARG A 364     6341   7219   6174    -16    296    499       N  
ATOM   2788  N   ILE A 365      32.470  20.351  -4.817  1.00 31.95           N  
ANISOU 2788  N   ILE A 365     3796   4377   3968   -179     79    567       N  
ATOM   2789  CA  ILE A 365      32.798  20.509  -3.402  1.00 36.11           C  
ANISOU 2789  CA  ILE A 365     4308   4863   4551   -184     66    559       C  
ATOM   2790  C   ILE A 365      32.083  19.485  -2.508  1.00 36.66           C  
ANISOU 2790  C   ILE A 365     4391   4900   4636   -159     54    506       C  
ATOM   2791  O   ILE A 365      32.681  18.941  -1.576  1.00 41.96           O  
ANISOU 2791  O   ILE A 365     5050   5559   5335   -148     61    486       O  
ATOM   2792  CB  ILE A 365      32.540  21.971  -2.939  1.00 33.95           C  
ANISOU 2792  CB  ILE A 365     4042   4547   4311   -213     33    599       C  
ATOM   2793  CG1 ILE A 365      33.442  22.902  -3.720  1.00 36.06           C  
ANISOU 2793  CG1 ILE A 365     4296   4842   4562   -248     46    656       C  
ATOM   2794  CG2 ILE A 365      32.763  22.157  -1.425  1.00 29.02           C  
ANISOU 2794  CG2 ILE A 365     3410   3876   3740   -217     13    587       C  
ATOM   2795  CD1 ILE A 365      33.006  24.371  -3.661  1.00 38.28           C  
ANISOU 2795  CD1 ILE A 365     4607   5077   4860   -276     11    700       C  
ATOM   2796  N   GLY A 366      30.821  19.194  -2.819  1.00 38.20           N  
ANISOU 2796  N   GLY A 366     4613   5088   4813   -153     36    485       N  
ATOM   2797  CA  GLY A 366      30.033  18.208  -2.072  1.00 32.53           C  
ANISOU 2797  CA  GLY A 366     3911   4345   4105   -141     25    438       C  
ATOM   2798  C   GLY A 366      30.440  16.762  -2.306  1.00 37.63           C  
ANISOU 2798  C   GLY A 366     4570   5003   4723   -121     50    399       C  
ATOM   2799  O   GLY A 366      30.183  15.904  -1.467  1.00 35.52           O  
ANISOU 2799  O   GLY A 366     4317   4707   4471   -114     45    365       O  
ATOM   2800  N   VAL A 367      31.056  16.480  -3.456  1.00 35.25           N  
ANISOU 2800  N   VAL A 367     4273   4743   4379   -111     76    403       N  
ATOM   2801  CA  VAL A 367      31.453  15.126  -3.786  1.00 28.53           C  
ANISOU 2801  CA  VAL A 367     3447   3901   3494    -83    100    363       C  
ATOM   2802  C   VAL A 367      32.923  15.206  -4.196  1.00 36.16           C  
ANISOU 2802  C   VAL A 367     4384   4910   4447    -60    138    383       C  
ATOM   2803  O   VAL A 367      33.263  14.949  -5.350  1.00 32.98           O  
ANISOU 2803  O   VAL A 367     3989   4549   3992    -45    163    384       O  
ATOM   2804  CB  VAL A 367      30.626  14.529  -4.954  1.00 34.23           C  
ANISOU 2804  CB  VAL A 367     4208   4639   4158    -85     95    339       C  
ATOM   2805  CG1 VAL A 367      30.879  13.024  -5.033  1.00 34.78           C  
ANISOU 2805  CG1 VAL A 367     4322   4696   4198    -57    110    289       C  
ATOM   2806  CG2 VAL A 367      29.089  14.815  -4.782  1.00 26.80           C  
ANISOU 2806  CG2 VAL A 367     3278   3680   3227   -117     53    336       C  
ATOM   2807  N   PRO A 368      33.799  15.553  -3.235  1.00 32.47           N  
ANISOU 2807  N   PRO A 368     3878   4436   4023    -58    143    400       N  
ATOM   2808  CA  PRO A 368      35.141  15.984  -3.620  1.00 31.92           C  
ANISOU 2808  CA  PRO A 368     3764   4420   3946    -52    175    435       C  
ATOM   2809  C   PRO A 368      35.951  14.822  -4.192  1.00 40.48           C  
ANISOU 2809  C   PRO A 368     4853   5545   4985      2    214    407       C  
ATOM   2810  O   PRO A 368      36.919  15.052  -4.890  1.00 41.82           O  
ANISOU 2810  O   PRO A 368     4986   5777   5126     13    248    434       O  
ATOM   2811  CB  PRO A 368      35.725  16.484  -2.312  1.00 29.04           C  
ANISOU 2811  CB  PRO A 368     3362   4034   3638    -65    161    451       C  
ATOM   2812  CG  PRO A 368      35.001  15.657  -1.271  1.00 30.29           C  
ANISOU 2812  CG  PRO A 368     3555   4134   3820    -49    140    406       C  
ATOM   2813  CD  PRO A 368      33.592  15.620  -1.770  1.00 25.42           C  
ANISOU 2813  CD  PRO A 368     2981   3493   3185    -66    119    391       C  
ATOM   2814  N   GLN A 369      35.523  13.588  -3.943  1.00 40.36           N  
ANISOU 2814  N   GLN A 369     4887   5494   4956     35    211    355       N  
ATOM   2815  CA  GLN A 369      36.261  12.432  -4.451  1.00 39.52           C  
ANISOU 2815  CA  GLN A 369     4800   5414   4803     96    246    323       C  
ATOM   2816  C   GLN A 369      35.832  12.064  -5.858  1.00 43.06           C  
ANISOU 2816  C   GLN A 369     5291   5886   5183    106    259    307       C  
ATOM   2817  O   GLN A 369      36.350  11.114  -6.421  1.00 42.62           O  
ANISOU 2817  O   GLN A 369     5265   5852   5079    162    287    276       O  
ATOM   2818  CB  GLN A 369      36.078  11.221  -3.532  1.00 34.38           C  
ANISOU 2818  CB  GLN A 369     4195   4704   4163    129    235    275       C  
ATOM   2819  CG  GLN A 369      34.698  10.538  -3.688  1.00 44.17           C  
ANISOU 2819  CG  GLN A 369     5510   5886   5386    107    206    235       C  
ATOM   2820  CD  GLN A 369      33.558  11.184  -2.863  1.00 43.00           C  
ANISOU 2820  CD  GLN A 369     5356   5694   5287     48    165    247       C  
ATOM   2821  OE1 GLN A 369      33.613  12.355  -2.478  1.00 35.41           O  
ANISOU 2821  OE1 GLN A 369     4344   4745   4364     18    155    286       O  
ATOM   2822  NE2 GLN A 369      32.517  10.400  -2.605  1.00 46.46           N  
ANISOU 2822  NE2 GLN A 369     5850   6084   5720     31    141    211       N  
ATOM   2823  N   ALA A 370      34.891  12.805  -6.437  1.00 42.59           N  
ANISOU 2823  N   ALA A 370     5241   5826   5118     59    236    325       N  
ATOM   2824  CA  ALA A 370      34.310  12.405  -7.734  1.00 42.21           C  
ANISOU 2824  CA  ALA A 370     5240   5795   5002     64    239    305       C  
ATOM   2825  C   ALA A 370      35.228  12.669  -8.932  1.00 43.04           C  
ANISOU 2825  C   ALA A 370     5323   5979   5051     90    283    330       C  
ATOM   2826  O   ALA A 370      35.837  13.712  -9.023  1.00 45.83           O  
ANISOU 2826  O   ALA A 370     5618   6376   5421     69    297    384       O  
ATOM   2827  CB  ALA A 370      32.943  13.098  -7.958  1.00 38.12           C  
ANISOU 2827  CB  ALA A 370     4736   5256   4491      8    197    318       C  
ATOM   2828  N   SER A 371      35.316  11.729  -9.864  1.00 41.31           N  
ANISOU 2828  N   SER A 371     5154   5780   4763    134    303    292       N  
ATOM   2829  CA  SER A 371      35.886  12.047 -11.169  1.00 39.52           C  
ANISOU 2829  CA  SER A 371     4913   5631   4472    152    341    317       C  
ATOM   2830  C   SER A 371      34.916  12.972 -11.906  1.00 38.82           C  
ANISOU 2830  C   SER A 371     4832   5549   4369     96    313    348       C  
ATOM   2831  O   SER A 371      33.808  13.230 -11.422  1.00 41.33           O  
ANISOU 2831  O   SER A 371     5166   5814   4724     53    266    343       O  
ATOM   2832  CB  SER A 371      36.063  10.779 -11.984  1.00 39.98           C  
ANISOU 2832  CB  SER A 371     5038   5700   4453    217    365    260       C  
ATOM   2833  OG  SER A 371      34.824  10.089 -12.143  1.00 44.88           O  
ANISOU 2833  OG  SER A 371     5740   6259   5055    197    322    211       O  
ATOM   2834  N   ASP A 372      35.308  13.426 -13.088  1.00 36.83           N  
ANISOU 2834  N   ASP A 372     4569   5366   4059    102    342    379       N  
ATOM   2835  CA  ASP A 372      34.459  14.282 -13.891  1.00 42.57           C  
ANISOU 2835  CA  ASP A 372     5307   6104   4762     57    317    411       C  
ATOM   2836  C   ASP A 372      33.163  13.590 -14.279  1.00 46.20           C  
ANISOU 2836  C   ASP A 372     5838   6525   5190     50    275    360       C  
ATOM   2837  O   ASP A 372      32.089  14.189 -14.233  1.00 42.99           O  
ANISOU 2837  O   ASP A 372     5437   6094   4803      5    230    375       O  
ATOM   2838  CB  ASP A 372      35.175  14.731 -15.154  1.00 44.84           C  
ANISOU 2838  CB  ASP A 372     5578   6477   4981     70    361    451       C  
ATOM   2839  CG  ASP A 372      36.175  15.824 -14.886  1.00 58.80           C  
ANISOU 2839  CG  ASP A 372     7270   8287   6783     44    388    522       C  
ATOM   2840  OD1 ASP A 372      36.251  16.261 -13.726  1.00 61.09           O  
ANISOU 2840  OD1 ASP A 372     7526   8535   7151     16    368    537       O  
ATOM   2841  OD2 ASP A 372      36.896  16.242 -15.825  1.00 67.67           O  
ANISOU 2841  OD2 ASP A 372     8369   9488   7854     48    430    564       O  
ATOM   2842  N   LEU A 373      33.273  12.338 -14.702  1.00 47.95           N  
ANISOU 2842  N   LEU A 373     6117   6744   5357     95    289    301       N  
ATOM   2843  CA  LEU A 373      32.096  11.611 -15.131  1.00 46.49           C  
ANISOU 2843  CA  LEU A 373     6004   6524   5135     80    247    251       C  
ATOM   2844  C   LEU A 373      31.157  11.391 -13.948  1.00 43.48           C  
ANISOU 2844  C   LEU A 373     5628   6069   4822     40    198    230       C  
ATOM   2845  O   LEU A 373      29.949  11.567 -14.079  1.00 49.99           O  
ANISOU 2845  O   LEU A 373     6469   6877   5647     -4    151    226       O  
ATOM   2846  CB  LEU A 373      32.476  10.299 -15.810  1.00 46.26           C  
ANISOU 2846  CB  LEU A 373     6047   6499   5030    137    270    189       C  
ATOM   2847  CG  LEU A 373      31.267   9.520 -16.343  1.00 55.77           C  
ANISOU 2847  CG  LEU A 373     7336   7668   6188    112    221    135       C  
ATOM   2848  CD1 LEU A 373      30.497  10.316 -17.392  1.00 54.86           C  
ANISOU 2848  CD1 LEU A 373     7217   7598   6029     74    196    165       C  
ATOM   2849  CD2 LEU A 373      31.698   8.185 -16.903  1.00 57.35           C  
ANISOU 2849  CD2 LEU A 373     7620   7855   6314    172    242     69       C  
ATOM   2850  N   ALA A 374      31.703  11.034 -12.785  1.00 43.46           N  
ANISOU 2850  N   ALA A 374     5609   6029   4877     57    210    219       N  
ATOM   2851  CA  ALA A 374      30.873  10.770 -11.617  1.00 42.76           C  
ANISOU 2851  CA  ALA A 374     5525   5873   4848     22    169    200       C  
ATOM   2852  C   ALA A 374      30.115  12.041 -11.223  1.00 41.62           C  
ANISOU 2852  C   ALA A 374     5329   5730   4755    -30    138    249       C  
ATOM   2853  O   ALA A 374      28.929  12.000 -10.895  1.00 42.48           O  
ANISOU 2853  O   ALA A 374     5448   5810   4880    -69     94    237       O  
ATOM   2854  CB  ALA A 374      31.703  10.255 -10.447  1.00 42.08           C  
ANISOU 2854  CB  ALA A 374     5427   5751   4810     54    190    187       C  
ATOM   2855  N   ALA A 375      30.799  13.169 -11.279  1.00 35.16           N  
ANISOU 2855  N   ALA A 375     4455   4947   3956    -29    159    305       N  
ATOM   2856  CA  ALA A 375      30.158  14.421 -10.959  1.00 36.37           C  
ANISOU 2856  CA  ALA A 375     4570   5096   4151    -68    130    352       C  
ATOM   2857  C   ALA A 375      29.043  14.712 -11.972  1.00 41.70           C  
ANISOU 2857  C   ALA A 375     5269   5795   4780    -91     97    357       C  
ATOM   2858  O   ALA A 375      27.947  15.151 -11.583  1.00 46.56           O  
ANISOU 2858  O   ALA A 375     5876   6391   5423   -119     55    364       O  
ATOM   2859  CB  ALA A 375      31.175  15.541 -10.921  1.00 36.43           C  
ANISOU 2859  CB  ALA A 375     4527   5134   4182    -68    158    411       C  
ATOM   2860  N   GLU A 376      29.293  14.490 -13.262  1.00 38.38           N  
ANISOU 2860  N   GLU A 376     4876   5420   4285    -74    115    354       N  
ATOM   2861  CA  GLU A 376      28.262  14.640 -14.282  1.00 42.97           C  
ANISOU 2861  CA  GLU A 376     5486   6029   4813    -93     81    354       C  
ATOM   2862  C   GLU A 376      27.055  13.748 -13.977  1.00 40.39           C  
ANISOU 2862  C   GLU A 376     5193   5669   4486   -117     35    302       C  
ATOM   2863  O   GLU A 376      25.898  14.144 -14.153  1.00 40.78           O  
ANISOU 2863  O   GLU A 376     5236   5728   4532   -147    -10    311       O  
ATOM   2864  CB  GLU A 376      28.834  14.351 -15.680  1.00 46.52           C  
ANISOU 2864  CB  GLU A 376     5968   6532   5175    -66    112    350       C  
ATOM   2865  CG  GLU A 376      29.755  15.473 -16.191  1.00 54.93           C  
ANISOU 2865  CG  GLU A 376     6995   7646   6231    -58    150    418       C  
ATOM   2866  CD  GLU A 376      30.426  15.168 -17.524  1.00 61.42           C  
ANISOU 2866  CD  GLU A 376     7843   8530   6962    -26    189    416       C  
ATOM   2867  OE1 GLU A 376      30.767  13.991 -17.780  1.00 60.21           O  
ANISOU 2867  OE1 GLU A 376     7731   8380   6767      9    210    360       O  
ATOM   2868  OE2 GLU A 376      30.631  16.121 -18.309  1.00 65.83           O  
ANISOU 2868  OE2 GLU A 376     8387   9136   7490    -35    201    473       O  
ATOM   2869  N   ALA A 377      27.320  12.527 -13.518  1.00 32.45           N  
ANISOU 2869  N   ALA A 377     4222   4626   3481   -106     45    248       N  
ATOM   2870  CA  ALA A 377      26.189  11.658 -13.185  1.00 31.32           C  
ANISOU 2870  CA  ALA A 377     4114   4448   3338   -142      1    202       C  
ATOM   2871  C   ALA A 377      25.350  12.307 -12.054  1.00 41.15           C  
ANISOU 2871  C   ALA A 377     5307   5672   4656   -176    -31    227       C  
ATOM   2872  O   ALA A 377      24.104  12.310 -12.124  1.00 34.44           O  
ANISOU 2872  O   ALA A 377     4453   4832   3799   -214    -77    221       O  
ATOM   2873  CB  ALA A 377      26.624  10.259 -12.808  1.00 26.68           C  
ANISOU 2873  CB  ALA A 377     3583   3813   2741   -125     15    144       C  
ATOM   2874  N   VAL A 378      26.031  12.883 -11.053  1.00 34.53           N  
ANISOU 2874  N   VAL A 378     4426   4812   3882   -160     -8    255       N  
ATOM   2875  CA  VAL A 378      25.347  13.511  -9.923  1.00 35.54           C  
ANISOU 2875  CA  VAL A 378     4510   4919   4075   -181    -33    275       C  
ATOM   2876  C   VAL A 378      24.483  14.674 -10.408  1.00 33.54           C  
ANISOU 2876  C   VAL A 378     4226   4703   3816   -194    -63    317       C  
ATOM   2877  O   VAL A 378      23.302  14.772 -10.060  1.00 32.68           O  
ANISOU 2877  O   VAL A 378     4099   4598   3719   -218   -102    315       O  
ATOM   2878  CB  VAL A 378      26.322  14.012  -8.818  1.00 29.84           C  
ANISOU 2878  CB  VAL A 378     3754   4167   3417   -161     -4    299       C  
ATOM   2879  CG1 VAL A 378      25.574  14.823  -7.777  1.00 25.47           C  
ANISOU 2879  CG1 VAL A 378     3160   3596   2921   -177    -31    322       C  
ATOM   2880  CG2 VAL A 378      27.043  12.869  -8.149  1.00 30.34           C  
ANISOU 2880  CG2 VAL A 378     3844   4192   3492   -144     20    259       C  
ATOM   2881  N   VAL A 379      25.071  15.544 -11.220  1.00 30.29           N  
ANISOU 2881  N   VAL A 379     3807   4322   3380   -175    -46    358       N  
ATOM   2882  CA  VAL A 379      24.348  16.663 -11.790  1.00 34.04           C  
ANISOU 2882  CA  VAL A 379     4263   4829   3842   -179    -74    401       C  
ATOM   2883  C   VAL A 379      23.154  16.230 -12.663  1.00 44.71           C  
ANISOU 2883  C   VAL A 379     5633   6218   5137   -198   -115    380       C  
ATOM   2884  O   VAL A 379      22.060  16.812 -12.596  1.00 41.33           O  
ANISOU 2884  O   VAL A 379     5179   5809   4715   -206   -155    399       O  
ATOM   2885  CB  VAL A 379      25.278  17.548 -12.612  1.00 36.71           C  
ANISOU 2885  CB  VAL A 379     4601   5191   4155   -161    -46    450       C  
ATOM   2886  CG1 VAL A 379      24.466  18.551 -13.405  1.00 38.27           C  
ANISOU 2886  CG1 VAL A 379     4796   5422   4323   -162    -79    492       C  
ATOM   2887  CG2 VAL A 379      26.259  18.264 -11.668  1.00 31.70           C  
ANISOU 2887  CG2 VAL A 379     3938   4524   3584   -155    -18    482       C  
ATOM   2888  N   LEU A 380      23.366  15.189 -13.454  1.00 44.72           N  
ANISOU 2888  N   LEU A 380     5680   6233   5081   -202   -107    340       N  
ATOM   2889  CA  LEU A 380      22.336  14.686 -14.325  1.00 46.29           C  
ANISOU 2889  CA  LEU A 380     5902   6467   5220   -227   -148    315       C  
ATOM   2890  C   LEU A 380      21.168  14.214 -13.483  1.00 42.94           C  
ANISOU 2890  C   LEU A 380     5458   6030   4827   -264   -189    290       C  
ATOM   2891  O   LEU A 380      20.017  14.478 -13.808  1.00 34.94           O  
ANISOU 2891  O   LEU A 380     4424   5058   3795   -285   -234    299       O  
ATOM   2892  CB  LEU A 380      22.871  13.513 -15.135  1.00 57.48           C  
ANISOU 2892  CB  LEU A 380     7383   7883   6572   -224   -130    266       C  
ATOM   2893  CG  LEU A 380      23.474  13.870 -16.489  1.00 68.09           C  
ANISOU 2893  CG  LEU A 380     8752   9273   7847   -196   -108    286       C  
ATOM   2894  CD1 LEU A 380      22.345  14.009 -17.488  1.00 75.24           C  
ANISOU 2894  CD1 LEU A 380     9669  10228   8692   -219   -159    288       C  
ATOM   2895  CD2 LEU A 380      24.322  15.138 -16.420  1.00 62.34           C  
ANISOU 2895  CD2 LEU A 380     7983   8555   7147   -168    -73    351       C  
ATOM   2896  N   HIS A 381      21.478  13.497 -12.414  1.00 35.88           N  
ANISOU 2896  N   HIS A 381     4570   5086   3978   -273   -172    261       N  
ATOM   2897  CA  HIS A 381      20.451  12.901 -11.590  1.00 38.84           C  
ANISOU 2897  CA  HIS A 381     4931   5449   4379   -316   -205    237       C  
ATOM   2898  C   HIS A 381      19.682  13.917 -10.768  1.00 37.13           C  
ANISOU 2898  C   HIS A 381     4645   5249   4213   -313   -225    276       C  
ATOM   2899  O   HIS A 381      18.488  13.765 -10.562  1.00 36.08           O  
ANISOU 2899  O   HIS A 381     4483   5146   4078   -346   -264    270       O  
ATOM   2900  CB  HIS A 381      21.065  11.864 -10.653  1.00 38.54           C  
ANISOU 2900  CB  HIS A 381     4924   5347   4371   -322   -180    199       C  
ATOM   2901  CG  HIS A 381      20.074  11.234  -9.732  1.00 37.28           C  
ANISOU 2901  CG  HIS A 381     4753   5174   4239   -371   -209    179       C  
ATOM   2902  ND1 HIS A 381      19.427  10.059 -10.036  1.00 40.81           N  
ANISOU 2902  ND1 HIS A 381     5245   5615   4646   -424   -238    136       N  
ATOM   2903  CD2 HIS A 381      19.627  11.611  -8.512  1.00 38.01           C  
ANISOU 2903  CD2 HIS A 381     4795   5258   4390   -378   -213    197       C  
ATOM   2904  CE1 HIS A 381      18.625   9.731  -9.034  1.00 41.98           C  
ANISOU 2904  CE1 HIS A 381     5367   5755   4829   -468   -257    133       C  
ATOM   2905  NE2 HIS A 381      18.732  10.649  -8.093  1.00 40.40           N  
ANISOU 2905  NE2 HIS A 381     5107   5555   4688   -437   -240    169       N  
ATOM   2906  N   TYR A 382      20.358  14.951 -10.288  1.00 34.62           N  
ANISOU 2906  N   TYR A 382     4302   4914   3939   -273   -199    314       N  
ATOM   2907  CA  TYR A 382      19.682  15.967  -9.474  1.00 34.67           C  
ANISOU 2907  CA  TYR A 382     4254   4928   3992   -260   -216    349       C  
ATOM   2908  C   TYR A 382      19.130  17.181 -10.226  1.00 32.68           C  
ANISOU 2908  C   TYR A 382     3979   4722   3717   -234   -242    394       C  
ATOM   2909  O   TYR A 382      18.434  17.977  -9.622  1.00 36.97           O  
ANISOU 2909  O   TYR A 382     4482   5275   4289   -216   -261    419       O  
ATOM   2910  CB  TYR A 382      20.577  16.455  -8.317  1.00 31.15           C  
ANISOU 2910  CB  TYR A 382     3798   4429   3610   -234   -183    364       C  
ATOM   2911  CG  TYR A 382      20.687  15.452  -7.201  1.00 35.03           C  
ANISOU 2911  CG  TYR A 382     4294   4880   4135   -255   -171    327       C  
ATOM   2912  CD1 TYR A 382      21.603  14.401  -7.276  1.00 29.80           C  
ANISOU 2912  CD1 TYR A 382     3677   4185   3462   -261   -144    293       C  
ATOM   2913  CD2 TYR A 382      19.863  15.547  -6.061  1.00 36.32           C  
ANISOU 2913  CD2 TYR A 382     4421   5041   4337   -263   -187    327       C  
ATOM   2914  CE1 TYR A 382      21.686  13.472  -6.271  1.00 30.90           C  
ANISOU 2914  CE1 TYR A 382     3829   4283   3628   -277   -136    262       C  
ATOM   2915  CE2 TYR A 382      19.959  14.641  -5.027  1.00 30.86           C  
ANISOU 2915  CE2 TYR A 382     3739   4313   3674   -284   -176    298       C  
ATOM   2916  CZ  TYR A 382      20.881  13.601  -5.143  1.00 35.60           C  
ANISOU 2916  CZ  TYR A 382     4389   4874   4263   -292   -151    267       C  
ATOM   2917  OH  TYR A 382      21.000  12.681  -4.148  1.00 34.66           O  
ANISOU 2917  OH  TYR A 382     4288   4714   4168   -310   -142    240       O  
ATOM   2918  N   THR A 383      19.458  17.347 -11.510  1.00 32.57           N  
ANISOU 2918  N   THR A 383     3994   4734   3648   -227   -241    406       N  
ATOM   2919  CA  THR A 383      18.951  18.476 -12.279  1.00 31.15           C  
ANISOU 2919  CA  THR A 383     3801   4595   3441   -201   -266    452       C  
ATOM   2920  C   THR A 383      17.489  18.206 -12.508  1.00 41.42           C  
ANISOU 2920  C   THR A 383     5071   5954   4713   -220   -318    440       C  
ATOM   2921  O   THR A 383      17.111  17.054 -12.713  1.00 43.90           O  
ANISOU 2921  O   THR A 383     5397   6284   5000   -264   -331    397       O  
ATOM   2922  CB  THR A 383      19.661  18.610 -13.633  1.00 33.87           C  
ANISOU 2922  CB  THR A 383     4186   4959   3725   -193   -251    468       C  
ATOM   2923  OG1 THR A 383      20.979  19.131 -13.421  1.00 35.54           O  
ANISOU 2923  OG1 THR A 383     4411   5129   3964   -175   -205    494       O  
ATOM   2924  CG2 THR A 383      18.889  19.545 -14.607  1.00 24.90           C  
ANISOU 2924  CG2 THR A 383     3042   3874   2543   -173   -289    510       C  
ATOM   2925  N   ASP A 384      16.659  19.241 -12.414  1.00 42.31           N  
ANISOU 2925  N   ASP A 384     5146   6098   4833   -188   -348    478       N  
ATOM   2926  CA  ASP A 384      15.256  19.128 -12.828  1.00 40.43           C  
ANISOU 2926  CA  ASP A 384     4869   5935   4558   -199   -400    476       C  
ATOM   2927  C   ASP A 384      15.178  19.455 -14.314  1.00 40.16           C  
ANISOU 2927  C   ASP A 384     4861   5945   4453   -189   -422    497       C  
ATOM   2928  O   ASP A 384      15.340  20.619 -14.693  1.00 36.45           O  
ANISOU 2928  O   ASP A 384     4397   5474   3976   -141   -423    546       O  
ATOM   2929  CB  ASP A 384      14.391  20.098 -12.041  1.00 37.17           C  
ANISOU 2929  CB  ASP A 384     4401   5542   4181   -156   -421    508       C  
ATOM   2930  CG  ASP A 384      12.946  20.100 -12.508  1.00 53.50           C  
ANISOU 2930  CG  ASP A 384     6417   7702   6208   -157   -476    513       C  
ATOM   2931  OD1 ASP A 384      12.633  19.517 -13.581  1.00 48.88           O  
ANISOU 2931  OD1 ASP A 384     5845   7166   5563   -192   -503    498       O  
ATOM   2932  OD2 ASP A 384      12.119  20.723 -11.804  1.00 63.39           O  
ANISOU 2932  OD2 ASP A 384     7616   8985   7486   -120   -494    532       O  
ATOM   2933  N   TRP A 385      14.945  18.455 -15.175  1.00 39.73           N  
ANISOU 2933  N   TRP A 385     4829   5926   4340   -233   -440    461       N  
ATOM   2934  CA  TRP A 385      15.135  18.726 -16.605  1.00 40.19           C  
ANISOU 2934  CA  TRP A 385     4925   6018   4327   -221   -451    480       C  
ATOM   2935  C   TRP A 385      13.968  19.473 -17.257  1.00 33.68           C  
ANISOU 2935  C   TRP A 385     4065   5270   3462   -196   -508    515       C  
ATOM   2936  O   TRP A 385      14.027  19.840 -18.431  1.00 39.87           O  
ANISOU 2936  O   TRP A 385     4878   6087   4184   -180   -522    538       O  
ATOM   2937  CB  TRP A 385      15.650  17.502 -17.401  1.00 45.27           C  
ANISOU 2937  CB  TRP A 385     5627   6658   4915   -264   -440    430       C  
ATOM   2938  CG  TRP A 385      17.047  17.072 -16.979  1.00 37.51           C  
ANISOU 2938  CG  TRP A 385     4685   5603   3963   -261   -378    411       C  
ATOM   2939  CD1 TRP A 385      17.371  16.075 -16.113  1.00 33.77           C  
ANISOU 2939  CD1 TRP A 385     4222   5082   3527   -290   -356    366       C  
ATOM   2940  CD2 TRP A 385      18.279  17.646 -17.408  1.00 34.36           C  
ANISOU 2940  CD2 TRP A 385     4318   5179   3556   -226   -330    441       C  
ATOM   2941  NE1 TRP A 385      18.730  16.000 -15.965  1.00 32.08           N  
ANISOU 2941  NE1 TRP A 385     4042   4818   3330   -268   -300    364       N  
ATOM   2942  CE2 TRP A 385      19.314  16.944 -16.753  1.00 31.47           C  
ANISOU 2942  CE2 TRP A 385     3974   4757   3226   -232   -282    410       C  
ATOM   2943  CE3 TRP A 385      18.609  18.706 -18.268  1.00 37.55           C  
ANISOU 2943  CE3 TRP A 385     4735   5606   3928   -192   -325    495       C  
ATOM   2944  CZ2 TRP A 385      20.660  17.265 -16.924  1.00 37.40           C  
ANISOU 2944  CZ2 TRP A 385     4747   5483   3980   -206   -228    431       C  
ATOM   2945  CZ3 TRP A 385      19.959  19.030 -18.442  1.00 35.86           C  
ANISOU 2945  CZ3 TRP A 385     4547   5362   3716   -174   -269    518       C  
ATOM   2946  CH2 TRP A 385      20.963  18.312 -17.774  1.00 38.82           C  
ANISOU 2946  CH2 TRP A 385     4932   5690   4126   -181   -222    486       C  
ATOM   2947  N   LEU A 386      12.940  19.758 -16.465  1.00 40.14           N  
ANISOU 2947  N   LEU A 386     4817   6119   4314   -186   -537    523       N  
ATOM   2948  CA  LEU A 386      11.892  20.694 -16.892  1.00 49.08           C  
ANISOU 2948  CA  LEU A 386     5907   7322   5418   -140   -586    565       C  
ATOM   2949  C   LEU A 386      12.290  22.138 -16.587  1.00 52.76           C  
ANISOU 2949  C   LEU A 386     6383   7745   5918    -64   -569    622       C  
ATOM   2950  O   LEU A 386      11.706  23.070 -17.120  1.00 53.76           O  
ANISOU 2950  O   LEU A 386     6499   7912   6014    -12   -603    666       O  
ATOM   2951  CB  LEU A 386      10.575  20.419 -16.173  1.00 47.47           C  
ANISOU 2951  CB  LEU A 386     5621   7183   5232   -154   -625    553       C  
ATOM   2952  CG  LEU A 386       9.414  19.995 -17.055  1.00 57.92           C  
ANISOU 2952  CG  LEU A 386     6908   8611   6488   -185   -688    544       C  
ATOM   2953  CD1 LEU A 386       8.145  20.034 -16.225  1.00 53.47           C  
ANISOU 2953  CD1 LEU A 386     6248   8119   5949   -182   -720    548       C  
ATOM   2954  CD2 LEU A 386       9.287  20.895 -18.325  1.00 52.56           C  
ANISOU 2954  CD2 LEU A 386     6252   7974   5746   -132   -719    589       C  
ATOM   2955  N   HIS A 387      13.259  22.312 -15.695  1.00 48.58           N  
ANISOU 2955  N   HIS A 387     5876   7132   5450    -59   -519    622       N  
ATOM   2956  CA  HIS A 387      13.652  23.637 -15.234  1.00 48.63           C  
ANISOU 2956  CA  HIS A 387     5896   7086   5494      2   -504    671       C  
ATOM   2957  C   HIS A 387      15.110  23.590 -14.798  1.00 37.65           C  
ANISOU 2957  C   HIS A 387     4553   5609   4145    -17   -447    667       C  
ATOM   2958  O   HIS A 387      15.407  23.801 -13.629  1.00 33.22           O  
ANISOU 2958  O   HIS A 387     3981   4995   3647     -7   -425    662       O  
ATOM   2959  CB  HIS A 387      12.803  24.041 -14.028  1.00 44.16           C  
ANISOU 2959  CB  HIS A 387     5275   6527   4978     40   -519    672       C  
ATOM   2960  CG  HIS A 387      11.337  24.094 -14.305  1.00 54.60           C  
ANISOU 2960  CG  HIS A 387     6535   7947   6264     63   -574    678       C  
ATOM   2961  ND1 HIS A 387      10.435  23.229 -13.719  1.00 54.94           N  
ANISOU 2961  ND1 HIS A 387     6510   8048   6316     27   -591    641       N  
ATOM   2962  CD2 HIS A 387      10.609  24.922 -15.088  1.00 54.29           C  
ANISOU 2962  CD2 HIS A 387     6488   7963   6179    118   -617    719       C  
ATOM   2963  CE1 HIS A 387       9.217  23.529 -14.125  1.00 53.65           C  
ANISOU 2963  CE1 HIS A 387     6292   7979   6115     58   -641    659       C  
ATOM   2964  NE2 HIS A 387       9.295  24.549 -14.959  1.00 53.25           N  
ANISOU 2964  NE2 HIS A 387     6277   7927   6030    118   -659    705       N  
ATOM   2965  N   PRO A 388      16.013  23.296 -15.733  1.00 37.89           N  
ANISOU 2965  N   PRO A 388     4629   5630   4135    -42   -422    668       N  
ATOM   2966  CA  PRO A 388      17.400  23.007 -15.358  1.00 35.16           C  
ANISOU 2966  CA  PRO A 388     4315   5220   3823    -66   -366    657       C  
ATOM   2967  C   PRO A 388      18.151  24.216 -14.770  1.00 36.84           C  
ANISOU 2967  C   PRO A 388     4547   5367   4084    -36   -344    704       C  
ATOM   2968  O   PRO A 388      19.222  23.999 -14.191  1.00 38.65           O  
ANISOU 2968  O   PRO A 388     4786   5546   4352    -57   -302    694       O  
ATOM   2969  CB  PRO A 388      18.064  22.572 -16.679  1.00 32.94           C  
ANISOU 2969  CB  PRO A 388     4077   4964   3474    -87   -349    656       C  
ATOM   2970  CG  PRO A 388      17.021  22.769 -17.771  1.00 40.65           C  
ANISOU 2970  CG  PRO A 388     5051   6013   4380    -73   -400    671       C  
ATOM   2971  CD  PRO A 388      15.817  23.439 -17.188  1.00 42.67           C  
ANISOU 2971  CD  PRO A 388     5261   6289   4661    -37   -445    690       C  
ATOM   2972  N   GLU A 389      17.640  25.433 -14.963  1.00 31.26           N  
ANISOU 2972  N   GLU A 389     3848   4660   3370     10   -374    755       N  
ATOM   2973  CA  GLU A 389      18.308  26.667 -14.511  1.00 36.36           C  
ANISOU 2973  CA  GLU A 389     4526   5235   4053     34   -360    804       C  
ATOM   2974  C   GLU A 389      17.559  27.330 -13.373  1.00 37.48           C  
ANISOU 2974  C   GLU A 389     4647   5349   4245     80   -385    807       C  
ATOM   2975  O   GLU A 389      17.938  28.404 -12.942  1.00 36.09           O  
ANISOU 2975  O   GLU A 389     4505   5110   4098    105   -384    844       O  
ATOM   2976  CB  GLU A 389      18.393  27.730 -15.607  1.00 35.67           C  
ANISOU 2976  CB  GLU A 389     4485   5150   3916     58   -376    868       C  
ATOM   2977  CG  GLU A 389      18.969  27.303 -16.928  1.00 57.23           C  
ANISOU 2977  CG  GLU A 389     7241   7922   6581     26   -357    877       C  
ATOM   2978  CD  GLU A 389      20.483  27.398 -16.961  1.00 76.37           C  
ANISOU 2978  CD  GLU A 389     9695  10303   9019    -12   -303    896       C  
ATOM   2979  OE1 GLU A 389      21.082  27.964 -16.010  1.00 80.09           O  
ANISOU 2979  OE1 GLU A 389    10171  10707   9551    -16   -286    910       O  
ATOM   2980  OE2 GLU A 389      21.073  26.915 -17.953  1.00 85.70           O  
ANISOU 2980  OE2 GLU A 389    10892  11522  10147    -37   -277    897       O  
ATOM   2981  N   ASP A 390      16.457  26.735 -12.928  1.00 36.14           N  
ANISOU 2981  N   ASP A 390     4424   5229   4079     91   -410    770       N  
ATOM   2982  CA  ASP A 390      15.709  27.330 -11.834  1.00 31.76           C  
ANISOU 2982  CA  ASP A 390     3844   4659   3565    142   -429    771       C  
ATOM   2983  C   ASP A 390      16.480  27.395 -10.482  1.00 32.95           C  
ANISOU 2983  C   ASP A 390     4003   4732   3786    132   -396    754       C  
ATOM   2984  O   ASP A 390      16.869  26.374  -9.906  1.00 32.48           O  
ANISOU 2984  O   ASP A 390     3921   4669   3752     86   -369    711       O  
ATOM   2985  CB  ASP A 390      14.385  26.617 -11.628  1.00 32.08           C  
ANISOU 2985  CB  ASP A 390     3815   4782   3593    149   -458    738       C  
ATOM   2986  CG  ASP A 390      13.599  27.264 -10.559  1.00 35.05           C  
ANISOU 2986  CG  ASP A 390     4160   5154   4001    210   -474    742       C  
ATOM   2987  OD1 ASP A 390      13.262  28.449 -10.714  1.00 42.97           O  
ANISOU 2987  OD1 ASP A 390     5188   6144   4994    280   -499    784       O  
ATOM   2988  OD2 ASP A 390      13.398  26.637  -9.530  1.00 42.36           O  
ANISOU 2988  OD2 ASP A 390     5047   6084   4964    193   -460    705       O  
ATOM   2989  N   PRO A 391      16.701  28.614  -9.975  1.00 34.53           N  
ANISOU 2989  N   PRO A 391     4242   4867   4012    175   -402    789       N  
ATOM   2990  CA  PRO A 391      17.572  28.797  -8.799  1.00 32.59           C  
ANISOU 2990  CA  PRO A 391     4015   4542   3827    161   -374    778       C  
ATOM   2991  C   PRO A 391      17.057  28.130  -7.542  1.00 35.05           C  
ANISOU 2991  C   PRO A 391     4276   4865   4175    166   -368    730       C  
ATOM   2992  O   PRO A 391      17.857  27.668  -6.711  1.00 35.68           O  
ANISOU 2992  O   PRO A 391     4357   4903   4297    130   -338    704       O  
ATOM   2993  CB  PRO A 391      17.644  30.330  -8.609  1.00 28.51           C  
ANISOU 2993  CB  PRO A 391     3558   3956   3319    214   -395    825       C  
ATOM   2994  CG  PRO A 391      17.241  30.898  -9.932  1.00 36.85           C  
ANISOU 2994  CG  PRO A 391     4640   5044   4317    239   -421    870       C  
ATOM   2995  CD  PRO A 391      16.336  29.892 -10.625  1.00 35.90           C  
ANISOU 2995  CD  PRO A 391     4458   5027   4154    233   -434    844       C  
ATOM   2996  N   THR A 392      15.744  28.068  -7.385  1.00 27.08           N  
ANISOU 2996  N   THR A 392     3221   3918   3151    210   -396    720       N  
ATOM   2997  CA  THR A 392      15.207  27.462  -6.185  1.00 28.93           C  
ANISOU 2997  CA  THR A 392     3405   4171   3417    213   -388    680       C  
ATOM   2998  C   THR A 392      15.443  25.958  -6.224  1.00 32.83           C  
ANISOU 2998  C   THR A 392     3865   4697   3911    137   -366    638       C  
ATOM   2999  O   THR A 392      15.845  25.394  -5.228  1.00 33.37           O  
ANISOU 2999  O   THR A 392     3925   4736   4018    111   -341    608       O  
ATOM   3000  CB  THR A 392      13.663  27.740  -6.004  1.00 39.27           C  
ANISOU 3000  CB  THR A 392     4660   5557   4705    279   -422    683       C  
ATOM   3001  OG1 THR A 392      13.436  29.147  -5.833  1.00 38.23           O  
ANISOU 3001  OG1 THR A 392     4567   5385   4573    363   -443    718       O  
ATOM   3002  CG2 THR A 392      13.139  27.003  -4.787  1.00 30.69           C  
ANISOU 3002  CG2 THR A 392     3515   4499   3646    270   -409    643       C  
ATOM   3003  N  AHIS A 393      15.174  25.296  -7.350  0.50 32.94           N  
ANISOU 3003  N  AHIS A 393     3866   4771   3880    103   -377    634       N  
ATOM   3004  N  BHIS A 393      15.163  25.346  -7.384  0.50 32.97           N  
ANISOU 3004  N  BHIS A 393     3870   4774   3882    105   -378    636       N  
ATOM   3005  CA AHIS A 393      15.432  23.862  -7.390  0.50 33.40           C  
ANISOU 3005  CA AHIS A 393     3908   4847   3935     33   -357    591       C  
ATOM   3006  CA BHIS A 393      15.385  23.922  -7.640  0.50 32.49           C  
ANISOU 3006  CA BHIS A 393     3795   4739   3810     35   -362    595       C  
ATOM   3007  C  AHIS A 393      16.926  23.575  -7.236  0.50 37.70           C  
ANISOU 3007  C  AHIS A 393     4498   5321   4507     -2   -317    582       C  
ATOM   3008  C  BHIS A 393      16.853  23.525  -7.419  0.50 37.39           C  
ANISOU 3008  C  BHIS A 393     4458   5291   4459     -4   -320    583       C  
ATOM   3009  O  AHIS A 393      17.309  22.627  -6.566  0.50 40.45           O  
ANISOU 3009  O  AHIS A 393     4839   5651   4879    -39   -293    546       O  
ATOM   3010  O  BHIS A 393      17.137  22.461  -6.884  0.50 38.93           O  
ANISOU 3010  O  BHIS A 393     4644   5477   4672    -46   -299    544       O  
ATOM   3011  CB AHIS A 393      14.937  23.191  -8.670  0.50 29.74           C  
ANISOU 3011  CB AHIS A 393     3434   4453   3412      1   -379    584       C  
ATOM   3012  CB BHIS A 393      15.023  23.570  -9.093  0.50 29.20           C  
ANISOU 3012  CB BHIS A 393     3380   4384   3330     14   -384    601       C  
ATOM   3013  CG AHIS A 393      15.445  21.790  -8.825  0.50 25.91           C  
ANISOU 3013  CG AHIS A 393     2960   3966   2921    -68   -358    540       C  
ATOM   3014  CG BHIS A 393      13.585  23.204  -9.306  0.50 36.33           C  
ANISOU 3014  CG BHIS A 393     4224   5380   4202     16   -424    591       C  
ATOM   3015  ND1AHIS A 393      14.871  20.709  -8.178  0.50 29.25           N  
ANISOU 3015  ND1AHIS A 393     3347   4413   3353   -109   -360    501       N  
ATOM   3016  ND1BHIS A 393      13.048  22.005  -8.883  0.50 44.78           N  
ANISOU 3016  ND1BHIS A 393     5253   6488   5273    -38   -426    550       N  
ATOM   3017  CD2AHIS A 393      16.512  21.299  -9.497  0.50 20.02           C  
ANISOU 3017  CD2AHIS A 393     2258   3190   2157   -100   -332    531       C  
ATOM   3018  CD2BHIS A 393      12.581  23.865  -9.932  0.50 31.66           C  
ANISOU 3018  CD2BHIS A 393     3605   4853   3571     61   -465    620       C  
ATOM   3019  CE1AHIS A 393      15.538  19.612  -8.478  0.50 27.69           C  
ANISOU 3019  CE1AHIS A 393     3182   4194   3144   -162   -340    468       C  
ATOM   3020  CE1BHIS A 393      11.771  21.954  -9.225  0.50 42.59           C  
ANISOU 3020  CE1BHIS A 393     4921   6301   4962    -32   -466    554       C  
ATOM   3021  NE2AHIS A 393      16.549  19.946  -9.270  0.50 31.66           N  
ANISOU 3021  NE2AHIS A 393     3732   4667   3630   -152   -321    483       N  
ATOM   3022  NE2BHIS A 393      11.462  23.075  -9.853  0.50 38.65           N  
ANISOU 3022  NE2BHIS A 393     4426   5822   4438     32   -491    596       N  
ATOM   3023  N   LEU A 394      17.770  24.372  -7.882  1.00 33.44           N  
ANISOU 3023  N   LEU A 394     4003   4745   3958      8   -309    618       N  
ATOM   3024  CA  LEU A 394      19.220  24.121  -7.800  1.00 32.90           C  
ANISOU 3024  CA  LEU A 394     3967   4623   3910    -27   -269    614       C  
ATOM   3025  C   LEU A 394      19.710  24.247  -6.359  1.00 37.06           C  
ANISOU 3025  C   LEU A 394     4492   5092   4498    -23   -252    601       C  
ATOM   3026  O   LEU A 394      20.495  23.423  -5.891  1.00 38.24           O  
ANISOU 3026  O   LEU A 394     4641   5220   4669    -55   -223    573       O  
ATOM   3027  CB  LEU A 394      20.002  25.090  -8.696  1.00 22.22           C  
ANISOU 3027  CB  LEU A 394     2658   3249   2538    -21   -264    664       C  
ATOM   3028  CG  LEU A 394      19.685  24.933 -10.183  1.00 26.70           C  
ANISOU 3028  CG  LEU A 394     3234   3873   3038    -26   -277    678       C  
ATOM   3029  CD1 LEU A 394      20.210  26.155 -10.958  1.00 28.60           C  
ANISOU 3029  CD1 LEU A 394     3519   4091   3258    -11   -279    739       C  
ATOM   3030  CD2 LEU A 394      20.267  23.614 -10.684  1.00 24.09           C  
ANISOU 3030  CD2 LEU A 394     2903   3568   2683    -71   -249    639       C  
ATOM   3031  N   ARG A 395      19.223  25.266  -5.655  1.00 32.48           N  
ANISOU 3031  N   ARG A 395     3914   4487   3942     22   -271    620       N  
ATOM   3032  CA  ARG A 395      19.542  25.413  -4.254  1.00 32.27           C  
ANISOU 3032  CA  ARG A 395     3887   4409   3966     31   -260    605       C  
ATOM   3033  C   ARG A 395      19.111  24.175  -3.450  1.00 37.42           C  
ANISOU 3033  C   ARG A 395     4498   5087   4632      9   -249    557       C  
ATOM   3034  O   ARG A 395      19.946  23.552  -2.792  1.00 35.83           O  
ANISOU 3034  O   ARG A 395     4302   4853   4460    -20   -223    535       O  
ATOM   3035  CB  ARG A 395      18.951  26.691  -3.683  1.00 34.41           C  
ANISOU 3035  CB  ARG A 395     4173   4651   4250     92   -286    629       C  
ATOM   3036  CG  ARG A 395      19.145  26.797  -2.184  1.00 37.93           C  
ANISOU 3036  CG  ARG A 395     4620   5050   4742    105   -277    608       C  
ATOM   3037  CD  ARG A 395      17.803  26.619  -1.507  1.00 41.82           C  
ANISOU 3037  CD  ARG A 395     5067   5590   5230    148   -291    587       C  
ATOM   3038  NE  ARG A 395      17.159  27.896  -1.403  1.00 42.38           N  
ANISOU 3038  NE  ARG A 395     5161   5648   5294    221   -319    614       N  
ATOM   3039  CZ  ARG A 395      15.838  28.104  -1.280  1.00 43.21           C  
ANISOU 3039  CZ  ARG A 395     5228   5812   5378    279   -340    614       C  
ATOM   3040  NH1 ARG A 395      14.951  27.102  -1.266  1.00 28.70           N  
ANISOU 3040  NH1 ARG A 395     3321   4059   3525    262   -338    590       N  
ATOM   3041  NH2 ARG A 395      15.416  29.360  -1.196  1.00 40.24           N  
ANISOU 3041  NH2 ARG A 395     4887   5410   4994    356   -364    640       N  
ATOM   3042  N   ASP A 396      17.842  23.781  -3.552  1.00 31.71           N  
ANISOU 3042  N   ASP A 396     3734   4428   3886     19   -269    545       N  
ATOM   3043  CA  ASP A 396      17.376  22.569  -2.868  1.00 30.88           C  
ANISOU 3043  CA  ASP A 396     3592   4351   3788    -13   -260    505       C  
ATOM   3044  C   ASP A 396      18.029  21.273  -3.359  1.00 30.00           C  
ANISOU 3044  C   ASP A 396     3494   4239   3664    -74   -240    476       C  
ATOM   3045  O   ASP A 396      18.119  20.324  -2.607  1.00 28.97           O  
ANISOU 3045  O   ASP A 396     3356   4098   3551   -103   -225    445       O  
ATOM   3046  CB  ASP A 396      15.855  22.413  -2.967  1.00 28.44           C  
ANISOU 3046  CB  ASP A 396     3231   4123   3453      0   -289    502       C  
ATOM   3047  CG  ASP A 396      15.084  23.591  -2.314  1.00 45.21           C  
ANISOU 3047  CG  ASP A 396     5336   6255   5586     74   -306    524       C  
ATOM   3048  OD1 ASP A 396      15.664  24.332  -1.483  1.00 37.90           O  
ANISOU 3048  OD1 ASP A 396     4440   5264   4694    107   -295    531       O  
ATOM   3049  OD2 ASP A 396      13.883  23.759  -2.631  1.00 46.12           O  
ANISOU 3049  OD2 ASP A 396     5406   6445   5672    101   -333    534       O  
ATOM   3050  N   ALA A 397      18.415  21.200  -4.628  1.00 30.37           N  
ANISOU 3050  N   ALA A 397     3564   4301   3676    -88   -241    486       N  
ATOM   3051  CA  ALA A 397      19.010  19.967  -5.135  1.00 35.21           C  
ANISOU 3051  CA  ALA A 397     4196   4913   4269   -135   -222    456       C  
ATOM   3052  C   ALA A 397      20.424  19.816  -4.537  1.00 31.82           C  
ANISOU 3052  C   ALA A 397     3793   4421   3875   -140   -186    449       C  
ATOM   3053  O   ALA A 397      20.863  18.723  -4.176  1.00 34.44           O  
ANISOU 3053  O   ALA A 397     4135   4736   4214   -166   -166    416       O  
ATOM   3054  CB  ALA A 397      19.071  19.980  -6.637  1.00 32.22           C  
ANISOU 3054  CB  ALA A 397     3837   4568   3836   -142   -231    468       C  
ATOM   3055  N   MET A 398      21.124  20.933  -4.392  1.00 28.48           N  
ANISOU 3055  N   MET A 398     3527   3608   3685   -192   -162    120       N  
ATOM   3056  CA  MET A 398      22.434  20.983  -3.775  1.00 29.73           C  
ANISOU 3056  CA  MET A 398     3689   3764   3843   -207   -164    145       C  
ATOM   3057  C   MET A 398      22.399  20.504  -2.370  1.00 32.80           C  
ANISOU 3057  C   MET A 398     4073   4150   4241   -191   -150    146       C  
ATOM   3058  O   MET A 398      23.227  19.755  -1.965  1.00 29.84           O  
ANISOU 3058  O   MET A 398     3685   3779   3875   -198   -131    158       O  
ATOM   3059  CB  MET A 398      23.024  22.380  -3.814  1.00 27.31           C  
ANISOU 3059  CB  MET A 398     3420   3444   3514   -223   -205    162       C  
ATOM   3060  CG  MET A 398      24.489  22.469  -3.478  1.00 32.35           C  
ANISOU 3060  CG  MET A 398     4056   4091   4145   -252   -208    189       C  
ATOM   3061  SD  MET A 398      25.557  21.718  -4.643  1.00 35.45           S  
ANISOU 3061  SD  MET A 398     4412   4521   4535   -280   -186    200       S  
ATOM   3062  CE  MET A 398      26.159  20.388  -3.701  1.00 35.92           C  
ANISOU 3062  CE  MET A 398     4439   4594   4613   -260   -151    199       C  
ATOM   3063  N   SER A 399      21.394  20.934  -1.645  1.00 31.76           N  
ANISOU 3063  N   SER A 399     3782   4306   3980    -99   -165    458       N  
ATOM   3064  CA  SER A 399      21.212  20.437  -0.292  1.00 28.47           C  
ANISOU 3064  CA  SER A 399     3353   3871   3595   -100   -159    432       C  
ATOM   3065  C   SER A 399      21.032  18.909  -0.261  1.00 29.35           C  
ANISOU 3065  C   SER A 399     3461   3999   3693   -139   -148    395       C  
ATOM   3066  O   SER A 399      21.636  18.205   0.555  1.00 26.03           O  
ANISOU 3066  O   SER A 399     3051   3545   3295   -150   -129    374       O  
ATOM   3067  CB  SER A 399      19.989  21.135   0.330  1.00 29.57           C  
ANISOU 3067  CB  SER A 399     3467   4031   3740    -66   -182    441       C  
ATOM   3068  OG  SER A 399      19.742  20.583   1.613  1.00 32.12           O  
ANISOU 3068  OG  SER A 399     3775   4344   4086    -69   -173    417       O  
ATOM   3069  N   ALA A 400      20.161  18.410  -1.133  1.00 32.57           N  
ANISOU 3069  N   ALA A 400     3858   4455   4062   -158   -163    388       N  
ATOM   3070  CA  ALA A 400      19.854  16.982  -1.228  1.00 30.46           C  
ANISOU 3070  CA  ALA A 400     3598   4200   3774   -203   -161    353       C  
ATOM   3071  C   ALA A 400      21.110  16.148  -1.610  1.00 30.76           C  
ANISOU 3071  C   ALA A 400     3680   4203   3806   -216   -135    333       C  
ATOM   3072  O   ALA A 400      21.318  15.050  -1.077  1.00 30.45           O  
ANISOU 3072  O   ALA A 400     3661   4138   3772   -238   -123    304       O  
ATOM   3073  CB  ALA A 400      18.741  16.769  -2.244  1.00 27.88           C  
ANISOU 3073  CB  ALA A 400     3254   3936   3402   -224   -189    352       C  
ATOM   3074  N   VAL A 401      21.920  16.672  -2.534  1.00 26.63           N  
ANISOU 3074  N   VAL A 401     3172   3680   3268   -200   -125    351       N  
ATOM   3075  CA  VAL A 401      23.186  16.024  -2.914  1.00 31.14           C  
ANISOU 3075  CA  VAL A 401     3775   4227   3830   -199    -95    337       C  
ATOM   3076  C   VAL A 401      24.010  15.755  -1.665  1.00 28.43           C  
ANISOU 3076  C   VAL A 401     3435   3838   3531   -190    -75    327       C  
ATOM   3077  O   VAL A 401      24.379  14.613  -1.394  1.00 28.05           O  
ANISOU 3077  O   VAL A 401     3412   3768   3478   -198    -62    296       O  
ATOM   3078  CB  VAL A 401      24.014  16.852  -3.918  1.00 27.40           C  
ANISOU 3078  CB  VAL A 401     3306   3767   3339   -181    -83    368       C  
ATOM   3079  CG1 VAL A 401      25.474  16.339  -4.002  1.00 25.03           C  
ANISOU 3079  CG1 VAL A 401     3023   3448   3038   -171    -46    359       C  
ATOM   3080  CG2 VAL A 401      23.345  16.874  -5.311  1.00 21.91           C  
ANISOU 3080  CG2 VAL A 401     2619   3118   2587   -190   -100    373       C  
ATOM   3081  N   VAL A 402      24.251  16.805  -0.886  1.00 30.68           N  
ANISOU 3081  N   VAL A 402     3698   4105   3854   -171    -77    353       N  
ATOM   3082  CA  VAL A 402      25.039  16.715   0.327  1.00 26.84           C  
ANISOU 3082  CA  VAL A 402     3211   3578   3408   -161    -63    347       C  
ATOM   3083  C   VAL A 402      24.384  15.818   1.410  1.00 36.61           C  
ANISOU 3083  C   VAL A 402     4452   4800   4658   -173    -67    319       C  
ATOM   3084  O   VAL A 402      25.073  14.976   2.016  1.00 27.77           O  
ANISOU 3084  O   VAL A 402     3351   3651   3550   -172    -51    299       O  
ATOM   3085  CB  VAL A 402      25.334  18.097   0.907  1.00 34.61           C  
ANISOU 3085  CB  VAL A 402     4180   4544   4426   -143    -71    379       C  
ATOM   3086  CG1 VAL A 402      25.967  17.932   2.300  1.00 28.83           C  
ANISOU 3086  CG1 VAL A 402     3447   3773   3733   -135    -63    369       C  
ATOM   3087  CG2 VAL A 402      26.284  18.931  -0.053  1.00 26.05           C  
ANISOU 3087  CG2 VAL A 402     3098   3469   3333   -141    -62    413       C  
ATOM   3088  N   GLY A 403      23.066  15.985   1.647  1.00 23.00           N  
ANISOU 3088  N   GLY A 403     2709   3100   2931   -183    -88    320       N  
ATOM   3089  CA  GLY A 403      22.388  15.196   2.671  1.00 19.31           C  
ANISOU 3089  CA  GLY A 403     2240   2626   2473   -201    -91    300       C  
ATOM   3090  C   GLY A 403      22.296  13.717   2.239  1.00 29.04           C  
ANISOU 3090  C   GLY A 403     3505   3853   3675   -237    -87    269       C  
ATOM   3091  O   GLY A 403      22.447  12.819   3.070  1.00 29.18           O  
ANISOU 3091  O   GLY A 403     3544   3840   3702   -250    -78    251       O  
ATOM   3092  N   ASP A 404      22.061  13.455   0.950  1.00 27.61           N  
ANISOU 3092  N   ASP A 404     3336   3699   3455   -254    -95    264       N  
ATOM   3093  CA  ASP A 404      21.912  12.080   0.474  1.00 24.99           C  
ANISOU 3093  CA  ASP A 404     3048   3359   3090   -290    -96    232       C  
ATOM   3094  C   ASP A 404      23.250  11.355   0.473  1.00 30.61           C  
ANISOU 3094  C   ASP A 404     3806   4023   3801   -268    -70    213       C  
ATOM   3095  O   ASP A 404      23.344  10.234   0.927  1.00 32.66           O  
ANISOU 3095  O   ASP A 404     4107   4246   4056   -283    -66    187       O  
ATOM   3096  CB  ASP A 404      21.338  12.066  -0.946  1.00 30.98           C  
ANISOU 3096  CB  ASP A 404     3810   4160   3802   -310   -115    229       C  
ATOM   3097  CG  ASP A 404      19.865  12.544  -0.994  1.00 35.81           C  
ANISOU 3097  CG  ASP A 404     4373   4829   4406   -335   -146    244       C  
ATOM   3098  OD1 ASP A 404      19.248  12.702   0.082  1.00 32.20           O  
ANISOU 3098  OD1 ASP A 404     3883   4377   3975   -341   -150    252       O  
ATOM   3099  OD2 ASP A 404      19.343  12.778  -2.108  1.00 33.95           O  
ANISOU 3099  OD2 ASP A 404     4129   4637   4134   -345   -166    250       O  
ATOM   3100  N   HIS A 405      24.283  12.010  -0.052  1.00 24.57           N  
ANISOU 3100  N   HIS A 405     3035   3262   3039   -230    -53    227       N  
ATOM   3101  CA  HIS A 405      25.577  11.388  -0.196  1.00 29.05           C  
ANISOU 3101  CA  HIS A 405     3636   3803   3600   -200    -26    212       C  
ATOM   3102  C   HIS A 405      26.121  11.066   1.205  1.00 34.29           C  
ANISOU 3102  C   HIS A 405     4302   4425   4303   -185    -16    208       C  
ATOM   3103  O   HIS A 405      26.643   9.989   1.421  1.00 30.03           O  
ANISOU 3103  O   HIS A 405     3806   3851   3753   -174     -4    183       O  
ATOM   3104  CB  HIS A 405      26.511  12.343  -0.958  1.00 29.64           C  
ANISOU 3104  CB  HIS A 405     3686   3905   3671   -169     -9    239       C  
ATOM   3105  CG  HIS A 405      27.932  11.881  -1.074  1.00 33.36           C  
ANISOU 3105  CG  HIS A 405     4173   4367   4138   -132     22    231       C  
ATOM   3106  ND1 HIS A 405      28.285  10.559  -1.260  1.00 33.11           N  
ANISOU 3106  ND1 HIS A 405     4193   4311   4076   -117     34    194       N  
ATOM   3107  CD2 HIS A 405      29.097  12.578  -1.082  1.00 31.87           C  
ANISOU 3107  CD2 HIS A 405     3952   4192   3964   -104     44    257       C  
ATOM   3108  CE1 HIS A 405      29.593  10.466  -1.384  1.00 32.64           C  
ANISOU 3108  CE1 HIS A 405     4128   4258   4013    -73     64    197       C  
ATOM   3109  NE2 HIS A 405      30.114  11.680  -1.278  1.00 36.24           N  
ANISOU 3109  NE2 HIS A 405     4529   4743   4497    -69     70    236       N  
ATOM   3110  N   ASN A 406      25.965  11.990   2.154  1.00 29.49           N  
ANISOU 3110  N   ASN A 406     3653   3817   3735   -181    -22    231       N  
ATOM   3111  CA  ASN A 406      26.681  11.895   3.446  1.00 26.89           C  
ANISOU 3111  CA  ASN A 406     3322   3453   3440   -160    -13    232       C  
ATOM   3112  C   ASN A 406      25.938  11.181   4.546  1.00 30.22           C  
ANISOU 3112  C   ASN A 406     3762   3849   3873   -182    -22    218       C  
ATOM   3113  O   ASN A 406      26.558  10.573   5.429  1.00 24.14           O  
ANISOU 3113  O   ASN A 406     3014   3043   3116   -166    -13    208       O  
ATOM   3114  CB  ASN A 406      27.100  13.276   3.939  1.00 17.38           C  
ANISOU 3114  CB  ASN A 406     2075   2256   2272   -143    -16    262       C  
ATOM   3115  CG  ASN A 406      28.191  13.845   3.081  1.00 32.83           C  
ANISOU 3115  CG  ASN A 406     4018   4232   4223   -124     -1    280       C  
ATOM   3116  OD1 ASN A 406      29.316  13.277   3.001  1.00 29.23           O  
ANISOU 3116  OD1 ASN A 406     3571   3772   3762   -101     19    272       O  
ATOM   3117  ND2 ASN A 406      27.864  14.906   2.355  1.00 28.80           N  
ANISOU 3117  ND2 ASN A 406     3486   3748   3707   -132    -10    306       N  
ATOM   3118  N   VAL A 407      24.608  11.221   4.472  1.00 23.98           N  
ANISOU 3118  N   VAL A 407     2960   3081   3072   -219    -39    219       N  
ATOM   3119  CA  VAL A 407      23.809  10.773   5.597  1.00 28.81           C  
ANISOU 3119  CA  VAL A 407     3573   3680   3692   -244    -46    215       C  
ATOM   3120  C   VAL A 407      22.629   9.896   5.191  1.00 31.93           C  
ANISOU 3120  C   VAL A 407     3986   4091   4056   -300    -61    201       C  
ATOM   3121  O   VAL A 407      22.585   8.748   5.612  1.00 29.37           O  
ANISOU 3121  O   VAL A 407     3707   3730   3721   -326    -59    184       O  
ATOM   3122  CB  VAL A 407      23.280  11.984   6.434  1.00 32.27           C  
ANISOU 3122  CB  VAL A 407     3960   4142   4159   -230    -53    238       C  
ATOM   3123  CG1 VAL A 407      22.283  11.535   7.496  1.00 26.16           C  
ANISOU 3123  CG1 VAL A 407     3180   3373   3386   -258    -57    237       C  
ATOM   3124  CG2 VAL A 407      24.435  12.740   7.054  1.00 26.95           C  
ANISOU 3124  CG2 VAL A 407     3279   3444   3516   -187    -45    249       C  
ATOM   3125  N   VAL A 408      21.680  10.430   4.396  1.00 26.94           N  
ANISOU 3125  N   VAL A 408     3319   3511   3407   -321    -78    211       N  
ATOM   3126  CA  VAL A 408      20.482   9.660   4.087  1.00 26.24           C  
ANISOU 3126  CA  VAL A 408     3236   3447   3288   -383    -97    201       C  
ATOM   3127  C   VAL A 408      20.783   8.307   3.417  1.00 36.68           C  
ANISOU 3127  C   VAL A 408     4632   4729   4577   -415    -99    170       C  
ATOM   3128  O   VAL A 408      20.209   7.294   3.805  1.00 30.93           O  
ANISOU 3128  O   VAL A 408     3935   3981   3834   -468   -108    158       O  
ATOM   3129  CB  VAL A 408      19.448  10.420   3.220  1.00 30.75           C  
ANISOU 3129  CB  VAL A 408     3755   4089   3841   -397   -119    216       C  
ATOM   3130  CG1 VAL A 408      18.242   9.483   2.976  1.00 22.96           C  
ANISOU 3130  CG1 VAL A 408     2771   3131   2821   -473   -141    205       C  
ATOM   3131  CG2 VAL A 408      19.003  11.689   3.906  1.00 22.12           C  
ANISOU 3131  CG2 VAL A 408     2598   3032   2775   -361   -119    244       C  
ATOM   3132  N   CYS A 409      21.698   8.281   2.438  1.00 33.39           N  
ANISOU 3132  N   CYS A 409     4245   4298   4143   -382    -90    158       N  
ATOM   3133  CA  CYS A 409      21.956   7.037   1.745  1.00 34.07           C  
ANISOU 3133  CA  CYS A 409     4408   4345   4190   -402    -93    125       C  
ATOM   3134  C   CYS A 409      22.850   6.056   2.544  1.00 38.72           C  
ANISOU 3134  C   CYS A 409     5061   4861   4788   -380    -76    107       C  
ATOM   3135  O   CYS A 409      22.550   4.857   2.587  1.00 40.43           O  
ANISOU 3135  O   CYS A 409     5347   5036   4981   -420    -86     84       O  
ATOM   3136  CB  CYS A 409      22.413   7.286   0.305  1.00 33.71           C  
ANISOU 3136  CB  CYS A 409     4374   4321   4112   -377    -92    116       C  
ATOM   3137  SG  CYS A 409      21.092   8.098  -0.710  1.00 34.18           S  
ANISOU 3137  SG  CYS A 409     4378   4463   4147   -417   -124    133       S  
ATOM   3138  N   PRO A 410      23.923   6.557   3.201  1.00 32.00           N  
ANISOU 3138  N   PRO A 410     4192   3997   3972   -318    -52    119       N  
ATOM   3139  CA  PRO A 410      24.591   5.686   4.168  1.00 27.18           C  
ANISOU 3139  CA  PRO A 410     3631   3325   3371   -298    -40    108       C  
ATOM   3140  C   PRO A 410      23.664   5.091   5.243  1.00 33.99           C  
ANISOU 3140  C   PRO A 410     4510   4165   4241   -354    -53    112       C  
ATOM   3141  O   PRO A 410      23.812   3.914   5.616  1.00 29.07           O  
ANISOU 3141  O   PRO A 410     3961   3482   3603   -367    -54     95       O  
ATOM   3142  CB  PRO A 410      25.630   6.606   4.809  1.00 29.87           C  
ANISOU 3142  CB  PRO A 410     3923   3675   3751   -237    -21    129       C  
ATOM   3143  CG  PRO A 410      25.990   7.584   3.664  1.00 30.73           C  
ANISOU 3143  CG  PRO A 410     3989   3832   3853   -213    -15    139       C  
ATOM   3144  CD  PRO A 410      24.682   7.809   2.946  1.00 30.73           C  
ANISOU 3144  CD  PRO A 410     3974   3870   3832   -267    -37    141       C  
ATOM   3145  N   VAL A 411      22.733   5.883   5.757  1.00 29.72           N  
ANISOU 3145  N   VAL A 411     3901   3671   3719   -384    -61    136       N  
ATOM   3146  CA  VAL A 411      21.765   5.334   6.703  1.00 34.77           C  
ANISOU 3146  CA  VAL A 411     4547   4305   4360   -442    -70    144       C  
ATOM   3147  C   VAL A 411      20.941   4.210   6.022  1.00 35.52           C  
ANISOU 3147  C   VAL A 411     4697   4385   4413   -519    -92    125       C  
ATOM   3148  O   VAL A 411      20.812   3.131   6.571  1.00 38.93           O  
ANISOU 3148  O   VAL A 411     5193   4766   4833   -557    -95    117       O  
ATOM   3149  CB  VAL A 411      20.897   6.459   7.350  1.00 32.11           C  
ANISOU 3149  CB  VAL A 411     4121   4033   4046   -449    -72    173       C  
ATOM   3150  CG1 VAL A 411      19.616   5.905   7.993  1.00 29.81           C  
ANISOU 3150  CG1 VAL A 411     3820   3764   3743   -523    -82    184       C  
ATOM   3151  CG2 VAL A 411      21.713   7.211   8.367  1.00 31.15           C  
ANISOU 3151  CG2 VAL A 411     3975   3900   3961   -386    -54    187       C  
ATOM   3152  N   ALA A 412      20.439   4.456   4.811  1.00 33.39           N  
ANISOU 3152  N   ALA A 412     4410   4159   4119   -542   -108    118       N  
ATOM   3153  CA  ALA A 412      19.713   3.437   4.053  1.00 33.10           C  
ANISOU 3153  CA  ALA A 412     4429   4110   4039   -618   -135     96       C  
ATOM   3154  C   ALA A 412      20.518   2.141   3.915  1.00 34.04           C  
ANISOU 3154  C   ALA A 412     4665   4135   4133   -610   -132     64       C  
ATOM   3155  O   ALA A 412      20.019   1.053   4.198  1.00 38.76           O  
ANISOU 3155  O   ALA A 412     5330   4687   4710   -676   -148     54       O  
ATOM   3156  CB  ALA A 412      19.329   3.975   2.660  1.00 28.83           C  
ANISOU 3156  CB  ALA A 412     3856   3626   3471   -624   -152     90       C  
ATOM   3157  N   GLN A 413      21.770   2.265   3.489  1.00 32.41           N  
ANISOU 3157  N   GLN A 413     4485   3902   3928   -526   -112     49       N  
ATOM   3158  CA  GLN A 413      22.644   1.106   3.352  1.00 35.97           C  
ANISOU 3158  CA  GLN A 413     5045   4268   4353   -495   -106     17       C  
ATOM   3159  C   GLN A 413      22.808   0.356   4.687  1.00 39.31           C  
ANISOU 3159  C   GLN A 413     5517   4627   4793   -501   -100     24       C  
ATOM   3160  O   GLN A 413      22.702  -0.878   4.725  1.00 35.68           O  
ANISOU 3160  O   GLN A 413     5159   4093   4303   -535   -114      4       O  
ATOM   3161  CB  GLN A 413      24.020   1.545   2.855  1.00 37.28           C  
ANISOU 3161  CB  GLN A 413     5205   4438   4523   -393    -78      9       C  
ATOM   3162  CG  GLN A 413      24.871   0.426   2.317  1.00 47.47           C  
ANISOU 3162  CG  GLN A 413     6605   5660   5774   -348    -72    -29       C  
ATOM   3163  CD  GLN A 413      26.147   0.968   1.745  1.00 60.06           C  
ANISOU 3163  CD  GLN A 413     8171   7281   7367   -250    -42    -32       C  
ATOM   3164  OE1 GLN A 413      26.341   0.984   0.523  1.00 70.55           O  
ANISOU 3164  OE1 GLN A 413     9516   8631   8658   -232    -39    -52       O  
ATOM   3165  NE2 GLN A 413      27.014   1.469   2.615  1.00 56.22           N  
ANISOU 3165  NE2 GLN A 413     7637   6802   6921   -191    -19    -10       N  
ATOM   3166  N   LEU A 414      23.084   1.105   5.767  1.00 30.31           N  
ANISOU 3166  N   LEU A 414     4309   3510   3696   -466    -82     54       N  
ATOM   3167  CA  LEU A 414      23.183   0.523   7.096  1.00 34.99           C  
ANISOU 3167  CA  LEU A 414     4938   4053   4305   -472    -77     66       C  
ATOM   3168  C   LEU A 414      21.921  -0.221   7.539  1.00 40.57           C  
ANISOU 3168  C   LEU A 414     5675   4745   4994   -578    -98     75       C  
ATOM   3169  O   LEU A 414      22.013  -1.384   7.928  1.00 42.64           O  
ANISOU 3169  O   LEU A 414     6036   4928   5237   -602   -105     65       O  
ATOM   3170  CB  LEU A 414      23.595   1.539   8.170  1.00 34.03           C  
ANISOU 3170  CB  LEU A 414     4736   3967   4229   -422    -58     95       C  
ATOM   3171  CG  LEU A 414      23.768   0.993   9.592  1.00 33.36           C  
ANISOU 3171  CG  LEU A 414     4685   3833   4155   -420    -52    109       C  
ATOM   3172  CD1 LEU A 414      24.847  -0.141   9.662  1.00 24.17           C  
ANISOU 3172  CD1 LEU A 414     3628   2582   2973   -366    -48     87       C  
ATOM   3173  CD2 LEU A 414      24.140   2.135  10.551  1.00 37.23           C  
ANISOU 3173  CD2 LEU A 414     5092   4367   4687   -371    -37    134       C  
ATOM   3174  N   ALA A 415      20.759   0.428   7.498  1.00 35.34           N  
ANISOU 3174  N   ALA A 415     4931   4159   4338   -642   -109     95       N  
ATOM   3175  CA  ALA A 415      19.545  -0.241   7.957  1.00 36.70           C  
ANISOU 3175  CA  ALA A 415     5118   4334   4494   -749   -127    109       C  
ATOM   3176  C   ALA A 415      19.336  -1.536   7.172  1.00 44.17           C  
ANISOU 3176  C   ALA A 415     6176   5212   5394   -813   -154     80       C  
ATOM   3177  O   ALA A 415      19.003  -2.597   7.738  1.00 45.33           O  
ANISOU 3177  O   ALA A 415     6402   5297   5524   -879   -165     83       O  
ATOM   3178  CB  ALA A 415      18.337   0.664   7.804  1.00 39.08           C  
ANISOU 3178  CB  ALA A 415     5306   4742   4801   -799   -136    133       C  
ATOM   3179  N   GLY A 416      19.534  -1.447   5.865  1.00 38.42           N  
ANISOU 3179  N   GLY A 416     5463   4493   4644   -795   -165     51       N  
ATOM   3180  CA  GLY A 416      19.333  -2.604   5.012  1.00 44.71           C  
ANISOU 3180  CA  GLY A 416     6370   5225   5391   -852   -195     17       C  
ATOM   3181  C   GLY A 416      20.264  -3.766   5.308  1.00 41.31           C  
ANISOU 3181  C   GLY A 416     6078   4674   4943   -813   -190     -7       C  
ATOM   3182  O   GLY A 416      19.810  -4.903   5.468  1.00 42.81           O  
ANISOU 3182  O   GLY A 416     6369   4793   5104   -891   -214    -14       O  
ATOM   3183  N   ARG A 417      21.562  -3.495   5.392  1.00 40.09           N  
ANISOU 3183  N   ARG A 417     5930   4497   4805   -693   -161    -16       N  
ATOM   3184  CA  ARG A 417      22.511  -4.558   5.721  1.00 42.54           C  
ANISOU 3184  CA  ARG A 417     6365   4699   5098   -636   -155    -37       C  
ATOM   3185  C   ARG A 417      22.225  -5.148   7.107  1.00 41.50           C  
ANISOU 3185  C   ARG A 417     6271   4517   4980   -680   -156     -9       C  
ATOM   3186  O   ARG A 417      22.317  -6.342   7.302  1.00 47.05           O  
ANISOU 3186  O   ARG A 417     7103   5121   5653   -702   -171    -22       O  
ATOM   3187  CB  ARG A 417      23.967  -4.074   5.611  1.00 38.69           C  
ANISOU 3187  CB  ARG A 417     5857   4218   4626   -496   -122    -47       C  
ATOM   3188  CG  ARG A 417      24.345  -3.575   4.218  1.00 48.67           C  
ANISOU 3188  CG  ARG A 417     7094   5528   5870   -450   -117    -73       C  
ATOM   3189  CD  ARG A 417      24.779  -4.666   3.243  1.00 63.89           C  
ANISOU 3189  CD  ARG A 417     9155   7380   7739   -422   -128   -121       C  
ATOM   3190  NE  ARG A 417      23.854  -5.797   3.178  1.00 81.57           N  
ANISOU 3190  NE  ARG A 417    11506   9546   9942   -525   -166   -138       N  
ATOM   3191  CZ  ARG A 417      24.223  -7.064   2.959  1.00 90.79           C  
ANISOU 3191  CZ  ARG A 417    12827  10604  11065   -508   -179   -174       C  
ATOM   3192  NH1 ARG A 417      25.512  -7.369   2.780  1.00 90.72           N  
ANISOU 3192  NH1 ARG A 417    12873  10556  11041   -379   -155   -198       N  
ATOM   3193  NH2 ARG A 417      23.302  -8.032   2.933  1.00 92.10           N  
ANISOU 3193  NH2 ARG A 417    13094  10702  11199   -619   -218   -185       N  
ATOM   3194  N   LEU A 418      21.877  -4.304   8.067  1.00 37.48           N  
ANISOU 3194  N   LEU A 418     5655   4075   4511   -691   -141     31       N  
ATOM   3195  CA  LEU A 418      21.708  -4.762   9.432  1.00 40.94           C  
ANISOU 3195  CA  LEU A 418     6121   4475   4961   -719   -136     61       C  
ATOM   3196  C   LEU A 418      20.492  -5.691   9.531  1.00 43.69           C  
ANISOU 3196  C   LEU A 418     6531   4791   5278   -859   -165     70       C  
ATOM   3197  O   LEU A 418      20.557  -6.719  10.199  1.00 45.03           O  
ANISOU 3197  O   LEU A 418     6806   4871   5430   -887   -172     77       O  
ATOM   3198  CB  LEU A 418      21.550  -3.578  10.383  1.00 38.69           C  
ANISOU 3198  CB  LEU A 418     5705   4276   4720   -699   -113     98       C  
ATOM   3199  CG  LEU A 418      22.715  -3.128  11.272  1.00 43.85           C  
ANISOU 3199  CG  LEU A 418     6336   4920   5404   -589    -88    108       C  
ATOM   3200  CD1 LEU A 418      24.084  -3.407  10.671  1.00 52.80           C  
ANISOU 3200  CD1 LEU A 418     7528   6004   6530   -482    -81     76       C  
ATOM   3201  CD2 LEU A 418      22.557  -1.676  11.590  1.00 33.89           C  
ANISOU 3201  CD2 LEU A 418     4938   3759   4181   -563    -72    130       C  
ATOM   3202  N   ALA A 419      19.392  -5.310   8.880  1.00 40.06           N  
ANISOU 3202  N   ALA A 419     6003   4406   4810   -947   -183     74       N  
ATOM   3203  CA  ALA A 419      18.202  -6.145   8.853  1.00 46.16           C  
ANISOU 3203  CA  ALA A 419     6823   5165   5553  -1091   -214     84       C  
ATOM   3204  C   ALA A 419      18.457  -7.443   8.084  1.00 48.00           C  
ANISOU 3204  C   ALA A 419     7221   5280   5738  -1119   -245     44       C  
ATOM   3205  O   ALA A 419      17.992  -8.503   8.483  1.00 52.69           O  
ANISOU 3205  O   ALA A 419     7914   5799   6306  -1211   -266     52       O  
ATOM   3206  CB  ALA A 419      17.002  -5.385   8.242  1.00 41.28           C  
ANISOU 3206  CB  ALA A 419     6083   4667   4934  -1170   -229     96       C  
ATOM   3207  N   ALA A 420      19.181  -7.363   6.974  1.00 48.06           N  
ANISOU 3207  N   ALA A 420     7261   5269   5730  -1041   -247      0       N  
ATOM   3208  CA  ALA A 420      19.339  -8.544   6.136  1.00 50.66           C  
ANISOU 3208  CA  ALA A 420     7749   5493   6008  -1066   -279    -43       C  
ATOM   3209  C   ALA A 420      20.074  -9.577   6.956  1.00 57.99           C  
ANISOU 3209  C   ALA A 420     8813   6293   6926  -1026   -273    -45       C  
ATOM   3210  O   ALA A 420      19.988 -10.774   6.704  1.00 62.11           O  
ANISOU 3210  O   ALA A 420     9490   6705   7405  -1075   -304    -68       O  
ATOM   3211  CB  ALA A 420      20.091  -8.225   4.845  1.00 41.11           C  
ANISOU 3211  CB  ALA A 420     6546   4293   4779   -971   -275    -89       C  
ATOM   3212  N   GLN A 421      20.756  -9.091   7.983  1.00 57.06           N  
ANISOU 3212  N   GLN A 421     8641   6192   6848   -939   -238    -17       N  
ATOM   3213  CA  GLN A 421      21.657  -9.914   8.764  1.00 51.74           C  
ANISOU 3213  CA  GLN A 421     8083   5409   6167   -869   -229    -18       C  
ATOM   3214  C   GLN A 421      21.216 -10.155  10.201  1.00 48.62           C  
ANISOU 3214  C   GLN A 421     7686   4998   5788   -929   -224     33       C  
ATOM   3215  O   GLN A 421      22.031 -10.470  11.068  1.00 51.76           O  
ANISOU 3215  O   GLN A 421     8135   5337   6193   -850   -208     44       O  
ATOM   3216  CB  GLN A 421      23.059  -9.317   8.693  1.00 51.87           C  
ANISOU 3216  CB  GLN A 421     8060   5444   6206   -701   -195    -33       C  
ATOM   3217  CG  GLN A 421      23.737  -9.775   7.419  1.00 64.10           C  
ANISOU 3217  CG  GLN A 421     9697   6945   7715   -631   -203    -88       C  
ATOM   3218  CD  GLN A 421      24.650  -8.749   6.893  1.00 73.78           C  
ANISOU 3218  CD  GLN A 421    10819   8253   8963   -512   -172   -100       C  
ATOM   3219  OE1 GLN A 421      24.692  -8.488   5.687  1.00 80.70           O  
ANISOU 3219  OE1 GLN A 421    11681   9163   9817   -497   -175   -131       O  
ATOM   3220  NE2 GLN A 421      25.386  -8.121   7.792  1.00 78.70           N  
ANISOU 3220  NE2 GLN A 421    11364   8913   9627   -430   -142    -73       N  
ATOM   3221  N   GLY A 422      19.917 -10.012  10.443  1.00 51.56           N  
ANISOU 3221  N   GLY A 422     7998   5430   6163  -1067   -236     64       N  
ATOM   3222  CA  GLY A 422      19.313 -10.474  11.677  1.00 43.07           C  
ANISOU 3222  CA  GLY A 422     6944   4334   5089  -1153   -236    112       C  
ATOM   3223  C   GLY A 422      19.089  -9.465  12.776  1.00 45.17           C  
ANISOU 3223  C   GLY A 422     7064   4703   5395  -1137   -202    158       C  
ATOM   3224  O   GLY A 422      18.573  -9.820  13.828  1.00 52.42           O  
ANISOU 3224  O   GLY A 422     7994   5612   6310  -1207   -198    200       O  
ATOM   3225  N   ALA A 423      19.472  -8.210  12.564  1.00 42.47           N  
ANISOU 3225  N   ALA A 423     6590   4457   5089  -1048   -179    152       N  
ATOM   3226  CA  ALA A 423      19.244  -7.200  13.585  1.00 36.06           C  
ANISOU 3226  CA  ALA A 423     5647   3742   4314  -1029   -149    191       C  
ATOM   3227  C   ALA A 423      17.810  -6.742  13.515  1.00 36.43           C  
ANISOU 3227  C   ALA A 423     5589   3895   4359  -1147   -155    217       C  
ATOM   3228  O   ALA A 423      17.236  -6.731  12.442  1.00 43.24           O  
ANISOU 3228  O   ALA A 423     6436   4787   5207  -1204   -178    198       O  
ATOM   3229  CB  ALA A 423      20.170  -5.987  13.347  1.00 35.92           C  
ANISOU 3229  CB  ALA A 423     5532   3783   4332   -896   -126    174       C  
ATOM   3230  N   ARG A 424      17.241  -6.317  14.638  1.00 38.37           N  
ANISOU 3230  N   ARG A 424     5756   4206   4618  -1177   -134    261       N  
ATOM   3231  CA  ARG A 424      15.952  -5.637  14.606  1.00 42.17           C  
ANISOU 3231  CA  ARG A 424     6107   4814   5101  -1261   -132    288       C  
ATOM   3232  C   ARG A 424      16.203  -4.134  14.464  1.00 37.87           C  
ANISOU 3232  C   ARG A 424     5427   4368   4593  -1159   -111    281       C  
ATOM   3233  O   ARG A 424      16.828  -3.553  15.329  1.00 37.74           O  
ANISOU 3233  O   ARG A 424     5380   4359   4601  -1072    -85    291       O  
ATOM   3234  CB  ARG A 424      15.169  -5.901  15.892  1.00 43.95           C  
ANISOU 3234  CB  ARG A 424     6312   5072   5317  -1339   -116    340       C  
ATOM   3235  CG  ARG A 424      13.829  -5.184  15.954  1.00 53.00           C  
ANISOU 3235  CG  ARG A 424     7313   6363   6461  -1415   -110    370       C  
ATOM   3236  CD  ARG A 424      12.739  -6.057  16.595  1.00 77.35           C  
ANISOU 3236  CD  ARG A 424    10416   9461   9511  -1566   -114    416       C  
ATOM   3237  NE  ARG A 424      12.765  -6.043  18.063  1.00 89.85           N  
ANISOU 3237  NE  ARG A 424    11990  11054  11094  -1551    -80    458       N  
ATOM   3238  CZ  ARG A 424      13.239  -7.034  18.819  1.00 95.93           C  
ANISOU 3238  CZ  ARG A 424    12888  11714  11847  -1569    -79    474       C  
ATOM   3239  NH1 ARG A 424      13.735  -8.129  18.249  1.00 97.63           N  
ANISOU 3239  NH1 ARG A 424    13253  11796  12045  -1597   -110    449       N  
ATOM   3240  NH2 ARG A 424      13.217  -6.929  20.148  1.00 97.05           N  
ANISOU 3240  NH2 ARG A 424    13012  11879  11986  -1553    -47    513       N  
ATOM   3241  N   VAL A 425      15.675  -3.529  13.399  1.00 34.39           N  
ANISOU 3241  N   VAL A 425     4912   4001   4153  -1176   -125    266       N  
ATOM   3242  CA  VAL A 425      15.926  -2.130  13.040  1.00 32.58           C  
ANISOU 3242  CA  VAL A 425     4570   3853   3954  -1083   -111    257       C  
ATOM   3243  C   VAL A 425      14.648  -1.326  13.050  1.00 35.89           C  
ANISOU 3243  C   VAL A 425     4858   4405   4374  -1135   -110    284       C  
ATOM   3244  O   VAL A 425      13.645  -1.810  12.569  1.00 40.24           O  
ANISOU 3244  O   VAL A 425     5400   4991   4898  -1242   -133    291       O  
ATOM   3245  CB  VAL A 425      16.488  -2.039  11.609  1.00 34.73           C  
ANISOU 3245  CB  VAL A 425     4872   4101   4224  -1042   -130    215       C  
ATOM   3246  CG1 VAL A 425      16.921  -0.586  11.289  1.00 32.45           C  
ANISOU 3246  CG1 VAL A 425     4480   3881   3967   -940   -114    210       C  
ATOM   3247  CG2 VAL A 425      17.648  -3.049  11.423  1.00 30.54           C  
ANISOU 3247  CG2 VAL A 425     4483   3439   3681   -999   -135    185       C  
ATOM   3248  N   TYR A 426      14.678  -0.114  13.609  1.00 31.76           N  
ANISOU 3248  N   TYR A 426     4235   3956   3878  -1058    -85    298       N  
ATOM   3249  CA  TYR A 426      13.578   0.836  13.489  1.00 26.81           C  
ANISOU 3249  CA  TYR A 426     3478   3458   3252  -1075    -83    318       C  
ATOM   3250  C   TYR A 426      14.134   2.102  12.872  1.00 34.20           C  
ANISOU 3250  C   TYR A 426     4357   4423   4214   -967    -80    299       C  
ATOM   3251  O   TYR A 426      15.144   2.598  13.345  1.00 33.11           O  
ANISOU 3251  O   TYR A 426     4234   4244   4101   -874    -62    291       O  
ATOM   3252  CB  TYR A 426      13.011   1.181  14.868  1.00 27.78           C  
ANISOU 3252  CB  TYR A 426     3537   3644   3376  -1076    -54    355       C  
ATOM   3253  CG  TYR A 426      12.342   0.022  15.523  1.00 44.38           C  
ANISOU 3253  CG  TYR A 426     5682   5733   5448  -1191    -54    384       C  
ATOM   3254  CD1 TYR A 426      13.066  -0.852  16.343  1.00 41.65           C  
ANISOU 3254  CD1 TYR A 426     5443   5282   5098  -1192    -44    388       C  
ATOM   3255  CD2 TYR A 426      10.989  -0.247  15.289  1.00 43.50           C  
ANISOU 3255  CD2 TYR A 426     5508   5713   5309  -1305    -66    408       C  
ATOM   3256  CE1 TYR A 426      12.467  -1.929  16.913  1.00 43.10           C  
ANISOU 3256  CE1 TYR A 426     5677   5446   5252  -1303    -46    417       C  
ATOM   3257  CE2 TYR A 426      10.368  -1.345  15.878  1.00 43.32           C  
ANISOU 3257  CE2 TYR A 426     5526   5677   5256  -1425    -67    439       C  
ATOM   3258  CZ  TYR A 426      11.105  -2.173  16.685  1.00 45.13           C  
ANISOU 3258  CZ  TYR A 426     5869   5794   5483  -1425    -57    444       C  
ATOM   3259  OH  TYR A 426      10.504  -3.261  17.266  1.00 48.53           O  
ANISOU 3259  OH  TYR A 426     6351   6206   5883  -1548    -59    478       O  
ATOM   3260  N   ALA A 427      13.501   2.625  11.826  1.00 32.11           N  
ANISOU 3260  N   ALA A 427     4029   4230   3942   -982    -99    293       N  
ATOM   3261  CA  ALA A 427      14.024   3.810  11.145  1.00 28.93           C  
ANISOU 3261  CA  ALA A 427     3582   3849   3561   -886    -99    279       C  
ATOM   3262  C   ALA A 427      13.044   4.972  11.217  1.00 38.92           C  
ANISOU 3262  C   ALA A 427     4724   5234   4828   -864    -95    301       C  
ATOM   3263  O   ALA A 427      11.807   4.775  11.251  1.00 36.35           O  
ANISOU 3263  O   ALA A 427     4339   4992   4480   -939   -104    322       O  
ATOM   3264  CB  ALA A 427      14.328   3.488   9.682  1.00 28.34           C  
ANISOU 3264  CB  ALA A 427     3554   3744   3472   -900   -125    249       C  
ATOM   3265  N   TYR A 428      13.570   6.194  11.212  1.00 32.81           N  
ANISOU 3265  N   TYR A 428     3913   4472   4080   -763    -85    298       N  
ATOM   3266  CA  TYR A 428      12.691   7.369  11.250  1.00 28.18           C  
ANISOU 3266  CA  TYR A 428     3221   3991   3494   -725    -83    318       C  
ATOM   3267  C   TYR A 428      13.233   8.482  10.355  1.00 38.48           C  
ANISOU 3267  C   TYR A 428     4511   5295   4815   -644    -92    306       C  
ATOM   3268  O   TYR A 428      14.444   8.542  10.040  1.00 34.17           O  
ANISOU 3268  O   TYR A 428     4026   4669   4287   -600    -90    287       O  
ATOM   3269  CB  TYR A 428      12.550   7.917  12.693  1.00 30.16           C  
ANISOU 3269  CB  TYR A 428     3434   4268   3755   -678    -53    337       C  
ATOM   3270  CG  TYR A 428      13.847   8.514  13.212  1.00 40.18           C  
ANISOU 3270  CG  TYR A 428     4750   5461   5056   -587    -39    323       C  
ATOM   3271  CD1 TYR A 428      14.263   9.789  12.829  1.00 38.69           C  
ANISOU 3271  CD1 TYR A 428     4535   5279   4888   -501    -42    318       C  
ATOM   3272  CD2 TYR A 428      14.671   7.789  14.051  1.00 40.24           C  
ANISOU 3272  CD2 TYR A 428     4829   5388   5072   -590    -25    318       C  
ATOM   3273  CE1 TYR A 428      15.461  10.316  13.280  1.00 33.56           C  
ANISOU 3273  CE1 TYR A 428     3926   4560   4265   -430    -34    307       C  
ATOM   3274  CE2 TYR A 428      15.854   8.294  14.491  1.00 38.51           C  
ANISOU 3274  CE2 TYR A 428     4646   5108   4880   -514    -17    307       C  
ATOM   3275  CZ  TYR A 428      16.248   9.557  14.107  1.00 36.42           C  
ANISOU 3275  CZ  TYR A 428     4350   4853   4634   -438    -21    301       C  
ATOM   3276  OH  TYR A 428      17.444  10.033  14.554  1.00 36.21           O  
ANISOU 3276  OH  TYR A 428     4358   4766   4633   -374    -16    291       O  
ATOM   3277  N   ILE A 429      12.337   9.387   9.975  1.00 37.97           N  
ANISOU 3277  N   ILE A 429     4362   5323   4742   -620   -102    320       N  
ATOM   3278  CA  ILE A 429      12.748  10.667   9.454  1.00 34.12           C  
ANISOU 3278  CA  ILE A 429     3855   4840   4270   -531   -106    319       C  
ATOM   3279  C   ILE A 429      12.114  11.741  10.338  1.00 38.37           C  
ANISOU 3279  C   ILE A 429     4323   5444   4813   -466    -92    339       C  
ATOM   3280  O   ILE A 429      10.896  11.726  10.594  1.00 35.97           O  
ANISOU 3280  O   ILE A 429     3946   5236   4487   -491    -93    357       O  
ATOM   3281  CB  ILE A 429      12.370  10.849   7.988  1.00 34.13           C  
ANISOU 3281  CB  ILE A 429     3837   4881   4252   -547   -136    315       C  
ATOM   3282  CG1 ILE A 429      12.753  12.258   7.548  1.00 31.26           C  
ANISOU 3282  CG1 ILE A 429     3454   4520   3904   -452   -139    320       C  
ATOM   3283  CG2 ILE A 429      10.868  10.601   7.811  1.00 39.02           C  
ANISOU 3283  CG2 ILE A 429     4377   5610   4839   -608   -153    333       C  
ATOM   3284  CD1 ILE A 429      13.031  12.371   6.084  1.00 40.51           C  
ANISOU 3284  CD1 ILE A 429     4646   5685   5062   -455   -163    312       C  
ATOM   3285  N   PHE A 430      12.943  12.654  10.833  1.00 31.71           N  
ANISOU 3285  N   PHE A 430     3501   4552   3995   -382    -80    335       N  
ATOM   3286  CA  PHE A 430      12.476  13.666  11.757  1.00 35.01           C  
ANISOU 3286  CA  PHE A 430     3872   5015   4415   -311    -67    348       C  
ATOM   3287  C   PHE A 430      12.133  14.916  10.955  1.00 37.22           C  
ANISOU 3287  C   PHE A 430     4113   5336   4692   -244    -85    355       C  
ATOM   3288  O   PHE A 430      12.974  15.417  10.241  1.00 36.06           O  
ANISOU 3288  O   PHE A 430     4007   5133   4562   -214    -97    347       O  
ATOM   3289  CB  PHE A 430      13.569  13.963  12.777  1.00 35.41           C  
ANISOU 3289  CB  PHE A 430     3977   4984   4492   -261    -49    337       C  
ATOM   3290  CG  PHE A 430      13.191  15.002  13.774  1.00 35.22           C  
ANISOU 3290  CG  PHE A 430     3921   4994   4467   -184    -36    345       C  
ATOM   3291  CD1 PHE A 430      13.407  16.354  13.504  1.00 34.93           C  
ANISOU 3291  CD1 PHE A 430     3885   4947   4441   -100    -48    344       C  
ATOM   3292  CD2 PHE A 430      12.633  14.641  14.990  1.00 33.79           C  
ANISOU 3292  CD2 PHE A 430     3717   4850   4270   -192    -13    353       C  
ATOM   3293  CE1 PHE A 430      13.069  17.325  14.423  1.00 30.57           C  
ANISOU 3293  CE1 PHE A 430     3315   4417   3883    -22    -39    347       C  
ATOM   3294  CE2 PHE A 430      12.285  15.617  15.926  1.00 33.27           C  
ANISOU 3294  CE2 PHE A 430     3627   4817   4196   -112      1    357       C  
ATOM   3295  CZ  PHE A 430      12.508  16.958  15.635  1.00 28.53           C  
ANISOU 3295  CZ  PHE A 430     3033   4201   3607    -24    -14    351       C  
ATOM   3296  N   GLU A 431      10.903  15.424  11.050  1.00 39.80           N  
ANISOU 3296  N   GLU A 431     4361   5765   4995   -218    -87    373       N  
ATOM   3297  CA  GLU A 431      10.507  16.465  10.091  1.00 40.21           C  
ANISOU 3297  CA  GLU A 431     4381   5859   5040   -160   -111    382       C  
ATOM   3298  C   GLU A 431       9.976  17.724  10.724  1.00 42.40           C  
ANISOU 3298  C   GLU A 431     4621   6180   5311    -57   -104    393       C  
ATOM   3299  O   GLU A 431       9.352  18.521  10.037  1.00 46.00           O  
ANISOU 3299  O   GLU A 431     5037   6690   5751     -6   -124    405       O  
ATOM   3300  CB  GLU A 431       9.407  15.959   9.161  1.00 39.64           C  
ANISOU 3300  CB  GLU A 431     4244   5883   4936   -220   -132    394       C  
ATOM   3301  CG  GLU A 431       9.776  14.860   8.230  1.00 46.99           C  
ANISOU 3301  CG  GLU A 431     5214   6779   5863   -314   -149    381       C  
ATOM   3302  CD  GLU A 431       8.565  14.382   7.431  1.00 50.69           C  
ANISOU 3302  CD  GLU A 431     5613   7353   6295   -378   -175    393       C  
ATOM   3303  OE1 GLU A 431       7.450  14.402   7.978  1.00 53.44           O  
ANISOU 3303  OE1 GLU A 431     5879   7802   6622   -384   -169    412       O  
ATOM   3304  OE2 GLU A 431       8.725  13.993   6.258  1.00 54.47           O  
ANISOU 3304  OE2 GLU A 431     6117   7818   6762   -423   -201    384       O  
ATOM   3305  N   HIS A 432      10.168  17.905  12.023  1.00 38.74           N  
ANISOU 3305  N   HIS A 432     4171   5694   4854    -20    -79    388       N  
ATOM   3306  CA  HIS A 432       9.632  19.104  12.650  1.00 41.59           C  
ANISOU 3306  CA  HIS A 432     4503   6094   5203     86    -73    394       C  
ATOM   3307  C   HIS A 432      10.728  20.166  12.845  1.00 41.51           C  
ANISOU 3307  C   HIS A 432     4574   5978   5220    160    -80    381       C  
ATOM   3308  O   HIS A 432      11.794  19.903  13.389  1.00 39.24           O  
ANISOU 3308  O   HIS A 432     4350   5602   4957    140    -71    366       O  
ATOM   3309  CB  HIS A 432       8.901  18.793  13.960  1.00 36.63           C  
ANISOU 3309  CB  HIS A 432     3829   5534   4554     93    -41    399       C  
ATOM   3310  CG  HIS A 432       8.604  20.010  14.772  1.00 42.26           C  
ANISOU 3310  CG  HIS A 432     4538   6266   5255    213    -31    398       C  
ATOM   3311  ND1 HIS A 432       7.557  20.861  14.485  1.00 44.92           N  
ANISOU 3311  ND1 HIS A 432     4809   6694   5562    293    -39    411       N  
ATOM   3312  CD2 HIS A 432       9.248  20.554  15.834  1.00 41.78           C  
ANISOU 3312  CD2 HIS A 432     4536   6137   5204    272    -17    382       C  
ATOM   3313  CE1 HIS A 432       7.545  21.854  15.355  1.00 41.58           C  
ANISOU 3313  CE1 HIS A 432     4410   6258   5130    400    -27    403       C  
ATOM   3314  NE2 HIS A 432       8.567  21.696  16.179  1.00 44.41           N  
ANISOU 3314  NE2 HIS A 432     4845   6518   5512    386    -16    384       N  
ATOM   3315  N   ARG A 433      10.446  21.371  12.386  1.00 41.74           N  
ANISOU 3315  N   ARG A 433     4601   6017   5242    245    -99    388       N  
ATOM   3316  CA  ARG A 433      11.372  22.472  12.539  1.00 41.81           C  
ANISOU 3316  CA  ARG A 433     4687   5926   5271    311   -110    380       C  
ATOM   3317  C   ARG A 433      11.057  23.239  13.834  1.00 43.58           C  
ANISOU 3317  C   ARG A 433     4919   6155   5482    400    -95    371       C  
ATOM   3318  O   ARG A 433       9.948  23.739  13.992  1.00 45.97           O  
ANISOU 3318  O   ARG A 433     5168   6544   5754    470    -92    380       O  
ATOM   3319  CB  ARG A 433      11.230  23.380  11.320  1.00 40.46           C  
ANISOU 3319  CB  ARG A 433     4523   5754   5095    354   -141    395       C  
ATOM   3320  CG  ARG A 433      12.079  24.597  11.333  1.00 41.32           C  
ANISOU 3320  CG  ARG A 433     4715   5764   5222    416   -158    392       C  
ATOM   3321  CD  ARG A 433      11.755  25.464  10.140  1.00 43.41           C  
ANISOU 3321  CD  ARG A 433     4981   6039   5473    461   -187    413       C  
ATOM   3322  NE  ARG A 433      12.936  26.205   9.726  1.00 52.74           N  
ANISOU 3322  NE  ARG A 433     6250   7109   6680    462   -205    416       N  
ATOM   3323  CZ  ARG A 433      13.253  27.404  10.170  1.00 56.51           C  
ANISOU 3323  CZ  ARG A 433     6793   7517   7162    535   -219    415       C  
ATOM   3324  NH1 ARG A 433      12.466  28.013  11.036  1.00 62.31           N  
ANISOU 3324  NH1 ARG A 433     7520   8281   7875    624   -215    407       N  
ATOM   3325  NH2 ARG A 433      14.354  27.985   9.746  1.00 60.85           N  
ANISOU 3325  NH2 ARG A 433     7417   7970   7734    517   -236    422       N  
ATOM   3326  N   ALA A 434      12.007  23.306  14.768  1.00 40.59           N  
ANISOU 3326  N   ALA A 434     4607   5693   5124    402    -87    353       N  
ATOM   3327  CA  ALA A 434      11.753  24.011  16.016  1.00 37.90           C  
ANISOU 3327  CA  ALA A 434     4283   5352   4766    487    -74    341       C  
ATOM   3328  C   ALA A 434      11.229  25.398  15.728  1.00 40.00           C  
ANISOU 3328  C   ALA A 434     4562   5624   5014    596    -94    345       C  
ATOM   3329  O   ALA A 434      11.780  26.105  14.879  1.00 38.70           O  
ANISOU 3329  O   ALA A 434     4446   5392   4865    608   -123    351       O  
ATOM   3330  CB  ALA A 434      12.994  24.119  16.836  1.00 30.97           C  
ANISOU 3330  CB  ALA A 434     3488   4368   3913    477    -75    320       C  
ATOM   3331  N   SER A 435      10.185  25.797  16.452  1.00 38.98           N  
ANISOU 3331  N   SER A 435     4391   5574   4847    680    -77    344       N  
ATOM   3332  CA  SER A 435       9.649  27.159  16.335  1.00 36.24           C  
ANISOU 3332  CA  SER A 435     4065   5230   4476    805    -95    345       C  
ATOM   3333  C   SER A 435      10.702  28.195  16.739  1.00 45.83           C  
ANISOU 3333  C   SER A 435     5400   6306   5708    851   -118    325       C  
ATOM   3334  O   SER A 435      10.583  29.362  16.406  1.00 51.88           O  
ANISOU 3334  O   SER A 435     6216   7033   6464    937   -144    327       O  
ATOM   3335  CB  SER A 435       8.439  27.324  17.235  1.00 35.18           C  
ANISOU 3335  CB  SER A 435     3868   5207   4294    893    -66    344       C  
ATOM   3336  OG  SER A 435       8.838  27.221  18.581  1.00 39.31           O  
ANISOU 3336  OG  SER A 435     4431   5694   4811    904    -44    321       O  
ATOM   3337  N   THR A 436      11.741  27.750  17.439  1.00 45.21           N  
ANISOU 3337  N   THR A 436     5372   6152   5655    790   -112    308       N  
ATOM   3338  CA  THR A 436      12.759  28.636  17.984  1.00 43.14           C  
ANISOU 3338  CA  THR A 436     5219   5765   5407    820   -135    287       C  
ATOM   3339  C   THR A 436      14.036  28.661  17.142  1.00 45.77           C  
ANISOU 3339  C   THR A 436     5607   5999   5785    739   -163    295       C  
ATOM   3340  O   THR A 436      15.055  29.179  17.581  1.00 47.44           O  
ANISOU 3340  O   THR A 436     5901   6110   6014    733   -182    281       O  
ATOM   3341  CB  THR A 436      13.143  28.164  19.392  1.00 46.18           C  
ANISOU 3341  CB  THR A 436     5623   6136   5788    807   -113    263       C  
ATOM   3342  OG1 THR A 436      13.625  26.822  19.319  1.00 48.14           O  
ANISOU 3342  OG1 THR A 436     5832   6399   6060    694    -95    270       O  
ATOM   3343  CG2 THR A 436      11.904  28.182  20.312  1.00 52.78           C  
ANISOU 3343  CG2 THR A 436     6407   7075   6573    891    -80    257       C  
ATOM   3344  N   LEU A 437      13.983  28.068  15.951  1.00 46.06           N  
ANISOU 3344  N   LEU A 437     5595   6071   5836    675   -164    317       N  
ATOM   3345  CA  LEU A 437      15.146  27.923  15.082  1.00 46.79           C  
ANISOU 3345  CA  LEU A 437     5724   6090   5965    595   -183    327       C  
ATOM   3346  C   LEU A 437      15.596  29.293  14.573  1.00 49.36           C  
ANISOU 3346  C   LEU A 437     6129   6329   6296    640   -219    336       C  
ATOM   3347  O   LEU A 437      14.747  30.100  14.154  1.00 46.29           O  
ANISOU 3347  O   LEU A 437     5741   5965   5882    719   -232    348       O  
ATOM   3348  CB  LEU A 437      14.768  27.050  13.886  1.00 47.78           C  
ANISOU 3348  CB  LEU A 437     5779   6284   6092    534   -176    348       C  
ATOM   3349  CG  LEU A 437      15.876  26.178  13.287  1.00 56.21           C  
ANISOU 3349  CG  LEU A 437     6854   7312   7191    430   -174    351       C  
ATOM   3350  CD1 LEU A 437      16.372  25.190  14.313  1.00 50.55           C  
ANISOU 3350  CD1 LEU A 437     6133   6586   6486    382   -151    331       C  
ATOM   3351  CD2 LEU A 437      15.361  25.435  12.067  1.00 59.80           C  
ANISOU 3351  CD2 LEU A 437     7249   7835   7638    383   -171    367       C  
ATOM   3352  N   THR A 438      16.909  29.553  14.597  1.00 45.25           N  
ANISOU 3352  N   THR A 438     5676   5711   5805    590   -237    334       N  
ATOM   3353  CA  THR A 438      17.452  30.853  14.177  1.00 48.08           C  
ANISOU 3353  CA  THR A 438     6121   5978   6170    615   -274    345       C  
ATOM   3354  C   THR A 438      18.028  30.810  12.759  1.00 57.99           C  
ANISOU 3354  C   THR A 438     7374   7217   7444    550   -286    376       C  
ATOM   3355  O   THR A 438      18.367  31.849  12.203  1.00 58.60           O  
ANISOU 3355  O   THR A 438     7516   7227   7521    565   -315    395       O  
ATOM   3356  CB  THR A 438      18.547  31.408  15.159  1.00 54.40           C  
ANISOU 3356  CB  THR A 438     7007   6675   6987    602   -294    325       C  
ATOM   3357  OG1 THR A 438      19.642  30.484  15.269  1.00 57.75           O  
ANISOU 3357  OG1 THR A 438     7412   7089   7443    505   -283    322       O  
ATOM   3358  CG2 THR A 438      17.972  31.651  16.558  1.00 52.28           C  
ANISOU 3358  CG2 THR A 438     6758   6414   6692    680   -286    293       C  
ATOM   3359  N   TRP A 439      18.169  29.608  12.190  1.00 63.07           N  
ANISOU 3359  N   TRP A 439     7950   7917   8098    478   -263    382       N  
ATOM   3360  CA  TRP A 439      18.551  29.451  10.774  1.00 57.14           C  
ANISOU 3360  CA  TRP A 439     7186   7170   7354    424   -268    410       C  
ATOM   3361  C   TRP A 439      17.336  29.827   9.924  1.00 48.78           C  
ANISOU 3361  C   TRP A 439     6097   6171   6264    482   -277    429       C  
ATOM   3362  O   TRP A 439      16.235  29.795  10.414  1.00 52.18           O  
ANISOU 3362  O   TRP A 439     6491   6664   6672    544   -269    419       O  
ATOM   3363  CB  TRP A 439      19.007  28.016  10.456  1.00 45.71           C  
ANISOU 3363  CB  TRP A 439     5682   5765   5921    339   -242    405       C  
ATOM   3364  CG  TRP A 439      20.220  27.575  11.174  1.00 39.19           C  
ANISOU 3364  CG  TRP A 439     4879   4890   5124    286   -235    390       C  
ATOM   3365  CD1 TRP A 439      20.276  26.735  12.251  1.00 45.74           C  
ANISOU 3365  CD1 TRP A 439     5687   5734   5958    274   -215    365       C  
ATOM   3366  CD2 TRP A 439      21.580  27.926  10.875  1.00 39.28           C  
ANISOU 3366  CD2 TRP A 439     4932   4833   5159    236   -248    402       C  
ATOM   3367  NE1 TRP A 439      21.590  26.571  12.665  1.00 39.35           N  
ANISOU 3367  NE1 TRP A 439     4907   4869   5175    227   -218    359       N  
ATOM   3368  CE2 TRP A 439      22.404  27.274  11.825  1.00 36.68           C  
ANISOU 3368  CE2 TRP A 439     4603   4486   4850    201   -237    381       C  
ATOM   3369  CE3 TRP A 439      22.181  28.716   9.895  1.00 36.18           C  
ANISOU 3369  CE3 TRP A 439     4575   4401   4771    216   -267    432       C  
ATOM   3370  CZ2 TRP A 439      23.790  27.392  11.818  1.00 43.23           C  
ANISOU 3370  CZ2 TRP A 439     5457   5265   5703    149   -246    388       C  
ATOM   3371  CZ3 TRP A 439      23.559  28.832   9.889  1.00 39.48           C  
ANISOU 3371  CZ3 TRP A 439     5019   4769   5213    157   -273    440       C  
ATOM   3372  CH2 TRP A 439      24.353  28.179  10.846  1.00 45.52           C  
ANISOU 3372  CH2 TRP A 439     5775   5523   5997    125   -263    418       C  
ATOM   3373  N   PRO A 440      17.544  30.228   8.657  1.00 47.88           N  
ANISOU 3373  N   PRO A 440     6000   6045   6147    465   -293    459       N  
ATOM   3374  CA  PRO A 440      16.446  30.637   7.764  1.00 36.79           C  
ANISOU 3374  CA  PRO A 440     4571   4697   4710    522   -307    481       C  
ATOM   3375  C   PRO A 440      15.584  29.468   7.295  1.00 41.34           C  
ANISOU 3375  C   PRO A 440     5051   5386   5270    496   -288    478       C  
ATOM   3376  O   PRO A 440      16.015  28.321   7.356  1.00 44.68           O  
ANISOU 3376  O   PRO A 440     5439   5829   5707    420   -266    464       O  
ATOM   3377  CB  PRO A 440      17.185  31.220   6.554  1.00 35.97           C  
ANISOU 3377  CB  PRO A 440     4517   4541   4610    487   -327    515       C  
ATOM   3378  CG  PRO A 440      18.538  30.529   6.574  1.00 42.14           C  
ANISOU 3378  CG  PRO A 440     5304   5285   5424    389   -310    509       C  
ATOM   3379  CD  PRO A 440      18.862  30.476   8.044  1.00 43.02           C  
ANISOU 3379  CD  PRO A 440     5433   5357   5554    397   -303    478       C  
ATOM   3380  N   LEU A 441      14.394  29.763   6.799  1.00 39.07           N  
ANISOU 3380  N   LEU A 441     4725   5170   4950    558   -300    491       N  
ATOM   3381  CA  LEU A 441      13.441  28.739   6.429  1.00 41.52           C  
ANISOU 3381  CA  LEU A 441     4941   5595   5240    534   -288    489       C  
ATOM   3382  C   LEU A 441      13.922  27.818   5.332  1.00 50.25           C  
ANISOU 3382  C   LEU A 441     6027   6718   6350    440   -284    496       C  
ATOM   3383  O   LEU A 441      13.527  26.658   5.276  1.00 52.41           O  
ANISOU 3383  O   LEU A 441     6237   7059   6616    386   -269    483       O  
ATOM   3384  CB  LEU A 441      12.161  29.385   5.935  1.00 42.20           C  
ANISOU 3384  CB  LEU A 441     4991   5756   5287    621   -308    508       C  
ATOM   3385  CG  LEU A 441      11.366  30.099   7.014  1.00 62.75           C  
ANISOU 3385  CG  LEU A 441     7591   8377   7874    727   -307    498       C  
ATOM   3386  CD1 LEU A 441      10.086  30.664   6.398  1.00 71.85           C  
ANISOU 3386  CD1 LEU A 441     8697   9617   8985    817   -328    520       C  
ATOM   3387  CD2 LEU A 441      11.048  29.153   8.174  1.00 62.20           C  
ANISOU 3387  CD2 LEU A 441     7462   8362   7809    702   -273    470       C  
ATOM   3388  N   TRP A 442      14.717  28.340   4.409  1.00 49.86           N  
ANISOU 3388  N   TRP A 442     6031   6609   6304    421   -299    517       N  
ATOM   3389  CA  TRP A 442      15.052  27.538   3.250  1.00 44.33           C  
ANISOU 3389  CA  TRP A 442     5312   5936   5596    347   -296    525       C  
ATOM   3390  C   TRP A 442      15.883  26.318   3.727  1.00 44.04           C  
ANISOU 3390  C   TRP A 442     5266   5882   5586    265   -267    497       C  
ATOM   3391  O   TRP A 442      15.840  25.267   3.106  1.00 37.25           O  
ANISOU 3391  O   TRP A 442     4373   5066   4715    206   -258    489       O  
ATOM   3392  CB  TRP A 442      15.730  28.379   2.134  1.00 37.41           C  
ANISOU 3392  CB  TRP A 442     4495   5007   4713    346   -314    558       C  
ATOM   3393  CG  TRP A 442      17.128  28.800   2.437  1.00 34.68           C  
ANISOU 3393  CG  TRP A 442     4217   4562   4400    313   -307    562       C  
ATOM   3394  CD1 TRP A 442      17.550  30.033   2.883  1.00 41.73           C  
ANISOU 3394  CD1 TRP A 442     5180   5372   5305    354   -324    577       C  
ATOM   3395  CD2 TRP A 442      18.299  27.981   2.366  1.00 38.75           C  
ANISOU 3395  CD2 TRP A 442     4736   5052   4937    233   -284    551       C  
ATOM   3396  NE1 TRP A 442      18.917  30.023   3.085  1.00 40.92           N  
ANISOU 3396  NE1 TRP A 442     5117   5200   5232    293   -313    577       N  
ATOM   3397  CE2 TRP A 442      19.397  28.775   2.775  1.00 39.08           C  
ANISOU 3397  CE2 TRP A 442     4839   5005   5004    224   -287    562       C  
ATOM   3398  CE3 TRP A 442      18.530  26.654   1.989  1.00 37.83           C  
ANISOU 3398  CE3 TRP A 442     4578   4978   4817    169   -262    533       C  
ATOM   3399  CZ2 TRP A 442      20.696  28.285   2.804  1.00 41.32           C  
ANISOU 3399  CZ2 TRP A 442     5133   5256   5312    156   -268    558       C  
ATOM   3400  CZ3 TRP A 442      19.834  26.172   2.021  1.00 31.58           C  
ANISOU 3400  CZ3 TRP A 442     3805   4145   4047    112   -241    526       C  
ATOM   3401  CH2 TRP A 442      20.890  26.976   2.435  1.00 37.87           C  
ANISOU 3401  CH2 TRP A 442     4652   4868   4871    107   -243    540       C  
ATOM   3402  N   MET A 443      16.593  26.452   4.853  1.00 40.96           N  
ANISOU 3402  N   MET A 443     4908   5430   5226    266   -254    481       N  
ATOM   3403  CA  MET A 443      17.370  25.337   5.389  1.00 39.36           C  
ANISOU 3403  CA  MET A 443     4700   5210   5046    200   -228    457       C  
ATOM   3404  C   MET A 443      16.489  24.215   5.923  1.00 37.09           C  
ANISOU 3404  C   MET A 443     4352   4993   4749    181   -213    435       C  
ATOM   3405  O   MET A 443      16.984  23.125   6.218  1.00 31.17           O  
ANISOU 3405  O   MET A 443     3597   4237   4011    124   -194    416       O  
ATOM   3406  CB  MET A 443      18.366  25.784   6.462  1.00 41.30           C  
ANISOU 3406  CB  MET A 443     4994   5375   5323    205   -223    447       C  
ATOM   3407  CG  MET A 443      19.347  26.860   5.980  1.00 47.26           C  
ANISOU 3407  CG  MET A 443     5811   6056   6090    206   -240    471       C  
ATOM   3408  SD  MET A 443      20.767  27.017   7.067  1.00 49.09           S  
ANISOU 3408  SD  MET A 443     6089   6203   6360    178   -235    459       S  
ATOM   3409  CE  MET A 443      21.389  28.611   6.563  1.00199.01           C  
ANISOU 3409  CE  MET A 443    25149  25114  25351    192   -265    494       C  
ATOM   3410  N   GLY A 444      15.182  24.448   6.015  1.00 34.14           N  
ANISOU 3410  N   GLY A 444     3931   4690   4349    227   -222    440       N  
ATOM   3411  CA  GLY A 444      14.273  23.374   6.404  1.00 26.55           C  
ANISOU 3411  CA  GLY A 444     2905   3808   3374    196   -209    426       C  
ATOM   3412  C   GLY A 444      14.485  22.886   7.833  1.00 34.53           C  
ANISOU 3412  C   GLY A 444     3918   4798   4403    187   -184    405       C  
ATOM   3413  O   GLY A 444      14.517  23.693   8.771  1.00 32.05           O  
ANISOU 3413  O   GLY A 444     3627   4455   4097    248   -183    402       O  
ATOM   3414  N   VAL A 445      14.624  21.564   7.998  1.00 33.56           N  
ANISOU 3414  N   VAL A 445     3780   4689   4284    113   -167    390       N  
ATOM   3415  CA  VAL A 445      14.877  20.958   9.305  1.00 36.22           C  
ANISOU 3415  CA  VAL A 445     4123   5005   4635     97   -144    372       C  
ATOM   3416  C   VAL A 445      16.308  20.489   9.295  1.00 34.04           C  
ANISOU 3416  C   VAL A 445     3903   4646   4386     55   -137    361       C  
ATOM   3417  O   VAL A 445      16.598  19.397   8.817  1.00 35.41           O  
ANISOU 3417  O   VAL A 445     4078   4818   4557     -9   -130    353       O  
ATOM   3418  CB  VAL A 445      13.974  19.709   9.597  1.00 30.94           C  
ANISOU 3418  CB  VAL A 445     3401   4410   3947     40   -130    367       C  
ATOM   3419  CG1 VAL A 445      14.341  19.121  10.943  1.00 27.77           C  
ANISOU 3419  CG1 VAL A 445     3016   3977   3557     24   -106    353       C  
ATOM   3420  CG2 VAL A 445      12.467  20.056   9.541  1.00 34.49           C  
ANISOU 3420  CG2 VAL A 445     3775   4966   4364     74   -137    382       C  
ATOM   3421  N   PRO A 446      17.221  21.313   9.813  1.00 33.24           N  
ANISOU 3421  N   PRO A 446     3848   4475   4307     90   -139    359       N  
ATOM   3422  CA  PRO A 446      18.607  21.037   9.494  1.00 25.30           C  
ANISOU 3422  CA  PRO A 446     2884   3403   3324     54   -137    355       C  
ATOM   3423  C   PRO A 446      19.228  19.997  10.415  1.00 27.86           C  
ANISOU 3423  C   PRO A 446     3222   3701   3662     19   -118    336       C  
ATOM   3424  O   PRO A 446      18.704  19.644  11.464  1.00 28.05           O  
ANISOU 3424  O   PRO A 446     3233   3744   3682     25   -107    328       O  
ATOM   3425  CB  PRO A 446      19.303  22.408   9.723  1.00 29.85           C  
ANISOU 3425  CB  PRO A 446     3504   3919   3917    100   -152    365       C  
ATOM   3426  CG  PRO A 446      18.202  23.403   9.907  1.00 28.59           C  
ANISOU 3426  CG  PRO A 446     3332   3791   3741    166   -165    374       C  
ATOM   3427  CD  PRO A 446      17.077  22.604  10.505  1.00 36.74           C  
ANISOU 3427  CD  PRO A 446     4311   4896   4754    165   -149    363       C  
ATOM   3428  N   HIS A 447      20.371  19.503   9.968  1.00 31.72           N  
ANISOU 3428  N   HIS A 447     3737   4149   4164    -15   -113    333       N  
ATOM   3429  CA  HIS A 447      21.166  18.514  10.671  1.00 34.74           C  
ANISOU 3429  CA  HIS A 447     4141   4501   4560    -43    -98    317       C  
ATOM   3430  C   HIS A 447      21.402  18.955  12.120  1.00 37.49           C  
ANISOU 3430  C   HIS A 447     4503   4819   4922    -11    -98    310       C  
ATOM   3431  O   HIS A 447      21.825  20.098  12.367  1.00 36.56           O  
ANISOU 3431  O   HIS A 447     4404   4670   4817     23   -112    316       O  
ATOM   3432  CB  HIS A 447      22.507  18.441   9.929  1.00 34.37           C  
ANISOU 3432  CB  HIS A 447     4118   4416   4527    -59    -97    319       C  
ATOM   3433  CG  HIS A 447      23.471  17.469  10.500  1.00 34.56           C  
ANISOU 3433  CG  HIS A 447     4163   4408   4561    -77    -84    304       C  
ATOM   3434  ND1 HIS A 447      23.426  16.122  10.211  1.00 39.54           N  
ANISOU 3434  ND1 HIS A 447     4801   5045   5178   -110    -71    291       N  
ATOM   3435  CD2 HIS A 447      24.541  17.649  11.309  1.00 36.94           C  
ANISOU 3435  CD2 HIS A 447     4483   4670   4885    -65    -85    302       C  
ATOM   3436  CE1 HIS A 447      24.436  15.510  10.812  1.00 38.58           C  
ANISOU 3436  CE1 HIS A 447     4703   4888   5069   -109    -62    281       C  
ATOM   3437  NE2 HIS A 447      25.126  16.416  11.485  1.00 40.53           N  
ANISOU 3437  NE2 HIS A 447     4951   5111   5337    -83    -71    288       N  
ATOM   3438  N   GLY A 448      21.159  18.053  13.072  1.00 31.55           N  
ANISOU 3438  N   GLY A 448     3749   4073   4164    -26    -83    299       N  
ATOM   3439  CA  GLY A 448      21.446  18.348  14.472  1.00 31.02           C  
ANISOU 3439  CA  GLY A 448     3701   3980   4105      3    -82    291       C  
ATOM   3440  C   GLY A 448      20.278  18.922  15.250  1.00 34.72           C  
ANISOU 3440  C   GLY A 448     4149   4488   4555     42    -79    292       C  
ATOM   3441  O   GLY A 448      20.345  18.991  16.466  1.00 34.46           O  
ANISOU 3441  O   GLY A 448     4130   4443   4520     64    -74    284       O  
ATOM   3442  N   TYR A 449      19.207  19.321  14.566  1.00 29.50           N  
ANISOU 3442  N   TYR A 449     3452   3879   3878     56    -83    302       N  
ATOM   3443  CA  TYR A 449      18.110  20.033  15.239  1.00 36.10           C  
ANISOU 3443  CA  TYR A 449     4263   4760   4692    109    -80    304       C  
ATOM   3444  C   TYR A 449      16.958  19.123  15.722  1.00 38.74           C  
ANISOU 3444  C   TYR A 449     4550   5169   5001     86    -58    307       C  
ATOM   3445  O   TYR A 449      15.888  19.593  16.106  1.00 35.98           O  
ANISOU 3445  O   TYR A 449     4163   4880   4627    129    -52    313       O  
ATOM   3446  CB  TYR A 449      17.664  21.301  14.443  1.00 29.22           C  
ANISOU 3446  CB  TYR A 449     3386   3900   3816    160   -100    316       C  
ATOM   3447  CG  TYR A 449      18.779  22.343  14.543  1.00 32.47           C  
ANISOU 3447  CG  TYR A 449     3857   4230   4251    188   -121    313       C  
ATOM   3448  CD1 TYR A 449      19.855  22.312  13.669  1.00 30.15           C  
ANISOU 3448  CD1 TYR A 449     3586   3890   3979    149   -131    320       C  
ATOM   3449  CD2 TYR A 449      18.806  23.286  15.584  1.00 32.46           C  
ANISOU 3449  CD2 TYR A 449     3890   4197   4246    247   -129    303       C  
ATOM   3450  CE1 TYR A 449      20.928  23.225  13.790  1.00 30.20           C  
ANISOU 3450  CE1 TYR A 449     3643   3827   4006    160   -151    321       C  
ATOM   3451  CE2 TYR A 449      19.873  24.200  15.720  1.00 30.47           C  
ANISOU 3451  CE2 TYR A 449     3698   3865   4015    258   -153    301       C  
ATOM   3452  CZ  TYR A 449      20.926  24.154  14.826  1.00 31.79           C  
ANISOU 3452  CZ  TYR A 449     3881   3993   4206    210   -164    312       C  
ATOM   3453  OH  TYR A 449      21.990  25.019  14.946  1.00 38.64           O  
ANISOU 3453  OH  TYR A 449     4800   4789   5093    208   -188    314       O  
ATOM   3454  N   GLU A 450      17.201  17.816  15.742  1.00 33.41           N  
ANISOU 3454  N   GLU A 450     3878   4489   4326     20    -46    305       N  
ATOM   3455  CA  GLU A 450      16.285  16.908  16.430  1.00 33.44           C  
ANISOU 3455  CA  GLU A 450     3849   4550   4306    -13    -24    310       C  
ATOM   3456  C   GLU A 450      16.740  16.686  17.875  1.00 34.31           C  
ANISOU 3456  C   GLU A 450     3992   4628   4416      0    -10    303       C  
ATOM   3457  O   GLU A 450      15.931  16.411  18.743  1.00 33.60           O  
ANISOU 3457  O   GLU A 450     3876   4590   4301      1     10    309       O  
ATOM   3458  CB  GLU A 450      16.150  15.564  15.696  1.00 29.67           C  
ANISOU 3458  CB  GLU A 450     3367   4083   3823    -98    -22    313       C  
ATOM   3459  CG  GLU A 450      17.181  14.523  16.061  1.00 25.78           C  
ANISOU 3459  CG  GLU A 450     2931   3520   3343   -139    -16    303       C  
ATOM   3460  CD  GLU A 450      18.599  14.770  15.467  1.00 35.42           C  
ANISOU 3460  CD  GLU A 450     4198   4666   4593   -123    -30    292       C  
ATOM   3461  OE1 GLU A 450      18.930  15.922  15.069  1.00 29.53           O  
ANISOU 3461  OE1 GLU A 450     3450   3909   3861    -77    -43    292       O  
ATOM   3462  OE2 GLU A 450      19.370  13.774  15.373  1.00 32.48           O  
ANISOU 3462  OE2 GLU A 450     3866   4249   4227   -159    -27    284       O  
ATOM   3463  N   ILE A 451      18.039  16.845  18.130  1.00 34.18           N  
ANISOU 3463  N   ILE A 451     4030   4533   4424     12    -20    290       N  
ATOM   3464  CA  ILE A 451      18.615  16.493  19.424  1.00 32.39           C  
ANISOU 3464  CA  ILE A 451     3839   4271   4196     19    -11    283       C  
ATOM   3465  C   ILE A 451      17.906  17.163  20.601  1.00 31.31           C  
ANISOU 3465  C   ILE A 451     3690   4171   4034     73      1    282       C  
ATOM   3466  O   ILE A 451      17.606  16.516  21.581  1.00 32.42           O  
ANISOU 3466  O   ILE A 451     3832   4332   4155     61     21    286       O  
ATOM   3467  CB  ILE A 451      20.119  16.882  19.488  1.00 28.88           C  
ANISOU 3467  CB  ILE A 451     3445   3746   3781     35    -31    271       C  
ATOM   3468  CG1 ILE A 451      20.884  16.162  18.382  1.00 25.68           C  
ANISOU 3468  CG1 ILE A 451     3052   3311   3396    -11    -36    272       C  
ATOM   3469  CG2 ILE A 451      20.669  16.529  20.835  1.00 26.43           C  
ANISOU 3469  CG2 ILE A 451     3169   3406   3466     45    -25    264       C  
ATOM   3470  CD1 ILE A 451      22.338  16.636  18.263  1.00 24.96           C  
ANISOU 3470  CD1 ILE A 451     2993   3159   3332      5    -55    265       C  
ATOM   3471  N   GLU A 452      17.660  18.467  20.506  1.00 31.06           N  
ANISOU 3471  N   GLU A 452     3655   4146   4002    138    -12    277       N  
ATOM   3472  CA  GLU A 452      17.024  19.205  21.584  1.00 24.51           C  
ANISOU 3472  CA  GLU A 452     2822   3348   3145    205     -2    271       C  
ATOM   3473  C   GLU A 452      15.610  18.621  21.895  1.00 34.77           C  
ANISOU 3473  C   GLU A 452     4055   4749   4406    194     30    287       C  
ATOM   3474  O   GLU A 452      15.101  18.750  23.019  1.00 33.65           O  
ANISOU 3474  O   GLU A 452     3908   4645   4234    231     50    286       O  
ATOM   3475  CB  GLU A 452      16.981  20.713  21.225  1.00 30.64           C  
ANISOU 3475  CB  GLU A 452     3612   4104   3924    278    -25    263       C  
ATOM   3476  CG  GLU A 452      15.971  21.070  20.098  1.00 37.82           C  
ANISOU 3476  CG  GLU A 452     4468   5077   4826    291    -27    278       C  
ATOM   3477  CD  GLU A 452      16.343  22.327  19.328  1.00 42.46           C  
ANISOU 3477  CD  GLU A 452     5088   5615   5429    337    -58    276       C  
ATOM   3478  OE1 GLU A 452      15.520  23.267  19.234  1.00 44.08           O  
ANISOU 3478  OE1 GLU A 452     5280   5855   5614    408    -63    278       O  
ATOM   3479  OE2 GLU A 452      17.467  22.400  18.816  1.00 39.51           O  
ANISOU 3479  OE2 GLU A 452     4755   5170   5087    303    -78    274       O  
ATOM   3480  N   PHE A 453      14.978  17.958  20.930  1.00 25.97           N  
ANISOU 3480  N   PHE A 453     2892   3684   3291    138     34    304       N  
ATOM   3481  CA  PHE A 453      13.683  17.329  21.258  1.00 30.34           C  
ANISOU 3481  CA  PHE A 453     3379   4340   3808    112     62    323       C  
ATOM   3482  C   PHE A 453      13.826  15.963  21.947  1.00 35.86           C  
ANISOU 3482  C   PHE A 453     4093   5033   4499     36     83    332       C  
ATOM   3483  O   PHE A 453      13.049  15.646  22.865  1.00 33.24           O  
ANISOU 3483  O   PHE A 453     3730   4767   4132     33    111    346       O  
ATOM   3484  CB  PHE A 453      12.780  17.199  20.033  1.00 30.22           C  
ANISOU 3484  CB  PHE A 453     3300   4395   3789     80     56    338       C  
ATOM   3485  CG  PHE A 453      12.319  18.507  19.506  1.00 33.80           C  
ANISOU 3485  CG  PHE A 453     3727   4877   4237    163     41    336       C  
ATOM   3486  CD1 PHE A 453      11.126  19.067  19.950  1.00 33.72           C  
ANISOU 3486  CD1 PHE A 453     3655   4966   4190    225     58    345       C  
ATOM   3487  CD2 PHE A 453      13.088  19.205  18.588  1.00 30.60           C  
ANISOU 3487  CD2 PHE A 453     3363   4403   3862    184     11    326       C  
ATOM   3488  CE1 PHE A 453      10.741  20.292  19.499  1.00 36.64           C  
ANISOU 3488  CE1 PHE A 453     4012   5355   4554    313     42    343       C  
ATOM   3489  CE2 PHE A 453      12.681  20.425  18.121  1.00 33.74           C  
ANISOU 3489  CE2 PHE A 453     3749   4818   4253    262     -5    327       C  
ATOM   3490  CZ  PHE A 453      11.502  20.965  18.582  1.00 34.30           C  
ANISOU 3490  CZ  PHE A 453     3764   4979   4287    330      9    334       C  
ATOM   3491  N   ILE A 454      14.804  15.167  21.497  1.00 30.46           N  
ANISOU 3491  N   ILE A 454     3458   4272   3842    -22     69    327       N  
ATOM   3492  CA  ILE A 454      15.083  13.875  22.087  1.00 25.47           C  
ANISOU 3492  CA  ILE A 454     2859   3615   3204    -88     83    335       C  
ATOM   3493  C   ILE A 454      15.463  14.058  23.549  1.00 32.46           C  
ANISOU 3493  C   ILE A 454     3780   4480   4075    -45     96    331       C  
ATOM   3494  O   ILE A 454      15.062  13.263  24.400  1.00 33.96           O  
ANISOU 3494  O   ILE A 454     3969   4697   4237    -80    120    347       O  
ATOM   3495  CB  ILE A 454      16.242  13.197  21.354  1.00 35.93           C  
ANISOU 3495  CB  ILE A 454     4240   4852   4561   -130     63    325       C  
ATOM   3496  CG1 ILE A 454      15.959  13.132  19.840  1.00 35.20           C  
ANISOU 3496  CG1 ILE A 454     4121   4775   4480   -164     47    325       C  
ATOM   3497  CG2 ILE A 454      16.564  11.801  21.959  1.00 29.36           C  
ANISOU 3497  CG2 ILE A 454     3454   3983   3718   -192     74    334       C  
ATOM   3498  CD1 ILE A 454      14.811  12.253  19.522  1.00 40.89           C  
ANISOU 3498  CD1 ILE A 454     4798   5563   5174   -239     57    344       C  
ATOM   3499  N   PHE A 455      16.214  15.120  23.855  1.00 30.89           N  
ANISOU 3499  N   PHE A 455     3612   4233   3890     29     80    310       N  
ATOM   3500  CA  PHE A 455      16.635  15.357  25.238  1.00 30.08           C  
ANISOU 3500  CA  PHE A 455     3550   4108   3771     73     87    301       C  
ATOM   3501  C   PHE A 455      15.596  16.093  26.071  1.00 33.26           C  
ANISOU 3501  C   PHE A 455     3916   4588   4132    135    109    303       C  
ATOM   3502  O   PHE A 455      15.770  16.264  27.274  1.00 36.52           O  
ANISOU 3502  O   PHE A 455     4359   4995   4520    173    119    296       O  
ATOM   3503  CB  PHE A 455      17.966  16.115  25.317  1.00 26.87           C  
ANISOU 3503  CB  PHE A 455     3201   3615   3394    116     55    277       C  
ATOM   3504  CG  PHE A 455      19.159  15.241  25.158  1.00 25.18           C  
ANISOU 3504  CG  PHE A 455     3032   3329   3206     71     41    275       C  
ATOM   3505  CD1 PHE A 455      19.556  14.806  23.892  1.00 22.64           C  
ANISOU 3505  CD1 PHE A 455     2706   2982   2913     27     29    278       C  
ATOM   3506  CD2 PHE A 455      19.894  14.848  26.267  1.00 26.35           C  
ANISOU 3506  CD2 PHE A 455     3227   3439   3345     77     39    272       C  
ATOM   3507  CE1 PHE A 455      20.700  13.976  23.748  1.00 24.23           C  
ANISOU 3507  CE1 PHE A 455     2950   3121   3136     -3     18    275       C  
ATOM   3508  CE2 PHE A 455      21.045  14.034  26.137  1.00 26.93           C  
ANISOU 3508  CE2 PHE A 455     3341   3450   3440     47     25    271       C  
ATOM   3509  CZ  PHE A 455      21.435  13.595  24.861  1.00 28.05           C  
ANISOU 3509  CZ  PHE A 455     3478   3569   3612      9     15    272       C  
ATOM   3510  N   GLY A 456      14.531  16.541  25.421  1.00 31.09           N  
ANISOU 3510  N   GLY A 456     3577   4389   3847    150    117    312       N  
ATOM   3511  CA  GLY A 456      13.398  17.116  26.113  1.00 29.88           C  
ANISOU 3511  CA  GLY A 456     3376   4329   3649    210    144    317       C  
ATOM   3512  C   GLY A 456      13.604  18.537  26.580  1.00 34.62           C  
ANISOU 3512  C   GLY A 456     4009   4904   4241    319    131    291       C  
ATOM   3513  O   GLY A 456      13.000  18.925  27.574  1.00 38.70           O  
ANISOU 3513  O   GLY A 456     4515   5475   4715    380    155    288       O  
ATOM   3514  N   LEU A 457      14.446  19.323  25.900  1.00 31.63           N  
ANISOU 3514  N   LEU A 457     3674   4443   3899    345     93    271       N  
ATOM   3515  CA  LEU A 457      14.518  20.757  26.228  1.00 35.85           C  
ANISOU 3515  CA  LEU A 457     4245   4952   4424    446     76    247       C  
ATOM   3516  C   LEU A 457      13.161  21.510  26.174  1.00 41.49           C  
ANISOU 3516  C   LEU A 457     4901   5762   5100    526     95    252       C  
ATOM   3517  O   LEU A 457      12.935  22.438  26.971  1.00 42.96           O  
ANISOU 3517  O   LEU A 457     5116   5952   5254    620     98    233       O  
ATOM   3518  CB  LEU A 457      15.529  21.503  25.361  1.00 32.24           C  
ANISOU 3518  CB  LEU A 457     3840   4400   4012    450     33    233       C  
ATOM   3519  CG  LEU A 457      16.979  21.455  25.886  1.00 37.41           C  
ANISOU 3519  CG  LEU A 457     4570   4953   4691    428      7    216       C  
ATOM   3520  CD1 LEU A 457      17.465  20.018  25.934  1.00 29.19           C  
ANISOU 3520  CD1 LEU A 457     3520   3906   3664    340     20    230       C  
ATOM   3521  CD2 LEU A 457      17.888  22.270  24.982  1.00 35.51           C  
ANISOU 3521  CD2 LEU A 457     4369   4633   4491    427    -34    207       C  
ATOM   3522  N   PRO A 458      12.275  21.149  25.224  1.00 32.89           N  
ANISOU 3522  N   PRO A 458     3733   4751   4010    493    105    276       N  
ATOM   3523  CA  PRO A 458      10.999  21.874  25.216  1.00 40.32           C  
ANISOU 3523  CA  PRO A 458     4614   5795   4913    578    122    282       C  
ATOM   3524  C   PRO A 458      10.257  21.840  26.563  1.00 42.16           C  
ANISOU 3524  C   PRO A 458     4822   6109   5089    631    163    282       C  
ATOM   3525  O   PRO A 458       9.397  22.691  26.749  1.00 44.87           O  
ANISOU 3525  O   PRO A 458     5134   6520   5395    731    175    278       O  
ATOM   3526  CB  PRO A 458      10.192  21.177  24.102  1.00 38.01           C  
ANISOU 3526  CB  PRO A 458     4231   5585   4626    509    127    312       C  
ATOM   3527  CG  PRO A 458      11.288  20.671  23.163  1.00 37.35           C  
ANISOU 3527  CG  PRO A 458     4193   5403   4596    423     96    309       C  
ATOM   3528  CD  PRO A 458      12.354  20.181  24.123  1.00 29.65           C  
ANISOU 3528  CD  PRO A 458     3288   4345   3631    392     98    296       C  
ATOM   3529  N   LEU A 459      10.601  20.932  27.480  1.00 40.00           N  
ANISOU 3529  N   LEU A 459     4565   5827   4804    574    185    287       N  
ATOM   3530  CA  LEU A 459       9.951  20.892  28.796  1.00 38.05           C  
ANISOU 3530  CA  LEU A 459     4300   5659   4499    623    227    290       C  
ATOM   3531  C   LEU A 459      10.336  22.050  29.686  1.00 44.77           C  
ANISOU 3531  C   LEU A 459     5228   6455   5325    738    217    253       C  
ATOM   3532  O   LEU A 459       9.691  22.301  30.703  1.00 49.87           O  
ANISOU 3532  O   LEU A 459     5861   7173   5915    809    251    249       O  
ATOM   3533  CB  LEU A 459      10.294  19.612  29.529  1.00 37.79           C  
ANISOU 3533  CB  LEU A 459     4278   5621   4461    529    248    307       C  
ATOM   3534  CG  LEU A 459       9.439  18.380  29.243  1.00 46.05           C  
ANISOU 3534  CG  LEU A 459     5237   6764   5495    427    279    350       C  
ATOM   3535  CD1 LEU A 459       9.041  18.299  27.790  1.00 53.27           C  
ANISOU 3535  CD1 LEU A 459     6095   7705   6443    384    259    362       C  
ATOM   3536  CD2 LEU A 459      10.208  17.159  29.628  1.00 42.78           C  
ANISOU 3536  CD2 LEU A 459     4872   6287   5097    326    280    362       C  
ATOM   3537  N   ASP A 460      11.423  22.727  29.336  1.00 45.15           N  
ANISOU 3537  N   ASP A 460     5363   6378   5414    753    170    225       N  
ATOM   3538  CA  ASP A 460      11.891  23.837  30.141  1.00 44.53           C  
ANISOU 3538  CA  ASP A 460     5372   6232   5314    850    151    187       C  
ATOM   3539  C   ASP A 460      11.107  25.062  29.680  1.00 45.26           C  
ANISOU 3539  C   ASP A 460     5453   6356   5387    962    144    177       C  
ATOM   3540  O   ASP A 460      11.261  25.503  28.546  1.00 45.18           O  
ANISOU 3540  O   ASP A 460     5446   6307   5415    956    113    180       O  
ATOM   3541  CB  ASP A 460      13.406  24.033  29.970  1.00 39.47           C  
ANISOU 3541  CB  ASP A 460     4825   5446   4724    807    100    166       C  
ATOM   3542  CG  ASP A 460      13.946  25.131  30.872  1.00 51.85           C  
ANISOU 3542  CG  ASP A 460     6493   6939   6269    893     75    126       C  
ATOM   3543  OD1 ASP A 460      13.123  25.957  31.346  1.00 53.40           O  
ANISOU 3543  OD1 ASP A 460     6693   7181   6414   1002     90    111       O  
ATOM   3544  OD2 ASP A 460      15.177  25.168  31.121  1.00 51.91           O  
ANISOU 3544  OD2 ASP A 460     6574   6845   6303    855     38    109       O  
ATOM   3545  N   PRO A 461      10.249  25.605  30.549  1.00 53.01           N  
ANISOU 3545  N   PRO A 461     6424   7412   6305   1069    174    165       N  
ATOM   3546  CA  PRO A 461       9.329  26.667  30.106  1.00 55.83           C  
ANISOU 3546  CA  PRO A 461     6758   7820   6636   1186    174    160       C  
ATOM   3547  C   PRO A 461      10.096  27.890  29.641  1.00 58.04           C  
ANISOU 3547  C   PRO A 461     7145   7966   6944   1240    118    129       C  
ATOM   3548  O   PRO A 461       9.687  28.528  28.672  1.00 65.58           O  
ANISOU 3548  O   PRO A 461     8083   8926   7910   1283     99    136       O  
ATOM   3549  CB  PRO A 461       8.531  27.012  31.363  1.00 55.50           C  
ANISOU 3549  CB  PRO A 461     6708   7864   6516   1297    217    145       C  
ATOM   3550  CG  PRO A 461       8.887  25.970  32.383  1.00 59.40           C  
ANISOU 3550  CG  PRO A 461     7203   8372   6995   1221    245    153       C  
ATOM   3551  CD  PRO A 461      10.227  25.413  32.007  1.00 56.82           C  
ANISOU 3551  CD  PRO A 461     6934   7920   6735   1102    205    152       C  
ATOM   3552  N   SER A 462      11.215  28.188  30.295  1.00 50.97           N  
ANISOU 3552  N   SER A 462     6358   6951   6059   1230     87     99       N  
ATOM   3553  CA  SER A 462      12.015  29.348  29.916  1.00 56.51           C  
ANISOU 3553  CA  SER A 462     7168   7517   6785   1267     30     71       C  
ATOM   3554  C   SER A 462      12.592  29.307  28.484  1.00 58.17           C  
ANISOU 3554  C   SER A 462     7372   7667   7063   1184     -6     93       C  
ATOM   3555  O   SER A 462      13.046  30.338  27.976  1.00 56.58           O  
ANISOU 3555  O   SER A 462     7249   7370   6880   1218    -51     79       O  
ATOM   3556  CB  SER A 462      13.142  29.595  30.934  1.00 54.70           C  
ANISOU 3556  CB  SER A 462     7051   7180   6554   1256      1     36       C  
ATOM   3557  OG  SER A 462      14.272  28.789  30.661  1.00 58.03           O  
ANISOU 3557  OG  SER A 462     7477   7540   7031   1127    -19     49       O  
ATOM   3558  N   LEU A 463      12.588  28.140  27.836  1.00 55.32           N  
ANISOU 3558  N   LEU A 463     6926   7358   6737   1077     11    126       N  
ATOM   3559  CA  LEU A 463      13.148  28.042  26.482  1.00 49.79           C  
ANISOU 3559  CA  LEU A 463     6219   6605   6094   1000    -19    145       C  
ATOM   3560  C   LEU A 463      12.150  28.484  25.386  1.00 53.81           C  
ANISOU 3560  C   LEU A 463     6669   7178   6597   1048    -18    166       C  
ATOM   3561  O   LEU A 463      12.512  28.571  24.208  1.00 58.90           O  
ANISOU 3561  O   LEU A 463     7314   7784   7282   1001    -45    182       O  
ATOM   3562  CB  LEU A 463      13.716  26.643  26.193  1.00 41.91           C  
ANISOU 3562  CB  LEU A 463     5174   5616   5135    867     -8    167       C  
ATOM   3563  CG  LEU A 463      14.880  26.147  27.069  1.00 47.81           C  
ANISOU 3563  CG  LEU A 463     5979   6291   5895    810    -17    151       C  
ATOM   3564  CD1 LEU A 463      15.471  24.885  26.497  1.00 46.10           C  
ANISOU 3564  CD1 LEU A 463     5725   6071   5720    690    -13    174       C  
ATOM   3565  CD2 LEU A 463      15.988  27.209  27.263  1.00 44.41           C  
ANISOU 3565  CD2 LEU A 463     5658   5734   5482    833    -67    123       C  
ATOM   3566  N   ASN A 464      10.909  28.770  25.758  1.00 48.73           N  
ANISOU 3566  N   ASN A 464     5974   6639   5901   1145     12    167       N  
ATOM   3567  CA  ASN A 464       9.975  29.410  24.802  1.00 56.69           C  
ANISOU 3567  CA  ASN A 464     6937   7705   6898   1217      6    183       C  
ATOM   3568  C   ASN A 464       9.438  28.516  23.665  1.00 53.88           C  
ANISOU 3568  C   ASN A 464     6469   7438   6563   1134     17    221       C  
ATOM   3569  O   ASN A 464       8.891  29.027  22.679  1.00 52.58           O  
ANISOU 3569  O   ASN A 464     6276   7302   6398   1175      0    237       O  
ATOM   3570  CB  ASN A 464      10.590  30.696  24.194  1.00 57.79           C  
ANISOU 3570  CB  ASN A 464     7183   7717   7056   1268    -47    169       C  
ATOM   3571  CG  ASN A 464      10.734  31.829  25.218  1.00 64.98           C  
ANISOU 3571  CG  ASN A 464     8204   8555   7929   1383    -61    130       C  
ATOM   3572  OD1 ASN A 464      10.142  31.777  26.302  1.00 65.45           O  
ANISOU 3572  OD1 ASN A 464     8248   8681   7939   1453    -27    114       O  
ATOM   3573  ND2 ASN A 464      11.516  32.867  24.864  1.00 71.98           N  
ANISOU 3573  ND2 ASN A 464     9207   9307   8837   1402   -113    116       N  
ATOM   3574  N   TYR A 465       9.606  27.199  23.784  1.00 43.08           N  
ANISOU 3574  N   TYR A 465     5047   6110   5213   1019     40    236       N  
ATOM   3575  CA  TYR A 465       8.997  26.274  22.831  1.00 41.44           C  
ANISOU 3575  CA  TYR A 465     4735   5993   5017    938     51    270       C  
ATOM   3576  C   TYR A 465       7.475  26.344  22.960  1.00 43.91           C  
ANISOU 3576  C   TYR A 465     4943   6465   5277   1009     83    287       C  
ATOM   3577  O   TYR A 465       6.970  26.810  23.974  1.00 47.99           O  
ANISOU 3577  O   TYR A 465     5461   7026   5748   1105    108    274       O  
ATOM   3578  CB  TYR A 465       9.443  24.853  23.116  1.00 37.51           C  
ANISOU 3578  CB  TYR A 465     4214   5499   4539    808     71    280       C  
ATOM   3579  CG  TYR A 465      10.857  24.572  22.719  1.00 34.78           C  
ANISOU 3579  CG  TYR A 465     3944   5024   4246    726     41    271       C  
ATOM   3580  CD1 TYR A 465      11.158  24.112  21.440  1.00 32.14           C  
ANISOU 3580  CD1 TYR A 465     3592   4672   3949    646     21    287       C  
ATOM   3581  CD2 TYR A 465      11.915  24.789  23.623  1.00 39.71           C  
ANISOU 3581  CD2 TYR A 465     4659   5549   4880    731     31    245       C  
ATOM   3582  CE1 TYR A 465      12.482  23.862  21.064  1.00 40.29           C  
ANISOU 3582  CE1 TYR A 465     4689   5594   5026    577     -3    279       C  
ATOM   3583  CE2 TYR A 465      13.235  24.540  23.255  1.00 38.37           C  
ANISOU 3583  CE2 TYR A 465     4549   5271   4758    658      4    239       C  
ATOM   3584  CZ  TYR A 465      13.507  24.079  21.983  1.00 36.99           C  
ANISOU 3584  CZ  TYR A 465     4350   5086   4618    584    -11    257       C  
ATOM   3585  OH  TYR A 465      14.798  23.818  21.629  1.00 44.08           O  
ANISOU 3585  OH  TYR A 465     5300   5890   5558    519    -34    252       O  
ATOM   3586  N   THR A 466       6.748  25.860  21.952  1.00 45.72           N  
ANISOU 3586  N   THR A 466     5078   6785   5510    963     83    317       N  
ATOM   3587  CA  THR A 466       5.290  25.805  22.026  1.00 42.25           C  
ANISOU 3587  CA  THR A 466     4520   6514   5020   1016    112    338       C  
ATOM   3588  C   THR A 466       4.813  24.595  22.833  1.00 49.77           C  
ANISOU 3588  C   THR A 466     5395   7566   5951    935    159    356       C  
ATOM   3589  O   THR A 466       5.595  23.663  23.144  1.00 44.89           O  
ANISOU 3589  O   THR A 466     4813   6884   5360    825    164    354       O  
ATOM   3590  CB  THR A 466       4.633  25.736  20.640  1.00 43.02           C  
ANISOU 3590  CB  THR A 466     4539   6683   5125    992     90    366       C  
ATOM   3591  OG1 THR A 466       4.923  24.470  20.019  1.00 46.26           O  
ANISOU 3591  OG1 THR A 466     4916   7093   5568    835     86    383       O  
ATOM   3592  CG2 THR A 466       5.096  26.893  19.740  1.00 35.45           C  
ANISOU 3592  CG2 THR A 466     3658   5625   4187   1064     43    356       C  
ATOM   3593  N   THR A 467       3.521  24.605  23.157  1.00 47.24           N  
ANISOU 3593  N   THR A 467     4966   7406   5577    989    192    375       N  
ATOM   3594  CA  THR A 467       2.925  23.563  23.970  1.00 45.77           C  
ANISOU 3594  CA  THR A 467     4698   7331   5360    920    240    398       C  
ATOM   3595  C   THR A 467       2.919  22.227  23.214  1.00 47.07           C  
ANISOU 3595  C   THR A 467     4810   7520   5556    749    232    426       C  
ATOM   3596  O   THR A 467       3.190  21.181  23.787  1.00 49.25           O  
ANISOU 3596  O   THR A 467     5091   7787   5835    645    254    436       O  
ATOM   3597  CB  THR A 467       1.498  23.963  24.432  1.00 55.92           C  
ANISOU 3597  CB  THR A 467     5869   8799   6577   1024    278    415       C  
ATOM   3598  OG1 THR A 467       1.595  24.996  25.424  1.00 51.06           O  
ANISOU 3598  OG1 THR A 467     5320   8153   5926   1174    294    384       O  
ATOM   3599  CG2 THR A 467       0.773  22.757  25.036  1.00 54.76           C  
ANISOU 3599  CG2 THR A 467     5617   8789   6400    923    326    451       C  
ATOM   3600  N   GLU A 468       2.630  22.284  21.920  1.00 46.54           N  
ANISOU 3600  N   GLU A 468     4700   7475   5506    724    199    439       N  
ATOM   3601  CA  GLU A 468       2.691  21.122  21.049  1.00 46.04           C  
ANISOU 3601  CA  GLU A 468     4604   7418   5472    569    182    460       C  
ATOM   3602  C   GLU A 468       4.104  20.538  21.005  1.00 48.22           C  
ANISOU 3602  C   GLU A 468     4995   7527   5799    480    165    440       C  
ATOM   3603  O   GLU A 468       4.288  19.320  21.033  1.00 47.53           O  
ANISOU 3603  O   GLU A 468     4904   7432   5723    351    172    453       O  
ATOM   3604  CB  GLU A 468       2.270  21.514  19.633  1.00 53.65           C  
ANISOU 3604  CB  GLU A 468     5522   8416   6445    580    143    470       C  
ATOM   3605  CG  GLU A 468       0.862  22.148  19.544  1.00 69.17           C  
ANISOU 3605  CG  GLU A 468     7367  10554   8359    680    153    491       C  
ATOM   3606  CD  GLU A 468       0.878  23.681  19.670  1.00 76.73           C  
ANISOU 3606  CD  GLU A 468     8374  11479   9303    862    144    470       C  
ATOM   3607  OE1 GLU A 468       1.187  24.215  20.758  1.00 70.87           O  
ANISOU 3607  OE1 GLU A 468     7693  10691   8545    948    168    447       O  
ATOM   3608  OE2 GLU A 468       0.564  24.361  18.667  1.00 87.27           O  
ANISOU 3608  OE2 GLU A 468     9691  12831  10637    921    110    475       O  
ATOM   3609  N   GLU A 469       5.095  21.421  20.909  1.00 41.99           N  
ANISOU 3609  N   GLU A 469     4310   6607   5039    549    140    410       N  
ATOM   3610  CA  GLU A 469       6.483  21.016  20.893  1.00 40.86           C  
ANISOU 3610  CA  GLU A 469     4271   6312   4941    482    123    391       C  
ATOM   3611  C   GLU A 469       6.822  20.321  22.210  1.00 41.34           C  
ANISOU 3611  C   GLU A 469     4361   6355   4991    446    156    388       C  
ATOM   3612  O   GLU A 469       7.555  19.333  22.221  1.00 40.17           O  
ANISOU 3612  O   GLU A 469     4254   6141   4869    344    153    388       O  
ATOM   3613  CB  GLU A 469       7.386  22.217  20.629  1.00 42.14           C  
ANISOU 3613  CB  GLU A 469     4528   6353   5129    568     90    365       C  
ATOM   3614  CG  GLU A 469       7.368  22.654  19.159  1.00 46.16           C  
ANISOU 3614  CG  GLU A 469     5031   6849   5660    569     52    372       C  
ATOM   3615  CD  GLU A 469       8.188  23.895  18.933  1.00 46.04           C  
ANISOU 3615  CD  GLU A 469     5110   6718   5665    652     21    351       C  
ATOM   3616  OE1 GLU A 469       8.124  24.783  19.809  1.00 42.67           O  
ANISOU 3616  OE1 GLU A 469     4720   6276   5216    755     29    335       O  
ATOM   3617  OE2 GLU A 469       8.914  23.965  17.913  1.00 50.18           O  
ANISOU 3617  OE2 GLU A 469     5676   7166   6224    610    -10    351       O  
ATOM   3618  N   ARG A 470       6.239  20.804  23.306  1.00 40.14           N  
ANISOU 3618  N   ARG A 470     4186   6269   4795    532    188    386       N  
ATOM   3619  CA  ARG A 470       6.388  20.156  24.600  1.00 44.25           C  
ANISOU 3619  CA  ARG A 470     4725   6795   5295    503    224    387       C  
ATOM   3620  C   ARG A 470       5.830  18.724  24.569  1.00 46.70           C  
ANISOU 3620  C   ARG A 470     4965   7185   5594    369    247    423       C  
ATOM   3621  O   ARG A 470       6.465  17.786  25.078  1.00 41.09           O  
ANISOU 3621  O   ARG A 470     4303   6414   4895    285    255    426       O  
ATOM   3622  CB  ARG A 470       5.721  20.998  25.696  1.00 52.60           C  
ANISOU 3622  CB  ARG A 470     5762   7926   6296    631    257    380       C  
ATOM   3623  CG  ARG A 470       6.360  20.889  27.069  1.00 65.59           C  
ANISOU 3623  CG  ARG A 470     7482   9515   7925    648    278    362       C  
ATOM   3624  CD  ARG A 470       5.477  20.168  28.105  1.00 77.44           C  
ANISOU 3624  CD  ARG A 470     8910  11144   9370    624    333    390       C  
ATOM   3625  NE  ARG A 470       4.312  20.977  28.458  1.00 88.24           N  
ANISOU 3625  NE  ARG A 470    10201  12645  10680    744    363    394       N  
ATOM   3626  CZ  ARG A 470       3.045  20.608  28.266  1.00 89.84           C  
ANISOU 3626  CZ  ARG A 470    10274  13013  10847    724    394    431       C  
ATOM   3627  NH1 ARG A 470       2.756  19.410  27.758  1.00 86.45           N  
ANISOU 3627  NH1 ARG A 470     9782  12631  10433    577    397    468       N  
ATOM   3628  NH2 ARG A 470       2.063  21.435  28.605  1.00 91.45           N  
ANISOU 3628  NH2 ARG A 470    10411  13338  10997    851    421    432       N  
ATOM   3629  N   ILE A 471       4.662  18.540  23.953  1.00 41.94           N  
ANISOU 3629  N   ILE A 471     4251   6714   4970    346    253    451       N  
ATOM   3630  CA  ILE A 471       4.073  17.203  23.880  1.00 42.97           C  
ANISOU 3630  CA  ILE A 471     4316   6923   5089    208    270    486       C  
ATOM   3631  C   ILE A 471       4.831  16.313  22.914  1.00 40.74           C  
ANISOU 3631  C   ILE A 471     4086   6539   4854     87    234    484       C  
ATOM   3632  O   ILE A 471       4.983  15.116  23.139  1.00 43.48           O  
ANISOU 3632  O   ILE A 471     4449   6868   5203    -29    243    500       O  
ATOM   3633  CB  ILE A 471       2.573  17.260  23.478  1.00 50.97           C  
ANISOU 3633  CB  ILE A 471     5186   8119   6062    210    283    519       C  
ATOM   3634  CG1 ILE A 471       1.761  17.872  24.630  1.00 46.61           C  
ANISOU 3634  CG1 ILE A 471     4574   7685   5452    318    331    527       C  
ATOM   3635  CG2 ILE A 471       2.058  15.863  23.067  1.00 39.49           C  
ANISOU 3635  CG2 ILE A 471     3673   6726   4605     42    284    555       C  
ATOM   3636  CD1 ILE A 471       0.482  18.483  24.190  1.00 52.22           C  
ANISOU 3636  CD1 ILE A 471     5158   8559   6126    388    337    546       C  
ATOM   3637  N   PHE A 472       5.267  16.901  21.814  1.00 39.37           N  
ANISOU 3637  N   PHE A 472     3941   6304   4714    118    195    465       N  
ATOM   3638  CA  PHE A 472       6.122  16.205  20.856  1.00 42.70           C  
ANISOU 3638  CA  PHE A 472     4423   6621   5179     24    161    456       C  
ATOM   3639  C   PHE A 472       7.403  15.679  21.545  1.00 38.48           C  
ANISOU 3639  C   PHE A 472     3998   5952   4670     -7    164    439       C  
ATOM   3640  O   PHE A 472       7.718  14.482  21.481  1.00 41.81           O  
ANISOU 3640  O   PHE A 472     4450   6336   5102   -115    163    447       O  
ATOM   3641  CB  PHE A 472       6.440  17.149  19.702  1.00 40.40           C  
ANISOU 3641  CB  PHE A 472     4150   6286   4914     86    122    439       C  
ATOM   3642  CG  PHE A 472       7.274  16.538  18.616  1.00 39.13           C  
ANISOU 3642  CG  PHE A 472     4045   6030   4791      4     90    430       C  
ATOM   3643  CD1 PHE A 472       6.942  15.308  18.072  1.00 35.70           C  
ANISOU 3643  CD1 PHE A 472     3585   5624   4353   -121     84    445       C  
ATOM   3644  CD2 PHE A 472       8.395  17.220  18.126  1.00 36.94           C  
ANISOU 3644  CD2 PHE A 472     3849   5636   4550     52     64    405       C  
ATOM   3645  CE1 PHE A 472       7.721  14.752  17.052  1.00 30.07           C  
ANISOU 3645  CE1 PHE A 472     2932   4824   3671   -188     54    433       C  
ATOM   3646  CE2 PHE A 472       9.165  16.688  17.113  1.00 37.30           C  
ANISOU 3646  CE2 PHE A 472     3941   5604   4625    -16     38    397       C  
ATOM   3647  CZ  PHE A 472       8.823  15.443  16.570  1.00 38.84           C  
ANISOU 3647  CZ  PHE A 472     4115   5828   4815   -131     34    409       C  
ATOM   3648  N   ALA A 473       8.099  16.548  22.264  1.00 32.75           N  
ANISOU 3648  N   ALA A 473     3332   5160   3951     90    167    415       N  
ATOM   3649  CA  ALA A 473       9.331  16.127  22.958  1.00 37.28           C  
ANISOU 3649  CA  ALA A 473     4003   5614   4546     69    167    399       C  
ATOM   3650  C   ALA A 473       9.057  14.960  23.913  1.00 39.46           C  
ANISOU 3650  C   ALA A 473     4274   5923   4795     -9    199    421       C  
ATOM   3651  O   ALA A 473       9.778  13.959  23.913  1.00 38.85           O  
ANISOU 3651  O   ALA A 473     4254   5769   4737    -89    192    423       O  
ATOM   3652  CB  ALA A 473       9.941  17.294  23.703  1.00 34.52           C  
ANISOU 3652  CB  ALA A 473     3709   5208   4197    183    164    372       C  
ATOM   3653  N   GLN A 474       7.982  15.073  24.698  1.00 40.00           N  
ANISOU 3653  N   GLN A 474     4271   6110   4816     17    235    442       N  
ATOM   3654  CA  GLN A 474       7.530  13.961  25.543  1.00 41.95           C  
ANISOU 3654  CA  GLN A 474     4499   6408   5031    -67    269    472       C  
ATOM   3655  C   GLN A 474       7.362  12.654  24.769  1.00 39.38           C  
ANISOU 3655  C   GLN A 474     4166   6079   4718   -210    256    495       C  
ATOM   3656  O   GLN A 474       7.826  11.599  25.212  1.00 40.19           O  
ANISOU 3656  O   GLN A 474     4326   6122   4822   -290    262    505       O  
ATOM   3657  CB  GLN A 474       6.256  14.316  26.312  1.00 41.53           C  
ANISOU 3657  CB  GLN A 474     4350   6507   4921    -21    311    496       C  
ATOM   3658  CG  GLN A 474       6.511  15.210  27.499  1.00 50.65           C  
ANISOU 3658  CG  GLN A 474     5541   7653   6050     99    333    476       C  
ATOM   3659  CD  GLN A 474       5.271  15.967  27.949  1.00 64.36           C  
ANISOU 3659  CD  GLN A 474     7180   9541   7733    188    368    488       C  
ATOM   3660  OE1 GLN A 474       4.294  16.107  27.200  1.00 69.93           O  
ANISOU 3660  OE1 GLN A 474     7787  10354   8428    183    368    506       O  
ATOM   3661  NE2 GLN A 474       5.311  16.478  29.171  1.00 67.11           N  
ANISOU 3661  NE2 GLN A 474     7554   9902   8042    277    398    477       N  
ATOM   3662  N   ARG A 475       6.708  12.708  23.613  1.00 38.16           N  
ANISOU 3662  N   ARG A 475     3946   5984   4570   -241    237    502       N  
ATOM   3663  CA  ARG A 475       6.586  11.496  22.792  1.00 42.00           C  
ANISOU 3663  CA  ARG A 475     4435   6456   5066   -377    218    517       C  
ATOM   3664  C   ARG A 475       7.970  10.924  22.401  1.00 39.16           C  
ANISOU 3664  C   ARG A 475     4195   5936   4749   -412    190    492       C  
ATOM   3665  O   ARG A 475       8.192   9.697  22.469  1.00 38.15           O  
ANISOU 3665  O   ARG A 475     4115   5760   4621   -515    189    504       O  
ATOM   3666  CB  ARG A 475       5.793  11.760  21.501  1.00 45.18           C  
ANISOU 3666  CB  ARG A 475     4758   6938   5470   -395    192    522       C  
ATOM   3667  CG  ARG A 475       4.315  11.610  21.596  1.00 45.01           C  
ANISOU 3667  CG  ARG A 475     4612   7085   5404   -435    212    560       C  
ATOM   3668  CD  ARG A 475       3.642  12.132  20.289  1.00 58.84           C  
ANISOU 3668  CD  ARG A 475     6285   8911   7158   -422    179    559       C  
ATOM   3669  NE  ARG A 475       4.091  11.345  19.154  1.00 49.45           N  
ANISOU 3669  NE  ARG A 475     5149   7644   5996   -522    139    549       N  
ATOM   3670  CZ  ARG A 475       4.269  11.808  17.928  1.00 40.50           C  
ANISOU 3670  CZ  ARG A 475     4017   6487   4883   -497    101    530       C  
ATOM   3671  NH1 ARG A 475       4.000  13.067  17.636  1.00 38.61           N  
ANISOU 3671  NH1 ARG A 475     3731   6297   4642   -378     96    523       N  
ATOM   3672  NH2 ARG A 475       4.713  10.990  16.988  1.00 40.46           N  
ANISOU 3672  NH2 ARG A 475     4068   6408   4896   -589     69    520       N  
ATOM   3673  N   LEU A 476       8.883  11.788  21.948  1.00 36.27           N  
ANISOU 3673  N   LEU A 476     3875   5489   4418   -328    167    459       N  
ATOM   3674  CA  LEU A 476      10.173  11.286  21.465  1.00 32.70           C  
ANISOU 3674  CA  LEU A 476     3521   4901   4003   -356    142    437       C  
ATOM   3675  C   LEU A 476      10.927  10.697  22.628  1.00 32.48           C  
ANISOU 3675  C   LEU A 476     3567   4802   3973   -363    159    438       C  
ATOM   3676  O   LEU A 476      11.568   9.661  22.486  1.00 41.45           O  
ANISOU 3676  O   LEU A 476     4771   5858   5120   -430    149    437       O  
ATOM   3677  CB  LEU A 476      11.010  12.361  20.756  1.00 34.45           C  
ANISOU 3677  CB  LEU A 476     3771   5059   4260   -270    115    407       C  
ATOM   3678  CG  LEU A 476      10.326  12.987  19.531  1.00 41.25           C  
ANISOU 3678  CG  LEU A 476     4567   5983   5122   -256     95    408       C  
ATOM   3679  CD1 LEU A 476      11.090  14.176  19.036  1.00 41.28           C  
ANISOU 3679  CD1 LEU A 476     4601   5928   5154   -165     74    385       C  
ATOM   3680  CD2 LEU A 476      10.221  11.983  18.454  1.00 43.40           C  
ANISOU 3680  CD2 LEU A 476     4845   6246   5399   -358     75    412       C  
ATOM   3681  N   MET A 477      10.851  11.343  23.786  1.00 32.37           N  
ANISOU 3681  N   MET A 477     3545   4816   3940   -290    183    439       N  
ATOM   3682  CA  MET A 477      11.547  10.812  24.957  1.00 36.14           C  
ANISOU 3682  CA  MET A 477     4092   5232   4409   -293    197    441       C  
ATOM   3683  C   MET A 477      11.029   9.420  25.272  1.00 41.54           C  
ANISOU 3683  C   MET A 477     4780   5937   5067   -407    214    474       C  
ATOM   3684  O   MET A 477      11.822   8.544  25.635  1.00 40.74           O  
ANISOU 3684  O   MET A 477     4761   5746   4972   -446    210    475       O  
ATOM   3685  CB  MET A 477      11.426  11.722  26.181  1.00 36.45           C  
ANISOU 3685  CB  MET A 477     4119   5307   4422   -198    221    436       C  
ATOM   3686  CG  MET A 477      12.209  13.028  26.077  1.00 39.80           C  
ANISOU 3686  CG  MET A 477     4573   5677   4872    -90    199    400       C  
ATOM   3687  SD  MET A 477      11.604  14.216  27.315  1.00 48.94           S  
ANISOU 3687  SD  MET A 477     5700   6909   5986     25    227    394       S  
ATOM   3688  CE  MET A 477      12.388  13.609  28.764  1.00 35.11           C  
ANISOU 3688  CE  MET A 477     4027   5099   4216     19    241    395       C  
ATOM   3689  N   LYS A 478       9.710   9.219  25.133  1.00 38.77           N  
ANISOU 3689  N   LYS A 478     4342   5704   4685   -461    232    503       N  
ATOM   3690  CA  LYS A 478       9.087   7.896  25.359  1.00 42.36           C  
ANISOU 3690  CA  LYS A 478     4795   6187   5111   -587    246    541       C  
ATOM   3691  C   LYS A 478       9.587   6.854  24.369  1.00 40.37           C  
ANISOU 3691  C   LYS A 478     4610   5843   4885   -680    212    534       C  
ATOM   3692  O   LYS A 478       9.944   5.727  24.770  1.00 42.92           O  
ANISOU 3692  O   LYS A 478     5009   6097   5200   -752    214    549       O  
ATOM   3693  CB  LYS A 478       7.557   7.961  25.229  1.00 46.48           C  
ANISOU 3693  CB  LYS A 478     5196   6867   5597   -632    266    574       C  
ATOM   3694  CG  LYS A 478       6.825   8.365  26.460  1.00 58.46           C  
ANISOU 3694  CG  LYS A 478     6652   8492   7068   -588    312    599       C  
ATOM   3695  CD  LYS A 478       6.819   7.252  27.483  1.00 69.32           C  
ANISOU 3695  CD  LYS A 478     8074   9851   8413   -673    338    634       C  
ATOM   3696  CE  LYS A 478       6.036   7.655  28.731  1.00 70.24           C  
ANISOU 3696  CE  LYS A 478     8124  10088   8475   -629    389    661       C  
ATOM   3697  NZ  LYS A 478       6.308   9.064  29.155  1.00 69.14           N  
ANISOU 3697  NZ  LYS A 478     7971   9962   8336   -469    397    627       N  
ATOM   3698  N   TYR A 479       9.593   7.209  23.077  1.00 38.80           N  
ANISOU 3698  N   TYR A 479     4389   5642   4712   -675    182    513       N  
ATOM   3699  CA  TYR A 479      10.112   6.292  22.042  1.00 39.81           C  
ANISOU 3699  CA  TYR A 479     4586   5681   4861   -750    149    500       C  
ATOM   3700  C   TYR A 479      11.525   5.849  22.378  1.00 36.84           C  
ANISOU 3700  C   TYR A 479     4326   5165   4508   -722    141    480       C  
ATOM   3701  O   TYR A 479      11.816   4.656  22.335  1.00 33.53           O  
ANISOU 3701  O   TYR A 479     3983   4674   4083   -800    133    487       O  
ATOM   3702  CB  TYR A 479      10.144   6.909  20.632  1.00 37.74           C  
ANISOU 3702  CB  TYR A 479     4293   5425   4623   -724    119    475       C  
ATOM   3703  CG  TYR A 479       8.782   7.153  20.010  1.00 41.23           C  
ANISOU 3703  CG  TYR A 479     4624   5997   5043   -765    115    494       C  
ATOM   3704  CD1 TYR A 479       7.744   6.241  20.153  1.00 37.21           C  
ANISOU 3704  CD1 TYR A 479     4076   5561   4500   -883    122    529       C  
ATOM   3705  CD2 TYR A 479       8.549   8.301  19.274  1.00 40.47           C  
ANISOU 3705  CD2 TYR A 479     4464   5954   4957   -689    102    480       C  
ATOM   3706  CE1 TYR A 479       6.501   6.492  19.583  1.00 40.22           C  
ANISOU 3706  CE1 TYR A 479     4346   6075   4859   -920    115    547       C  
ATOM   3707  CE2 TYR A 479       7.339   8.555  18.708  1.00 49.20           C  
ANISOU 3707  CE2 TYR A 479     5468   7184   6041   -716     96    498       C  
ATOM   3708  CZ  TYR A 479       6.306   7.652  18.862  1.00 47.69           C  
ANISOU 3708  CZ  TYR A 479     5227   7075   5817   -831    102    531       C  
ATOM   3709  OH  TYR A 479       5.099   7.952  18.270  1.00 50.05           O  
ANISOU 3709  OH  TYR A 479     5413   7510   6093   -855     93    550       O  
ATOM   3710  N   TRP A 480      12.388   6.809  22.712  1.00 33.15           N  
ANISOU 3710  N   TRP A 480     3873   4659   4062   -611    142    456       N  
ATOM   3711  CA  TRP A 480      13.817   6.517  22.909  1.00 38.07           C  
ANISOU 3711  CA  TRP A 480     4594   5160   4710   -575    129    434       C  
ATOM   3712  C   TRP A 480      14.032   5.656  24.174  1.00 34.99           C  
ANISOU 3712  C   TRP A 480     4264   4733   4296   -602    148    456       C  
ATOM   3713  O   TRP A 480      14.739   4.649  24.149  1.00 34.12           O  
ANISOU 3713  O   TRP A 480     4242   4532   4190   -638    137    455       O  
ATOM   3714  CB  TRP A 480      14.633   7.826  22.973  1.00 32.32           C  
ANISOU 3714  CB  TRP A 480     3859   4412   4010   -459    122    407       C  
ATOM   3715  CG  TRP A 480      15.378   8.232  21.686  1.00 31.94           C  
ANISOU 3715  CG  TRP A 480     3824   4314   3997   -431     93    378       C  
ATOM   3716  CD1 TRP A 480      16.727   8.414  21.550  1.00 29.77           C  
ANISOU 3716  CD1 TRP A 480     3605   3954   3751   -381     78    355       C  
ATOM   3717  CD2 TRP A 480      14.812   8.501  20.386  1.00 34.97           C  
ANISOU 3717  CD2 TRP A 480     4159   4740   4387   -454     78    374       C  
ATOM   3718  NE1 TRP A 480      17.038   8.781  20.259  1.00 29.84           N  
ANISOU 3718  NE1 TRP A 480     3605   3949   3783   -371     58    338       N  
ATOM   3719  CE2 TRP A 480      15.883   8.851  19.530  1.00 31.33           C  
ANISOU 3719  CE2 TRP A 480     3734   4212   3958   -414     57    348       C  
ATOM   3720  CE3 TRP A 480      13.515   8.463  19.865  1.00 34.41           C  
ANISOU 3720  CE3 TRP A 480     4017   4762   4296   -506     80    390       C  
ATOM   3721  CZ2 TRP A 480      15.689   9.172  18.198  1.00 29.51           C  
ANISOU 3721  CZ2 TRP A 480     3475   4000   3736   -421     38    339       C  
ATOM   3722  CZ3 TRP A 480      13.334   8.779  18.553  1.00 34.59           C  
ANISOU 3722  CZ3 TRP A 480     4012   4802   4328   -512     57    379       C  
ATOM   3723  CH2 TRP A 480      14.421   9.134  17.724  1.00 35.27           C  
ANISOU 3723  CH2 TRP A 480     4141   4815   4445   -468     37    354       C  
ATOM   3724  N   THR A 481      13.364   6.013  25.264  1.00 32.94           N  
ANISOU 3724  N   THR A 481     3960   4549   4006   -585    178    478       N  
ATOM   3725  CA  THR A 481      13.509   5.227  26.485  1.00 33.34           C  
ANISOU 3725  CA  THR A 481     4067   4572   4028   -612    197    503       C  
ATOM   3726  C   THR A 481      12.760   3.879  26.410  1.00 37.90           C  
ANISOU 3726  C   THR A 481     4665   5158   4578   -743    203    540       C  
ATOM   3727  O   THR A 481      13.251   2.897  26.971  1.00 36.67           O  
ANISOU 3727  O   THR A 481     4598   4925   4410   -780    203    554       O  
ATOM   3728  CB  THR A 481      13.151   6.026  27.759  1.00 36.06           C  
ANISOU 3728  CB  THR A 481     4369   4989   4344   -545    229    514       C  
ATOM   3729  OG1 THR A 481      11.824   6.557  27.641  1.00 40.84           O  
ANISOU 3729  OG1 THR A 481     4868   5725   4926   -557    250    531       O  
ATOM   3730  CG2 THR A 481      14.094   7.196  27.911  1.00 40.00           C  
ANISOU 3730  CG2 THR A 481     4879   5450   4870   -427    214    476       C  
ATOM   3731  N   ASN A 482      11.606   3.813  25.722  1.00 33.89           N  
ANISOU 3731  N   ASN A 482     4081   4738   4058   -815    205    555       N  
ATOM   3732  CA  ASN A 482      11.006   2.479  25.452  1.00 40.01           C  
ANISOU 3732  CA  ASN A 482     4888   5503   4811   -954    200    586       C  
ATOM   3733  C   ASN A 482      11.999   1.589  24.716  1.00 41.10           C  
ANISOU 3733  C   ASN A 482     5142   5501   4972   -981    165    562       C  
ATOM   3734  O   ASN A 482      12.183   0.411  25.061  1.00 36.81           O  
ANISOU 3734  O   ASN A 482     4690   4884   4411  -1052    161    582       O  
ATOM   3735  CB  ASN A 482       9.730   2.547  24.620  1.00 36.48           C  
ANISOU 3735  CB  ASN A 482     4341   5166   4351  -1031    196    600       C  
ATOM   3736  CG  ASN A 482       8.553   3.048  25.406  1.00 39.36           C  
ANISOU 3736  CG  ASN A 482     4595   5681   4679  -1035    234    636       C  
ATOM   3737  OD1 ASN A 482       8.577   3.046  26.630  1.00 39.49           O  
ANISOU 3737  OD1 ASN A 482     4621   5712   4670  -1010    266    658       O  
ATOM   3738  ND2 ASN A 482       7.517   3.491  24.705  1.00 40.91           N  
ANISOU 3738  ND2 ASN A 482     4680   5994   4868  -1059    231    643       N  
ATOM   3739  N   PHE A 483      12.627   2.175  23.693  1.00 40.39           N  
ANISOU 3739  N   PHE A 483     5049   5377   4919   -918    140    521       N  
ATOM   3740  CA  PHE A 483      13.635   1.467  22.921  1.00 42.45           C  
ANISOU 3740  CA  PHE A 483     5412   5515   5201   -922    110    494       C  
ATOM   3741  C   PHE A 483      14.813   0.978  23.795  1.00 39.79           C  
ANISOU 3741  C   PHE A 483     5179   5074   4867   -872    112    491       C  
ATOM   3742  O   PHE A 483      15.208  -0.190  23.712  1.00 35.84           O  
ANISOU 3742  O   PHE A 483     4779   4480   4357   -922     98    494       O  
ATOM   3743  CB  PHE A 483      14.143   2.284  21.722  1.00 35.83           C  
ANISOU 3743  CB  PHE A 483     4546   4671   4399   -856     88    453       C  
ATOM   3744  CG  PHE A 483      15.208   1.572  20.968  1.00 35.46           C  
ANISOU 3744  CG  PHE A 483     4599   4506   4367   -850     63    425       C  
ATOM   3745  CD1 PHE A 483      14.885   0.449  20.185  1.00 38.86           C  
ANISOU 3745  CD1 PHE A 483     5088   4895   4781   -947     42    424       C  
ATOM   3746  CD2 PHE A 483      16.532   1.926  21.121  1.00 29.80           C  
ANISOU 3746  CD2 PHE A 483     3925   3721   3676   -751     59    401       C  
ATOM   3747  CE1 PHE A 483      15.870  -0.274  19.517  1.00 33.65           C  
ANISOU 3747  CE1 PHE A 483     4531   4124   4129   -933     20    396       C  
ATOM   3748  CE2 PHE A 483      17.526   1.207  20.458  1.00 31.14           C  
ANISOU 3748  CE2 PHE A 483     4186   3792   3856   -738     39    376       C  
ATOM   3749  CZ  PHE A 483      17.200   0.114  19.649  1.00 28.24           C  
ANISOU 3749  CZ  PHE A 483     3879   3380   3470   -823     21    372       C  
ATOM   3750  N   ALA A 484      15.357   1.868  24.628  1.00 34.66           N  
ANISOU 3750  N   ALA A 484     4505   4437   4227   -773    126    484       N  
ATOM   3751  CA  ALA A 484      16.466   1.523  25.530  1.00 33.82           C  
ANISOU 3751  CA  ALA A 484     4483   4246   4121   -718    126    483       C  
ATOM   3752  C   ALA A 484      16.053   0.384  26.450  1.00 40.40           C  
ANISOU 3752  C   ALA A 484     5379   5057   4914   -796    140    524       C  
ATOM   3753  O   ALA A 484      16.832  -0.535  26.738  1.00 36.84           O  
ANISOU 3753  O   ALA A 484     5034   4507   4458   -797    129    527       O  
ATOM   3754  CB  ALA A 484      16.848   2.708  26.371  1.00 24.98           C  
ANISOU 3754  CB  ALA A 484     3318   3165   3010   -617    139    474       C  
ATOM   3755  N   ARG A 485      14.814   0.481  26.918  1.00 38.87           N  
ANISOU 3755  N   ARG A 485     5117   4962   4690   -858    166    558       N  
ATOM   3756  CA  ARG A 485      14.277  -0.432  27.906  1.00 43.02           C  
ANISOU 3756  CA  ARG A 485     5683   5490   5172   -936    186    605       C  
ATOM   3757  C   ARG A 485      14.008  -1.834  27.320  1.00 45.68           C  
ANISOU 3757  C   ARG A 485     6103   5758   5495  -1058    167    622       C  
ATOM   3758  O   ARG A 485      14.304  -2.834  27.963  1.00 48.65           O  
ANISOU 3758  O   ARG A 485     6581   6057   5847  -1096    167    647       O  
ATOM   3759  CB  ARG A 485      12.999   0.185  28.498  1.00 51.81           C  
ANISOU 3759  CB  ARG A 485     6682   6749   6255   -963    223    636       C  
ATOM   3760  CG  ARG A 485      12.579  -0.298  29.882  1.00 60.27           C  
ANISOU 3760  CG  ARG A 485     7772   7849   7277  -1000    256    685       C  
ATOM   3761  CD  ARG A 485      11.236   0.348  30.335  1.00 84.15           C  
ANISOU 3761  CD  ARG A 485    10668  11036  10268  -1023    296    715       C  
ATOM   3762  NE  ARG A 485      10.966   1.701  29.800  1.00 82.91           N  
ANISOU 3762  NE  ARG A 485    10402  10965  10134   -939    297    682       N  
ATOM   3763  CZ  ARG A 485      11.344   2.852  30.372  1.00 79.56           C  
ANISOU 3763  CZ  ARG A 485     9945  10568   9715   -814    309    658       C  
ATOM   3764  NH1 ARG A 485      12.033   2.840  31.512  1.00 82.31           N  
ANISOU 3764  NH1 ARG A 485    10355  10872  10046   -758    320    661       N  
ATOM   3765  NH2 ARG A 485      11.029   4.025  29.807  1.00 69.29           N  
ANISOU 3765  NH2 ARG A 485     8555   9338   8433   -746    307    630       N  
ATOM   3766  N   THR A 486      13.470  -1.910  26.103  1.00 42.23           N  
ANISOU 3766  N   THR A 486     5632   5343   5070  -1119    148    608       N  
ATOM   3767  CA  THR A 486      12.950  -3.186  25.579  1.00 43.29           C  
ANISOU 3767  CA  THR A 486     5836   5430   5183  -1255    129    628       C  
ATOM   3768  C   THR A 486      13.433  -3.553  24.164  1.00 45.00           C  
ANISOU 3768  C   THR A 486     6109   5566   5424  -1262     90    585       C  
ATOM   3769  O   THR A 486      13.169  -4.651  23.685  1.00 45.96           O  
ANISOU 3769  O   THR A 486     6312   5625   5528  -1365     67    593       O  
ATOM   3770  CB  THR A 486      11.417  -3.136  25.479  1.00 40.41           C  
ANISOU 3770  CB  THR A 486     5366   5195   4791  -1368    144    664       C  
ATOM   3771  OG1 THR A 486      11.062  -2.245  24.418  1.00 43.65           O  
ANISOU 3771  OG1 THR A 486     5676   5681   5227  -1340    132    634       O  
ATOM   3772  CG2 THR A 486      10.783  -2.628  26.792  1.00 33.94           C  
ANISOU 3772  CG2 THR A 486     4467   4486   3944  -1355    189    706       C  
ATOM   3773  N   GLY A 487      14.118  -2.638  23.481  1.00 40.09           N  
ANISOU 3773  N   GLY A 487     5448   4946   4840  -1157     80    541       N  
ATOM   3774  CA  GLY A 487      14.477  -2.861  22.086  1.00 35.38           C  
ANISOU 3774  CA  GLY A 487     4888   4295   4261  -1160     48    501       C  
ATOM   3775  C   GLY A 487      13.324  -2.526  21.146  1.00 40.72           C  
ANISOU 3775  C   GLY A 487     5469   5071   4933  -1236     38    502       C  
ATOM   3776  O   GLY A 487      13.367  -2.845  19.960  1.00 44.59           O  
ANISOU 3776  O   GLY A 487     5989   5526   5427  -1267      9    475       O  
ATOM   3777  N   ASP A 488      12.299  -1.848  21.660  1.00 40.32           N  
ANISOU 3777  N   ASP A 488     5299   5149   4871  -1258     62    532       N  
ATOM   3778  CA  ASP A 488      11.103  -1.580  20.861  1.00 44.30           C  
ANISOU 3778  CA  ASP A 488     5704   5762   5365  -1333     53    539       C  
ATOM   3779  C   ASP A 488      10.530  -0.188  21.188  1.00 37.48           C  
ANISOU 3779  C   ASP A 488     4695   5037   4509  -1260     79    547       C  
ATOM   3780  O   ASP A 488      10.114   0.040  22.306  1.00 40.24           O  
ANISOU 3780  O   ASP A 488     5000   5448   4840  -1253    112    579       O  
ATOM   3781  CB  ASP A 488      10.060  -2.690  21.114  1.00 41.59           C  
ANISOU 3781  CB  ASP A 488     5379   5441   4982  -1494     50    583       C  
ATOM   3782  CG  ASP A 488       8.809  -2.536  20.265  1.00 49.23           C  
ANISOU 3782  CG  ASP A 488     6243   6525   5935  -1587     33    593       C  
ATOM   3783  OD1 ASP A 488       8.608  -1.457  19.680  1.00 53.40           O  
ANISOU 3783  OD1 ASP A 488     6670   7137   6482  -1517     33    574       O  
ATOM   3784  OD2 ASP A 488       8.007  -3.497  20.179  1.00 55.18           O  
ANISOU 3784  OD2 ASP A 488     7019   7290   6658  -1733     19    623       O  
ATOM   3785  N   PRO A 489      10.501   0.741  20.209  1.00 43.38           N  
ANISOU 3785  N   PRO A 489     5374   5829   5279  -1202     65    518       N  
ATOM   3786  CA  PRO A 489      10.075   2.101  20.593  1.00 38.67           C  
ANISOU 3786  CA  PRO A 489     4658   5347   4688  -1114     89    523       C  
ATOM   3787  C   PRO A 489       8.590   2.166  20.986  1.00 46.04           C  
ANISOU 3787  C   PRO A 489     5480   6428   5587  -1187    109    566       C  
ATOM   3788  O   PRO A 489       8.155   3.138  21.603  1.00 49.61           O  
ANISOU 3788  O   PRO A 489     5841   6976   6032  -1115    137    577       O  
ATOM   3789  CB  PRO A 489      10.318   2.947  19.331  1.00 34.33           C  
ANISOU 3789  CB  PRO A 489     4072   4806   4166  -1052     64    487       C  
ATOM   3790  CG  PRO A 489      10.669   1.985  18.208  1.00 38.18           C  
ANISOU 3790  CG  PRO A 489     4645   5208   4656  -1122     28    465       C  
ATOM   3791  CD  PRO A 489      10.779   0.591  18.761  1.00 39.72           C  
ANISOU 3791  CD  PRO A 489     4940   5321   4829  -1216     27    483       C  
ATOM   3792  N   ASN A 490       7.823   1.145  20.630  1.00 45.69           N  
ANISOU 3792  N   ASN A 490     5442   6402   5517  -1327     93    589       N  
ATOM   3793  CA  ASN A 490       6.373   1.176  20.840  1.00 49.03           C  
ANISOU 3793  CA  ASN A 490     5745   6979   5905  -1408    108    632       C  
ATOM   3794  C   ASN A 490       6.007   0.966  22.300  1.00 51.93           C  
ANISOU 3794  C   ASN A 490     6096   7393   6241  -1426    153    676       C  
ATOM   3795  O   ASN A 490       6.701   0.250  23.021  1.00 56.90           O  
ANISOU 3795  O   ASN A 490     6834   7918   6869  -1440    161    683       O  
ATOM   3796  CB  ASN A 490       5.670   0.116  19.967  1.00 38.49           C  
ANISOU 3796  CB  ASN A 490     4425   5650   4550  -1569     72    645       C  
ATOM   3797  CG  ASN A 490       5.894   0.342  18.481  1.00 40.92           C  
ANISOU 3797  CG  ASN A 490     4740   5929   4878  -1555     27    603       C  
ATOM   3798  OD1 ASN A 490       5.409   1.330  17.897  1.00 46.55           O  
ANISOU 3798  OD1 ASN A 490     5345   6744   5598  -1498     22    595       O  
ATOM   3799  ND2 ASN A 490       6.639  -0.560  17.859  1.00 34.42           N  
ANISOU 3799  ND2 ASN A 490     4048   4967   4063  -1599     -5    576       N  
ATOM   3800  N   ASP A 491       4.928   1.605  22.731  1.00 61.96           N  
ANISOU 3800  N   ASP A 491     7230   8825   7486  -1419    182    707       N  
ATOM   3801  CA  ASP A 491       4.357   1.378  24.058  1.00 76.94           C  
ANISOU 3801  CA  ASP A 491     9093  10797   9343  -1451    228    755       C  
ATOM   3802  C   ASP A 491       3.317   0.246  24.018  1.00 80.53           C  
ANISOU 3802  C   ASP A 491     9523  11313   9760  -1635    224    807       C  
ATOM   3803  O   ASP A 491       2.353   0.315  23.260  1.00 79.50           O  
ANISOU 3803  O   ASP A 491     9295  11294   9619  -1703    207    818       O  
ATOM   3804  CB  ASP A 491       3.715   2.672  24.566  1.00 91.61           C  
ANISOU 3804  CB  ASP A 491    10815  12807  11187  -1339    266    762       C  
ATOM   3805  CG  ASP A 491       3.226   2.565  26.003  1.00103.40           C  
ANISOU 3805  CG  ASP A 491    12272  14379  12634  -1346    320    808       C  
ATOM   3806  OD1 ASP A 491       2.846   3.616  26.572  1.00105.67           O  
ANISOU 3806  OD1 ASP A 491    12469  14773  12906  -1236    354    809       O  
ATOM   3807  OD2 ASP A 491       3.221   1.442  26.564  1.00106.91           O  
ANISOU 3807  OD2 ASP A 491    12786  14779  13057  -1459    328    843       O  
ATOM   3808  N   PRO A 492       3.521  -0.810  24.826  1.00 88.94           N  
ANISOU 3808  N   PRO A 492    10684  12307  10804  -1722    236    839       N  
ATOM   3809  CA  PRO A 492       2.614  -1.977  24.867  1.00 90.78           C  
ANISOU 3809  CA  PRO A 492    10915  12578  10998  -1913    231    892       C  
ATOM   3810  C   PRO A 492       1.142  -1.645  25.155  1.00 89.59           C  
ANISOU 3810  C   PRO A 492    10590  12645  10806  -1973    262    943       C  
ATOM   3811  O   PRO A 492       0.768  -1.334  26.288  1.00 88.27           O  
ANISOU 3811  O   PRO A 492    10361  12571  10607  -1938    315    979       O  
ATOM   3812  CB  PRO A 492       3.196  -2.833  25.992  1.00 89.58           C  
ANISOU 3812  CB  PRO A 492    10889  12320  10828  -1945    252    920       C  
ATOM   3813  CG  PRO A 492       4.642  -2.465  26.029  1.00 90.97           C  
ANISOU 3813  CG  PRO A 492    11174  12347  11045  -1799    242    865       C  
ATOM   3814  CD  PRO A 492       4.721  -1.008  25.661  1.00 87.99           C  
ANISOU 3814  CD  PRO A 492    10692  12046  10695  -1648    249    825       C  
ATOM   3815  N   SER A 497      -2.382   4.409  19.904  1.00 93.91           N  
ANISOU 3815  N   SER A 497    10374  13913  11395  -1536    162    835       N  
ATOM   3816  CA  SER A 497      -1.498   5.115  18.980  1.00 90.59           C  
ANISOU 3816  CA  SER A 497    10020  13382  11018  -1424    127    778       C  
ATOM   3817  C   SER A 497      -1.011   4.218  17.840  1.00 84.82           C  
ANISOU 3817  C   SER A 497     9393  12528  10308  -1536     69    753       C  
ATOM   3818  O   SER A 497      -0.889   2.997  18.003  1.00 82.86           O  
ANISOU 3818  O   SER A 497     9225  12206  10051  -1676     60    767       O  
ATOM   3819  CB  SER A 497      -0.290   5.690  19.725  1.00 89.78           C  
ANISOU 3819  CB  SER A 497    10020  13147  10945  -1284    156    746       C  
ATOM   3820  OG  SER A 497      -0.641   6.100  21.035  1.00 94.17           O  
ANISOU 3820  OG  SER A 497    10519  13787  11473  -1221    213    772       O  
ATOM   3821  N   PRO A 498      -0.721   4.831  16.680  1.00 78.16           N  
ANISOU 3821  N   PRO A 498     8554  11657   9488  -1469     30    716       N  
ATOM   3822  CA  PRO A 498      -0.201   4.106  15.515  1.00 72.55           C  
ANISOU 3822  CA  PRO A 498     7943  10829   8793  -1552    -25    685       C  
ATOM   3823  C   PRO A 498       1.123   3.439  15.881  1.00 67.31           C  
ANISOU 3823  C   PRO A 498     7452   9967   8157  -1553    -18    658       C  
ATOM   3824  O   PRO A 498       1.850   3.978  16.715  1.00 67.76           O  
ANISOU 3824  O   PRO A 498     7546   9967   8233  -1440     18    648       O  
ATOM   3825  CB  PRO A 498       0.022   5.214  14.477  1.00 71.64           C  
ANISOU 3825  CB  PRO A 498     7799  10723   8698  -1428    -51    651       C  
ATOM   3826  CG  PRO A 498      -0.811   6.372  14.947  1.00 72.25           C  
ANISOU 3826  CG  PRO A 498     7730  10964   8758  -1319    -21    675       C  
ATOM   3827  CD  PRO A 498      -0.822   6.280  16.438  1.00 74.05           C  
ANISOU 3827  CD  PRO A 498     7953  11206   8975  -1302     37    700       C  
ATOM   3828  N   GLN A 499       1.412   2.286  15.284  1.00 63.14           N  
ANISOU 3828  N   GLN A 499     7026   9336   7627  -1677    -56    646       N  
ATOM   3829  CA  GLN A 499       2.602   1.505  15.608  1.00 57.16           C  
ANISOU 3829  CA  GLN A 499     6434   8395   6889  -1687    -53    623       C  
ATOM   3830  C   GLN A 499       3.793   1.861  14.728  1.00 56.65           C  
ANISOU 3830  C   GLN A 499     6464   8203   6860  -1590    -76    569       C  
ATOM   3831  O   GLN A 499       3.643   2.338  13.611  1.00 53.04           O  
ANISOU 3831  O   GLN A 499     5969   7778   6405  -1565   -108    548       O  
ATOM   3832  CB  GLN A 499       2.320   0.007  15.480  1.00 60.52           C  
ANISOU 3832  CB  GLN A 499     6940   8766   7290  -1869    -80    639       C  
ATOM   3833  CG  GLN A 499       1.325  -0.525  16.504  1.00 64.84           C  
ANISOU 3833  CG  GLN A 499     7420   9415   7801  -1980    -53    699       C  
ATOM   3834  CD  GLN A 499       1.859  -0.418  17.928  1.00 69.30           C  
ANISOU 3834  CD  GLN A 499     8021   9938   8372  -1910      3    716       C  
ATOM   3835  OE1 GLN A 499       1.382   0.402  18.732  1.00 70.52           O  
ANISOU 3835  OE1 GLN A 499     8064  10213   8517  -1836     46    742       O  
ATOM   3836  NE2 GLN A 499       2.870  -1.233  18.240  1.00 62.45           N  
ANISOU 3836  NE2 GLN A 499     7313   8900   7516  -1924      0    701       N  
ATOM   3837  N   TRP A 500       4.984   1.616  15.258  1.00 51.66           N  
ANISOU 3837  N   TRP A 500     5950   7429   6251  -1534    -58    549       N  
ATOM   3838  CA  TRP A 500       6.212   1.821  14.534  1.00 44.27           C  
ANISOU 3838  CA  TRP A 500     5108   6367   5345  -1450    -75    501       C  
ATOM   3839  C   TRP A 500       6.736   0.443  14.109  1.00 45.96           C  
ANISOU 3839  C   TRP A 500     5465   6448   5551  -1548   -104    483       C  
ATOM   3840  O   TRP A 500       7.302  -0.309  14.930  1.00 47.72           O  
ANISOU 3840  O   TRP A 500     5783   6574   5773  -1567    -88    489       O  
ATOM   3841  CB  TRP A 500       7.190   2.552  15.454  1.00 40.69           C  
ANISOU 3841  CB  TRP A 500     4679   5859   4920  -1313    -37    491       C  
ATOM   3842  CG  TRP A 500       8.484   3.021  14.846  1.00 43.13           C  
ANISOU 3842  CG  TRP A 500     5061   6063   5264  -1208    -47    448       C  
ATOM   3843  CD1 TRP A 500       9.117   2.519  13.741  1.00 48.10           C  
ANISOU 3843  CD1 TRP A 500     5774   6604   5898  -1226    -79    415       C  
ATOM   3844  CD2 TRP A 500       9.339   4.040  15.371  1.00 38.99           C  
ANISOU 3844  CD2 TRP A 500     4535   5511   4769  -1071    -23    435       C  
ATOM   3845  NE1 TRP A 500      10.305   3.186  13.530  1.00 45.45           N  
ANISOU 3845  NE1 TRP A 500     5479   6196   5594  -1109    -73    385       N  
ATOM   3846  CE2 TRP A 500      10.465   4.124  14.522  1.00 46.02           C  
ANISOU 3846  CE2 TRP A 500     5501   6303   5684  -1017    -41    397       C  
ATOM   3847  CE3 TRP A 500       9.257   4.901  16.472  1.00 35.52           C  
ANISOU 3847  CE3 TRP A 500     4039   5121   4335   -990     11    451       C  
ATOM   3848  CZ2 TRP A 500      11.504   5.041  14.741  1.00 39.21           C  
ANISOU 3848  CZ2 TRP A 500     4652   5393   4852   -896    -28    379       C  
ATOM   3849  CZ3 TRP A 500      10.285   5.815  16.687  1.00 37.51           C  
ANISOU 3849  CZ3 TRP A 500     4315   5319   4618   -867     21    428       C  
ATOM   3850  CH2 TRP A 500      11.397   5.872  15.828  1.00 36.85           C  
ANISOU 3850  CH2 TRP A 500     4301   5139   4559   -826      1    395       C  
ATOM   3851  N   PRO A 501       6.539   0.086  12.828  1.00 36.95           N  
ANISOU 3851  N   PRO A 501     4345   5297   4397  -1608   -149    460       N  
ATOM   3852  CA  PRO A 501       6.987  -1.247  12.422  1.00 41.70           C  
ANISOU 3852  CA  PRO A 501     5092   5768   4984  -1700   -178    440       C  
ATOM   3853  C   PRO A 501       8.493  -1.268  12.278  1.00 41.21           C  
ANISOU 3853  C   PRO A 501     5149   5562   4949  -1592   -171    399       C  
ATOM   3854  O   PRO A 501       9.074  -0.236  11.946  1.00 40.99           O  
ANISOU 3854  O   PRO A 501     5082   5545   4947  -1469   -161    379       O  
ATOM   3855  CB  PRO A 501       6.371  -1.424  11.035  1.00 43.63           C  
ANISOU 3855  CB  PRO A 501     5317   6054   5205  -1775   -229    422       C  
ATOM   3856  CG  PRO A 501       6.133  -0.024  10.527  1.00 40.43           C  
ANISOU 3856  CG  PRO A 501     4786   5760   4815  -1670   -224    418       C  
ATOM   3857  CD  PRO A 501       6.095   0.909  11.694  1.00 35.30           C  
ANISOU 3857  CD  PRO A 501     4050   5175   4187  -1575   -175    446       C  
ATOM   3858  N   PRO A 502       9.113  -2.427  12.491  1.00 40.41           N  
ANISOU 3858  N   PRO A 502     5189   5328   4838  -1637   -179    389       N  
ATOM   3859  CA  PRO A 502      10.529  -2.636  12.165  1.00 36.00           C  
ANISOU 3859  CA  PRO A 502     4750   4632   4297  -1543   -179    346       C  
ATOM   3860  C   PRO A 502      10.835  -2.418  10.677  1.00 46.92           C  
ANISOU 3860  C   PRO A 502     6150   6002   5677  -1513   -210    303       C  
ATOM   3861  O   PRO A 502      10.024  -2.773   9.827  1.00 50.07           O  
ANISOU 3861  O   PRO A 502     6536   6440   6046  -1610   -246    299       O  
ATOM   3862  CB  PRO A 502      10.746  -4.101  12.483  1.00 37.26           C  
ANISOU 3862  CB  PRO A 502     5056   4670   4432  -1632   -193    347       C  
ATOM   3863  CG  PRO A 502       9.670  -4.458  13.495  1.00 41.92           C  
ANISOU 3863  CG  PRO A 502     5597   5328   5004  -1744   -181    401       C  
ATOM   3864  CD  PRO A 502       8.477  -3.640  13.037  1.00 42.44           C  
ANISOU 3864  CD  PRO A 502     5503   5558   5064  -1782   -189    419       C  
ATOM   3865  N   TYR A 503      11.992  -1.819  10.382  1.00 45.29           N  
ANISOU 3865  N   TYR A 503     5966   5747   5496  -1383   -196    274       N  
ATOM   3866  CA  TYR A 503      12.517  -1.724   9.030  1.00 39.30           C  
ANISOU 3866  CA  TYR A 503     5246   4957   4731  -1344   -219    232       C  
ATOM   3867  C   TYR A 503      12.998  -3.084   8.533  1.00 40.32           C  
ANISOU 3867  C   TYR A 503     5531   4958   4830  -1394   -244    200       C  
ATOM   3868  O   TYR A 503      13.754  -3.746   9.222  1.00 44.59           O  
ANISOU 3868  O   TYR A 503     6169   5399   5376  -1368   -230    197       O  
ATOM   3869  CB  TYR A 503      13.693  -0.744   9.020  1.00 32.44           C  
ANISOU 3869  CB  TYR A 503     4359   4071   3897  -1194   -191    216       C  
ATOM   3870  CG  TYR A 503      14.231  -0.443   7.630  1.00 34.86           C  
ANISOU 3870  CG  TYR A 503     4684   4364   4196  -1144   -207    180       C  
ATOM   3871  CD1 TYR A 503      15.225  -1.229   7.058  1.00 33.73           C  
ANISOU 3871  CD1 TYR A 503     4663   4113   4038  -1115   -214    142       C  
ATOM   3872  CD2 TYR A 503      13.752   0.636   6.898  1.00 35.60           C  
ANISOU 3872  CD2 TYR A 503     4675   4558   4293  -1119   -215    184       C  
ATOM   3873  CE1 TYR A 503      15.728  -0.945   5.792  1.00 35.78           C  
ANISOU 3873  CE1 TYR A 503     4939   4370   4286  -1066   -225    110       C  
ATOM   3874  CE2 TYR A 503      14.237   0.917   5.633  1.00 39.92           C  
ANISOU 3874  CE2 TYR A 503     5241   5097   4829  -1075   -228    155       C  
ATOM   3875  CZ  TYR A 503      15.238   0.129   5.090  1.00 39.53           C  
ANISOU 3875  CZ  TYR A 503     5310   4944   4764  -1049   -231    118       C  
ATOM   3876  OH  TYR A 503      15.731   0.416   3.832  1.00 44.93           O  
ANISOU 3876  OH  TYR A 503     6012   5628   5432  -1002   -241     90       O  
ATOM   3877  N   THR A 504      12.582  -3.480   7.331  1.00 45.06           N  
ANISOU 3877  N   THR A 504     6163   5560   5397  -1458   -284    175       N  
ATOM   3878  CA  THR A 504      12.968  -4.764   6.727  1.00 50.68           C  
ANISOU 3878  CA  THR A 504     7034   6150   6074  -1506   -314    138       C  
ATOM   3879  C   THR A 504      13.427  -4.549   5.289  1.00 50.15           C  
ANISOU 3879  C   THR A 504     6994   6073   5988  -1454   -333     93       C  
ATOM   3880  O   THR A 504      13.026  -3.581   4.652  1.00 42.11           O  
ANISOU 3880  O   THR A 504     5867   5157   4974  -1433   -338     96       O  
ATOM   3881  CB  THR A 504      11.775  -5.758   6.663  1.00 50.54           C  
ANISOU 3881  CB  THR A 504     7052   6135   6017  -1680   -355    152       C  
ATOM   3882  OG1 THR A 504      10.704  -5.158   5.927  1.00 50.06           O  
ANISOU 3882  OG1 THR A 504     6874   6204   5944  -1741   -381    161       O  
ATOM   3883  CG2 THR A 504      11.283  -6.133   8.055  1.00 41.53           C  
ANISOU 3883  CG2 THR A 504     5896   4998   4884  -1749   -337    200       C  
ATOM   3884  N   THR A 505      14.265  -5.441   4.768  1.00 50.95           N  
ANISOU 3884  N   THR A 505     7242   6054   6064  -1429   -345     51       N  
ATOM   3885  CA  THR A 505      14.692  -5.307   3.378  1.00 51.49           C  
ANISOU 3885  CA  THR A 505     7343   6115   6106  -1380   -361      6       C  
ATOM   3886  C   THR A 505      13.506  -5.335   2.401  1.00 53.76           C  
ANISOU 3886  C   THR A 505     7593   6477   6357  -1493   -410      1       C  
ATOM   3887  O   THR A 505      13.503  -4.611   1.398  1.00 55.82           O  
ANISOU 3887  O   THR A 505     7797   6802   6608  -1451   -417    -14       O  
ATOM   3888  CB  THR A 505      15.694  -6.394   2.977  1.00 56.07           C  
ANISOU 3888  CB  THR A 505     8098   6553   6655  -1339   -368    -41       C  
ATOM   3889  OG1 THR A 505      15.173  -7.677   3.330  1.00 60.20           O  
ANISOU 3889  OG1 THR A 505     8737   6990   7147  -1456   -399    -42       O  
ATOM   3890  CG2 THR A 505      17.019  -6.183   3.693  1.00 60.47           C  
ANISOU 3890  CG2 THR A 505     8674   7057   7245  -1201   -320    -40       C  
ATOM   3891  N   ALA A 506      12.494  -6.145   2.703  1.00 47.02           N  
ANISOU 3891  N   ALA A 506     6766   5619   5480  -1639   -444     17       N  
ATOM   3892  CA  ALA A 506      11.357  -6.304   1.801  1.00 51.32           C  
ANISOU 3892  CA  ALA A 506     7281   6232   5985  -1760   -497     12       C  
ATOM   3893  C   ALA A 506      10.438  -5.097   1.782  1.00 59.00           C  
ANISOU 3893  C   ALA A 506     8066   7373   6979  -1767   -494     50       C  
ATOM   3894  O   ALA A 506      10.110  -4.605   0.707  1.00 70.14           O  
ANISOU 3894  O   ALA A 506     9428   8853   8369  -1764   -520     35       O  
ATOM   3895  CB  ALA A 506      10.547  -7.559   2.143  1.00 45.26           C  
ANISOU 3895  CB  ALA A 506     6600   5412   5186  -1926   -537     20       C  
ATOM   3896  N   ALA A 507      10.006  -4.633   2.956  1.00 52.87           N  
ANISOU 3896  N   ALA A 507     7188   6662   6239  -1774   -463     99       N  
ATOM   3897  CA  ALA A 507       9.011  -3.554   3.033  1.00 48.35           C  
ANISOU 3897  CA  ALA A 507     6437   6252   5681  -1783   -461    138       C  
ATOM   3898  C   ALA A 507       9.619  -2.168   3.221  1.00 45.33           C  
ANISOU 3898  C   ALA A 507     5961   5923   5342  -1628   -417    148       C  
ATOM   3899  O   ALA A 507       8.981  -1.162   2.916  1.00 49.37           O  
ANISOU 3899  O   ALA A 507     6344   6556   5858  -1605   -420    167       O  
ATOM   3900  CB  ALA A 507       8.010  -3.827   4.148  1.00 44.87           C  
ANISOU 3900  CB  ALA A 507     5930   5873   5245  -1889   -456    188       C  
ATOM   3901  N   GLN A 508      10.820  -2.114   3.781  1.00 38.30           N  
ANISOU 3901  N   GLN A 508     5131   4940   4481  -1525   -376    137       N  
ATOM   3902  CA  GLN A 508      11.542  -0.847   3.965  1.00 40.18           C  
ANISOU 3902  CA  GLN A 508     5298   5211   4760  -1383   -337    144       C  
ATOM   3903  C   GLN A 508      10.721   0.228   4.655  1.00 37.77           C  
ANISOU 3903  C   GLN A 508     4841   5032   4479  -1368   -319    189       C  
ATOM   3904  O   GLN A 508      10.663   1.372   4.199  1.00 42.61           O  
ANISOU 3904  O   GLN A 508     5367   5720   5104  -1294   -315    194       O  
ATOM   3905  CB  GLN A 508      12.035  -0.302   2.619  1.00 43.53           C  
ANISOU 3905  CB  GLN A 508     5727   5642   5170  -1314   -349    114       C  
ATOM   3906  CG  GLN A 508      13.003  -1.219   1.899  1.00 54.02           C  
ANISOU 3906  CG  GLN A 508     7203   6851   6471  -1297   -358     66       C  
ATOM   3907  CD  GLN A 508      13.225  -0.812   0.451  1.00 58.83           C  
ANISOU 3907  CD  GLN A 508     7816   7485   7052  -1257   -377     38       C  
ATOM   3908  OE1 GLN A 508      13.627   0.319   0.170  1.00 49.02           O  
ANISOU 3908  OE1 GLN A 508     6501   6293   5831  -1163   -356     47       O  
ATOM   3909  NE2 GLN A 508      12.963  -1.736  -0.475  1.00 59.04           N  
ANISOU 3909  NE2 GLN A 508     7931   7473   7027  -1331   -419      3       N  
ATOM   3910  N   GLN A 509      10.100  -0.124   5.760  1.00 39.02           N  
ANISOU 3910  N   GLN A 509     4971   5214   4643  -1432   -308    221       N  
ATOM   3911  CA  GLN A 509       9.231   0.809   6.449  1.00 43.05           C  
ANISOU 3911  CA  GLN A 509     5338   5850   5168  -1420   -290    262       C  
ATOM   3912  C   GLN A 509       9.978   1.693   7.456  1.00 43.65           C  
ANISOU 3912  C   GLN A 509     5384   5913   5286  -1297   -241    274       C  
ATOM   3913  O   GLN A 509      10.867   1.230   8.181  1.00 43.56           O  
ANISOU 3913  O   GLN A 509     5455   5803   5291  -1267   -218    267       O  
ATOM   3914  CB  GLN A 509       8.110   0.045   7.154  1.00 46.33           C  
ANISOU 3914  CB  GLN A 509     5724   6316   5562  -1553   -299    295       C  
ATOM   3915  CG  GLN A 509       7.132  -0.621   6.231  1.00 48.60           C  
ANISOU 3915  CG  GLN A 509     6008   6651   5808  -1686   -351    292       C  
ATOM   3916  CD  GLN A 509       6.162  -1.535   6.980  1.00 51.73           C  
ANISOU 3916  CD  GLN A 509     6394   7080   6182  -1833   -359    327       C  
ATOM   3917  OE1 GLN A 509       6.511  -2.659   7.371  1.00 49.46           O  
ANISOU 3917  OE1 GLN A 509     6227   6680   5884  -1902   -363    321       O  
ATOM   3918  NE2 GLN A 509       4.948  -1.053   7.188  1.00 50.14           N  
ANISOU 3918  NE2 GLN A 509     6048   7034   5971  -1881   -363    366       N  
ATOM   3919  N   TYR A 510       9.593   2.962   7.497  1.00 34.36           N  
ANISOU 3919  N   TYR A 510     4093   4837   4125  -1225   -230    293       N  
ATOM   3920  CA  TYR A 510      10.077   3.880   8.512  1.00 39.86           C  
ANISOU 3920  CA  TYR A 510     4751   5538   4857  -1120   -189    307       C  
ATOM   3921  C   TYR A 510       8.963   4.837   8.861  1.00 41.66           C  
ANISOU 3921  C   TYR A 510     4842   5904   5082  -1103   -183    340       C  
ATOM   3922  O   TYR A 510       7.994   4.937   8.126  1.00 50.59           O  
ANISOU 3922  O   TYR A 510     5906   7127   6189  -1152   -211    348       O  
ATOM   3923  CB  TYR A 510      11.281   4.681   7.977  1.00 32.66           C  
ANISOU 3923  CB  TYR A 510     3871   4567   3970  -1003   -181    282       C  
ATOM   3924  CG  TYR A 510      10.958   5.562   6.784  1.00 34.15           C  
ANISOU 3924  CG  TYR A 510     4001   4824   4150   -968   -204    278       C  
ATOM   3925  CD1 TYR A 510      10.876   5.038   5.487  1.00 33.64           C  
ANISOU 3925  CD1 TYR A 510     3976   4748   4056  -1019   -239    256       C  
ATOM   3926  CD2 TYR A 510      10.732   6.925   6.953  1.00 37.11           C  
ANISOU 3926  CD2 TYR A 510     4288   5270   4543   -882   -192    296       C  
ATOM   3927  CE1 TYR A 510      10.587   5.863   4.389  1.00 34.71           C  
ANISOU 3927  CE1 TYR A 510     4061   4948   4181   -984   -260    254       C  
ATOM   3928  CE2 TYR A 510      10.439   7.756   5.877  1.00 31.73           C  
ANISOU 3928  CE2 TYR A 510     3558   4647   3851   -845   -214    296       C  
ATOM   3929  CZ  TYR A 510      10.375   7.235   4.603  1.00 38.49           C  
ANISOU 3929  CZ  TYR A 510     4450   5496   4678   -896   -247    277       C  
ATOM   3930  OH  TYR A 510      10.093   8.106   3.559  1.00 39.89           O  
ANISOU 3930  OH  TYR A 510     4581   5734   4843   -854   -269    280       O  
ATOM   3931  N   VAL A 511       9.083   5.552   9.973  1.00 40.99           N  
ANISOU 3931  N   VAL A 511     4715   5839   5018  -1029   -147    357       N  
ATOM   3932  CA  VAL A 511       8.045   6.503  10.326  1.00 34.06           C  
ANISOU 3932  CA  VAL A 511     3712   5094   4135   -995   -138    386       C  
ATOM   3933  C   VAL A 511       8.531   7.939  10.261  1.00 43.14           C  
ANISOU 3933  C   VAL A 511     4832   6251   5310   -858   -126    380       C  
ATOM   3934  O   VAL A 511       9.760   8.220  10.310  1.00 41.09           O  
ANISOU 3934  O   VAL A 511     4644   5891   5078   -789   -116    359       O  
ATOM   3935  CB  VAL A 511       7.468   6.228  11.719  1.00 37.17           C  
ANISOU 3935  CB  VAL A 511     4068   5534   4521  -1027   -106    417       C  
ATOM   3936  CG1 VAL A 511       6.772   4.856  11.750  1.00 36.66           C  
ANISOU 3936  CG1 VAL A 511     4021   5481   4426  -1179   -121    432       C  
ATOM   3937  CG2 VAL A 511       8.555   6.316  12.793  1.00 36.21           C  
ANISOU 3937  CG2 VAL A 511     4016   5316   4426   -957    -73    409       C  
ATOM   3938  N   SER A 512       7.561   8.835  10.131  1.00 39.66           N  
ANISOU 3938  N   SER A 512     4283   5928   4856   -821   -131    400       N  
ATOM   3939  CA  SER A 512       7.781  10.266  10.250  1.00 45.88           C  
ANISOU 3939  CA  SER A 512     5035   6735   5662   -691   -119    401       C  
ATOM   3940  C   SER A 512       7.575  10.735  11.698  1.00 44.21           C  
ANISOU 3940  C   SER A 512     4788   6556   5456   -636    -81    418       C  
ATOM   3941  O   SER A 512       6.501  10.531  12.295  1.00 38.13           O  
ANISOU 3941  O   SER A 512     3939   5888   4659   -673    -69    444       O  
ATOM   3942  CB  SER A 512       6.812  11.026   9.333  1.00 48.29           C  
ANISOU 3942  CB  SER A 512     5250   7153   5946   -666   -146    414       C  
ATOM   3943  OG  SER A 512       5.460  10.678   9.612  1.00 49.74           O  
ANISOU 3943  OG  SER A 512     5335   7466   6097   -730   -148    441       O  
ATOM   3944  N   LEU A 513       8.599  11.367  12.258  1.00 37.69           N  
ANISOU 3944  N   LEU A 513     4017   5646   4659   -548    -63    404       N  
ATOM   3945  CA  LEU A 513       8.462  12.039  13.545  1.00 37.09           C  
ANISOU 3945  CA  LEU A 513     3912   5597   4584   -475    -31    415       C  
ATOM   3946  C   LEU A 513       8.165  13.527  13.351  1.00 38.34           C  
ANISOU 3946  C   LEU A 513     4019   5806   4743   -359    -35    417       C  
ATOM   3947  O   LEU A 513       9.057  14.311  12.966  1.00 42.22           O  
ANISOU 3947  O   LEU A 513     4562   6222   5259   -289    -46    401       O  
ATOM   3948  CB  LEU A 513       9.729  11.866  14.394  1.00 37.04           C  
ANISOU 3948  CB  LEU A 513     3997   5471   4604   -449    -12    398       C  
ATOM   3949  CG  LEU A 513      10.149  10.411  14.623  1.00 36.93           C  
ANISOU 3949  CG  LEU A 513     4051   5391   4590   -548     -9    395       C  
ATOM   3950  CD1 LEU A 513      11.436  10.315  15.428  1.00 30.76           C  
ANISOU 3950  CD1 LEU A 513     3356   4499   3833   -509      6    379       C  
ATOM   3951  CD2 LEU A 513       8.997   9.612  15.282  1.00 35.93           C  
ANISOU 3951  CD2 LEU A 513     3871   5351   4430   -633      6    423       C  
ATOM   3952  N   ASN A 514       6.932  13.919  13.650  1.00 40.28           N  
ANISOU 3952  N   ASN A 514     4166   6178   4959   -336    -27    439       N  
ATOM   3953  CA  ASN A 514       6.519  15.317  13.616  1.00 40.23           C  
ANISOU 3953  CA  ASN A 514     4112   6227   4946   -215    -29    444       C  
ATOM   3954  C   ASN A 514       5.336  15.532  14.558  1.00 43.41           C  
ANISOU 3954  C   ASN A 514     4419   6760   5314   -184     -1    467       C  
ATOM   3955  O   ASN A 514       5.015  14.633  15.333  1.00 50.08           O  
ANISOU 3955  O   ASN A 514     5246   7637   6145   -258     23    480       O  
ATOM   3956  CB  ASN A 514       6.194  15.783  12.191  1.00 38.21           C  
ANISOU 3956  CB  ASN A 514     3827   6006   4685   -202    -67    446       C  
ATOM   3957  CG  ASN A 514       5.148  14.910  11.504  1.00 44.81           C  
ANISOU 3957  CG  ASN A 514     4588   6947   5492   -305    -85    464       C  
ATOM   3958  OD1 ASN A 514       4.108  14.553  12.093  1.00 48.09           O  
ANISOU 3958  OD1 ASN A 514     4919   7475   5879   -340    -70    486       O  
ATOM   3959  ND2 ASN A 514       5.412  14.570  10.241  1.00 42.71           N  
ANISOU 3959  ND2 ASN A 514     4351   6648   5228   -357   -120    454       N  
ATOM   3960  N   LEU A 515       4.710  16.709  14.521  1.00 37.08           N  
ANISOU 3960  N   LEU A 515     3561   6032   4496    -73     -2    474       N  
ATOM   3961  CA  LEU A 515       3.616  17.028  15.473  1.00 43.52           C  
ANISOU 3961  CA  LEU A 515     4283   6978   5273    -20     29    494       C  
ATOM   3962  C   LEU A 515       2.412  16.122  15.317  1.00 39.60           C  
ANISOU 3962  C   LEU A 515     3679   6624   4744   -121     32    525       C  
ATOM   3963  O   LEU A 515       1.690  15.911  16.261  1.00 43.21           O  
ANISOU 3963  O   LEU A 515     4070   7177   5171   -125     66    544       O  
ATOM   3964  CB  LEU A 515       3.159  18.487  15.372  1.00 34.77           C  
ANISOU 3964  CB  LEU A 515     3141   5921   4150    131     24    494       C  
ATOM   3965  CG  LEU A 515       4.314  19.485  15.488  1.00 48.36           C  
ANISOU 3965  CG  LEU A 515     4973   7499   5902    228     16    466       C  
ATOM   3966  CD1 LEU A 515       3.798  20.926  15.537  1.00 46.49           C  
ANISOU 3966  CD1 LEU A 515     4714   7308   5645    382     11    466       C  
ATOM   3967  CD2 LEU A 515       5.254  19.171  16.694  1.00 36.65           C  
ANISOU 3967  CD2 LEU A 515     3572   5916   4437    216     44    447       C  
ATOM   3968  N   LYS A 516       2.232  15.564  14.129  1.00 45.19           N  
ANISOU 3968  N   LYS A 516     4371   7345   5454   -209     -5    529       N  
ATOM   3969  CA  LYS A 516       1.132  14.638  13.850  1.00 48.21           C  
ANISOU 3969  CA  LYS A 516     4656   7856   5804   -326    -12    557       C  
ATOM   3970  C   LYS A 516       1.465  13.223  14.323  1.00 47.26           C  
ANISOU 3970  C   LYS A 516     4586   7679   5690   -470      0    560       C  
ATOM   3971  O   LYS A 516       2.614  12.918  14.601  1.00 50.42           O  
ANISOU 3971  O   LYS A 516     5101   7936   6122   -480      7    537       O  
ATOM   3972  CB  LYS A 516       0.845  14.644  12.353  1.00 48.65           C  
ANISOU 3972  CB  LYS A 516     4687   7940   5857   -360    -63    557       C  
ATOM   3973  CG  LYS A 516       0.413  16.014  11.827  1.00 51.52           C  
ANISOU 3973  CG  LYS A 516     4999   8368   6210   -219    -79    560       C  
ATOM   3974  CD  LYS A 516       0.656  16.132  10.321  1.00 62.57           C  
ANISOU 3974  CD  LYS A 516     6426   9731   7617   -236   -131    550       C  
ATOM   3975  CE  LYS A 516       0.026  14.975   9.530  1.00 74.60           C  
ANISOU 3975  CE  LYS A 516     7901  11324   9119   -389   -163    562       C  
ATOM   3976  NZ  LYS A 516       0.272  15.089   8.032  1.00 80.44           N  
ANISOU 3976  NZ  LYS A 516     8674  12030   9860   -402   -214    550       N  
ATOM   3977  N   PRO A 517       0.456  12.353  14.433  1.00 48.79           N  
ANISOU 3977  N   PRO A 517     4696   7990   5853   -584      3    591       N  
ATOM   3978  CA  PRO A 517       0.749  10.998  14.923  1.00 39.13           C  
ANISOU 3978  CA  PRO A 517     3531   6704   4631   -723     14    597       C  
ATOM   3979  C   PRO A 517       1.575  10.241  13.911  1.00 43.02           C  
ANISOU 3979  C   PRO A 517     4130   7067   5150   -808    -26    570       C  
ATOM   3980  O   PRO A 517       1.547  10.590  12.724  1.00 43.69           O  
ANISOU 3980  O   PRO A 517     4206   7156   5237   -792    -65    558       O  
ATOM   3981  CB  PRO A 517      -0.658  10.364  15.061  1.00 40.27           C  
ANISOU 3981  CB  PRO A 517     3548   7021   4731   -830     17    640       C  
ATOM   3982  CG  PRO A 517      -1.582  11.585  15.290  1.00 34.46           C  
ANISOU 3982  CG  PRO A 517     2682   6443   3969   -698     35    658       C  
ATOM   3983  CD  PRO A 517      -1.003  12.624  14.360  1.00 42.18           C  
ANISOU 3983  CD  PRO A 517     3703   7351   4972   -580      4    626       C  
ATOM   3984  N   LEU A 518       2.303   9.226  14.372  1.00 46.39           N  
ANISOU 3984  N   LEU A 518     4657   7380   5589   -889    -17    563       N  
ATOM   3985  CA  LEU A 518       3.210   8.473  13.513  1.00 46.73           C  
ANISOU 3985  CA  LEU A 518     4815   7286   5654   -954    -50    534       C  
ATOM   3986  C   LEU A 518       2.555   8.126  12.190  1.00 46.29           C  
ANISOU 3986  C   LEU A 518     4720   7290   5580  -1036    -98    534       C  
ATOM   3987  O   LEU A 518       1.467   7.559  12.170  1.00 53.40           O  
ANISOU 3987  O   LEU A 518     5540   8302   6447  -1139   -108    563       O  
ATOM   3988  CB  LEU A 518       3.603   7.152  14.169  1.00 40.18           C  
ANISOU 3988  CB  LEU A 518     4072   6372   4824  -1065    -38    538       C  
ATOM   3989  CG  LEU A 518       4.688   7.137  15.226  1.00 45.76           C  
ANISOU 3989  CG  LEU A 518     4871   6961   5553  -1006     -4    526       C  
ATOM   3990  CD1 LEU A 518       5.206   5.717  15.345  1.00 42.65           C  
ANISOU 3990  CD1 LEU A 518     4587   6458   5160  -1121    -12    523       C  
ATOM   3991  CD2 LEU A 518       5.813   8.105  14.887  1.00 39.41           C  
ANISOU 3991  CD2 LEU A 518     4123   6065   4786   -876     -8    491       C  
ATOM   3992  N   GLU A 519       3.230   8.425  11.093  1.00 42.75           N  
ANISOU 3992  N   GLU A 519     4329   6767   5149   -998   -129    504       N  
ATOM   3993  CA  GLU A 519       2.798   7.938   9.796  1.00 44.44           C  
ANISOU 3993  CA  GLU A 519     4534   7009   5342  -1085   -179    497       C  
ATOM   3994  C   GLU A 519       3.857   7.008   9.214  1.00 48.14           C  
ANISOU 3994  C   GLU A 519     5144   7322   5824  -1145   -198    463       C  
ATOM   3995  O   GLU A 519       5.034   7.346   9.202  1.00 50.37           O  
ANISOU 3995  O   GLU A 519     5512   7490   6137  -1063   -186    437       O  
ATOM   3996  CB  GLU A 519       2.529   9.111   8.859  1.00 48.70           C  
ANISOU 3996  CB  GLU A 519     5009   7614   5878   -987   -202    494       C  
ATOM   3997  CG  GLU A 519       2.752   8.786   7.394  1.00 62.14           C  
ANISOU 3997  CG  GLU A 519     6760   9279   7573  -1034   -252    470       C  
ATOM   3998  CD  GLU A 519       2.446   9.969   6.495  1.00 70.43           C  
ANISOU 3998  CD  GLU A 519     7747  10399   8615   -935   -275    473       C  
ATOM   3999  OE1 GLU A 519       1.397  10.617   6.756  1.00 80.07           O  
ANISOU 3999  OE1 GLU A 519     8846  11761   9817   -895   -272    502       O  
ATOM   4000  OE2 GLU A 519       3.242  10.250   5.553  1.00 63.18           O  
ANISOU 4000  OE2 GLU A 519     6901   9398   7707   -895   -295    447       O  
ATOM   4001  N   VAL A 520       3.449   5.838   8.745  1.00 43.80           N  
ANISOU 4001  N   VAL A 520     4622   6770   5250  -1286   -229    463       N  
ATOM   4002  CA  VAL A 520       4.386   4.869   8.187  1.00 42.70           C  
ANISOU 4002  CA  VAL A 520     4624   6484   5116  -1343   -249    428       C  
ATOM   4003  C   VAL A 520       4.635   5.125   6.704  1.00 44.51           C  
ANISOU 4003  C   VAL A 520     4879   6697   5337  -1322   -290    399       C  
ATOM   4004  O   VAL A 520       3.700   5.406   5.949  1.00 45.92           O  
ANISOU 4004  O   VAL A 520     4971   6988   5489  -1351   -324    410       O  
ATOM   4005  CB  VAL A 520       3.873   3.419   8.380  1.00 44.11           C  
ANISOU 4005  CB  VAL A 520     4844   6650   5267  -1510   -267    439       C  
ATOM   4006  CG1 VAL A 520       4.675   2.445   7.533  1.00 36.74           C  
ANISOU 4006  CG1 VAL A 520     4054   5576   4327  -1566   -298    399       C  
ATOM   4007  CG2 VAL A 520       3.919   3.032   9.852  1.00 41.57           C  
ANISOU 4007  CG2 VAL A 520     4533   6308   4953  -1528   -222    465       C  
ATOM   4008  N   ARG A 521       5.899   5.048   6.289  1.00 38.19           N  
ANISOU 4008  N   ARG A 521     4191   5763   4555  -1269   -287    364       N  
ATOM   4009  CA  ARG A 521       6.275   5.264   4.895  1.00 40.12           C  
ANISOU 4009  CA  ARG A 521     4472   5983   4790  -1244   -320    335       C  
ATOM   4010  C   ARG A 521       7.167   4.129   4.425  1.00 39.55           C  
ANISOU 4010  C   ARG A 521     4544   5774   4710  -1297   -333    298       C  
ATOM   4011  O   ARG A 521       7.655   3.328   5.223  1.00 41.28           O  
ANISOU 4011  O   ARG A 521     4839   5906   4940  -1329   -313    294       O  
ATOM   4012  CB  ARG A 521       7.010   6.609   4.718  1.00 46.06           C  
ANISOU 4012  CB  ARG A 521     5209   6722   5571  -1094   -300    331       C  
ATOM   4013  CG  ARG A 521       6.154   7.790   5.111  1.00 45.29           C  
ANISOU 4013  CG  ARG A 521     4982   6750   5476  -1026   -290    364       C  
ATOM   4014  CD  ARG A 521       6.834   9.110   4.822  1.00 42.75           C  
ANISOU 4014  CD  ARG A 521     4658   6407   5178   -889   -278    360       C  
ATOM   4015  NE  ARG A 521       6.079  10.217   5.412  1.00 38.79           N  
ANISOU 4015  NE  ARG A 521     4050   6009   4680   -811   -265    390       N  
ATOM   4016  CZ  ARG A 521       6.588  11.420   5.658  1.00 42.14           C  
ANISOU 4016  CZ  ARG A 521     4470   6412   5128   -688   -245    393       C  
ATOM   4017  NH1 ARG A 521       7.871  11.674   5.380  1.00 36.29           N  
ANISOU 4017  NH1 ARG A 521     3819   5558   4413   -637   -236    372       N  
ATOM   4018  NH2 ARG A 521       5.836  12.354   6.233  1.00 36.70           N  
ANISOU 4018  NH2 ARG A 521     3692   5816   4437   -617   -234    417       N  
ATOM   4019  N   ARG A 522       7.385   4.049   3.126  1.00 41.47           N  
ANISOU 4019  N   ARG A 522     4828   5997   4930  -1301   -367    271       N  
ATOM   4020  CA  ARG A 522       8.165   2.941   2.598  1.00 51.32           C  
ANISOU 4020  CA  ARG A 522     6216   7121   6162  -1347   -381    232       C  
ATOM   4021  C   ARG A 522       9.275   3.466   1.690  1.00 49.87           C  
ANISOU 4021  C   ARG A 522     6087   6876   5984  -1245   -376    203       C  
ATOM   4022  O   ARG A 522       9.053   4.362   0.873  1.00 47.61           O  
ANISOU 4022  O   ARG A 522     5742   6660   5690  -1196   -390    207       O  
ATOM   4023  CB  ARG A 522       7.261   1.956   1.844  1.00 54.68           C  
ANISOU 4023  CB  ARG A 522     6661   7576   6540  -1488   -435    223       C  
ATOM   4024  CG  ARG A 522       6.124   1.347   2.693  1.00 65.47           C  
ANISOU 4024  CG  ARG A 522     7971   9010   7896  -1611   -443    256       C  
ATOM   4025  CD  ARG A 522       5.529   0.101   2.026  1.00 76.55           C  
ANISOU 4025  CD  ARG A 522     9440  10395   9252  -1766   -498    240       C  
ATOM   4026  NE  ARG A 522       6.532  -0.561   1.185  1.00 91.51           N  
ANISOU 4026  NE  ARG A 522    11486  12153  11129  -1752   -514    189       N  
ATOM   4027  CZ  ARG A 522       6.353  -1.699   0.513  1.00100.16           C  
ANISOU 4027  CZ  ARG A 522    12684  13190  12182  -1865   -561    160       C  
ATOM   4028  NH1 ARG A 522       5.192  -2.346   0.575  1.00102.58           N  
ANISOU 4028  NH1 ARG A 522    12956  13560  12459  -2017   -601    179       N  
ATOM   4029  NH2 ARG A 522       7.347  -2.194  -0.224  1.00 98.76           N  
ANISOU 4029  NH2 ARG A 522    12644  12892  11988  -1826   -568    111       N  
ATOM   4030  N   GLY A 523      10.473   2.919   1.849  1.00 43.05           N  
ANISOU 4030  N   GLY A 523     5335   5889   5132  -1210   -354    176       N  
ATOM   4031  CA  GLY A 523      11.577   3.281   0.984  1.00 39.48           C  
ANISOU 4031  CA  GLY A 523     4939   5381   4680  -1122   -346    148       C  
ATOM   4032  C   GLY A 523      12.215   4.583   1.392  1.00 42.53           C  
ANISOU 4032  C   GLY A 523     5267   5784   5108  -1001   -309    167       C  
ATOM   4033  O   GLY A 523      11.632   5.645   1.266  1.00 49.76           O  
ANISOU 4033  O   GLY A 523     6086   6790   6031   -966   -313    192       O  
ATOM   4034  N   LEU A 524      13.436   4.497   1.888  1.00 50.21           N  
ANISOU 4034  N   LEU A 524     6302   6668   6108   -936   -275    156       N  
ATOM   4035  CA  LEU A 524      14.185   5.677   2.292  1.00 49.65           C  
ANISOU 4035  CA  LEU A 524     6189   6599   6077   -828   -242    172       C  
ATOM   4036  C   LEU A 524      14.937   6.197   1.075  1.00 46.02           C  
ANISOU 4036  C   LEU A 524     5752   6130   5605   -768   -244    157       C  
ATOM   4037  O   LEU A 524      16.015   5.699   0.775  1.00 48.85           O  
ANISOU 4037  O   LEU A 524     6190   6412   5958   -739   -230    132       O  
ATOM   4038  CB  LEU A 524      15.164   5.261   3.381  1.00 53.82           C  
ANISOU 4038  CB  LEU A 524     6774   7041   6635   -795   -209    167       C  
ATOM   4039  CG  LEU A 524      15.559   6.254   4.469  1.00 61.70           C  
ANISOU 4039  CG  LEU A 524     7719   8048   7678   -720   -178    191       C  
ATOM   4040  CD1 LEU A 524      14.790   7.576   4.353  1.00 62.75           C  
ANISOU 4040  CD1 LEU A 524     7748   8275   7818   -687   -184    218       C  
ATOM   4041  CD2 LEU A 524      15.356   5.581   5.835  1.00 62.65           C  
ANISOU 4041  CD2 LEU A 524     7854   8140   7810   -756   -164    201       C  
ATOM   4042  N   ARG A 525      14.369   7.175   0.368  1.00 38.97           N  
ANISOU 4042  N   ARG A 525     4789   5317   4702   -747   -260    174       N  
ATOM   4043  CA  ARG A 525      14.924   7.618  -0.920  1.00 42.45           C  
ANISOU 4043  CA  ARG A 525     5251   5759   5120   -704   -267    164       C  
ATOM   4044  C   ARG A 525      15.471   6.444  -1.747  1.00 42.36           C  
ANISOU 4044  C   ARG A 525     5342   5684   5070   -738   -276    123       C  
ATOM   4045  O   ARG A 525      16.631   6.496  -2.215  1.00 35.29           O  
ANISOU 4045  O   ARG A 525     4497   4740   4172   -678   -254    108       O  
ATOM   4046  CB  ARG A 525      16.087   8.580  -0.713  1.00 40.95           C  
ANISOU 4046  CB  ARG A 525     5058   5537   4966   -608   -232    176       C  
ATOM   4047  CG  ARG A 525      15.797   9.725   0.171  1.00 50.99           C  
ANISOU 4047  CG  ARG A 525     6253   6846   6276   -563   -220    209       C  
ATOM   4048  CD  ARG A 525      15.389  10.875  -0.663  1.00 58.54           C  
ANISOU 4048  CD  ARG A 525     7156   7866   7219   -526   -237    232       C  
ATOM   4049  NE  ARG A 525      16.050  12.098  -0.243  1.00 64.72           N  
ANISOU 4049  NE  ARG A 525     7917   8636   8039   -447   -215    255       N  
ATOM   4050  CZ  ARG A 525      15.674  12.830   0.795  1.00 64.71           C  
ANISOU 4050  CZ  ARG A 525     7866   8652   8069   -416   -207    276       C  
ATOM   4051  NH1 ARG A 525      14.648  12.436   1.535  1.00 64.37           N  
ANISOU 4051  NH1 ARG A 525     7783   8650   8024   -455   -215    279       N  
ATOM   4052  NH2 ARG A 525      16.329  13.954   1.086  1.00 65.97           N  
ANISOU 4052  NH2 ARG A 525     8019   8789   8257   -348   -193    294       N  
ATOM   4053  N   ALA A 526      14.654   5.414  -1.936  1.00 29.75           N  
ANISOU 4053  N   ALA A 526     3775   4090   3439   -830   -308    106       N  
ATOM   4054  CA  ALA A 526      15.107   4.163  -2.522  1.00 33.29           C  
ANISOU 4054  CA  ALA A 526     4336   4462   3848   -867   -319     64       C  
ATOM   4055  C   ALA A 526      15.774   4.345  -3.877  1.00 35.16           C  
ANISOU 4055  C   ALA A 526     4616   4695   4048   -819   -321     42       C  
ATOM   4056  O   ALA A 526      16.840   3.803  -4.133  1.00 42.25           O  
ANISOU 4056  O   ALA A 526     5599   5520   4935   -778   -300     13       O  
ATOM   4057  CB  ALA A 526      13.923   3.165  -2.632  1.00 32.67           C  
ANISOU 4057  CB  ALA A 526     4278   4401   3735   -990   -364     53       C  
ATOM   4058  N   GLN A 527      15.154   5.132  -4.733  1.00 31.20           N  
ANISOU 4058  N   GLN A 527     4053   4275   3525   -819   -344     57       N  
ATOM   4059  CA  GLN A 527      15.615   5.311  -6.092  1.00 36.44           C  
ANISOU 4059  CA  GLN A 527     4754   4947   4144   -784   -350     39       C  
ATOM   4060  C   GLN A 527      16.937   6.101  -6.130  1.00 38.92           C  
ANISOU 4060  C   GLN A 527     5067   5237   4483   -678   -302     51       C  
ATOM   4061  O   GLN A 527      17.926   5.704  -6.750  1.00 42.70           O  
ANISOU 4061  O   GLN A 527     5619   5671   4936   -638   -283     25       O  
ATOM   4062  CB  GLN A 527      14.488   6.015  -6.878  1.00 46.06           C  
ANISOU 4062  CB  GLN A 527     5897   6269   5335   -812   -392     61       C  
ATOM   4063  CG  GLN A 527      14.305   5.577  -8.301  1.00 46.52           C  
ANISOU 4063  CG  GLN A 527     6009   6343   5322   -841   -427     31       C  
ATOM   4064  CD  GLN A 527      14.107   4.061  -8.468  1.00 47.12           C  
ANISOU 4064  CD  GLN A 527     6186   6359   5358   -927   -455    -17       C  
ATOM   4065  OE1 GLN A 527      13.549   3.376  -7.599  1.00 46.61           O  
ANISOU 4065  OE1 GLN A 527     6124   6274   5312   -999   -468    -18       O  
ATOM   4066  NE2 GLN A 527      14.570   3.542  -9.598  1.00 42.11           N  
ANISOU 4066  NE2 GLN A 527     5640   5694   4664   -919   -466    -55       N  
ATOM   4067  N   THR A 528      16.972   7.211  -5.434  1.00 35.57           N  
ANISOU 4067  N   THR A 528     4563   4843   4109   -634   -283     91       N  
ATOM   4068  CA  THR A 528      18.187   7.998  -5.398  1.00 33.27           C  
ANISOU 4068  CA  THR A 528     4267   4531   3844   -548   -242    106       C  
ATOM   4069  C   THR A 528      19.309   7.261  -4.642  1.00 35.04           C  
ANISOU 4069  C   THR A 528     4551   4672   4091   -520   -206     86       C  
ATOM   4070  O   THR A 528      20.478   7.311  -5.037  1.00 34.71           O  
ANISOU 4070  O   THR A 528     4543   4604   4043   -463   -176     78       O  
ATOM   4071  CB  THR A 528      17.920   9.344  -4.747  1.00 35.71           C  
ANISOU 4071  CB  THR A 528     4487   4883   4199   -512   -235    151       C  
ATOM   4072  OG1 THR A 528      17.215  10.165  -5.684  1.00 42.43           O  
ANISOU 4072  OG1 THR A 528     5294   5806   5022   -509   -261    173       O  
ATOM   4073  CG2 THR A 528      19.266  10.047  -4.370  1.00 49.78           C  
ANISOU 4073  CG2 THR A 528     6269   6627   6018   -437   -192    168       C  
ATOM   4074  N   CYS A 529      18.957   6.537  -3.589  1.00 31.69           N  
ANISOU 4074  N   CYS A 529     4139   4211   3688   -561   -210     78       N  
ATOM   4075  CA  CYS A 529      19.980   5.826  -2.843  1.00 34.28           C  
ANISOU 4075  CA  CYS A 529     4527   4462   4037   -531   -180     60       C  
ATOM   4076  C   CYS A 529      20.599   4.648  -3.612  1.00 37.78           C  
ANISOU 4076  C   CYS A 529     5076   4848   4431   -528   -179     15       C  
ATOM   4077  O   CYS A 529      21.743   4.284  -3.349  1.00 39.97           O  
ANISOU 4077  O   CYS A 529     5397   5073   4715   -470   -148      2       O  
ATOM   4078  CB  CYS A 529      19.495   5.459  -1.428  1.00 31.24           C  
ANISOU 4078  CB  CYS A 529     4129   4053   3689   -569   -181     70       C  
ATOM   4079  SG  CYS A 529      19.438   6.957  -0.347  1.00 37.11           S  
ANISOU 4079  SG  CYS A 529     4765   4842   4495   -523   -162    117       S  
ATOM   4080  N   ALA A 530      19.863   4.074  -4.566  1.00 34.25           N  
ANISOU 4080  N   ALA A 530     4670   4414   3931   -584   -214     -9       N  
ATOM   4081  CA  ALA A 530      20.446   3.078  -5.459  1.00 33.44           C  
ANISOU 4081  CA  ALA A 530     4673   4260   3772   -571   -215    -55       C  
ATOM   4082  C   ALA A 530      21.559   3.699  -6.297  1.00 39.80           C  
ANISOU 4082  C   ALA A 530     5473   5088   4561   -482   -181    -53       C  
ATOM   4083  O   ALA A 530      22.584   3.056  -6.557  1.00 41.42           O  
ANISOU 4083  O   ALA A 530     5750   5244   4742   -427   -155    -82       O  
ATOM   4084  CB  ALA A 530      19.384   2.440  -6.372  1.00 31.03           C  
ANISOU 4084  CB  ALA A 530     4412   3971   3409   -655   -265    -81       C  
ATOM   4085  N   PHE A 531      21.368   4.948  -6.716  1.00 34.72           N  
ANISOU 4085  N   PHE A 531     4745   4519   3929   -466   -179    -17       N  
ATOM   4086  CA  PHE A 531      22.430   5.651  -7.407  1.00 33.34           C  
ANISOU 4086  CA  PHE A 531     4555   4370   3744   -389   -144     -4       C  
ATOM   4087  C   PHE A 531      23.717   5.776  -6.565  1.00 32.83           C  
ANISOU 4087  C   PHE A 531     4481   4270   3722   -321    -97      6       C  
ATOM   4088  O   PHE A 531      24.803   5.434  -7.027  1.00 34.90           O  
ANISOU 4088  O   PHE A 531     4785   4517   3959   -262    -66    -11       O  
ATOM   4089  CB  PHE A 531      21.944   7.028  -7.843  1.00 37.71           C  
ANISOU 4089  CB  PHE A 531     5022   5000   4306   -389   -153     40       C  
ATOM   4090  CG  PHE A 531      23.037   7.944  -8.293  1.00 37.95           C  
ANISOU 4090  CG  PHE A 531     5022   5056   4339   -319   -115     67       C  
ATOM   4091  CD1 PHE A 531      23.528   7.879  -9.594  1.00 40.59           C  
ANISOU 4091  CD1 PHE A 531     5394   5417   4613   -291   -103     55       C  
ATOM   4092  CD2 PHE A 531      23.569   8.883  -7.423  1.00 42.91           C  
ANISOU 4092  CD2 PHE A 531     5588   5687   5028   -287    -90    106       C  
ATOM   4093  CE1 PHE A 531      24.525   8.712 -10.027  1.00 39.00           C  
ANISOU 4093  CE1 PHE A 531     5161   5245   4410   -235    -66     85       C  
ATOM   4094  CE2 PHE A 531      24.593   9.733  -7.852  1.00 42.04           C  
ANISOU 4094  CE2 PHE A 531     5451   5602   4919   -235    -57    135       C  
ATOM   4095  CZ  PHE A 531      25.063   9.646  -9.160  1.00 42.10           C  
ANISOU 4095  CZ  PHE A 531     5490   5639   4866   -211    -43    127       C  
ATOM   4096  N   TRP A 532      23.604   6.294  -5.354  1.00 32.09           N  
ANISOU 4096  N   TRP A 532     4331   4171   3691   -326    -93     35       N  
ATOM   4097  CA  TRP A 532      24.783   6.504  -4.506  1.00 38.91           C  
ANISOU 4097  CA  TRP A 532     5178   5010   4598   -266    -55     48       C  
ATOM   4098  C   TRP A 532      25.397   5.209  -4.007  1.00 40.76           C  
ANISOU 4098  C   TRP A 532     5491   5173   4824   -246    -43     12       C  
ATOM   4099  O   TRP A 532      26.608   5.092  -3.964  1.00 41.62           O  
ANISOU 4099  O   TRP A 532     5612   5270   4934   -179    -10      8       O  
ATOM   4100  CB  TRP A 532      24.433   7.338  -3.273  1.00 32.86           C  
ANISOU 4100  CB  TRP A 532     4339   4250   3895   -279    -58     84       C  
ATOM   4101  CG  TRP A 532      24.064   8.719  -3.573  1.00 32.05           C  
ANISOU 4101  CG  TRP A 532     4162   4206   3808   -279    -65    123       C  
ATOM   4102  CD1 TRP A 532      22.801   9.247  -3.598  1.00 32.38           C  
ANISOU 4102  CD1 TRP A 532     4163   4286   3853   -322    -96    140       C  
ATOM   4103  CD2 TRP A 532      24.957   9.789  -3.910  1.00 27.56           C  
ANISOU 4103  CD2 TRP A 532     3554   3667   3252   -232    -41    154       C  
ATOM   4104  NE1 TRP A 532      22.860  10.589  -3.910  1.00 27.12           N  
ANISOU 4104  NE1 TRP A 532     3440   3663   3200   -297    -94    178       N  
ATOM   4105  CE2 TRP A 532      24.168  10.945  -4.108  1.00 25.65           C  
ANISOU 4105  CE2 TRP A 532     3257   3468   3020   -248    -61    188       C  
ATOM   4106  CE3 TRP A 532      26.351   9.881  -4.068  1.00 27.27           C  
ANISOU 4106  CE3 TRP A 532     3520   3626   3216   -179     -4    159       C  
ATOM   4107  CZ2 TRP A 532      24.721  12.174  -4.480  1.00 27.36           C  
ANISOU 4107  CZ2 TRP A 532     3435   3714   3247   -218    -48    227       C  
ATOM   4108  CZ3 TRP A 532      26.907  11.118  -4.416  1.00 23.54           C  
ANISOU 4108  CZ3 TRP A 532     2997   3192   2756   -157     10    200       C  
ATOM   4109  CH2 TRP A 532      26.088  12.246  -4.608  1.00 23.00           C  
ANISOU 4109  CH2 TRP A 532     2887   3154   2697   -179    -13    233       C  
ATOM   4110  N   ASN A 533      24.549   4.256  -3.621  1.00 40.90           N  
ANISOU 4110  N   ASN A 533     5562   5147   4833   -304    -72    -12       N  
ATOM   4111  CA  ASN A 533      24.985   3.014  -2.958  1.00 43.39           C  
ANISOU 4111  CA  ASN A 533     5960   5381   5143   -292    -66    -42       C  
ATOM   4112  C   ASN A 533      25.410   1.871  -3.889  1.00 44.99           C  
ANISOU 4112  C   ASN A 533     6273   5539   5281   -267    -66    -91       C  
ATOM   4113  O   ASN A 533      26.315   1.136  -3.558  1.00 42.46           O  
ANISOU 4113  O   ASN A 533     6013   5165   4955   -210    -45   -111       O  
ATOM   4114  CB  ASN A 533      23.898   2.502  -2.002  1.00 31.54           C  
ANISOU 4114  CB  ASN A 533     4472   3848   3664   -372    -96    -40       C  
ATOM   4115  CG  ASN A 533      23.631   3.459  -0.872  1.00 32.26           C  
ANISOU 4115  CG  ASN A 533     4470   3971   3816   -379    -90      3       C  
ATOM   4116  OD1 ASN A 533      24.389   4.397  -0.672  1.00 32.15           O  
ANISOU 4116  OD1 ASN A 533     4396   3986   3833   -322    -65     27       O  
ATOM   4117  ND2 ASN A 533      22.533   3.256  -0.144  1.00 30.17           N  
ANISOU 4117  ND2 ASN A 533     4193   3706   3567   -452   -114     13       N  
ATOM   4118  N   ARG A 534      24.744   1.728  -5.034  1.00 44.75           N  
ANISOU 4118  N   ARG A 534     6273   5531   5200   -307    -91   -111       N  
ATOM   4119  CA  ARG A 534      25.062   0.679  -6.006  1.00 46.78           C  
ANISOU 4119  CA  ARG A 534     6642   5746   5386   -286    -96   -162       C  
ATOM   4120  C   ARG A 534      25.803   1.189  -7.234  1.00 46.10           C  
ANISOU 4120  C   ARG A 534     6542   5716   5257   -218    -69   -165       C  
ATOM   4121  O   ARG A 534      26.707   0.531  -7.715  1.00 49.12           O  
ANISOU 4121  O   ARG A 534     6996   6070   5597   -147    -45   -198       O  
ATOM   4122  CB  ARG A 534      23.803  -0.050  -6.478  1.00 41.86           C  
ANISOU 4122  CB  ARG A 534     6084   5100   4722   -384   -148   -190       C  
ATOM   4123  CG  ARG A 534      23.021  -0.728  -5.363  1.00 44.75           C  
ANISOU 4123  CG  ARG A 534     6477   5409   5117   -464   -176   -187       C  
ATOM   4124  CD  ARG A 534      21.624  -1.117  -5.819  1.00 45.92           C  
ANISOU 4124  CD  ARG A 534     6648   5567   5232   -580   -232   -200       C  
ATOM   4125  NE  ARG A 534      20.801  -1.526  -4.688  1.00 52.84           N  
ANISOU 4125  NE  ARG A 534     7520   6414   6144   -665   -254   -183       N  
ATOM   4126  CZ  ARG A 534      20.682  -2.789  -4.267  1.00 56.39           C  
ANISOU 4126  CZ  ARG A 534     8082   6769   6575   -709   -272   -210       C  
ATOM   4127  NH1 ARG A 534      21.330  -3.779  -4.891  1.00 52.20           N  
ANISOU 4127  NH1 ARG A 534     7685   6159   5991   -670   -274   -259       N  
ATOM   4128  NH2 ARG A 534      19.913  -3.060  -3.222  1.00 53.34           N  
ANISOU 4128  NH2 ARG A 534     7680   6367   6221   -790   -289   -186       N  
ATOM   4129  N   PHE A 535      25.417   2.345  -7.755  1.00 43.65           N  
ANISOU 4129  N   PHE A 535     6144   5486   4955   -237    -72   -131       N  
ATOM   4130  CA  PHE A 535      25.977   2.783  -9.026  1.00 43.56           C  
ANISOU 4130  CA  PHE A 535     6127   5530   4892   -186    -51   -132       C  
ATOM   4131  C   PHE A 535      27.240   3.649  -8.881  1.00 42.73           C  
ANISOU 4131  C   PHE A 535     5950   5468   4816   -105      2    -96       C  
ATOM   4132  O   PHE A 535      28.217   3.389  -9.558  1.00 43.29           O  
ANISOU 4132  O   PHE A 535     6053   5552   4845    -34     37   -113       O  
ATOM   4133  CB  PHE A 535      24.932   3.471  -9.919  1.00 38.89           C  
ANISOU 4133  CB  PHE A 535     5498   5002   4276   -245    -85   -117       C  
ATOM   4134  CG  PHE A 535      25.457   3.833 -11.281  1.00 39.15           C  
ANISOU 4134  CG  PHE A 535     5539   5090   4247   -198    -65   -120       C  
ATOM   4135  CD1 PHE A 535      25.675   2.846 -12.239  1.00 42.86           C  
ANISOU 4135  CD1 PHE A 535     6113   5535   4637   -175    -68   -173       C  
ATOM   4136  CD2 PHE A 535      25.774   5.140 -11.591  1.00 36.56           C  
ANISOU 4136  CD2 PHE A 535     5121   4834   3936   -173    -42    -69       C  
ATOM   4137  CE1 PHE A 535      26.203   3.164 -13.488  1.00 44.76           C  
ANISOU 4137  CE1 PHE A 535     6362   5831   4815   -126    -44   -175       C  
ATOM   4138  CE2 PHE A 535      26.279   5.472 -12.847  1.00 40.37           C  
ANISOU 4138  CE2 PHE A 535     5610   5370   4357   -131    -21    -66       C  
ATOM   4139  CZ  PHE A 535      26.500   4.491 -13.791  1.00 42.05           C  
ANISOU 4139  CZ  PHE A 535     5921   5567   4490   -106    -20   -119       C  
ATOM   4140  N   LEU A 536      27.231   4.660  -8.016  1.00 39.35           N  
ANISOU 4140  N   LEU A 536     5428   5065   4457   -116      9    -48       N  
ATOM   4141  CA  LEU A 536      28.396   5.556  -7.892  1.00 40.66           C  
ANISOU 4141  CA  LEU A 536     5523   5275   4650    -54     53    -10       C  
ATOM   4142  C   LEU A 536      29.743   4.816  -7.726  1.00 45.02           C  
ANISOU 4142  C   LEU A 536     6112   5804   5189     29     94    -33       C  
ATOM   4143  O   LEU A 536      30.715   5.157  -8.400  1.00 52.03           O  
ANISOU 4143  O   LEU A 536     6976   6743   6050     87    132    -21       O  
ATOM   4144  CB  LEU A 536      28.220   6.526  -6.723  1.00 43.54           C  
ANISOU 4144  CB  LEU A 536     5803   5646   5094    -79     48     35       C  
ATOM   4145  CG  LEU A 536      28.900   7.911  -6.692  1.00 54.44           C  
ANISOU 4145  CG  LEU A 536     7094   7082   6508    -56     73     88       C  
ATOM   4146  CD1 LEU A 536      29.512   8.190  -5.299  1.00 56.31           C  
ANISOU 4146  CD1 LEU A 536     7287   7295   6812    -39     85    108       C  
ATOM   4147  CD2 LEU A 536      29.967   8.070  -7.744  1.00 54.67           C  
ANISOU 4147  CD2 LEU A 536     7120   7160   6491     -2    112     94       C  
ATOM   4148  N   PRO A 537      29.815   3.829  -6.807  1.00 47.04           N  
ANISOU 4148  N   PRO A 537     6423   5989   5462     38     87    -60       N  
ATOM   4149  CA  PRO A 537      31.065   3.074  -6.638  1.00 50.08           C  
ANISOU 4149  CA  PRO A 537     6846   6351   5829    127    123    -82       C  
ATOM   4150  C   PRO A 537      31.548   2.459  -7.953  1.00 49.97           C  
ANISOU 4150  C   PRO A 537     6900   6353   5732    184    144   -120       C  
ATOM   4151  O   PRO A 537      32.720   2.611  -8.283  1.00 57.91           O  
ANISOU 4151  O   PRO A 537     7877   7407   6720    265    188   -112       O  
ATOM   4152  CB  PRO A 537      30.678   1.966  -5.647  1.00 46.80           C  
ANISOU 4152  CB  PRO A 537     6509   5843   5430    110     98   -112       C  
ATOM   4153  CG  PRO A 537      29.495   2.519  -4.920  1.00 44.53           C  
ANISOU 4153  CG  PRO A 537     6176   5550   5194     16     62    -86       C  
ATOM   4154  CD  PRO A 537      28.744   3.300  -5.941  1.00 44.61           C  
ANISOU 4154  CD  PRO A 537     6148   5619   5182    -32     47    -72       C  
ATOM   4155  N   LYS A 538      30.672   1.790  -8.691  1.00 47.73           N  
ANISOU 4155  N   LYS A 538     6703   6037   5396    144    112   -159       N  
ATOM   4156  CA  LYS A 538      31.052   1.225  -9.994  1.00 49.05           C  
ANISOU 4156  CA  LYS A 538     6942   6218   5475    197    128   -199       C  
ATOM   4157  C   LYS A 538      31.539   2.287 -10.978  1.00 49.44           C  
ANISOU 4157  C   LYS A 538     6914   6371   5501    223    161   -164       C  
ATOM   4158  O   LYS A 538      32.476   2.063 -11.739  1.00 49.47           O  
ANISOU 4158  O   LYS A 538     6936   6412   5449    305    202   -178       O  
ATOM   4159  CB  LYS A 538      29.907   0.430 -10.599  1.00 49.71           C  
ANISOU 4159  CB  LYS A 538     7130   6249   5508    131     78   -245       C  
ATOM   4160  CG  LYS A 538      29.606  -0.850  -9.841  1.00 53.35           C  
ANISOU 4160  CG  LYS A 538     7699   6602   5972    116     50   -287       C  
ATOM   4161  CD  LYS A 538      28.372  -1.535 -10.393  1.00 60.39           C  
ANISOU 4161  CD  LYS A 538     8683   7446   6818     27     -7   -326       C  
ATOM   4162  CE  LYS A 538      27.823  -2.539  -9.391  1.00 66.54           C  
ANISOU 4162  CE  LYS A 538     9542   8121   7621    -27    -42   -347       C  
ATOM   4163  NZ  LYS A 538      28.521  -3.856  -9.518  1.00 71.46           N  
ANISOU 4163  NZ  LYS A 538    10307   8655   8189     48    -34   -403       N  
ATOM   4164  N   LEU A 539      30.929   3.462 -10.944  1.00 43.91           N  
ANISOU 4164  N   LEU A 539     6126   5717   4840    158    145   -116       N  
ATOM   4165  CA  LEU A 539      31.340   4.520 -11.851  1.00 46.41           C  
ANISOU 4165  CA  LEU A 539     6374   6125   5135    173    173    -76       C  
ATOM   4166  C   LEU A 539      32.694   5.115 -11.471  1.00 52.04           C  
ANISOU 4166  C   LEU A 539     7005   6889   5879    237    227    -36       C  
ATOM   4167  O   LEU A 539      33.458   5.491 -12.347  1.00 54.10           O  
ANISOU 4167  O   LEU A 539     7239   7222   6096    282    267    -20       O  
ATOM   4168  CB  LEU A 539      30.298   5.625 -11.870  1.00 47.96           C  
ANISOU 4168  CB  LEU A 539     6506   6350   5366     90    138    -33       C  
ATOM   4169  CG  LEU A 539      30.520   6.734 -12.881  1.00 49.12           C  
ANISOU 4169  CG  LEU A 539     6597   6582   5485     94    158     10       C  
ATOM   4170  CD1 LEU A 539      30.640   6.106 -14.265  1.00 51.01           C  
ANISOU 4170  CD1 LEU A 539     6911   6847   5626    129    168    -28       C  
ATOM   4171  CD2 LEU A 539      29.367   7.715 -12.822  1.00 48.81           C  
ANISOU 4171  CD2 LEU A 539     6508   6557   5478     18    115     48       C  
ATOM   4172  N   LEU A 540      32.979   5.232 -10.173  1.00 56.05           N  
ANISOU 4172  N   LEU A 540     7471   7367   6460    235    227    -18       N  
ATOM   4173  CA  LEU A 540      34.263   5.789  -9.710  1.00 57.10           C  
ANISOU 4173  CA  LEU A 540     7521   7549   6624    287    270     20       C  
ATOM   4174  C   LEU A 540      35.492   4.991 -10.219  1.00 65.80           C  
ANISOU 4174  C   LEU A 540     8653   8681   7668    391    319     -7       C  
ATOM   4175  O   LEU A 540      36.518   5.595 -10.571  1.00 68.11           O  
ANISOU 4175  O   LEU A 540     8872   9056   7950    432    364     29       O  
ATOM   4176  CB  LEU A 540      34.286   5.975  -8.185  1.00 53.58           C  
ANISOU 4176  CB  LEU A 540     7034   7061   6263    265    255     39       C  
ATOM   4177  CG  LEU A 540      33.503   7.199  -7.662  1.00 57.52           C  
ANISOU 4177  CG  LEU A 540     7465   7565   6824    184    225     85       C  
ATOM   4178  CD1 LEU A 540      33.471   7.254  -6.129  1.00 52.36           C  
ANISOU 4178  CD1 LEU A 540     6785   6865   6244    167    208     95       C  
ATOM   4179  CD2 LEU A 540      34.046   8.528  -8.251  1.00 56.45           C  
ANISOU 4179  CD2 LEU A 540     7246   7512   6692    176    249    142       C  
ATOM   4180  N   SER A 541      35.385   3.661 -10.283  1.00 52.39           N  
ANISOU 4180  N   SER A 541     7061   6918   5928    434    311    -68       N  
ATOM   4181  CA  SER A 541      36.282   2.868 -11.140  1.00 60.42           C  
ANISOU 4181  CA  SER A 541     8130   7963   6863    536    353   -104       C  
ATOM   4182  C   SER A 541      35.628   2.441 -12.475  1.00 75.06           C  
ANISOU 4182  C   SER A 541    10074   9814   8632    528    341   -145       C  
ATOM   4183  O   SER A 541      35.078   1.339 -12.523  1.00 91.00           O  
ANISOU 4183  O   SER A 541    12209  11748  10617    530    311   -203       O  
ATOM   4184  CB  SER A 541      36.671   1.603 -10.391  1.00 57.33           C  
ANISOU 4184  CB  SER A 541     7819   7495   6470    604    352   -151       C  
ATOM   4185  OG  SER A 541      35.561   1.049  -9.693  1.00 50.81           O  
ANISOU 4185  OG  SER A 541     7065   6563   5675    534    297   -176       O  
ATOM   4186  N   ALA A 542      35.698   3.209 -13.572  1.00 69.21           N  
ANISOU 4186  N   ALA A 542     9291   9157   7848    520    362   -119       N  
ATOM   4187  CA  ALA A 542      36.558   4.374 -13.783  1.00 66.98           C  
ANISOU 4187  CA  ALA A 542     8888   8980   7582    532    407    -53       C  
ATOM   4188  C   ALA A 542      35.875   5.723 -13.448  1.00 74.76           C  
ANISOU 4188  C   ALA A 542     9788   9982   8635    429    379      9       C  
ATOM   4189  O   ALA A 542      35.862   6.694 -14.229  1.00 71.80           O  
ANISOU 4189  O   ALA A 542     9362   9677   8241    401    391     52       O  
ATOM   4190  CB  ALA A 542      37.036   4.363 -15.212  1.00 57.00           C  
ANISOU 4190  CB  ALA A 542     7641   7796   6223    585    449    -60       C  
TER    4191      ALA A 542                                                      
ATOM   4192  N   GLU B   4     -16.887   5.450 -69.655  1.00 86.55           N  
ANISOU 4192  N   GLU B   4     9867  12412  10605   1369  -1821  -1696       N  
ATOM   4193  CA  GLU B   4     -15.707   6.241 -69.302  1.00 85.00           C  
ANISOU 4193  CA  GLU B   4     9805  12092  10398   1405  -1745  -1584       C  
ATOM   4194  C   GLU B   4     -16.043   7.454 -68.415  1.00 83.22           C  
ANISOU 4194  C   GLU B   4     9541  11891  10187   1475  -1717  -1577       C  
ATOM   4195  O   GLU B   4     -16.353   8.545 -68.913  1.00 85.33           O  
ANISOU 4195  O   GLU B   4     9847  12170  10403   1635  -1769  -1581       O  
ATOM   4196  CB  GLU B   4     -14.964   6.694 -70.564  1.00 82.57           C  
ANISOU 4196  CB  GLU B   4     9657  11706  10011   1525  -1779  -1527       C  
ATOM   4197  N   ASP B   5     -15.981   7.259 -67.100  1.00 74.92           N  
ANISOU 4197  N   ASP B   5     8424  10841   9200   1359  -1637  -1567       N  
ATOM   4198  CA  ASP B   5     -16.165   8.358 -66.151  1.00 68.79           C  
ANISOU 4198  CA  ASP B   5     7622  10075   8438   1413  -1599  -1555       C  
ATOM   4199  C   ASP B   5     -14.953   9.291 -66.242  1.00 70.89           C  
ANISOU 4199  C   ASP B   5     8062  10202   8669   1481  -1555  -1444       C  
ATOM   4200  O   ASP B   5     -13.837   8.895 -65.917  1.00 76.17           O  
ANISOU 4200  O   ASP B   5     8811  10774   9356   1386  -1483  -1368       O  
ATOM   4201  CB  ASP B   5     -16.338   7.786 -64.740  1.00 63.26           C  
ANISOU 4201  CB  ASP B   5     6816   9410   7812   1256  -1520  -1570       C  
ATOM   4202  CG  ASP B   5     -16.732   8.840 -63.701  1.00 61.33           C  
ANISOU 4202  CG  ASP B   5     6517   9202   7582   1311  -1486  -1579       C  
ATOM   4203  OD1 ASP B   5     -17.260   8.425 -62.633  1.00 50.46           O  
ANISOU 4203  OD1 ASP B   5     5017   7899   6256   1201  -1440  -1621       O  
ATOM   4204  OD2 ASP B   5     -16.487  10.053 -63.938  1.00 59.51           O  
ANISOU 4204  OD2 ASP B   5     6378   8923   7312   1455  -1503  -1542       O  
ATOM   4205  N   PRO B   6     -15.171  10.530 -66.704  1.00 66.52           N  
ANISOU 4205  N   PRO B   6     7573   9641   8061   1646  -1603  -1438       N  
ATOM   4206  CA  PRO B   6     -14.123  11.524 -66.993  1.00 63.43           C  
ANISOU 4206  CA  PRO B   6     7362   9121   7619   1719  -1575  -1338       C  
ATOM   4207  C   PRO B   6     -13.378  11.955 -65.741  1.00 61.96           C  
ANISOU 4207  C   PRO B   6     7206   8861   7473   1645  -1477  -1272       C  
ATOM   4208  O   PRO B   6     -12.242  12.431 -65.839  1.00 63.02           O  
ANISOU 4208  O   PRO B   6     7482   8882   7581   1640  -1430  -1180       O  
ATOM   4209  CB  PRO B   6     -14.907  12.725 -67.542  1.00 69.81           C  
ANISOU 4209  CB  PRO B   6     8200   9960   8363   1910  -1661  -1374       C  
ATOM   4210  CG  PRO B   6     -16.266  12.203 -67.869  1.00 68.89           C  
ANISOU 4210  CG  PRO B   6     7923   9995   8256   1948  -1746  -1494       C  
ATOM   4211  CD  PRO B   6     -16.520  11.057 -66.949  1.00 67.07           C  
ANISOU 4211  CD  PRO B   6     7540   9834   8109   1773  -1691  -1536       C  
ATOM   4212  N   GLN B   7     -14.029  11.819 -64.587  1.00 58.55           N  
ANISOU 4212  N   GLN B   7     6643   8502   7102   1588  -1447  -1322       N  
ATOM   4213  CA  GLN B   7     -13.372  12.038 -63.301  1.00 60.66           C  
ANISOU 4213  CA  GLN B   7     6924   8710   7415   1500  -1353  -1268       C  
ATOM   4214  C   GLN B   7     -12.244  11.050 -63.086  1.00 55.30           C  
ANISOU 4214  C   GLN B   7     6288   7958   6767   1350  -1283  -1205       C  
ATOM   4215  O   GLN B   7     -11.355  11.301 -62.287  1.00 52.25           O  
ANISOU 4215  O   GLN B   7     5959   7494   6401   1290  -1208  -1139       O  
ATOM   4216  CB  GLN B   7     -14.363  11.880 -62.143  1.00 64.90           C  
ANISOU 4216  CB  GLN B   7     7297   9355   8006   1453  -1334  -1344       C  
ATOM   4217  CG  GLN B   7     -15.361  13.024 -62.012  1.00 66.61           C  
ANISOU 4217  CG  GLN B   7     7469   9642   8197   1608  -1387  -1404       C  
ATOM   4218  CD  GLN B   7     -14.692  14.302 -61.588  1.00 65.18           C  
ANISOU 4218  CD  GLN B   7     7423   9353   7990   1682  -1355  -1334       C  
ATOM   4219  OE1 GLN B   7     -13.860  14.304 -60.695  1.00 70.17           O  
ANISOU 4219  OE1 GLN B   7     8096   9911   8655   1585  -1272  -1271       O  
ATOM   4220  NE2 GLN B   7     -15.038  15.392 -62.235  1.00 69.00           N  
ANISOU 4220  NE2 GLN B   7     7983   9822   8411   1855  -1426  -1344       N  
ATOM   4221  N   LEU B   8     -12.311   9.911 -63.774  1.00 51.12           N  
ANISOU 4221  N   LEU B   8     5729   7456   6239   1294  -1311  -1232       N  
ATOM   4222  CA  LEU B   8     -11.361   8.838 -63.548  1.00 54.06           C  
ANISOU 4222  CA  LEU B   8     6133   7768   6640   1159  -1255  -1188       C  
ATOM   4223  C   LEU B   8     -10.288   8.816 -64.627  1.00 52.08           C  
ANISOU 4223  C   LEU B   8     6018   7435   6336   1195  -1260  -1124       C  
ATOM   4224  O   LEU B   8      -9.429   7.944 -64.646  1.00 49.10           O  
ANISOU 4224  O   LEU B   8     5677   7008   5968   1109  -1224  -1091       O  
ATOM   4225  CB  LEU B   8     -12.078   7.490 -63.488  1.00 51.95           C  
ANISOU 4225  CB  LEU B   8     5754   7576   6410   1055  -1278  -1261       C  
ATOM   4226  CG  LEU B   8     -13.078   7.398 -62.337  1.00 50.31           C  
ANISOU 4226  CG  LEU B   8     5404   7459   6253    990  -1258  -1323       C  
ATOM   4227  CD1 LEU B   8     -13.740   6.027 -62.298  1.00 49.95           C  
ANISOU 4227  CD1 LEU B   8     5261   7480   6237    865  -1276  -1390       C  
ATOM   4228  CD2 LEU B   8     -12.361   7.711 -61.040  1.00 44.84           C  
ANISOU 4228  CD2 LEU B   8     4740   6703   5595    924  -1168  -1262       C  
ATOM   4229  N   LEU B   9     -10.348   9.790 -65.523  1.00 51.95           N  
ANISOU 4229  N   LEU B   9     6079   7404   6256   1326  -1306  -1110       N  
ATOM   4230  CA  LEU B   9      -9.343   9.919 -66.563  1.00 52.48           C  
ANISOU 4230  CA  LEU B   9     6282   7399   6260   1363  -1304  -1046       C  
ATOM   4231  C   LEU B   9      -8.427  11.098 -66.287  1.00 51.05           C  
ANISOU 4231  C   LEU B   9     6217   7131   6049   1392  -1250   -961       C  
ATOM   4232  O   LEU B   9      -8.888  12.229 -66.151  1.00 51.58           O  
ANISOU 4232  O   LEU B   9     6311   7192   6093   1481  -1271   -961       O  
ATOM   4233  CB  LEU B   9     -10.006  10.085 -67.922  1.00 55.09           C  
ANISOU 4233  CB  LEU B   9     6638   7770   6525   1482  -1398  -1087       C  
ATOM   4234  CG  LEU B   9      -9.945   8.854 -68.799  1.00 63.59           C  
ANISOU 4234  CG  LEU B   9     7702   8870   7589   1445  -1432  -1118       C  
ATOM   4235  CD1 LEU B   9     -10.582   9.182 -70.149  1.00 67.50           C  
ANISOU 4235  CD1 LEU B   9     8235   9401   8009   1576  -1528  -1154       C  
ATOM   4236  CD2 LEU B   9      -8.466   8.429 -68.961  1.00 64.00           C  
ANISOU 4236  CD2 LEU B   9     7852   8838   7625   1378  -1363  -1041       C  
ATOM   4237  N   VAL B  10      -7.127  10.826 -66.218  1.00 43.84           N  
ANISOU 4237  N   VAL B  10     5374   6151   5131   1317  -1182   -893       N  
ATOM   4238  CA  VAL B  10      -6.144  11.839 -65.911  1.00 45.24           C  
ANISOU 4238  CA  VAL B  10     5657   6250   5284   1315  -1122   -812       C  
ATOM   4239  C   VAL B  10      -4.915  11.715 -66.813  1.00 48.25           C  
ANISOU 4239  C   VAL B  10     6145   6584   5605   1300  -1091   -751       C  
ATOM   4240  O   VAL B  10      -4.461  10.604 -67.093  1.00 46.27           O  
ANISOU 4240  O   VAL B  10     5868   6350   5364   1245  -1080   -760       O  
ATOM   4241  CB  VAL B  10      -5.697  11.706 -64.442  1.00 51.82           C  
ANISOU 4241  CB  VAL B  10     6438   7062   6187   1211  -1047   -793       C  
ATOM   4242  CG1 VAL B  10      -4.527  12.639 -64.138  1.00 46.12           C  
ANISOU 4242  CG1 VAL B  10     5824   6260   5439   1189   -982   -709       C  
ATOM   4243  CG2 VAL B  10      -6.883  11.997 -63.515  1.00 58.87           C  
ANISOU 4243  CG2 VAL B  10     7233   8006   7130   1229  -1068   -850       C  
ATOM   4244  N   ARG B  11      -4.378  12.854 -67.257  1.00 45.35           N  
ANISOU 4244  N   ARG B  11     5903   6160   5170   1348  -1077   -690       N  
ATOM   4245  CA  ARG B  11      -3.111  12.873 -67.981  1.00 45.29           C  
ANISOU 4245  CA  ARG B  11     5994   6113   5100   1317  -1030   -626       C  
ATOM   4246  C   ARG B  11      -1.992  13.426 -67.112  1.00 48.95           C  
ANISOU 4246  C   ARG B  11     6497   6522   5577   1232   -941   -559       C  
ATOM   4247  O   ARG B  11      -2.106  14.519 -66.554  1.00 47.97           O  
ANISOU 4247  O   ARG B  11     6422   6353   5451   1247   -930   -533       O  
ATOM   4248  CB  ARG B  11      -3.211  13.667 -69.281  1.00 47.75           C  
ANISOU 4248  CB  ARG B  11     6432   6403   5309   1415  -1073   -601       C  
ATOM   4249  CG  ARG B  11      -1.861  13.982 -69.907  1.00 58.22           C  
ANISOU 4249  CG  ARG B  11     7874   7688   6561   1373  -1009   -525       C  
ATOM   4250  CD  ARG B  11      -1.964  14.314 -71.397  1.00 68.18           C  
ANISOU 4250  CD  ARG B  11     9248   8944   7713   1459  -1056   -511       C  
ATOM   4251  NE  ARG B  11      -1.509  13.176 -72.190  1.00 81.39           N  
ANISOU 4251  NE  ARG B  11    10891  10667   9366   1440  -1052   -531       N  
ATOM   4252  CZ  ARG B  11      -2.283  12.427 -72.974  1.00 87.50           C  
ANISOU 4252  CZ  ARG B  11    11628  11490  10129   1506  -1128   -592       C  
ATOM   4253  NH1 ARG B  11      -3.576  12.701 -73.120  1.00 82.93           N  
ANISOU 4253  NH1 ARG B  11    11027  10928   9555   1598  -1216   -642       N  
ATOM   4254  NH2 ARG B  11      -1.748  11.401 -73.626  1.00 92.82           N  
ANISOU 4254  NH2 ARG B  11    12284  12200  10783   1483  -1118   -607       N  
ATOM   4255  N   VAL B  12      -0.924  12.643 -66.981  1.00 48.64           N  
ANISOU 4255  N   VAL B  12     6436   6492   5552   1147   -883   -540       N  
ATOM   4256  CA  VAL B  12       0.277  13.067 -66.279  1.00 44.78           C  
ANISOU 4256  CA  VAL B  12     5980   5967   5070   1063   -800   -481       C  
ATOM   4257  C   VAL B  12       1.385  13.111 -67.320  1.00 51.51           C  
ANISOU 4257  C   VAL B  12     6913   6819   5838   1049   -763   -436       C  
ATOM   4258  O   VAL B  12       1.182  12.673 -68.450  1.00 59.69           O  
ANISOU 4258  O   VAL B  12     7971   7884   6824   1104   -802   -454       O  
ATOM   4259  CB  VAL B  12       0.626  12.115 -65.115  1.00 38.60           C  
ANISOU 4259  CB  VAL B  12     5092   5203   4372    977   -762   -502       C  
ATOM   4260  CG1 VAL B  12      -0.393  12.259 -64.014  1.00 44.89           C  
ANISOU 4260  CG1 VAL B  12     5818   5998   5240    978   -784   -538       C  
ATOM   4261  CG2 VAL B  12       0.678  10.669 -65.583  1.00 37.61           C  
ANISOU 4261  CG2 VAL B  12     4908   5124   4259    969   -784   -545       C  
ATOM   4262  N   ARG B  13       2.535  13.654 -66.959  1.00 47.46           N  
ANISOU 4262  N   ARG B  13     6444   6282   5307    975   -689   -380       N  
ATOM   4263  CA  ARG B  13       3.657  13.758 -67.881  1.00 48.06           C  
ANISOU 4263  CA  ARG B  13     6589   6373   5300    948   -641   -337       C  
ATOM   4264  C   ARG B  13       3.961  12.464 -68.654  1.00 44.60           C  
ANISOU 4264  C   ARG B  13     6100   6000   4847    964   -651   -374       C  
ATOM   4265  O   ARG B  13       4.272  12.518 -69.838  1.00 42.29           O  
ANISOU 4265  O   ARG B  13     5874   5727   4469    994   -651   -360       O  
ATOM   4266  CB  ARG B  13       4.913  14.245 -67.150  1.00 52.85           C  
ANISOU 4266  CB  ARG B  13     7206   6968   5908    844   -555   -288       C  
ATOM   4267  CG  ARG B  13       4.863  15.711 -66.710  1.00 66.46           C  
ANISOU 4267  CG  ARG B  13     9024   8616   7610    822   -538   -238       C  
ATOM   4268  CD  ARG B  13       6.269  16.261 -66.483  1.00 78.41           C  
ANISOU 4268  CD  ARG B  13    10577  10128   9088    712   -450   -183       C  
ATOM   4269  NE  ARG B  13       6.255  17.600 -65.886  1.00 89.40           N  
ANISOU 4269  NE  ARG B  13    12061  11439  10469    677   -434   -138       N  
ATOM   4270  CZ  ARG B  13       7.328  18.217 -65.379  1.00 93.35           C  
ANISOU 4270  CZ  ARG B  13    12589  11925  10953    568   -364    -95       C  
ATOM   4271  NH1 ARG B  13       8.518  17.622 -65.389  1.00 96.72           N  
ANISOU 4271  NH1 ARG B  13    12948  12427  11375    489   -300    -93       N  
ATOM   4272  NH2 ARG B  13       7.215  19.433 -64.853  1.00 88.08           N  
ANISOU 4272  NH2 ARG B  13    12018  11173  10274    541   -359    -58       N  
ATOM   4273  N   GLY B  14       3.874  11.311 -67.996  1.00 38.91           N  
ANISOU 4273  N   GLY B  14     5274   5308   4202    944   -661   -422       N  
ATOM   4274  CA  GLY B  14       4.179  10.045 -68.639  1.00 31.49           C  
ANISOU 4274  CA  GLY B  14     4295   4419   3250    961   -675   -462       C  
ATOM   4275  C   GLY B  14       3.145   9.509 -69.612  1.00 39.17           C  
ANISOU 4275  C   GLY B  14     5273   5408   4201   1044   -756   -510       C  
ATOM   4276  O   GLY B  14       3.434   8.611 -70.410  1.00 40.60           O  
ANISOU 4276  O   GLY B  14     5451   5626   4347   1069   -771   -538       O  
ATOM   4277  N   GLY B  15       1.938  10.068 -69.579  1.00 39.01           N  
ANISOU 4277  N   GLY B  15     5262   5363   4195   1092   -813   -524       N  
ATOM   4278  CA  GLY B  15       0.842   9.526 -70.366  1.00 44.06           C  
ANISOU 4278  CA  GLY B  15     5889   6028   4826   1167   -899   -580       C  
ATOM   4279  C   GLY B  15      -0.500   9.550 -69.647  1.00 45.15           C  
ANISOU 4279  C   GLY B  15     5955   6163   5035   1185   -955   -626       C  
ATOM   4280  O   GLY B  15      -0.665  10.245 -68.636  1.00 47.03           O  
ANISOU 4280  O   GLY B  15     6177   6375   5318   1157   -931   -608       O  
ATOM   4281  N   GLN B  16      -1.458   8.784 -70.156  1.00 38.96           N  
ANISOU 4281  N   GLN B  16     5127   5415   4260   1228  -1030   -692       N  
ATOM   4282  CA  GLN B  16      -2.790   8.758 -69.575  1.00 43.21           C  
ANISOU 4282  CA  GLN B  16     5584   5974   4859   1243  -1085   -746       C  
ATOM   4283  C   GLN B  16      -3.012   7.647 -68.556  1.00 41.67           C  
ANISOU 4283  C   GLN B  16     5285   5794   4753   1158  -1077   -789       C  
ATOM   4284  O   GLN B  16      -2.488   6.549 -68.714  1.00 41.16           O  
ANISOU 4284  O   GLN B  16     5212   5734   4694   1117  -1071   -804       O  
ATOM   4285  CB  GLN B  16      -3.835   8.612 -70.679  1.00 53.11           C  
ANISOU 4285  CB  GLN B  16     6840   7269   6071   1334  -1178   -800       C  
ATOM   4286  CG  GLN B  16      -4.022   9.853 -71.508  1.00 65.02           C  
ANISOU 4286  CG  GLN B  16     8449   8759   7497   1433  -1206   -768       C  
ATOM   4287  CD  GLN B  16      -5.467  10.029 -71.894  1.00 77.70           C  
ANISOU 4287  CD  GLN B  16    10015  10410   9099   1524  -1304   -834       C  
ATOM   4288  OE1 GLN B  16      -5.974   9.384 -72.838  1.00 73.50           O  
ANISOU 4288  OE1 GLN B  16     9471   9920   8536   1570  -1372   -885       O  
ATOM   4289  NE2 GLN B  16      -6.164  10.883 -71.139  1.00 85.09           N  
ANISOU 4289  NE2 GLN B  16    10921  11344  10066   1554  -1315   -842       N  
ATOM   4290  N   LEU B  17      -3.827   7.930 -67.538  1.00 34.85           N  
ANISOU 4290  N   LEU B  17     4350   4941   3952   1135  -1082   -812       N  
ATOM   4291  CA  LEU B  17      -4.110   6.972 -66.472  1.00 41.57           C  
ANISOU 4291  CA  LEU B  17     5109   5804   4881   1044  -1070   -849       C  
ATOM   4292  C   LEU B  17      -5.609   6.841 -66.330  1.00 45.44           C  
ANISOU 4292  C   LEU B  17     5508   6353   5404   1060  -1133   -921       C  
ATOM   4293  O   LEU B  17      -6.329   7.823 -66.514  1.00 46.55           O  
ANISOU 4293  O   LEU B  17     5646   6516   5526   1138  -1164   -931       O  
ATOM   4294  CB  LEU B  17      -3.575   7.479 -65.114  1.00 36.84           C  
ANISOU 4294  CB  LEU B  17     4499   5170   4330    981   -997   -805       C  
ATOM   4295  CG  LEU B  17      -2.074   7.713 -64.997  1.00 47.83           C  
ANISOU 4295  CG  LEU B  17     5961   6514   5698    951   -927   -736       C  
ATOM   4296  CD1 LEU B  17      -1.741   8.506 -63.755  1.00 43.31           C  
ANISOU 4296  CD1 LEU B  17     5383   5911   5163    906   -868   -697       C  
ATOM   4297  CD2 LEU B  17      -1.306   6.373 -65.043  1.00 45.58           C  
ANISOU 4297  CD2 LEU B  17     5671   6226   5422    897   -914   -747       C  
ATOM   4298  N   ARG B  18      -6.081   5.659 -65.945  1.00 44.39           N  
ANISOU 4298  N   ARG B  18     5303   6246   5318    983  -1150   -974       N  
ATOM   4299  CA  ARG B  18      -7.498   5.499 -65.583  1.00 44.27           C  
ANISOU 4299  CA  ARG B  18     5179   6301   5342    969  -1196  -1047       C  
ATOM   4300  C   ARG B  18      -7.589   4.977 -64.157  1.00 38.77           C  
ANISOU 4300  C   ARG B  18     4416   5600   4714    851  -1146  -1054       C  
ATOM   4301  O   ARG B  18      -7.092   3.892 -63.860  1.00 42.81           O  
ANISOU 4301  O   ARG B  18     4942   6079   5247    764  -1126  -1051       O  
ATOM   4302  CB  ARG B  18      -8.194   4.515 -66.538  1.00 47.75           C  
ANISOU 4302  CB  ARG B  18     5591   6787   5765    972  -1272  -1116       C  
ATOM   4303  CG  ARG B  18      -9.600   4.110 -66.134  1.00 48.17           C  
ANISOU 4303  CG  ARG B  18     5518   6925   5860    927  -1315  -1200       C  
ATOM   4304  CD  ARG B  18     -10.405   3.657 -67.347  1.00 65.79           C  
ANISOU 4304  CD  ARG B  18     7726   9215   8055    976  -1408  -1270       C  
ATOM   4305  NE  ARG B  18      -9.649   2.683 -68.137  1.00 80.48           N  
ANISOU 4305  NE  ARG B  18     9669  11024   9885    956  -1421  -1259       N  
ATOM   4306  CZ  ARG B  18      -9.372   2.807 -69.431  1.00 85.06           C  
ANISOU 4306  CZ  ARG B  18    10323  11597  10398   1052  -1466  -1255       C  
ATOM   4307  NH1 ARG B  18      -9.809   3.849 -70.125  1.00 82.11           N  
ANISOU 4307  NH1 ARG B  18     9960  11259   9979   1172  -1507  -1257       N  
ATOM   4308  NH2 ARG B  18      -8.665   1.867 -70.037  1.00 93.35           N  
ANISOU 4308  NH2 ARG B  18    11443  12603  11422   1030  -1473  -1250       N  
ATOM   4309  N   GLY B  19      -8.213   5.748 -63.277  1.00 37.32           N  
ANISOU 4309  N   GLY B  19     4170   5448   4561    853  -1126  -1063       N  
ATOM   4310  CA  GLY B  19      -8.381   5.350 -61.892  1.00 40.75           C  
ANISOU 4310  CA  GLY B  19     4541   5887   5054    743  -1076  -1070       C  
ATOM   4311  C   GLY B  19      -9.735   4.673 -61.697  1.00 47.21           C  
ANISOU 4311  C   GLY B  19     5241   6795   5901    686  -1116  -1156       C  
ATOM   4312  O   GLY B  19     -10.423   4.371 -62.670  1.00 45.15           O  
ANISOU 4312  O   GLY B  19     4952   6587   5617    725  -1185  -1210       O  
ATOM   4313  N   ILE B  20     -10.113   4.448 -60.442  1.00 41.95           N  
ANISOU 4313  N   ILE B  20     4506   6151   5280    589  -1072  -1171       N  
ATOM   4314  CA  ILE B  20     -11.339   3.725 -60.111  1.00 42.65           C  
ANISOU 4314  CA  ILE B  20     4479   6331   5396    503  -1094  -1251       C  
ATOM   4315  C   ILE B  20     -12.137   4.499 -59.051  1.00 46.09           C  
ANISOU 4315  C   ILE B  20     4813   6840   5857    500  -1060  -1279       C  
ATOM   4316  O   ILE B  20     -11.553   5.169 -58.205  1.00 48.25           O  
ANISOU 4316  O   ILE B  20     5122   7068   6144    507  -1002  -1226       O  
ATOM   4317  CB  ILE B  20     -11.033   2.286 -59.625  1.00 41.20           C  
ANISOU 4317  CB  ILE B  20     4320   6099   5234    350  -1072  -1249       C  
ATOM   4318  CG1 ILE B  20     -12.296   1.611 -59.082  1.00 43.41           C  
ANISOU 4318  CG1 ILE B  20     4481   6474   5541    233  -1079  -1327       C  
ATOM   4319  CG2 ILE B  20      -9.940   2.274 -58.549  1.00 35.64           C  
ANISOU 4319  CG2 ILE B  20     3688   5304   4549    296   -996  -1176       C  
ATOM   4320  CD1 ILE B  20     -12.157   0.084 -58.908  1.00 41.44           C  
ANISOU 4320  CD1 ILE B  20     4274   6174   5299     83  -1080  -1337       C  
ATOM   4321  N   ARG B  21     -13.463   4.441 -59.121  1.00 46.65           N  
ANISOU 4321  N   ARG B  21     4756   7034   5934    494  -1099  -1366       N  
ATOM   4322  CA  ARG B  21     -14.318   5.133 -58.152  1.00 46.93           C  
ANISOU 4322  CA  ARG B  21     4680   7164   5990    498  -1069  -1407       C  
ATOM   4323  C   ARG B  21     -14.489   4.228 -56.949  1.00 46.64           C  
ANISOU 4323  C   ARG B  21     4594   7140   5989    320  -1006  -1415       C  
ATOM   4324  O   ARG B  21     -14.915   3.089 -57.080  1.00 49.75           O  
ANISOU 4324  O   ARG B  21     4952   7562   6389    202  -1022  -1456       O  
ATOM   4325  CB  ARG B  21     -15.689   5.461 -58.749  1.00 50.17           C  
ANISOU 4325  CB  ARG B  21     4958   7719   6384    574  -1139  -1506       C  
ATOM   4326  CG  ARG B  21     -16.531   6.448 -57.920  1.00 59.28           C  
ANISOU 4326  CG  ARG B  21     6002   8976   7545    632  -1119  -1553       C  
ATOM   4327  CD  ARG B  21     -17.943   6.678 -58.527  1.00 74.50           C  
ANISOU 4327  CD  ARG B  21     7782  11070   9455    712  -1196  -1666       C  
ATOM   4328  NE  ARG B  21     -18.947   5.796 -57.932  1.00 79.30           N  
ANISOU 4328  NE  ARG B  21     8234  11808  10089    563  -1178  -1749       N  
ATOM   4329  CZ  ARG B  21     -20.025   6.219 -57.264  1.00 91.74           C  
ANISOU 4329  CZ  ARG B  21     9652  13537  11670    573  -1166  -1831       C  
ATOM   4330  NH1 ARG B  21     -20.275   7.519 -57.126  1.00 88.64           N  
ANISOU 4330  NH1 ARG B  21     9240  13181  11259    742  -1180  -1846       N  
ATOM   4331  NH2 ARG B  21     -20.875   5.337 -56.745  1.00 99.31           N  
ANISOU 4331  NH2 ARG B  21    10472  14614  12646    413  -1142  -1903       N  
ATOM   4332  N   LEU B  22     -14.134   4.723 -55.775  1.00 45.20           N  
ANISOU 4332  N   LEU B  22     4422   6928   5823    297   -935  -1376       N  
ATOM   4333  CA  LEU B  22     -14.211   3.892 -54.589  1.00 51.76           C  
ANISOU 4333  CA  LEU B  22     5226   7759   6680    129   -872  -1375       C  
ATOM   4334  C   LEU B  22     -15.245   4.484 -53.673  1.00 52.69           C  
ANISOU 4334  C   LEU B  22     5209   8003   6808    121   -838  -1433       C  
ATOM   4335  O   LEU B  22     -15.529   5.682 -53.728  1.00 56.40           O  
ANISOU 4335  O   LEU B  22     5643   8518   7268    259   -851  -1449       O  
ATOM   4336  CB  LEU B  22     -12.862   3.809 -53.870  1.00 48.94           C  
ANISOU 4336  CB  LEU B  22     4999   7263   6332     91   -813  -1280       C  
ATOM   4337  CG  LEU B  22     -11.727   3.027 -54.533  1.00 54.77           C  
ANISOU 4337  CG  LEU B  22     5870   7879   7060     76   -832  -1224       C  
ATOM   4338  CD1 LEU B  22     -10.524   3.021 -53.586  1.00 48.59           C  
ANISOU 4338  CD1 LEU B  22     5187   6988   6287     37   -769  -1144       C  
ATOM   4339  CD2 LEU B  22     -12.121   1.602 -54.914  1.00 53.07           C  
ANISOU 4339  CD2 LEU B  22     5650   7670   6843    -43   -864  -1263       C  
ATOM   4340  N   LYS B  23     -15.816   3.639 -52.830  1.00 56.52           N  
ANISOU 4340  N   LYS B  23     5624   8543   7306    -42   -796  -1467       N  
ATOM   4341  CA  LYS B  23     -16.855   4.082 -51.916  1.00 55.26           C  
ANISOU 4341  CA  LYS B  23     5322   8523   7152    -68   -756  -1532       C  
ATOM   4342  C   LYS B  23     -16.260   4.317 -50.527  1.00 53.45           C  
ANISOU 4342  C   LYS B  23     5143   8232   6932   -124   -669  -1474       C  
ATOM   4343  O   LYS B  23     -15.703   3.408 -49.916  1.00 49.55           O  
ANISOU 4343  O   LYS B  23     4726   7657   6445   -264   -626  -1427       O  
ATOM   4344  CB  LYS B  23     -17.970   3.044 -51.870  1.00 58.02           C  
ANISOU 4344  CB  LYS B  23     5548   8995   7502   -222   -760  -1615       C  
ATOM   4345  CG  LYS B  23     -18.891   3.190 -50.691  1.00 72.56           C  
ANISOU 4345  CG  LYS B  23     7252  10973   9345   -307   -694  -1672       C  
ATOM   4346  CD  LYS B  23     -20.071   2.228 -50.784  1.00 84.51           C  
ANISOU 4346  CD  LYS B  23     8629  12628  10853   -462   -702  -1764       C  
ATOM   4347  CE  LYS B  23     -20.990   2.355 -49.555  1.00 88.23           C  
ANISOU 4347  CE  LYS B  23     8955  13250  11320   -561   -625  -1823       C  
ATOM   4348  NZ  LYS B  23     -21.242   3.781 -49.171  1.00 85.27           N  
ANISOU 4348  NZ  LYS B  23     8505  12952  10940   -384   -613  -1848       N  
ATOM   4349  N   ALA B  24     -16.343   5.556 -50.052  1.00 48.26           N  
ANISOU 4349  N   ALA B  24     4457   7608   6273     -6   -649  -1476       N  
ATOM   4350  CA  ALA B  24     -16.100   5.855 -48.651  1.00 45.56           C  
ANISOU 4350  CA  ALA B  24     4125   7250   5936    -59   -568  -1446       C  
ATOM   4351  C   ALA B  24     -17.470   5.998 -47.967  1.00 50.44           C  
ANISOU 4351  C   ALA B  24     4565   8053   6548   -100   -537  -1543       C  
ATOM   4352  O   ALA B  24     -18.470   6.213 -48.646  1.00 55.30           O  
ANISOU 4352  O   ALA B  24     5058   8799   7155    -35   -588  -1628       O  
ATOM   4353  CB  ALA B  24     -15.286   7.117 -48.523  1.00 43.45           C  
ANISOU 4353  CB  ALA B  24     3947   6896   5665     90   -564  -1389       C  
ATOM   4354  N   PRO B  25     -17.529   5.886 -46.626  1.00 52.29           N  
ANISOU 4354  N   PRO B  25     4780   8306   6781   -205   -455  -1535       N  
ATOM   4355  CA  PRO B  25     -18.862   5.844 -45.990  1.00 49.83           C  
ANISOU 4355  CA  PRO B  25     4289   8186   6458   -271   -418  -1633       C  
ATOM   4356  C   PRO B  25     -19.691   7.085 -46.307  1.00 56.40           C  
ANISOU 4356  C   PRO B  25     5000   9151   7278    -82   -457  -1713       C  
ATOM   4357  O   PRO B  25     -20.917   7.011 -46.427  1.00 64.29           O  
ANISOU 4357  O   PRO B  25     5827  10334   8267    -93   -469  -1817       O  
ATOM   4358  CB  PRO B  25     -18.558   5.801 -44.482  1.00 44.79           C  
ANISOU 4358  CB  PRO B  25     3684   7521   5814   -374   -322  -1595       C  
ATOM   4359  CG  PRO B  25     -17.069   5.436 -44.384  1.00 52.70           C  
ANISOU 4359  CG  PRO B  25     4886   8310   6827   -404   -315  -1477       C  
ATOM   4360  CD  PRO B  25     -16.434   5.973 -45.641  1.00 46.93           C  
ANISOU 4360  CD  PRO B  25     4232   7493   6107   -243   -395  -1445       C  
ATOM   4361  N   GLY B  26     -19.025   8.219 -46.449  1.00 56.09           N  
ANISOU 4361  N   GLY B  26     5054   9020   7237     90   -481  -1668       N  
ATOM   4362  CA  GLY B  26     -19.714   9.469 -46.702  1.00 56.78           C  
ANISOU 4362  CA  GLY B  26     5061   9207   7307    286   -523  -1736       C  
ATOM   4363  C   GLY B  26     -19.916   9.791 -48.171  1.00 58.64           C  
ANISOU 4363  C   GLY B  26     5299   9449   7535    432   -626  -1763       C  
ATOM   4364  O   GLY B  26     -20.613  10.745 -48.488  1.00 62.61           O  
ANISOU 4364  O   GLY B  26     5729  10044   8015    600   -675  -1832       O  
ATOM   4365  N   GLY B  27     -19.321   9.013 -49.071  1.00 52.62           N  
ANISOU 4365  N   GLY B  27     4623   8588   6783    377   -663  -1713       N  
ATOM   4366  CA  GLY B  27     -19.367   9.362 -50.482  1.00 52.79           C  
ANISOU 4366  CA  GLY B  27     4673   8595   6789    520   -760  -1725       C  
ATOM   4367  C   GLY B  27     -18.253   8.743 -51.314  1.00 56.95           C  
ANISOU 4367  C   GLY B  27     5355   8959   7324    481   -784  -1636       C  
ATOM   4368  O   GLY B  27     -17.417   8.007 -50.793  1.00 55.36           O  
ANISOU 4368  O   GLY B  27     5239   8653   7141    346   -730  -1565       O  
ATOM   4369  N   PRO B  28     -18.241   9.023 -52.629  1.00 55.75           N  
ANISOU 4369  N   PRO B  28     5241   8788   7153    606   -869  -1642       N  
ATOM   4370  CA  PRO B  28     -17.254   8.373 -53.495  1.00 49.54           C  
ANISOU 4370  CA  PRO B  28     4588   7867   6368    570   -893  -1568       C  
ATOM   4371  C   PRO B  28     -15.913   9.077 -53.413  1.00 51.14           C  
ANISOU 4371  C   PRO B  28     4962   7904   6565    634   -869  -1462       C  
ATOM   4372  O   PRO B  28     -15.854  10.240 -53.012  1.00 44.94           O  
ANISOU 4372  O   PRO B  28     4202   7106   5768    744   -860  -1452       O  
ATOM   4373  CB  PRO B  28     -17.827   8.569 -54.905  1.00 42.81           C  
ANISOU 4373  CB  PRO B  28     3707   7072   5488    696   -993  -1622       C  
ATOM   4374  CG  PRO B  28     -19.130   9.283 -54.716  1.00 44.11           C  
ANISOU 4374  CG  PRO B  28     3716   7405   5638    795  -1023  -1727       C  
ATOM   4375  CD  PRO B  28     -19.161   9.885 -53.390  1.00 42.33           C  
ANISOU 4375  CD  PRO B  28     3463   7197   5424    785   -950  -1722       C  
ATOM   4376  N   VAL B  29     -14.849   8.376 -53.802  1.00 47.67           N  
ANISOU 4376  N   VAL B  29     4640   7342   6132    566   -861  -1388       N  
ATOM   4377  CA  VAL B  29     -13.548   9.005 -53.959  1.00 46.95           C  
ANISOU 4377  CA  VAL B  29     4705   7107   6029    627   -847  -1293       C  
ATOM   4378  C   VAL B  29     -12.907   8.447 -55.225  1.00 45.13           C  
ANISOU 4378  C   VAL B  29     4560   6806   5780    639   -894  -1259       C  
ATOM   4379  O   VAL B  29     -13.197   7.326 -55.619  1.00 51.80           O  
ANISOU 4379  O   VAL B  29     5367   7682   6633    555   -915  -1290       O  
ATOM   4380  CB  VAL B  29     -12.638   8.756 -52.731  1.00 50.84           C  
ANISOU 4380  CB  VAL B  29     5256   7515   6546    516   -764  -1227       C  
ATOM   4381  CG1 VAL B  29     -13.333   9.226 -51.451  1.00 51.65           C  
ANISOU 4381  CG1 VAL B  29     5268   7695   6661    496   -715  -1267       C  
ATOM   4382  CG2 VAL B  29     -12.315   7.295 -52.625  1.00 54.18           C  
ANISOU 4382  CG2 VAL B  29     5690   7908   6987    363   -745  -1214       C  
ATOM   4383  N   SER B  30     -12.069   9.235 -55.883  1.00 42.63           N  
ANISOU 4383  N   SER B  30     4362   6401   5434    743   -911  -1199       N  
ATOM   4384  CA  SER B  30     -11.314   8.740 -57.024  1.00 49.47           C  
ANISOU 4384  CA  SER B  30     5320   7199   6279    752   -943  -1160       C  
ATOM   4385  C   SER B  30      -9.985   8.141 -56.577  1.00 49.70           C  
ANISOU 4385  C   SER B  30     5440   7122   6323    655   -884  -1083       C  
ATOM   4386  O   SER B  30      -9.187   8.799 -55.913  1.00 53.20           O  
ANISOU 4386  O   SER B  30     5946   7499   6769    659   -835  -1026       O  
ATOM   4387  CB  SER B  30     -11.039   9.871 -58.010  1.00 48.95           C  
ANISOU 4387  CB  SER B  30     5342   7093   6162    905   -987  -1132       C  
ATOM   4388  OG  SER B  30     -12.218  10.621 -58.250  1.00 53.21           O  
ANISOU 4388  OG  SER B  30     5809   7723   6684   1018  -1041  -1201       O  
ATOM   4389  N   ALA B  31      -9.719   6.900 -56.948  1.00 47.97           N  
ANISOU 4389  N   ALA B  31     5232   6886   6110    572   -894  -1085       N  
ATOM   4390  CA  ALA B  31      -8.417   6.324 -56.619  1.00 41.97           C  
ANISOU 4390  CA  ALA B  31     4563   6028   5357    502   -849  -1018       C  
ATOM   4391  C   ALA B  31      -7.611   5.955 -57.875  1.00 43.88           C  
ANISOU 4391  C   ALA B  31     4891   6218   5563    545   -883   -990       C  
ATOM   4392  O   ALA B  31      -8.155   5.420 -58.836  1.00 45.63           O  
ANISOU 4392  O   ALA B  31     5092   6478   5768    565   -940  -1033       O  
ATOM   4393  CB  ALA B  31      -8.595   5.140 -55.709  1.00 38.54           C  
ANISOU 4393  CB  ALA B  31     4091   5598   4955    361   -820  -1037       C  
ATOM   4394  N   PHE B  32      -6.328   6.294 -57.867  1.00 42.74           N  
ANISOU 4394  N   PHE B  32     4839   5996   5404    562   -847   -920       N  
ATOM   4395  CA  PHE B  32      -5.399   5.961 -58.947  1.00 41.94           C  
ANISOU 4395  CA  PHE B  32     4820   5851   5264    597   -865   -889       C  
ATOM   4396  C   PHE B  32      -4.286   5.176 -58.296  1.00 39.79           C  
ANISOU 4396  C   PHE B  32     4592   5518   5007    518   -820   -851       C  
ATOM   4397  O   PHE B  32      -3.402   5.743 -57.661  1.00 36.88           O  
ANISOU 4397  O   PHE B  32     4262   5110   4642    512   -770   -800       O  
ATOM   4398  CB  PHE B  32      -4.857   7.229 -59.621  1.00 39.44           C  
ANISOU 4398  CB  PHE B  32     4572   5511   4903    698   -862   -843       C  
ATOM   4399  CG  PHE B  32      -5.946   8.114 -60.167  1.00 38.72           C  
ANISOU 4399  CG  PHE B  32     4452   5470   4791    792   -911   -879       C  
ATOM   4400  CD1 PHE B  32      -6.643   8.968 -59.331  1.00 41.05           C  
ANISOU 4400  CD1 PHE B  32     4698   5791   5107    812   -900   -895       C  
ATOM   4401  CD2 PHE B  32      -6.317   8.036 -61.503  1.00 42.59           C  
ANISOU 4401  CD2 PHE B  32     4960   5986   5238    867   -974   -905       C  
ATOM   4402  CE1 PHE B  32      -7.666   9.736 -59.827  1.00 45.72           C  
ANISOU 4402  CE1 PHE B  32     5261   6434   5675    913   -953   -937       C  
ATOM   4403  CE2 PHE B  32      -7.339   8.810 -62.008  1.00 46.39           C  
ANISOU 4403  CE2 PHE B  32     5414   6517   5695    965  -1029   -943       C  
ATOM   4404  CZ  PHE B  32      -8.023   9.656 -61.169  1.00 45.64           C  
ANISOU 4404  CZ  PHE B  32     5271   6450   5622    991  -1020   -962       C  
ATOM   4405  N   LEU B  33      -4.382   3.857 -58.418  1.00 39.24           N  
ANISOU 4405  N   LEU B  33     4520   5443   4945    458   -844   -882       N  
ATOM   4406  CA  LEU B  33      -3.524   2.946 -57.712  1.00 38.58           C  
ANISOU 4406  CA  LEU B  33     4479   5305   4875    384   -815   -859       C  
ATOM   4407  C   LEU B  33      -2.516   2.305 -58.664  1.00 43.14           C  
ANISOU 4407  C   LEU B  33     5131   5846   5415    422   -834   -845       C  
ATOM   4408  O   LEU B  33      -2.870   1.970 -59.789  1.00 43.81           O  
ANISOU 4408  O   LEU B  33     5223   5952   5472    463   -885   -876       O  
ATOM   4409  CB  LEU B  33      -4.377   1.865 -57.061  1.00 37.99           C  
ANISOU 4409  CB  LEU B  33     4365   5240   4830    280   -828   -905       C  
ATOM   4410  CG  LEU B  33      -5.579   2.327 -56.235  1.00 35.83           C  
ANISOU 4410  CG  LEU B  33     3998   5028   4589    236   -812   -937       C  
ATOM   4411  CD1 LEU B  33      -6.276   1.131 -55.677  1.00 29.60           C  
ANISOU 4411  CD1 LEU B  33     3183   4246   3818    115   -820   -979       C  
ATOM   4412  CD2 LEU B  33      -5.120   3.249 -55.098  1.00 35.07           C  
ANISOU 4412  CD2 LEU B  33     3902   4914   4510    234   -750   -893       C  
ATOM   4413  N   GLY B  34      -1.265   2.155 -58.213  1.00 38.53           N  
ANISOU 4413  N   GLY B  34     4599   5216   4826    413   -797   -803       N  
ATOM   4414  CA  GLY B  34      -0.254   1.448 -58.984  1.00 41.22           C  
ANISOU 4414  CA  GLY B  34     5003   5532   5129    449   -812   -797       C  
ATOM   4415  C   GLY B  34       0.308   2.222 -60.164  1.00 36.44           C  
ANISOU 4415  C   GLY B  34     4422   4949   4474    539   -811   -775       C  
ATOM   4416  O   GLY B  34       0.572   1.651 -61.197  1.00 42.17           O  
ANISOU 4416  O   GLY B  34     5181   5680   5160    582   -844   -793       O  
ATOM   4417  N   ILE B  35       0.483   3.526 -60.008  1.00 33.94           N  
ANISOU 4417  N   ILE B  35     4098   4645   4154    564   -773   -736       N  
ATOM   4418  CA  ILE B  35       1.112   4.380 -61.006  1.00 31.58           C  
ANISOU 4418  CA  ILE B  35     3837   4360   3801    633   -761   -703       C  
ATOM   4419  C   ILE B  35       2.635   4.235 -60.960  1.00 35.30           C  
ANISOU 4419  C   ILE B  35     4345   4821   4246    631   -718   -670       C  
ATOM   4420  O   ILE B  35       3.263   4.473 -59.925  1.00 34.09           O  
ANISOU 4420  O   ILE B  35     4183   4651   4118    588   -674   -643       O  
ATOM   4421  CB  ILE B  35       0.799   5.865 -60.712  1.00 33.69           C  
ANISOU 4421  CB  ILE B  35     4100   4630   4071    650   -735   -671       C  
ATOM   4422  CG1 ILE B  35      -0.727   6.113 -60.750  1.00 33.27           C  
ANISOU 4422  CG1 ILE B  35     3999   4602   4038    669   -780   -712       C  
ATOM   4423  CG2 ILE B  35       1.497   6.762 -61.702  1.00 26.09           C  
ANISOU 4423  CG2 ILE B  35     3196   3672   3045    706   -718   -631       C  
ATOM   4424  CD1 ILE B  35      -1.171   7.375 -59.978  1.00 25.83           C  
ANISOU 4424  CD1 ILE B  35     3042   3657   3117    675   -755   -693       C  
ATOM   4425  N   PRO B  36       3.249   3.861 -62.093  1.00 36.86           N  
ANISOU 4425  N   PRO B  36     4578   5039   4389    681   -731   -675       N  
ATOM   4426  CA  PRO B  36       4.716   3.694 -62.078  1.00 31.27           C  
ANISOU 4426  CA  PRO B  36     3889   4341   3651    685   -689   -652       C  
ATOM   4427  C   PRO B  36       5.409   5.042 -61.960  1.00 31.64           C  
ANISOU 4427  C   PRO B  36     3945   4400   3677    676   -629   -598       C  
ATOM   4428  O   PRO B  36       5.059   5.959 -62.680  1.00 37.84           O  
ANISOU 4428  O   PRO B  36     4756   5194   4429    704   -628   -578       O  
ATOM   4429  CB  PRO B  36       5.035   3.132 -63.471  1.00 31.29           C  
ANISOU 4429  CB  PRO B  36     3924   4374   3590    749   -716   -676       C  
ATOM   4430  CG  PRO B  36       3.749   3.207 -64.293  1.00 34.17           C  
ANISOU 4430  CG  PRO B  36     4295   4741   3947    782   -772   -702       C  
ATOM   4431  CD  PRO B  36       2.665   3.832 -63.447  1.00 31.35           C  
ANISOU 4431  CD  PRO B  36     3900   4364   3646    743   -777   -698       C  
ATOM   4432  N   PHE B  37       6.390   5.177 -61.083  1.00 31.99           N  
ANISOU 4432  N   PHE B  37     3976   4445   3736    635   -582   -575       N  
ATOM   4433  CA  PHE B  37       7.095   6.438 -61.036  1.00 34.93           C  
ANISOU 4433  CA  PHE B  37     4361   4829   4081    615   -526   -526       C  
ATOM   4434  C   PHE B  37       8.563   6.241 -61.340  1.00 37.23           C  
ANISOU 4434  C   PHE B  37     4649   5171   4327    615   -485   -518       C  
ATOM   4435  O   PHE B  37       9.313   7.201 -61.397  1.00 29.93           O  
ANISOU 4435  O   PHE B  37     3734   4268   3369    586   -433   -480       O  
ATOM   4436  CB  PHE B  37       6.887   7.141 -59.687  1.00 33.27           C  
ANISOU 4436  CB  PHE B  37     4133   4584   3925    558   -500   -503       C  
ATOM   4437  CG  PHE B  37       7.462   6.408 -58.512  1.00 30.81           C  
ANISOU 4437  CG  PHE B  37     3789   4264   3654    518   -489   -515       C  
ATOM   4438  CD1 PHE B  37       8.777   6.615 -58.124  1.00 29.28           C  
ANISOU 4438  CD1 PHE B  37     3584   4098   3444    493   -444   -495       C  
ATOM   4439  CD2 PHE B  37       6.671   5.555 -57.751  1.00 31.69           C  
ANISOU 4439  CD2 PHE B  37     3882   4343   3817    501   -524   -545       C  
ATOM   4440  CE1 PHE B  37       9.307   5.966 -57.000  1.00 31.91           C  
ANISOU 4440  CE1 PHE B  37     3891   4423   3811    465   -441   -508       C  
ATOM   4441  CE2 PHE B  37       7.174   4.894 -56.625  1.00 29.91           C  
ANISOU 4441  CE2 PHE B  37     3641   4100   3622    466   -517   -553       C  
ATOM   4442  CZ  PHE B  37       8.517   5.096 -56.250  1.00 32.92           C  
ANISOU 4442  CZ  PHE B  37     4015   4507   3986    455   -479   -534       C  
ATOM   4443  N   ALA B  38       8.964   4.982 -61.530  1.00 33.47           N  
ANISOU 4443  N   ALA B  38     4160   4715   3843    648   -511   -559       N  
ATOM   4444  CA  ALA B  38      10.329   4.683 -61.893  1.00 35.53           C  
ANISOU 4444  CA  ALA B  38     4406   5040   4054    666   -479   -566       C  
ATOM   4445  C   ALA B  38      10.435   3.485 -62.849  1.00 38.69           C  
ANISOU 4445  C   ALA B  38     4819   5465   4415    739   -521   -614       C  
ATOM   4446  O   ALA B  38       9.558   2.608 -62.887  1.00 37.14           O  
ANISOU 4446  O   ALA B  38     4641   5224   4245    762   -581   -648       O  
ATOM   4447  CB  ALA B  38      11.139   4.430 -60.635  1.00 37.67           C  
ANISOU 4447  CB  ALA B  38     4639   5314   4361    631   -458   -568       C  
ATOM   4448  N   GLU B  39      11.527   3.432 -63.600  1.00 36.82           N  
ANISOU 4448  N   GLU B  39     4574   5305   4113    772   -489   -621       N  
ATOM   4449  CA  GLU B  39      11.877   2.195 -64.275  1.00 36.98           C  
ANISOU 4449  CA  GLU B  39     4601   5355   4095    848   -527   -676       C  
ATOM   4450  C   GLU B  39      12.030   1.075 -63.233  1.00 38.27           C  
ANISOU 4450  C   GLU B  39     4755   5478   4305    858   -566   -712       C  
ATOM   4451  O   GLU B  39      12.690   1.235 -62.219  1.00 37.93           O  
ANISOU 4451  O   GLU B  39     4679   5444   4289    825   -539   -702       O  
ATOM   4452  CB  GLU B  39      13.166   2.368 -65.077  1.00 32.24           C  
ANISOU 4452  CB  GLU B  39     3976   4859   3413    878   -476   -681       C  
ATOM   4453  CG  GLU B  39      13.027   3.323 -66.241  1.00 30.95           C  
ANISOU 4453  CG  GLU B  39     3842   4730   3186    871   -441   -647       C  
ATOM   4454  CD  GLU B  39      12.084   2.808 -67.316  1.00 39.97           C  
ANISOU 4454  CD  GLU B  39     5039   5846   4304    933   -500   -671       C  
ATOM   4455  OE1 GLU B  39      12.497   1.942 -68.124  1.00 41.12           O  
ANISOU 4455  OE1 GLU B  39     5191   6037   4396   1005   -519   -717       O  
ATOM   4456  OE2 GLU B  39      10.924   3.275 -67.362  1.00 40.80           O  
ANISOU 4456  OE2 GLU B  39     5178   5887   4438    916   -529   -650       O  
ATOM   4457  N   PRO B  40      11.420  -0.073 -63.484  1.00 32.46           N  
ANISOU 4457  N   PRO B  40     4060   4695   3576    902   -634   -756       N  
ATOM   4458  CA  PRO B  40      11.580  -1.224 -62.582  1.00 34.09           C  
ANISOU 4458  CA  PRO B  40     4284   4853   3815    915   -677   -791       C  
ATOM   4459  C   PRO B  40      13.066  -1.494 -62.251  1.00 37.24           C  
ANISOU 4459  C   PRO B  40     4649   5319   4181    958   -652   -810       C  
ATOM   4460  O   PRO B  40      13.894  -1.640 -63.137  1.00 39.37           O  
ANISOU 4460  O   PRO B  40     4903   5670   4386   1024   -638   -836       O  
ATOM   4461  CB  PRO B  40      11.022  -2.380 -63.402  1.00 30.82           C  
ANISOU 4461  CB  PRO B  40     3930   4404   3377    973   -748   -842       C  
ATOM   4462  CG  PRO B  40      10.045  -1.710 -64.359  1.00 31.51           C  
ANISOU 4462  CG  PRO B  40     4023   4495   3455    959   -749   -825       C  
ATOM   4463  CD  PRO B  40      10.692  -0.404 -64.713  1.00 32.47           C  
ANISOU 4463  CD  PRO B  40     4102   4692   3543    947   -675   -779       C  
ATOM   4464  N   PRO B  41      13.401  -1.568 -60.962  1.00 34.25           N  
ANISOU 4464  N   PRO B  41     4256   4913   3844    925   -648   -802       N  
ATOM   4465  CA  PRO B  41      14.826  -1.593 -60.593  1.00 35.14           C  
ANISOU 4465  CA  PRO B  41     4318   5106   3927    962   -620   -819       C  
ATOM   4466  C   PRO B  41      15.357  -3.014 -60.596  1.00 39.51           C  
ANISOU 4466  C   PRO B  41     4911   5651   4450   1061   -682   -883       C  
ATOM   4467  O   PRO B  41      15.814  -3.489 -59.552  1.00 41.83           O  
ANISOU 4467  O   PRO B  41     5212   5920   4762   1072   -704   -896       O  
ATOM   4468  CB  PRO B  41      14.809  -1.069 -59.167  1.00 34.70           C  
ANISOU 4468  CB  PRO B  41     4241   5012   3930    885   -599   -784       C  
ATOM   4469  CG  PRO B  41      13.426  -1.519 -58.662  1.00 34.27           C  
ANISOU 4469  CG  PRO B  41     4251   4838   3931    842   -646   -775       C  
ATOM   4470  CD  PRO B  41      12.526  -1.252 -59.823  1.00 27.59           C  
ANISOU 4470  CD  PRO B  41     3422   3988   3072    841   -651   -769       C  
ATOM   4471  N   VAL B  42      15.289  -3.675 -61.747  1.00 39.04           N  
ANISOU 4471  N   VAL B  42     4886   5607   4340   1136   -714   -922       N  
ATOM   4472  CA  VAL B  42      15.576  -5.099 -61.828  1.00 41.42           C  
ANISOU 4472  CA  VAL B  42     5252   5875   4611   1236   -788   -986       C  
ATOM   4473  C   VAL B  42      16.830  -5.391 -62.652  1.00 42.42           C  
ANISOU 4473  C   VAL B  42     5336   6124   4656   1348   -776  -1039       C  
ATOM   4474  O   VAL B  42      17.305  -4.549 -63.401  1.00 42.99           O  
ANISOU 4474  O   VAL B  42     5339   6306   4691   1340   -711  -1025       O  
ATOM   4475  CB  VAL B  42      14.398  -5.860 -62.453  1.00 40.63           C  
ANISOU 4475  CB  VAL B  42     5243   5680   4516   1240   -852  -1004       C  
ATOM   4476  CG1 VAL B  42      13.159  -5.778 -61.527  1.00 41.94           C  
ANISOU 4476  CG1 VAL B  42     5446   5730   4758   1132   -870   -966       C  
ATOM   4477  CG2 VAL B  42      14.109  -5.313 -63.857  1.00 34.08           C  
ANISOU 4477  CG2 VAL B  42     4392   4911   3645   1252   -825   -999       C  
ATOM   4478  N   GLY B  43      17.340  -6.609 -62.540  1.00 44.18           N  
ANISOU 4478  N   GLY B  43     5610   6328   4847   1455   -842  -1102       N  
ATOM   4479  CA  GLY B  43      18.523  -6.980 -63.295  1.00 38.81           C  
ANISOU 4479  CA  GLY B  43     4888   5772   4085   1578   -837  -1164       C  
ATOM   4480  C   GLY B  43      19.671  -6.103 -62.885  1.00 39.94           C  
ANISOU 4480  C   GLY B  43     4907   6052   4217   1560   -762  -1154       C  
ATOM   4481  O   GLY B  43      20.030  -6.048 -61.718  1.00 43.29           O  
ANISOU 4481  O   GLY B  43     5310   6460   4677   1539   -767  -1145       O  
ATOM   4482  N   SER B  44      20.254  -5.413 -63.854  1.00 45.03           N  
ANISOU 4482  N   SER B  44     5469   6834   4805   1564   -693  -1156       N  
ATOM   4483  CA  SER B  44      21.436  -4.589 -63.619  1.00 47.24           C  
ANISOU 4483  CA  SER B  44     5622   7266   5060   1540   -616  -1155       C  
ATOM   4484  C   SER B  44      21.097  -3.377 -62.759  1.00 49.25           C  
ANISOU 4484  C   SER B  44     5842   7488   5383   1390   -561  -1075       C  
ATOM   4485  O   SER B  44      21.990  -2.712 -62.222  1.00 48.80           O  
ANISOU 4485  O   SER B  44     5692   7528   5323   1350   -508  -1070       O  
ATOM   4486  CB  SER B  44      21.978  -4.086 -64.956  1.00 49.61           C  
ANISOU 4486  CB  SER B  44     5859   7712   5279   1554   -548  -1167       C  
ATOM   4487  OG  SER B  44      21.050  -3.153 -65.522  1.00 57.07           O  
ANISOU 4487  OG  SER B  44     6833   8608   6241   1447   -505  -1096       O  
ATOM   4488  N   ARG B  45      19.814  -3.046 -62.661  1.00 43.18           N  
ANISOU 4488  N   ARG B  45     5144   6590   4671   1308   -572  -1018       N  
ATOM   4489  CA  ARG B  45      19.443  -1.886 -61.858  1.00 45.71           C  
ANISOU 4489  CA  ARG B  45     5440   6876   5052   1177   -523   -947       C  
ATOM   4490  C   ARG B  45      19.275  -2.184 -60.360  1.00 45.92           C  
ANISOU 4490  C   ARG B  45     5488   6813   5146   1152   -562   -938       C  
ATOM   4491  O   ARG B  45      19.038  -1.268 -59.572  1.00 46.80           O  
ANISOU 4491  O   ARG B  45     5579   6897   5307   1051   -525   -886       O  
ATOM   4492  CB  ARG B  45      18.189  -1.217 -62.397  1.00 35.05           C  
ANISOU 4492  CB  ARG B  45     4141   5447   3728   1102   -510   -890       C  
ATOM   4493  CG  ARG B  45      18.278  -0.697 -63.830  1.00 42.85           C  
ANISOU 4493  CG  ARG B  45     5118   6515   4647   1108   -465   -883       C  
ATOM   4494  CD  ARG B  45      16.959   0.007 -64.163  1.00 59.09           C  
ANISOU 4494  CD  ARG B  45     7234   8481   6737   1038   -464   -826       C  
ATOM   4495  NE  ARG B  45      16.720   0.301 -65.576  1.00 74.20           N  
ANISOU 4495  NE  ARG B  45     9172  10435   8587   1058   -446   -821       N  
ATOM   4496  CZ  ARG B  45      15.796  -0.303 -66.335  1.00 77.59           C  
ANISOU 4496  CZ  ARG B  45     9668  10804   9009   1106   -503   -839       C  
ATOM   4497  NH1 ARG B  45      15.008  -1.272 -65.841  1.00 66.48           N  
ANISOU 4497  NH1 ARG B  45     8311   9295   7654   1132   -580   -866       N  
ATOM   4498  NH2 ARG B  45      15.662   0.065 -67.607  1.00 79.10           N  
ANISOU 4498  NH2 ARG B  45     9881  11039   9134   1124   -482   -832       N  
ATOM   4499  N   ARG B  46      19.397  -3.446 -59.965  1.00 38.95           N  
ANISOU 4499  N   ARG B  46     4659   5880   4260   1244   -638   -990       N  
ATOM   4500  CA  ARG B  46      19.363  -3.767 -58.550  1.00 39.96           C  
ANISOU 4500  CA  ARG B  46     4815   5931   4438   1226   -675   -984       C  
ATOM   4501  C   ARG B  46      20.489  -3.031 -57.818  1.00 46.46           C  
ANISOU 4501  C   ARG B  46     5535   6860   5258   1200   -626   -982       C  
ATOM   4502  O   ARG B  46      21.631  -2.989 -58.300  1.00 45.72           O  
ANISOU 4502  O   ARG B  46     5357   6908   5106   1260   -600  -1025       O  
ATOM   4503  CB  ARG B  46      19.473  -5.275 -58.322  1.00 41.59           C  
ANISOU 4503  CB  ARG B  46     5109   6071   4623   1341   -768  -1044       C  
ATOM   4504  CG  ARG B  46      19.443  -5.657 -56.845  1.00 42.40           C  
ANISOU 4504  CG  ARG B  46     5258   6085   4766   1325   -810  -1036       C  
ATOM   4505  CD  ARG B  46      19.708  -7.139 -56.652  1.00 47.70           C  
ANISOU 4505  CD  ARG B  46     6030   6693   5402   1449   -905  -1098       C  
ATOM   4506  NE  ARG B  46      18.538  -7.993 -56.890  1.00 43.79           N  
ANISOU 4506  NE  ARG B  46     5667   6050   4919   1437   -964  -1094       N  
ATOM   4507  CZ  ARG B  46      18.593  -9.322 -56.887  1.00 46.65           C  
ANISOU 4507  CZ  ARG B  46     6146   6333   5244   1536  -1052  -1145       C  
ATOM   4508  NH1 ARG B  46      19.759  -9.937 -56.674  1.00 46.39           N  
ANISOU 4508  NH1 ARG B  46     6113   6356   5159   1670  -1094  -1205       N  
ATOM   4509  NH2 ARG B  46      17.504 -10.045 -57.095  1.00 35.64           N  
ANISOU 4509  NH2 ARG B  46     4873   4805   3862   1503  -1102  -1141       N  
ATOM   4510  N   PHE B  47      20.144  -2.458 -56.660  1.00 44.92           N  
ANISOU 4510  N   PHE B  47     5342   6603   5123   1108   -613   -935       N  
ATOM   4511  CA  PHE B  47      21.047  -1.675 -55.808  1.00 38.24           C  
ANISOU 4511  CA  PHE B  47     4408   5837   4286   1061   -570   -926       C  
ATOM   4512  C   PHE B  47      21.326  -0.261 -56.337  1.00 35.31           C  
ANISOU 4512  C   PHE B  47     3953   5559   3904    964   -478   -886       C  
ATOM   4513  O   PHE B  47      21.919   0.536 -55.636  1.00 38.01           O  
ANISOU 4513  O   PHE B  47     4230   5955   4258    898   -437   -870       O  
ATOM   4514  CB  PHE B  47      22.384  -2.407 -55.545  1.00 42.56           C  
ANISOU 4514  CB  PHE B  47     4902   6486   4783   1176   -604   -999       C  
ATOM   4515  CG  PHE B  47      22.220  -3.829 -55.053  1.00 43.61           C  
ANISOU 4515  CG  PHE B  47     5136   6521   4912   1285   -702  -1042       C  
ATOM   4516  CD1 PHE B  47      21.503  -4.099 -53.884  1.00 38.40           C  
ANISOU 4516  CD1 PHE B  47     4564   5721   4305   1241   -742  -1010       C  
ATOM   4517  CD2 PHE B  47      22.772  -4.898 -55.761  1.00 37.56           C  
ANISOU 4517  CD2 PHE B  47     4389   5800   4083   1430   -753  -1114       C  
ATOM   4518  CE1 PHE B  47      21.334  -5.412 -53.421  1.00 42.23           C  
ANISOU 4518  CE1 PHE B  47     5165   6104   4779   1329   -833  -1044       C  
ATOM   4519  CE2 PHE B  47      22.616  -6.219 -55.300  1.00 38.92           C  
ANISOU 4519  CE2 PHE B  47     4679   5865   4245   1530   -851  -1153       C  
ATOM   4520  CZ  PHE B  47      21.889  -6.478 -54.132  1.00 39.58           C  
ANISOU 4520  CZ  PHE B  47     4859   5799   4379   1474   -890  -1114       C  
ATOM   4521  N   MET B  48      20.929   0.037 -57.569  1.00 32.83           N  
ANISOU 4521  N   MET B  48     3649   5265   3562    955   -447   -871       N  
ATOM   4522  CA  MET B  48      21.184   1.354 -58.155  1.00 36.41           C  
ANISOU 4522  CA  MET B  48     4045   5796   3992    862   -362   -830       C  
ATOM   4523  C   MET B  48      20.061   2.374 -57.872  1.00 38.07           C  
ANISOU 4523  C   MET B  48     4308   5900   4258    750   -337   -755       C  
ATOM   4524  O   MET B  48      18.907   1.989 -57.648  1.00 34.12           O  
ANISOU 4524  O   MET B  48     3885   5278   3804    754   -382   -739       O  
ATOM   4525  CB  MET B  48      21.347   1.212 -59.666  1.00 38.68           C  
ANISOU 4525  CB  MET B  48     4326   6162   4210    911   -340   -851       C  
ATOM   4526  CG  MET B  48      22.360   0.142 -60.086  1.00 49.91           C  
ANISOU 4526  CG  MET B  48     5702   7691   5570   1041   -369   -934       C  
ATOM   4527  SD  MET B  48      23.026   0.447 -61.753  1.00 63.83           S  
ANISOU 4527  SD  MET B  48     7409   9611   7232   1064   -303   -956       S  
ATOM   4528  CE  MET B  48      24.259   1.669 -61.264  1.00 62.13           C  
ANISOU 4528  CE  MET B  48     7065   9545   6998    952   -210   -942       C  
ATOM   4529  N   PRO B  49      20.397   3.675 -57.902  1.00 37.91           N  
ANISOU 4529  N   PRO B  49     4248   5929   4228    649   -265   -713       N  
ATOM   4530  CA  PRO B  49      19.397   4.761 -57.765  1.00 37.03           C  
ANISOU 4530  CA  PRO B  49     4192   5724   4156    554   -240   -644       C  
ATOM   4531  C   PRO B  49      18.253   4.544 -58.750  1.00 41.03           C  
ANISOU 4531  C   PRO B  49     4771   6161   4657    588   -266   -631       C  
ATOM   4532  O   PRO B  49      18.506   3.968 -59.801  1.00 38.40           O  
ANISOU 4532  O   PRO B  49     4435   5884   4271    656   -273   -662       O  
ATOM   4533  CB  PRO B  49      20.169   6.021 -58.182  1.00 31.68           C  
ANISOU 4533  CB  PRO B  49     3470   5135   3431    464   -159   -614       C  
ATOM   4534  CG  PRO B  49      21.648   5.682 -57.864  1.00 38.69           C  
ANISOU 4534  CG  PRO B  49     4254   6162   4285    483   -141   -667       C  
ATOM   4535  CD  PRO B  49      21.774   4.179 -58.104  1.00 36.12           C  
ANISOU 4535  CD  PRO B  49     3923   5855   3946    621   -205   -733       C  
ATOM   4536  N   PRO B  50      17.018   5.015 -58.431  1.00 36.75           N  
ANISOU 4536  N   PRO B  50     4290   5507   4166    546   -281   -589       N  
ATOM   4537  CA  PRO B  50      15.919   4.828 -59.382  1.00 33.13           C  
ANISOU 4537  CA  PRO B  50     3892   4994   3701    580   -310   -582       C  
ATOM   4538  C   PRO B  50      16.092   5.733 -60.577  1.00 37.33           C  
ANISOU 4538  C   PRO B  50     4437   5578   4170    557   -261   -553       C  
ATOM   4539  O   PRO B  50      16.750   6.758 -60.456  1.00 40.26           O  
ANISOU 4539  O   PRO B  50     4787   5992   4518    485   -201   -521       O  
ATOM   4540  CB  PRO B  50      14.690   5.274 -58.587  1.00 28.51           C  
ANISOU 4540  CB  PRO B  50     3348   4299   3184    534   -330   -549       C  
ATOM   4541  CG  PRO B  50      15.254   6.273 -57.607  1.00 33.18           C  
ANISOU 4541  CG  PRO B  50     3912   4899   3795    453   -283   -517       C  
ATOM   4542  CD  PRO B  50      16.535   5.612 -57.171  1.00 31.07           C  
ANISOU 4542  CD  PRO B  50     3583   4711   3512    477   -280   -556       C  
ATOM   4543  N   GLU B  51      15.521   5.349 -61.711  1.00 34.24           N  
ANISOU 4543  N   GLU B  51     4086   5181   3745    614   -286   -564       N  
ATOM   4544  CA  GLU B  51      15.473   6.191 -62.889  1.00 38.71           C  
ANISOU 4544  CA  GLU B  51     4686   5776   4246    597   -248   -532       C  
ATOM   4545  C   GLU B  51      14.012   6.448 -63.167  1.00 37.88           C  
ANISOU 4545  C   GLU B  51     4650   5573   4168    608   -291   -510       C  
ATOM   4546  O   GLU B  51      13.152   5.612 -62.856  1.00 34.75           O  
ANISOU 4546  O   GLU B  51     4264   5118   3823    649   -353   -538       O  
ATOM   4547  CB  GLU B  51      16.099   5.486 -64.101  1.00 43.14           C  
ANISOU 4547  CB  GLU B  51     5233   6428   4729    668   -244   -572       C  
ATOM   4548  CG  GLU B  51      17.589   5.240 -63.970  1.00 58.65           C  
ANISOU 4548  CG  GLU B  51     7115   8515   6652    668   -200   -604       C  
ATOM   4549  CD  GLU B  51      18.139   4.400 -65.124  1.00 81.65           C  
ANISOU 4549  CD  GLU B  51    10012  11521   9489    757   -204   -655       C  
ATOM   4550  OE1 GLU B  51      17.331   3.790 -65.875  1.00 85.53           O  
ANISOU 4550  OE1 GLU B  51    10560  11966   9970    826   -255   -672       O  
ATOM   4551  OE2 GLU B  51      19.387   4.353 -65.287  1.00 91.57           O  
ANISOU 4551  OE2 GLU B  51    11195  12906  10691    760   -156   -684       O  
ATOM   4552  N   PRO B  52      13.721   7.607 -63.751  1.00 36.83           N  
ANISOU 4552  N   PRO B  52     4568   5426   3999    570   -260   -462       N  
ATOM   4553  CA  PRO B  52      12.344   8.039 -64.029  1.00 33.95           C  
ANISOU 4553  CA  PRO B  52     4268   4978   3654    587   -302   -441       C  
ATOM   4554  C   PRO B  52      11.663   7.085 -64.999  1.00 35.72           C  
ANISOU 4554  C   PRO B  52     4511   5201   3858    672   -360   -481       C  
ATOM   4555  O   PRO B  52      12.301   6.605 -65.951  1.00 38.36           O  
ANISOU 4555  O   PRO B  52     4844   5604   4128    713   -350   -502       O  
ATOM   4556  CB  PRO B  52      12.531   9.399 -64.710  1.00 38.55           C  
ANISOU 4556  CB  PRO B  52     4913   5564   4170    542   -253   -385       C  
ATOM   4557  CG  PRO B  52      13.914   9.902 -64.186  1.00 44.13           C  
ANISOU 4557  CG  PRO B  52     5577   6334   4857    458   -178   -367       C  
ATOM   4558  CD  PRO B  52      14.740   8.630 -64.055  1.00 39.23           C  
ANISOU 4558  CD  PRO B  52     4871   5793   4240    500   -183   -424       C  
ATOM   4559  N   LYS B  53      10.381   6.845 -64.777  1.00 34.67           N  
ANISOU 4559  N   LYS B  53     4396   4999   3778    697   -420   -494       N  
ATOM   4560  CA  LYS B  53       9.581   5.960 -65.633  1.00 39.86           C  
ANISOU 4560  CA  LYS B  53     5073   5649   4424    768   -485   -535       C  
ATOM   4561  C   LYS B  53       9.444   6.528 -67.031  1.00 39.99           C  
ANISOU 4561  C   LYS B  53     5147   5689   4357    805   -482   -517       C  
ATOM   4562  O   LYS B  53       9.121   7.705 -67.199  1.00 43.77           O  
ANISOU 4562  O   LYS B  53     5673   6142   4815    783   -464   -471       O  
ATOM   4563  CB  LYS B  53       8.186   5.738 -65.018  1.00 33.22           C  
ANISOU 4563  CB  LYS B  53     4228   4739   3657    768   -544   -552       C  
ATOM   4564  CG  LYS B  53       7.161   5.038 -65.928  1.00 35.18           C  
ANISOU 4564  CG  LYS B  53     4498   4977   3893    829   -615   -594       C  
ATOM   4565  CD  LYS B  53       7.477   3.525 -66.066  1.00 39.83           C  
ANISOU 4565  CD  LYS B  53     5072   5578   4482    861   -650   -649       C  
ATOM   4566  CE  LYS B  53       6.508   2.826 -67.015  1.00 40.34           C  
ANISOU 4566  CE  LYS B  53     5163   5634   4530    914   -722   -693       C  
ATOM   4567  NZ  LYS B  53       6.890   2.999 -68.442  1.00 42.65           N  
ANISOU 4567  NZ  LYS B  53     5496   5974   4733    974   -718   -692       N  
ATOM   4568  N   ARG B  54       9.703   5.700 -68.036  1.00 36.48           N  
ANISOU 4568  N   ARG B  54     4711   5289   3859    864   -501   -553       N  
ATOM   4569  CA  ARG B  54       9.545   6.125 -69.419  1.00 36.78           C  
ANISOU 4569  CA  ARG B  54     4811   5352   3811    906   -503   -540       C  
ATOM   4570  C   ARG B  54       8.059   6.315 -69.703  1.00 39.03           C  
ANISOU 4570  C   ARG B  54     5134   5577   4119    942   -574   -546       C  
ATOM   4571  O   ARG B  54       7.205   5.603 -69.157  1.00 39.24           O  
ANISOU 4571  O   ARG B  54     5128   5565   4216    952   -631   -585       O  
ATOM   4572  CB  ARG B  54      10.141   5.087 -70.390  1.00 39.00           C  
ANISOU 4572  CB  ARG B  54     5089   5700   4030    969   -513   -587       C  
ATOM   4573  CG  ARG B  54      11.671   4.912 -70.320  1.00 37.19           C  
ANISOU 4573  CG  ARG B  54     4814   5558   3759    951   -443   -591       C  
ATOM   4574  CD  ARG B  54      12.122   3.709 -71.192  1.00 37.06           C  
ANISOU 4574  CD  ARG B  54     4791   5601   3687   1035   -467   -653       C  
ATOM   4575  NE  ARG B  54      11.444   2.492 -70.742  1.00 43.94           N  
ANISOU 4575  NE  ARG B  54     5654   6415   4625   1078   -547   -708       N  
ATOM   4576  CZ  ARG B  54      10.625   1.732 -71.479  1.00 45.40           C  
ANISOU 4576  CZ  ARG B  54     5880   6572   4800   1141   -620   -749       C  
ATOM   4577  NH1 ARG B  54      10.049   0.672 -70.918  1.00 43.04           N  
ANISOU 4577  NH1 ARG B  54     5576   6213   4563   1156   -687   -794       N  
ATOM   4578  NH2 ARG B  54      10.404   1.994 -72.772  1.00 42.05           N  
ANISOU 4578  NH2 ARG B  54     5505   6176   4295   1184   -626   -747       N  
ATOM   4579  N   PRO B  55       7.735   7.266 -70.576  1.00 45.31           N  
ANISOU 4579  N   PRO B  55     6001   6367   4850    961   -572   -511       N  
ATOM   4580  CA  PRO B  55       6.361   7.542 -71.047  1.00 42.20           C  
ANISOU 4580  CA  PRO B  55     5646   5929   4458   1013   -644   -521       C  
ATOM   4581  C   PRO B  55       5.690   6.283 -71.611  1.00 39.32           C  
ANISOU 4581  C   PRO B  55     5261   5577   4102   1076   -720   -589       C  
ATOM   4582  O   PRO B  55       6.379   5.434 -72.157  1.00 43.12           O  
ANISOU 4582  O   PRO B  55     5738   6102   4545   1099   -713   -617       O  
ATOM   4583  CB  PRO B  55       6.584   8.545 -72.172  1.00 48.38           C  
ANISOU 4583  CB  PRO B  55     6526   6723   5136   1034   -620   -474       C  
ATOM   4584  CG  PRO B  55       7.905   9.216 -71.818  1.00 50.75           C  
ANISOU 4584  CG  PRO B  55     6830   7047   5404    954   -523   -422       C  
ATOM   4585  CD  PRO B  55       8.741   8.141 -71.193  1.00 44.26           C  
ANISOU 4585  CD  PRO B  55     5917   6273   4627    931   -498   -460       C  
ATOM   4586  N   TRP B  56       4.384   6.135 -71.462  1.00 38.22           N  
ANISOU 4586  N   TRP B  56     5107   5404   4011   1101   -791   -621       N  
ATOM   4587  CA  TRP B  56       3.704   4.941 -71.981  1.00 42.22           C  
ANISOU 4587  CA  TRP B  56     5595   5920   4525   1145   -867   -689       C  
ATOM   4588  C   TRP B  56       2.638   5.356 -72.983  1.00 46.11           C  
ANISOU 4588  C   TRP B  56     6133   6414   4974   1214   -933   -702       C  
ATOM   4589  O   TRP B  56       2.250   6.516 -73.021  1.00 47.68           O  
ANISOU 4589  O   TRP B  56     6367   6594   5155   1227   -930   -664       O  
ATOM   4590  CB  TRP B  56       3.044   4.143 -70.858  1.00 35.84           C  
ANISOU 4590  CB  TRP B  56     4717   5084   3819   1101   -900   -730       C  
ATOM   4591  CG  TRP B  56       2.149   4.977 -70.060  1.00 37.58           C  
ANISOU 4591  CG  TRP B  56     4909   5276   4095   1076   -908   -714       C  
ATOM   4592  CD1 TRP B  56       0.844   5.269 -70.323  1.00 41.86           C  
ANISOU 4592  CD1 TRP B  56     5441   5818   4647   1111   -972   -741       C  
ATOM   4593  CD2 TRP B  56       2.491   5.689 -68.851  1.00 34.24           C  
ANISOU 4593  CD2 TRP B  56     4461   4827   3720   1015   -850   -671       C  
ATOM   4594  NE1 TRP B  56       0.351   6.124 -69.349  1.00 41.57           N  
ANISOU 4594  NE1 TRP B  56     5375   5759   4661   1083   -956   -720       N  
ATOM   4595  CE2 TRP B  56       1.347   6.394 -68.441  1.00 39.09           C  
ANISOU 4595  CE2 TRP B  56     5056   5425   4371   1022   -881   -675       C  
ATOM   4596  CE3 TRP B  56       3.655   5.795 -68.087  1.00 29.80           C  
ANISOU 4596  CE3 TRP B  56     3889   4261   3171    960   -778   -636       C  
ATOM   4597  CZ2 TRP B  56       1.324   7.183 -67.278  1.00 33.22           C  
ANISOU 4597  CZ2 TRP B  56     4291   4655   3677    976   -841   -643       C  
ATOM   4598  CZ3 TRP B  56       3.639   6.591 -66.954  1.00 36.68           C  
ANISOU 4598  CZ3 TRP B  56     4740   5104   4092    909   -741   -602       C  
ATOM   4599  CH2 TRP B  56       2.471   7.283 -66.567  1.00 35.63           C  
ANISOU 4599  CH2 TRP B  56     4596   4948   3994    918   -772   -605       C  
ATOM   4600  N   SER B  57       2.158   4.400 -73.781  1.00 46.80           N  
ANISOU 4600  N   SER B  57     6221   6519   5041   1261  -1000   -761       N  
ATOM   4601  CA  SER B  57       1.097   4.651 -74.756  1.00 43.64           C  
ANISOU 4601  CA  SER B  57     5855   6128   4598   1333  -1076   -786       C  
ATOM   4602  C   SER B  57      -0.311   4.323 -74.217  1.00 44.63           C  
ANISOU 4602  C   SER B  57     5912   6245   4802   1325  -1151   -841       C  
ATOM   4603  O   SER B  57      -0.459   3.640 -73.206  1.00 45.53           O  
ANISOU 4603  O   SER B  57     5958   6344   4998   1259  -1148   -866       O  
ATOM   4604  CB  SER B  57       1.370   3.838 -76.031  1.00 44.35           C  
ANISOU 4604  CB  SER B  57     5990   6251   4610   1391  -1109   -823       C  
ATOM   4605  OG  SER B  57       1.307   2.442 -75.757  1.00 45.52           O  
ANISOU 4605  OG  SER B  57     6093   6396   4806   1370  -1143   -885       O  
ATOM   4606  N   GLY B  58      -1.346   4.794 -74.908  1.00 40.26           N  
ANISOU 4606  N   GLY B  58     5375   5705   4218   1391  -1220   -862       N  
ATOM   4607  CA  GLY B  58      -2.713   4.550 -74.483  1.00 41.44           C  
ANISOU 4607  CA  GLY B  58     5446   5867   4432   1386  -1291   -922       C  
ATOM   4608  C   GLY B  58      -3.048   4.966 -73.061  1.00 42.48           C  
ANISOU 4608  C   GLY B  58     5505   5982   4652   1322  -1258   -909       C  
ATOM   4609  O   GLY B  58      -2.495   5.933 -72.511  1.00 37.56           O  
ANISOU 4609  O   GLY B  58     4909   5332   4030   1308  -1195   -847       O  
ATOM   4610  N   VAL B  59      -3.959   4.220 -72.448  1.00 43.94           N  
ANISOU 4610  N   VAL B  59     5602   6185   4910   1275  -1300   -970       N  
ATOM   4611  CA  VAL B  59      -4.397   4.533 -71.096  1.00 45.07           C  
ANISOU 4611  CA  VAL B  59     5669   6322   5133   1213  -1272   -968       C  
ATOM   4612  C   VAL B  59      -3.915   3.456 -70.159  1.00 48.85           C  
ANISOU 4612  C   VAL B  59     6111   6775   5673   1110  -1234   -976       C  
ATOM   4613  O   VAL B  59      -4.313   2.303 -70.289  1.00 50.04           O  
ANISOU 4613  O   VAL B  59     6235   6935   5842   1074  -1278  -1032       O  
ATOM   4614  CB  VAL B  59      -5.939   4.619 -71.008  1.00 44.94           C  
ANISOU 4614  CB  VAL B  59     5568   6359   5148   1232  -1345  -1035       C  
ATOM   4615  CG1 VAL B  59      -6.377   5.123 -69.617  1.00 37.69           C  
ANISOU 4615  CG1 VAL B  59     4574   5443   4303   1178  -1308  -1030       C  
ATOM   4616  CG2 VAL B  59      -6.497   5.527 -72.128  1.00 39.67           C  
ANISOU 4616  CG2 VAL B  59     4947   5719   4408   1355  -1406  -1041       C  
ATOM   4617  N   LEU B  60      -3.039   3.827 -69.226  1.00 49.29           N  
ANISOU 4617  N   LEU B  60     6175   6795   5756   1063  -1156   -920       N  
ATOM   4618  CA  LEU B  60      -2.522   2.875 -68.231  1.00 45.43           C  
ANISOU 4618  CA  LEU B  60     5662   6277   5322    972  -1120   -923       C  
ATOM   4619  C   LEU B  60      -3.550   2.591 -67.133  1.00 38.60           C  
ANISOU 4619  C   LEU B  60     4712   5422   4533    898  -1133   -960       C  
ATOM   4620  O   LEU B  60      -4.086   3.497 -66.525  1.00 40.21           O  
ANISOU 4620  O   LEU B  60     4874   5641   4764    899  -1118   -949       O  
ATOM   4621  CB  LEU B  60      -1.218   3.397 -67.624  1.00 45.87           C  
ANISOU 4621  CB  LEU B  60     5752   6301   5375    952  -1036   -854       C  
ATOM   4622  CG  LEU B  60      -0.475   2.446 -66.678  1.00 50.31           C  
ANISOU 4622  CG  LEU B  60     6305   6832   5980    878  -1001   -853       C  
ATOM   4623  CD1 LEU B  60       1.011   2.788 -66.568  1.00 46.64           C  
ANISOU 4623  CD1 LEU B  60     5882   6355   5485    883   -932   -798       C  
ATOM   4624  CD2 LEU B  60      -1.108   2.486 -65.301  1.00 56.59           C  
ANISOU 4624  CD2 LEU B  60     7038   7614   6850    801   -986   -858       C  
ATOM   4625  N   ASP B  61      -3.828   1.327 -66.884  1.00 38.92           N  
ANISOU 4625  N   ASP B  61     4732   5453   4603    831  -1160  -1006       N  
ATOM   4626  CA  ASP B  61      -4.788   0.974 -65.865  1.00 44.79           C  
ANISOU 4626  CA  ASP B  61     5397   6210   5410    744  -1167  -1043       C  
ATOM   4627  C   ASP B  61      -4.217   1.223 -64.453  1.00 41.80           C  
ANISOU 4627  C   ASP B  61     5008   5795   5077    678  -1093   -996       C  
ATOM   4628  O   ASP B  61      -3.243   0.610 -64.063  1.00 46.26           O  
ANISOU 4628  O   ASP B  61     5622   6311   5646    644  -1061   -971       O  
ATOM   4629  CB  ASP B  61      -5.193  -0.491 -66.041  1.00 53.71           C  
ANISOU 4629  CB  ASP B  61     6530   7330   6549    678  -1218  -1102       C  
ATOM   4630  CG  ASP B  61      -6.064  -0.989 -64.914  1.00 65.39           C  
ANISOU 4630  CG  ASP B  61     7938   8818   8087    561  -1214  -1136       C  
ATOM   4631  OD1 ASP B  61      -5.756  -2.055 -64.328  1.00 70.91           O  
ANISOU 4631  OD1 ASP B  61     8673   9465   8806    475  -1206  -1141       O  
ATOM   4632  OD2 ASP B  61      -7.056  -0.305 -64.609  1.00 73.14           O  
ANISOU 4632  OD2 ASP B  61     8834   9863   9093    558  -1218  -1158       O  
ATOM   4633  N   ALA B  62      -4.833   2.122 -63.696  1.00 43.48           N  
ANISOU 4633  N   ALA B  62     5161   6036   5324    668  -1069   -990       N  
ATOM   4634  CA  ALA B  62      -4.429   2.407 -62.315  1.00 38.42           C  
ANISOU 4634  CA  ALA B  62     4506   5366   4725    605  -1003   -952       C  
ATOM   4635  C   ALA B  62      -5.604   2.233 -61.364  1.00 41.91           C  
ANISOU 4635  C   ALA B  62     4859   5847   5218    527  -1005   -995       C  
ATOM   4636  O   ALA B  62      -6.005   3.176 -60.668  1.00 39.66           O  
ANISOU 4636  O   ALA B  62     4527   5589   4955    536   -977   -986       O  
ATOM   4637  CB  ALA B  62      -3.889   3.812 -62.209  1.00 34.44           C  
ANISOU 4637  CB  ALA B  62     4025   4855   4206    668   -960   -895       C  
ATOM   4638  N   THR B  63      -6.165   1.032 -61.361  1.00 36.25           N  
ANISOU 4638  N   THR B  63     4123   5137   4515    451  -1040  -1045       N  
ATOM   4639  CA  THR B  63      -7.378   0.749 -60.610  1.00 41.39           C  
ANISOU 4639  CA  THR B  63     4681   5841   5203    363  -1045  -1096       C  
ATOM   4640  C   THR B  63      -7.096  -0.288 -59.537  1.00 43.05           C  
ANISOU 4640  C   THR B  63     4918   5998   5442    235  -1012  -1089       C  
ATOM   4641  O   THR B  63      -8.013  -0.704 -58.811  1.00 38.46           O  
ANISOU 4641  O   THR B  63     4272   5454   4888    134  -1007  -1127       O  
ATOM   4642  CB  THR B  63      -8.508   0.200 -61.517  1.00 48.86           C  
ANISOU 4642  CB  THR B  63     5574   6853   6138    358  -1120  -1174       C  
ATOM   4643  OG1 THR B  63      -8.099  -1.053 -62.075  1.00 48.28           O  
ANISOU 4643  OG1 THR B  63     5573   6725   6045    319  -1155  -1187       O  
ATOM   4644  CG2 THR B  63      -8.814   1.178 -62.644  1.00 51.79           C  
ANISOU 4644  CG2 THR B  63     5930   7274   6472    495  -1164  -1184       C  
ATOM   4645  N   THR B  64      -5.830  -0.703 -59.441  1.00 35.07           N  
ANISOU 4645  N   THR B  64     4003   4904   4418    242   -990  -1040       N  
ATOM   4646  CA  THR B  64      -5.452  -1.741 -58.506  1.00 35.03           C  
ANISOU 4646  CA  THR B  64     4048   4834   4429    138   -970  -1031       C  
ATOM   4647  C   THR B  64      -4.013  -1.535 -57.961  1.00 41.71           C  
ANISOU 4647  C   THR B  64     4967   5613   5269    170   -922   -965       C  
ATOM   4648  O   THR B  64      -3.150  -1.055 -58.675  1.00 36.76           O  
ANISOU 4648  O   THR B  64     4375   4979   4615    264   -920   -937       O  
ATOM   4649  CB  THR B  64      -5.551  -3.105 -59.211  1.00 46.05           C  
ANISOU 4649  CB  THR B  64     5504   6193   5802    100  -1030  -1072       C  
ATOM   4650  OG1 THR B  64      -5.237  -4.128 -58.278  1.00 66.53           O  
ANISOU 4650  OG1 THR B  64     8162   8712   8403     -1  -1016  -1063       O  
ATOM   4651  CG2 THR B  64      -4.547  -3.203 -60.320  1.00 41.53           C  
ANISOU 4651  CG2 THR B  64     5006   5586   5186    208  -1056  -1056       C  
ATOM   4652  N   PHE B  65      -3.772  -1.909 -56.705  1.00 35.84           N  
ANISOU 4652  N   PHE B  65     4243   4826   4547     87   -884   -945       N  
ATOM   4653  CA  PHE B  65      -2.453  -1.811 -56.094  1.00 43.83           C  
ANISOU 4653  CA  PHE B  65     5319   5781   5555    111   -845   -892       C  
ATOM   4654  C   PHE B  65      -1.442  -2.675 -56.839  1.00 44.69           C  
ANISOU 4654  C   PHE B  65     5518   5837   5626    162   -880   -890       C  
ATOM   4655  O   PHE B  65      -1.734  -3.808 -57.215  1.00 40.34           O  
ANISOU 4655  O   PHE B  65     5013   5253   5060    128   -928   -927       O  
ATOM   4656  CB  PHE B  65      -2.507  -2.269 -54.630  1.00 41.32           C  
ANISOU 4656  CB  PHE B  65     5017   5423   5259      7   -811   -879       C  
ATOM   4657  CG  PHE B  65      -3.190  -1.298 -53.693  1.00 39.93           C  
ANISOU 4657  CG  PHE B  65     4758   5298   5115    -30   -762   -871       C  
ATOM   4658  CD1 PHE B  65      -2.673  -0.022 -53.487  1.00 37.76           C  
ANISOU 4658  CD1 PHE B  65     4457   5043   4847     39   -722   -833       C  
ATOM   4659  CD2 PHE B  65      -4.320  -1.682 -52.979  1.00 39.37           C  
ANISOU 4659  CD2 PHE B  65     4642   5255   5064   -139   -753   -904       C  
ATOM   4660  CE1 PHE B  65      -3.296   0.867 -52.616  1.00 35.96           C  
ANISOU 4660  CE1 PHE B  65     4162   4857   4644     14   -681   -830       C  
ATOM   4661  CE2 PHE B  65      -4.942  -0.807 -52.094  1.00 34.93           C  
ANISOU 4661  CE2 PHE B  65     3999   4746   4525   -167   -706   -903       C  
ATOM   4662  CZ  PHE B  65      -4.444   0.460 -51.920  1.00 34.94           C  
ANISOU 4662  CZ  PHE B  65     3980   4763   4534    -84   -673   -867       C  
ATOM   4663  N   GLN B  66      -0.244  -2.149 -57.040  1.00 44.61           N  
ANISOU 4663  N   GLN B  66     5532   5821   5596    243   -855   -852       N  
ATOM   4664  CA  GLN B  66       0.828  -2.936 -57.650  1.00 39.28           C  
ANISOU 4664  CA  GLN B  66     4935   5109   4882    301   -882   -855       C  
ATOM   4665  C   GLN B  66       1.538  -3.840 -56.629  1.00 40.39           C  
ANISOU 4665  C   GLN B  66     5145   5178   5022    261   -879   -845       C  
ATOM   4666  O   GLN B  66       1.156  -3.890 -55.441  1.00 37.74           O  
ANISOU 4666  O   GLN B  66     4804   4819   4717    177   -855   -833       O  
ATOM   4667  CB  GLN B  66       1.846  -2.019 -58.311  1.00 38.61           C  
ANISOU 4667  CB  GLN B  66     4839   5061   4768    397   -853   -823       C  
ATOM   4668  CG  GLN B  66       1.617  -1.788 -59.798  1.00 39.27           C  
ANISOU 4668  CG  GLN B  66     4918   5188   4816    469   -884   -842       C  
ATOM   4669  CD  GLN B  66       1.947  -3.007 -60.634  1.00 46.02           C  
ANISOU 4669  CD  GLN B  66     5839   6016   5631    506   -938   -881       C  
ATOM   4670  OE1 GLN B  66       2.599  -3.955 -60.157  1.00 49.31           O  
ANISOU 4670  OE1 GLN B  66     6314   6381   6041    497   -950   -888       O  
ATOM   4671  NE2 GLN B  66       1.514  -2.995 -61.889  1.00 45.41           N  
ANISOU 4671  NE2 GLN B  66     5760   5971   5523    556   -976   -908       N  
ATOM   4672  N   ASN B  67       2.579  -4.534 -57.098  1.00 36.20           N  
ANISOU 4672  N   ASN B  67     4683   4618   4453    328   -904   -852       N  
ATOM   4673  CA  ASN B  67       3.331  -5.464 -56.269  1.00 35.57           C  
ANISOU 4673  CA  ASN B  67     4684   4468   4362    317   -916   -849       C  
ATOM   4674  C   ASN B  67       4.040  -4.786 -55.115  1.00 35.40           C  
ANISOU 4674  C   ASN B  67     4640   4452   4360    308   -862   -806       C  
ATOM   4675  O   ASN B  67       4.280  -3.581 -55.127  1.00 41.45           O  
ANISOU 4675  O   ASN B  67     5334   5276   5139    331   -814   -777       O  
ATOM   4676  CB  ASN B  67       4.359  -6.221 -57.090  1.00 38.25           C  
ANISOU 4676  CB  ASN B  67     5092   4793   4650    416   -956   -873       C  
ATOM   4677  CG  ASN B  67       3.718  -7.150 -58.113  1.00 49.44           C  
ANISOU 4677  CG  ASN B  67     6559   6183   6042    422  -1022   -922       C  
ATOM   4678  OD1 ASN B  67       2.585  -7.600 -57.929  1.00 48.41           O  
ANISOU 4678  OD1 ASN B  67     6441   6021   5932    329  -1046   -942       O  
ATOM   4679  ND2 ASN B  67       4.444  -7.439 -59.194  1.00 43.27           N  
ANISOU 4679  ND2 ASN B  67     5806   5421   5213    526  -1049   -945       N  
ATOM   4680  N   VAL B  68       4.371  -5.592 -54.120  1.00 27.46           N  
ANISOU 4680  N   VAL B  68     3705   3377   3350    272   -874   -803       N  
ATOM   4681  CA  VAL B  68       5.031  -5.155 -52.921  1.00 28.90           C  
ANISOU 4681  CA  VAL B  68     3882   3554   3547    259   -834   -768       C  
ATOM   4682  C   VAL B  68       6.511  -5.401 -53.119  1.00 34.09           C  
ANISOU 4682  C   VAL B  68     4571   4217   4166    363   -846   -771       C  
ATOM   4683  O   VAL B  68       6.914  -6.454 -53.640  1.00 35.83           O  
ANISOU 4683  O   VAL B  68     4868   4399   4348    419   -901   -803       O  
ATOM   4684  CB  VAL B  68       4.511  -5.961 -51.708  1.00 37.53           C  
ANISOU 4684  CB  VAL B  68     5045   4566   4647    161   -845   -766       C  
ATOM   4685  CG1 VAL B  68       5.467  -5.838 -50.489  1.00 35.59           C  
ANISOU 4685  CG1 VAL B  68     4827   4297   4399    171   -822   -736       C  
ATOM   4686  CG2 VAL B  68       3.097  -5.522 -51.354  1.00 32.82           C  
ANISOU 4686  CG2 VAL B  68     4389   3992   4090     52   -816   -764       C  
ATOM   4687  N   CYS B  69       7.318  -4.417 -52.748  1.00 33.46           N  
ANISOU 4687  N   CYS B  69     4430   4191   4094    392   -798   -741       N  
ATOM   4688  CA  CYS B  69       8.757  -4.527 -52.899  1.00 29.35           C  
ANISOU 4688  CA  CYS B  69     3914   3701   3536    486   -803   -748       C  
ATOM   4689  C   CYS B  69       9.226  -5.781 -52.188  1.00 37.59           C  
ANISOU 4689  C   CYS B  69     5060   4667   4554    506   -854   -768       C  
ATOM   4690  O   CYS B  69       8.725  -6.123 -51.105  1.00 40.29           O  
ANISOU 4690  O   CYS B  69     5453   4941   4914    431   -859   -754       O  
ATOM   4691  CB  CYS B  69       9.442  -3.276 -52.352  1.00 25.20           C  
ANISOU 4691  CB  CYS B  69     3309   3237   3027    482   -741   -713       C  
ATOM   4692  SG  CYS B  69       9.270  -1.756 -53.394  1.00 37.68           S  
ANISOU 4692  SG  CYS B  69     4794   4908   4615    487   -686   -689       S  
ATOM   4693  N   TYR B  70      10.170  -6.484 -52.803  1.00 43.91           N  
ANISOU 4693  N   TYR B  70     5899   5477   5307    611   -895   -803       N  
ATOM   4694  CA  TYR B  70      10.614  -7.772 -52.275  1.00 38.68           C  
ANISOU 4694  CA  TYR B  70     5354   4732   4609    652   -960   -829       C  
ATOM   4695  C   TYR B  70      11.163  -7.662 -50.851  1.00 40.78           C  
ANISOU 4695  C   TYR B  70     5637   4975   4882    635   -948   -806       C  
ATOM   4696  O   TYR B  70      12.020  -6.824 -50.563  1.00 35.61           O  
ANISOU 4696  O   TYR B  70     4899   4398   4232    666   -908   -793       O  
ATOM   4697  CB  TYR B  70      11.631  -8.450 -53.197  1.00 38.74           C  
ANISOU 4697  CB  TYR B  70     5390   4770   4559    790  -1005   -878       C  
ATOM   4698  CG  TYR B  70      11.503  -9.941 -53.054  1.00 42.60           C  
ANISOU 4698  CG  TYR B  70     6033   5143   5011    819  -1089   -913       C  
ATOM   4699  CD1 TYR B  70      10.671 -10.667 -53.892  1.00 43.13           C  
ANISOU 4699  CD1 TYR B  70     6168   5153   5066    800  -1132   -939       C  
ATOM   4700  CD2 TYR B  70      12.132 -10.610 -52.014  1.00 42.66           C  
ANISOU 4700  CD2 TYR B  70     6129   5086   4993    853  -1128   -918       C  
ATOM   4701  CE1 TYR B  70      10.506 -12.045 -53.725  1.00 44.87           C  
ANISOU 4701  CE1 TYR B  70     6549   5251   5249    812  -1212   -969       C  
ATOM   4702  CE2 TYR B  70      11.969 -11.961 -51.838  1.00 46.00           C  
ANISOU 4702  CE2 TYR B  70     6716   5386   5377    873  -1208   -945       C  
ATOM   4703  CZ  TYR B  70      11.155 -12.685 -52.703  1.00 43.98           C  
ANISOU 4703  CZ  TYR B  70     6533   5069   5107    849  -1249   -970       C  
ATOM   4704  OH  TYR B  70      10.985 -14.040 -52.518  1.00 41.63           O  
ANISOU 4704  OH  TYR B  70     6416   4636   4766    859  -1332   -997       O  
ATOM   4705  N   GLN B  71      10.677  -8.527 -49.960  1.00 41.11           N  
ANISOU 4705  N   GLN B  71     5792   4907   4919    579   -985   -802       N  
ATOM   4706  CA  GLN B  71      10.969  -8.375 -48.534  1.00 40.01           C  
ANISOU 4706  CA  GLN B  71     5676   4738   4787    543   -972   -774       C  
ATOM   4707  C   GLN B  71      10.709  -9.631 -47.753  1.00 42.32           C  
ANISOU 4707  C   GLN B  71     6131   4900   5047    515  -1032   -779       C  
ATOM   4708  O   GLN B  71       9.966 -10.524 -48.178  1.00 44.43           O  
ANISOU 4708  O   GLN B  71     6492   5089   5300    478  -1072   -796       O  
ATOM   4709  CB  GLN B  71      10.094  -7.264 -47.906  1.00 30.23           C  
ANISOU 4709  CB  GLN B  71     4355   3527   3606    421   -898   -729       C  
ATOM   4710  CG  GLN B  71       8.594  -7.606 -47.836  1.00 27.36           C  
ANISOU 4710  CG  GLN B  71     4031   3100   3263    299   -896   -722       C  
ATOM   4711  CD  GLN B  71       7.735  -6.353 -47.516  1.00 35.69           C  
ANISOU 4711  CD  GLN B  71     4975   4214   4373    207   -822   -690       C  
ATOM   4712  OE1 GLN B  71       7.129  -6.257 -46.462  1.00 36.43           O  
ANISOU 4712  OE1 GLN B  71     5084   4275   4482    114   -796   -668       O  
ATOM   4713  NE2 GLN B  71       7.739  -5.383 -48.418  1.00 32.16           N  
ANISOU 4713  NE2 GLN B  71     4420   3853   3946    240   -789   -689       N  
ATOM   4714  N   TYR B  72      11.298  -9.646 -46.572  1.00 45.26           N  
ANISOU 4714  N   TYR B  72     6542   5248   5408    523  -1035   -763       N  
ATOM   4715  CA  TYR B  72      11.025 -10.638 -45.548  1.00 45.00           C  
ANISOU 4715  CA  TYR B  72     6669   5087   5342    476  -1080   -754       C  
ATOM   4716  C   TYR B  72       9.561 -10.609 -45.103  1.00 44.05           C  
ANISOU 4716  C   TYR B  72     6572   4913   5253    306  -1042   -722       C  
ATOM   4717  O   TYR B  72       8.938  -9.536 -44.968  1.00 41.08           O  
ANISOU 4717  O   TYR B  72     6073   4607   4929    226   -970   -696       O  
ATOM   4718  CB  TYR B  72      11.945 -10.368 -44.354  1.00 45.31           C  
ANISOU 4718  CB  TYR B  72     6714   5136   5367    517  -1079   -738       C  
ATOM   4719  CG  TYR B  72      11.660 -11.239 -43.167  1.00 57.45           C  
ANISOU 4719  CG  TYR B  72     8419   6543   6868    461  -1117   -720       C  
ATOM   4720  CD1 TYR B  72      10.947 -10.750 -42.070  1.00 62.44           C  
ANISOU 4720  CD1 TYR B  72     9045   7156   7524    330  -1062   -675       C  
ATOM   4721  CD2 TYR B  72      12.084 -12.565 -43.140  1.00 54.49           C  
ANISOU 4721  CD2 TYR B  72     8218   6060   6425    539  -1208   -747       C  
ATOM   4722  CE1 TYR B  72      10.676 -11.562 -40.978  1.00 58.57           C  
ANISOU 4722  CE1 TYR B  72     8718   6546   6991    269  -1093   -655       C  
ATOM   4723  CE2 TYR B  72      11.826 -13.367 -42.057  1.00 53.35           C  
ANISOU 4723  CE2 TYR B  72     8247   5787   6237    483  -1245   -726       C  
ATOM   4724  CZ  TYR B  72      11.126 -12.869 -40.987  1.00 54.89           C  
ANISOU 4724  CZ  TYR B  72     8433   5968   6457    344  -1185   -678       C  
ATOM   4725  OH  TYR B  72      10.875 -13.692 -39.924  1.00 61.13           O  
ANISOU 4725  OH  TYR B  72     9405   6628   7194    283  -1218   -655       O  
ATOM   4726  N   VAL B  73       9.003 -11.792 -44.888  1.00 41.83           N  
ANISOU 4726  N   VAL B  73     6450   4510   4935    250  -1093   -728       N  
ATOM   4727  CA  VAL B  73       7.626 -11.922 -44.450  1.00 39.69           C  
ANISOU 4727  CA  VAL B  73     6208   4189   4682     79  -1060   -705       C  
ATOM   4728  C   VAL B  73       7.625 -12.534 -43.051  1.00 51.46           C  
ANISOU 4728  C   VAL B  73     7845   5576   6133     15  -1074   -677       C  
ATOM   4729  O   VAL B  73       8.218 -13.604 -42.814  1.00 49.49           O  
ANISOU 4729  O   VAL B  73     7764   5220   5821     77  -1150   -689       O  
ATOM   4730  CB  VAL B  73       6.834 -12.819 -45.393  1.00 48.00           C  
ANISOU 4730  CB  VAL B  73     7333   5184   5720     34  -1102   -735       C  
ATOM   4731  CG1 VAL B  73       5.470 -13.125 -44.817  1.00 46.89           C  
ANISOU 4731  CG1 VAL B  73     7240   4991   5587   -155  -1074   -717       C  
ATOM   4732  CG2 VAL B  73       6.717 -12.174 -46.770  1.00 52.38           C  
ANISOU 4732  CG2 VAL B  73     7746   5845   6312     88  -1085   -761       C  
ATOM   4733  N   ASP B  74       6.965 -11.851 -42.123  1.00 53.31           N  
ANISOU 4733  N   ASP B  74     8023   5838   6396   -103  -1005   -642       N  
ATOM   4734  CA  ASP B  74       6.939 -12.283 -40.733  1.00 55.04           C  
ANISOU 4734  CA  ASP B  74     8368   5970   6575   -172  -1006   -610       C  
ATOM   4735  C   ASP B  74       6.103 -13.547 -40.525  1.00 55.66           C  
ANISOU 4735  C   ASP B  74     8629   5916   6605   -294  -1042   -608       C  
ATOM   4736  O   ASP B  74       4.965 -13.628 -40.974  1.00 58.54           O  
ANISOU 4736  O   ASP B  74     8958   6292   6991   -415  -1014   -616       O  
ATOM   4737  CB  ASP B  74       6.411 -11.158 -39.861  1.00 66.90           C  
ANISOU 4737  CB  ASP B  74     9750   7548   8119   -266   -917   -577       C  
ATOM   4738  CG  ASP B  74       6.432 -11.506 -38.399  1.00 76.90           C  
ANISOU 4738  CG  ASP B  74    11141   8737   9341   -333   -912   -544       C  
ATOM   4739  OD1 ASP B  74       5.513 -11.051 -37.691  1.00 80.20           O  
ANISOU 4739  OD1 ASP B  74    11515   9181   9775   -466   -843   -520       O  
ATOM   4740  OD2 ASP B  74       7.361 -12.234 -37.966  1.00 80.98           O  
ANISOU 4740  OD2 ASP B  74    11799   9169   9800   -246   -979   -543       O  
ATOM   4741  N   THR B  75       6.678 -14.527 -39.837  1.00 55.51           N  
ANISOU 4741  N   THR B  75     8806   5771   6515   -261  -1106   -600       N  
ATOM   4742  CA  THR B  75       6.021 -15.815 -39.623  1.00 66.97           C  
ANISOU 4742  CA  THR B  75    10466   7075   7905   -372  -1151   -597       C  
ATOM   4743  C   THR B  75       5.940 -16.171 -38.138  1.00 69.13           C  
ANISOU 4743  C   THR B  75    10887   7256   8124   -462  -1142   -553       C  
ATOM   4744  O   THR B  75       5.616 -17.305 -37.779  1.00 64.45           O  
ANISOU 4744  O   THR B  75    10508   6519   7462   -543  -1187   -543       O  
ATOM   4745  CB  THR B  75       6.766 -16.952 -40.362  1.00 69.77           C  
ANISOU 4745  CB  THR B  75    10981   7325   8203   -240  -1261   -634       C  
ATOM   4746  OG1 THR B  75       8.186 -16.777 -40.198  1.00 74.07           O  
ANISOU 4746  OG1 THR B  75    11522   7893   8728    -43  -1306   -645       O  
ATOM   4747  CG2 THR B  75       6.405 -16.958 -41.855  1.00 60.34           C  
ANISOU 4747  CG2 THR B  75     9696   6185   7046   -216  -1272   -676       C  
ATOM   4748  N   LEU B  76       6.228 -15.188 -37.286  1.00 73.92           N  
ANISOU 4748  N   LEU B  76    11387   7943   8755   -451  -1083   -527       N  
ATOM   4749  CA  LEU B  76       6.282 -15.395 -35.843  1.00 77.47           C  
ANISOU 4749  CA  LEU B  76    11963   8320   9150   -515  -1073   -486       C  
ATOM   4750  C   LEU B  76       4.978 -15.967 -35.273  1.00 79.33           C  
ANISOU 4750  C   LEU B  76    12305   8484   9353   -739  -1031   -459       C  
ATOM   4751  O   LEU B  76       5.002 -16.922 -34.495  1.00 85.52           O  
ANISOU 4751  O   LEU B  76    13313   9127  10054   -794  -1071   -434       O  
ATOM   4752  CB  LEU B  76       6.667 -14.098 -35.128  1.00 80.71           C  
ANISOU 4752  CB  LEU B  76    12212   8849   9604   -479  -1008   -467       C  
ATOM   4753  CG  LEU B  76       6.494 -14.107 -33.606  1.00 81.50           C  
ANISOU 4753  CG  LEU B  76    12411   8900   9656   -572   -975   -423       C  
ATOM   4754  CD1 LEU B  76       7.338 -15.200 -32.976  1.00 78.06           C  
ANISOU 4754  CD1 LEU B  76    12219   8315   9126   -493  -1071   -414       C  
ATOM   4755  CD2 LEU B  76       6.814 -12.745 -33.007  1.00 79.01           C  
ANISOU 4755  CD2 LEU B  76    11921   8710   9391   -537   -909   -412       C  
ATOM   4756  N   TYR B  77       3.841 -15.395 -35.652  1.00 73.06           N  
ANISOU 4756  N   TYR B  77    11355   7788   8618   -871   -952   -465       N  
ATOM   4757  CA  TYR B  77       2.561 -15.974 -35.251  1.00 64.45           C  
ANISOU 4757  CA  TYR B  77    10345   6649   7496  -1093   -910   -451       C  
ATOM   4758  C   TYR B  77       1.678 -16.174 -36.476  1.00 66.34           C  
ANISOU 4758  C   TYR B  77    10504   6927   7774  -1162   -909   -490       C  
ATOM   4759  O   TYR B  77       0.807 -15.352 -36.761  1.00 58.40           O  
ANISOU 4759  O   TYR B  77     9303   6055   6831  -1239   -834   -504       O  
ATOM   4760  CB  TYR B  77       1.849 -15.082 -34.249  1.00 65.53           C  
ANISOU 4760  CB  TYR B  77    10364   6882   7652  -1216   -804   -425       C  
ATOM   4761  CG  TYR B  77       2.579 -14.867 -32.938  1.00 67.17           C  
ANISOU 4761  CG  TYR B  77    10652   7053   7816  -1172   -798   -385       C  
ATOM   4762  CD1 TYR B  77       2.609 -15.857 -31.960  1.00 66.51           C  
ANISOU 4762  CD1 TYR B  77    10810   6824   7635  -1253   -827   -350       C  
ATOM   4763  CD2 TYR B  77       3.199 -13.659 -32.661  1.00 64.00           C  
ANISOU 4763  CD2 TYR B  77    10090   6761   7465  -1059   -764   -383       C  
ATOM   4764  CE1 TYR B  77       3.264 -15.654 -30.751  1.00 67.01           C  
ANISOU 4764  CE1 TYR B  77    10950   6856   7654  -1209   -825   -316       C  
ATOM   4765  CE2 TYR B  77       3.851 -13.444 -31.459  1.00 68.76           C  
ANISOU 4765  CE2 TYR B  77    10762   7337   8027  -1021   -762   -352       C  
ATOM   4766  CZ  TYR B  77       3.883 -14.442 -30.508  1.00 70.08           C  
ANISOU 4766  CZ  TYR B  77    11165   7363   8098  -1091   -793   -319       C  
ATOM   4767  OH  TYR B  77       4.528 -14.217 -29.315  1.00 71.00           O  
ANISOU 4767  OH  TYR B  77    11352   7455   8171  -1048   -795   -289       O  
ATOM   4768  N   PRO B  78       1.893 -17.286 -37.199  1.00 72.03           N  
ANISOU 4768  N   PRO B  78    11384   7531   8454  -1131   -997   -511       N  
ATOM   4769  CA  PRO B  78       1.235 -17.565 -38.483  1.00 69.56           C  
ANISOU 4769  CA  PRO B  78    11013   7244   8173  -1167  -1016   -554       C  
ATOM   4770  C   PRO B  78      -0.282 -17.387 -38.412  1.00 69.40           C  
ANISOU 4770  C   PRO B  78    10894   7299   8177  -1391   -935   -560       C  
ATOM   4771  O   PRO B  78      -0.919 -18.070 -37.609  1.00 70.74           O  
ANISOU 4771  O   PRO B  78    11201   7388   8287  -1568   -916   -537       O  
ATOM   4772  CB  PRO B  78       1.578 -19.038 -38.735  1.00 73.18           C  
ANISOU 4772  CB  PRO B  78    11739   7516   8550  -1154  -1121   -563       C  
ATOM   4773  CG  PRO B  78       2.874 -19.248 -38.016  1.00 77.30           C  
ANISOU 4773  CG  PRO B  78    12398   7953   9021   -997  -1176   -540       C  
ATOM   4774  CD  PRO B  78       2.771 -18.392 -36.772  1.00 76.35           C  
ANISOU 4774  CD  PRO B  78    12196   7903   8912  -1057  -1091   -497       C  
ATOM   4775  N   GLY B  79      -0.840 -16.479 -39.217  1.00 62.66           N  
ANISOU 4775  N   GLY B  79     9807   6599   7401  -1382   -889   -592       N  
ATOM   4776  CA  GLY B  79      -2.280 -16.290 -39.275  1.00 65.55           C  
ANISOU 4776  CA  GLY B  79    10056   7057   7792  -1574   -821   -611       C  
ATOM   4777  C   GLY B  79      -2.919 -15.420 -38.201  1.00 69.38           C  
ANISOU 4777  C   GLY B  79    10416   7649   8294  -1679   -716   -589       C  
ATOM   4778  O   GLY B  79      -4.144 -15.265 -38.181  1.00 71.32           O  
ANISOU 4778  O   GLY B  79    10556   7986   8555  -1839   -656   -612       O  
ATOM   4779  N   PHE B  80      -2.098 -14.863 -37.311  1.00 62.56           N  
ANISOU 4779  N   PHE B  80     9563   6782   7426  -1586   -696   -551       N  
ATOM   4780  CA  PHE B  80      -2.546 -13.950 -36.260  1.00 59.69           C  
ANISOU 4780  CA  PHE B  80     9084   6518   7075  -1655   -601   -531       C  
ATOM   4781  C   PHE B  80      -2.761 -12.553 -36.867  1.00 59.77           C  
ANISOU 4781  C   PHE B  80     8833   6702   7174  -1564   -555   -560       C  
ATOM   4782  O   PHE B  80      -1.895 -12.057 -37.587  1.00 55.22           O  
ANISOU 4782  O   PHE B  80     8200   6143   6637  -1387   -595   -567       O  
ATOM   4783  CB  PHE B  80      -1.481 -13.929 -35.155  1.00 56.87           C  
ANISOU 4783  CB  PHE B  80     8853   6081   6675  -1575   -612   -483       C  
ATOM   4784  CG  PHE B  80      -1.706 -12.897 -34.077  1.00 58.55           C  
ANISOU 4784  CG  PHE B  80     8953   6391   6902  -1607   -523   -463       C  
ATOM   4785  CD1 PHE B  80      -2.899 -12.850 -33.366  1.00 54.40           C  
ANISOU 4785  CD1 PHE B  80     8388   5926   6357  -1801   -439   -462       C  
ATOM   4786  CD2 PHE B  80      -0.690 -12.003 -33.741  1.00 59.17           C  
ANISOU 4786  CD2 PHE B  80     8972   6502   7007  -1446   -524   -446       C  
ATOM   4787  CE1 PHE B  80      -3.093 -11.918 -32.356  1.00 58.89           C  
ANISOU 4787  CE1 PHE B  80     8859   6584   6932  -1822   -358   -447       C  
ATOM   4788  CE2 PHE B  80      -0.870 -11.066 -32.729  1.00 61.46           C  
ANISOU 4788  CE2 PHE B  80     9173   6874   7306  -1472   -448   -429       C  
ATOM   4789  CZ  PHE B  80      -2.077 -11.019 -32.033  1.00 60.84           C  
ANISOU 4789  CZ  PHE B  80     9056   6852   7206  -1655   -364   -430       C  
ATOM   4790  N   GLU B  81      -3.911 -11.930 -36.603  1.00 58.38           N  
ANISOU 4790  N   GLU B  81     8504   6654   7025  -1682   -473   -579       N  
ATOM   4791  CA  GLU B  81      -4.216 -10.630 -37.211  1.00 61.65           C  
ANISOU 4791  CA  GLU B  81     8684   7224   7515  -1594   -437   -610       C  
ATOM   4792  C   GLU B  81      -3.190  -9.571 -36.824  1.00 60.89           C  
ANISOU 4792  C   GLU B  81     8536   7153   7447  -1432   -426   -583       C  
ATOM   4793  O   GLU B  81      -2.808  -8.731 -37.632  1.00 58.21           O  
ANISOU 4793  O   GLU B  81     8077   6878   7160  -1295   -440   -597       O  
ATOM   4794  CB  GLU B  81      -5.629 -10.145 -36.862  1.00 64.39           C  
ANISOU 4794  CB  GLU B  81     8879   7711   7877  -1740   -353   -641       C  
ATOM   4795  CG  GLU B  81      -6.109  -8.971 -37.738  1.00 75.62           C  
ANISOU 4795  CG  GLU B  81    10074   9287   9372  -1650   -334   -685       C  
ATOM   4796  CD  GLU B  81      -6.055  -9.268 -39.257  1.00 89.68           C  
ANISOU 4796  CD  GLU B  81    11832  11060  11181  -1575   -407   -718       C  
ATOM   4797  OE1 GLU B  81      -6.761 -10.200 -39.715  1.00 96.30           O  
ANISOU 4797  OE1 GLU B  81    12712  11877  11999  -1695   -431   -747       O  
ATOM   4798  OE2 GLU B  81      -5.321  -8.564 -40.002  1.00 88.80           O  
ANISOU 4798  OE2 GLU B  81    11663  10967  11111  -1404   -438   -717       O  
ATOM   4799  N   GLY B  82      -2.745  -9.633 -35.577  1.00 62.16           N  
ANISOU 4799  N   GLY B  82     8794   7259   7566  -1456   -403   -543       N  
ATOM   4800  CA  GLY B  82      -1.755  -8.710 -35.062  1.00 57.10           C  
ANISOU 4800  CA  GLY B  82     8119   6633   6942  -1321   -394   -517       C  
ATOM   4801  C   GLY B  82      -0.477  -8.622 -35.867  1.00 48.88           C  
ANISOU 4801  C   GLY B  82     7099   5551   5922  -1139   -466   -515       C  
ATOM   4802  O   GLY B  82       0.110  -7.560 -35.964  1.00 45.37           O  
ANISOU 4802  O   GLY B  82     6550   5171   5518  -1024   -454   -512       O  
ATOM   4803  N   THR B  83      -0.031  -9.725 -36.448  1.00 52.12           N  
ANISOU 4803  N   THR B  83     7644   5857   6300  -1114   -542   -518       N  
ATOM   4804  CA  THR B  83       1.207  -9.675 -37.218  1.00 51.60           C  
ANISOU 4804  CA  THR B  83     7592   5766   6248   -936   -608   -522       C  
ATOM   4805  C   THR B  83       0.916  -9.590 -38.714  1.00 50.63           C  
ANISOU 4805  C   THR B  83     7375   5696   6168   -889   -633   -560       C  
ATOM   4806  O   THR B  83       1.620  -8.895 -39.461  1.00 46.26           O  
ANISOU 4806  O   THR B  83     6731   5195   5650   -752   -648   -570       O  
ATOM   4807  CB  THR B  83       2.162 -10.853 -36.881  1.00 67.63           C  
ANISOU 4807  CB  THR B  83     9837   7650   8210   -889   -686   -505       C  
ATOM   4808  OG1 THR B  83       1.483 -12.101 -37.069  1.00 71.97           O  
ANISOU 4808  OG1 THR B  83    10526   8105   8714  -1005   -718   -513       O  
ATOM   4809  CG2 THR B  83       2.639 -10.757 -35.436  1.00 62.33           C  
ANISOU 4809  CG2 THR B  83     9248   6937   7497   -901   -667   -467       C  
ATOM   4810  N   GLU B  84      -0.152 -10.262 -39.132  1.00 49.15           N  
ANISOU 4810  N   GLU B  84     7204   5498   5972  -1011   -635   -584       N  
ATOM   4811  CA  GLU B  84      -0.483 -10.376 -40.542  1.00 51.58           C  
ANISOU 4811  CA  GLU B  84     7448   5841   6308   -976   -670   -623       C  
ATOM   4812  C   GLU B  84      -0.846  -9.033 -41.164  1.00 52.81           C  
ANISOU 4812  C   GLU B  84     7395   6141   6530   -919   -626   -641       C  
ATOM   4813  O   GLU B  84      -0.588  -8.812 -42.352  1.00 50.10           O  
ANISOU 4813  O   GLU B  84     6993   5830   6211   -819   -660   -664       O  
ATOM   4814  CB  GLU B  84      -1.631 -11.360 -40.743  1.00 52.30           C  
ANISOU 4814  CB  GLU B  84     7599   5898   6374  -1140   -679   -647       C  
ATOM   4815  CG  GLU B  84      -1.282 -12.782 -40.402  1.00 63.67           C  
ANISOU 4815  CG  GLU B  84     9271   7177   7743  -1190   -739   -633       C  
ATOM   4816  CD  GLU B  84      -0.290 -13.406 -41.393  1.00 72.47           C  
ANISOU 4816  CD  GLU B  84    10480   8212   8842  -1041   -831   -649       C  
ATOM   4817  OE1 GLU B  84       0.015 -12.756 -42.435  1.00 68.22           O  
ANISOU 4817  OE1 GLU B  84     9817   7755   8350   -917   -842   -672       O  
ATOM   4818  OE2 GLU B  84       0.176 -14.553 -41.126  1.00 71.44           O  
ANISOU 4818  OE2 GLU B  84    10558   7939   8649  -1045   -893   -639       O  
ATOM   4819  N   MET B  85      -1.436  -8.139 -40.372  1.00 48.83           N  
ANISOU 4819  N   MET B  85     6786   5719   6048   -976   -552   -633       N  
ATOM   4820  CA  MET B  85      -1.908  -6.857 -40.905  1.00 46.18           C  
ANISOU 4820  CA  MET B  85     6265   5514   5768   -925   -513   -653       C  
ATOM   4821  C   MET B  85      -0.735  -6.008 -41.417  1.00 42.76           C  
ANISOU 4821  C   MET B  85     5790   5098   5360   -755   -531   -639       C  
ATOM   4822  O   MET B  85      -0.921  -5.043 -42.155  1.00 43.67           O  
ANISOU 4822  O   MET B  85     5780   5298   5513   -688   -518   -654       O  
ATOM   4823  CB  MET B  85      -2.714  -6.097 -39.855  1.00 44.82           C  
ANISOU 4823  CB  MET B  85     6004   5421   5606  -1010   -434   -651       C  
ATOM   4824  CG  MET B  85      -1.913  -5.735 -38.601  1.00 54.09           C  
ANISOU 4824  CG  MET B  85     7234   6557   6762   -987   -406   -608       C  
ATOM   4825  SD  MET B  85      -2.801  -4.636 -37.446  1.00 57.59           S  
ANISOU 4825  SD  MET B  85     7558   7107   7218  -1058   -311   -611       S  
ATOM   4826  CE  MET B  85      -2.864  -3.170 -38.433  1.00 29.33           C  
ANISOU 4826  CE  MET B  85     3806   3637   3701   -924   -305   -635       C  
ATOM   4827  N   TRP B  86       0.469  -6.390 -41.021  1.00 34.90           N  
ANISOU 4827  N   TRP B  86     4903   4021   4336   -689   -562   -611       N  
ATOM   4828  CA  TRP B  86       1.678  -5.727 -41.475  1.00 39.30           C  
ANISOU 4828  CA  TRP B  86     5428   4596   4908   -541   -580   -601       C  
ATOM   4829  C   TRP B  86       2.346  -6.406 -42.670  1.00 46.41           C  
ANISOU 4829  C   TRP B  86     6379   5460   5795   -449   -648   -619       C  
ATOM   4830  O   TRP B  86       3.210  -5.803 -43.308  1.00 40.10           O  
ANISOU 4830  O   TRP B  86     5529   4700   5009   -332   -657   -619       O  
ATOM   4831  CB  TRP B  86       2.666  -5.637 -40.318  1.00 35.58           C  
ANISOU 4831  CB  TRP B  86     5025   4081   4414   -511   -574   -568       C  
ATOM   4832  CG  TRP B  86       2.060  -4.941 -39.134  1.00 43.53           C  
ANISOU 4832  CG  TRP B  86     5985   5124   5429   -594   -507   -551       C  
ATOM   4833  CD1 TRP B  86       1.750  -5.494 -37.928  1.00 44.47           C  
ANISOU 4833  CD1 TRP B  86     6195   5191   5512   -694   -488   -533       C  
ATOM   4834  CD2 TRP B  86       1.658  -3.561 -39.060  1.00 38.24           C  
ANISOU 4834  CD2 TRP B  86     5175   4551   4801   -582   -450   -553       C  
ATOM   4835  NE1 TRP B  86       1.215  -4.541 -37.095  1.00 42.08           N  
ANISOU 4835  NE1 TRP B  86     5808   4955   5226   -741   -420   -526       N  
ATOM   4836  CE2 TRP B  86       1.136  -3.352 -37.765  1.00 41.49           C  
ANISOU 4836  CE2 TRP B  86     5594   4970   5201   -671   -398   -540       C  
ATOM   4837  CE3 TRP B  86       1.709  -2.488 -39.952  1.00 40.19           C  
ANISOU 4837  CE3 TRP B  86     5305   4875   5089   -501   -440   -564       C  
ATOM   4838  CZ2 TRP B  86       0.660  -2.090 -37.335  1.00 41.94           C  
ANISOU 4838  CZ2 TRP B  86     5538   5110   5287   -673   -339   -542       C  
ATOM   4839  CZ3 TRP B  86       1.233  -1.228 -39.526  1.00 39.47           C  
ANISOU 4839  CZ3 TRP B  86     5113   4857   5026   -506   -384   -563       C  
ATOM   4840  CH2 TRP B  86       0.714  -1.047 -38.228  1.00 37.19           C  
ANISOU 4840  CH2 TRP B  86     4829   4575   4726   -587   -336   -555       C  
ATOM   4841  N   ASN B  87       1.949  -7.654 -42.955  1.00 44.17           N  
ANISOU 4841  N   ASN B  87     6200   5102   5480   -506   -693   -637       N  
ATOM   4842  CA  ASN B  87       2.562  -8.462 -44.009  1.00 43.17           C  
ANISOU 4842  CA  ASN B  87     6146   4928   5330   -420   -765   -660       C  
ATOM   4843  C   ASN B  87       2.080  -8.043 -45.404  1.00 41.91           C  
ANISOU 4843  C   ASN B  87     5879   4844   5201   -382   -770   -691       C  
ATOM   4844  O   ASN B  87       0.997  -7.497 -45.544  1.00 41.16           O  
ANISOU 4844  O   ASN B  87     5684   4818   5137   -454   -733   -702       O  
ATOM   4845  CB  ASN B  87       2.247  -9.946 -43.785  1.00 43.98           C  
ANISOU 4845  CB  ASN B  87     6416   4911   5382   -502   -815   -669       C  
ATOM   4846  CG  ASN B  87       3.179 -10.616 -42.776  1.00 53.77           C  
ANISOU 4846  CG  ASN B  87     7809   6049   6572   -473   -846   -643       C  
ATOM   4847  OD1 ASN B  87       4.362 -10.266 -42.646  1.00 53.35           O  
ANISOU 4847  OD1 ASN B  87     7750   6008   6514   -347   -860   -634       O  
ATOM   4848  ND2 ASN B  87       2.646 -11.618 -42.072  1.00 53.95           N  
ANISOU 4848  ND2 ASN B  87     7974   5972   6551   -593   -861   -635       N  
ATOM   4849  N   PRO B  88       2.876  -8.322 -46.445  1.00 40.73           N  
ANISOU 4849  N   PRO B  88     5752   4686   5037   -265   -820   -708       N  
ATOM   4850  CA  PRO B  88       2.474  -7.978 -47.826  1.00 39.39           C  
ANISOU 4850  CA  PRO B  88     5496   4583   4886   -222   -831   -738       C  
ATOM   4851  C   PRO B  88       1.081  -8.507 -48.144  1.00 43.48           C  
ANISOU 4851  C   PRO B  88     6013   5099   5410   -341   -841   -767       C  
ATOM   4852  O   PRO B  88       0.765  -9.691 -47.837  1.00 42.80           O  
ANISOU 4852  O   PRO B  88     6048   4922   5292   -423   -877   -778       O  
ATOM   4853  CB  PRO B  88       3.495  -8.717 -48.697  1.00 33.35           C  
ANISOU 4853  CB  PRO B  88     4812   3776   4083   -104   -895   -758       C  
ATOM   4854  CG  PRO B  88       4.674  -8.948 -47.805  1.00 39.60           C  
ANISOU 4854  CG  PRO B  88     5679   4518   4847    -46   -904   -736       C  
ATOM   4855  CD  PRO B  88       4.146  -9.065 -46.390  1.00 40.27           C  
ANISOU 4855  CD  PRO B  88     5809   4557   4934   -166   -873   -708       C  
ATOM   4856  N   ASN B  89       0.257  -7.657 -48.756  1.00 38.84           N  
ANISOU 4856  N   ASN B  89     5293   4607   4858   -351   -814   -783       N  
ATOM   4857  CA  ASN B  89      -1.076  -8.066 -49.176  1.00 44.57           C  
ANISOU 4857  CA  ASN B  89     5989   5354   5590   -454   -826   -821       C  
ATOM   4858  C   ASN B  89      -1.212  -8.073 -50.710  1.00 47.06           C  
ANISOU 4858  C   ASN B  89     6268   5708   5905   -378   -872   -857       C  
ATOM   4859  O   ASN B  89      -2.327  -8.105 -51.247  1.00 46.64           O  
ANISOU 4859  O   ASN B  89     6152   5705   5864   -439   -882   -894       O  
ATOM   4860  CB  ASN B  89      -2.145  -7.182 -48.521  1.00 45.97           C  
ANISOU 4860  CB  ASN B  89     6043   5621   5804   -540   -763   -820       C  
ATOM   4861  CG  ASN B  89      -2.066  -5.745 -48.984  1.00 46.86           C  
ANISOU 4861  CG  ASN B  89     6025   5831   5950   -441   -731   -814       C  
ATOM   4862  OD1 ASN B  89      -3.036  -4.989 -48.890  1.00 52.94           O  
ANISOU 4862  OD1 ASN B  89     6682   6687   6747   -477   -698   -830       O  
ATOM   4863  ND2 ASN B  89      -0.918  -5.368 -49.521  1.00 35.76           N  
ANISOU 4863  ND2 ASN B  89     4635   4416   4537   -313   -744   -794       N  
ATOM   4864  N   ARG B  90      -0.077  -8.001 -51.408  1.00 39.44           N  
ANISOU 4864  N   ARG B  90     5333   4730   4922   -243   -898   -850       N  
ATOM   4865  CA  ARG B  90      -0.029  -8.230 -52.859  1.00 38.85           C  
ANISOU 4865  CA  ARG B  90     5256   4673   4831   -165   -948   -884       C  
ATOM   4866  C   ARG B  90       1.200  -9.077 -53.137  1.00 43.90           C  
ANISOU 4866  C   ARG B  90     6018   5236   5427    -72   -995   -886       C  
ATOM   4867  O   ARG B  90       1.973  -9.349 -52.225  1.00 40.89           O  
ANISOU 4867  O   ARG B  90     5706   4799   5033    -63   -988   -860       O  
ATOM   4868  CB  ARG B  90       0.037  -6.920 -53.655  1.00 35.84           C  
ANISOU 4868  CB  ARG B  90     4753   4394   4470    -73   -920   -878       C  
ATOM   4869  CG  ARG B  90      -1.218  -6.045 -53.569  1.00 39.83           C  
ANISOU 4869  CG  ARG B  90     5136   4984   5013   -135   -886   -888       C  
ATOM   4870  CD  ARG B  90      -2.446  -6.798 -54.058  1.00 42.12           C  
ANISOU 4870  CD  ARG B  90     5422   5281   5302   -222   -928   -939       C  
ATOM   4871  NE  ARG B  90      -3.641  -5.966 -54.180  1.00 52.70           N  
ANISOU 4871  NE  ARG B  90     6631   6722   6672   -257   -907   -962       N  
ATOM   4872  CZ  ARG B  90      -4.498  -5.703 -53.187  1.00 56.95           C  
ANISOU 4872  CZ  ARG B  90     7106   7297   7235   -360   -865   -965       C  
ATOM   4873  NH1 ARG B  90      -4.278  -6.192 -51.969  1.00 55.66           N  
ANISOU 4873  NH1 ARG B  90     7006   7072   7068   -447   -835   -940       N  
ATOM   4874  NH2 ARG B  90      -5.578  -4.940 -53.408  1.00 52.76           N  
ANISOU 4874  NH2 ARG B  90     6449   6870   6727   -371   -853   -996       N  
ATOM   4875  N   GLU B  91       1.390  -9.483 -54.386  1.00 51.22           N  
ANISOU 4875  N   GLU B  91     6969   6164   6327      4  -1045   -920       N  
ATOM   4876  CA  GLU B  91       2.541 -10.318 -54.761  1.00 50.85           C  
ANISOU 4876  CA  GLU B  91     7034   6055   6232    109  -1095   -933       C  
ATOM   4877  C   GLU B  91       3.854  -9.600 -54.537  1.00 42.36           C  
ANISOU 4877  C   GLU B  91     5921   5021   5152    220  -1060   -902       C  
ATOM   4878  O   GLU B  91       3.953  -8.384 -54.726  1.00 40.79           O  
ANISOU 4878  O   GLU B  91     5607   4913   4979    250  -1007   -879       O  
ATOM   4879  CB  GLU B  91       2.459 -10.724 -56.231  1.00 57.41           C  
ANISOU 4879  CB  GLU B  91     7880   6900   7034    178  -1149   -978       C  
ATOM   4880  CG  GLU B  91       1.343 -11.702 -56.548  1.00 71.54           C  
ANISOU 4880  CG  GLU B  91     9735   8632   8815     76  -1203  -1019       C  
ATOM   4881  CD  GLU B  91       1.594 -13.098 -55.982  1.00 81.44           C  
ANISOU 4881  CD  GLU B  91    11164   9750  10029     37  -1257  -1032       C  
ATOM   4882  OE1 GLU B  91       2.713 -13.377 -55.487  1.00 76.93           O  
ANISOU 4882  OE1 GLU B  91    10668   9130   9432    118  -1265  -1015       O  
ATOM   4883  OE2 GLU B  91       0.659 -13.928 -56.049  1.00 94.39           O  
ANISOU 4883  OE2 GLU B  91    12872  11332  11662    -76  -1297  -1061       O  
ATOM   4884  N   LEU B  92       4.864 -10.354 -54.133  1.00 41.99           N  
ANISOU 4884  N   LEU B  92     5977   4910   5068    282  -1092   -905       N  
ATOM   4885  CA  LEU B  92       6.182  -9.795 -53.925  1.00 39.43           C  
ANISOU 4885  CA  LEU B  92     5615   4632   4732    388  -1065   -886       C  
ATOM   4886  C   LEU B  92       6.904  -9.637 -55.263  1.00 45.89           C  
ANISOU 4886  C   LEU B  92     6398   5519   5520    516  -1079   -913       C  
ATOM   4887  O   LEU B  92       6.863 -10.526 -56.110  1.00 47.79           O  
ANISOU 4887  O   LEU B  92     6712   5724   5723    562  -1138   -955       O  
ATOM   4888  CB  LEU B  92       6.990 -10.717 -53.043  1.00 37.19           C  
ANISOU 4888  CB  LEU B  92     5454   4262   4414    421  -1104   -888       C  
ATOM   4889  CG  LEU B  92       6.582 -10.982 -51.592  1.00 43.32           C  
ANISOU 4889  CG  LEU B  92     6295   4962   5205    311  -1093   -858       C  
ATOM   4890  CD1 LEU B  92       7.742 -11.737 -50.918  1.00 37.15           C  
ANISOU 4890  CD1 LEU B  92     5626   4113   4375    397  -1137   -863       C  
ATOM   4891  CD2 LEU B  92       6.274  -9.706 -50.846  1.00 41.30           C  
ANISOU 4891  CD2 LEU B  92     5915   4776   4999    244  -1013   -815       C  
ATOM   4892  N   SER B  93       7.597  -8.526 -55.453  1.00 41.33           N  
ANISOU 4892  N   SER B  93     5714   5038   4950    572  -1024   -891       N  
ATOM   4893  CA  SER B  93       8.387  -8.365 -56.661  1.00 35.53           C  
ANISOU 4893  CA  SER B  93     4947   4376   4175    688  -1029   -915       C  
ATOM   4894  C   SER B  93       9.430  -7.270 -56.483  1.00 38.57           C  
ANISOU 4894  C   SER B  93     5236   4856   4562    735   -966   -886       C  
ATOM   4895  O   SER B  93       9.192  -6.304 -55.754  1.00 44.27           O  
ANISOU 4895  O   SER B  93     5894   5601   5326    666   -912   -844       O  
ATOM   4896  CB  SER B  93       7.455  -8.026 -57.823  1.00 32.77           C  
ANISOU 4896  CB  SER B  93     4556   4063   3831    670  -1030   -926       C  
ATOM   4897  OG  SER B  93       8.157  -7.853 -59.032  1.00 31.63           O  
ANISOU 4897  OG  SER B  93     4386   3990   3642    775  -1031   -947       O  
ATOM   4898  N   GLU B  94      10.570  -7.389 -57.162  1.00 34.75           N  
ANISOU 4898  N   GLU B  94     4741   4434   4029    847   -971   -912       N  
ATOM   4899  CA  GLU B  94      11.511  -6.263 -57.245  1.00 29.81           C  
ANISOU 4899  CA  GLU B  94     4012   3917   3398    879   -905   -889       C  
ATOM   4900  C   GLU B  94      10.980  -5.157 -58.123  1.00 34.27           C  
ANISOU 4900  C   GLU B  94     4503   4545   3973    847   -857   -863       C  
ATOM   4901  O   GLU B  94      11.417  -4.028 -58.040  1.00 35.62           O  
ANISOU 4901  O   GLU B  94     4597   4786   4152    830   -796   -829       O  
ATOM   4902  CB  GLU B  94      12.862  -6.709 -57.753  1.00 28.27           C  
ANISOU 4902  CB  GLU B  94     3813   3787   3141   1003   -920   -930       C  
ATOM   4903  CG  GLU B  94      13.573  -7.528 -56.701  1.00 34.15           C  
ANISOU 4903  CG  GLU B  94     4616   4483   3875   1045   -960   -950       C  
ATOM   4904  CD  GLU B  94      14.954  -7.968 -57.152  1.00 40.84           C  
ANISOU 4904  CD  GLU B  94     5449   5411   4658   1183   -979  -1001       C  
ATOM   4905  OE1 GLU B  94      15.869  -7.114 -57.212  1.00 37.33           O  
ANISOU 4905  OE1 GLU B  94     4899   5084   4203   1203   -922   -994       O  
ATOM   4906  OE2 GLU B  94      15.105  -9.170 -57.462  1.00 40.93           O  
ANISOU 4906  OE2 GLU B  94     5555   5369   4626   1269  -1051  -1052       O  
ATOM   4907  N   ASP B  95      10.036  -5.515 -58.982  1.00 32.35           N  
ANISOU 4907  N   ASP B  95     4292   4273   3725    840   -892   -881       N  
ATOM   4908  CA  ASP B  95       9.388  -4.562 -59.824  1.00 35.46           C  
ANISOU 4908  CA  ASP B  95     4633   4715   4125    818   -861   -861       C  
ATOM   4909  C   ASP B  95       8.238  -4.020 -58.988  1.00 34.69           C  
ANISOU 4909  C   ASP B  95     4515   4576   4091    712   -845   -828       C  
ATOM   4910  O   ASP B  95       7.132  -4.552 -59.007  1.00 36.92           O  
ANISOU 4910  O   ASP B  95     4829   4804   4393    665   -885   -846       O  
ATOM   4911  CB  ASP B  95       8.927  -5.260 -61.087  1.00 31.50           C  
ANISOU 4911  CB  ASP B  95     4176   4208   3586    867   -913   -903       C  
ATOM   4912  CG  ASP B  95       8.055  -4.396 -61.946  1.00 39.25           C  
ANISOU 4912  CG  ASP B  95     5117   5225   4571    844   -897   -887       C  
ATOM   4913  OD1 ASP B  95       7.872  -3.199 -61.617  1.00 35.15           O  
ANISOU 4913  OD1 ASP B  95     4539   4737   4079    799   -844   -842       O  
ATOM   4914  OD2 ASP B  95       7.527  -4.943 -62.945  1.00 42.44           O  
ANISOU 4914  OD2 ASP B  95     5557   5622   4948    876   -945   -922       O  
ATOM   4915  N   CYS B  96       8.526  -2.986 -58.200  1.00 30.98           N  
ANISOU 4915  N   CYS B  96     3989   4132   3648    672   -788   -786       N  
ATOM   4916  CA  CYS B  96       7.563  -2.510 -57.203  1.00 30.56           C  
ANISOU 4916  CA  CYS B  96     3918   4042   3653    580   -770   -759       C  
ATOM   4917  C   CYS B  96       7.496  -0.997 -57.048  1.00 33.18           C  
ANISOU 4917  C   CYS B  96     4182   4420   4004    552   -709   -715       C  
ATOM   4918  O   CYS B  96       6.901  -0.527 -56.083  1.00 31.61           O  
ANISOU 4918  O   CYS B  96     3964   4199   3849    486   -689   -694       O  
ATOM   4919  CB  CYS B  96       7.903  -3.074 -55.818  1.00 22.39           C  
ANISOU 4919  CB  CYS B  96     2916   2953   2639    543   -774   -754       C  
ATOM   4920  SG  CYS B  96       9.605  -2.629 -55.204  1.00 37.48           S  
ANISOU 4920  SG  CYS B  96     4798   4913   4530    591   -734   -736       S  
ATOM   4921  N   LEU B  97       8.112  -0.236 -57.952  1.00 29.67           N  
ANISOU 4921  N   LEU B  97     3711   4038   3523    600   -680   -701       N  
ATOM   4922  CA  LEU B  97       8.177   1.216 -57.737  1.00 32.30           C  
ANISOU 4922  CA  LEU B  97     4002   4404   3868    570   -624   -657       C  
ATOM   4923  C   LEU B  97       6.935   1.894 -58.330  1.00 35.97           C  
ANISOU 4923  C   LEU B  97     4458   4866   4343    559   -632   -650       C  
ATOM   4924  O   LEU B  97       6.951   2.438 -59.450  1.00 35.50           O  
ANISOU 4924  O   LEU B  97     4401   4842   4243    600   -627   -643       O  
ATOM   4925  CB  LEU B  97       9.484   1.809 -58.261  1.00 30.48           C  
ANISOU 4925  CB  LEU B  97     3752   4240   3590    605   -581   -640       C  
ATOM   4926  CG  LEU B  97      10.743   1.299 -57.517  1.00 32.22           C  
ANISOU 4926  CG  LEU B  97     3961   4479   3802    617   -571   -650       C  
ATOM   4927  CD1 LEU B  97      11.965   2.010 -58.015  1.00 29.55           C  
ANISOU 4927  CD1 LEU B  97     3586   4225   3417    636   -520   -637       C  
ATOM   4928  CD2 LEU B  97      10.617   1.469 -55.968  1.00 28.65           C  
ANISOU 4928  CD2 LEU B  97     3502   3980   3402    554   -559   -632       C  
ATOM   4929  N   TYR B  98       5.855   1.841 -57.555  1.00 34.31           N  
ANISOU 4929  N   TYR B  98     4238   4618   4182    507   -646   -655       N  
ATOM   4930  CA  TYR B  98       4.594   2.455 -57.944  1.00 34.41           C  
ANISOU 4930  CA  TYR B  98     4230   4636   4208    501   -659   -658       C  
ATOM   4931  C   TYR B  98       4.083   3.306 -56.790  1.00 36.30           C  
ANISOU 4931  C   TYR B  98     4438   4862   4491    448   -626   -636       C  
ATOM   4932  O   TYR B  98       4.453   3.085 -55.638  1.00 34.91           O  
ANISOU 4932  O   TYR B  98     4260   4661   4341    403   -606   -626       O  
ATOM   4933  CB  TYR B  98       3.569   1.381 -58.334  1.00 31.28           C  
ANISOU 4933  CB  TYR B  98     3842   4224   3820    494   -718   -707       C  
ATOM   4934  CG  TYR B  98       4.079   0.442 -59.432  1.00 38.15           C  
ANISOU 4934  CG  TYR B  98     4753   5099   4643    550   -756   -735       C  
ATOM   4935  CD1 TYR B  98       3.743   0.644 -60.775  1.00 42.20           C  
ANISOU 4935  CD1 TYR B  98     5272   5645   5118    607   -782   -749       C  
ATOM   4936  CD2 TYR B  98       4.893  -0.632 -59.127  1.00 38.02           C  
ANISOU 4936  CD2 TYR B  98     4777   5055   4616    556   -770   -750       C  
ATOM   4937  CE1 TYR B  98       4.221  -0.198 -61.778  1.00 40.39           C  
ANISOU 4937  CE1 TYR B  98     5083   5423   4841    663   -816   -778       C  
ATOM   4938  CE2 TYR B  98       5.382  -1.484 -60.121  1.00 43.21           C  
ANISOU 4938  CE2 TYR B  98     5474   5717   5225    619   -806   -782       C  
ATOM   4939  CZ  TYR B  98       5.033  -1.264 -61.446  1.00 49.25           C  
ANISOU 4939  CZ  TYR B  98     6241   6518   5954    670   -827   -796       C  
ATOM   4940  OH  TYR B  98       5.524  -2.095 -62.427  1.00 46.69           O  
ANISOU 4940  OH  TYR B  98     5960   6203   5579    736   -862   -830       O  
ATOM   4941  N   LEU B  99       3.229   4.276 -57.101  1.00 33.80           N  
ANISOU 4941  N   LEU B  99     4102   4562   4179    462   -626   -630       N  
ATOM   4942  CA  LEU B  99       2.618   5.063 -56.065  1.00 34.32           C  
ANISOU 4942  CA  LEU B  99     4138   4620   4283    424   -601   -619       C  
ATOM   4943  C   LEU B  99       1.089   5.117 -56.249  1.00 41.30           C  
ANISOU 4943  C   LEU B  99     4982   5524   5185    427   -637   -656       C  
ATOM   4944  O   LEU B  99       0.564   4.744 -57.291  1.00 38.55           O  
ANISOU 4944  O   LEU B  99     4634   5197   4817    464   -680   -685       O  
ATOM   4945  CB  LEU B  99       3.246   6.469 -55.993  1.00 28.22           C  
ANISOU 4945  CB  LEU B  99     3382   3848   3493    440   -558   -573       C  
ATOM   4946  CG  LEU B  99       3.243   7.361 -57.245  1.00 35.20           C  
ANISOU 4946  CG  LEU B  99     4296   4749   4329    502   -564   -556       C  
ATOM   4947  CD1 LEU B  99       1.839   7.860 -57.602  1.00 29.12           C  
ANISOU 4947  CD1 LEU B  99     3510   3990   3565    540   -601   -580       C  
ATOM   4948  CD2 LEU B  99       4.258   8.570 -57.101  1.00 35.22           C  
ANISOU 4948  CD2 LEU B  99     4335   4741   4305    493   -513   -503       C  
ATOM   4949  N   ASN B 100       0.396   5.607 -55.224  1.00 40.32           N  
ANISOU 4949  N   ASN B 100     4820   5401   5096    391   -618   -659       N  
ATOM   4950  CA  ASN B 100      -1.043   5.629 -55.194  1.00 35.26           C  
ANISOU 4950  CA  ASN B 100     4124   4797   4476    386   -645   -703       C  
ATOM   4951  C   ASN B 100      -1.520   7.035 -54.858  1.00 37.60           C  
ANISOU 4951  C   ASN B 100     4401   5108   4776    423   -627   -692       C  
ATOM   4952  O   ASN B 100      -0.920   7.704 -54.026  1.00 34.61           O  
ANISOU 4952  O   ASN B 100     4043   4703   4406    406   -584   -657       O  
ATOM   4953  CB  ASN B 100      -1.532   4.690 -54.104  1.00 32.20           C  
ANISOU 4953  CB  ASN B 100     3705   4405   4125    296   -638   -728       C  
ATOM   4954  CG  ASN B 100      -0.852   3.329 -54.150  1.00 32.79           C  
ANISOU 4954  CG  ASN B 100     3826   4441   4193    256   -652   -730       C  
ATOM   4955  OD1 ASN B 100      -0.983   2.571 -55.132  1.00 36.99           O  
ANISOU 4955  OD1 ASN B 100     4374   4977   4705    275   -696   -756       O  
ATOM   4956  ND2 ASN B 100      -0.157   2.987 -53.060  1.00 28.43           N  
ANISOU 4956  ND2 ASN B 100     3300   3848   3653    204   -620   -706       N  
ATOM   4957  N   VAL B 101      -2.603   7.475 -55.505  1.00 40.62           N  
ANISOU 4957  N   VAL B 101     4749   5534   5149    479   -665   -727       N  
ATOM   4958  CA  VAL B 101      -3.194   8.777 -55.234  1.00 37.51           C  
ANISOU 4958  CA  VAL B 101     4342   5155   4754    532   -660   -727       C  
ATOM   4959  C   VAL B 101      -4.696   8.620 -54.983  1.00 36.44           C  
ANISOU 4959  C   VAL B 101     4114   5090   4641    532   -689   -794       C  
ATOM   4960  O   VAL B 101      -5.394   8.017 -55.781  1.00 37.25           O  
ANISOU 4960  O   VAL B 101     4180   5235   4736    547   -737   -838       O  
ATOM   4961  CB  VAL B 101      -3.020   9.742 -56.438  1.00 43.55           C  
ANISOU 4961  CB  VAL B 101     5168   5909   5468    630   -687   -706       C  
ATOM   4962  CG1 VAL B 101      -3.648  11.078 -56.136  1.00 35.95           C  
ANISOU 4962  CG1 VAL B 101     4210   4950   4498    695   -691   -709       C  
ATOM   4963  CG2 VAL B 101      -1.514   9.920 -56.841  1.00 29.56           C  
ANISOU 4963  CG2 VAL B 101     3483   4085   3664    623   -655   -643       C  
ATOM   4964  N   TRP B 102      -5.185   9.158 -53.874  1.00 34.66           N  
ANISOU 4964  N   TRP B 102     3847   4883   4441    515   -660   -806       N  
ATOM   4965  CA  TRP B 102      -6.618   9.296 -53.653  1.00 34.95           C  
ANISOU 4965  CA  TRP B 102     3786   5003   4489    534   -683   -873       C  
ATOM   4966  C   TRP B 102      -6.981  10.771 -53.699  1.00 40.75           C  
ANISOU 4966  C   TRP B 102     4536   5745   5204    643   -694   -875       C  
ATOM   4967  O   TRP B 102      -6.254  11.591 -53.123  1.00 43.59           O  
ANISOU 4967  O   TRP B 102     4959   6044   5558    652   -657   -828       O  
ATOM   4968  CB  TRP B 102      -6.975   8.820 -52.261  1.00 34.70           C  
ANISOU 4968  CB  TRP B 102     3693   4997   4495    434   -637   -893       C  
ATOM   4969  CG  TRP B 102      -6.942   7.359 -52.069  1.00 34.54           C  
ANISOU 4969  CG  TRP B 102     3655   4977   4492    322   -632   -904       C  
ATOM   4970  CD1 TRP B 102      -7.994   6.487 -52.215  1.00 35.24           C  
ANISOU 4970  CD1 TRP B 102     3663   5137   4590    266   -657   -966       C  
ATOM   4971  CD2 TRP B 102      -5.821   6.580 -51.663  1.00 33.02           C  
ANISOU 4971  CD2 TRP B 102     3533   4709   4306    248   -603   -856       C  
ATOM   4972  NE1 TRP B 102      -7.589   5.218 -51.910  1.00 39.58           N  
ANISOU 4972  NE1 TRP B 102     4244   5646   5150    157   -644   -955       N  
ATOM   4973  CE2 TRP B 102      -6.255   5.242 -51.589  1.00 36.04           C  
ANISOU 4973  CE2 TRP B 102     3889   5107   4698    154   -615   -889       C  
ATOM   4974  CE3 TRP B 102      -4.483   6.882 -51.364  1.00 32.10           C  
ANISOU 4974  CE3 TRP B 102     3500   4515   4183    253   -572   -793       C  
ATOM   4975  CZ2 TRP B 102      -5.399   4.207 -51.224  1.00 30.72           C  
ANISOU 4975  CZ2 TRP B 102     3282   4365   4026     78   -601   -858       C  
ATOM   4976  CZ3 TRP B 102      -3.640   5.861 -50.997  1.00 35.49           C  
ANISOU 4976  CZ3 TRP B 102     3977   4893   4617    182   -558   -768       C  
ATOM   4977  CH2 TRP B 102      -4.096   4.539 -50.919  1.00 36.27           C  
ANISOU 4977  CH2 TRP B 102     4060   4998   4723    101   -574   -799       C  
ATOM   4978  N   THR B 103      -8.094  11.121 -54.353  1.00 38.71           N  
ANISOU 4978  N   THR B 103     4223   5556   4928    729   -749   -933       N  
ATOM   4979  CA  THR B 103      -8.587  12.504 -54.336  1.00 42.47           C  
ANISOU 4979  CA  THR B 103     4715   6041   5379    848   -769   -946       C  
ATOM   4980  C   THR B 103     -10.079  12.488 -54.089  1.00 48.58           C  
ANISOU 4980  C   THR B 103     5358   6936   6165    883   -799  -1037       C  
ATOM   4981  O   THR B 103     -10.715  11.445 -54.249  1.00 50.40           O  
ANISOU 4981  O   THR B 103     5495   7241   6414    820   -814  -1087       O  
ATOM   4982  CB  THR B 103      -8.360  13.263 -55.664  1.00 45.13           C  
ANISOU 4982  CB  THR B 103     5148   6338   5663    965   -823   -922       C  
ATOM   4983  OG1 THR B 103      -9.082  12.614 -56.716  1.00 57.63           O  
ANISOU 4983  OG1 THR B 103     6677   7986   7232    998   -885   -972       O  
ATOM   4984  CG2 THR B 103      -6.928  13.260 -56.045  1.00 52.56           C  
ANISOU 4984  CG2 THR B 103     6206   7179   6584    928   -793   -839       C  
ATOM   4985  N   PRO B 104     -10.646  13.647 -53.691  1.00 49.19           N  
ANISOU 4985  N   PRO B 104     5427   7035   6226    983   -810  -1064       N  
ATOM   4986  CA  PRO B 104     -12.097  13.822 -53.671  1.00 47.66           C  
ANISOU 4986  CA  PRO B 104     5107   6971   6030   1054   -852  -1160       C  
ATOM   4987  C   PRO B 104     -12.676  13.536 -55.050  1.00 50.45           C  
ANISOU 4987  C   PRO B 104     5436   7376   6357   1126   -932  -1201       C  
ATOM   4988  O   PRO B 104     -11.983  13.715 -56.051  1.00 56.33           O  
ANISOU 4988  O   PRO B 104     6293   8040   7069   1171   -961  -1149       O  
ATOM   4989  CB  PRO B 104     -12.247  15.309 -53.349  1.00 44.44           C  
ANISOU 4989  CB  PRO B 104     4757   6536   5592   1188   -864  -1162       C  
ATOM   4990  CG  PRO B 104     -11.051  15.619 -52.558  1.00 44.37           C  
ANISOU 4990  CG  PRO B 104     4853   6411   5594   1119   -798  -1080       C  
ATOM   4991  CD  PRO B 104      -9.964  14.876 -53.259  1.00 42.00           C  
ANISOU 4991  CD  PRO B 104     4629   6034   5297   1039   -787  -1010       C  
ATOM   4992  N   TYR B 105     -13.920  13.074 -55.074  1.00 51.24           N  
ANISOU 4992  N   TYR B 105     5387   7615   6467   1129   -963  -1295       N  
ATOM   4993  CA  TYR B 105     -14.689  12.831 -56.283  1.00 51.06           C  
ANISOU 4993  CA  TYR B 105     5314   7667   6419   1204  -1047  -1354       C  
ATOM   4994  C   TYR B 105     -15.965  13.636 -56.123  1.00 54.27           C  
ANISOU 4994  C   TYR B 105     5615   8197   6807   1335  -1094  -1449       C  
ATOM   4995  O   TYR B 105     -16.747  13.359 -55.211  1.00 57.53           O  
ANISOU 4995  O   TYR B 105     5888   8723   7248   1277  -1061  -1514       O  
ATOM   4996  CB  TYR B 105     -15.074  11.351 -56.371  1.00 46.02           C  
ANISOU 4996  CB  TYR B 105     4570   7103   5814   1061  -1042  -1395       C  
ATOM   4997  CG  TYR B 105     -15.917  11.018 -57.580  1.00 48.46           C  
ANISOU 4997  CG  TYR B 105     4814   7500   6098   1125  -1131  -1466       C  
ATOM   4998  CD1 TYR B 105     -15.428  10.186 -58.578  1.00 49.84           C  
ANISOU 4998  CD1 TYR B 105     5049   7625   6264   1082  -1160  -1438       C  
ATOM   4999  CD2 TYR B 105     -17.189  11.559 -57.743  1.00 51.12           C  
ANISOU 4999  CD2 TYR B 105     5032   7974   6416   1239  -1190  -1564       C  
ATOM   5000  CE1 TYR B 105     -16.171   9.888 -59.692  1.00 53.40           C  
ANISOU 5000  CE1 TYR B 105     5447   8153   6689   1142  -1244  -1503       C  
ATOM   5001  CE2 TYR B 105     -17.947  11.265 -58.857  1.00 56.54           C  
ANISOU 5001  CE2 TYR B 105     5659   8746   7077   1302  -1277  -1632       C  
ATOM   5002  CZ  TYR B 105     -17.426  10.427 -59.834  1.00 61.36           C  
ANISOU 5002  CZ  TYR B 105     6337   9298   7681   1249  -1304  -1599       C  
ATOM   5003  OH  TYR B 105     -18.156  10.121 -60.953  1.00 64.14           O  
ANISOU 5003  OH  TYR B 105     6634   9731   8005   1310  -1394  -1667       O  
ATOM   5004  N   PRO B 106     -16.206  14.625 -57.002  1.00 57.28           N  
ANISOU 5004  N   PRO B 106     6064   8565   7136   1514  -1171  -1460       N  
ATOM   5005  CA  PRO B 106     -15.409  15.010 -58.173  1.00 57.15           C  
ANISOU 5005  CA  PRO B 106     6213   8427   7072   1588  -1214  -1390       C  
ATOM   5006  C   PRO B 106     -14.122  15.644 -57.699  1.00 55.40           C  
ANISOU 5006  C   PRO B 106     6152   8050   6847   1559  -1152  -1283       C  
ATOM   5007  O   PRO B 106     -14.033  15.973 -56.523  1.00 55.68           O  
ANISOU 5007  O   PRO B 106     6168   8078   6909   1521  -1094  -1277       O  
ATOM   5008  CB  PRO B 106     -16.282  16.066 -58.859  1.00 52.08           C  
ANISOU 5008  CB  PRO B 106     5583   7834   6373   1797  -1310  -1449       C  
ATOM   5009  CG  PRO B 106     -17.047  16.673 -57.749  1.00 50.75           C  
ANISOU 5009  CG  PRO B 106     5317   7747   6218   1846  -1293  -1513       C  
ATOM   5010  CD  PRO B 106     -17.284  15.593 -56.728  1.00 50.27           C  
ANISOU 5010  CD  PRO B 106     5101   7775   6223   1666  -1216  -1545       C  
ATOM   5011  N   ARG B 107     -13.159  15.832 -58.592  1.00 58.53           N  
ANISOU 5011  N   ARG B 107     6701   8332   7207   1576  -1163  -1204       N  
ATOM   5012  CA  ARG B 107     -11.833  16.248 -58.176  1.00 60.66           C  
ANISOU 5012  CA  ARG B 107     7109   8465   7476   1515  -1096  -1104       C  
ATOM   5013  C   ARG B 107     -11.785  17.724 -57.775  1.00 61.76           C  
ANISOU 5013  C   ARG B 107     7351   8537   7578   1625  -1103  -1084       C  
ATOM   5014  O   ARG B 107     -12.501  18.549 -58.331  1.00 65.17           O  
ANISOU 5014  O   ARG B 107     7814   8986   7960   1781  -1177  -1123       O  
ATOM   5015  CB  ARG B 107     -10.781  15.864 -59.231  1.00 66.41           C  
ANISOU 5015  CB  ARG B 107     7950   9108   8174   1477  -1095  -1030       C  
ATOM   5016  CG  ARG B 107     -10.356  16.926 -60.233  1.00 73.23           C  
ANISOU 5016  CG  ARG B 107     8981   9881   8960   1592  -1138   -979       C  
ATOM   5017  CD  ARG B 107      -9.178  16.385 -61.060  1.00 78.09           C  
ANISOU 5017  CD  ARG B 107     9690  10428   9554   1517  -1111   -905       C  
ATOM   5018  NE  ARG B 107      -9.463  15.027 -61.544  1.00 79.31           N  
ANISOU 5018  NE  ARG B 107     9741  10658   9736   1458  -1127   -947       N  
ATOM   5019  CZ  ARG B 107      -9.350  14.616 -62.807  1.00 78.06           C  
ANISOU 5019  CZ  ARG B 107     9624  10502   9535   1489  -1171   -943       C  
ATOM   5020  NH1 ARG B 107      -9.656  13.368 -63.119  1.00 77.66           N  
ANISOU 5020  NH1 ARG B 107     9478  10518   9513   1429  -1187   -987       N  
ATOM   5021  NH2 ARG B 107      -8.910  15.431 -63.756  1.00 78.42           N  
ANISOU 5021  NH2 ARG B 107     9813  10478   9504   1573  -1198   -894       N  
ATOM   5022  N   PRO B 108     -10.938  18.056 -56.796  1.00 58.60           N  
ANISOU 5022  N   PRO B 108     7010   8057   7200   1548  -1030  -1026       N  
ATOM   5023  CA  PRO B 108     -10.963  19.403 -56.221  1.00 61.83           C  
ANISOU 5023  CA  PRO B 108     7508   8405   7580   1639  -1033  -1017       C  
ATOM   5024  C   PRO B 108     -11.048  20.486 -57.303  1.00 67.96           C  
ANISOU 5024  C   PRO B 108     8433   9112   8274   1794  -1110  -1001       C  
ATOM   5025  O   PRO B 108     -10.330  20.426 -58.306  1.00 66.70           O  
ANISOU 5025  O   PRO B 108     8382   8884   8078   1780  -1120   -940       O  
ATOM   5026  CB  PRO B 108      -9.622  19.500 -55.486  1.00 59.06           C  
ANISOU 5026  CB  PRO B 108     7247   7945   7249   1514   -950   -929       C  
ATOM   5027  CG  PRO B 108      -9.259  18.075 -55.160  1.00 57.39           C  
ANISOU 5027  CG  PRO B 108     6929   7781   7097   1359   -895   -923       C  
ATOM   5028  CD  PRO B 108      -9.815  17.244 -56.297  1.00 52.64           C  
ANISOU 5028  CD  PRO B 108     6262   7251   6486   1382   -949   -962       C  
ATOM   5029  N   ALA B 109     -11.922  21.464 -57.090  1.00 66.74           N  
ANISOU 5029  N   ALA B 109     8290   8979   8088   1944  -1164  -1057       N  
ATOM   5030  CA  ALA B 109     -12.030  22.603 -57.987  1.00 74.98           C  
ANISOU 5030  CA  ALA B 109     9499   9942   9047   2103  -1242  -1041       C  
ATOM   5031  C   ALA B 109     -10.862  23.564 -57.792  1.00 72.99           C  
ANISOU 5031  C   ALA B 109     9454   9520   8758   2069  -1203   -942       C  
ATOM   5032  O   ALA B 109     -10.451  24.256 -58.723  1.00 73.58           O  
ANISOU 5032  O   ALA B 109     9705   9493   8759   2129  -1243   -889       O  
ATOM   5033  CB  ALA B 109     -13.340  23.321 -57.760  1.00 80.47           C  
ANISOU 5033  CB  ALA B 109    10140  10716   9717   2285  -1317  -1140       C  
ATOM   5034  N   SER B 110     -10.337  23.624 -56.576  1.00 67.38           N  
ANISOU 5034  N   SER B 110     8728   8780   8094   1967  -1127   -919       N  
ATOM   5035  CA  SER B 110      -9.163  24.450 -56.326  1.00 63.18           C  
ANISOU 5035  CA  SER B 110     8378   8095   7533   1908  -1084   -827       C  
ATOM   5036  C   SER B 110      -8.045  23.589 -55.741  1.00 55.79           C  
ANISOU 5036  C   SER B 110     7392   7148   6657   1709   -986   -770       C  
ATOM   5037  O   SER B 110      -8.306  22.570 -55.119  1.00 61.77           O  
ANISOU 5037  O   SER B 110     7984   8004   7483   1631   -949   -808       O  
ATOM   5038  CB  SER B 110      -9.510  25.634 -55.417  1.00 61.42           C  
ANISOU 5038  CB  SER B 110     8226   7820   7289   2000  -1099   -852       C  
ATOM   5039  OG  SER B 110     -10.119  25.196 -54.218  1.00 65.53           O  
ANISOU 5039  OG  SER B 110     8575   8447   7876   1975  -1064   -921       O  
ATOM   5040  N   PRO B 111      -6.793  23.977 -55.978  1.00 48.58           N  
ANISOU 5040  N   PRO B 111     6626   6118   5714   1626   -947   -679       N  
ATOM   5041  CA  PRO B 111      -5.629  23.233 -55.485  1.00 47.88           C  
ANISOU 5041  CA  PRO B 111     6500   6017   5673   1449   -860   -624       C  
ATOM   5042  C   PRO B 111      -5.701  22.853 -54.000  1.00 47.29           C  
ANISOU 5042  C   PRO B 111     6309   5989   5672   1375   -806   -655       C  
ATOM   5043  O   PRO B 111      -5.798  23.710 -53.133  1.00 46.91           O  
ANISOU 5043  O   PRO B 111     6308   5896   5618   1404   -800   -662       O  
ATOM   5044  CB  PRO B 111      -4.480  24.210 -55.737  1.00 45.67           C  
ANISOU 5044  CB  PRO B 111     6416   5600   5336   1404   -837   -538       C  
ATOM   5045  CG  PRO B 111      -4.893  24.918 -56.986  1.00 44.12           C  
ANISOU 5045  CG  PRO B 111     6350   5357   5055   1530   -911   -530       C  
ATOM   5046  CD  PRO B 111      -6.394  25.106 -56.834  1.00 48.53           C  
ANISOU 5046  CD  PRO B 111     6833   5988   5618   1692   -985   -623       C  
ATOM   5047  N   THR B 112      -5.620  21.558 -53.717  1.00 48.21           N  
ANISOU 5047  N   THR B 112     6283   6188   5848   1277   -767   -670       N  
ATOM   5048  CA  THR B 112      -5.757  21.052 -52.355  1.00 47.59           C  
ANISOU 5048  CA  THR B 112     6090   6161   5833   1202   -717   -700       C  
ATOM   5049  C   THR B 112      -4.414  20.650 -51.728  1.00 40.58           C  
ANISOU 5049  C   THR B 112     5224   5223   4974   1053   -643   -637       C  
ATOM   5050  O   THR B 112      -3.609  20.054 -52.406  1.00 42.40           O  
ANISOU 5050  O   THR B 112     5472   5440   5200    988   -628   -594       O  
ATOM   5051  CB  THR B 112      -6.614  19.785 -52.400  1.00 47.95           C  
ANISOU 5051  CB  THR B 112     5964   6331   5923   1183   -725   -763       C  
ATOM   5052  OG1 THR B 112      -7.703  20.025 -53.276  1.00 61.56           O  
ANISOU 5052  OG1 THR B 112     7665   8109   7614   1315   -799   -819       O  
ATOM   5053  CG2 THR B 112      -7.149  19.465 -51.047  1.00 43.77           C  
ANISOU 5053  CG2 THR B 112     5320   5868   5442   1141   -687   -811       C  
ATOM   5054  N   PRO B 113      -4.214  20.925 -50.422  1.00 35.63           N  
ANISOU 5054  N   PRO B 113     4586   4578   4374   1005   -601   -638       N  
ATOM   5055  CA  PRO B 113      -3.086  20.374 -49.657  1.00 36.68           C  
ANISOU 5055  CA  PRO B 113     4707   4687   4540    867   -536   -594       C  
ATOM   5056  C   PRO B 113      -2.901  18.900 -49.947  1.00 37.45           C  
ANISOU 5056  C   PRO B 113     4705   4849   4674    791   -520   -597       C  
ATOM   5057  O   PRO B 113      -3.890  18.169 -50.010  1.00 40.29           O  
ANISOU 5057  O   PRO B 113     4959   5292   5056    814   -540   -652       O  
ATOM   5058  CB  PRO B 113      -3.523  20.538 -48.200  1.00 29.96           C  
ANISOU 5058  CB  PRO B 113     3802   3860   3722    855   -508   -631       C  
ATOM   5059  CG  PRO B 113      -4.369  21.805 -48.252  1.00 40.17           C  
ANISOU 5059  CG  PRO B 113     5158   5130   4975    990   -554   -665       C  
ATOM   5060  CD  PRO B 113      -5.052  21.823 -49.605  1.00 39.09           C  
ANISOU 5060  CD  PRO B 113     5027   5020   4806   1091   -617   -686       C  
ATOM   5061  N   VAL B 114      -1.651  18.489 -50.128  1.00 31.81           N  
ANISOU 5061  N   VAL B 114     4028   4099   3960    702   -487   -542       N  
ATOM   5062  CA  VAL B 114      -1.310  17.096 -50.390  1.00 30.68           C  
ANISOU 5062  CA  VAL B 114     3810   4001   3844    634   -474   -542       C  
ATOM   5063  C   VAL B 114      -0.631  16.459 -49.178  1.00 32.48           C  
ANISOU 5063  C   VAL B 114     3999   4229   4112    531   -424   -531       C  
ATOM   5064  O   VAL B 114       0.245  17.051 -48.578  1.00 34.48           O  
ANISOU 5064  O   VAL B 114     4310   4432   4360    489   -393   -495       O  
ATOM   5065  CB  VAL B 114      -0.329  16.996 -51.572  1.00 34.16           C  
ANISOU 5065  CB  VAL B 114     4319   4413   4249    620   -476   -494       C  
ATOM   5066  CG1 VAL B 114      -0.022  15.499 -51.904  1.00 28.48           C  
ANISOU 5066  CG1 VAL B 114     3527   3742   3553    565   -471   -502       C  
ATOM   5067  CG2 VAL B 114      -0.895  17.734 -52.775  1.00 33.68           C  
ANISOU 5067  CG2 VAL B 114     4322   4338   4136    721   -526   -496       C  
ATOM   5068  N   LEU B 115      -1.017  15.243 -48.826  1.00 32.41           N  
ANISOU 5068  N   LEU B 115     3900   4276   4139    487   -419   -562       N  
ATOM   5069  CA  LEU B 115      -0.337  14.522 -47.769  1.00 29.34           C  
ANISOU 5069  CA  LEU B 115     3487   3881   3778    394   -379   -549       C  
ATOM   5070  C   LEU B 115       0.318  13.332 -48.463  1.00 39.64           C  
ANISOU 5070  C   LEU B 115     4781   5195   5084    355   -385   -536       C  
ATOM   5071  O   LEU B 115      -0.337  12.644 -49.256  1.00 36.43           O  
ANISOU 5071  O   LEU B 115     4336   4827   4678    379   -417   -564       O  
ATOM   5072  CB  LEU B 115      -1.336  14.019 -46.730  1.00 31.98           C  
ANISOU 5072  CB  LEU B 115     3742   4266   4145    369   -368   -596       C  
ATOM   5073  CG  LEU B 115      -1.766  14.954 -45.595  1.00 44.74           C  
ANISOU 5073  CG  LEU B 115     5360   5876   5763    384   -346   -612       C  
ATOM   5074  CD1 LEU B 115      -3.144  14.657 -45.130  1.00 48.05           C  
ANISOU 5074  CD1 LEU B 115     5687   6373   6198    397   -349   -674       C  
ATOM   5075  CD2 LEU B 115      -0.852  14.802 -44.424  1.00 48.67           C  
ANISOU 5075  CD2 LEU B 115     5880   6337   6273    305   -304   -583       C  
ATOM   5076  N   ILE B 116       1.598  13.093 -48.171  1.00 32.10           N  
ANISOU 5076  N   ILE B 116     3858   4210   4127    300   -358   -498       N  
ATOM   5077  CA  ILE B 116       2.310  11.962 -48.739  1.00 32.31           C  
ANISOU 5077  CA  ILE B 116     3877   4247   4151    273   -365   -491       C  
ATOM   5078  C   ILE B 116       2.744  11.035 -47.620  1.00 34.09           C  
ANISOU 5078  C   ILE B 116     4081   4469   4401    205   -346   -493       C  
ATOM   5079  O   ILE B 116       3.450  11.462 -46.719  1.00 34.27           O  
ANISOU 5079  O   ILE B 116     4125   4469   4428    171   -318   -472       O  
ATOM   5080  CB  ILE B 116       3.573  12.432 -49.432  1.00 36.12           C  
ANISOU 5080  CB  ILE B 116     4414   4709   4599    275   -353   -449       C  
ATOM   5081  CG1 ILE B 116       3.233  13.565 -50.414  1.00 33.67           C  
ANISOU 5081  CG1 ILE B 116     4154   4386   4254    336   -368   -436       C  
ATOM   5082  CG2 ILE B 116       4.287  11.250 -50.103  1.00 22.44           C  
ANISOU 5082  CG2 ILE B 116     2669   2999   2857    264   -363   -449       C  
ATOM   5083  CD1 ILE B 116       4.302  13.868 -51.423  1.00 28.35           C  
ANISOU 5083  CD1 ILE B 116     3533   3704   3535    335   -358   -399       C  
ATOM   5084  N   TRP B 117       2.291   9.788 -47.668  1.00 30.98           N  
ANISOU 5084  N   TRP B 117     3653   4095   4021    184   -364   -520       N  
ATOM   5085  CA  TRP B 117       2.558   8.815 -46.640  1.00 27.64           C  
ANISOU 5085  CA  TRP B 117     3227   3662   3615    122   -353   -524       C  
ATOM   5086  C   TRP B 117       3.758   7.924 -46.973  1.00 32.40           C  
ANISOU 5086  C   TRP B 117     3859   4250   4203    114   -364   -509       C  
ATOM   5087  O   TRP B 117       3.883   7.430 -48.080  1.00 29.77           O  
ANISOU 5087  O   TRP B 117     3529   3929   3854    147   -390   -516       O  
ATOM   5088  CB  TRP B 117       1.356   7.910 -46.473  1.00 29.41           C  
ANISOU 5088  CB  TRP B 117     3411   3910   3855     91   -368   -563       C  
ATOM   5089  CG  TRP B 117       1.618   6.797 -45.529  1.00 31.48           C  
ANISOU 5089  CG  TRP B 117     3689   4149   4123     23   -361   -564       C  
ATOM   5090  CD1 TRP B 117       1.854   5.479 -45.840  1.00 31.92           C  
ANISOU 5090  CD1 TRP B 117     3769   4187   4171      0   -389   -572       C  
ATOM   5091  CD2 TRP B 117       1.696   6.900 -44.096  1.00 29.59           C  
ANISOU 5091  CD2 TRP B 117     3458   3893   3892    -28   -329   -556       C  
ATOM   5092  NE1 TRP B 117       2.068   4.756 -44.675  1.00 36.53           N  
ANISOU 5092  NE1 TRP B 117     4385   4740   4756    -62   -377   -568       N  
ATOM   5093  CE2 TRP B 117       1.975   5.605 -43.595  1.00 34.59           C  
ANISOU 5093  CE2 TRP B 117     4126   4497   4519    -82   -339   -557       C  
ATOM   5094  CE3 TRP B 117       1.535   7.960 -43.187  1.00 27.43           C  
ANISOU 5094  CE3 TRP B 117     3175   3624   3625    -31   -295   -550       C  
ATOM   5095  CZ2 TRP B 117       2.097   5.344 -42.231  1.00 26.93           C  
ANISOU 5095  CZ2 TRP B 117     3181   3503   3547   -140   -315   -549       C  
ATOM   5096  CZ3 TRP B 117       1.654   7.698 -41.817  1.00 23.74           C  
ANISOU 5096  CZ3 TRP B 117     2724   3139   3159    -89   -269   -545       C  
ATOM   5097  CH2 TRP B 117       1.931   6.394 -41.359  1.00 32.00           C  
ANISOU 5097  CH2 TRP B 117     3804   4157   4196   -144   -279   -543       C  
ATOM   5098  N   ILE B 118       4.608   7.692 -45.986  1.00 29.98           N  
ANISOU 5098  N   ILE B 118     3572   3922   3898     79   -347   -494       N  
ATOM   5099  CA  ILE B 118       5.792   6.857 -46.161  1.00 31.69           C  
ANISOU 5099  CA  ILE B 118     3812   4132   4097     84   -361   -487       C  
ATOM   5100  C   ILE B 118       5.740   5.751 -45.100  1.00 28.92           C  
ANISOU 5100  C   ILE B 118     3482   3753   3754     39   -370   -498       C  
ATOM   5101  O   ILE B 118       5.947   5.994 -43.902  1.00 29.07           O  
ANISOU 5101  O   ILE B 118     3511   3755   3779      4   -349   -488       O  
ATOM   5102  CB  ILE B 118       7.084   7.685 -45.993  1.00 26.72           C  
ANISOU 5102  CB  ILE B 118     3190   3509   3452     89   -337   -460       C  
ATOM   5103  CG1 ILE B 118       7.095   8.862 -46.987  1.00 28.61           C  
ANISOU 5103  CG1 ILE B 118     3428   3765   3677    118   -324   -444       C  
ATOM   5104  CG2 ILE B 118       8.356   6.775 -46.190  1.00 28.03           C  
ANISOU 5104  CG2 ILE B 118     3366   3687   3596    106   -354   -464       C  
ATOM   5105  CD1 ILE B 118       8.404   9.735 -46.835  1.00 24.42           C  
ANISOU 5105  CD1 ILE B 118     2908   3244   3126    102   -296   -417       C  
ATOM   5106  N   TYR B 119       5.438   4.537 -45.521  1.00 28.33           N  
ANISOU 5106  N   TYR B 119     3425   3667   3673     38   -403   -519       N  
ATOM   5107  CA  TYR B 119       5.237   3.465 -44.540  1.00 32.06           C  
ANISOU 5107  CA  TYR B 119     3937   4100   4145    -13   -414   -527       C  
ATOM   5108  C   TYR B 119       6.494   3.143 -43.762  1.00 28.56           C  
ANISOU 5108  C   TYR B 119     3534   3632   3684     -6   -419   -513       C  
ATOM   5109  O   TYR B 119       7.583   3.472 -44.202  1.00 26.33           O  
ANISOU 5109  O   TYR B 119     3243   3372   3388     43   -421   -506       O  
ATOM   5110  CB  TYR B 119       4.721   2.185 -45.214  1.00 32.21           C  
ANISOU 5110  CB  TYR B 119     3984   4101   4155    -20   -455   -553       C  
ATOM   5111  CG  TYR B 119       5.551   1.674 -46.376  1.00 27.58           C  
ANISOU 5111  CG  TYR B 119     3417   3519   3544     48   -491   -561       C  
ATOM   5112  CD1 TYR B 119       6.743   1.000 -46.155  1.00 35.92           C  
ANISOU 5112  CD1 TYR B 119     4521   4553   4575     82   -513   -559       C  
ATOM   5113  CD2 TYR B 119       5.116   1.822 -47.687  1.00 28.98           C  
ANISOU 5113  CD2 TYR B 119     3566   3727   3719     86   -506   -575       C  
ATOM   5114  CE1 TYR B 119       7.490   0.493 -47.213  1.00 39.05           C  
ANISOU 5114  CE1 TYR B 119     4930   4963   4944    152   -545   -574       C  
ATOM   5115  CE2 TYR B 119       5.868   1.360 -48.749  1.00 32.29           C  
ANISOU 5115  CE2 TYR B 119     4004   4156   4111    149   -535   -585       C  
ATOM   5116  CZ  TYR B 119       7.044   0.667 -48.506  1.00 35.95           C  
ANISOU 5116  CZ  TYR B 119     4510   4601   4549    182   -553   -586       C  
ATOM   5117  OH  TYR B 119       7.796   0.153 -49.547  1.00 37.97           O  
ANISOU 5117  OH  TYR B 119     4780   4876   4773    253   -582   -603       O  
ATOM   5118  N   GLY B 120       6.319   2.512 -42.605  1.00 30.35           N  
ANISOU 5118  N   GLY B 120     3806   3820   3907    -56   -419   -512       N  
ATOM   5119  CA  GLY B 120       7.428   1.993 -41.823  1.00 36.28           C  
ANISOU 5119  CA  GLY B 120     4608   4541   4635    -42   -437   -505       C  
ATOM   5120  C   GLY B 120       7.562   0.484 -42.013  1.00 34.64           C  
ANISOU 5120  C   GLY B 120     4477   4285   4400    -31   -488   -521       C  
ATOM   5121  O   GLY B 120       7.019  -0.056 -42.982  1.00 36.06           O  
ANISOU 5121  O   GLY B 120     4659   4462   4579    -25   -510   -538       O  
ATOM   5122  N   GLY B 121       8.250  -0.193 -41.092  1.00 34.83           N  
ANISOU 5122  N   GLY B 121     4571   4265   4397    -28   -512   -517       N  
ATOM   5123  CA  GLY B 121       8.691  -1.582 -41.312  1.00 33.64           C  
ANISOU 5123  CA  GLY B 121     4509   4061   4210     10   -572   -534       C  
ATOM   5124  C   GLY B 121      10.200  -1.815 -41.215  1.00 34.04           C  
ANISOU 5124  C   GLY B 121     4579   4124   4231    100   -608   -543       C  
ATOM   5125  O   GLY B 121      10.753  -2.767 -41.812  1.00 40.41           O  
ANISOU 5125  O   GLY B 121     5436   4912   5007    169   -661   -567       O  
ATOM   5126  N   GLY B 122      10.885  -0.965 -40.445  1.00 35.27           N  
ANISOU 5126  N   GLY B 122     4695   4315   4392    104   -583   -530       N  
ATOM   5127  CA  GLY B 122      12.291  -1.187 -40.099  1.00 31.55           C  
ANISOU 5127  CA  GLY B 122     4236   3863   3889    181   -618   -544       C  
ATOM   5128  C   GLY B 122      13.257  -1.123 -41.274  1.00 34.40           C  
ANISOU 5128  C   GLY B 122     4536   4296   4238    270   -634   -569       C  
ATOM   5129  O   GLY B 122      14.404  -1.573 -41.174  1.00 37.22           O  
ANISOU 5129  O   GLY B 122     4903   4678   4562    349   -675   -594       O  
ATOM   5130  N   PHE B 123      12.786  -0.585 -42.401  1.00 29.65           N  
ANISOU 5130  N   PHE B 123     3872   3734   3660    260   -604   -567       N  
ATOM   5131  CA  PHE B 123      13.594  -0.502 -43.622  1.00 30.00           C  
ANISOU 5131  CA  PHE B 123     3861   3851   3687    334   -611   -589       C  
ATOM   5132  C   PHE B 123      13.819  -1.855 -44.261  1.00 34.17           C  
ANISOU 5132  C   PHE B 123     4454   4350   4179    411   -673   -624       C  
ATOM   5133  O   PHE B 123      14.570  -1.936 -45.220  1.00 40.16           O  
ANISOU 5133  O   PHE B 123     5172   5173   4915    485   -684   -649       O  
ATOM   5134  CB  PHE B 123      14.962   0.163 -43.379  1.00 25.28           C  
ANISOU 5134  CB  PHE B 123     3194   3336   3075    371   -599   -598       C  
ATOM   5135  CG  PHE B 123      14.882   1.663 -43.067  1.00 30.56           C  
ANISOU 5135  CG  PHE B 123     3793   4044   3775    300   -536   -568       C  
ATOM   5136  CD1 PHE B 123      14.437   2.569 -44.035  1.00 28.57           C  
ANISOU 5136  CD1 PHE B 123     3490   3825   3540    272   -493   -551       C  
ATOM   5137  CD2 PHE B 123      15.295   2.159 -41.821  1.00 30.51           C  
ANISOU 5137  CD2 PHE B 123     3783   4037   3774    268   -526   -558       C  
ATOM   5138  CE1 PHE B 123      14.348   3.935 -43.746  1.00 30.21           C  
ANISOU 5138  CE1 PHE B 123     3655   4052   3769    211   -441   -524       C  
ATOM   5139  CE2 PHE B 123      15.235   3.537 -41.531  1.00 29.53           C  
ANISOU 5139  CE2 PHE B 123     3607   3939   3674    203   -473   -533       C  
ATOM   5140  CZ  PHE B 123      14.771   4.418 -42.504  1.00 27.33           C  
ANISOU 5140  CZ  PHE B 123     3289   3685   3412    176   -432   -516       C  
ATOM   5141  N   TYR B 124      13.189  -2.904 -43.721  1.00 32.01           N  
ANISOU 5141  N   TYR B 124     4288   3981   3895    391   -713   -625       N  
ATOM   5142  CA  TYR B 124      13.254  -4.249 -44.295  1.00 32.21           C  
ANISOU 5142  CA  TYR B 124     4400   3954   3882    456   -779   -657       C  
ATOM   5143  C   TYR B 124      11.876  -4.759 -44.777  1.00 35.48           C  
ANISOU 5143  C   TYR B 124     4867   4302   4311    388   -783   -652       C  
ATOM   5144  O   TYR B 124      11.778  -5.840 -45.347  1.00 36.81           O  
ANISOU 5144  O   TYR B 124     5115   4420   4451    427   -836   -678       O  
ATOM   5145  CB  TYR B 124      13.867  -5.261 -43.302  1.00 37.67           C  
ANISOU 5145  CB  TYR B 124     5202   4579   4531    503   -840   -671       C  
ATOM   5146  CG  TYR B 124      12.953  -5.584 -42.128  1.00 40.35           C  
ANISOU 5146  CG  TYR B 124     5636   4819   4876    403   -837   -640       C  
ATOM   5147  CD1 TYR B 124      11.852  -6.420 -42.287  1.00 36.25           C  
ANISOU 5147  CD1 TYR B 124     5210   4211   4354    339   -855   -636       C  
ATOM   5148  CD2 TYR B 124      13.192  -5.042 -40.860  1.00 37.57           C  
ANISOU 5148  CD2 TYR B 124     5277   4468   4529    366   -815   -616       C  
ATOM   5149  CE1 TYR B 124      11.008  -6.706 -41.226  1.00 33.94           C  
ANISOU 5149  CE1 TYR B 124     4998   3837   4059    234   -845   -608       C  
ATOM   5150  CE2 TYR B 124      12.336  -5.308 -39.790  1.00 40.03           C  
ANISOU 5150  CE2 TYR B 124     5673   4696   4839    270   -804   -588       C  
ATOM   5151  CZ  TYR B 124      11.244  -6.138 -39.989  1.00 38.34           C  
ANISOU 5151  CZ  TYR B 124     5547   4401   4620    201   -817   -584       C  
ATOM   5152  OH  TYR B 124      10.412  -6.432 -38.937  1.00 39.38           O  
ANISOU 5152  OH  TYR B 124     5761   4460   4743     96   -801   -557       O  
ATOM   5153  N   SER B 125      10.826  -3.969 -44.581  1.00 32.95           N  
ANISOU 5153  N   SER B 125     4499   3987   4034    289   -729   -623       N  
ATOM   5154  CA  SER B 125       9.489  -4.417 -44.909  1.00 30.26           C  
ANISOU 5154  CA  SER B 125     4193   3597   3707    215   -732   -624       C  
ATOM   5155  C   SER B 125       8.518  -3.269 -45.085  1.00 29.59           C  
ANISOU 5155  C   SER B 125     4012   3562   3668    146   -671   -605       C  
ATOM   5156  O   SER B 125       8.846  -2.103 -44.816  1.00 30.21           O  
ANISOU 5156  O   SER B 125     4014   3697   3768    147   -626   -585       O  
ATOM   5157  CB  SER B 125       8.971  -5.378 -43.826  1.00 39.63           C  
ANISOU 5157  CB  SER B 125     5498   4683   4875    146   -757   -617       C  
ATOM   5158  OG  SER B 125       8.878  -4.743 -42.550  1.00 37.85           O  
ANISOU 5158  OG  SER B 125     5259   4458   4664     85   -715   -587       O  
ATOM   5159  N   GLY B 126       7.310  -3.594 -45.528  1.00 34.62           N  
ANISOU 5159  N   GLY B 126     4657   4178   4318     86   -674   -614       N  
ATOM   5160  CA  GLY B 126       6.236  -2.610 -45.619  1.00 31.53           C  
ANISOU 5160  CA  GLY B 126     4181   3834   3967     24   -625   -604       C  
ATOM   5161  C   GLY B 126       5.712  -2.426 -47.027  1.00 35.24           C  
ANISOU 5161  C   GLY B 126     4600   4345   4445     53   -635   -624       C  
ATOM   5162  O   GLY B 126       6.319  -2.945 -47.973  1.00 33.09           O  
ANISOU 5162  O   GLY B 126     4352   4074   4147    125   -672   -642       O  
ATOM   5163  N   ALA B 127       4.601  -1.679 -47.161  1.00 29.29           N  
ANISOU 5163  N   ALA B 127     3777   3630   3721      5   -603   -624       N  
ATOM   5164  CA  ALA B 127       3.937  -1.468 -48.438  1.00 31.32           C  
ANISOU 5164  CA  ALA B 127     3988   3929   3985     29   -616   -645       C  
ATOM   5165  C   ALA B 127       2.817  -0.432 -48.319  1.00 34.49           C  
ANISOU 5165  C   ALA B 127     4306   4380   4417    -11   -579   -644       C  
ATOM   5166  O   ALA B 127       2.200  -0.297 -47.269  1.00 35.86           O  
ANISOU 5166  O   ALA B 127     4468   4550   4608    -82   -550   -639       O  
ATOM   5167  CB  ALA B 127       3.335  -2.783 -48.929  1.00 34.49           C  
ANISOU 5167  CB  ALA B 127     4448   4287   4370     -2   -667   -678       C  
ATOM   5168  N   ALA B 128       2.509   0.242 -49.419  1.00 31.48           N  
ANISOU 5168  N   ALA B 128     3873   4049   4040     40   -582   -652       N  
ATOM   5169  CA  ALA B 128       1.598   1.365 -49.378  1.00 30.46           C  
ANISOU 5169  CA  ALA B 128     3670   3970   3934     32   -554   -653       C  
ATOM   5170  C   ALA B 128       0.180   0.842 -49.567  1.00 38.76           C  
ANISOU 5170  C   ALA B 128     4688   5042   4996    -24   -574   -694       C  
ATOM   5171  O   ALA B 128      -0.782   1.583 -49.452  1.00 34.96           O  
ANISOU 5171  O   ALA B 128     4140   4612   4534    -35   -556   -708       O  
ATOM   5172  CB  ALA B 128       1.982   2.427 -50.455  1.00 25.41           C  
ANISOU 5172  CB  ALA B 128     3002   3369   3283    118   -551   -641       C  
ATOM   5173  N   SER B 129       0.079  -0.463 -49.812  1.00 36.47           N  
ANISOU 5173  N   SER B 129     4451   4714   4692    -61   -612   -716       N  
ATOM   5174  CA  SER B 129      -1.186  -1.122 -50.076  1.00 35.42           C  
ANISOU 5174  CA  SER B 129     4294   4601   4564   -128   -637   -759       C  
ATOM   5175  C   SER B 129      -1.881  -1.710 -48.838  1.00 35.12           C  
ANISOU 5175  C   SER B 129     4265   4545   4534   -251   -614   -766       C  
ATOM   5176  O   SER B 129      -3.023  -2.174 -48.945  1.00 37.73           O  
ANISOU 5176  O   SER B 129     4561   4907   4869   -327   -625   -805       O  
ATOM   5177  CB  SER B 129      -1.019  -2.196 -51.181  1.00 38.07           C  
ANISOU 5177  CB  SER B 129     4687   4905   4875   -106   -697   -784       C  
ATOM   5178  OG  SER B 129      -0.112  -3.227 -50.820  1.00 35.72           O  
ANISOU 5178  OG  SER B 129     4493   4525   4553   -114   -717   -772       O  
ATOM   5179  N   LEU B 130      -1.221  -1.692 -47.678  1.00 28.26           N  
ANISOU 5179  N   LEU B 130     3442   3633   3663   -276   -582   -732       N  
ATOM   5180  CA  LEU B 130      -1.868  -2.202 -46.456  1.00 38.14           C  
ANISOU 5180  CA  LEU B 130     4710   4868   4913   -397   -553   -735       C  
ATOM   5181  C   LEU B 130      -3.175  -1.470 -46.165  1.00 42.70           C  
ANISOU 5181  C   LEU B 130     5174   5537   5513   -447   -516   -763       C  
ATOM   5182  O   LEU B 130      -3.284  -0.241 -46.421  1.00 36.36           O  
ANISOU 5182  O   LEU B 130     4291   4794   4729   -371   -498   -763       O  
ATOM   5183  CB  LEU B 130      -0.966  -2.058 -45.243  1.00 39.53           C  
ANISOU 5183  CB  LEU B 130     4944   4996   5082   -401   -522   -693       C  
ATOM   5184  CG  LEU B 130       0.444  -2.610 -45.430  1.00 42.87           C  
ANISOU 5184  CG  LEU B 130     5464   5345   5480   -331   -558   -669       C  
ATOM   5185  CD1 LEU B 130       1.174  -2.516 -44.121  1.00 41.05           C  
ANISOU 5185  CD1 LEU B 130     5283   5074   5239   -346   -531   -635       C  
ATOM   5186  CD2 LEU B 130       0.372  -4.062 -45.944  1.00 35.47           C  
ANISOU 5186  CD2 LEU B 130     4620   4342   4514   -363   -615   -690       C  
ATOM   5187  N   ASP B 131      -4.158  -2.217 -45.645  1.00 37.73           N  
ANISOU 5187  N   ASP B 131     4540   4919   4877   -572   -506   -790       N  
ATOM   5188  CA  ASP B 131      -5.460  -1.644 -45.294  1.00 46.36           C  
ANISOU 5188  CA  ASP B 131     5513   6115   5986   -628   -468   -827       C  
ATOM   5189  C   ASP B 131      -5.355  -0.440 -44.329  1.00 43.91           C  
ANISOU 5189  C   ASP B 131     5152   5842   5688   -593   -411   -806       C  
ATOM   5190  O   ASP B 131      -6.091   0.512 -44.479  1.00 40.93           O  
ANISOU 5190  O   ASP B 131     4669   5555   5328   -553   -394   -835       O  
ATOM   5191  CB  ASP B 131      -6.395  -2.677 -44.667  1.00 50.07           C  
ANISOU 5191  CB  ASP B 131     5994   6591   6438   -791   -453   -854       C  
ATOM   5192  CG  ASP B 131      -6.723  -3.853 -45.593  1.00 56.35           C  
ANISOU 5192  CG  ASP B 131     6836   7357   7219   -845   -510   -884       C  
ATOM   5193  OD1 ASP B 131      -6.585  -3.772 -46.850  1.00 50.44           O  
ANISOU 5193  OD1 ASP B 131     6070   6617   6479   -755   -561   -902       O  
ATOM   5194  OD2 ASP B 131      -7.157  -4.883 -45.025  1.00 64.19           O  
ANISOU 5194  OD2 ASP B 131     7888   8314   8187   -987   -503   -892       O  
ATOM   5195  N   VAL B 132      -4.459  -0.474 -43.344  1.00 42.26           N  
ANISOU 5195  N   VAL B 132     5023   5565   5469   -603   -386   -761       N  
ATOM   5196  CA  VAL B 132      -4.369   0.660 -42.418  1.00 42.60           C  
ANISOU 5196  CA  VAL B 132     5024   5642   5522   -573   -335   -745       C  
ATOM   5197  C   VAL B 132      -3.830   1.946 -43.040  1.00 44.03           C  
ANISOU 5197  C   VAL B 132     5167   5842   5722   -438   -342   -732       C  
ATOM   5198  O   VAL B 132      -3.790   2.977 -42.362  1.00 49.78           O  
ANISOU 5198  O   VAL B 132     5863   6594   6457   -407   -305   -723       O  
ATOM   5199  CB  VAL B 132      -3.507   0.368 -41.192  1.00 41.45           C  
ANISOU 5199  CB  VAL B 132     4974   5420   5356   -612   -310   -701       C  
ATOM   5200  CG1 VAL B 132      -4.311  -0.377 -40.165  1.00 39.92           C  
ANISOU 5200  CG1 VAL B 132     4796   5234   5139   -753   -274   -713       C  
ATOM   5201  CG2 VAL B 132      -2.217  -0.375 -41.593  1.00 34.31           C  
ANISOU 5201  CG2 VAL B 132     4182   4417   4436   -568   -357   -667       C  
ATOM   5202  N   TYR B 133      -3.395   1.885 -44.302  1.00 40.80           N  
ANISOU 5202  N   TYR B 133     4771   5417   5314   -363   -389   -731       N  
ATOM   5203  CA  TYR B 133      -2.917   3.083 -45.000  1.00 42.60           C  
ANISOU 5203  CA  TYR B 133     4974   5661   5552   -246   -396   -717       C  
ATOM   5204  C   TYR B 133      -3.944   3.568 -46.029  1.00 37.85           C  
ANISOU 5204  C   TYR B 133     4289   5135   4958   -197   -420   -760       C  
ATOM   5205  O   TYR B 133      -3.653   4.404 -46.859  1.00 36.45           O  
ANISOU 5205  O   TYR B 133     4104   4965   4779   -101   -438   -752       O  
ATOM   5206  CB  TYR B 133      -1.569   2.836 -45.694  1.00 36.47           C  
ANISOU 5206  CB  TYR B 133     4272   4820   4763   -184   -426   -682       C  
ATOM   5207  CG  TYR B 133      -0.485   2.271 -44.790  1.00 33.74           C  
ANISOU 5207  CG  TYR B 133     4009   4405   4405   -216   -416   -647       C  
ATOM   5208  CD1 TYR B 133      -0.412   2.640 -43.454  1.00 33.89           C  
ANISOU 5208  CD1 TYR B 133     4034   4416   4426   -258   -373   -631       C  
ATOM   5209  CD2 TYR B 133       0.484   1.391 -45.287  1.00 28.91           C  
ANISOU 5209  CD2 TYR B 133     3470   3739   3774   -192   -453   -635       C  
ATOM   5210  CE1 TYR B 133       0.574   2.131 -42.625  1.00 30.76           C  
ANISOU 5210  CE1 TYR B 133     3715   3958   4014   -278   -371   -601       C  
ATOM   5211  CE2 TYR B 133       1.473   0.871 -44.474  1.00 26.09           C  
ANISOU 5211  CE2 TYR B 133     3188   3324   3401   -205   -452   -609       C  
ATOM   5212  CZ  TYR B 133       1.522   1.249 -43.146  1.00 33.35           C  
ANISOU 5212  CZ  TYR B 133     4113   4235   4323   -248   -413   -591       C  
ATOM   5213  OH  TYR B 133       2.498   0.767 -42.307  1.00 27.86           O  
ANISOU 5213  OH  TYR B 133     3493   3484   3608   -255   -417   -568       O  
ATOM   5214  N   ASP B 134      -5.141   3.013 -45.983  1.00 37.36           N  
ANISOU 5214  N   ASP B 134     4167   5131   4899   -267   -423   -808       N  
ATOM   5215  CA  ASP B 134      -6.174   3.334 -46.956  1.00 31.61           C  
ANISOU 5215  CA  ASP B 134     3352   4484   4175   -222   -455   -859       C  
ATOM   5216  C   ASP B 134      -6.490   4.829 -46.932  1.00 36.88           C  
ANISOU 5216  C   ASP B 134     3961   5203   4848   -124   -441   -867       C  
ATOM   5217  O   ASP B 134      -6.989   5.356 -45.925  1.00 32.05           O  
ANISOU 5217  O   ASP B 134     3303   4634   4242   -146   -399   -881       O  
ATOM   5218  CB  ASP B 134      -7.410   2.551 -46.589  1.00 37.63           C  
ANISOU 5218  CB  ASP B 134     4046   5313   4938   -335   -447   -913       C  
ATOM   5219  CG  ASP B 134      -8.504   2.643 -47.637  1.00 46.58           C  
ANISOU 5219  CG  ASP B 134     5086   6540   6074   -301   -489   -976       C  
ATOM   5220  OD1 ASP B 134      -8.590   3.646 -48.377  1.00 43.16           O  
ANISOU 5220  OD1 ASP B 134     4618   6139   5642   -179   -514   -984       O  
ATOM   5221  OD2 ASP B 134      -9.306   1.697 -47.696  1.00 55.50           O  
ANISOU 5221  OD2 ASP B 134     6179   7709   7200   -403   -500  -1019       O  
ATOM   5222  N   GLY B 135      -6.226   5.514 -48.041  1.00 33.29           N  
ANISOU 5222  N   GLY B 135     3517   4745   4387    -14   -478   -860       N  
ATOM   5223  CA  GLY B 135      -6.424   6.955 -48.098  1.00 34.46           C  
ANISOU 5223  CA  GLY B 135     3639   4921   4532     88   -474   -862       C  
ATOM   5224  C   GLY B 135      -7.857   7.457 -48.369  1.00 32.69           C  
ANISOU 5224  C   GLY B 135     3308   4805   4308    135   -495   -932       C  
ATOM   5225  O   GLY B 135      -8.075   8.661 -48.436  1.00 34.61           O  
ANISOU 5225  O   GLY B 135     3540   5068   4543    233   -500   -938       O  
ATOM   5226  N   ARG B 136      -8.840   6.582 -48.550  1.00 33.62           N  
ANISOU 5226  N   ARG B 136     3349   4995   4430     70   -512   -988       N  
ATOM   5227  CA  ARG B 136     -10.121   7.116 -49.018  1.00 41.19           C  
ANISOU 5227  CA  ARG B 136     4199   6068   5385    136   -543  -1060       C  
ATOM   5228  C   ARG B 136     -10.776   8.001 -47.960  1.00 46.81           C  
ANISOU 5228  C   ARG B 136     4841   6846   6098    157   -503  -1090       C  
ATOM   5229  O   ARG B 136     -11.525   8.927 -48.303  1.00 45.43           O  
ANISOU 5229  O   ARG B 136     4606   6744   5913    268   -531  -1136       O  
ATOM   5230  CB  ARG B 136     -11.088   6.022 -49.463  1.00 39.54           C  
ANISOU 5230  CB  ARG B 136     3908   5937   5178     55   -572  -1122       C  
ATOM   5231  CG  ARG B 136     -11.650   5.197 -48.324  1.00 38.71           C  
ANISOU 5231  CG  ARG B 136     3748   5879   5083    -98   -520  -1148       C  
ATOM   5232  CD  ARG B 136     -11.445   3.729 -48.628  1.00 46.27           C  
ANISOU 5232  CD  ARG B 136     4752   6789   6039   -220   -536  -1141       C  
ATOM   5233  NE  ARG B 136     -12.584   3.150 -49.280  1.00 56.55           N  
ANISOU 5233  NE  ARG B 136     5957   8191   7338   -263   -575  -1216       N  
ATOM   5234  CZ  ARG B 136     -12.562   2.052 -50.044  1.00 59.25           C  
ANISOU 5234  CZ  ARG B 136     6335   8503   7675   -327   -617  -1226       C  
ATOM   5235  NH1 ARG B 136     -11.432   1.380 -50.290  1.00 44.18           N  
ANISOU 5235  NH1 ARG B 136     4561   6464   5761   -343   -628  -1165       N  
ATOM   5236  NH2 ARG B 136     -13.707   1.638 -50.578  1.00 54.20           N  
ANISOU 5236  NH2 ARG B 136     5590   7971   7031   -369   -652  -1304       N  
ATOM   5237  N   PHE B 137     -10.489   7.732 -46.683  1.00 37.84           N  
ANISOU 5237  N   PHE B 137     3720   5687   4971     61   -441  -1067       N  
ATOM   5238  CA  PHE B 137     -11.212   8.417 -45.633  1.00 40.78           C  
ANISOU 5238  CA  PHE B 137     4017   6137   5342     68   -398  -1106       C  
ATOM   5239  C   PHE B 137     -10.764   9.859 -45.516  1.00 45.39           C  
ANISOU 5239  C   PHE B 137     4653   6678   5917    201   -400  -1080       C  
ATOM   5240  O   PHE B 137     -11.601  10.756 -45.350  1.00 43.14           O  
ANISOU 5240  O   PHE B 137     4297   6473   5621    288   -406  -1134       O  
ATOM   5241  CB  PHE B 137     -11.092   7.684 -44.295  1.00 40.30           C  
ANISOU 5241  CB  PHE B 137     3961   6066   5283    -77   -331  -1090       C  
ATOM   5242  CG  PHE B 137     -11.567   6.272 -44.349  1.00 40.75           C  
ANISOU 5242  CG  PHE B 137     3985   6156   5342   -221   -328  -1114       C  
ATOM   5243  CD1 PHE B 137     -12.926   5.989 -44.386  1.00 43.57           C  
ANISOU 5243  CD1 PHE B 137     4206   6655   5695   -268   -327  -1196       C  
ATOM   5244  CD2 PHE B 137     -10.658   5.223 -44.373  1.00 39.29           C  
ANISOU 5244  CD2 PHE B 137     3907   5864   5159   -308   -329  -1058       C  
ATOM   5245  CE1 PHE B 137     -13.367   4.676 -44.450  1.00 47.72           C  
ANISOU 5245  CE1 PHE B 137     4709   7205   6217   -417   -325  -1218       C  
ATOM   5246  CE2 PHE B 137     -11.075   3.901 -44.444  1.00 46.11           C  
ANISOU 5246  CE2 PHE B 137     4762   6740   6017   -443   -333  -1078       C  
ATOM   5247  CZ  PHE B 137     -12.429   3.614 -44.487  1.00 43.88           C  
ANISOU 5247  CZ  PHE B 137     4351   6591   5731   -506   -329  -1156       C  
ATOM   5248  N   LEU B 138      -9.451  10.090 -45.585  1.00 40.72           N  
ANISOU 5248  N   LEU B 138     4184   5962   5324    216   -396  -1003       N  
ATOM   5249  CA  LEU B 138      -8.940  11.459 -45.506  1.00 45.63           C  
ANISOU 5249  CA  LEU B 138     4874   6530   5935    326   -399   -974       C  
ATOM   5250  C   LEU B 138      -9.331  12.251 -46.750  1.00 42.69           C  
ANISOU 5250  C   LEU B 138     4503   6174   5543    463   -463   -996       C  
ATOM   5251  O   LEU B 138      -9.587  13.436 -46.656  1.00 45.34           O  
ANISOU 5251  O   LEU B 138     4853   6513   5861    570   -474  -1011       O  
ATOM   5252  CB  LEU B 138      -7.414  11.490 -45.312  1.00 38.49           C  
ANISOU 5252  CB  LEU B 138     4093   5499   5032    295   -379   -890       C  
ATOM   5253  CG  LEU B 138      -6.881  11.087 -43.934  1.00 33.68           C  
ANISOU 5253  CG  LEU B 138     3507   4857   4433    192   -320   -862       C  
ATOM   5254  CD1 LEU B 138      -5.438  10.501 -44.014  1.00 23.92           C  
ANISOU 5254  CD1 LEU B 138     2368   3520   3200    139   -315   -792       C  
ATOM   5255  CD2 LEU B 138      -6.920  12.267 -43.005  1.00 30.93           C  
ANISOU 5255  CD2 LEU B 138     3172   4505   4076    242   -292   -865       C  
ATOM   5256  N   ALA B 139      -9.366  11.586 -47.906  1.00 40.11           N  
ANISOU 5256  N   ALA B 139     4173   5853   5214    464   -507   -999       N  
ATOM   5257  CA  ALA B 139      -9.768  12.226 -49.153  1.00 43.54           C  
ANISOU 5257  CA  ALA B 139     4613   6305   5624    593   -573  -1022       C  
ATOM   5258  C   ALA B 139     -11.239  12.619 -49.090  1.00 45.59           C  
ANISOU 5258  C   ALA B 139     4752   6695   5877    663   -599  -1113       C  
ATOM   5259  O   ALA B 139     -11.616  13.743 -49.424  1.00 48.49           O  
ANISOU 5259  O   ALA B 139     5135   7072   6218    801   -637  -1135       O  
ATOM   5260  CB  ALA B 139      -9.514  11.293 -50.375  1.00 28.87           C  
ANISOU 5260  CB  ALA B 139     2774   4433   3763    569   -614  -1011       C  
ATOM   5261  N   GLN B 140     -12.072  11.687 -48.659  1.00 41.29           N  
ANISOU 5261  N   GLN B 140     4087   6250   5350    569   -581  -1170       N  
ATOM   5262  CA  GLN B 140     -13.505  11.946 -48.600  1.00 42.12           C  
ANISOU 5262  CA  GLN B 140     4051   6504   5448    624   -603  -1268       C  
ATOM   5263  C   GLN B 140     -13.876  12.960 -47.517  1.00 47.73           C  
ANISOU 5263  C   GLN B 140     4733   7252   6150    683   -568  -1295       C  
ATOM   5264  O   GLN B 140     -14.488  13.993 -47.799  1.00 49.32           O  
ANISOU 5264  O   GLN B 140     4913   7500   6326    834   -611  -1342       O  
ATOM   5265  CB  GLN B 140     -14.279  10.649 -48.392  1.00 40.47           C  
ANISOU 5265  CB  GLN B 140     3721   6400   5258    483   -585  -1322       C  
ATOM   5266  CG  GLN B 140     -15.695  10.711 -48.990  1.00 50.81           C  
ANISOU 5266  CG  GLN B 140     4881   7870   6554    548   -638  -1428       C  
ATOM   5267  CD  GLN B 140     -16.638  11.590 -48.187  1.00 53.03           C  
ANISOU 5267  CD  GLN B 140     5055   8270   6822    625   -620  -1501       C  
ATOM   5268  OE1 GLN B 140     -16.768  11.442 -46.971  1.00 50.57           O  
ANISOU 5268  OE1 GLN B 140     4701   7995   6520    534   -548  -1508       O  
ATOM   5269  NE2 GLN B 140     -17.302  12.508 -48.867  1.00 61.05           N  
ANISOU 5269  NE2 GLN B 140     6033   9349   7812    798   -687  -1558       N  
ATOM   5270  N   VAL B 141     -13.499  12.677 -46.280  1.00 47.39           N  
ANISOU 5270  N   VAL B 141     4698   7186   6122    574   -495  -1268       N  
ATOM   5271  CA  VAL B 141     -13.975  13.491 -45.173  1.00 48.43           C  
ANISOU 5271  CA  VAL B 141     4785   7372   6243    617   -457  -1306       C  
ATOM   5272  C   VAL B 141     -13.338  14.867 -45.126  1.00 51.01           C  
ANISOU 5272  C   VAL B 141     5234   7597   6550    750   -473  -1266       C  
ATOM   5273  O   VAL B 141     -14.043  15.849 -44.898  1.00 45.12           O  
ANISOU 5273  O   VAL B 141     4451   6910   5781    873   -491  -1323       O  
ATOM   5274  CB  VAL B 141     -13.794  12.786 -43.836  1.00 48.74           C  
ANISOU 5274  CB  VAL B 141     4803   7419   6297    460   -373  -1289       C  
ATOM   5275  CG1 VAL B 141     -14.190  13.737 -42.654  1.00 35.22           C  
ANISOU 5275  CG1 VAL B 141     3059   5754   4567    515   -331  -1325       C  
ATOM   5276  CG2 VAL B 141     -14.607  11.494 -43.838  1.00 45.90           C  
ANISOU 5276  CG2 VAL B 141     4322   7170   5948    324   -357  -1340       C  
ATOM   5277  N   GLU B 142     -12.025  14.931 -45.370  1.00 40.42           N  
ANISOU 5277  N   GLU B 142     4036   6107   5214    725   -470  -1173       N  
ATOM   5278  CA  GLU B 142     -11.282  16.183 -45.265  1.00 36.87           C  
ANISOU 5278  CA  GLU B 142     3717   5547   4744    818   -478  -1126       C  
ATOM   5279  C   GLU B 142     -10.925  16.843 -46.599  1.00 42.08           C  
ANISOU 5279  C   GLU B 142     4477   6134   5378    932   -546  -1096       C  
ATOM   5280  O   GLU B 142     -10.236  17.871 -46.629  1.00 41.68           O  
ANISOU 5280  O   GLU B 142     4554   5979   5305    996   -555  -1050       O  
ATOM   5281  CB  GLU B 142     -10.014  15.953 -44.458  1.00 33.53           C  
ANISOU 5281  CB  GLU B 142     3386   5016   4337    708   -421  -1046       C  
ATOM   5282  CG  GLU B 142     -10.300  15.600 -43.022  1.00 38.20           C  
ANISOU 5282  CG  GLU B 142     3912   5661   4941    618   -355  -1069       C  
ATOM   5283  CD  GLU B 142     -10.796  16.814 -42.261  1.00 52.51           C  
ANISOU 5283  CD  GLU B 142     5723   7499   6731    720   -349  -1111       C  
ATOM   5284  OE1 GLU B 142     -10.552  17.953 -42.736  1.00 58.87           O  
ANISOU 5284  OE1 GLU B 142     6621   8236   7513    842   -391  -1098       O  
ATOM   5285  OE2 GLU B 142     -11.431  16.641 -41.202  1.00 57.18           O  
ANISOU 5285  OE2 GLU B 142     6228   8176   7322    678   -302  -1158       O  
ATOM   5286  N   GLY B 143     -11.376  16.254 -47.700  1.00 42.31           N  
ANISOU 5286  N   GLY B 143     4456   6213   5405    948   -594  -1121       N  
ATOM   5287  CA  GLY B 143     -11.048  16.778 -49.011  1.00 43.93           C  
ANISOU 5287  CA  GLY B 143     4759   6353   5580   1048   -657  -1091       C  
ATOM   5288  C   GLY B 143      -9.552  16.799 -49.341  1.00 47.49           C  
ANISOU 5288  C   GLY B 143     5354   6662   6026    992   -637   -990       C  
ATOM   5289  O   GLY B 143      -9.121  17.583 -50.178  1.00 48.06           O  
ANISOU 5289  O   GLY B 143     5540   6659   6063   1075   -675   -953       O  
ATOM   5290  N   ALA B 144      -8.757  15.950 -48.694  1.00 44.00           N  
ANISOU 5290  N   ALA B 144     4912   6188   5616    853   -579   -947       N  
ATOM   5291  CA  ALA B 144      -7.311  15.907 -48.963  1.00 43.18           C  
ANISOU 5291  CA  ALA B 144     4926   5970   5509    798   -559   -860       C  
ATOM   5292  C   ALA B 144      -6.961  15.128 -50.231  1.00 43.17           C  
ANISOU 5292  C   ALA B 144     4941   5961   5501    783   -590   -839       C  
ATOM   5293  O   ALA B 144      -7.698  14.213 -50.641  1.00 37.72           O  
ANISOU 5293  O   ALA B 144     4160   5349   4824    764   -613   -886       O  
ATOM   5294  CB  ALA B 144      -6.574  15.294 -47.782  1.00 39.50           C  
ANISOU 5294  CB  ALA B 144     4455   5477   5075    670   -493   -828       C  
ATOM   5295  N   VAL B 145      -5.840  15.496 -50.848  1.00 37.65           N  
ANISOU 5295  N   VAL B 145     4357   5172   4778    787   -590   -772       N  
ATOM   5296  CA  VAL B 145      -5.204  14.628 -51.818  1.00 35.16           C  
ANISOU 5296  CA  VAL B 145     4061   4841   4456    748   -600   -743       C  
ATOM   5297  C   VAL B 145      -4.142  13.794 -51.104  1.00 38.31           C  
ANISOU 5297  C   VAL B 145     4466   5206   4884    627   -546   -703       C  
ATOM   5298  O   VAL B 145      -3.199  14.322 -50.481  1.00 36.70           O  
ANISOU 5298  O   VAL B 145     4326   4941   4678    594   -508   -656       O  
ATOM   5299  CB  VAL B 145      -4.594  15.400 -52.982  1.00 35.85           C  
ANISOU 5299  CB  VAL B 145     4262   4867   4493    817   -628   -698       C  
ATOM   5300  CG1 VAL B 145      -3.745  14.458 -53.860  1.00 29.20           C  
ANISOU 5300  CG1 VAL B 145     3441   4012   3643    765   -626   -665       C  
ATOM   5301  CG2 VAL B 145      -5.686  16.031 -53.826  1.00 30.43           C  
ANISOU 5301  CG2 VAL B 145     3574   4216   3771    945   -694   -743       C  
ATOM   5302  N   LEU B 146      -4.318  12.485 -51.149  1.00 34.61           N  
ANISOU 5302  N   LEU B 146     3934   4777   4439    561   -548   -725       N  
ATOM   5303  CA  LEU B 146      -3.436  11.619 -50.412  1.00 33.73           C  
ANISOU 5303  CA  LEU B 146     3829   4635   4350    458   -506   -695       C  
ATOM   5304  C   LEU B 146      -2.557  10.778 -51.348  1.00 40.70           C  
ANISOU 5304  C   LEU B 146     4751   5492   5220    438   -519   -668       C  
ATOM   5305  O   LEU B 146      -3.063  10.119 -52.275  1.00 44.40           O  
ANISOU 5305  O   LEU B 146     5194   5995   5681    457   -559   -697       O  
ATOM   5306  CB  LEU B 146      -4.225  10.758 -49.422  1.00 33.66           C  
ANISOU 5306  CB  LEU B 146     3736   4677   4375    382   -488   -739       C  
ATOM   5307  CG  LEU B 146      -3.221  10.293 -48.371  1.00 46.79           C  
ANISOU 5307  CG  LEU B 146     5434   6290   6053    295   -441   -699       C  
ATOM   5308  CD1 LEU B 146      -3.687  10.558 -46.980  1.00 43.57           C  
ANISOU 5308  CD1 LEU B 146     4991   5902   5663    255   -402   -716       C  
ATOM   5309  CD2 LEU B 146      -2.762   8.807 -48.590  1.00 45.06           C  
ANISOU 5309  CD2 LEU B 146     5222   6057   5841    223   -449   -694       C  
ATOM   5310  N   VAL B 147      -1.245  10.810 -51.111  1.00 36.46           N  
ANISOU 5310  N   VAL B 147     4275   4902   4677    403   -488   -617       N  
ATOM   5311  CA  VAL B 147      -0.293  10.050 -51.934  1.00 31.52           C  
ANISOU 5311  CA  VAL B 147     3684   4260   4034    391   -496   -594       C  
ATOM   5312  C   VAL B 147       0.492   9.085 -51.058  1.00 33.21           C  
ANISOU 5312  C   VAL B 147     3897   4454   4268    313   -469   -583       C  
ATOM   5313  O   VAL B 147       0.900   9.445 -49.987  1.00 38.59           O  
ANISOU 5313  O   VAL B 147     4586   5113   4963    277   -434   -564       O  
ATOM   5314  CB  VAL B 147       0.687  10.979 -52.680  1.00 33.54           C  
ANISOU 5314  CB  VAL B 147     4013   4483   4249    431   -486   -547       C  
ATOM   5315  CG1 VAL B 147       1.700  10.182 -53.531  1.00 30.32           C  
ANISOU 5315  CG1 VAL B 147     3630   4075   3816    423   -489   -530       C  
ATOM   5316  CG2 VAL B 147      -0.084  11.960 -53.553  1.00 39.83           C  
ANISOU 5316  CG2 VAL B 147     4833   5286   5014    516   -519   -555       C  
ATOM   5317  N   SER B 148       0.686   7.850 -51.511  1.00 30.94           N  
ANISOU 5317  N   SER B 148     3608   4170   3978    293   -491   -596       N  
ATOM   5318  CA  SER B 148       1.640   6.944 -50.879  1.00 32.81           C  
ANISOU 5318  CA  SER B 148     3867   4378   4221    241   -475   -582       C  
ATOM   5319  C   SER B 148       2.417   6.230 -51.982  1.00 35.11           C  
ANISOU 5319  C   SER B 148     4189   4668   4483    272   -500   -579       C  
ATOM   5320  O   SER B 148       1.849   5.948 -53.053  1.00 35.68           O  
ANISOU 5320  O   SER B 148     4255   4761   4540    308   -536   -603       O  
ATOM   5321  CB  SER B 148       0.933   5.888 -50.029  1.00 26.52           C  
ANISOU 5321  CB  SER B 148     3045   3580   3450    173   -481   -612       C  
ATOM   5322  OG  SER B 148       0.146   5.070 -50.883  1.00 31.35           O  
ANISOU 5322  OG  SER B 148     3639   4214   4058    177   -523   -650       O  
ATOM   5323  N   MET B 149       3.693   5.922 -51.718  1.00 28.99           N  
ANISOU 5323  N   MET B 149     3443   3875   3696    262   -483   -557       N  
ATOM   5324  CA  MET B 149       4.549   5.235 -52.699  1.00 31.48           C  
ANISOU 5324  CA  MET B 149     3784   4199   3978    299   -503   -559       C  
ATOM   5325  C   MET B 149       5.152   3.970 -52.093  1.00 33.70           C  
ANISOU 5325  C   MET B 149     4086   4456   4262    274   -516   -572       C  
ATOM   5326  O   MET B 149       5.374   3.908 -50.882  1.00 32.73           O  
ANISOU 5326  O   MET B 149     3967   4309   4158    231   -497   -562       O  
ATOM   5327  CB  MET B 149       5.703   6.162 -53.149  1.00 33.03           C  
ANISOU 5327  CB  MET B 149     3995   4414   4142    326   -471   -524       C  
ATOM   5328  CG  MET B 149       6.955   6.163 -52.207  1.00 29.13           C  
ANISOU 5328  CG  MET B 149     3503   3916   3648    296   -439   -505       C  
ATOM   5329  SD  MET B 149       6.693   6.917 -50.565  1.00 33.45           S  
ANISOU 5329  SD  MET B 149     4040   4432   4235    236   -407   -488       S  
ATOM   5330  CE  MET B 149       6.649   8.676 -51.026  1.00 26.94           C  
ANISOU 5330  CE  MET B 149     3227   3613   3393    248   -376   -454       C  
ATOM   5331  N   ASN B 150       5.424   2.960 -52.921  1.00 35.64           N  
ANISOU 5331  N   ASN B 150     4357   4703   4483    308   -552   -595       N  
ATOM   5332  CA  ASN B 150       6.332   1.895 -52.508  1.00 30.45           C  
ANISOU 5332  CA  ASN B 150     3735   4022   3813    312   -568   -605       C  
ATOM   5333  C   ASN B 150       7.784   2.366 -52.642  1.00 32.50           C  
ANISOU 5333  C   ASN B 150     3987   4317   4044    350   -540   -585       C  
ATOM   5334  O   ASN B 150       8.083   3.135 -53.533  1.00 31.24           O  
ANISOU 5334  O   ASN B 150     3810   4199   3861    381   -521   -572       O  
ATOM   5335  CB  ASN B 150       6.109   0.631 -53.336  1.00 34.20           C  
ANISOU 5335  CB  ASN B 150     4247   4481   4267    340   -621   -642       C  
ATOM   5336  CG  ASN B 150       4.855  -0.111 -52.929  1.00 39.85           C  
ANISOU 5336  CG  ASN B 150     4978   5156   5008    279   -650   -666       C  
ATOM   5337  OD1 ASN B 150       4.186   0.252 -51.950  1.00 38.79           O  
ANISOU 5337  OD1 ASN B 150     4822   5012   4906    215   -626   -656       O  
ATOM   5338  ND2 ASN B 150       4.522  -1.145 -53.679  1.00 37.72           N  
ANISOU 5338  ND2 ASN B 150     4745   4868   4720    292   -699   -700       N  
ATOM   5339  N   TYR B 151       8.670   1.915 -51.751  1.00 26.43           N  
ANISOU 5339  N   TYR B 151     3232   3536   3274    345   -539   -585       N  
ATOM   5340  CA  TYR B 151      10.094   2.167 -51.907  1.00 32.34           C  
ANISOU 5340  CA  TYR B 151     3963   4334   3991    384   -520   -580       C  
ATOM   5341  C   TYR B 151      10.822   0.885 -51.556  1.00 30.38           C  
ANISOU 5341  C   TYR B 151     3750   4069   3723    423   -560   -610       C  
ATOM   5342  O   TYR B 151      10.299   0.055 -50.815  1.00 35.80           O  
ANISOU 5342  O   TYR B 151     4485   4692   4426    398   -591   -620       O  
ATOM   5343  CB  TYR B 151      10.571   3.333 -51.038  1.00 31.65           C  
ANISOU 5343  CB  TYR B 151     3843   4263   3919    340   -471   -547       C  
ATOM   5344  CG  TYR B 151      10.364   3.138 -49.546  1.00 34.73           C  
ANISOU 5344  CG  TYR B 151     4249   4605   4341    293   -472   -542       C  
ATOM   5345  CD1 TYR B 151       9.171   3.529 -48.924  1.00 28.89           C  
ANISOU 5345  CD1 TYR B 151     3514   3827   3638    238   -461   -530       C  
ATOM   5346  CD2 TYR B 151      11.371   2.572 -48.753  1.00 26.02           C  
ANISOU 5346  CD2 TYR B 151     3158   3504   3226    307   -485   -552       C  
ATOM   5347  CE1 TYR B 151       8.997   3.368 -47.569  1.00 27.66           C  
ANISOU 5347  CE1 TYR B 151     3374   3632   3503    192   -457   -524       C  
ATOM   5348  CE2 TYR B 151      11.204   2.399 -47.405  1.00 27.66           C  
ANISOU 5348  CE2 TYR B 151     3389   3665   3454    265   -487   -545       C  
ATOM   5349  CZ  TYR B 151      10.014   2.796 -46.803  1.00 32.61           C  
ANISOU 5349  CZ  TYR B 151     4023   4252   4116    203   -470   -529       C  
ATOM   5350  OH  TYR B 151       9.856   2.616 -45.431  1.00 29.74           O  
ANISOU 5350  OH  TYR B 151     3687   3847   3766    158   -468   -523       O  
ATOM   5351  N   ARG B 152      12.004   0.705 -52.120  1.00 32.96           N  
ANISOU 5351  N   ARG B 152     4061   4455   4010    486   -561   -627       N  
ATOM   5352  CA  ARG B 152      12.771  -0.521 -51.908  1.00 33.28           C  
ANISOU 5352  CA  ARG B 152     4137   4485   4021    548   -608   -664       C  
ATOM   5353  C   ARG B 152      13.229  -0.672 -50.454  1.00 35.53           C  
ANISOU 5353  C   ARG B 152     4438   4742   4322    526   -612   -658       C  
ATOM   5354  O   ARG B 152      13.698   0.283 -49.836  1.00 35.11           O  
ANISOU 5354  O   ARG B 152     4335   4724   4280    490   -570   -634       O  
ATOM   5355  CB  ARG B 152      13.957  -0.559 -52.861  1.00 33.71           C  
ANISOU 5355  CB  ARG B 152     4153   4632   4024    627   -602   -689       C  
ATOM   5356  CG  ARG B 152      13.599  -1.071 -54.249  1.00 33.60           C  
ANISOU 5356  CG  ARG B 152     4160   4627   3979    679   -626   -714       C  
ATOM   5357  CD  ARG B 152      14.769  -0.941 -55.194  1.00 34.46           C  
ANISOU 5357  CD  ARG B 152     4219   4843   4032    749   -607   -737       C  
ATOM   5358  NE  ARG B 152      15.006   0.460 -55.543  1.00 37.85           N  
ANISOU 5358  NE  ARG B 152     4584   5339   4458    697   -537   -699       N  
ATOM   5359  CZ  ARG B 152      16.086   0.890 -56.185  1.00 36.08           C  
ANISOU 5359  CZ  ARG B 152     4302   5222   4186    723   -498   -708       C  
ATOM   5360  NH1 ARG B 152      17.041   0.018 -56.556  1.00 29.26           N  
ANISOU 5360  NH1 ARG B 152     3422   4422   3273    813   -523   -760       N  
ATOM   5361  NH2 ARG B 152      16.204   2.188 -56.458  1.00 26.44           N  
ANISOU 5361  NH2 ARG B 152     3042   4045   2959    659   -435   -668       N  
ATOM   5362  N   VAL B 153      13.056  -1.866 -49.905  1.00 26.63           N  
ANISOU 5362  N   VAL B 153     3388   3543   3188    544   -666   -679       N  
ATOM   5363  CA  VAL B 153      13.456  -2.155 -48.539  1.00 25.82           C  
ANISOU 5363  CA  VAL B 153     3320   3402   3089    531   -681   -675       C  
ATOM   5364  C   VAL B 153      14.549  -3.249 -48.544  1.00 39.80           C  
ANISOU 5364  C   VAL B 153     5133   5178   4810    636   -739   -719       C  
ATOM   5365  O   VAL B 153      14.888  -3.811 -49.610  1.00 35.78           O  
ANISOU 5365  O   VAL B 153     4629   4700   4266    714   -766   -753       O  
ATOM   5366  CB  VAL B 153      12.217  -2.618 -47.735  1.00 33.82           C  
ANISOU 5366  CB  VAL B 153     4407   4313   4130    452   -695   -658       C  
ATOM   5367  CG1 VAL B 153      11.201  -1.422 -47.557  1.00 25.92           C  
ANISOU 5367  CG1 VAL B 153     3350   3322   3177    360   -636   -621       C  
ATOM   5368  CG2 VAL B 153      11.502  -3.768 -48.467  1.00 28.35           C  
ANISOU 5368  CG2 VAL B 153     3790   3560   3422    466   -745   -684       C  
ATOM   5369  N   GLY B 154      15.102  -3.533 -47.363  1.00 39.68           N  
ANISOU 5369  N   GLY B 154     5151   5139   4788    646   -760   -721       N  
ATOM   5370  CA  GLY B 154      16.112  -4.556 -47.192  1.00 36.33           C  
ANISOU 5370  CA  GLY B 154     4776   4714   4313    755   -824   -765       C  
ATOM   5371  C   GLY B 154      17.357  -4.310 -48.044  1.00 40.11           C  
ANISOU 5371  C   GLY B 154     5161   5322   4756    850   -817   -803       C  
ATOM   5372  O   GLY B 154      17.732  -3.155 -48.317  1.00 35.75           O  
ANISOU 5372  O   GLY B 154     4500   4866   4219    813   -754   -787       O  
ATOM   5373  N   THR B 155      18.008  -5.394 -48.460  1.00 37.46           N  
ANISOU 5373  N   THR B 155     4873   4991   4369    970   -880   -856       N  
ATOM   5374  CA  THR B 155      19.169  -5.277 -49.331  1.00 41.18           C  
ANISOU 5374  CA  THR B 155     5251   5597   4798   1067   -874   -903       C  
ATOM   5375  C   THR B 155      18.825  -4.484 -50.587  1.00 38.59           C  
ANISOU 5375  C   THR B 155     4846   5337   4481   1025   -811   -886       C  
ATOM   5376  O   THR B 155      19.587  -3.606 -50.998  1.00 38.16           O  
ANISOU 5376  O   THR B 155     4678   5407   4415   1021   -757   -889       O  
ATOM   5377  CB  THR B 155      19.764  -6.656 -49.719  1.00 40.10           C  
ANISOU 5377  CB  THR B 155     5190   5447   4599   1217   -958   -969       C  
ATOM   5378  OG1 THR B 155      18.763  -7.431 -50.360  1.00 41.95           O  
ANISOU 5378  OG1 THR B 155     5530   5577   4832   1211   -992   -968       O  
ATOM   5379  CG2 THR B 155      20.251  -7.410 -48.479  1.00 37.55           C  
ANISOU 5379  CG2 THR B 155     4951   5064   4254   1276  -1027   -988       C  
ATOM   5380  N   PHE B 156      17.665  -4.750 -51.178  1.00 37.38           N  
ANISOU 5380  N   PHE B 156     4756   5102   4345    985   -818   -868       N  
ATOM   5381  CA  PHE B 156      17.319  -4.093 -52.444  1.00 37.81           C  
ANISOU 5381  CA  PHE B 156     4752   5214   4399    961   -770   -857       C  
ATOM   5382  C   PHE B 156      17.329  -2.590 -52.312  1.00 36.50           C  
ANISOU 5382  C   PHE B 156     4492   5112   4266    866   -689   -809       C  
ATOM   5383  O   PHE B 156      17.693  -1.884 -53.245  1.00 35.84           O  
ANISOU 5383  O   PHE B 156     4338   5120   4161    866   -642   -807       O  
ATOM   5384  CB  PHE B 156      15.969  -4.605 -52.977  1.00 35.79           C  
ANISOU 5384  CB  PHE B 156     4579   4857   4161    926   -797   -846       C  
ATOM   5385  CG  PHE B 156      15.867  -6.079 -52.895  1.00 42.13           C  
ANISOU 5385  CG  PHE B 156     5501   5572   4937    996   -880   -887       C  
ATOM   5386  CD1 PHE B 156      16.509  -6.881 -53.852  1.00 39.06           C  
ANISOU 5386  CD1 PHE B 156     5132   5221   4489   1117   -922   -944       C  
ATOM   5387  CD2 PHE B 156      15.258  -6.682 -51.797  1.00 35.57           C  
ANISOU 5387  CD2 PHE B 156     4766   4621   4127    946   -917   -872       C  
ATOM   5388  CE1 PHE B 156      16.481  -8.246 -53.743  1.00 42.45           C  
ANISOU 5388  CE1 PHE B 156     5684   5558   4885   1190  -1006   -984       C  
ATOM   5389  CE2 PHE B 156      15.229  -8.054 -51.682  1.00 41.96           C  
ANISOU 5389  CE2 PHE B 156     5704   5338   4902   1007   -998   -907       C  
ATOM   5390  CZ  PHE B 156      15.850  -8.841 -52.649  1.00 45.25           C  
ANISOU 5390  CZ  PHE B 156     6149   5782   5262   1133  -1046   -964       C  
ATOM   5391  N   GLY B 157      16.932  -2.107 -51.142  1.00 33.17           N  
ANISOU 5391  N   GLY B 157     4080   4636   3889    785   -673   -772       N  
ATOM   5392  CA  GLY B 157      16.874  -0.683 -50.894  1.00 33.92           C  
ANISOU 5392  CA  GLY B 157     4104   4771   4014    694   -603   -727       C  
ATOM   5393  C   GLY B 157      18.064  -0.065 -50.170  1.00 33.80           C  
ANISOU 5393  C   GLY B 157     4015   4837   3989    688   -577   -731       C  
ATOM   5394  O   GLY B 157      18.308   1.132 -50.335  1.00 33.10           O  
ANISOU 5394  O   GLY B 157     3861   4810   3907    625   -516   -704       O  
ATOM   5395  N   PHE B 158      18.791  -0.846 -49.370  1.00 31.47           N  
ANISOU 5395  N   PHE B 158     3738   4542   3676    750   -624   -766       N  
ATOM   5396  CA  PHE B 158      19.805  -0.248 -48.483  1.00 38.18           C  
ANISOU 5396  CA  PHE B 158     4520   5464   4523    734   -606   -771       C  
ATOM   5397  C   PHE B 158      21.166  -0.934 -48.402  1.00 39.12           C  
ANISOU 5397  C   PHE B 158     4597   5676   4591    845   -647   -834       C  
ATOM   5398  O   PHE B 158      22.066  -0.466 -47.696  1.00 40.88           O  
ANISOU 5398  O   PHE B 158     4752   5973   4808    836   -636   -847       O  
ATOM   5399  CB  PHE B 158      19.215   0.042 -47.077  1.00 32.07           C  
ANISOU 5399  CB  PHE B 158     3794   4598   3794    659   -608   -733       C  
ATOM   5400  CG  PHE B 158      17.999   0.961 -47.127  1.00 31.63           C  
ANISOU 5400  CG  PHE B 158     3752   4481   3786    552   -558   -678       C  
ATOM   5401  CD1 PHE B 158      18.160   2.337 -47.204  1.00 30.04           C  
ANISOU 5401  CD1 PHE B 158     3483   4332   3598    477   -494   -648       C  
ATOM   5402  CD2 PHE B 158      16.705   0.440 -47.167  1.00 36.79           C  
ANISOU 5402  CD2 PHE B 158     4486   5030   4463    531   -578   -660       C  
ATOM   5403  CE1 PHE B 158      17.071   3.186 -47.290  1.00 30.55           C  
ANISOU 5403  CE1 PHE B 158     3566   4342   3699    398   -456   -603       C  
ATOM   5404  CE2 PHE B 158      15.564   1.307 -47.263  1.00 28.95           C  
ANISOU 5404  CE2 PHE B 158     3493   3996   3510    446   -535   -618       C  
ATOM   5405  CZ  PHE B 158      15.762   2.652 -47.342  1.00 35.29           C  
ANISOU 5405  CZ  PHE B 158     4235   4849   4325    390   -478   -591       C  
ATOM   5406  N   LEU B 159      21.354  -2.027 -49.126  1.00 38.27           N  
ANISOU 5406  N   LEU B 159     4526   5573   4443    955   -697   -881       N  
ATOM   5407  CA  LEU B 159      22.724  -2.543 -49.232  1.00 38.98           C  
ANISOU 5407  CA  LEU B 159     4553   5781   4476   1073   -729   -950       C  
ATOM   5408  C   LEU B 159      23.620  -1.490 -49.892  1.00 46.21           C  
ANISOU 5408  C   LEU B 159     5323   6864   5371   1037   -655   -960       C  
ATOM   5409  O   LEU B 159      23.297  -0.952 -50.954  1.00 50.07           O  
ANISOU 5409  O   LEU B 159     5784   7385   5857    991   -601   -938       O  
ATOM   5410  CB  LEU B 159      22.768  -3.840 -50.010  1.00 38.13           C  
ANISOU 5410  CB  LEU B 159     4512   5654   4323   1205   -794  -1002       C  
ATOM   5411  CG  LEU B 159      24.124  -4.531 -50.066  1.00 39.29           C  
ANISOU 5411  CG  LEU B 159     4608   5915   4405   1353   -843  -1085       C  
ATOM   5412  CD1 LEU B 159      23.971  -6.015 -49.796  1.00 40.93           C  
ANISOU 5412  CD1 LEU B 159     4957   6012   4582   1478   -946  -1124       C  
ATOM   5413  CD2 LEU B 159      24.707  -4.272 -51.440  1.00 38.40           C  
ANISOU 5413  CD2 LEU B 159     4392   5948   4248   1391   -797  -1120       C  
ATOM   5414  N   ALA B 160      24.744  -1.190 -49.256  1.00 45.76           N  
ANISOU 5414  N   ALA B 160     5175   6915   5295   1051   -652   -993       N  
ATOM   5415  CA  ALA B 160      25.607  -0.120 -49.720  1.00 42.85           C  
ANISOU 5415  CA  ALA B 160     4667   6707   4907    988   -577  -1000       C  
ATOM   5416  C   ALA B 160      27.061  -0.582 -49.668  1.00 42.73           C  
ANISOU 5416  C   ALA B 160     4548   6855   4834   1098   -605  -1086       C  
ATOM   5417  O   ALA B 160      27.520  -1.080 -48.656  1.00 43.90           O  
ANISOU 5417  O   ALA B 160     4705   6996   4978   1163   -667  -1119       O  
ATOM   5418  CB  ALA B 160      25.430   1.094 -48.828  1.00 38.00           C  
ANISOU 5418  CB  ALA B 160     4030   6067   4339    846   -528   -945       C  
ATOM   5419  N   LEU B 161      27.788  -0.418 -50.756  1.00 40.02           N  
ANISOU 5419  N   LEU B 161     4103   6664   4439   1123   -562  -1125       N  
ATOM   5420  CA  LEU B 161      29.237  -0.463 -50.628  1.00 45.45           C  
ANISOU 5420  CA  LEU B 161     4650   7545   5075   1187   -566  -1204       C  
ATOM   5421  C   LEU B 161      29.684   0.976 -50.772  1.00 38.03           C  
ANISOU 5421  C   LEU B 161     3593   6717   4138   1026   -466  -1174       C  
ATOM   5422  O   LEU B 161      29.885   1.458 -51.884  1.00 46.10           O  
ANISOU 5422  O   LEU B 161     4555   7835   5125    980   -396  -1172       O  
ATOM   5423  CB  LEU B 161      29.856  -1.400 -51.676  1.00 48.33           C  
ANISOU 5423  CB  LEU B 161     4974   8020   5367   1341   -592  -1285       C  
ATOM   5424  CG  LEU B 161      29.574  -2.864 -51.322  1.00 48.21           C  
ANISOU 5424  CG  LEU B 161     5086   7889   5343   1509   -706  -1324       C  
ATOM   5425  CD1 LEU B 161      29.740  -3.722 -52.512  1.00 65.14           C  
ANISOU 5425  CD1 LEU B 161     7239  10084   7427   1640   -727  -1381       C  
ATOM   5426  CD2 LEU B 161      30.508  -3.354 -50.221  1.00 48.51           C  
ANISOU 5426  CD2 LEU B 161     5086   7984   5360   1611   -779  -1389       C  
ATOM   5427  N   PRO B 162      29.796   1.684 -49.644  1.00 39.70           N  
ANISOU 5427  N   PRO B 162     3788   6908   4388    933   -460  -1148       N  
ATOM   5428  CA  PRO B 162      29.912   3.143 -49.742  1.00 47.28           C  
ANISOU 5428  CA  PRO B 162     4684   7919   5361    753   -366  -1099       C  
ATOM   5429  C   PRO B 162      31.084   3.495 -50.615  1.00 52.41           C  
ANISOU 5429  C   PRO B 162     5179   8790   5943    737   -305  -1154       C  
ATOM   5430  O   PRO B 162      32.159   2.905 -50.470  1.00 51.82           O  
ANISOU 5430  O   PRO B 162     4998   8866   5823    840   -340  -1241       O  
ATOM   5431  CB  PRO B 162      30.165   3.578 -48.297  1.00 46.70           C  
ANISOU 5431  CB  PRO B 162     4599   7822   5324    698   -390  -1094       C  
ATOM   5432  CG  PRO B 162      29.587   2.494 -47.474  1.00 45.48           C  
ANISOU 5432  CG  PRO B 162     4560   7526   5196    814   -484  -1099       C  
ATOM   5433  CD  PRO B 162      29.810   1.222 -48.250  1.00 38.01           C  
ANISOU 5433  CD  PRO B 162     3623   6616   4202    982   -536  -1160       C  
ATOM   5434  N   GLY B 163      30.876   4.417 -51.537  1.00 53.07           N  
ANISOU 5434  N   GLY B 163     5253   8898   6014    614   -217  -1105       N  
ATOM   5435  CA  GLY B 163      31.934   4.775 -52.457  1.00 55.91           C  
ANISOU 5435  CA  GLY B 163     5473   9470   6300    581   -148  -1152       C  
ATOM   5436  C   GLY B 163      31.781   4.101 -53.801  1.00 56.39           C  
ANISOU 5436  C   GLY B 163     5548   9567   6310    677   -139  -1173       C  
ATOM   5437  O   GLY B 163      32.160   4.654 -54.827  1.00 60.17           O  
ANISOU 5437  O   GLY B 163     5966  10162   6735    606    -58  -1171       O  
ATOM   5438  N   SER B 164      31.222   2.900 -53.803  1.00 56.29           N  
ANISOU 5438  N   SER B 164     5626   9452   6312    834   -222  -1194       N  
ATOM   5439  CA  SER B 164      31.006   2.171 -55.049  1.00 53.41           C  
ANISOU 5439  CA  SER B 164     5289   9104   5899    936   -225  -1217       C  
ATOM   5440  C   SER B 164      30.098   2.954 -55.991  1.00 54.28           C  
ANISOU 5440  C   SER B 164     5478   9132   6015    821   -157  -1134       C  
ATOM   5441  O   SER B 164      29.351   3.840 -55.566  1.00 56.22           O  
ANISOU 5441  O   SER B 164     5793   9254   6315    692   -131  -1053       O  
ATOM   5442  CB  SER B 164      30.371   0.825 -54.744  1.00 53.99           C  
ANISOU 5442  CB  SER B 164     5480   9037   5996   1099   -333  -1240       C  
ATOM   5443  OG  SER B 164      28.975   0.977 -54.528  1.00 49.18           O  
ANISOU 5443  OG  SER B 164     5020   8212   5454   1037   -347  -1155       O  
ATOM   5444  N   ARG B 165      30.153   2.642 -57.274  1.00 58.40           N  
ANISOU 5444  N   ARG B 165     5992   9722   6476    873   -130  -1155       N  
ATOM   5445  CA  ARG B 165      29.289   3.334 -58.217  1.00 64.81           C  
ANISOU 5445  CA  ARG B 165     6885  10455   7285    779    -73  -1078       C  
ATOM   5446  C   ARG B 165      27.952   2.614 -58.313  1.00 63.00           C  
ANISOU 5446  C   ARG B 165     6807  10026   7103    854   -144  -1046       C  
ATOM   5447  O   ARG B 165      26.918   3.232 -58.572  1.00 64.22           O  
ANISOU 5447  O   ARG B 165     7057  10055   7290    770   -123   -969       O  
ATOM   5448  CB  ARG B 165      29.940   3.431 -59.596  1.00 72.28           C  
ANISOU 5448  CB  ARG B 165     7757  11569   8136    784     -4  -1111       C  
ATOM   5449  CG  ARG B 165      29.206   4.357 -60.552  1.00 86.34           C  
ANISOU 5449  CG  ARG B 165     9618  13287   9900    666     65  -1028       C  
ATOM   5450  CD  ARG B 165      29.611   4.118 -62.006  1.00102.15           C  
ANISOU 5450  CD  ARG B 165    11584  15422  11805    712    112  -1063       C  
ATOM   5451  NE  ARG B 165      28.821   4.934 -62.929  1.00114.81           N  
ANISOU 5451  NE  ARG B 165    13287  16948  13389    614    166   -981       N  
ATOM   5452  CZ  ARG B 165      27.587   4.629 -63.334  1.00119.74           C  
ANISOU 5452  CZ  ARG B 165    14046  17407  14045    663    118   -941       C  
ATOM   5453  NH1 ARG B 165      26.993   3.520 -62.900  1.00118.77           N  
ANISOU 5453  NH1 ARG B 165    13977  17176  13974    794     21   -971       N  
ATOM   5454  NH2 ARG B 165      26.945   5.433 -64.176  1.00120.33           N  
ANISOU 5454  NH2 ARG B 165    14204  17424  14092    578    165   -871       N  
ATOM   5455  N   GLU B 166      27.975   1.308 -58.069  1.00 57.37           N  
ANISOU 5455  N   GLU B 166     6121   9286   6392   1012   -231  -1107       N  
ATOM   5456  CA  GLU B 166      26.842   0.464 -58.418  1.00 58.21           C  
ANISOU 5456  CA  GLU B 166     6361   9233   6522   1091   -296  -1093       C  
ATOM   5457  C   GLU B 166      26.000   0.023 -57.217  1.00 50.78           C  
ANISOU 5457  C   GLU B 166     5522   8112   5660   1099   -371  -1065       C  
ATOM   5458  O   GLU B 166      24.951  -0.601 -57.394  1.00 48.84           O  
ANISOU 5458  O   GLU B 166     5391   7724   5441   1137   -421  -1047       O  
ATOM   5459  CB  GLU B 166      27.307  -0.734 -59.269  1.00 65.49           C  
ANISOU 5459  CB  GLU B 166     7274  10234   7376   1259   -339  -1177       C  
ATOM   5460  CG  GLU B 166      28.495  -1.484 -58.702  1.00 75.56           C  
ANISOU 5460  CG  GLU B 166     8462  11631   8617   1383   -384  -1269       C  
ATOM   5461  CD  GLU B 166      29.858  -0.955 -59.186  1.00 79.48           C  
ANISOU 5461  CD  GLU B 166     8785  12374   9039   1367   -307  -1322       C  
ATOM   5462  OE1 GLU B 166      30.140  -1.028 -60.407  1.00 77.04           O  
ANISOU 5462  OE1 GLU B 166     8439  12173   8660   1401   -265  -1351       O  
ATOM   5463  OE2 GLU B 166      30.656  -0.493 -58.332  1.00 77.83           O  
ANISOU 5463  OE2 GLU B 166     8475  12257   8839   1320   -290  -1339       O  
ATOM   5464  N   ALA B 167      26.466   0.362 -56.013  1.00 44.28           N  
ANISOU 5464  N   ALA B 167     4653   7301   4870   1056   -375  -1064       N  
ATOM   5465  CA  ALA B 167      25.699   0.208 -54.773  1.00 41.96           C  
ANISOU 5465  CA  ALA B 167     4449   6847   4649   1031   -427  -1027       C  
ATOM   5466  C   ALA B 167      26.044   1.327 -53.790  1.00 45.95           C  
ANISOU 5466  C   ALA B 167     4895   7378   5188    906   -382   -992       C  
ATOM   5467  O   ALA B 167      26.645   1.085 -52.729  1.00 48.40           O  
ANISOU 5467  O   ALA B 167     5171   7710   5507    936   -419  -1023       O  
ATOM   5468  CB  ALA B 167      25.977  -1.134 -54.145  1.00 41.68           C  
ANISOU 5468  CB  ALA B 167     4455   6778   4605   1176   -523  -1089       C  
ATOM   5469  N   PRO B 168      25.695   2.563 -54.150  1.00 44.34           N  
ANISOU 5469  N   PRO B 168     4682   7169   4996    769   -306   -929       N  
ATOM   5470  CA  PRO B 168      26.012   3.772 -53.369  1.00 42.43           C  
ANISOU 5470  CA  PRO B 168     4392   6949   4779    635   -255   -892       C  
ATOM   5471  C   PRO B 168      25.303   3.836 -51.999  1.00 43.49           C  
ANISOU 5471  C   PRO B 168     4600   6939   4985    601   -296   -856       C  
ATOM   5472  O   PRO B 168      25.684   4.657 -51.152  1.00 41.94           O  
ANISOU 5472  O   PRO B 168     4364   6763   4808    512   -271   -840       O  
ATOM   5473  CB  PRO B 168      25.483   4.900 -54.263  1.00 37.33           C  
ANISOU 5473  CB  PRO B 168     3773   6286   4126    518   -179   -827       C  
ATOM   5474  CG  PRO B 168      24.348   4.216 -55.056  1.00 40.68           C  
ANISOU 5474  CG  PRO B 168     4299   6600   4557    589   -215   -811       C  
ATOM   5475  CD  PRO B 168      24.933   2.873 -55.374  1.00 41.55           C  
ANISOU 5475  CD  PRO B 168     4381   6779   4628    739   -269   -889       C  
ATOM   5476  N   GLY B 169      24.293   2.992 -51.784  1.00 39.52           N  
ANISOU 5476  N   GLY B 169     4203   6296   4517    664   -357   -845       N  
ATOM   5477  CA  GLY B 169      23.468   3.069 -50.584  1.00 39.10           C  
ANISOU 5477  CA  GLY B 169     4227   6104   4526    622   -387   -806       C  
ATOM   5478  C   GLY B 169      22.342   4.105 -50.666  1.00 33.94           C  
ANISOU 5478  C   GLY B 169     3631   5351   3915    509   -342   -732       C  
ATOM   5479  O   GLY B 169      22.319   4.953 -51.569  1.00 36.56           O  
ANISOU 5479  O   GLY B 169     3941   5723   4226    449   -284   -705       O  
ATOM   5480  N   ASN B 170      21.406   4.032 -49.724  1.00 34.94           N  
ANISOU 5480  N   ASN B 170     3832   5348   4094    484   -370   -701       N  
ATOM   5481  CA  ASN B 170      20.287   4.978 -49.643  1.00 34.49           C  
ANISOU 5481  CA  ASN B 170     3828   5198   4078    391   -337   -640       C  
ATOM   5482  C   ASN B 170      19.326   5.006 -50.864  1.00 37.70           C  
ANISOU 5482  C   ASN B 170     4280   5564   4481    399   -326   -617       C  
ATOM   5483  O   ASN B 170      18.532   5.951 -51.013  1.00 37.75           O  
ANISOU 5483  O   ASN B 170     4318   5517   4509    330   -294   -570       O  
ATOM   5484  CB  ASN B 170      20.807   6.389 -49.344  1.00 28.62           C  
ANISOU 5484  CB  ASN B 170     3038   4501   3334    285   -276   -611       C  
ATOM   5485  CG  ASN B 170      21.465   6.494 -47.981  1.00 33.89           C  
ANISOU 5485  CG  ASN B 170     3675   5184   4018    263   -291   -627       C  
ATOM   5486  OD1 ASN B 170      21.141   5.745 -47.066  1.00 35.85           O  
ANISOU 5486  OD1 ASN B 170     3965   5366   4291    306   -341   -638       O  
ATOM   5487  ND2 ASN B 170      22.407   7.441 -47.836  1.00 41.46           N  
ANISOU 5487  ND2 ASN B 170     4565   6231   4958    189   -247   -628       N  
ATOM   5488  N   VAL B 171      19.368   3.989 -51.725  1.00 36.00           N  
ANISOU 5488  N   VAL B 171     4073   5370   4235    487   -358   -652       N  
ATOM   5489  CA  VAL B 171      18.540   4.018 -52.932  1.00 34.64           C  
ANISOU 5489  CA  VAL B 171     3939   5170   4051    497   -352   -636       C  
ATOM   5490  C   VAL B 171      17.027   3.929 -52.631  1.00 37.33           C  
ANISOU 5490  C   VAL B 171     4357   5382   4444    474   -378   -606       C  
ATOM   5491  O   VAL B 171      16.194   4.416 -53.399  1.00 36.24           O  
ANISOU 5491  O   VAL B 171     4246   5215   4308    453   -363   -579       O  
ATOM   5492  CB  VAL B 171      18.962   2.962 -53.995  1.00 34.68           C  
ANISOU 5492  CB  VAL B 171     3937   5234   4006    600   -381   -685       C  
ATOM   5493  CG1 VAL B 171      20.481   3.033 -54.273  1.00 29.16           C  
ANISOU 5493  CG1 VAL B 171     3145   4684   3251    628   -352   -724       C  
ATOM   5494  CG2 VAL B 171      18.510   1.528 -53.606  1.00 26.29           C  
ANISOU 5494  CG2 VAL B 171     2938   4091   2958    681   -459   -720       C  
ATOM   5495  N   GLY B 172      16.669   3.310 -51.513  1.00 34.42           N  
ANISOU 5495  N   GLY B 172     4023   4943   4112    478   -417   -613       N  
ATOM   5496  CA  GLY B 172      15.287   3.332 -51.064  1.00 29.03           C  
ANISOU 5496  CA  GLY B 172     3397   4156   3476    437   -431   -587       C  
ATOM   5497  C   GLY B 172      14.834   4.736 -50.662  1.00 32.28           C  
ANISOU 5497  C   GLY B 172     3799   4549   3917    353   -383   -541       C  
ATOM   5498  O   GLY B 172      13.658   5.084 -50.832  1.00 33.81           O  
ANISOU 5498  O   GLY B 172     4024   4687   4136    328   -382   -520       O  
ATOM   5499  N   LEU B 173      15.748   5.565 -50.140  1.00 31.23           N  
ANISOU 5499  N   LEU B 173     3626   4464   3777    312   -347   -530       N  
ATOM   5500  CA  LEU B 173      15.384   6.955 -49.863  1.00 28.24           C  
ANISOU 5500  CA  LEU B 173     3251   4062   3416    235   -303   -488       C  
ATOM   5501  C   LEU B 173      15.275   7.724 -51.172  1.00 32.83           C  
ANISOU 5501  C   LEU B 173     3836   4672   3965    227   -271   -467       C  
ATOM   5502  O   LEU B 173      14.393   8.591 -51.342  1.00 32.56           O  
ANISOU 5502  O   LEU B 173     3839   4588   3945    195   -256   -435       O  
ATOM   5503  CB  LEU B 173      16.358   7.622 -48.878  1.00 25.55           C  
ANISOU 5503  CB  LEU B 173     2875   3755   3076    183   -277   -483       C  
ATOM   5504  CG  LEU B 173      16.378   7.087 -47.434  1.00 31.07           C  
ANISOU 5504  CG  LEU B 173     3584   4416   3806    183   -308   -497       C  
ATOM   5505  CD1 LEU B 173      17.505   7.696 -46.655  1.00 29.59           C  
ANISOU 5505  CD1 LEU B 173     3352   4281   3609    141   -287   -501       C  
ATOM   5506  CD2 LEU B 173      15.066   7.335 -46.708  1.00 29.00           C  
ANISOU 5506  CD2 LEU B 173     3373   4057   3587    150   -312   -473       C  
ATOM   5507  N   LEU B 174      16.155   7.389 -52.114  1.00 34.76           N  
ANISOU 5507  N   LEU B 174     4046   4999   4161    261   -262   -487       N  
ATOM   5508  CA  LEU B 174      16.058   7.950 -53.468  1.00 36.72           C  
ANISOU 5508  CA  LEU B 174     4308   5278   4367    260   -234   -469       C  
ATOM   5509  C   LEU B 174      14.720   7.567 -54.149  1.00 37.36           C  
ANISOU 5509  C   LEU B 174     4442   5293   4462    305   -269   -466       C  
ATOM   5510  O   LEU B 174      14.152   8.376 -54.891  1.00 29.73           O  
ANISOU 5510  O   LEU B 174     3510   4307   3478    290   -253   -437       O  
ATOM   5511  CB  LEU B 174      17.271   7.561 -54.335  1.00 34.52           C  
ANISOU 5511  CB  LEU B 174     3976   5113   4027    292   -215   -498       C  
ATOM   5512  CG  LEU B 174      18.589   8.217 -53.846  1.00 40.55           C  
ANISOU 5512  CG  LEU B 174     4677   5963   4769    229   -170   -500       C  
ATOM   5513  CD1 LEU B 174      19.815   7.717 -54.614  1.00 31.50           C  
ANISOU 5513  CD1 LEU B 174     3459   4951   3560    268   -152   -542       C  
ATOM   5514  CD2 LEU B 174      18.505   9.747 -53.914  1.00 32.05           C  
ANISOU 5514  CD2 LEU B 174     3630   4865   3682    127   -116   -447       C  
ATOM   5515  N   ASP B 175      14.210   6.354 -53.892  1.00 31.14           N  
ANISOU 5515  N   ASP B 175     3663   4469   3699    357   -321   -498       N  
ATOM   5516  CA  ASP B 175      12.909   5.999 -54.452  1.00 31.57           C  
ANISOU 5516  CA  ASP B 175     3759   4468   3769    385   -356   -500       C  
ATOM   5517  C   ASP B 175      11.853   6.980 -53.914  1.00 33.50           C  
ANISOU 5517  C   ASP B 175     4028   4650   4053    336   -345   -468       C  
ATOM   5518  O   ASP B 175      11.043   7.493 -54.668  1.00 32.67           O  
ANISOU 5518  O   ASP B 175     3948   4527   3939    346   -348   -454       O  
ATOM   5519  CB  ASP B 175      12.492   4.554 -54.106  1.00 28.96           C  
ANISOU 5519  CB  ASP B 175     3445   4098   3460    427   -412   -539       C  
ATOM   5520  CG  ASP B 175      13.454   3.500 -54.653  1.00 30.78           C  
ANISOU 5520  CG  ASP B 175     3664   4382   3648    496   -435   -579       C  
ATOM   5521  OD1 ASP B 175      14.219   3.786 -55.616  1.00 32.59           O  
ANISOU 5521  OD1 ASP B 175     3868   4688   3828    521   -409   -583       O  
ATOM   5522  OD2 ASP B 175      13.451   2.370 -54.098  1.00 31.84           O  
ANISOU 5522  OD2 ASP B 175     3821   4481   3794    526   -480   -609       O  
ATOM   5523  N   GLN B 176      11.881   7.242 -52.609  1.00 32.35           N  
ANISOU 5523  N   GLN B 176     3874   4473   3944    291   -335   -459       N  
ATOM   5524  CA  GLN B 176      10.917   8.127 -51.993  1.00 27.56           C  
ANISOU 5524  CA  GLN B 176     3287   3812   3371    254   -326   -436       C  
ATOM   5525  C   GLN B 176      11.014   9.509 -52.619  1.00 34.99           C  
ANISOU 5525  C   GLN B 176     4252   4760   4284    233   -291   -400       C  
ATOM   5526  O   GLN B 176       9.992  10.149 -52.940  1.00 35.43           O  
ANISOU 5526  O   GLN B 176     4339   4779   4344    243   -299   -388       O  
ATOM   5527  CB  GLN B 176      11.191   8.233 -50.503  1.00 29.64           C  
ANISOU 5527  CB  GLN B 176     3541   4053   3668    209   -316   -432       C  
ATOM   5528  CG  GLN B 176      10.833   6.977 -49.726  1.00 29.52           C  
ANISOU 5528  CG  GLN B 176     3527   4009   3681    219   -352   -460       C  
ATOM   5529  CD  GLN B 176      11.419   6.991 -48.343  1.00 29.97           C  
ANISOU 5529  CD  GLN B 176     3578   4055   3754    183   -343   -458       C  
ATOM   5530  OE1 GLN B 176      11.750   8.063 -47.827  1.00 30.12           O  
ANISOU 5530  OE1 GLN B 176     3590   4076   3777    143   -310   -436       O  
ATOM   5531  NE2 GLN B 176      11.544   5.803 -47.717  1.00 29.63           N  
ANISOU 5531  NE2 GLN B 176     3547   3994   3718    198   -375   -481       N  
ATOM   5532  N   ARG B 177      12.245   9.975 -52.767  1.00 27.74           N  
ANISOU 5532  N   ARG B 177     3319   3889   3330    203   -254   -387       N  
ATOM   5533  CA  ARG B 177      12.509  11.278 -53.355  1.00 31.39           C  
ANISOU 5533  CA  ARG B 177     3817   4355   3753    166   -217   -350       C  
ATOM   5534  C   ARG B 177      11.963  11.407 -54.778  1.00 37.99           C  
ANISOU 5534  C   ARG B 177     4692   5193   4549    210   -227   -341       C  
ATOM   5535  O   ARG B 177      11.337  12.440 -55.126  1.00 33.40           O  
ANISOU 5535  O   ARG B 177     4170   4567   3953    205   -222   -312       O  
ATOM   5536  CB  ARG B 177      14.009  11.595 -53.357  1.00 24.33           C  
ANISOU 5536  CB  ARG B 177     2891   3531   2821    114   -173   -344       C  
ATOM   5537  CG  ARG B 177      14.336  12.932 -54.000  1.00 33.06           C  
ANISOU 5537  CG  ARG B 177     4047   4637   3877     57   -129   -302       C  
ATOM   5538  CD  ARG B 177      15.826  13.213 -53.965  1.00 32.47           C  
ANISOU 5538  CD  ARG B 177     3928   4646   3764    -11    -82   -302       C  
ATOM   5539  NE  ARG B 177      16.182  13.619 -52.619  1.00 41.76           N  
ANISOU 5539  NE  ARG B 177     5087   5804   4977    -69    -74   -301       N  
ATOM   5540  CZ  ARG B 177      17.426  13.648 -52.136  1.00 46.01           C  
ANISOU 5540  CZ  ARG B 177     5563   6417   5501   -123    -47   -316       C  
ATOM   5541  NH1 ARG B 177      18.465  13.300 -52.920  1.00 44.66           N  
ANISOU 5541  NH1 ARG B 177     5334   6356   5279   -128    -20   -335       N  
ATOM   5542  NH2 ARG B 177      17.625  14.043 -50.881  1.00 33.20           N  
ANISOU 5542  NH2 ARG B 177     3934   4768   3913   -172    -47   -317       N  
ATOM   5543  N   LEU B 178      12.211  10.375 -55.595  1.00 30.81           N  
ANISOU 5543  N   LEU B 178     3757   4332   3617    260   -244   -369       N  
ATOM   5544  CA  LEU B 178      11.741  10.371 -56.966  1.00 31.18           C  
ANISOU 5544  CA  LEU B 178     3840   4388   3621    308   -258   -366       C  
ATOM   5545  C   LEU B 178      10.206  10.485 -56.967  1.00 32.71           C  
ANISOU 5545  C   LEU B 178     4065   4514   3848    344   -301   -369       C  
ATOM   5546  O   LEU B 178       9.626  11.245 -57.764  1.00 38.42           O  
ANISOU 5546  O   LEU B 178     4842   5216   4539    364   -307   -349       O  
ATOM   5547  CB  LEU B 178      12.222   9.131 -57.717  1.00 28.13           C  
ANISOU 5547  CB  LEU B 178     3419   4061   3207    362   -276   -404       C  
ATOM   5548  CG  LEU B 178      11.788   9.137 -59.177  1.00 36.53           C  
ANISOU 5548  CG  LEU B 178     4523   5138   4220    412   -290   -403       C  
ATOM   5549  CD1 LEU B 178      12.335  10.386 -59.852  1.00 35.06           C  
ANISOU 5549  CD1 LEU B 178     4379   4972   3970    368   -238   -358       C  
ATOM   5550  CD2 LEU B 178      12.263   7.886 -59.907  1.00 36.67           C  
ANISOU 5550  CD2 LEU B 178     4511   5213   4207    471   -310   -445       C  
ATOM   5551  N   ALA B 179       9.549   9.781 -56.050  1.00 28.61           N  
ANISOU 5551  N   ALA B 179     3516   3965   3387    349   -332   -396       N  
ATOM   5552  CA  ALA B 179       8.078   9.926 -55.887  1.00 30.82           C  
ANISOU 5552  CA  ALA B 179     3809   4200   3703    373   -368   -406       C  
ATOM   5553  C   ALA B 179       7.666  11.348 -55.443  1.00 30.52           C  
ANISOU 5553  C   ALA B 179     3808   4118   3668    352   -349   -375       C  
ATOM   5554  O   ALA B 179       6.686  11.884 -55.915  1.00 35.66           O  
ANISOU 5554  O   ALA B 179     4490   4747   4311    392   -374   -374       O  
ATOM   5555  CB  ALA B 179       7.540   8.883 -54.915  1.00 26.62           C  
ANISOU 5555  CB  ALA B 179     3237   3651   3226    364   -394   -440       C  
ATOM   5556  N   LEU B 180       8.433  11.965 -54.555  1.00 32.51           N  
ANISOU 5556  N   LEU B 180     4064   4361   3928    295   -310   -352       N  
ATOM   5557  CA  LEU B 180       8.203  13.371 -54.183  1.00 33.67           C  
ANISOU 5557  CA  LEU B 180     4265   4460   4069    272   -293   -321       C  
ATOM   5558  C   LEU B 180       8.304  14.292 -55.417  1.00 35.43           C  
ANISOU 5558  C   LEU B 180     4563   4674   4226    289   -286   -288       C  
ATOM   5559  O   LEU B 180       7.488  15.213 -55.566  1.00 36.90           O  
ANISOU 5559  O   LEU B 180     4808   4811   4400    320   -303   -276       O  
ATOM   5560  CB  LEU B 180       9.158  13.820 -53.060  1.00 24.97           C  
ANISOU 5560  CB  LEU B 180     3154   3351   2980    199   -253   -304       C  
ATOM   5561  CG  LEU B 180       8.756  13.627 -51.589  1.00 29.83           C  
ANISOU 5561  CG  LEU B 180     3738   3942   3654    179   -258   -322       C  
ATOM   5562  CD1 LEU B 180       7.981  12.320 -51.324  1.00 32.66           C  
ANISOU 5562  CD1 LEU B 180     4043   4313   4052    212   -292   -361       C  
ATOM   5563  CD2 LEU B 180       9.926  13.785 -50.603  1.00 28.96           C  
ANISOU 5563  CD2 LEU B 180     3611   3843   3551    111   -224   -312       C  
ATOM   5564  N   GLN B 181       9.274  14.019 -56.300  1.00 35.08           N  
ANISOU 5564  N   GLN B 181     4518   4678   4133    275   -263   -277       N  
ATOM   5565  CA  GLN B 181       9.460  14.776 -57.553  1.00 35.78           C  
ANISOU 5565  CA  GLN B 181     4683   4765   4146    283   -251   -245       C  
ATOM   5566  C   GLN B 181       8.223  14.578 -58.433  1.00 35.42           C  
ANISOU 5566  C   GLN B 181     4664   4702   4091    373   -305   -262       C  
ATOM   5567  O   GLN B 181       7.678  15.531 -59.025  1.00 34.85           O  
ANISOU 5567  O   GLN B 181     4677   4586   3978    404   -320   -238       O  
ATOM   5568  CB  GLN B 181      10.712  14.316 -58.311  1.00 35.81           C  
ANISOU 5568  CB  GLN B 181     4662   4845   4099    253   -213   -241       C  
ATOM   5569  CG  GLN B 181      11.992  15.164 -58.054  1.00 86.62           C  
ANISOU 5569  CG  GLN B 181    11114  11300  10497    154   -149   -206       C  
ATOM   5570  CD  GLN B 181      13.328  14.344 -57.955  1.00 79.23           C  
ANISOU 5570  CD  GLN B 181    10087  10465   9553    117   -114   -229       C  
ATOM   5571  OE1 GLN B 181      13.392  13.147 -58.276  1.00 81.42           O  
ANISOU 5571  OE1 GLN B 181    10304  10794   9839    174   -136   -268       O  
ATOM   5572  NE2 GLN B 181      14.384  15.007 -57.492  1.00 70.24           N  
ANISOU 5572  NE2 GLN B 181     8940   9353   8395     25    -63   -210       N  
ATOM   5573  N   TRP B 182       7.775  13.332 -58.495  1.00 33.28           N  
ANISOU 5573  N   TRP B 182     4325   4465   3856    415   -340   -306       N  
ATOM   5574  CA  TRP B 182       6.630  12.981 -59.318  1.00 32.57           C  
ANISOU 5574  CA  TRP B 182     4243   4373   3760    494   -395   -332       C  
ATOM   5575  C   TRP B 182       5.437  13.789 -58.857  1.00 32.98           C  
ANISOU 5575  C   TRP B 182     4320   4373   3836    528   -426   -335       C  
ATOM   5576  O   TRP B 182       4.736  14.369 -59.686  1.00 39.02           O  
ANISOU 5576  O   TRP B 182     5144   5121   4562    589   -459   -331       O  
ATOM   5577  CB  TRP B 182       6.343  11.482 -59.252  1.00 30.27           C  
ANISOU 5577  CB  TRP B 182     3875   4117   3508    516   -427   -382       C  
ATOM   5578  CG  TRP B 182       5.280  11.037 -60.182  1.00 36.69           C  
ANISOU 5578  CG  TRP B 182     4692   4940   4310    587   -485   -413       C  
ATOM   5579  CD1 TRP B 182       5.443  10.497 -61.441  1.00 32.05           C  
ANISOU 5579  CD1 TRP B 182     4120   4385   3672    629   -504   -424       C  
ATOM   5580  CD2 TRP B 182       3.866  11.091 -59.950  1.00 39.28           C  
ANISOU 5580  CD2 TRP B 182     4999   5251   4674    625   -533   -445       C  
ATOM   5581  NE1 TRP B 182       4.217  10.196 -61.984  1.00 33.26           N  
ANISOU 5581  NE1 TRP B 182     4267   4539   3830    689   -565   -460       N  
ATOM   5582  CE2 TRP B 182       3.236  10.543 -61.088  1.00 36.97           C  
ANISOU 5582  CE2 TRP B 182     4709   4984   4353    687   -584   -475       C  
ATOM   5583  CE3 TRP B 182       3.075  11.535 -58.882  1.00 34.80           C  
ANISOU 5583  CE3 TRP B 182     4406   4660   4157    615   -538   -455       C  
ATOM   5584  CZ2 TRP B 182       1.856  10.440 -61.189  1.00 40.85           C  
ANISOU 5584  CZ2 TRP B 182     5172   5483   4868    734   -640   -517       C  
ATOM   5585  CZ3 TRP B 182       1.705  11.422 -58.973  1.00 35.48           C  
ANISOU 5585  CZ3 TRP B 182     4459   4758   4264    664   -590   -498       C  
ATOM   5586  CH2 TRP B 182       1.102  10.890 -60.119  1.00 40.99           C  
ANISOU 5586  CH2 TRP B 182     5154   5486   4935    721   -641   -529       C  
ATOM   5587  N   VAL B 183       5.245  13.878 -57.537  1.00 35.04           N  
ANISOU 5587  N   VAL B 183     4544   4615   4156    493   -415   -344       N  
ATOM   5588  CA  VAL B 183       4.179  14.712 -56.983  1.00 32.54           C  
ANISOU 5588  CA  VAL B 183     4247   4257   3859    527   -439   -352       C  
ATOM   5589  C   VAL B 183       4.291  16.201 -57.434  1.00 42.85           C  
ANISOU 5589  C   VAL B 183     5668   5508   5106    545   -433   -309       C  
ATOM   5590  O   VAL B 183       3.284  16.820 -57.883  1.00 34.57           O  
ANISOU 5590  O   VAL B 183     4665   4434   4035    624   -478   -319       O  
ATOM   5591  CB  VAL B 183       4.074  14.570 -55.458  1.00 31.77           C  
ANISOU 5591  CB  VAL B 183     4094   4151   3825    481   -421   -368       C  
ATOM   5592  CG1 VAL B 183       3.139  15.695 -54.842  1.00 25.98           C  
ANISOU 5592  CG1 VAL B 183     3394   3375   3101    518   -436   -373       C  
ATOM   5593  CG2 VAL B 183       3.561  13.174 -55.110  1.00 28.88           C  
ANISOU 5593  CG2 VAL B 183     3636   3827   3509    477   -442   -414       C  
ATOM   5594  N   GLN B 184       5.494  16.763 -57.348  1.00 30.36           N  
ANISOU 5594  N   GLN B 184     4136   3907   3492    472   -382   -263       N  
ATOM   5595  CA  GLN B 184       5.692  18.150 -57.801  1.00 36.50           C  
ANISOU 5595  CA  GLN B 184     5042   4622   4204    470   -373   -217       C  
ATOM   5596  C   GLN B 184       5.234  18.329 -59.243  1.00 39.89           C  
ANISOU 5596  C   GLN B 184     5542   5049   4567    543   -410   -209       C  
ATOM   5597  O   GLN B 184       4.515  19.284 -59.564  1.00 40.29           O  
ANISOU 5597  O   GLN B 184     5687   5041   4580    607   -446   -199       O  
ATOM   5598  CB  GLN B 184       7.160  18.594 -57.667  1.00 29.06           C  
ANISOU 5598  CB  GLN B 184     4135   3678   3228    361   -308   -172       C  
ATOM   5599  CG  GLN B 184       7.560  18.838 -56.242  1.00 35.49           C  
ANISOU 5599  CG  GLN B 184     4917   4474   4093    294   -279   -173       C  
ATOM   5600  CD  GLN B 184       6.667  19.884 -55.599  1.00 41.35           C  
ANISOU 5600  CD  GLN B 184     5729   5136   4845    334   -307   -173       C  
ATOM   5601  OE1 GLN B 184       6.584  21.011 -56.079  1.00 50.46           O  
ANISOU 5601  OE1 GLN B 184     7009   6224   5941    345   -315   -140       O  
ATOM   5602  NE2 GLN B 184       5.988  19.516 -54.526  1.00 37.17           N  
ANISOU 5602  NE2 GLN B 184     5127   4614   4384    357   -324   -212       N  
ATOM   5603  N   GLU B 185       5.632  17.393 -60.101  1.00 38.47           N  
ANISOU 5603  N   GLU B 185     5320   4931   4368    544   -405   -217       N  
ATOM   5604  CA  GLU B 185       5.403  17.534 -61.536  1.00 42.09           C  
ANISOU 5604  CA  GLU B 185     5851   5392   4751    603   -432   -205       C  
ATOM   5605  C   GLU B 185       3.978  17.182 -61.983  1.00 40.93           C  
ANISOU 5605  C   GLU B 185     5681   5253   4618    717   -510   -252       C  
ATOM   5606  O   GLU B 185       3.546  17.634 -63.045  1.00 42.82           O  
ANISOU 5606  O   GLU B 185     6005   5474   4792    785   -547   -242       O  
ATOM   5607  CB  GLU B 185       6.382  16.661 -62.327  1.00 46.01           C  
ANISOU 5607  CB  GLU B 185     6310   5958   5215    567   -398   -201       C  
ATOM   5608  CG  GLU B 185       7.842  16.913 -62.041  1.00 58.67           C  
ANISOU 5608  CG  GLU B 185     7916   7581   6795    457   -321   -164       C  
ATOM   5609  CD  GLU B 185       8.751  15.943 -62.794  1.00 68.88           C  
ANISOU 5609  CD  GLU B 185     9154   8961   8057    439   -292   -175       C  
ATOM   5610  OE1 GLU B 185       8.229  15.186 -63.652  1.00 72.37           O  
ANISOU 5610  OE1 GLU B 185     9579   9433   8484    514   -332   -204       O  
ATOM   5611  OE2 GLU B 185       9.981  15.934 -62.522  1.00 70.99           O  
ANISOU 5611  OE2 GLU B 185     9391   9272   8311    354   -230   -160       O  
ATOM   5612  N   ASN B 186       3.262  16.367 -61.206  1.00 39.00           N  
ANISOU 5612  N   ASN B 186     5324   5040   4453    734   -535   -305       N  
ATOM   5613  CA  ASN B 186       2.009  15.779 -61.688  1.00 35.88           C  
ANISOU 5613  CA  ASN B 186     4880   4678   4073    823   -604   -359       C  
ATOM   5614  C   ASN B 186       0.785  15.996 -60.803  1.00 36.53           C  
ANISOU 5614  C   ASN B 186     4910   4757   4211    868   -642   -403       C  
ATOM   5615  O   ASN B 186      -0.343  15.796 -61.229  1.00 41.40           O  
ANISOU 5615  O   ASN B 186     5495   5404   4830    948   -704   -450       O  
ATOM   5616  CB  ASN B 186       2.200  14.268 -61.904  1.00 39.21           C  
ANISOU 5616  CB  ASN B 186     5207   5164   4526    800   -606   -395       C  
ATOM   5617  CG  ASN B 186       3.220  13.963 -62.983  1.00 42.72           C  
ANISOU 5617  CG  ASN B 186     5695   5631   4907    784   -581   -367       C  
ATOM   5618  OD1 ASN B 186       3.015  14.301 -64.135  1.00 45.13           O  
ANISOU 5618  OD1 ASN B 186     6070   5933   5145    841   -608   -357       O  
ATOM   5619  ND2 ASN B 186       4.343  13.364 -62.600  1.00 40.71           N  
ANISOU 5619  ND2 ASN B 186     5399   5401   4667    711   -528   -356       N  
ATOM   5620  N   ILE B 187       0.989  16.383 -59.557  1.00 38.65           N  
ANISOU 5620  N   ILE B 187     5162   5000   4523    816   -606   -395       N  
ATOM   5621  CA  ILE B 187      -0.124  16.344 -58.615  1.00 37.58           C  
ANISOU 5621  CA  ILE B 187     4951   4882   4446    847   -633   -445       C  
ATOM   5622  C   ILE B 187      -1.232  17.369 -58.937  1.00 38.01           C  
ANISOU 5622  C   ILE B 187     5058   4916   4467    961   -691   -466       C  
ATOM   5623  O   ILE B 187      -2.398  17.141 -58.615  1.00 42.19           O  
ANISOU 5623  O   ILE B 187     5506   5493   5031   1015   -731   -526       O  
ATOM   5624  CB  ILE B 187       0.348  16.479 -57.154  1.00 34.14           C  
ANISOU 5624  CB  ILE B 187     4485   4426   4061    768   -580   -434       C  
ATOM   5625  CG1 ILE B 187      -0.580  15.678 -56.228  1.00 38.54           C  
ANISOU 5625  CG1 ILE B 187     4921   5036   4688    761   -592   -494       C  
ATOM   5626  CG2 ILE B 187       0.459  17.952 -56.762  1.00 33.83           C  
ANISOU 5626  CG2 ILE B 187     4549   4314   3992    786   -571   -402       C  
ATOM   5627  CD1 ILE B 187      -0.670  14.166 -56.545  1.00 31.03           C  
ANISOU 5627  CD1 ILE B 187     3883   4143   3765    729   -603   -526       C  
ATOM   5628  N   ALA B 188      -0.875  18.473 -59.587  1.00 34.62           N  
ANISOU 5628  N   ALA B 188     4767   4421   3967    997   -697   -419       N  
ATOM   5629  CA  ALA B 188      -1.872  19.451 -60.021  1.00 36.91           C  
ANISOU 5629  CA  ALA B 188     5131   4682   4211   1122   -762   -437       C  
ATOM   5630  C   ALA B 188      -2.939  18.816 -60.934  1.00 42.23           C  
ANISOU 5630  C   ALA B 188     5741   5427   4876   1216   -834   -495       C  
ATOM   5631  O   ALA B 188      -4.101  19.224 -60.918  1.00 44.05           O  
ANISOU 5631  O   ALA B 188     5954   5680   5104   1323   -896   -547       O  
ATOM   5632  CB  ALA B 188      -1.203  20.608 -60.722  1.00 36.89           C  
ANISOU 5632  CB  ALA B 188     5308   4588   4120   1133   -758   -370       C  
ATOM   5633  N   ALA B 189      -2.555  17.800 -61.709  1.00 37.82           N  
ANISOU 5633  N   ALA B 189     5145   4911   4314   1180   -829   -494       N  
ATOM   5634  CA  ALA B 189      -3.496  17.151 -62.609  1.00 38.99           C  
ANISOU 5634  CA  ALA B 189     5238   5126   4452   1258   -898   -550       C  
ATOM   5635  C   ALA B 189      -4.605  16.454 -61.843  1.00 41.52           C  
ANISOU 5635  C   ALA B 189     5404   5526   4847   1267   -924   -629       C  
ATOM   5636  O   ALA B 189      -5.633  16.138 -62.411  1.00 48.64           O  
ANISOU 5636  O   ALA B 189     6248   6489   5742   1343   -991   -689       O  
ATOM   5637  CB  ALA B 189      -2.783  16.146 -63.500  1.00 40.60           C  
ANISOU 5637  CB  ALA B 189     5434   5355   4637   1209   -883   -534       C  
ATOM   5638  N   PHE B 190      -4.394  16.196 -60.558  1.00 43.02           N  
ANISOU 5638  N   PHE B 190     5523   5720   5102   1182   -871   -632       N  
ATOM   5639  CA  PHE B 190      -5.398  15.527 -59.737  1.00 38.81           C  
ANISOU 5639  CA  PHE B 190     4846   5264   4635   1169   -883   -703       C  
ATOM   5640  C   PHE B 190      -6.113  16.542 -58.856  1.00 39.48           C  
ANISOU 5640  C   PHE B 190     4924   5346   4730   1229   -892   -729       C  
ATOM   5641  O   PHE B 190      -6.918  16.179 -58.009  1.00 40.41           O  
ANISOU 5641  O   PHE B 190     4925   5531   4898   1214   -890   -786       O  
ATOM   5642  CB  PHE B 190      -4.746  14.472 -58.841  1.00 37.61           C  
ANISOU 5642  CB  PHE B 190     4623   5122   4545   1036   -820   -694       C  
ATOM   5643  CG  PHE B 190      -4.019  13.389 -59.604  1.00 40.94           C  
ANISOU 5643  CG  PHE B 190     5048   5548   4959    982   -813   -677       C  
ATOM   5644  CD1 PHE B 190      -2.714  13.592 -60.074  1.00 36.40           C  
ANISOU 5644  CD1 PHE B 190     4568   4917   4345    952   -775   -611       C  
ATOM   5645  CD2 PHE B 190      -4.622  12.171 -59.836  1.00 38.20           C  
ANISOU 5645  CD2 PHE B 190     4610   5265   4640    958   -843   -731       C  
ATOM   5646  CE1 PHE B 190      -2.057  12.609 -60.784  1.00 35.00           C  
ANISOU 5646  CE1 PHE B 190     4392   4754   4155    917   -770   -603       C  
ATOM   5647  CE2 PHE B 190      -3.961  11.175 -60.551  1.00 39.55           C  
ANISOU 5647  CE2 PHE B 190     4795   5434   4799    920   -842   -721       C  
ATOM   5648  CZ  PHE B 190      -2.677  11.401 -61.024  1.00 37.06           C  
ANISOU 5648  CZ  PHE B 190     4571   5068   4443    907   -806   -658       C  
ATOM   5649  N   GLY B 191      -5.782  17.815 -59.020  1.00 42.27           N  
ANISOU 5649  N   GLY B 191     5410   5620   5031   1290   -897   -685       N  
ATOM   5650  CA  GLY B 191      -6.280  18.832 -58.103  1.00 41.18           C  
ANISOU 5650  CA  GLY B 191     5287   5461   4898   1344   -900   -703       C  
ATOM   5651  C   GLY B 191      -5.435  19.052 -56.853  1.00 45.31           C  
ANISOU 5651  C   GLY B 191     5826   5932   5457   1242   -824   -662       C  
ATOM   5652  O   GLY B 191      -5.844  19.787 -55.959  1.00 44.98           O  
ANISOU 5652  O   GLY B 191     5786   5879   5426   1278   -821   -683       O  
ATOM   5653  N   GLY B 192      -4.261  18.423 -56.772  1.00 40.78           N  
ANISOU 5653  N   GLY B 192     5262   5332   4901   1122   -765   -609       N  
ATOM   5654  CA  GLY B 192      -3.396  18.606 -55.619  1.00 32.59           C  
ANISOU 5654  CA  GLY B 192     4239   4249   3895   1025   -698   -572       C  
ATOM   5655  C   GLY B 192      -2.634  19.894 -55.786  1.00 39.34           C  
ANISOU 5655  C   GLY B 192     5253   5002   4693   1036   -687   -510       C  
ATOM   5656  O   GLY B 192      -2.452  20.334 -56.902  1.00 53.94           O  
ANISOU 5656  O   GLY B 192     7201   6814   6480   1083   -715   -481       O  
ATOM   5657  N   ASP B 193      -2.204  20.514 -54.695  1.00 42.81           N  
ANISOU 5657  N   ASP B 193     5725   5393   5149    990   -647   -491       N  
ATOM   5658  CA  ASP B 193      -1.428  21.751 -54.750  1.00 42.12           C  
ANISOU 5658  CA  ASP B 193     5796   5200   5008    979   -633   -432       C  
ATOM   5659  C   ASP B 193       0.033  21.427 -54.468  1.00 44.11           C  
ANISOU 5659  C   ASP B 193     6059   5430   5271    838   -563   -376       C  
ATOM   5660  O   ASP B 193       0.375  21.133 -53.338  1.00 46.92           O  
ANISOU 5660  O   ASP B 193     6354   5797   5677    766   -523   -381       O  
ATOM   5661  CB  ASP B 193      -1.953  22.702 -53.680  1.00 48.72           C  
ANISOU 5661  CB  ASP B 193     6662   5998   5852   1026   -641   -457       C  
ATOM   5662  CG  ASP B 193      -1.162  24.027 -53.584  1.00 47.59           C  
ANISOU 5662  CG  ASP B 193     6696   5732   5653   1004   -628   -398       C  
ATOM   5663  OD1 ASP B 193      -0.238  24.266 -54.380  1.00 41.95           O  
ANISOU 5663  OD1 ASP B 193     6081   4967   4891    948   -611   -338       O  
ATOM   5664  OD2 ASP B 193      -1.496  24.845 -52.691  1.00 48.41           O  
ANISOU 5664  OD2 ASP B 193     6841   5794   5760   1040   -635   -417       O  
ATOM   5665  N   PRO B 194       0.909  21.482 -55.493  1.00 43.40           N  
ANISOU 5665  N   PRO B 194     6046   5314   5128    800   -550   -324       N  
ATOM   5666  CA  PRO B 194       2.303  21.085 -55.221  1.00 40.30           C  
ANISOU 5666  CA  PRO B 194     5640   4925   4747    669   -483   -282       C  
ATOM   5667  C   PRO B 194       2.992  22.090 -54.296  1.00 42.08           C  
ANISOU 5667  C   PRO B 194     5945   5078   4966    602   -447   -249       C  
ATOM   5668  O   PRO B 194       4.078  21.830 -53.767  1.00 41.20           O  
ANISOU 5668  O   PRO B 194     5805   4976   4872    494   -394   -226       O  
ATOM   5669  CB  PRO B 194       2.979  21.108 -56.604  1.00 38.67           C  
ANISOU 5669  CB  PRO B 194     5508   4712   4471    655   -478   -239       C  
ATOM   5670  CG  PRO B 194       1.904  21.544 -57.602  1.00 42.13           C  
ANISOU 5670  CG  PRO B 194     6013   5133   4861    783   -547   -255       C  
ATOM   5671  CD  PRO B 194       0.728  22.066 -56.838  1.00 37.76           C  
ANISOU 5671  CD  PRO B 194     5448   4563   4335    873   -591   -301       C  
ATOM   5672  N   MET B 195       2.361  23.240 -54.096  1.00 43.16           N  
ANISOU 5672  N   MET B 195     6182   5142   5073    671   -481   -252       N  
ATOM   5673  CA  MET B 195       2.909  24.217 -53.154  1.00 48.28           C  
ANISOU 5673  CA  MET B 195     6913   5714   5715    612   -454   -228       C  
ATOM   5674  C   MET B 195       2.472  23.987 -51.705  1.00 42.37           C  
ANISOU 5674  C   MET B 195     6070   4992   5036    612   -445   -273       C  
ATOM   5675  O   MET B 195       2.857  24.736 -50.812  1.00 45.23           O  
ANISOU 5675  O   MET B 195     6490   5296   5398    568   -426   -261       O  
ATOM   5676  CB  MET B 195       2.614  25.658 -53.599  1.00 43.61           C  
ANISOU 5676  CB  MET B 195     6508   5014   5049    677   -492   -203       C  
ATOM   5677  CG  MET B 195       3.405  26.079 -54.812  1.00 39.41           C  
ANISOU 5677  CG  MET B 195     6102   4436   4436    629   -481   -141       C  
ATOM   5678  SD  MET B 195       3.119  27.819 -55.184  1.00 67.90           S  
ANISOU 5678  SD  MET B 195     9960   7892   7949    692   -527   -107       S  
ATOM   5679  CE  MET B 195       1.378  27.798 -55.600  1.00108.73           C  
ANISOU 5679  CE  MET B 195    15111  13085  13117    906   -622   -173       C  
ATOM   5680  N   SER B 196       1.674  22.955 -51.467  1.00 38.69           N  
ANISOU 5680  N   SER B 196     5463   4612   4624    653   -458   -325       N  
ATOM   5681  CA  SER B 196       1.425  22.543 -50.087  1.00 37.73           C  
ANISOU 5681  CA  SER B 196     5244   4528   4566    626   -436   -362       C  
ATOM   5682  C   SER B 196       1.487  21.037 -49.898  1.00 40.21           C  
ANISOU 5682  C   SER B 196     5412   4932   4934    575   -414   -383       C  
ATOM   5683  O   SER B 196       0.464  20.324 -50.010  1.00 35.44           O  
ANISOU 5683  O   SER B 196     4716   4394   4357    631   -441   -432       O  
ATOM   5684  CB  SER B 196       0.107  23.088 -49.550  1.00 40.32           C  
ANISOU 5684  CB  SER B 196     5563   4858   4899    736   -475   -417       C  
ATOM   5685  OG  SER B 196      -0.100  22.610 -48.235  1.00 42.85           O  
ANISOU 5685  OG  SER B 196     5785   5222   5275    698   -446   -451       O  
ATOM   5686  N   VAL B 197       2.688  20.559 -49.581  1.00 31.81           N  
ANISOU 5686  N   VAL B 197     4330   3872   3885    469   -369   -351       N  
ATOM   5687  CA  VAL B 197       2.909  19.119 -49.469  1.00 26.87           C  
ANISOU 5687  CA  VAL B 197     3592   3318   3301    423   -354   -367       C  
ATOM   5688  C   VAL B 197       3.461  18.808 -48.101  1.00 30.84           C  
ANISOU 5688  C   VAL B 197     4051   3825   3842    346   -317   -369       C  
ATOM   5689  O   VAL B 197       4.443  19.414 -47.673  1.00 33.16           O  
ANISOU 5689  O   VAL B 197     4398   4078   4122    285   -289   -337       O  
ATOM   5690  CB  VAL B 197       3.903  18.589 -50.558  1.00 35.77           C  
ANISOU 5690  CB  VAL B 197     4729   4463   4401    384   -342   -333       C  
ATOM   5691  CG1 VAL B 197       4.317  17.134 -50.267  1.00 31.61           C  
ANISOU 5691  CG1 VAL B 197     4100   3996   3913    334   -327   -349       C  
ATOM   5692  CG2 VAL B 197       3.292  18.717 -51.955  1.00 32.26           C  
ANISOU 5692  CG2 VAL B 197     4320   4021   3914    463   -382   -334       C  
ATOM   5693  N   THR B 198       2.834  17.862 -47.422  1.00 27.15           N  
ANISOU 5693  N   THR B 198     3491   3407   3419    343   -317   -407       N  
ATOM   5694  CA  THR B 198       3.224  17.468 -46.095  1.00 23.62           C  
ANISOU 5694  CA  THR B 198     3006   2965   3004    278   -287   -412       C  
ATOM   5695  C   THR B 198       3.571  16.008 -46.179  1.00 33.78           C  
ANISOU 5695  C   THR B 198     4222   4298   4314    236   -282   -418       C  
ATOM   5696  O   THR B 198       2.743  15.211 -46.613  1.00 35.33           O  
ANISOU 5696  O   THR B 198     4366   4535   4523    265   -304   -448       O  
ATOM   5697  CB  THR B 198       2.016  17.617 -45.135  1.00 27.22           C  
ANISOU 5697  CB  THR B 198     3422   3438   3483    313   -290   -457       C  
ATOM   5698  OG1 THR B 198       1.618  18.992 -45.100  1.00 33.04           O  
ANISOU 5698  OG1 THR B 198     4232   4129   4194    372   -303   -459       O  
ATOM   5699  CG2 THR B 198       2.339  17.176 -43.706  1.00 20.39           C  
ANISOU 5699  CG2 THR B 198     2523   2579   2646    245   -258   -463       C  
ATOM   5700  N   LEU B 199       4.785  15.654 -45.766  1.00 27.10           N  
ANISOU 5700  N   LEU B 199     3378   3448   3469    171   -259   -395       N  
ATOM   5701  CA  LEU B 199       5.163  14.257 -45.618  1.00 28.49           C  
ANISOU 5701  CA  LEU B 199     3502   3660   3665    138   -259   -404       C  
ATOM   5702  C   LEU B 199       4.676  13.759 -44.272  1.00 31.02           C  
ANISOU 5702  C   LEU B 199     3787   3984   4016    108   -249   -428       C  
ATOM   5703  O   LEU B 199       4.786  14.463 -43.286  1.00 33.40           O  
ANISOU 5703  O   LEU B 199     4110   4262   4320     88   -230   -424       O  
ATOM   5704  CB  LEU B 199       6.685  14.121 -45.680  1.00 27.82           C  
ANISOU 5704  CB  LEU B 199     3430   3577   3564     92   -242   -377       C  
ATOM   5705  CG  LEU B 199       7.320  14.847 -46.856  1.00 28.82           C  
ANISOU 5705  CG  LEU B 199     3600   3701   3651    101   -238   -349       C  
ATOM   5706  CD1 LEU B 199       8.847  14.641 -46.798  1.00 31.37           C  
ANISOU 5706  CD1 LEU B 199     3914   4048   3956     47   -216   -331       C  
ATOM   5707  CD2 LEU B 199       6.708  14.304 -48.170  1.00 25.36           C  
ANISOU 5707  CD2 LEU B 199     3150   3286   3199    157   -265   -359       C  
ATOM   5708  N   PHE B 200       4.065  12.587 -44.213  1.00 29.68           N  
ANISOU 5708  N   PHE B 200     3571   3842   3863    101   -261   -453       N  
ATOM   5709  CA  PHE B 200       3.955  11.960 -42.902  1.00 27.61           C  
ANISOU 5709  CA  PHE B 200     3292   3580   3619     52   -246   -465       C  
ATOM   5710  C   PHE B 200       4.401  10.495 -43.003  1.00 32.81           C  
ANISOU 5710  C   PHE B 200     3941   4245   4280     24   -261   -468       C  
ATOM   5711  O   PHE B 200       4.340   9.908 -44.079  1.00 32.50           O  
ANISOU 5711  O   PHE B 200     3893   4221   4235     48   -285   -473       O  
ATOM   5712  CB  PHE B 200       2.591  12.198 -42.209  1.00 24.86           C  
ANISOU 5712  CB  PHE B 200     2911   3250   3284     57   -237   -498       C  
ATOM   5713  CG  PHE B 200       1.357  11.570 -42.909  1.00 33.26           C  
ANISOU 5713  CG  PHE B 200     3923   4358   4356     78   -258   -533       C  
ATOM   5714  CD1 PHE B 200       1.174  11.652 -44.282  1.00 31.71           C  
ANISOU 5714  CD1 PHE B 200     3724   4174   4151    131   -288   -536       C  
ATOM   5715  CD2 PHE B 200       0.364  10.951 -42.144  1.00 29.92           C  
ANISOU 5715  CD2 PHE B 200     3454   3969   3946     39   -246   -567       C  
ATOM   5716  CE1 PHE B 200       0.044  11.112 -44.888  1.00 35.10           C  
ANISOU 5716  CE1 PHE B 200     4101   4649   4586    149   -312   -573       C  
ATOM   5717  CE2 PHE B 200      -0.764  10.405 -42.723  1.00 31.04           C  
ANISOU 5717  CE2 PHE B 200     3540   4162   4094     46   -264   -605       C  
ATOM   5718  CZ  PHE B 200      -0.941  10.475 -44.103  1.00 35.37           C  
ANISOU 5718  CZ  PHE B 200     4081   4722   4636    103   -300   -610       C  
ATOM   5719  N   GLY B 201       4.895   9.945 -41.902  1.00 29.55           N  
ANISOU 5719  N   GLY B 201     3540   3817   3870    -21   -251   -464       N  
ATOM   5720  CA  GLY B 201       5.332   8.555 -41.871  1.00 38.62           C  
ANISOU 5720  CA  GLY B 201     4700   4961   5014    -41   -272   -467       C  
ATOM   5721  C   GLY B 201       5.443   8.061 -40.445  1.00 37.95           C  
ANISOU 5721  C   GLY B 201     4637   4854   4928    -90   -261   -467       C  
ATOM   5722  O   GLY B 201       5.473   8.851 -39.527  1.00 44.29           O  
ANISOU 5722  O   GLY B 201     5444   5650   5733   -107   -236   -461       O  
ATOM   5723  N   GLU B 202       5.461   6.758 -40.258  1.00 32.79           N  
ANISOU 5723  N   GLU B 202     4007   4184   4267   -113   -281   -475       N  
ATOM   5724  CA  GLU B 202       5.489   6.171 -38.925  1.00 33.18           C  
ANISOU 5724  CA  GLU B 202     4095   4206   4307   -163   -274   -473       C  
ATOM   5725  C   GLU B 202       6.681   5.217 -38.839  1.00 31.32           C  
ANISOU 5725  C   GLU B 202     3908   3943   4049   -147   -309   -465       C  
ATOM   5726  O   GLU B 202       6.999   4.555 -39.813  1.00 31.36           O  
ANISOU 5726  O   GLU B 202     3918   3949   4047   -113   -340   -472       O  
ATOM   5727  CB  GLU B 202       4.176   5.438 -38.616  1.00 26.29           C  
ANISOU 5727  CB  GLU B 202     3220   3333   3436   -218   -266   -492       C  
ATOM   5728  CG  GLU B 202       4.052   4.941 -37.187  1.00 28.47           C  
ANISOU 5728  CG  GLU B 202     3541   3581   3694   -281   -249   -487       C  
ATOM   5729  CD  GLU B 202       4.529   3.498 -37.037  1.00 40.73           C  
ANISOU 5729  CD  GLU B 202     5172   5084   5220   -302   -286   -482       C  
ATOM   5730  OE1 GLU B 202       4.774   2.854 -38.084  1.00 41.44           O  
ANISOU 5730  OE1 GLU B 202     5269   5165   5309   -269   -322   -488       O  
ATOM   5731  OE2 GLU B 202       4.653   3.007 -35.883  1.00 41.21           O  
ANISOU 5731  OE2 GLU B 202     5293   5109   5256   -347   -281   -472       O  
HETATM 5732  N   SGB B 203       7.344   5.182 -37.684  1.00 30.97           N  
ANISOU 5732  N   SGB B 203     3900   3878   3990   -164   -306   -456       N  
HETATM 5733  CA  SGB B 203       8.520   4.341 -37.458  1.00 31.37           C  
ANISOU 5733  CA  SGB B 203     3998   3907   4014   -136   -345   -454       C  
HETATM 5734  C   SGB B 203       9.603   4.606 -38.489  1.00 33.48           C  
ANISOU 5734  C   SGB B 203     4230   4212   4279    -73   -363   -457       C  
HETATM 5735  O   SGB B 203      10.012   5.731 -38.630  1.00 35.09           O  
ANISOU 5735  O   SGB B 203     4391   4449   4493    -68   -340   -449       O  
HETATM 5736  CB  SGB B 203       8.075   2.887 -37.451  1.00 26.46           C  
ANISOU 5736  CB  SGB B 203     3440   3241   3373   -153   -377   -463       C  
HETATM 5737  OG  SGB B 203       9.013   2.162 -36.711  1.00 34.59           O  
ANISOU 5737  OG  SGB B 203     4537   4236   4370   -134   -412   -460       O  
HETATM 5738  O1  SGB B 203       9.654   0.733 -38.753  1.00 35.57           O  
ANISOU 5738  O1  SGB B 203     4680   4359   4475    -35   -487   -489       O  
HETATM 5739  P1  SGB B 203       9.678   0.739 -37.250  1.00 47.65           P  
ANISOU 5739  P1  SGB B 203     6260   5854   5991    -78   -477   -475       P  
HETATM 5740  C1  SGB B 203      11.112   0.653 -36.760  1.00 45.10           C  
ANISOU 5740  C1  SGB B 203     5955   5540   5640    -15   -511   -480       C  
HETATM 5741  O2  SGB B 203       8.682  -0.483 -36.736  1.00 52.74           O  
ANISOU 5741  O2  SGB B 203     7005   6422   6612   -146   -491   -472       O  
HETATM 5742  C2  SGB B 203       8.506  -1.779 -37.335  1.00 49.01           C  
ANISOU 5742  C2  SGB B 203     6608   5897   6116   -137   -538   -485       C  
HETATM 5743  C4  SGB B 203       9.801  -2.587 -37.392  1.00 49.86           C  
ANISOU 5743  C4  SGB B 203     6785   5977   6184    -43   -604   -498       C  
HETATM 5744  C3  SGB B 203       7.552  -2.562 -36.452  1.00 44.31           C  
ANISOU 5744  C3  SGB B 203     6106   5235   5497   -236   -531   -475       C  
ATOM   5745  N   ALA B 204      10.061   3.586 -39.217  1.00 32.30           N  
ANISOU 5745  N   ALA B 204     4102   4059   4112    -29   -404   -470       N  
ATOM   5746  CA  ALA B 204      11.016   3.839 -40.296  1.00 32.55           C  
ANISOU 5746  CA  ALA B 204     4090   4141   4136     29   -414   -478       C  
ATOM   5747  C   ALA B 204      10.484   4.864 -41.329  1.00 33.81           C  
ANISOU 5747  C   ALA B 204     4194   4334   4316     25   -381   -469       C  
ATOM   5748  O   ALA B 204      11.261   5.624 -41.909  1.00 29.35           O  
ANISOU 5748  O   ALA B 204     3591   3815   3746     45   -368   -464       O  
ATOM   5749  CB  ALA B 204      11.480   2.536 -40.973  1.00 31.74           C  
ANISOU 5749  CB  ALA B 204     4022   4031   4007     87   -465   -499       C  
ATOM   5750  N   GLY B 205       9.167   4.926 -41.527  1.00 26.76           N  
ANISOU 5750  N   GLY B 205     3301   3424   3444     -3   -369   -469       N  
ATOM   5751  CA  GLY B 205       8.609   5.977 -42.374  1.00 26.57           C  
ANISOU 5751  CA  GLY B 205     3235   3426   3435      2   -344   -462       C  
ATOM   5752  C   GLY B 205       8.880   7.370 -41.776  1.00 27.30           C  
ANISOU 5752  C   GLY B 205     3312   3527   3535    -18   -308   -444       C  
ATOM   5753  O   GLY B 205       9.142   8.344 -42.503  1.00 33.34           O  
ANISOU 5753  O   GLY B 205     4057   4314   4296     -4   -292   -433       O  
ATOM   5754  N   ALA B 206       8.818   7.491 -40.449  1.00 28.42           N  
ANISOU 5754  N   ALA B 206     3471   3647   3682    -55   -295   -441       N  
ATOM   5755  CA  ALA B 206       9.120   8.787 -39.795  1.00 23.93           C  
ANISOU 5755  CA  ALA B 206     2897   3079   3117    -76   -266   -428       C  
ATOM   5756  C   ALA B 206      10.602   9.103 -39.904  1.00 31.90           C  
ANISOU 5756  C   ALA B 206     3897   4115   4108    -68   -270   -421       C  
ATOM   5757  O   ALA B 206      10.980  10.248 -40.120  1.00 34.62           O  
ANISOU 5757  O   ALA B 206     4232   4472   4450    -80   -248   -408       O  
ATOM   5758  CB  ALA B 206       8.699   8.763 -38.338  1.00 23.89           C  
ANISOU 5758  CB  ALA B 206     2916   3047   3116   -115   -253   -430       C  
ATOM   5759  N   ALA B 207      11.455   8.095 -39.736  1.00 26.03           N  
ANISOU 5759  N   ALA B 207     3158   3383   3348    -49   -299   -432       N  
ATOM   5760  CA  ALA B 207      12.905   8.343 -39.854  1.00 27.98           C  
ANISOU 5760  CA  ALA B 207     3378   3677   3574    -38   -304   -436       C  
ATOM   5761  C   ALA B 207      13.210   8.787 -41.274  1.00 34.08           C  
ANISOU 5761  C   ALA B 207     4118   4492   4338    -21   -291   -431       C  
ATOM   5762  O   ALA B 207      14.111   9.623 -41.488  1.00 26.24           O  
ANISOU 5762  O   ALA B 207     3099   3540   3331    -41   -272   -425       O  
ATOM   5763  CB  ALA B 207      13.715   7.082 -39.507  1.00 23.32           C  
ANISOU 5763  CB  ALA B 207     2800   3099   2963      0   -346   -457       C  
ATOM   5764  N   SER B 208      12.435   8.253 -42.245  1.00 25.45           N  
ANISOU 5764  N   SER B 208     3030   3390   3248     10   -301   -434       N  
ATOM   5765  CA  SER B 208      12.584   8.671 -43.665  1.00 27.25           C  
ANISOU 5765  CA  SER B 208     3237   3655   3462     30   -290   -428       C  
ATOM   5766  C   SER B 208      12.194  10.128 -43.835  1.00 29.09           C  
ANISOU 5766  C   SER B 208     3479   3874   3700     -5   -255   -403       C  
ATOM   5767  O   SER B 208      12.922  10.929 -44.426  1.00 29.52           O  
ANISOU 5767  O   SER B 208     3523   3960   3732    -21   -233   -390       O  
ATOM   5768  CB  SER B 208      11.763   7.794 -44.628  1.00 25.56           C  
ANISOU 5768  CB  SER B 208     3032   3431   3249     72   -314   -439       C  
ATOM   5769  OG  SER B 208      12.154   6.419 -44.551  1.00 30.55           O  
ANISOU 5769  OG  SER B 208     3673   4064   3869    108   -352   -464       O  
ATOM   5770  N   VAL B 209      11.026  10.484 -43.334  1.00 29.97           N  
ANISOU 5770  N   VAL B 209     3613   3938   3836    -15   -250   -398       N  
ATOM   5771  CA  VAL B 209      10.628  11.914 -43.313  1.00 28.49           C  
ANISOU 5771  CA  VAL B 209     3448   3726   3650    -37   -224   -379       C  
ATOM   5772  C   VAL B 209      11.760  12.789 -42.742  1.00 27.34           C  
ANISOU 5772  C   VAL B 209     3308   3590   3490    -85   -203   -366       C  
ATOM   5773  O   VAL B 209      12.156  13.776 -43.362  1.00 33.95           O  
ANISOU 5773  O   VAL B 209     4163   4431   4307   -106   -183   -347       O  
ATOM   5774  CB  VAL B 209       9.333  12.094 -42.521  1.00 24.36           C  
ANISOU 5774  CB  VAL B 209     2940   3164   3153    -37   -223   -387       C  
ATOM   5775  CG1 VAL B 209       8.971  13.598 -42.352  1.00 26.78           C  
ANISOU 5775  CG1 VAL B 209     3280   3439   3456    -46   -202   -373       C  
ATOM   5776  CG2 VAL B 209       8.181  11.331 -43.268  1.00 25.66           C  
ANISOU 5776  CG2 VAL B 209     3089   3332   3327      1   -243   -403       C  
ATOM   5777  N   GLY B 210      12.314  12.396 -41.596  1.00 26.76           N  
ANISOU 5777  N   GLY B 210     3224   3520   3423   -106   -209   -377       N  
ATOM   5778  CA  GLY B 210      13.422  13.134 -40.985  1.00 32.58           C  
ANISOU 5778  CA  GLY B 210     3958   4275   4147   -155   -195   -373       C  
ATOM   5779  C   GLY B 210      14.638  13.239 -41.888  1.00 31.13           C  
ANISOU 5779  C   GLY B 210     3739   4156   3933   -169   -185   -372       C  
ATOM   5780  O   GLY B 210      15.286  14.275 -42.010  1.00 34.50           O  
ANISOU 5780  O   GLY B 210     4173   4595   4341   -223   -161   -359       O  
ATOM   5781  N   MET B 211      14.934  12.158 -42.579  1.00 30.12           N  
ANISOU 5781  N   MET B 211     3576   4072   3795   -123   -204   -388       N  
ATOM   5782  CA  MET B 211      16.005  12.214 -43.533  1.00 33.09           C  
ANISOU 5782  CA  MET B 211     3912   4524   4137   -129   -191   -392       C  
ATOM   5783  C   MET B 211      15.734  13.152 -44.713  1.00 38.43           C  
ANISOU 5783  C   MET B 211     4615   5193   4792   -150   -161   -364       C  
ATOM   5784  O   MET B 211      16.654  13.821 -45.165  1.00 38.16           O  
ANISOU 5784  O   MET B 211     4566   5208   4726   -200   -132   -355       O  
ATOM   5785  CB  MET B 211      16.426  10.809 -43.923  1.00 33.03           C  
ANISOU 5785  CB  MET B 211     3866   4567   4119    -63   -222   -422       C  
ATOM   5786  CG  MET B 211      17.415  10.262 -42.839  1.00 39.92           C  
ANISOU 5786  CG  MET B 211     4704   5477   4988    -58   -246   -451       C  
ATOM   5787  SD  MET B 211      17.352   8.498 -42.888  1.00 55.98           S  
ANISOU 5787  SD  MET B 211     6740   7512   7017     36   -300   -484       S  
ATOM   5788  CE  MET B 211      17.661   8.071 -41.193  1.00 41.37           C  
ANISOU 5788  CE  MET B 211     4909   5635   5176     36   -333   -500       C  
ATOM   5789  N   HIS B 212      14.491  13.248 -45.190  1.00 34.34           N  
ANISOU 5789  N   HIS B 212     4141   4619   4288   -117   -167   -350       N  
ATOM   5790  CA  HIS B 212      14.218  14.247 -46.213  1.00 31.14           C  
ANISOU 5790  CA  HIS B 212     3779   4197   3857   -132   -145   -321       C  
ATOM   5791  C   HIS B 212      14.390  15.674 -45.659  1.00 37.50           C  
ANISOU 5791  C   HIS B 212     4635   4959   4654   -202   -120   -297       C  
ATOM   5792  O   HIS B 212      14.840  16.560 -46.375  1.00 33.15           O  
ANISOU 5792  O   HIS B 212     4118   4412   4065   -247    -94   -273       O  
ATOM   5793  CB  HIS B 212      12.861  14.045 -46.900  1.00 27.17           C  
ANISOU 5793  CB  HIS B 212     3307   3651   3365    -71   -165   -318       C  
ATOM   5794  CG  HIS B 212      12.774  12.756 -47.646  1.00 30.56           C  
ANISOU 5794  CG  HIS B 212     3700   4120   3793    -13   -189   -340       C  
ATOM   5795  ND1 HIS B 212      13.460  12.531 -48.830  1.00 27.99           N  
ANISOU 5795  ND1 HIS B 212     3357   3852   3427      0   -180   -340       N  
ATOM   5796  CD2 HIS B 212      12.134  11.604 -47.358  1.00 28.00           C  
ANISOU 5796  CD2 HIS B 212     3357   3786   3497     30   -221   -365       C  
ATOM   5797  CE1 HIS B 212      13.217  11.303 -49.239  1.00 32.21           C  
ANISOU 5797  CE1 HIS B 212     3866   4406   3967     58   -210   -366       C  
ATOM   5798  NE2 HIS B 212      12.420  10.713 -48.362  1.00 32.17           N  
ANISOU 5798  NE2 HIS B 212     3864   4357   4003     74   -237   -380       N  
ATOM   5799  N   ILE B 213      14.038  15.883 -44.392  1.00 33.05           N  
ANISOU 5799  N   ILE B 213     4084   4350   4121   -214   -128   -304       N  
ATOM   5800  CA  ILE B 213      14.327  17.150 -43.751  1.00 36.54           C  
ANISOU 5800  CA  ILE B 213     4576   4752   4554   -280   -109   -289       C  
ATOM   5801  C   ILE B 213      15.836  17.468 -43.746  1.00 41.99           C  
ANISOU 5801  C   ILE B 213     5234   5506   5214   -361    -86   -289       C  
ATOM   5802  O   ILE B 213      16.243  18.622 -43.954  1.00 38.89           O  
ANISOU 5802  O   ILE B 213     4893   5092   4791   -432    -61   -266       O  
ATOM   5803  CB  ILE B 213      13.786  17.160 -42.301  1.00 36.18           C  
ANISOU 5803  CB  ILE B 213     4541   4661   4544   -275   -123   -304       C  
ATOM   5804  CG1 ILE B 213      12.239  17.212 -42.329  1.00 31.70           C  
ANISOU 5804  CG1 ILE B 213     4009   4036   3998   -211   -137   -305       C  
ATOM   5805  CG2 ILE B 213      14.399  18.340 -41.535  1.00 28.90           C  
ANISOU 5805  CG2 ILE B 213     3662   3711   3609   -351   -108   -295       C  
ATOM   5806  CD1 ILE B 213      11.579  17.012 -40.997  1.00 32.10           C  
ANISOU 5806  CD1 ILE B 213     4058   4059   4080   -199   -146   -324       C  
ATOM   5807  N   LEU B 214      16.663  16.442 -43.529  1.00 36.76           N  
ANISOU 5807  N   LEU B 214     4489   4924   4556   -349    -95   -317       N  
ATOM   5808  CA  LEU B 214      18.101  16.639 -43.378  1.00 33.89           C  
ANISOU 5808  CA  LEU B 214     4071   4640   4164   -419    -77   -330       C  
ATOM   5809  C   LEU B 214      18.896  16.537 -44.683  1.00 41.85           C  
ANISOU 5809  C   LEU B 214     5038   5735   5128   -437    -51   -328       C  
ATOM   5810  O   LEU B 214      20.128  16.638 -44.677  1.00 39.52           O  
ANISOU 5810  O   LEU B 214     4680   5531   4804   -495    -32   -346       O  
ATOM   5811  CB  LEU B 214      18.677  15.671 -42.340  1.00 26.87           C  
ANISOU 5811  CB  LEU B 214     3114   3800   3294   -391   -107   -369       C  
ATOM   5812  CG  LEU B 214      17.984  15.794 -40.984  1.00 32.49           C  
ANISOU 5812  CG  LEU B 214     3869   4434   4041   -384   -128   -370       C  
ATOM   5813  CD1 LEU B 214      18.544  14.807 -39.996  1.00 31.49           C  
ANISOU 5813  CD1 LEU B 214     3691   4349   3924   -353   -161   -405       C  
ATOM   5814  CD2 LEU B 214      18.103  17.228 -40.426  1.00 35.01           C  
ANISOU 5814  CD2 LEU B 214     4244   4705   4353   -470   -107   -353       C  
ATOM   5815  N   SER B 215      18.207  16.348 -45.801  1.00 41.47           N  
ANISOU 5815  N   SER B 215     5020   5668   5069   -388    -49   -311       N  
ATOM   5816  CA  SER B 215      18.904  16.255 -47.074  1.00 37.08           C  
ANISOU 5816  CA  SER B 215     4431   5194   4464   -402    -21   -309       C  
ATOM   5817  C   SER B 215      18.446  17.335 -48.061  1.00 41.97           C  
ANISOU 5817  C   SER B 215     5143   5758   5047   -441      8   -263       C  
ATOM   5818  O   SER B 215      17.283  17.404 -48.473  1.00 39.33           O  
ANISOU 5818  O   SER B 215     4874   5346   4723   -382    -11   -245       O  
ATOM   5819  CB  SER B 215      18.755  14.857 -47.665  1.00 36.79           C  
ANISOU 5819  CB  SER B 215     4340   5206   4432   -300    -47   -337       C  
ATOM   5820  OG  SER B 215      19.431  14.765 -48.917  1.00 38.72           O  
ANISOU 5820  OG  SER B 215     4552   5537   4624   -308    -18   -339       O  
ATOM   5821  N   LEU B 216      19.377  18.196 -48.439  1.00 46.02           N  
ANISOU 5821  N   LEU B 216     5664   6313   5509   -545     52   -247       N  
ATOM   5822  CA  LEU B 216      19.017  19.384 -49.191  1.00 46.29           C  
ANISOU 5822  CA  LEU B 216     5813   6276   5501   -599     77   -199       C  
ATOM   5823  C   LEU B 216      18.158  19.113 -50.427  1.00 40.91           C  
ANISOU 5823  C   LEU B 216     5178   5566   4798   -518     68   -180       C  
ATOM   5824  O   LEU B 216      17.117  19.701 -50.599  1.00 40.29           O  
ANISOU 5824  O   LEU B 216     5201   5386   4723   -485     49   -153       O  
ATOM   5825  CB  LEU B 216      20.261  20.155 -49.585  1.00 56.77           C  
ANISOU 5825  CB  LEU B 216     7133   7672   6765   -733    132   -187       C  
ATOM   5826  CG  LEU B 216      20.109  21.625 -49.216  1.00 68.77           C  
ANISOU 5826  CG  LEU B 216     8780   9086   8266   -831    145   -148       C  
ATOM   5827  CD1 LEU B 216      20.352  21.782 -47.696  1.00 68.30           C  
ANISOU 5827  CD1 LEU B 216     8690   9007   8253   -864    125   -173       C  
ATOM   5828  CD2 LEU B 216      21.057  22.502 -50.062  1.00 64.18           C  
ANISOU 5828  CD2 LEU B 216     8237   8547   7601   -971    205   -119       C  
ATOM   5829  N   PRO B 217      18.603  18.235 -51.314  1.00 40.02           N  
ANISOU 5829  N   PRO B 217     4995   5551   4661   -482     77   -199       N  
ATOM   5830  CA  PRO B 217      17.744  18.070 -52.494  1.00 44.20           C  
ANISOU 5830  CA  PRO B 217     5581   6046   5166   -408     65   -180       C  
ATOM   5831  C   PRO B 217      16.281  17.675 -52.201  1.00 45.47           C  
ANISOU 5831  C   PRO B 217     5776   6117   5383   -301      9   -186       C  
ATOM   5832  O   PRO B 217      15.442  17.891 -53.059  1.00 46.48           O  
ANISOU 5832  O   PRO B 217     5974   6197   5491   -252     -6   -166       O  
ATOM   5833  CB  PRO B 217      18.466  16.969 -53.297  1.00 38.67           C  
ANISOU 5833  CB  PRO B 217     4783   5471   4439   -370     76   -212       C  
ATOM   5834  CG  PRO B 217      19.903  17.058 -52.805  1.00 28.87           C  
ANISOU 5834  CG  PRO B 217     3454   4336   3179   -461    115   -234       C  
ATOM   5835  CD  PRO B 217      19.786  17.358 -51.353  1.00 29.36           C  
ANISOU 5835  CD  PRO B 217     3517   4339   3298   -488     94   -241       C  
ATOM   5836  N   SER B 218      15.964  17.120 -51.035  1.00 43.84           N  
ANISOU 5836  N   SER B 218     5524   5893   5241   -269    -21   -213       N  
ATOM   5837  CA  SER B 218      14.561  16.818 -50.750  1.00 37.31           C  
ANISOU 5837  CA  SER B 218     4726   4990   4461   -184    -66   -220       C  
ATOM   5838  C   SER B 218      13.769  18.044 -50.340  1.00 39.08           C  
ANISOU 5838  C   SER B 218     5048   5113   4689   -198    -72   -194       C  
ATOM   5839  O   SER B 218      12.552  18.058 -50.457  1.00 37.31           O  
ANISOU 5839  O   SER B 218     4860   4834   4484   -127   -104   -196       O  
ATOM   5840  CB  SER B 218      14.435  15.764 -49.664  1.00 35.99           C  
ANISOU 5840  CB  SER B 218     4485   4838   4352   -148    -94   -258       C  
ATOM   5841  OG  SER B 218      14.789  14.483 -50.151  1.00 38.04           O  
ANISOU 5841  OG  SER B 218     4676   5168   4609    -99   -107   -287       O  
ATOM   5842  N   ARG B 219      14.459  19.076 -49.857  1.00 44.14           N  
ANISOU 5842  N   ARG B 219     5732   5732   5310   -289    -43   -173       N  
ATOM   5843  CA  ARG B 219      13.796  20.198 -49.182  1.00 44.88           C  
ANISOU 5843  CA  ARG B 219     5918   5722   5410   -300    -53   -156       C  
ATOM   5844  C   ARG B 219      12.905  21.038 -50.076  1.00 40.28           C  
ANISOU 5844  C   ARG B 219     5451   5062   4790   -257    -69   -127       C  
ATOM   5845  O   ARG B 219      11.971  21.658 -49.599  1.00 43.29           O  
ANISOU 5845  O   ARG B 219     5898   5362   5186   -214    -95   -128       O  
ATOM   5846  CB  ARG B 219      14.811  21.074 -48.445  1.00 45.17           C  
ANISOU 5846  CB  ARG B 219     5980   5751   5431   -415    -23   -144       C  
ATOM   5847  CG  ARG B 219      15.408  20.364 -47.232  1.00 45.49           C  
ANISOU 5847  CG  ARG B 219     5918   5847   5517   -436    -25   -180       C  
ATOM   5848  CD  ARG B 219      14.338  20.037 -46.224  1.00 50.65           C  
ANISOU 5848  CD  ARG B 219     6567   6448   6228   -363    -60   -202       C  
ATOM   5849  NE  ARG B 219      13.697  21.232 -45.685  1.00 53.19           N  
ANISOU 5849  NE  ARG B 219     6992   6670   6547   -371    -68   -187       N  
ATOM   5850  CZ  ARG B 219      14.158  21.905 -44.629  1.00 63.05           C  
ANISOU 5850  CZ  ARG B 219     8267   7889   7801   -438    -60   -190       C  
ATOM   5851  NH1 ARG B 219      15.270  21.492 -44.015  1.00 60.31           N  
ANISOU 5851  NH1 ARG B 219     7842   7611   7461   -503    -46   -207       N  
ATOM   5852  NH2 ARG B 219      13.530  22.997 -44.188  1.00 63.86           N  
ANISOU 5852  NH2 ARG B 219     8474   7895   7897   -434    -72   -180       N  
ATOM   5853  N   SER B 220      13.178  21.039 -51.370  1.00 38.33           N  
ANISOU 5853  N   SER B 220     5231   4843   4489   -260    -54   -106       N  
ATOM   5854  CA  SER B 220      12.337  21.757 -52.301  1.00 43.98           C  
ANISOU 5854  CA  SER B 220     6062   5487   5160   -208    -76    -79       C  
ATOM   5855  C   SER B 220      11.090  20.955 -52.649  1.00 42.96           C  
ANISOU 5855  C   SER B 220     5895   5363   5065    -80   -124   -107       C  
ATOM   5856  O   SER B 220      10.242  21.409 -53.433  1.00 46.79           O  
ANISOU 5856  O   SER B 220     6462   5798   5518    -12   -154    -95       O  
ATOM   5857  CB  SER B 220      13.116  22.037 -53.585  1.00 51.02           C  
ANISOU 5857  CB  SER B 220     7001   6410   5972   -264    -40    -43       C  
ATOM   5858  OG  SER B 220      13.383  20.821 -54.286  1.00 56.77           O  
ANISOU 5858  OG  SER B 220     7627   7240   6703   -227    -35    -66       O  
ATOM   5859  N   LEU B 221      10.963  19.757 -52.104  1.00 36.19           N  
ANISOU 5859  N   LEU B 221     4919   4564   4267    -48   -135   -147       N  
ATOM   5860  CA  LEU B 221       9.854  18.896 -52.541  1.00 38.20           C  
ANISOU 5860  CA  LEU B 221     5132   4834   4549     55   -177   -176       C  
ATOM   5861  C   LEU B 221       8.697  18.807 -51.554  1.00 37.47           C  
ANISOU 5861  C   LEU B 221     5017   4707   4513    110   -211   -208       C  
ATOM   5862  O   LEU B 221       7.739  18.062 -51.771  1.00 44.01           O  
ANISOU 5862  O   LEU B 221     5799   5556   5369    182   -245   -238       O  
ATOM   5863  CB  LEU B 221      10.370  17.499 -52.905  1.00 35.11           C  
ANISOU 5863  CB  LEU B 221     4639   4531   4170     61   -173   -200       C  
ATOM   5864  CG  LEU B 221      11.598  17.485 -53.830  1.00 38.09           C  
ANISOU 5864  CG  LEU B 221     5018   4967   4489      8   -134   -179       C  
ATOM   5865  CD1 LEU B 221      12.213  16.098 -53.978  1.00 36.90           C  
ANISOU 5865  CD1 LEU B 221     4763   4906   4352     22   -132   -212       C  
ATOM   5866  CD2 LEU B 221      11.246  18.054 -55.197  1.00 32.93           C  
ANISOU 5866  CD2 LEU B 221     4453   4291   3770     39   -140   -151       C  
ATOM   5867  N   PHE B 222       8.785  19.557 -50.464  1.00 38.43           N  
ANISOU 5867  N   PHE B 222     5169   4782   4652     72   -200   -203       N  
ATOM   5868  CA  PHE B 222       7.761  19.513 -49.413  1.00 35.85           C  
ANISOU 5868  CA  PHE B 222     4816   4432   4374    117   -223   -236       C  
ATOM   5869  C   PHE B 222       7.894  20.687 -48.476  1.00 35.60           C  
ANISOU 5869  C   PHE B 222     4857   4334   4338     81   -212   -224       C  
ATOM   5870  O   PHE B 222       8.915  21.375 -48.471  1.00 40.28           O  
ANISOU 5870  O   PHE B 222     5504   4902   4897      2   -184   -192       O  
ATOM   5871  CB  PHE B 222       7.814  18.186 -48.616  1.00 34.33           C  
ANISOU 5871  CB  PHE B 222     4509   4297   4236    105   -220   -269       C  
ATOM   5872  CG  PHE B 222       9.037  18.041 -47.723  1.00 34.26           C  
ANISOU 5872  CG  PHE B 222     4472   4307   4238     21   -188   -262       C  
ATOM   5873  CD1 PHE B 222      10.256  17.655 -48.257  1.00 31.17           C  
ANISOU 5873  CD1 PHE B 222     4055   3965   3822    -28   -165   -248       C  
ATOM   5874  CD2 PHE B 222       8.942  18.265 -46.348  1.00 34.79           C  
ANISOU 5874  CD2 PHE B 222     4533   4350   4337     -4   -182   -274       C  
ATOM   5875  CE1 PHE B 222      11.362  17.512 -47.451  1.00 43.37           C  
ANISOU 5875  CE1 PHE B 222     5563   5539   5375    -97   -142   -249       C  
ATOM   5876  CE2 PHE B 222      10.032  18.119 -45.530  1.00 35.76           C  
ANISOU 5876  CE2 PHE B 222     4628   4492   4466    -74   -160   -272       C  
ATOM   5877  CZ  PHE B 222      11.259  17.751 -46.082  1.00 46.44           C  
ANISOU 5877  CZ  PHE B 222     5950   5898   5795   -120   -142   -261       C  
ATOM   5878  N   HIS B 223       6.875  20.897 -47.652  1.00 39.45           N  
ANISOU 5878  N   HIS B 223     5339   4795   4855    135   -233   -253       N  
ATOM   5879  CA  HIS B 223       6.788  22.108 -46.842  1.00 36.93           C  
ANISOU 5879  CA  HIS B 223     5105   4403   4524    125   -232   -249       C  
ATOM   5880  C   HIS B 223       6.663  21.857 -45.349  1.00 34.39           C  
ANISOU 5880  C   HIS B 223     4727   4091   4249    105   -222   -278       C  
ATOM   5881  O   HIS B 223       7.028  22.712 -44.558  1.00 42.36           O  
ANISOU 5881  O   HIS B 223     5796   5048   5249     66   -211   -271       O  
ATOM   5882  CB  HIS B 223       5.643  22.966 -47.350  1.00 34.29           C  
ANISOU 5882  CB  HIS B 223     4853   4015   4162    227   -272   -257       C  
ATOM   5883  CG  HIS B 223       5.606  23.037 -48.840  1.00 43.29           C  
ANISOU 5883  CG  HIS B 223     6042   5152   5255    261   -289   -233       C  
ATOM   5884  ND1 HIS B 223       6.288  24.002 -49.558  1.00 43.88           N  
ANISOU 5884  ND1 HIS B 223     6244   5162   5265    220   -281   -185       N  
ATOM   5885  CD2 HIS B 223       5.026  22.220 -49.756  1.00 37.71           C  
ANISOU 5885  CD2 HIS B 223     5277   4500   4552    322   -312   -249       C  
ATOM   5886  CE1 HIS B 223       6.110  23.787 -50.849  1.00 45.99           C  
ANISOU 5886  CE1 HIS B 223     6531   5446   5496    262   -298   -172       C  
ATOM   5887  NE2 HIS B 223       5.349  22.712 -50.995  1.00 43.15           N  
ANISOU 5887  NE2 HIS B 223     6058   5159   5179    327   -319   -211       N  
ATOM   5888  N   ARG B 224       6.185  20.679 -44.966  1.00 32.13           N  
ANISOU 5888  N   ARG B 224     4333   3867   4006    125   -224   -309       N  
ATOM   5889  CA  ARG B 224       5.911  20.380 -43.558  1.00 32.73           C  
ANISOU 5889  CA  ARG B 224     4360   3955   4119    111   -214   -338       C  
ATOM   5890  C   ARG B 224       6.069  18.883 -43.427  1.00 28.84           C  
ANISOU 5890  C   ARG B 224     3767   3531   3660     88   -207   -352       C  
ATOM   5891  O   ARG B 224       6.024  18.197 -44.436  1.00 27.93           O  
ANISOU 5891  O   ARG B 224     3622   3449   3542    107   -218   -349       O  
ATOM   5892  CB  ARG B 224       4.464  20.751 -43.209  1.00 37.71           C  
ANISOU 5892  CB  ARG B 224     4991   4580   4759    197   -235   -377       C  
ATOM   5893  CG  ARG B 224       4.225  22.212 -43.216  1.00 45.26           C  
ANISOU 5893  CG  ARG B 224     6057   5461   5679    238   -250   -371       C  
ATOM   5894  CD  ARG B 224       2.797  22.568 -42.882  1.00 41.62           C  
ANISOU 5894  CD  ARG B 224     5585   5006   5221    340   -274   -419       C  
ATOM   5895  NE  ARG B 224       2.034  22.688 -44.092  1.00 45.57           N  
ANISOU 5895  NE  ARG B 224     6099   5515   5701    427   -311   -427       N  
ATOM   5896  CZ  ARG B 224       2.202  23.654 -44.989  1.00 56.43           C  
ANISOU 5896  CZ  ARG B 224     7591   6823   7027    463   -336   -399       C  
ATOM   5897  NH1 ARG B 224       3.125  24.590 -44.803  1.00 49.01           N  
ANISOU 5897  NH1 ARG B 224     6764   5801   6056    405   -323   -360       N  
ATOM   5898  NH2 ARG B 224       1.450  23.673 -46.090  1.00 61.67           N  
ANISOU 5898  NH2 ARG B 224     8262   7500   7668    551   -374   -409       N  
ATOM   5899  N   ALA B 225       6.241  18.393 -42.199  1.00 26.81           N  
ANISOU 5899  N   ALA B 225     3469   3287   3428     49   -192   -366       N  
ATOM   5900  CA  ALA B 225       6.483  16.980 -41.956  1.00 33.43           C  
ANISOU 5900  CA  ALA B 225     4235   4175   4291     23   -190   -377       C  
ATOM   5901  C   ALA B 225       5.800  16.518 -40.672  1.00 33.22           C  
ANISOU 5901  C   ALA B 225     4173   4159   4289     16   -183   -405       C  
ATOM   5902  O   ALA B 225       5.586  17.295 -39.733  1.00 31.00           O  
ANISOU 5902  O   ALA B 225     3922   3852   4007     12   -171   -413       O  
ATOM   5903  CB  ALA B 225       7.980  16.755 -41.846  1.00 31.38           C  
ANISOU 5903  CB  ALA B 225     3975   3925   4021    -40   -178   -354       C  
ATOM   5904  N   VAL B 226       5.478  15.239 -40.631  1.00 32.09           N  
ANISOU 5904  N   VAL B 226     3976   4053   4164     10   -188   -420       N  
ATOM   5905  CA  VAL B 226       4.915  14.630 -39.449  1.00 29.06           C  
ANISOU 5905  CA  VAL B 226     3564   3682   3795    -14   -176   -443       C  
ATOM   5906  C   VAL B 226       5.734  13.378 -39.227  1.00 32.04           C  
ANISOU 5906  C   VAL B 226     3928   4071   4177    -55   -182   -435       C  
ATOM   5907  O   VAL B 226       5.835  12.565 -40.126  1.00 32.02           O  
ANISOU 5907  O   VAL B 226     3906   4086   4174    -44   -200   -434       O  
ATOM   5908  CB  VAL B 226       3.441  14.231 -39.662  1.00 27.48           C  
ANISOU 5908  CB  VAL B 226     3317   3517   3607     18   -182   -477       C  
ATOM   5909  CG1 VAL B 226       2.861  13.589 -38.372  1.00 27.63           C  
ANISOU 5909  CG1 VAL B 226     3309   3556   3634    -24   -160   -499       C  
ATOM   5910  CG2 VAL B 226       2.594  15.460 -40.130  1.00 32.08           C  
ANISOU 5910  CG2 VAL B 226     3913   4097   4181     87   -189   -492       C  
ATOM   5911  N   LEU B 227       6.344  13.256 -38.049  1.00 32.18           N  
ANISOU 5911  N   LEU B 227     3961   4075   4191    -95   -171   -431       N  
ATOM   5912  CA  LEU B 227       7.078  12.063 -37.681  1.00 35.23           C  
ANISOU 5912  CA  LEU B 227     4345   4467   4574   -123   -183   -427       C  
ATOM   5913  C   LEU B 227       6.338  11.350 -36.558  1.00 35.57           C  
ANISOU 5913  C   LEU B 227     4389   4507   4618   -153   -173   -443       C  
ATOM   5914  O   LEU B 227       6.279  11.831 -35.428  1.00 35.26           O  
ANISOU 5914  O   LEU B 227     4368   4455   4573   -175   -155   -446       O  
ATOM   5915  CB  LEU B 227       8.501  12.405 -37.250  1.00 32.30           C  
ANISOU 5915  CB  LEU B 227     3993   4089   4189   -144   -186   -412       C  
ATOM   5916  CG  LEU B 227       9.396  12.852 -38.415  1.00 31.42           C  
ANISOU 5916  CG  LEU B 227     3875   3994   4068   -132   -192   -397       C  
ATOM   5917  CD1 LEU B 227       9.163  14.336 -38.721  1.00 26.05           C  
ANISOU 5917  CD1 LEU B 227     3222   3293   3384   -130   -175   -386       C  
ATOM   5918  CD2 LEU B 227      10.893  12.624 -38.103  1.00 25.87           C  
ANISOU 5918  CD2 LEU B 227     3166   3314   3350   -154   -201   -394       C  
ATOM   5919  N   GLN B 228       5.748  10.208 -36.881  1.00 26.62           N  
ANISOU 5919  N   GLN B 228     3243   3384   3489   -160   -185   -453       N  
ATOM   5920  CA  GLN B 228       5.065   9.387 -35.880  1.00 28.48           C  
ANISOU 5920  CA  GLN B 228     3488   3616   3718   -206   -173   -465       C  
ATOM   5921  C   GLN B 228       5.980   8.244 -35.442  1.00 33.44           C  
ANISOU 5921  C   GLN B 228     4162   4217   4327   -226   -198   -453       C  
ATOM   5922  O   GLN B 228       6.327   7.393 -36.258  1.00 37.84           O  
ANISOU 5922  O   GLN B 228     4726   4771   4883   -209   -228   -452       O  
ATOM   5923  CB  GLN B 228       3.772   8.807 -36.475  1.00 24.29           C  
ANISOU 5923  CB  GLN B 228     2921   3113   3196   -214   -172   -487       C  
ATOM   5924  CG  GLN B 228       2.917   9.881 -37.134  1.00 27.40           C  
ANISOU 5924  CG  GLN B 228     3267   3539   3604   -170   -161   -504       C  
ATOM   5925  CD  GLN B 228       1.704   9.320 -37.902  1.00 33.07           C  
ANISOU 5925  CD  GLN B 228     3936   4298   4332   -170   -169   -533       C  
ATOM   5926  OE1 GLN B 228       1.207   8.214 -37.620  1.00 33.58           O  
ANISOU 5926  OE1 GLN B 228     3998   4370   4392   -226   -168   -544       O  
ATOM   5927  NE2 GLN B 228       1.224  10.089 -38.867  1.00 26.31           N  
ANISOU 5927  NE2 GLN B 228     3046   3466   3484   -111   -180   -545       N  
ATOM   5928  N   SER B 229       6.389   8.243 -34.171  1.00 27.92           N  
ANISOU 5928  N   SER B 229     3500   3498   3610   -254   -190   -447       N  
ATOM   5929  CA  SER B 229       7.109   7.126 -33.593  1.00 29.31           C  
ANISOU 5929  CA  SER B 229     3733   3644   3761   -268   -218   -439       C  
ATOM   5930  C   SER B 229       8.388   6.793 -34.362  1.00 31.99           C  
ANISOU 5930  C   SER B 229     4073   3985   4096   -219   -259   -434       C  
ATOM   5931  O   SER B 229       8.714   5.621 -34.577  1.00 29.95           O  
ANISOU 5931  O   SER B 229     3851   3707   3820   -207   -294   -436       O  
ATOM   5932  CB  SER B 229       6.216   5.875 -33.543  1.00 30.76           C  
ANISOU 5932  CB  SER B 229     3945   3809   3932   -310   -221   -445       C  
ATOM   5933  OG  SER B 229       5.105   6.057 -32.689  1.00 33.31           O  
ANISOU 5933  OG  SER B 229     4264   4142   4249   -365   -179   -453       O  
ATOM   5934  N   GLY B 230       9.134   7.809 -34.763  1.00 28.79           N  
ANISOU 5934  N   GLY B 230     3633   3605   3701   -193   -255   -430       N  
ATOM   5935  CA  GLY B 230      10.353   7.550 -35.496  1.00 24.61           C  
ANISOU 5935  CA  GLY B 230     3090   3097   3163   -152   -286   -431       C  
ATOM   5936  C   GLY B 230      11.140   8.798 -35.771  1.00 29.31           C  
ANISOU 5936  C   GLY B 230     3650   3724   3764   -148   -271   -426       C  
ATOM   5937  O   GLY B 230      10.572   9.892 -35.897  1.00 28.34           O  
ANISOU 5937  O   GLY B 230     3513   3599   3656   -163   -241   -420       O  
ATOM   5938  N   THR B 231      12.450   8.638 -35.886  1.00 22.78           N  
ANISOU 5938  N   THR B 231     2808   2927   2920   -127   -295   -432       N  
ATOM   5939  CA  THR B 231      13.329   9.774 -36.078  1.00 27.21           C  
ANISOU 5939  CA  THR B 231     3335   3524   3480   -141   -280   -429       C  
ATOM   5940  C   THR B 231      14.547   9.380 -36.854  1.00 29.83           C  
ANISOU 5940  C   THR B 231     3627   3914   3793   -109   -302   -441       C  
ATOM   5941  O   THR B 231      14.917   8.202 -36.873  1.00 27.69           O  
ANISOU 5941  O   THR B 231     3363   3651   3506    -65   -339   -457       O  
ATOM   5942  CB  THR B 231      13.834  10.356 -34.718  1.00 40.71           C  
ANISOU 5942  CB  THR B 231     5062   5226   5181   -174   -278   -432       C  
ATOM   5943  OG1 THR B 231      14.456   9.318 -33.957  1.00 36.19           O  
ANISOU 5943  OG1 THR B 231     4509   4655   4585   -151   -317   -446       O  
ATOM   5944  CG2 THR B 231      12.691  10.981 -33.909  1.00 29.86           C  
ANISOU 5944  CG2 THR B 231     3723   3804   3819   -206   -249   -423       C  
ATOM   5945  N   PRO B 232      15.198  10.370 -37.489  1.00 31.06           N  
ANISOU 5945  N   PRO B 232     3745   4112   3945   -131   -280   -437       N  
ATOM   5946  CA  PRO B 232      16.411  10.034 -38.239  1.00 31.00           C  
ANISOU 5946  CA  PRO B 232     3684   4179   3914   -105   -294   -454       C  
ATOM   5947  C   PRO B 232      17.584   9.883 -37.285  1.00 33.08           C  
ANISOU 5947  C   PRO B 232     3925   4486   4159   -106   -319   -478       C  
ATOM   5948  O   PRO B 232      18.503   9.160 -37.591  1.00 40.92           O  
ANISOU 5948  O   PRO B 232     4879   5541   5129    -60   -348   -505       O  
ATOM   5949  CB  PRO B 232      16.593  11.236 -39.194  1.00 27.15           C  
ANISOU 5949  CB  PRO B 232     3174   3719   3424   -147   -254   -437       C  
ATOM   5950  CG  PRO B 232      15.877  12.384 -38.504  1.00 31.01           C  
ANISOU 5950  CG  PRO B 232     3707   4146   3930   -199   -229   -416       C  
ATOM   5951  CD  PRO B 232      14.743  11.757 -37.724  1.00 31.57           C  
ANISOU 5951  CD  PRO B 232     3818   4155   4021   -175   -242   -416       C  
ATOM   5952  N   ASN B 233      17.540  10.555 -36.147  1.00 35.92           N  
ANISOU 5952  N   ASN B 233     4308   4815   4524   -151   -312   -473       N  
ATOM   5953  CA  ASN B 233      18.569  10.432 -35.127  1.00 35.67           C  
ANISOU 5953  CA  ASN B 233     4260   4820   4472   -151   -342   -498       C  
ATOM   5954  C   ASN B 233      18.249   9.199 -34.322  1.00 40.97           C  
ANISOU 5954  C   ASN B 233     4984   5449   5136    -98   -384   -507       C  
ATOM   5955  O   ASN B 233      17.153   8.638 -34.474  1.00 31.49           O  
ANISOU 5955  O   ASN B 233     3832   4187   3947    -84   -380   -490       O  
ATOM   5956  CB  ASN B 233      18.607  11.665 -34.211  1.00 30.25           C  
ANISOU 5956  CB  ASN B 233     3590   4111   3792   -223   -320   -490       C  
ATOM   5957  CG  ASN B 233      17.221  12.062 -33.694  1.00 31.33           C  
ANISOU 5957  CG  ASN B 233     3795   4157   3951   -243   -296   -464       C  
ATOM   5958  OD1 ASN B 233      16.339  12.408 -34.471  1.00 31.99           O  
ANISOU 5958  OD1 ASN B 233     3892   4211   4052   -247   -268   -444       O  
ATOM   5959  ND2 ASN B 233      17.036  12.027 -32.383  1.00 27.92           N  
ANISOU 5959  ND2 ASN B 233     3405   3689   3514   -252   -308   -469       N  
ATOM   5960  N   GLY B 234      19.190   8.763 -33.475  1.00 38.29           N  
ANISOU 5960  N   GLY B 234     4638   5141   4769    -70   -427   -535       N  
ATOM   5961  CA  GLY B 234      18.927   7.597 -32.646  1.00 34.79           C  
ANISOU 5961  CA  GLY B 234     4266   4646   4307    -20   -472   -540       C  
ATOM   5962  C   GLY B 234      19.639   6.324 -33.084  1.00 39.20           C  
ANISOU 5962  C   GLY B 234     4820   5240   4836     72   -528   -570       C  
ATOM   5963  O   GLY B 234      20.364   6.304 -34.073  1.00 42.11           O  
ANISOU 5963  O   GLY B 234     5115   5686   5197    103   -530   -592       O  
ATOM   5964  N   PRO B 235      19.416   5.242 -32.351  1.00 38.82           N  
ANISOU 5964  N   PRO B 235     4857   5132   4762    118   -574   -573       N  
ATOM   5965  CA  PRO B 235      20.290   4.070 -32.410  1.00 45.71           C  
ANISOU 5965  CA  PRO B 235     5742   6031   5592    219   -645   -610       C  
ATOM   5966  C   PRO B 235      20.050   3.141 -33.603  1.00 47.30           C  
ANISOU 5966  C   PRO B 235     5956   6225   5791    277   -660   -616       C  
ATOM   5967  O   PRO B 235      20.947   2.344 -33.904  1.00 44.83           O  
ANISOU 5967  O   PRO B 235     5631   5959   5443    373   -715   -656       O  
ATOM   5968  CB  PRO B 235      19.961   3.319 -31.111  1.00 49.54           C  
ANISOU 5968  CB  PRO B 235     6347   6430   6047    234   -686   -601       C  
ATOM   5969  CG  PRO B 235      18.854   4.103 -30.439  1.00 48.05           C  
ANISOU 5969  CG  PRO B 235     6194   6178   5886    134   -628   -560       C  
ATOM   5970  CD  PRO B 235      18.297   5.062 -31.422  1.00 42.79           C  
ANISOU 5970  CD  PRO B 235     5454   5535   5267     75   -562   -542       C  
ATOM   5971  N   TRP B 236      18.893   3.214 -34.271  1.00 34.74           N  
ANISOU 5971  N   TRP B 236     4387   4581   4232    230   -617   -584       N  
ATOM   5972  CA  TRP B 236      18.612   2.187 -35.287  1.00 31.63           C  
ANISOU 5972  CA  TRP B 236     4023   4166   3829    287   -641   -592       C  
ATOM   5973  C   TRP B 236      18.492   2.702 -36.719  1.00 36.03           C  
ANISOU 5973  C   TRP B 236     4499   4779   4410    276   -599   -591       C  
ATOM   5974  O   TRP B 236      18.520   1.905 -37.646  1.00 38.81           O  
ANISOU 5974  O   TRP B 236     4860   5136   4749    336   -624   -608       O  
ATOM   5975  CB  TRP B 236      17.325   1.432 -34.938  1.00 29.59           C  
ANISOU 5975  CB  TRP B 236     3878   3793   3573    253   -644   -564       C  
ATOM   5976  CG  TRP B 236      16.174   2.388 -34.673  1.00 35.48           C  
ANISOU 5976  CG  TRP B 236     4614   4508   4360    150   -576   -527       C  
ATOM   5977  CD1 TRP B 236      15.834   2.958 -33.457  1.00 34.86           C  
ANISOU 5977  CD1 TRP B 236     4561   4399   4284     90   -553   -508       C  
ATOM   5978  CD2 TRP B 236      15.231   2.899 -35.630  1.00 32.90           C  
ANISOU 5978  CD2 TRP B 236     4247   4182   4070    106   -527   -509       C  
ATOM   5979  NE1 TRP B 236      14.726   3.765 -33.608  1.00 36.51           N  
ANISOU 5979  NE1 TRP B 236     4748   4593   4531     17   -492   -483       N  
ATOM   5980  CE2 TRP B 236      14.338   3.754 -34.932  1.00 31.93           C  
ANISOU 5980  CE2 TRP B 236     4128   4033   3973     27   -478   -484       C  
ATOM   5981  CE3 TRP B 236      15.026   2.690 -37.007  1.00 38.14           C  
ANISOU 5981  CE3 TRP B 236     4878   4869   4745    132   -524   -516       C  
ATOM   5982  CZ2 TRP B 236      13.279   4.423 -35.559  1.00 30.28           C  
ANISOU 5982  CZ2 TRP B 236     3885   3821   3798    -18   -430   -468       C  
ATOM   5983  CZ3 TRP B 236      13.962   3.362 -37.652  1.00 32.73           C  
ANISOU 5983  CZ3 TRP B 236     4163   4178   4095     81   -476   -496       C  
ATOM   5984  CH2 TRP B 236      13.111   4.226 -36.918  1.00 34.40           C  
ANISOU 5984  CH2 TRP B 236     4374   4365   4330     10   -431   -473       C  
ATOM   5985  N   ALA B 237      18.305   4.012 -36.909  1.00 35.28           N  
ANISOU 5985  N   ALA B 237     4340   4717   4348    202   -539   -570       N  
ATOM   5986  CA  ALA B 237      17.848   4.505 -38.217  1.00 36.21           C  
ANISOU 5986  CA  ALA B 237     4414   4858   4487    181   -497   -557       C  
ATOM   5987  C   ALA B 237      18.965   4.702 -39.221  1.00 36.39           C  
ANISOU 5987  C   ALA B 237     4349   4989   4490    220   -494   -584       C  
ATOM   5988  O   ALA B 237      18.691   4.771 -40.410  1.00 41.60           O  
ANISOU 5988  O   ALA B 237     4986   5667   5152    226   -472   -579       O  
ATOM   5989  CB  ALA B 237      16.966   5.814 -38.096  1.00 27.60           C  
ANISOU 5989  CB  ALA B 237     3314   3739   3433     90   -436   -519       C  
ATOM   5990  N   THR B 238      20.212   4.785 -38.758  1.00 34.01           N  
ANISOU 5990  N   THR B 238     3995   4764   4162    245   -515   -616       N  
ATOM   5991  CA  THR B 238      21.331   4.855 -39.680  1.00 38.49           C  
ANISOU 5991  CA  THR B 238     4469   5452   4702    283   -511   -652       C  
ATOM   5992  C   THR B 238      22.476   3.925 -39.264  1.00 40.66           C  
ANISOU 5992  C   THR B 238     4722   5791   4935    383   -577   -708       C  
ATOM   5993  O   THR B 238      22.545   3.461 -38.135  1.00 43.17           O  
ANISOU 5993  O   THR B 238     5095   6063   5245    409   -622   -715       O  
ATOM   5994  CB  THR B 238      21.928   6.257 -39.757  1.00 38.06           C  
ANISOU 5994  CB  THR B 238     4332   5474   4653    196   -457   -644       C  
ATOM   5995  OG1 THR B 238      22.342   6.632 -38.443  1.00 40.00           O  
ANISOU 5995  OG1 THR B 238     4580   5719   4901    165   -472   -651       O  
ATOM   5996  CG2 THR B 238      20.916   7.265 -40.260  1.00 38.31           C  
ANISOU 5996  CG2 THR B 238     4389   5449   4717    111   -397   -594       C  
ATOM   5997  N   VAL B 239      23.370   3.650 -40.199  1.00 35.25           N  
ANISOU 5997  N   VAL B 239     3959   5216   4218    444   -583   -750       N  
ATOM   5998  CA  VAL B 239      24.666   3.095 -39.861  1.00 35.71           C  
ANISOU 5998  CA  VAL B 239     3960   5377   4234    534   -636   -814       C  
ATOM   5999  C   VAL B 239      25.733   3.931 -40.545  1.00 37.32           C  
ANISOU 5999  C   VAL B 239     4019   5741   4418    499   -590   -843       C  
ATOM   6000  O   VAL B 239      25.465   4.647 -41.521  1.00 39.66           O  
ANISOU 6000  O   VAL B 239     4282   6061   4726    429   -526   -816       O  
ATOM   6001  CB  VAL B 239      24.799   1.635 -40.314  1.00 31.54           C  
ANISOU 6001  CB  VAL B 239     3480   4836   3669    675   -704   -854       C  
ATOM   6002  CG1 VAL B 239      23.809   0.768 -39.532  1.00 35.35           C  
ANISOU 6002  CG1 VAL B 239     4115   5156   4160    696   -752   -825       C  
ATOM   6003  CG2 VAL B 239      24.571   1.528 -41.814  1.00 31.42           C  
ANISOU 6003  CG2 VAL B 239     3436   4855   3648    690   -671   -855       C  
ATOM   6004  N   SER B 240      26.944   3.847 -40.023  1.00 37.63           N  
ANISOU 6004  N   SER B 240     3977   5894   4425    543   -625   -901       N  
ATOM   6005  CA  SER B 240      28.085   4.484 -40.651  1.00 43.96           C  
ANISOU 6005  CA  SER B 240     4631   6873   5199    513   -586   -943       C  
ATOM   6006  C   SER B 240      28.474   3.697 -41.896  1.00 45.21           C  
ANISOU 6006  C   SER B 240     4742   7116   5318    615   -593   -986       C  
ATOM   6007  O   SER B 240      28.052   2.538 -42.085  1.00 40.75           O  
ANISOU 6007  O   SER B 240     4262   6478   4742    730   -648   -996       O  
ATOM   6008  CB  SER B 240      29.269   4.428 -39.698  1.00 44.45           C  
ANISOU 6008  CB  SER B 240     4613   7044   5233    552   -634  -1005       C  
ATOM   6009  OG  SER B 240      29.576   3.070 -39.477  1.00 43.15           O  
ANISOU 6009  OG  SER B 240     4486   6877   5033    718   -723  -1057       O  
ATOM   6010  N   ALA B 241      29.316   4.314 -42.721  1.00 41.03           N  
ANISOU 6010  N   ALA B 241     4083   6746   4761    571   -539  -1014       N  
ATOM   6011  CA  ALA B 241      29.780   3.670 -43.944  1.00 41.76           C  
ANISOU 6011  CA  ALA B 241     4116   6943   4808    663   -536  -1061       C  
ATOM   6012  C   ALA B 241      30.516   2.367 -43.676  1.00 53.88           C  
ANISOU 6012  C   ALA B 241     5635   8538   6299    845   -628  -1143       C  
ATOM   6013  O   ALA B 241      30.309   1.374 -44.395  1.00 58.43           O  
ANISOU 6013  O   ALA B 241     6258   9092   6851    963   -663  -1166       O  
ATOM   6014  CB  ALA B 241      30.627   4.596 -44.728  1.00 40.51           C  
ANISOU 6014  CB  ALA B 241     3816   6955   4620    572   -458  -1080       C  
ATOM   6015  N   GLY B 242      31.363   2.359 -42.643  1.00 52.61           N  
ANISOU 6015  N   GLY B 242     5416   8449   6123    875   -674  -1191       N  
ATOM   6016  CA  GLY B 242      32.123   1.171 -42.295  1.00 43.59           C  
ANISOU 6016  CA  GLY B 242     4262   7366   4932   1060   -772  -1275       C  
ATOM   6017  C   GLY B 242      31.217   0.031 -41.882  1.00 47.25           C  
ANISOU 6017  C   GLY B 242     4912   7637   5405   1163   -850  -1250       C  
ATOM   6018  O   GLY B 242      31.410  -1.122 -42.288  1.00 48.17           O  
ANISOU 6018  O   GLY B 242     5068   7756   5480   1321   -915  -1299       O  
ATOM   6019  N   GLU B 243      30.203   0.326 -41.074  1.00 46.38           N  
ANISOU 6019  N   GLU B 243     4922   7355   5344   1073   -844  -1174       N  
ATOM   6020  CA  GLU B 243      29.337  -0.765 -40.661  1.00 45.48           C  
ANISOU 6020  CA  GLU B 243     4985   7062   5233   1153   -913  -1150       C  
ATOM   6021  C   GLU B 243      28.496  -1.308 -41.843  1.00 48.61           C  
ANISOU 6021  C   GLU B 243     5453   7382   5634   1175   -896  -1125       C  
ATOM   6022  O   GLU B 243      28.256  -2.519 -41.926  1.00 48.42           O  
ANISOU 6022  O   GLU B 243     5540   7275   5582   1295   -968  -1145       O  
ATOM   6023  CB  GLU B 243      28.516  -0.385 -39.431  1.00 45.54           C  
ANISOU 6023  CB  GLU B 243     5098   6922   5283   1057   -913  -1084       C  
ATOM   6024  CG  GLU B 243      27.460  -1.407 -39.016  1.00 43.88           C  
ANISOU 6024  CG  GLU B 243     5079   6518   5076   1101   -966  -1047       C  
ATOM   6025  CD  GLU B 243      28.058  -2.684 -38.461  1.00 51.54           C  
ANISOU 6025  CD  GLU B 243     6127   7470   5987   1270  -1079  -1105       C  
ATOM   6026  OE1 GLU B 243      27.267  -3.538 -37.980  1.00 46.17           O  
ANISOU 6026  OE1 GLU B 243     5618   6626   5300   1297  -1128  -1074       O  
ATOM   6027  OE2 GLU B 243      29.308  -2.831 -38.505  1.00 47.83           O  
ANISOU 6027  OE2 GLU B 243     5549   7151   5472   1375  -1119  -1183       O  
ATOM   6028  N   ALA B 244      28.093  -0.428 -42.769  1.00 47.49           N  
ANISOU 6028  N   ALA B 244     5254   7270   5521   1062   -805  -1085       N  
ATOM   6029  CA  ALA B 244      27.341  -0.832 -43.976  1.00 41.77           C  
ANISOU 6029  CA  ALA B 244     4582   6492   4799   1077   -785  -1065       C  
ATOM   6030  C   ALA B 244      28.187  -1.756 -44.843  1.00 48.38           C  
ANISOU 6030  C   ALA B 244     5371   7439   5573   1233   -828  -1146       C  
ATOM   6031  O   ALA B 244      27.731  -2.820 -45.297  1.00 38.64           O  
ANISOU 6031  O   ALA B 244     4241   6120   4320   1330   -880  -1158       O  
ATOM   6032  CB  ALA B 244      26.943   0.379 -44.795  1.00 34.73           C  
ANISOU 6032  CB  ALA B 244     3626   5634   3937    936   -684  -1015       C  
ATOM   6033  N   ARG B 245      29.426  -1.321 -45.079  1.00 45.02           N  
ANISOU 6033  N   ARG B 245     4785   7208   5111   1253   -805  -1205       N  
ATOM   6034  CA  ARG B 245      30.350  -2.061 -45.911  1.00 46.17           C  
ANISOU 6034  CA  ARG B 245     4856   7495   5191   1400   -836  -1292       C  
ATOM   6035  C   ARG B 245      30.555  -3.443 -45.288  1.00 49.16           C  
ANISOU 6035  C   ARG B 245     5339   7806   5533   1581   -957  -1345       C  
ATOM   6036  O   ARG B 245      30.643  -4.461 -45.983  1.00 51.59           O  
ANISOU 6036  O   ARG B 245     5694   8111   5797   1721  -1008  -1393       O  
ATOM   6037  CB  ARG B 245      31.684  -1.306 -46.010  1.00 49.64           C  
ANISOU 6037  CB  ARG B 245     5095   8167   5598   1376   -792  -1350       C  
ATOM   6038  CG  ARG B 245      32.826  -2.119 -46.637  1.00 49.52           C  
ANISOU 6038  CG  ARG B 245     4980   8330   5506   1551   -835  -1461       C  
ATOM   6039  CD  ARG B 245      33.935  -1.218 -47.127  1.00 45.85           C  
ANISOU 6039  CD  ARG B 245     4303   8108   5009   1483   -757  -1507       C  
ATOM   6040  NE  ARG B 245      33.496  -0.335 -48.200  1.00 51.53           N  
ANISOU 6040  NE  ARG B 245     4992   8845   5742   1337   -647  -1449       N  
ATOM   6041  CZ  ARG B 245      33.462  -0.692 -49.482  1.00 60.66           C  
ANISOU 6041  CZ  ARG B 245     6135  10054   6858   1391   -620  -1469       C  
ATOM   6042  NH1 ARG B 245      33.056   0.169 -50.408  1.00 61.68           N  
ANISOU 6042  NH1 ARG B 245     6247  10194   6996   1254   -521  -1411       N  
ATOM   6043  NH2 ARG B 245      33.835  -1.917 -49.844  1.00 64.15           N  
ANISOU 6043  NH2 ARG B 245     6592  10534   7248   1589   -694  -1548       N  
ATOM   6044  N   ARG B 246      30.615  -3.467 -43.965  1.00 45.87           N  
ANISOU 6044  N   ARG B 246     4971   7327   5130   1578  -1006  -1336       N  
ATOM   6045  CA  ARG B 246      30.869  -4.691 -43.239  1.00 51.34           C  
ANISOU 6045  CA  ARG B 246     5775   7951   5781   1744  -1124  -1384       C  
ATOM   6046  C   ARG B 246      29.706  -5.634 -43.483  1.00 52.42           C  
ANISOU 6046  C   ARG B 246     6111   7882   5926   1772  -1164  -1341       C  
ATOM   6047  O   ARG B 246      29.902  -6.807 -43.856  1.00 47.20           O  
ANISOU 6047  O   ARG B 246     5529   7193   5212   1933  -1243  -1395       O  
ATOM   6048  CB  ARG B 246      31.004  -4.372 -41.754  1.00 51.54           C  
ANISOU 6048  CB  ARG B 246     5826   7934   5823   1703  -1156  -1366       C  
ATOM   6049  CG  ARG B 246      31.724  -5.400 -40.920  1.00 52.75           C  
ANISOU 6049  CG  ARG B 246     6041   8085   5917   1884  -1279  -1435       C  
ATOM   6050  CD  ARG B 246      31.122  -5.451 -39.499  1.00 58.85           C  
ANISOU 6050  CD  ARG B 246     6959   8690   6711   1831  -1319  -1378       C  
ATOM   6051  NE  ARG B 246      30.473  -6.745 -39.302  1.00 64.00           N  
ANISOU 6051  NE  ARG B 246     7828   9154   7333   1931  -1404  -1366       N  
ATOM   6052  CZ  ARG B 246      29.213  -6.953 -38.927  1.00 57.34           C  
ANISOU 6052  CZ  ARG B 246     7155   8108   6523   1837  -1395  -1283       C  
ATOM   6053  NH1 ARG B 246      28.393  -5.947 -38.649  1.00 42.48           N  
ANISOU 6053  NH1 ARG B 246     5255   6177   4709   1649  -1306  -1203       N  
ATOM   6054  NH2 ARG B 246      28.786  -8.210 -38.807  1.00 61.86           N  
ANISOU 6054  NH2 ARG B 246     7923   8526   7056   1935  -1480  -1285       N  
ATOM   6055  N   ARG B 247      28.494  -5.096 -43.302  1.00 47.58           N  
ANISOU 6055  N   ARG B 247     5574   7129   5376   1614  -1107  -1248       N  
ATOM   6056  CA  ARG B 247      27.261  -5.864 -43.474  1.00 46.03           C  
ANISOU 6056  CA  ARG B 247     5557   6738   5194   1604  -1133  -1200       C  
ATOM   6057  C   ARG B 247      27.060  -6.364 -44.902  1.00 43.06           C  
ANISOU 6057  C   ARG B 247     5185   6378   4797   1661  -1126  -1224       C  
ATOM   6058  O   ARG B 247      26.641  -7.503 -45.114  1.00 46.13           O  
ANISOU 6058  O   ARG B 247     5717   6652   5158   1750  -1195  -1237       O  
ATOM   6059  CB  ARG